ID   A0A445DJD7_ARAHY        Unreviewed;       926 AA.
AC   A0A445DJD7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=Ahy_A04g021123 {ECO:0000313|EMBL:RYR63315.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR63315.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR63315.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR63315.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RYR63315.1}.
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DR   EMBL; SDMP01000004; RYR63315.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445DJD7; -.
DR   Proteomes; UP000289738; Chromosome a04.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
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:UP000289738};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          101..177
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   DOMAIN          555..895
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          65..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        861
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   926 AA;  104890 MW;  269E75D083B40252 CRC64;
     MPITQTTTAD SVFQLQRANH SSKRKLDDYG DEYGADAGAD FAGGDPEVAY AAGFLAGIKR
     EETKNASNSR YRGADARVSS STPSSSRAAQ YRSGSRSGSR LQFFVRMMSR GNTVVMQASP
     HDTVKSIHER IMVLTGIPVF EQGLTYRGKQ LQWENTLQEC GVQNDANLHL VGRMRSTEHP
     QAWQVLENMV SLVFRLCRGE IVHEATKVIK SLITSYMNMA PKVDDATASY FHIFIASNAP
     SMLVTLYVSP YAGNKERGDL FVRHFLNSCR NNMAKPYHGQ CASVVLELCS LLMRVGCDDP
     LYLHCRNTLG SMLESAGCCH VYAGKHGKGG GSILLQDICP FVRELSNRLL RDLELCIQRP
     NSSGPLQTDV SDFAAFLTPL RKGITQLQAM RGMGLDEKCH EGILLAEEVD YLHLIFIQML
     EKMEQCLRSM QEFLSDKLRR DRDVGLTYSG CSQYLSILKE LYQISKLYDG AEEKFWKVLM
     NQRSMLCILV IQYAKRSDDH QWILDHRSVT NFEVRRHLAM LLFPDVKEDY EELHEMLIDR
     SQLLAESYEY IAQAKPASLH AGLFMEFKNE EATGPGVLRE WFLLVCQAIF NPENALFVAC
     PNDCRRFYPN PASKVDPLHL KYFSFAGRVI ALALMHKVQV GIVFDRLFFK QLAGKCVTLE
     DIQAADPYLY SSCKQILEMD ADFIDSDALG LTFVREVDEL GHRKVVELCS GGKNLVVNSK
     NREKYVSLLI QNYFETSISE QVSHFAKGFG DILSNSRQQP FFFKSLELED LDWMLHGSES
     TISVEDWKAH TEYNGYKETD CQISWFWEIV GRMPAEQRKI LLFFWTSVKY LPVEGFRGLA
     SRLYIYRSME TEDRLPSSHT CFYRLCFPPY SSKAVMQDRL RIITQEHIGC SFGVGVGLGS
     SSPVTCKFGQ NHVQGATLPP FNLLGV
//