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Database: UniProt
Entry: M1CQN8_SOLTU
LinkDB: M1CQN8_SOLTU
Original site: M1CQN8_SOLTU 
ID   M1CQN8_SOLTU            Unreviewed;       794 AA.
AC   M1CQN8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=102600294 {ECO:0000313|EnsemblPlants:PGSC0003DMT400072624};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400072624, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|Proteomes:UP000011115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400072624}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400072624};
RG   EnsemblPlants;
RL   Submitted (JUN-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};
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DR   RefSeq; XP_006339124.1; XM_006339062.2.
DR   AlphaFoldDB; M1CQN8; -.
DR   STRING; 4113.M1CQN8; -.
DR   PaxDb; 4113-PGSC0003DMT400072624; -.
DR   EnsemblPlants; PGSC0003DMT400072624; PGSC0003DMT400072624; PGSC0003DMG400028257.
DR   GeneID; 102600294; -.
DR   Gramene; PGSC0003DMT400072624; PGSC0003DMT400072624; PGSC0003DMG400028257.
DR   KEGG; sot:102600294; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   HOGENOM; CLU_002173_8_1_1; -.
DR   InParanoid; M1CQN8; -.
DR   OMA; YLEIFIS; -.
DR   OrthoDB; 5480520at2759; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; M1CQN8; baseline.
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:SF418; E3 UBIQUITIN-PROTEIN LIGASE UPL5-LIKE; 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:UP000011115};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          4..80
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          455..794
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   ACT_SITE        760
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   794 AA;  91196 MW;  B5CD9FBFFEAD1702 CRC64;
     MNRIHFFVRL FSGGKTLVVQ ADSTNRVEVI HQKISLITGI PISVQSLIYR GKQLQSDQMI
     SDCGIEMESN LQLVGRLRST KHSRAWKLMN ELSSIIWGFC KTEFRSVRYD KDHIEDVLIE
     ILIMIPHDID EASEYLEIFI SSSVPAALVM LYMSSRLDNK TLADKCIRQI INSFKSESLT
     PMYSTCAIML EFCKILREAG IEDDLYIFCR SSFCDIIELV GIARCKADMK KFISLQDVLP
     FVREIVAQLH HNLNLTMEST DLSLPCSLVH DFAAFMLPVR NAILFQVPFD FTITFPLMEN
     DTGEAEYYRE SIECLHCSFH GLLEATLLSL GLLETQLGLK EEVEDARVVQ WWSLYLTILK
     ELNNISKVYT GLEKVFWQKM RQVKASLCFL VVKFATKSED YGWLFEHKEV MSFEVRRHLA
     IMMLPEVGDG GGLYCMFIDR SRLLENSFEY IGNATPKNLQ GCLFIKFKHE EATGPGVLRE
     WFLLVCQAMF NPQNALFVAC PNDRRRFFPN SASKVNPLHL NYFCFSGRMI ALTLMHKVQI
     GVVFDRTFFL QLAGKDITLE DVRDADPPFY KSCKEILEMD PEMVDGDNLG LRFICDVESM
     GSRKGIELCP NGKDTIVDSK NREKYINLLI KHYFVTSVAE QVACFAKGFA DITTTSRHQP
     LFRCLNLEDL DLMLDGSGND ISVEDWKAHT DYSGYKKSDR QISWFWKIVE CMSVEQRNAL
     LFFWTSIKFL PPNGFAGLSS RLYIHRSSTP YDHLPTSQTC FNCLRFPPYK SESIMQDRLH
     IITQEHIGCS FGTS
//
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