ID A0A1I7XFG1_HETBA Unreviewed; 606 AA.
AC A0A1I7XFG1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
OS Heterorhabditis bacteriophora (Entomopathogenic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heterorhabditidae;
OC Heterorhabditis.
OX NCBI_TaxID=37862 {ECO:0000313|Proteomes:UP000095283, ECO:0000313|WBParaSite:Hba_16065};
RN [1] {ECO:0000313|WBParaSite:Hba_16065}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) 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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00104}.
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DR AlphaFoldDB; A0A1I7XFG1; -.
DR WBParaSite; Hba_16065; Hba_16065; Hba_16065.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000095283; Unplaced.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd14358; UBA_NAC_euk; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR044034; NAC-like_UBA.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF429; E3 UBIQUITIN-PROTEIN LIGASE SU(DX); 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF19026; HYPK_UBA; 1.
DR Pfam; PF00397; WW; 3.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 3.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 4: Predicted;
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 10..127
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 179..201
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 240..274
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 280..313
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 365..446
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 68733 MW; 07412ECB821618A7 CRC64;
MARNESSLLP SGSSSTSLQQ NGVPKQVKIN VKVSSAKLHS SGGILSKPAD SYVEVGVEDT
AVLKKTAVKK KSNNPEWDET VSIPVLESSS ITFRVMNKSK LFEDTLIAQS TLKVSSVPKS
EHGDLNPTAI SLQLNGKDNS RVGTLKVSLS GNIDRKRRSA GNIIILKMYS CCNNLYYRDP
RGRVYYVDHN TRTTTWQRPT ADMLEAHEQW QSGRDQAMHQ WEQRFLLQAN SLTASDDPLG
PLPEGWEKRA DPHTGRVYFV NHVNKTTQWE DPRTQGISDQ PLPDGWEMRF TEQGVPFFID
HSNKSTTYND PRTGKPVGPL GVYGVSMTFE RTFRWKIAQF RYLCLITVSR ANVFEDSFQE
ITRKNAVDLR RRLYIQFRGE EGLDYGGVAR EWFFLLSHEV LNPMYCLFMY AGNSNYSLQI
NPASFVNPDH LKYFEYIGRF IAMVCYISKC YMSDLYLAFQ IFYYSRVTAE TWSARLKLIS
RKKRLRRRSV GIRSFYDDFL LNISLKVVTD DGSDDSDDEA PGLEGELTEE QKRVAEAAGL
GDQVDKQAKQ SRSEKKDDGV DEDATGIEEK DIELVMSQAN TSRNKAVRAL RASDNDIVNA
IMSLTM
//
