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Database: UniProt
Entry: E3KC85_PUCGT
LinkDB: E3KC85_PUCGT
Original site: E3KC85_PUCGT 
ID   E3KC85_PUCGT            Unreviewed;       266 AA.
AC   E3KC85;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=PGTG_08270 {ECO:0000313|EMBL:EFP82021.1};
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:EFP82021.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; DS178280; EFP82021.1; -; Genomic_DNA.
DR   RefSeq; XP_003326440.1; XM_003326392.2.
DR   AlphaFoldDB; E3KC85; -.
DR   STRING; 418459.E3KC85; -.
DR   EnsemblFungi; EFP82021; EFP82021; PGTG_08270.
DR   GeneID; 10534389; -.
DR   KEGG; pgr:PGTG_08270; -.
DR   VEuPathDB; FungiDB:PGTG_08270; -.
DR   HOGENOM; CLU_1046392_0_0_1; -.
DR   InParanoid; E3KC85; -.
DR   OMA; DASNMAT; -.
DR   OrthoDB; 901818at2759; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR047134; RNF4-like.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23041:SF78; E3 UBIQUITIN-PROTEIN LIGASE RNF4; 1.
DR   PANTHER; PTHR23041; RING FINGER DOMAIN-CONTAINING; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008783};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..266
FT                   /note="RING-type E3 ubiquitin transferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003173430"
FT   DOMAIN          185..244
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          39..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   266 AA;  27972 MW;  0AC988DC32910213 CRC64;
     MHPLFQLAGS LTVVHLISGS STMAHSTASC SSGSDTELDL WAEFPDAGGD GPSENKPRIG
     QDGPSENKPS TGQPADQPLD TPHRIKRSSS TEETAIDPIP HKSSEKRARE PDDQDKSNDR
     PLKIQSTSSH SPQTQKPSKS SPMNPKSSPI NPKNSPMNPK SSPINPPAAT KNEDSDSQSL
     GNLTCAICLS APSPAVVTKC GHVTCGECLA SSIVSQHNSS YGVFPPFLQP VGARINNGQC
     PVCRAPLVGG WGTAMRGVIL KVRKAP
//
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