ID I1J3E6_BRADI Unreviewed; 348 AA.
AC I1J3E6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=SIAH-type domain-containing protein {ECO:0000259|PROSITE:PS51081};
GN Name=100843005 {ECO:0000313|EnsemblPlants:PNT62148};
GN ORFNames=BRADI_5g26310v3 {ECO:0000313|EMBL:PNT62148.1};
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|EMBL:PNT62148.1};
RN [1] {ECO:0000313|EMBL:PNT62148.1, ECO:0000313|EnsemblPlants:PNT62148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT62148.1,
RC ECO:0000313|EnsemblPlants:PNT62148};
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:PNT62148.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:PNT62148.1};
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:PNT62148}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:PNT62148};
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}.
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DR EMBL; CM000884; PNT62148.1; -; Genomic_DNA.
DR EMBL; CM000884; PNT62149.1; -; Genomic_DNA.
DR RefSeq; XP_003579487.1; XM_003579439.2.
DR AlphaFoldDB; I1J3E6; -.
DR STRING; 15368.I1J3E6; -.
DR EnsemblPlants; PNT62148; PNT62148; BRADI_5g26310v3.
DR EnsemblPlants; PNT62149; PNT62149; BRADI_5g26310v3.
DR GeneID; 100843005; -.
DR Gramene; PNT62148; PNT62148; BRADI_5g26310v3.
DR Gramene; PNT62149; PNT62149; BRADI_5g26310v3.
DR KEGG; bdi:100843005; -.
DR eggNOG; KOG3002; Eukaryota.
DR HOGENOM; CLU_060441_0_0_1; -.
DR InParanoid; I1J3E6; -.
DR OMA; CENNGHI; -.
DR OrthoDB; 387406at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008810; Chromosome 5.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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:SF17; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF21361; Sina_ZnF; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 4: Predicted;
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 165..223
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 348 AA; 39461 MW; B5503C82BE66BABF CRC64;
MEMRSVKRMR SSPTDTESSR SPSPYRRSSS PSPSPYRSPS PSPCRSWSRR PRSYDDADGE
DRSLSRSRGS DGNDAQGRAV WRPHSCRQSG ERGHGGEFSV RIDDYDRLFT CRSCHRLLTP
PVYQCPFSHV TCSRCHIEFG DNRCSSCGAS NGYARNRIVE EFLGRISFSC RNKEYGCTTF
LPQHEVHVHE QSCRHEPCYC PVDRCGFAGP TNAVEAHLTG FHHWRVIKFR YGESFIASAH
KSTIYHSKDD SELFLIDSVG EGRGIAMSMI CLRCDNAREQ EFTYELKAPP GNVRGQHQLQ
LQSVVRRTSL RKGLGEKDKV FLLVPKDLLC AMNDYVVEVC VRKEDTGA
//
