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Database: UniProt
Entry: G7KEX0_MEDTR
LinkDB: G7KEX0_MEDTR
Original site: G7KEX0_MEDTR 
ID   G7KEX0_MEDTR            Unreviewed;       782 AA.
AC   G7KEX0; A0A0C3XDA4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 2.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=11412831 {ECO:0000313|EnsemblPlants:AES94989};
GN   OrderedLocusNames=MTR_5g020570 {ECO:0000313|EMBL:AES94989.2};
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:AES94989.2, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:AES94989.2, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES94989.2}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES94989,
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:AES94989.2, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES94989,
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:AES94989}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES94989};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; CM001221; AES94989.2; -; Genomic_DNA.
DR   RefSeq; XP_003612031.2; XM_003611983.2.
DR   AlphaFoldDB; G7KEX0; -.
DR   PaxDb; 3880-AES94990; -.
DR   EnsemblPlants; AES94989; AES94989; MTR_5g020570.
DR   GeneID; 11412831; -.
DR   Gramene; AES94989; AES94989; MTR_5g020570.
DR   KEGG; mtr:11412831; -.
DR   OrthoDB; 458417at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000002051; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd16664; RING-Ubox_PUB; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR045210; RING-Ubox_PUB.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23315; U BOX DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23315:SF240; U-BOX DOMAIN-CONTAINING PROTEIN 5; 1.
DR   Pfam; PF05804; KAP; 1.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00185; ARM; 4.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:AES94989.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          287..361
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          246..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..751
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   782 AA;  88264 MW;  A89A090F8DC502B6 CRC64;
     MFFPCLICSC RTLLLMRTNS GEIVETFPNT LSFQVHSKIC IELMKIVDSI MRIFPDIEEA
     RPRCSSGIES LCFLNNSIEK AKLLLQHCSE CSKLYLAVTG ETVLSRCQKA KKSLEQSLIP
     IQGMVPVMLA VEVSRIIDDL EYATFVLDFA EEEAGRVVRE LLHQGSTSDS VDDFEVKALQ
     FAAPRLNITS QKAILIERRS IKKFLDKVGP NDPKKKTILR YLMYLMKKHG NLMVVGEHME
     NFYSRSEEPI ARDNSSRDSR RRNRVESHHS MNYDQNKTEM NQSDRVAPPE EYKCPISSRL
     MHDPVIIASG VTYERMWIRK WINEGKTICP KTEKELPHMT LTPNIVMKDL ISKWCKNNGV
     TIPDPSRHTE DFMLLDASIT SIKSLGSYFN DLNLPMDLTN MSLGSLDNSF SSDVSRVKTN
     HALNLMMTKS NENSHPHKDT VHAEIHDTDL MLLPQLHDLQ WDSQCKVIED LKDHMKSNSQ
     AILSVSAENL VEPVVRFLSN ANDRHDLKAL RAGTQLLSEF VNNCRSGMAD LSEDTFIKLA
     NLLDSEVIGD VLAIMEELSG DGNSKAKIAA SSALTSVLKL LDSDNKGCQQ HAIRIIYNLS
     FNSEVCPHMV SVNCIPKLLP FFKDRAVLRY CIYILKNICD TEEGRNSIAE TKGCISSIAE
     ILESGSNEEQ EHALDVLLSL CTCSQNVDYC KLILDEDVIT PLFYISQNGN DKGKESALEL
     LHILRDAKYV ENEDRSSQPI TNNSSTDSNS HPEENRSSKK SQFLKKLGLF SKSTPHASKP
     RR
//
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