ID A0A072PIG4_9EURO Unreviewed; 710 AA.
AC A0A072PIG4;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Multicopper oxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O9_08929 {ECO:0000313|EMBL:KEF55275.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF55275.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF55275.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF55275.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) 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:KEF55275.1}.
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DR EMBL; AMGV01000008; KEF55275.1; -; Genomic_DNA.
DR RefSeq; XP_013257865.1; XM_013402411.1.
DR AlphaFoldDB; A0A072PIG4; -.
DR STRING; 1182545.A0A072PIG4; -.
DR GeneID; 25283839; -.
DR VEuPathDB; FungiDB:A1O9_08929; -.
DR HOGENOM; CLU_006504_5_0_1; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000027920; 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; cd13850; CuRO_1_Abr2_like; 1.
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:UP000027920};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..710
FT /note="Multicopper oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001683496"
FT DOMAIN 50..161
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 241..385
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 470..592
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
FT REGION 607..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 710 AA; 74361 MW; 53E9F7E9C069CE2C CRC64;
MAFTRLTKAL TALSFALSSF QLVTASSDTY NSACGPSTGH IPFTIDVTWG PTDSSKAFSR
NAFLINGTLP GPPLHLKVGD VVDFTVINHT PDVTGVHFHG IRQLSTPWAD GVPGVSQTVI
KSQTTYTYTW EADASGTYFY HAHYKGQMMD GLYGAIIISP ADTADTPFGQ IGDAQQVKAA
ADKVTPVFAS DWNRFTFDEF FQIEQEANID WACTDSITLN GFGSQLCPSL DFLTANAAPP
AIKILNGTAL TAKGCIPPSN PVIQGQFQRN LAALPPGAYD VCTPFTGQNF TLQVDPKDGW
AAMSFISPAS FAIFTVAIDN HKLYVYEYNG NYIQPQVVDK LTLANGDRIS FMVKLDQTPA
DYIIRVANAG INQVVSGFGI LAYKGGDDFI STQGVINYGG VNTTTVTSFA PGRAAPYPPV
AVSSHADQTF VLDILKDPAQ PTEAWAWTLS GIQAYDESRD DAVPPLLFQD PSAIPNSDLI
LKTKFNQWID LIIKVEGPVA QPHPIHKHAN KFFAIGAGTG AFNFTTVAAA QAGGMQFNLQ
NPPFLDGFTS IPAEGTGSWM VFRYQADTPG AWLLHCHIQT HFSGGMGVAI LDAIDNFPKV
PTDLGSTCSG TGKSTDNGSD SGSGSGSGSG SDSGSGSGSG SGSSSGSGSG SDSGTGSGSG
SGSGSTTTAS GSTGTRPATI ATFTGAASSE RPMVWSVSLG LLAFVLALTS
//
