ID A0A453LM39_AEGTS Unreviewed; 595 AA.
AC A0A453LM39;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 27.
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:AET5Gv20839600.1, 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:AET5Gv20839600.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|EnsemblPlants:AET5Gv20839600.1};
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:AET5Gv20839600.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
RN [5] {ECO:0000313|EnsemblPlants:AET5Gv20839600.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|EnsemblPlants:AET5Gv20839600.1};
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_020169908.1; XM_020314319.1.
DR AlphaFoldDB; A0A453LM39; -.
DR STRING; 200361.A0A453LM39; -.
DR EnsemblPlants; AET5Gv20839600.1; AET5Gv20839600.1; AET5Gv20839600.
DR GeneID; 109755399; -.
DR Gramene; AET5Gv20839600.1; AET5Gv20839600.1; AET5Gv20839600.
DR OMA; CTLAVEY; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000015105; Chromosome 5D.
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; cd22583; Rcat_RBR_ARI7-like; 1.
DR FunFam; 1.20.120.1750:FF:000027; 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; IPR048962; ARIH1-like_UBL.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF22191; IBR_1; 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; PS00518; ZF_RING_1; 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}.
FT DOMAIN 171..383
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..81
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..595
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 66407 MW; E5081789812AD16D CRC64;
MALTSDNEEE YYSSPEEAEE AGDDDDRMSF RTASNESDND AGAGDDADDD CLYGDSDGDG
DDGMYDEYEG DEEEGLEEVD EEGGVLDEMR FTATQYAVLT MDEVRARQEE HTARVADLIA
LPPALAAAVL RHFKWSAQGV WERWFSDEHK VRDAVGLPAD GDAVSVAVND APLTCYICFD
AHGPGEMRSA GCAHFYCRGC WSGYVRAAVG DGARCLSIRC PDMGCSAAVV RDLVDDVADA
DDAKRYGEFL VRSYVEESKR LRWCPAPGCD RAVEFDGEKC TVQLDAWCAC GHGFCLACGE
EAHRPVACDT VREWLDKNRS DSETAQWVLA NTKHCPECRR PIEKNQGCMH MTCSPPCKHQ
FCWLCLGPWG KHDGGNYNCN TYNAARAEGK YTKEELRRAQ AKASVDRYLH YYERWGAHER
SRQKALEDTA ALGKDGAQRE AVAAAFGVVE TELDFLEEAY RQVAECRRML RWTYAFGYYV
DDPAKRDLFE DLQSQADKSL ERLHECAEKD RTSLVAEAAG EHGAVADKYL EFRPRLSSLT
AVARNHFENM ARAFRDGLAE VEVDPAVAAR RAAATPPPPP LDDDDDEDFF EELRM
//
