GenomeNet

Database: UniProt
Entry: Q2HT46_MEDTR
LinkDB: Q2HT46_MEDTR
Original site: Q2HT46_MEDTR 
ID   Q2HT46_MEDTR            Unreviewed;       826 AA.
AC   Q2HT46; A0A0C3UZD7; G7IM25;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 93.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=11406418 {ECO:0000313|EnsemblPlants:AES64476};
GN   OrderedLocusNames=MTR_2g025790 {ECO:0000313|EMBL:AES64476.2};
GN   ORFNames=MtrDRAFT_AC150798g3v2 {ECO:0000313|EMBL:ABD32998.1};
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:ABD32998.1};
RN   [1] {ECO:0000313|EMBL:ABD32998.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Town C.D.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABD32998.1}
RP   NUCLEOTIDE SEQUENCE.
RG   The International Medicago Genome Annotation Group;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AES64476.2, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES64476.2}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES64476,
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   [4] {ECO:0000313|EMBL:AES64476.2, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES64476,
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   [5] {ECO:0000313|EnsemblPlants:AES64476}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES64476};
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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
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; AC150798; ABD32998.1; -; Genomic_DNA.
DR   EMBL; CM001218; AES64476.2; -; Genomic_DNA.
DR   RefSeq; XP_003594225.2; XM_003594177.2.
DR   AlphaFoldDB; Q2HT46; -.
DR   STRING; 3880.Q2HT46; -.
DR   PaxDb; 3880-AES64476; -.
DR   EnsemblPlants; AES64476; AES64476; MTR_2g025790.
DR   GeneID; 11406418; -.
DR   Gramene; AES64476; AES64476; MTR_2g025790.
DR   KEGG; mtr:11406418; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   HOGENOM; CLU_002173_8_1_1; -.
DR   OrthoDB; 948916at2759; -.
DR   Proteomes; UP000002051; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   CDD; cd00078; HECTc; 1.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 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   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   PANTHER; PTHR11254:SF424; E3 UBIQUITIN-PROTEIN LIGASE UPL5; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          45..120
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          508..826
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        792
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   826 AA;  94458 MW;  C531CC40E71A4659 CRC64;
     MSSITKTIAG GCFHQQSING ATADHLSNHS PELKFNDTKT TSSELQFFVR MMWKCNTIVI
     HASREDTVES ILQQISSKTK IPIEYQRLIY NGKQLQQQQS LSQCGIENDA NLQLVGQLRS
     IGRSVVWNSA DDIVSMILNL CRGESLNGAS MIIHNHFAKY MNNFEYFYFF KLMKIPSLLV
     ALYMSPFACN KNIADFSIES FIEICLDLKC KKLQGFYLEI LLDFCELLRG VGFTCDEPLY
     VSCRDGFGNL LTLVGGVPIN NPNMKVLLRG VVDCVHEIAD ELLMYLDLSM NWDTAKGISY
     KVVLDFVKFC GPLRMGFAEE QATSDESLNY DICYEEDPLF SGVPDQLHIV FIKLLSKMDE
     CLQVMEDCLV NKEQGKGDVI HNGWSHYLII LKELFHISKF YSGAQEKFWG LLLHRKNVLP
     HMIVRYVKKT DDHQWLLENK IVTDFESRRH LALMLFPDSK DEISGYEMLI DRSQVLAESF
     EYMSRAKAKS LQGGIFMAFK NEKATGPGVL REWFVLVCRE IFNPKNALFV ACPNDHRRFF
     PNAASKVNSL HLKYFIVSGR IIALALKKKV HVGIVFDRVF FKQLAGNYII TLEDIRDADP
     IMYSSCKQIL EMDADYIDSD ALGLTFSTEV EELGHRELIE LCPGGESLVV DSKNREKYVH
     LLIQNRFVTS ISKQVSHFAE GFADILSCSR LEFFQFLDLE DFDLMLHGSE NAISVEDWKV
     HTKYHGYKEN DHQISWFWKI VGRMSAEQKK VLLFFWTSVK HLPVEGFRGL SSTLLISKSS
     KPDNHLPSSH TCFYKLCFPP YSSMAIMQDR LGIITQEHIS CSFGTA
//
DBGET integrated database retrieval system