ID A0A0L9TW72_PHAAN Unreviewed; 1428 AA.
AC A0A0L9TW72;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=LR48_Vigan02g095000 {ECO:0000313|EMBL:KOM34800.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM34800.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
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}.
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DR EMBL; CM003372; KOM34800.1; -; Genomic_DNA.
DR STRING; 3914.A0A0L9TW72; -.
DR EnsemblPlants; KOM34800; KOM34800; LR48_Vigan02g095000.
DR Gramene; KOM34800; KOM34800; LR48_Vigan02g095000.
DR OMA; FESRCAE; -.
DR Proteomes; UP000053144; Chromosome 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1061..1403
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 730..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1389
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1428 AA; 161608 MW; E833F16B4B6F85CD CRC64;
MERHENYFDE KFERAAQNLS KETEPSSQLA LLIEICGVLP VCSKDIVSHS LDLLSPLLVD
HAKKKSNPDI MLFSLRAITF VCDLHPPGLE FFVEHDFVPT LCESLFAIQY VDVAEQCVIV
LEKISLRRPL VCLKAGVVMA VLNHIDFFST DVKRVALSTM VNLCKKLPSE SPLPFLEAAP
ILCNLLGYED HKLVENVATC LIKIVDSVYQ SSELLDELCK HGLIQQVTLL LSSSAQTTLS
ELTYYGLVGL LVKLSSRSFV AFRKLYELNI SSTLIDILST FELTNEVSMS QQIGGNCNWV
NEVLKLLNEL VPDRTKDQND QLVVDKESFL DNHSDLLQRL GMDVFPMLIK MLNCGASLYV
WHGCLSVMYK IVRLSKSGVH DELLKNVNIS SFLAEVFTQK DQHMLMLALQ IAEIILQKFP
DDFLILFLKD GVYFAIDSLV RQEKRTTKLY PVNCGIQSDF SQKSATRQAL KCLCYAFSSG
HSSTSSEVRK CKLAKNSVFD LAEHIKTTYF VRELYHSQTD ALQNLRTLSN DLLSMSTDNG
VLSVHEEMTK SILYQIMDKL TGKEQVSISE FIESGVLKSL ADYLSQGRYM RNNMGIHDVF
KDDAVIKKRF ETLATVCLFA SQPLSCEKTL SVFIRNLQTA LTSLETFPVI LSSGLQLRGS
YVTVPKRRHL PYPSLNVCFI KVEGEDSLNE YSNGSARFIC TVDPFSSQHS IEGFLRPKLG
SKSTEHAGSS SIHALWQPET SPQSPLSSST VPVEIPVSLG HTDMMTDLPE TQGYDEELQM
NIGPNPEQKK CEPARCSSEA TQKVVLYYEG QRMDHKSTLY QEILRHALRQ NDPFSSLKLW
TKMHKITFRT AVENEDIIPP QCHSSPQDSS DDNVLAYCEH TPFFSDLLSG ELVTDLEKPS
PTYDILFLLK SLEKINRIIF HLMSRERIYA FAKGNIGDLD SLKITVPCIP QNEFVNTKLT
EKLEQQMRDP LAVSIGAIPS WCNQLMASCP FLFGFEARCK YFKLEVLSQS QAQPGWSYNG
SGSMSGLRVS PGELPSKIFF IHRNQILEST AKMMKVHGNN KSVLLVKYNG EVGSGLGPTL
EFYTLVCHEF QKPGLGMWRE EVNLQVEETR IRSFHGLFPR PWLRDTSGGI HFSEVEKKFF
LLGQVVGKAL QDGRILDFHF SKAFYKLILG KELSLYDIQS FDPELYVVLQ EFQALVMRKK
YMESINERNS DIVSFRDQRI EDLCLDFTLP GYPDIVLASG TDRSMVNMRN LEDYVSLIVN
ATVRSGISRQ VKAFQSGFNQ ILPIERIQIF NEEELERVFC GESDSWAIND LEHQIIFHHG
YTARSPPIVN FLEILREFDH EQKRAFLQFV TGAPRLPLGG LASLSPMLTI VRKHSNHHPD
TDLPSVMTCV NYLKLPPYSS KRVKDLFIFR DSTPCTGRFL SYKDAVLG
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