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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//