ID A0A453HCZ7_AEGTS Unreviewed; 533 AA.
AC A0A453HCZ7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 02-APR-2025, entry version 24.
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:AET4Gv20145100.1, 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:AET4Gv20145100.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|EnsemblPlants:AET4Gv20145100.1};
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:AET4Gv20145100.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
RN [5] {ECO:0000313|EnsemblPlants:AET4Gv20145100.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|EnsemblPlants:AET4Gv20145100.1};
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 AlphaFoldDB; A0A453HCZ7; -.
DR STRING; 200361.A0A453HCZ7; -.
DR EnsemblPlants; AET4Gv20145100.1; AET4Gv20145100.1; AET4Gv20145100.
DR Gramene; AET4Gv20145100.1; AET4Gv20145100.1; AET4Gv20145100.
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; cd16773; RING-HC_RBR_TRIAD1; 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; 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 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 127..335
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 131..181
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..24
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 60738 MW; 82F8AAA663BC7A4B CRC64;
QRRRVLPLLR RGHDEEEDGL EADEDDVGLF EDAAPQPEHR ADHWAITRKS LSAAQQQDVS
MVMNLVNLER HNARALLMHH RWKMDRIHDF LERRGREGLF REAGIVVPPE DSSTAARARV
PPHKRPRTVT CNVCFEDVSR PSDVSTMDCG HCFCNDCWTE HFFASLGNGK KHIHCMQVKC
PAICDDGTVR RLLGRKYPDA AKRFDNLVLD SYLDNNASVK WCPSAPHCGR AIRVVDASER
YCEVECPCGV SFCFNCAAPA HSPCPCPMWD KWDAKFRGES ENLKWIAVNT KSCPKCLRPI
EKNGGCNHVS CPCGQHLCYA CGGRLDSLHN CNRYDEAGHA NYDSIRRQML RYTHYCDRFN
VHINSRKVEQ TELWPAIQKR AVLLESATAI RPLIREASWM ARAHRALLAS RLVLARSYAF
AYYMFGDEVR TYPSEKANLP IAKVLFEDQQ WQLEENAEKL SKVLAAEAKP VLAEEEVLRA
MQETSNLAKI VDTHCREMYK CIQDELLPLL LEPMTIAPYR PDGPDKAKDL PAP
//
