ID   A0A194VRM0_9PEZI        Unreviewed;       705 AA.
AC   A0A194VRM0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Laccase {ECO:0000313|EMBL:KUI66846.1};
GN   ORFNames=VM1G_01560 {ECO:0000313|EMBL:KUI66846.1};
OS   Valsa mali.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI66846.1};
RN   [1] {ECO:0000313|EMBL:KUI66846.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03-8 {ECO:0000313|EMBL:KUI66846.1};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT   Colonization on Woody Bark.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
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DR   EMBL; CM003099; KUI66846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194VRM0; -.
DR   OrthoDB; 449862at2759; -.
DR   Proteomes; UP000078559; Chromosome 2.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   CDD; cd13910; CuRO_3_MCO_like_4; 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:SF515; ADR239WP; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        76..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          142..255
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          268..434
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          513..660
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          46..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   705 AA;  79431 MW;  9AC8C55AE7371DD8 CRC64;
     MLKMAQYEHV RSSSPSGKCR TSNDLELQEY NEEKIGNLVS EQEERLLPGD AEETLRSDDD
     DGDEHDHSRK RRRRRWYHLG LFGLIGIILF AVIAVFLDHL YFQKSEGEVN GTFRRQSSDY
     TIDPDWDYNA PPTRREFHWV ITDITANPDG VFRPMMVING QFPGPMIVCN EGDTIVVNVV
     NEAKNATAIH WHGLFQNGTN WHDGTVGVTQ CPIAPGRSFR YEFTVKGQAG SYFYHGHQGT
     QSLDGLVGPF IILSAEEKEN QPIPYDTDRV VMVQDWYHVL SDGLLRETLS PGSESSPTPN
     GALINGANKL DCSLHPRRHC DASTALLPTF DLAPNKQHRL RVINIGGFAW FEVSIDKHIN
     LPVTEVDGVT VEPAADSSIL IGPGQRYSII LSTNQTDPSN LYWFRARMIN HCFAENVLPD
     KGVATARAVI RYNTSDPVNQ FDAQPDLPTT ENDSGKFTVV CKDNNEAYRP FPARPAPEYA
     HHSWYLRVNL EIGAWRLERG FLNQSTFRPQ IQSPTLHRFV QGLNTGNETF AIEGVNDRAF
     GKKNELVVSS EGVEVVDVIL QNFDEGNHPF HLHGQQMFIL AQGHGYFPGY EKLGLNPEGK
     GLLDPNDRSI ISNPLRRDVT AVEAFGWTLI RFVADNPGIW LLHCHMIWHG EAGMAMQFAS
     RLDIMRNWTI PEQSATLCEA PLEELERGSV PKDSIWYGHF ASDDP
//