ID   A0A395N372_9HYPO        Unreviewed;       627 AA.
AC   A0A395N372;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Multicopper oxidase {ECO:0000313|EMBL:RFN54390.1};
GN   ORFNames=FIE12Z_1517 {ECO:0000313|EMBL:RFN54390.1};
OS   Fusarium flagelliforme.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN54390.1, ECO:0000313|Proteomes:UP000265631};
RN   [1] {ECO:0000313|EMBL:RFN54390.1, ECO:0000313|Proteomes:UP000265631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN54390.1,
RC   ECO:0000313|Proteomes:UP000265631};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFN54390.1}.
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DR   EMBL; PXXK01000028; RFN54390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395N372; -.
DR   STRING; 2594813.A0A395N372; -.
DR   Proteomes; UP000265631; Unassembled WGS sequence.
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:InterPro.
DR   CDD; cd13876; CuRO_2_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; IPR008972; Cupredoxin.
DR   PANTHER; PTHR11709:SF218; FI03373P-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.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008}; Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          71..179
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07732"
FT   DOMAIN          224..380
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00394"
FT   DOMAIN          489..597
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000259|Pfam:PF07731"
FT   REGION          382..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   627 AA;  70716 MW;  251C35C206DA3B11 CRC64;
     MESKQTLLPN VRRHTTSRNA WLFTALLISS FLLWAFWHQD IHHVFPNWGD RTDKSARLVR
     KYHLQTGVRW MNPDGGRWRV MFTCNGQSPC PVLYAEEGDI VELTLKSDIY AQSSIHLSGI
     GHKQSWNDGT AGLSQFPTLP RSNWTNAYDT SGSWGLNWFI DHTTTASADG ISGALYVAPS
     LDRPRPYHLI TNNSLELRQI REAERDIRHV IIQNHQHRDS VWKLLRMRAE GSEYYCYDSI
     LVNGKGRVHC RQPGYDHLNG HTLDQKGCIQ PPGLPDEKCT PSLADYEVIE TQGRKYMMMN
     LINLGFEHSV KLSIDHHKII LIANNGGFVY PEEADVVYIP DPSRVTVLVK LDAEPDDYAV
     RISSTSELQN LHGYAILSYR SKRPPQYGEP MTPPSTTPET PCLLPDGNTH SSCKIADGQF
     APPYPANPPP SPSKNHPARA DFTFRLAADS QPSKTERVPE YFLNGKPWQL FHGSMMPLLF
     HAANETLDRP VISNLPLGSV VDLILENRFN ETISFYKHGE PSWLLGSNAN EKFPGSTVED
     AKKYLNLRDS ALVIVHDLPA LGWSVLRFKV TSQTATMLHA AKLRYFALGM TVPILEGITE
     DTPLKIPEDM IERPHVDFKP AHDGVFG
//