ID A0A168AYD7_CORDF Unreviewed; 561 AA.
AC A0A168AYD7;
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=Multicopper oxidase, type 3 {ECO:0000313|EMBL:OAA69360.1};
GN ORFNames=LEL_10236 {ECO:0000313|EMBL:OAA69360.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA69360.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA69360.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA69360.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA69360.1}.
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DR EMBL; AZHF01000011; OAA69360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168AYD7; -.
DR STRING; 1081108.A0A168AYD7; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd13880; CuRO_2_MaLCC_like; 1.
DR CDD; cd13901; CuRO_3_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; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR PANTHER; PTHR11709:SF394; 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.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..561
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007895561"
FT DOMAIN 63..179
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 189..335
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 403..525
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 561 AA; 61635 MW; 8135E18F52A371BE CRC64;
MKSSLLFVGG LATLARCSDL QPRVACAGNT AAARSKWCDL SIDTNYYDVV PTTGITREYY
FNVEELQAAP DGYLRTVYAV NGLVPGPTIV ADWGDVVVVH VNNSLATARN GTSIHFHGIR
QNYTSQMDGV TSITQCPIAV GDVMTYVWRA TQYGSSWYHS HIGLQAWEGV AGAILINGPA
TANYEVDKGT IMLSDWSHRT ADELYTVALT TGPPELDTGL INGTNVWNNT GTIVGHRFNT
SFTSGQSYRL RLINGAIDTQ FKFSIDNHTM TVIAADLVPI KPYDTTVLDI SMGQRYDVVV
SADQASVANN FWMRAIPQVA CSNNANTADI RGIVYYGSEP ATPTTTGYDY KDACIDEPVS
SLVPYLAVDA GEQHWADLEQ VDIFNASGVF LWTLNGTSFN SSWTNPTLLQ LYNRKTNYTS
DSHVIQLDEA DQWAYLIIEN QNAVPHPIHL HGHDFFILGQ GSGAYNSSYL LSLKNAVRRD
VAMLSGSGYL VLAFKTDNPG AWLMHCHIGW HTNAGFALQF LEQPEVARKL MNYELLNSTC
AAWSSYTTKL AIEQPTYDDG V
//
