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Database: UniProt
Entry: I1HAS0_BRADI
LinkDB: I1HAS0_BRADI
Original site: I1HAS0_BRADI 
ID   I1HAS0_BRADI            Unreviewed;       329 AA.
AC   I1HAS0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=100837925 {ECO:0000313|EnsemblPlants:KQK24097};
GN   ORFNames=BRADI_1g78140v3 {ECO:0000313|EMBL:KQK24097.1};
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:KQK24097};
RN   [1] {ECO:0000313|EMBL:KQK24097.1, ECO:0000313|EnsemblPlants:KQK24097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK24097.1,
RC   ECO:0000313|EnsemblPlants:KQK24097};
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:KQK24097.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK24097.1};
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:KQK24097}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK24097};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC       subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC       ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC       form of a thioester and then directly transfers the ubiquitin to
CC       targeted substrates. It probably triggers the ubiquitin-mediated
CC       degradation of different substrates. {ECO:0000256|ARBA:ARBA00024004}.
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   -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC       {ECO:0000256|ARBA:ARBA00009119}.
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DR   EMBL; CM000880; KQK24097.1; -; Genomic_DNA.
DR   RefSeq; XP_003559018.1; XM_003558970.3.
DR   AlphaFoldDB; I1HAS0; -.
DR   STRING; 15368.I1HAS0; -.
DR   EnsemblPlants; KQK24097; KQK24097; BRADI_1g78140v3.
DR   GeneID; 100837925; -.
DR   Gramene; KQK24097; KQK24097; BRADI_1g78140v3.
DR   KEGG; bdi:100837925; -.
DR   eggNOG; KOG3002; Eukaryota.
DR   HOGENOM; CLU_040603_1_0_1; -.
DR   InParanoid; I1HAS0; -.
DR   OMA; SCSYAKW; -.
DR   OrthoDB; 3132375at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008810; Chromosome 1.
DR   ExpressionAtlas; I1HAS0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd16571; RING-HC_SIAHs; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR044286; SINL_plant.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR013010; Znf_SIAH.
DR   PANTHER; PTHR46632; E3 UBIQUITIN-PROTEIN LIGASE SINA-LIKE 4; 1.
DR   PANTHER; PTHR46632:SF35; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR   Pfam; PF21362; Sina_RING; 1.
DR   Pfam; PF21361; Sina_ZnF; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS51081; ZF_SIAH; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00455};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00455}.
FT   DOMAIN          148..206
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   329 AA;  35036 MW;  98E0D96C25515A8C CRC64;
     MAKFSFDDAD EDPPAAAAAG AGGDKRKREG SAAADGADGG GPPPTSKARN SAVVGGERDG
     RAVVGASCCE RRVDGDGEPG TGGISMRIDT DLLDCSICFE PLSPPLYQCQ NGHVACFSCW
     SRLSNKCHVC SHDAIFARNI ALEKIVESIK SSCAYAKWGC SKLVSYAQRS VHEEACLFAP
     STCPIPGCGY RGFTGCWSGH FLVDHSADCL HFTYGQSFEV NLAVSLPFLV LLGEDDHLFL
     LLNKNMMPFG HAFTVVCLRN GNLNWNFSYE IEAASRGNPG NCLRLKASVT NTKEWGGLHP
     AEAFLLVPYA FCSSANQTLS VSVARSASV
//
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