ID   A0A0W0FU26_9AGAR        Unreviewed;      1152 AA.
AC   A0A0W0FU26;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Blue (type 1) copper domain-containing protein {ECO:0000259|Pfam:PF00127};
GN   ORFNames=WG66_7509 {ECO:0000313|EMBL:KTB39808.1};
OS   Moniliophthora roreri.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB39808.1, ECO:0000313|Proteomes:UP000054988};
RN   [1] {ECO:0000313|EMBL:KTB39808.1, ECO:0000313|Proteomes:UP000054988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB39808.1,
RC   ECO:0000313|Proteomes:UP000054988};
RA   Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT   "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT   pod rot of cacao.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KTB39808.1}.
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DR   EMBL; LATX01001627; KTB39808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0FU26; -.
DR   eggNOG; KOG2226; Eukaryota.
DR   Proteomes; UP000054988; Unassembled WGS sequence.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   CDD; cd00920; Cupredoxin; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR   InterPro; IPR000923; BlueCu_1.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR026705; Hid-1/Ecm30.
DR   PANTHER; PTHR21575; PROTEIN HID1; 1.
DR   PANTHER; PTHR21575:SF12; PROTEIN HID1; 1.
DR   Pfam; PF00127; Copper-bind; 1.
DR   Pfam; PF12722; Hid1; 1.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
PE   4: Predicted;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..1152
FT                   /note="Blue (type 1) copper domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006902112"
FT   DOMAIN          52..146
FT                   /note="Blue (type 1) copper"
FT                   /evidence="ECO:0000259|Pfam:PF00127"
FT   REGION          164..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          896..994
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..429
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        896..937
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1152 AA;  125381 MW;  A5840B51A47F3F96 CRC64;
     MSLLVVIVLA ILPFALAQYG GYGGGSPTTA APSVPSAPPD TDGHVNIDVF FNGNFAFNPS
     SVTAKNGTLV TFWFPGGAFP HSVTQSSFES PCTHLEANAT AGTPAGFDSG LVNAMQFTIN
     ITDDTKPIWY HCKFPLHCGM GMVGAINAPT SGNTFEAFQA AAQQIGGSET TEPDNGPVTG
     GVNGVATAAP TASGSNSATS VVASGGAASQ AASSSGAGPE PNDPPNTRSS NDMFAKIPQR
     LTSSFGLLPD SEKLAFRSRP DGLQKLAATR HIPESDSYWN QYFVLFDSAS EVFSLITPND
     VRRALLDAPE NIATLIRVVC LRLFNLISDH TFPTPSSASV SAFASSLIKA ASSERNTTKE
     VLNCLRVLQR VLPVVFELEG DTSVFDLEVL WKKIEVEEDE DNDNTATTAT GEEPQFVIED
     EEDDESEEGQ TTVGSQSQTP QPKRKRVKQL PSLGERLFNS LIDLLFCCGF TLPTKIQKDH
     YKINYVIWEK GIGSTSDPGP SQQYDNNKAE VLRLLLVLLS RQIYIPASSL FTNPSLYTLH
     LVQKTPRRDV LTVLCSLLNT AMNSATGPPT SIGNMAGRLP YNHLVFKGED PRINLVAICF
     EVLVVLLDFQ SGNARDTVVG SGEQQSSVPT AHTNAFRYFL MKLHRTQDFT FILDGILGIM
     EQEIASMNNI LPGARKSVPY IAENIILFWK MIELNKKFRA YVLESEKAMD LVAFFLCYNL
     EIKDKPQQHG LCRALSYIMQ TLSAEPAFGS RLSDPIKAQI PAKWATPGGA ADFLINSIYS
     VVATTSGTLN SLYPALIITL SNCAPYFKRL SVTSSTRLIQ LFTSFSNPMF LLSDEGHPRL
     LFFMLEVFNS IILHNPSENP HLLYGIISAH KIFKDLGTLT LYSGLREIRR IQLAKEEHAR
     KADDKGSRRS SAEHGHGPSE EKKSLLFSAE GVDEEAGESR QPSSGAPADA DVSSPEPVVS
     PTSDAIPSGN APSEKAKGKM KEQRRSSSID NNGSLERLAA SGIGRNGFVP TQEWVTSWQQ
     GLPLDIVMLM ISELLPKIEN MQAGHHKVSS ASSILEFLGS VTLKDVLPPT PPLSPRKFVW
     SDASIVWLTS LIWGEIFVRA MTPLGIWNST NIRLFYVKQR REQRQISETV SNVVGGFLGR
     ANSEQSISRS RS
//