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Database: UniProt
Entry: G7JPH6_MEDTR
LinkDB: G7JPH6_MEDTR
Original site: G7JPH6_MEDTR 
ID   G7JPH6_MEDTR            Unreviewed;       580 AA.
AC   G7JPH6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   18-JUN-2025, entry version 69.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   OrderedLocusNames=MTR_4g075010 {ECO:0000313|EMBL:AES89443.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:AES89443.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:AES89443.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES89443.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES89443,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:AES89443.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES89443,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:AES89443}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES89443};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   EMBL; CM001220; AES89443.1; -; Genomic_DNA.
DR   RefSeq; XP_003607246.1; XM_003607198.1.
DR   AlphaFoldDB; G7JPH6; -.
DR   STRING; 3880.G7JPH6; -.
DR   PaxDb; 3880-AES89443; -.
DR   EnsemblPlants; AES89443; AES89443; MTR_4g075010.
DR   eggNOG; KOG1815; Eukaryota.
DR   HOGENOM; CLU_470428_0_0_1; -.
DR   OMA; CLCYHSF; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000002051; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd20346; BRcat_RBR_ANKIB1; 1.
DR   FunFam; 3.30.40.10:FF:000019; RBR-type E3 ubiquitin transferase; 1.
DR   Gene3D; 1.20.120.1750; -; 2.
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; IPR001878; Znf_CCHC.
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; 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; 4.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS50158; ZF_CCHC; 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:UP000002051};
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:PRU00047}.
FT   DOMAIN          81..301
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          85..130
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          212..225
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
SQ   SEQUENCE   580 AA;  67695 MW;  61654A83849A55CC CRC64;
     MEQHFYVLSE SDIKRLQDAD INHLSSILFV SRPVACLLLS HYNWNVTQAS ESWFDNQQKV
     RNAIGLSNET HIELGLAYSS HTLICGICLE IFSSEAIRSS WCRHSFCINC WNQYVDTHID
     DHNCFKLKCP EPSCNAAVDE DMIQQLASES RKIKYDQFFF RSYVENNNNM KLKWCPAPDC
     CNAISYELPY HHGSSSSRIN YDVTCLCYHS FCWNCGEEAH TPVDCEIVAK WMKKTSSEFK
     ITTNGWIIAN TKRCPKCKTP IEKNNGCNHM SCKCGIQFCW LCLRDFSNCR DGVNCAYTYY
     HQGWANNEIS RKKSGTNFGN FMVKDALKHI VECRRILRWS YVYGYYLPED ENAKIEFFDH
     IQSIAQVVLD RLHHFAENGL RKQLLHNGSE EEFCDFRTKL TTRARVAKSY FMNLVKELDN
     GLEVVCVKNY AVMAFSWQLL LRRLPTRRNL VNLGMGVELS CMWSVVPNLR SLLVVGLLPT
     QNHVLNHMTC KCGFQFCWLC LHSPCICNGS NRLQQVQEFQ EIFGNEKKGS STYLNFKDAW
     KQVIECRRVM RWSYVYEYYL PEDENAKIEF FDHIQLGFKY
//
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