ID A0A453IKC9_AEGTS Unreviewed; 620 AA.
AC A0A453IKC9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 28.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET4Gv20595900.1, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET4Gv20595900.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|EnsemblPlants:AET4Gv20595900.1};
RX PubMed=29143815;
RA Luo M.C., Gu Y.Q., Puiu D., Wang H., Twardziok S.O., Deal K.R., Huo N.,
RA Zhu T., Wang L., Wang Y., McGuire P.E., Liu S., Long H., Ramasamy R.K.,
RA Rodriguez J.C., Van S.L., Yuan L., Wang Z., Xia Z., Xiao L., Anderson O.D.,
RA Ouyang S., Liang Y., Zimin A.V., Pertea G., Qi P., Bennetzen J.L., Dai X.,
RA Dawson M.W., Muller H.G., Kugler K., Rivarola-Duarte L., Spannagl M.,
RA Mayer K.F.X., Lu F.H., Bevan M.W., Leroy P., Li P., You F.M., Sun Q.,
RA Liu Z., Lyons E., Wicker T., Salzberg S.L., Devos K.M., Dvorak J.;
RT "Genome sequence of the progenitor of the wheat D genome Aegilops
RT tauschii.";
RL Nature 551:498-502(2017).
RN [4] {ECO:0000313|EnsemblPlants:AET4Gv20595900.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
RN [5] {ECO:0000313|EnsemblPlants:AET4Gv20595900.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|EnsemblPlants:AET4Gv20595900.1};
RX PubMed=34515796;
RA Wang L., Zhu T., Rodriguez J.C., Deal K.R., Dubcovsky J., McGuire P.E.,
RA Lux T., Spannagl M., Mayer K.F.X., Baldrich P., Meyers B.C., Huo N.,
RA Gu Y.Q., Zhou H., Devos K.M., Bennetzen J.L., Unver T., Budak H.,
RA Gulick P.J., Galiba G., Kalapos B., Nelson D.R., Li P., You F.M., Luo M.C.,
RA Dvorak J.;
RT "Aegilops tauschii genome assembly Aet v5.0 features greater sequence
RT contiguity and improved annotation.";
RL G3 (Bethesda) 0:0-0(2021).
CC -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part of E3
CC complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating
CC enzymes and then transfers it to substrates.
CC {ECO:0000256|ARBA:ARBA00003976}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC {ECO:0000256|ARBA:ARBA00005884}.
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DR RefSeq; XP_020148054.1; XM_020292465.3.
DR AlphaFoldDB; A0A453IKC9; -.
DR STRING; 200361.A0A453IKC9; -.
DR EnsemblPlants; AET4Gv20595900.1; AET4Gv20595900.1; AET4Gv20595900.
DR GeneID; 109733273; -.
DR Gramene; AET4Gv20595900.1; AET4Gv20595900.1; AET4Gv20595900.
DR OMA; VMTRMEC; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000015105; Chromosome 4D.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd22586; Rcat_RBR_ARI1-like; 1.
DR CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR FunFam; 1.20.120.1750:FF:000013; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045840; Ariadne.
DR InterPro; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR054694; Parkin-like_IBR.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22605; IBR_2; 1.
DR Pfam; PF21235; UBA_ARI1; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 133..347
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 137..185
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..26
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 70933 MW; 6064EA0DB758C36D CRC64;
MGSDAEEVSQ PASSPEYEQD DEDEDCYLSD QEDDALEESV LQVLEDGNLE DCHWSSSSVI
TKEYLLAAQR EDLRKVMELL GLKEHHARTL LIHYRWDVER IFELLDQKGR DRLFSEAGIP
LGTANNAGSP SATEVTCNVC YDDVPLTAAS HMDCGHNYCN ECWTEYFIVK INEGQSRRVK
CMAPKCNAIC DEALVRKLVS AKRPDIAERF ERFLLESYIE DNDTVKWCPS TPHCGNAIRV
KGDIHCEVEC TCGRQFCFNC SSEAHSPCSC VMWELWIKKC RDESETVNWI TVNTKPCPKC
HKPVEKNGGC NLVACICGQA FCWLCGGATG RDHTWSSISG HSCGRFTEDQ STRTEQARRD
LYRYMHYHNR YKAHTDSLKQ EAKLKRDIQW KISISENKES KIKDYSWVIN GLNRLFRSRR
VLSYSYPFAF YMFGDEIFKD EMTPEERELK QNLFEDQQQQ LEFNVERLSG FLEKDFQNFS
DEEVMDTMKH VINLSNVVDR LCKQMYQCIE NDLLYPLRTP HNIAPYKSKG LDRASELHIC
LDSAEQSSPS MKCSQDEHKS QLGLCSESGS SLTGKRPIIQ MHGSSSDNSG RPSHKRERRD
AHGGGALFDL NVPAEVADKI
//
