ID A0A0V0VBG0_9BILA Unreviewed; 821 AA.
AC A0A0V0VBG0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE Flags: Fragment;
GN ORFNames=T09_146 {ECO:0000313|EMBL:KRX60677.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX60677.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX60677.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX60677.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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:KRX60677.1}.
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DR EMBL; JYDN01000056; KRX60677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VBG0; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd04033; C2_NEDD4_NEDD4L; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 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; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF443; E3 UBIQUITIN-PROTEIN LIGASE NEDD-4; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 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; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 8..129
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 202..235
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 339..372
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 394..427
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 488..820
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 261..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 788
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX60677.1"
SQ SEQUENCE 821 AA; 94864 MW; 63FEF80CB08D9C5D CRC64;
LLIYRIEVMS ETRIYGLPES AQGRTKILRI LVVRGIDLAK KDIFGASDPY VSVHLCQQGR
EVDKVHTKTI KKTLYPVWNE EFLFRVDPSN CKIVFEVFDE NRITRDDFLG IVEIDLQTVR
IPKERTGRDI REKNCLLRPR SLKSRVRGEL RLALSYLSDP NSEDELDTAE TEADSDSGDW
EMLPASSRAG LLAESPTAQQ IPPLPSGWEE RIDANGRTFY VNHTNRTTQW ERPSNSNLHI
ASRPDDLWLK QRSCFQQRWD ENKLENRGIP SSSGPSTSAA TTSRATSSST VQDELSQLQI
ALSNNYNLQN RHVHSAPSLE TDSDWQEIGL LSEEDDGNGP LPLNWQVQVA PNGRKFFIDH
NTKTTTWIDP RTGKPTKLPE RKTYRPKHQC DELGPLPSGW EERVHVDGRV FFIDHNTKTT
QWEDPRFYNP QIAGPAVPYS RDYKRKYEYF RAHLIKPENV PSKFDMHIRR DHVFEDSFRA
IMSVTTSRAD VLKAKLWIEF DGEANYGGVA REWFFLLSHE MFNPYYGLFE YSAMDNYTLQ
INPNSGLCND DHLSYFRFVG RVMGIALHHG KLLDAFFIRP FYKMMLGKPI CLNDMESVDS
EYYNSLLWIE DNDPSELELR FVVDEEVFGV TQTRELKPGG ADILVTNDNK NEYINLVIKW
RFVSRVTDQM NALMSGLNEF IMQNLLTIFD PHELELLMCG LQKIDVKDWK DNTLYKGGYN
ANHPVIQNFW KCVLSFDNEM RSRLLQFVTG TSRVPMNGFR ELYGSNGLQK FTIEKWSTPE
MLPRAHTCFN RLDLPPYTSY QDLKDKLVKA IENSASFEGV D
//
