ID A0A072VLJ0_MEDTR Unreviewed; 1505 AA.
AC A0A072VLJ0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN OrderedLocusNames=MTR_1g066940 {ECO:0000313|EMBL:KEH42288.1};
GN ORFNames=MtrunA17_Chr1g0181721 {ECO:0000313|EMBL:RHN79838.1};
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:KEH42288.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:KEH42288.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:KEH42288.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH42288,
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:KEH42288.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:KEH42288.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH42288,
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:KEH42288}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH42288};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [4] {ECO:0000313|EMBL:RHN79838.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN79838.1};
RA Pecrix Y., Gamas P., Carrere S.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 0:0-0(2018).
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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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DR EMBL; CM001217; KEH42288.1; -; Genomic_DNA.
DR EMBL; PSQE01000001; RHN79838.1; -; Genomic_DNA.
DR RefSeq; XP_013468251.1; XM_013612797.1.
DR EnsemblPlants; KEH42288; KEH42288; MTR_1g066940.
DR Gramene; KEH42288; KEH42288; MTR_1g066940.
DR Proteomes; UP000002051; Chromosome 1.
DR Proteomes; UP000265566; Chromosome 1.
DR ExpressionAtlas; A0A072VLJ0; differential.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF10; E3 UBIQUITIN-PROTEIN LIGASE UPL4; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:RHN79838.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW Transferase {ECO:0000313|EMBL:RHN79838.1};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1164..1501
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1505 AA; 168020 MW; B5D99195F46CB5DA CRC64;
MGSRGQKRPE MVDELPADKR ACSSLDFRPS SSTASVQTDI SSTQSTMEPH DDMDTSSSAS
SHSEEEPEKD SADGSCDSDE MEHYHSTLHE YHRQRLSSDH GKFKTIISSL SGQTEPSGQL
AVLTELCEVL SFCTEGSISS MTSDLLSPLL VKLAKHESNP EIMLLSIRAI TYICDLYPRS
AGFLVRHDAV SALCQRLLTI EYQDVADQCL QALEKISREQ PLACLQAGAI MAVLNYIDFF
STSIQRVALS TVVNICKKLP SESPTPFMEA VPILCNLLLY EDRQLVENVA TCLIKIVDRV
SHSSEMSDEL CKHGLIQQVT HLLSVNGRAT LSQLIYNGLI GLLVKLSSGS VVAFRTLYEL
NISITLRDIL SAFDLSHGVS TSQLVGGHCN RVYEVLKLLN ELLPGLEKDL NNQLALDKES
FLANHPDLLQ KLGMDVFPML IQVFNSGASL SVCHGCLFVM YKFVCLTKSG MLVELLKNAN
ISSFLAGVFT RKDHHMIMLA LQIAEIILQN FSDIFLKLFI KEGVFFAIEA LLTPERSSKL
VYPSGIQLSL DSGQRSASRE VPKCLCYTFS TAQSPTSSET KKCKLDKDSV HYLAEHIKTK
YLAPELYDSE KGLTDILKNL RALSSDLLSM STDVGALTVH EEKINRVLDQ IMDKLIGKEE
VSTFEFIESG VAKALLNYLS LGHYMGENKG MHGVFGHNAV IEKRFEALAS ICLRTFQPLS
GDTPLSILIR NLLSALTSLE AFPIILSNVQ KMRNSFATVP NGCAVPYPCL KVRFVKEEKE
TCLSDCAEDF FTVDPFSSLH SIERYLWPKV SVKSAEDEKF SSSQVVLQPE SPPLQLPSNT
RSCVDEVPAI SERAGMSTDL CETQGEEPKT AHPRPDQAVN VNAGESSSGI QIAEQEMHFV
AEPDSKLGKE HPASCSNKAA DKLIFYLEGQ PLDHKLTLYQ AILGQIIKQN GSGVSAKLWS
HVHALTYRAA VKPEDIMPSD CHSSSQDFPH DKVLAFYQRT PFLSDMFYSE LVSDLEKSSP
TYDILFLLKS LEGMNRFIFH LMSRERMCAF AEGKVDNLDS LKITVPSVQL NEFVSSKLTE
KLEQQMRDSM AVCIGSMPFW CNQLMASCPF LFSFEARCKY FKLAAFGQPR IPHNNSETVN
DRRLSHGALP RKKFLVYRDR ILESATQMMK LHASHKVVLE VEYDEEVGTG LGPTLEFYTL
VCQELQKSGS GMWREDASSY TIKTNLQAEE TGIHSLYGLF PRPWLSTQDT SGGIQFSEVT
NKFFLLGQVV AKALQDGRVL DLHFSKAFYK LILGKELYLY DIQSLDPELG RVLHEFQALV
NRKFCLESVC EGNSELEQGL SFRDSRIEDL CLDFTLPGYP DIVLASGSDH TMVNMRNLED
YVSLIVDATV KSGISRQVEA FKSGFNQVFP IENLQIFYEE ELERILCGED DSWAINELAD
HIKFDHGYTA SSPPIVNLLE IIREFDHGQR RAFLQFVTGT PRLPPGGLAS LNPKLTIVRK
VYRFY
//
