ID A0A150VHL4_9PEZI Unreviewed; 365 AA.
AC A0A150VHL4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Plastocyanin-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=M433DRAFT_58180 {ECO:0000313|EMBL:KYG49937.1};
OS Acidomyces richmondensis BFW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Acidomyces.
OX NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG49937.1, ECO:0000313|Proteomes:UP000075602};
RN [1] {ECO:0000313|EMBL:KYG49937.1, ECO:0000313|Proteomes:UP000075602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFW {ECO:0000313|EMBL:KYG49937.1,
RC ECO:0000313|Proteomes:UP000075602};
RX PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z., LaButti K.,
RA Lapidus A., Lipzen A., Chen C., Johnson J., Lindquist E.A., Pan C.,
RA Hettich R.L., Grigoriev I.V., Singer S.W., Banfield J.F.;
RT "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT Carbon Cycling in Acid Mine Drainage.";
RL Front. Microbiol. 7:238-238(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:KYG49937.1}.
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DR EMBL; JPDO01000013; KYG49937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150VHL4; -.
DR STRING; 766039.A0A150VHL4; -.
DR Proteomes; UP000075602; Unassembled WGS sequence.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR InterPro; IPR011707; Cu-oxidase-like_N.
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:SF504; MULTICOPPER OXIDASE; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 2.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..365
FT /note="Plastocyanin-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012136208"
FT DOMAIN 95..201
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 267..362
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 365 AA; 40780 MW; 8641CFF45241C872 CRC64;
MLIALWFVTF TGSFALNSNG TVRTYFVGAV EEDWDYMPTG MDLINEQRIA DSPQAAATAA
QNGQRIGHLY TKAMFREFTD DTFVSQSERP EWLGMLGPIL RAEVGDTLRV VFKNMASHNY
SIHPHGLRYT KPNEGLYGPE QVFGGNSVPP GDTWTYTWEV PERAGPGPMD PPSLAWTYHS
DVSGAQDIYS GLVGALIVYR PGELRKHTLD VPAPKNSNLT EEVLTLFMIV DENRSFYIDQ
NTLSRTNITA GELQVNRFDP GFQESNLKHS INGRLFGNLE GLNLTVGRQA RWHVQSLGSV
ANAHTPHWHG NTLLWAGQRL DVVSVLPAQT KSLTMTVDNP GEWVHHCQVV NHRAKGMITK
YRAQE
//
