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Database: UniProt
Entry: E3KGV4_PUCGT
LinkDB: E3KGV4_PUCGT
Original site: E3KGV4_PUCGT 
ID   E3KGV4_PUCGT            Unreviewed;       297 AA.
AC   E3KGV4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Blue (type 1) copper domain-containing protein {ECO:0000259|Pfam:PF00127};
GN   ORFNames=PGTG_08715 {ECO:0000313|EMBL:EFP83529.2};
OS   Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS   (Black stem rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP83529.2, ECO:0000313|Proteomes:UP000008783};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CRL 75-36-700-3;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA   Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA   Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA   Schein J.;
RT   "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT   700-3.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRL 75-36-700-3 / race SCCL
RC   {ECO:0000313|Proteomes:UP000008783};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602387-1};
CC       Note=The crystal structure with reduced Cu(1+) has also been
CC       determined. {ECO:0000256|PIRSR:PIRSR602387-1};
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DR   EMBL; DS178286; EFP83529.2; -; Genomic_DNA.
DR   RefSeq; XP_003327948.2; XM_003327900.2.
DR   AlphaFoldDB; E3KGV4; -.
DR   STRING; 418459.E3KGV4; -.
DR   EnsemblFungi; EFP83529; EFP83529; PGTG_08715.
DR   GeneID; 10532211; -.
DR   KEGG; pgr:PGTG_08715; -.
DR   VEuPathDB; FungiDB:PGTG_08715; -.
DR   eggNOG; ENOG502S40X; Eukaryota.
DR   HOGENOM; CLU_1058218_0_0_1; -.
DR   InParanoid; E3KGV4; -.
DR   OrthoDB; 1383464at2759; -.
DR   Proteomes; UP000008783; 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; IPR002387; Plastocyanin.
DR   PANTHER; PTHR34883:SF15; PHYTOCYANIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34883; SERINE-RICH PROTEIN, PUTATIVE-RELATED-RELATED; 1.
DR   Pfam; PF00127; Copper-bind; 1.
DR   PRINTS; PR00157; PLASTOCYANIN.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
PE   4: Predicted;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|PIRSR:PIRSR602387-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602387-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008783};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..297
FT                   /note="Blue (type 1) copper domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003173883"
FT   DOMAIN          52..151
FT                   /note="Blue (type 1) copper"
FT                   /evidence="ECO:0000259|Pfam:PF00127"
FT   REGION          21..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..37
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         139
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602387-1"
FT   BINDING         142
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602387-1"
FT   BINDING         147
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602387-1"
SQ   SEQUENCE   297 AA;  31158 MW;  7BD15946FC32AC8E CRC64;
     MSKLFHFLLV FVTWASIVSP LSSQGPPPPP PEKKTNPGQP SNIPQGKNFV IKVGNEEAAK
     IFSPATIQAQ VGDMVTFEFH PKAHTVAQAS FDKPCEVLAS PEGNGFNSGK QTVELKTPNS
     NLPRWTMQIT KPETIWFYCD PHCGLGMVGA INPPTSGEKT FEKYVENSKK AGSKPKNLRA
     GSAAAPGDPA LRLGENPGDK NAGRLADKAG GQTTDLAGAK PGGQSGTLQR GPPKTANEVA
     TLNANSASVD GKDPSTLASK GKDGGSGAAS YFMEKRRAIL SSVSLSMILP GVLTTIY
//
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