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Database: UniProt
Entry: I1HSJ8_BRADI
LinkDB: I1HSJ8_BRADI
Original site: I1HSJ8_BRADI 
ID   I1HSJ8_BRADI            Unreviewed;       328 AA.
AC   I1HSJ8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=100840196 {ECO:0000313|EnsemblPlants:KQK10198};
GN   ORFNames=BRADI_2g52600v3 {ECO:0000313|EMBL:KQK10198.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:KQK10198};
RN   [1] {ECO:0000313|EMBL:KQK10198.1, ECO:0000313|EnsemblPlants:KQK10198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK10198.1,
RC   ECO:0000313|EnsemblPlants:KQK10198};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQK10198.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK10198.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQK10198}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK10198};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
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};
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DR   EMBL; CM000881; KQK10198.1; -; Genomic_DNA.
DR   RefSeq; XP_003564415.1; XM_003564367.2.
DR   RefSeq; XP_010232462.1; XM_010234160.1.
DR   AlphaFoldDB; I1HSJ8; -.
DR   EnsemblPlants; KQK10198; KQK10198; BRADI_2g52600v3.
DR   GeneID; 100840196; -.
DR   Gramene; KQK10198; KQK10198; BRADI_2g52600v3.
DR   KEGG; bdi:100840196; -.
DR   eggNOG; KOG0800; Eukaryota.
DR   HOGENOM; CLU_034892_1_2_1; -.
DR   InParanoid; I1HSJ8; -.
DR   OMA; HDDAGQM; -.
DR   OrthoDB; 398710at2759; -.
DR   Proteomes; UP000008810; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR   PANTHER; PTHR15710:SF126; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   Pfam; PF14369; zinc_ribbon_9; 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|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          193..234
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          241..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   328 AA;  36144 MW;  445FC74C2574FA41 CRC64;
     MSNRPTHWCY ACRRPIRLRG EDIICPNCND GFIQEISEIG DTLNTYGIFG PSLEDRQDRR
     FGMMEAMSAI MRQQMAEMDS NPVFDIHGTQ GASTVPVRRP SIGPRLIFGS NMPADASESS
     GLNVFVRGGR RIGADRPNFS GFLVSPSLEA LFEQLLRQND STRHGPPPAP QSAIDSMPVV
     KINRRHLHDD PHCPVCTDKF EVGSEAREMP CKHLYHAACI IPWLVQHNSC PVCRHPLPPQ
     RGRSDNATST LPSTQHNEAA SSHGVTEADL GPVTRSDDGS SGSFSFLWPF GSSSSGPSSY
     QYEGGVGEPA VYDDDPSQIT YSEWHYDP
//
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