ID A0A2S6CFH5_9PEZI Unreviewed; 646 AA.
AC A0A2S6CFH5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Plastocyanin-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CBER1_05606 {ECO:0000313|EMBL:PPJ58492.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ58492.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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:PPJ58492.1}.
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DR EMBL; PNEN01000455; PPJ58492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6CFH5; -.
DR STRING; 357750.A0A2S6CFH5; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000237631; Unassembled WGS sequence.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000237631}.
FT DOMAIN 86..198
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 233..399
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 502..617
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 646 AA; 72971 MW; 96E2EDCBF5C6E59B CRC64;
MEDKIEAVPF ISQEKSSKQR NAAPNLLLGL ACGLVLLDLG TRWIGSHRDV LPQWHSQRKG
CDLPSTPIAE VREPGVVEYT LTLSQAWRNP DGSWWRPMFV GNSETPFETI HAQEGDIVKI
HMFNELQLPW AIHWLGLDSG SETWNDGSAG VTTYPLLPRA NRTAVFNTTG QWGLKRCLDH
VSVPSVEGNY GTMWIRPSPN RERPYSVISD DKQDVQDMLE AEARPHPVTV YNYQHRQAAG
LIAQLRAEGH DPYCFQSVLI NGKGRVHCKP PQLDELDGKP LDTYGCVPQA SGAVGHGECK
PSNGDYEIIH TDNRRWILLQ FTNTGFEHVW RISIDNHKMW IVANDGGFVQ PQEVDVLHLI
DADTIHVMVR LDQPARDYAI RFYSYSKMQS IQGFAYLRYP HRRMGQTIGE PMPQPELEDG
PVKLDGTVKK GFVLEEVDKL APFTPVKPDQ KADLTLRLKA TGAPDPVNPF VTNCSLNGAP
WQLFREFMEP VALHVKEQSS EPEPIIRNLP LGSVVDIILE NDLPVDLPFY KHNNPTFKIG
SGQGKYPYKS VAEGLKKSDT KKSFNLENPT YGYMHELPAG GWLALRWKIN KPAATMFTVY
KVRYFIQGMQ VALLEGDDAP WPELPKDQRE LPHVDFPIPP RRGIFD
//
