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Database: UniProt
Entry: D7M129_ARALL
LinkDB: D7M129_ARALL
Original site: D7M129_ARALL 
ID   D7M129_ARALL            Unreviewed;       877 AA.
AC   D7M129;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=ARALYDRAFT_490058 {ECO:0000313|EMBL:EFH48920.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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   EMBL; GL348718; EFH48920.1; -; Genomic_DNA.
DR   RefSeq; XP_002872661.1; XM_002872615.1.
DR   AlphaFoldDB; D7M129; -.
DR   STRING; 81972.D7M129; -.
DR   EnsemblPlants; fgenesh2_kg.6__3192__AT4G12570.1; fgenesh2_kg.6__3192__AT4G12570.1; fgenesh2_kg.6__3192__AT4G12570.1.
DR   Gramene; fgenesh2_kg.6__3192__AT4G12570.1; fgenesh2_kg.6__3192__AT4G12570.1; fgenesh2_kg.6__3192__AT4G12570.1.
DR   eggNOG; KOG0940; Eukaryota.
DR   HOGENOM; CLU_002173_8_1_1; -.
DR   OrthoDB; 5480520at2759; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblPlants.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:EnsemblPlants.
DR   GO; GO:0010150; P:leaf senescence; IEA:EnsemblPlants.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:EnsemblPlants.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:EnsemblPlants.
DR   GO; GO:0009753; P:response to jasmonic acid; IEA:EnsemblPlants.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd16107; Ubl_AtUPL5_like; 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:UP000008694};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          102..178
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          536..875
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        843
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   877 AA;  100879 MW;  72B91DA832D1F8FF CRC64;
     MTLSRSSAAD STNNSNRSYS AVAGTDHKRK LDDYDASSSP DYVGVVDFLQ KMKKHEIDAD
     HMAASAQQTL ISWRSGENSG FNRSLSSSGE CSSSNRPEST RLQIFVRMMS GGKTIVIHAD
     KNDTVEKLHE RIEWKTKIPV SEQRVIYKGK QLQYEHSLAY YSIEQDASLQ LVGRMQSTEH
     PVAWQTIDDI MYTISRMYKG ENLQSNINEK IVTFFAMIPV ENDESIAKYL KIFSNSSVPA
     ALVMLYASSL ERNKSCAKSS VKLFLSSCVA LPKNQQNYCL PIVLEFCKIL RKVCPDQKLY
     VTCRNTLGSM LETFDNPRGV FNDGYSTFGV EIFPFFTELT GLLVNELVQN SGPSFCDFHK
     FSSFWQQLRK AIEFKDADSI PNVLPRRNTP LEAEIRHLHQ LFGSLLTTMD LCMCRVESDK
     EGGNSETVSS SWSQYLSILK IINSMSNIYQ GAKGQLTVML NKNKVSFCFL LVKFAKRGDD
     HQWVFEYKEA TNFEARRHLA MLLFPDVKED FEEMHEMLID RSNLLAESFE YIVGASPEAL
     HGGLFMEFKN EEATGPGVLR EWFYLVCQEI FNPKNTLFLR SADDFRRFSP NPASKVDPLH
     PDFFEFTGRV IALALMHKVQ VGVLFDRVFF LQLAGLKISL EDIKDTDRIM YNSCKQILEM
     DPVFFDSNAG LGLTFVLETE ELGKRDTIEL CPGGKFKAVN SENRKQYVDL LIERRFATPI
     FEQVKQFSRG FTDMLSDSIQ PRSFFKRLYL EDLDGMLRGG ENPISIDDWK AHTEYNGFKE
     TDRQIDWFWK ILKKMTEEEQ RSILFFWTSN KFVPVEGFRG LSSKLYIYRL YEANDRLPLS
     HTCFYRLCIP RYPTMTLMEQ RLRLIAQDHV SSSFGKW
//
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