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
//