ID I1LJH7_SOYBN Unreviewed; 532 AA.
AC I1LJH7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN Name=ARI7 {ECO:0000313|EMBL:AGL44351.1};
GN ORFNames=Glyma11g12920 {ECO:0000313|EMBL:AGL44351.1}, GLYMA_11G121300
GN {ECO:0000313|EMBL:KRH29522.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH29522};
RN [1] {ECO:0000313|EMBL:KRH29522.1, ECO:0000313|EnsemblPlants:KRH29522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH29522};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH29522.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EMBL:AGL44351.1}
RP NUCLEOTIDE SEQUENCE.
RA Chen P., Zhang X.L., Zhao T.J., Li Y., Gai J.Y.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KRH29522}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH29522};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KRH29522.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH29522.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JX392393; AGL44351.1; -; mRNA.
DR EMBL; CM000844; KRH29522.1; -; Genomic_DNA.
DR RefSeq; XP_006590909.1; XM_006590846.2.
DR AlphaFoldDB; I1LJH7; -.
DR EnsemblPlants; KRH29522; KRH29522; GLYMA_11G121300.
DR Gramene; KRH29522; KRH29522; GLYMA_11G121300.
DR HOGENOM; CLU_009823_2_0_1; -.
DR OMA; HRFCMIC; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008827; Chromosome 11.
DR ExpressionAtlas; I1LJH7; baseline and differential.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR CDD; cd22586; Rcat_RBR_ARI1-like; 1.
DR CDD; cd16773; RING-HC_RBR_TRIAD1; 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; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685:SF371; E3 UBIQUITIN-PROTEIN LIGASE ARI2-RELATED; 1.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF21235; ARI1_UBAl; 1.
DR Pfam; PF19422; Ariadne; 1.
DR Pfam; PF01485; IBR; 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 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
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 116..330
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 120..168
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 532 AA; 61460 MW; ED0CD12D46574284 CRC64;
MDVYASSDED YHYDSDHEDS VEAYENDENY ALLSSKGTTT KVITKESLLA AQKEDLRRVM
DMLSVREQHA RTLLIFHRWD VENLFEVLVD KGKSFLFAEA GVSVDEHRNS DSPVPPAFMC
YICMEEVPSS KTTRMDCGHC FCNGCWIEHF IVKINEGQSK RIRCMEHKCN SICDDAVVRT
LLSREHPHMA EKYERFLLES YIEDNKRVKW CPSTPHCGNA IRVEDDELCE VECSCGVQFC
FSCLSEAHSP CSCLMWELWA KKCRDESETV NWITVHTKPC PKCHKPVEKN GGCNLVSCIC
GQAFCWLCGG ATGREHTWSS IAGHSCGRYK EQEKTAERAK RDLYRYMHYH NRYKAHTDSF
KIESKLKETI QGKIAISEEK DSTLRDYSWV NNGLSRLFRS RRVLSYSYAF AFYMFGDELF
KDEMTDAQRE IKQNLFEDQQ QQLEANVEKL SKILEEPFET FSDDKVVEIR MQILNLSTII
DKLCQKMYEC IENDLLGSLN LGIHSIAPYK SKGIERASEL SVGWNNKVNN TV
//
