ID I1HLE2_BRADI Unreviewed; 404 AA.
AC I1HLE2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=BRADI_2g34430v3 {ECO:0000313|EMBL:KQK07305.1};
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:KQK07305.1};
RN [1] {ECO:0000313|EMBL:KQK07305.1, ECO:0000313|EnsemblPlants:KQK07305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK07305.1,
RC ECO:0000313|EnsemblPlants:KQK07305};
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:KQK07305.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK07305.1};
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:KQK07305}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK07305};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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DR EMBL; CM000881; KQK07305.1; -; Genomic_DNA.
DR AlphaFoldDB; I1HLE2; -.
DR EnsemblPlants; KQK07305; KQK07305; BRADI_2g34430v3.
DR Gramene; KQK07305; KQK07305; BRADI_2g34430v3.
DR eggNOG; KOG0802; Eukaryota.
DR eggNOG; KOG4638; Eukaryota.
DR HOGENOM; CLU_039460_0_1_1; -.
DR InParanoid; I1HLE2; -.
DR OMA; WIAIVND; -.
DR Proteomes; UP000008810; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:1904294; P:positive regulation of ERAD pathway; IEA:InterPro.
DR CDD; cd16532; RING-HC_RNFT1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR044235; RNFT1/2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR15860:SF32; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR15860; UNCHARACTERIZED RING FINGER-CONTAINING PROTEIN; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 130..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 343..381
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 51..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 404 AA; 45004 MW; A68785049B915D71 CRC64;
MDQPPHPPQP AVSEAAGGYA TRFSPAGLIH APLSALLEYS SGLLRAQATA GAHRGEAADR
EVSIRIVGPG GDAGPRAPGA GEVPPAADEE APAVRGDEAG AGSGRAESPY QGYDVQRVAR
WLDHALPFSL LLLGVFIRQH LQGFFVMIWI AAVMFKSNDI LRKQTALKGE RKMPMLIGIV
VVFIVHVFGV YWWYRNDDLV RPLMMLPPKE IPPFWHAIFF IAVNDTMVRQ AAMVVKCVLL
MYYKNSKGRH YRRQGQMLTV VEYSLLLYRA LLPAPVWYRF FLNKEYGGLF SSLTTGLYLT
FKVASLVEKV RWLLASLRAL SHKDLHYGAH ATTEQVLAAG DLCAICQEKM HSPILLQCKH
IFCEDCASEW LERERTCPLC RALVKPGDIR SFSDGSTTLF FQLF
//
