ID A0A0V1CHN1_TRIBR Unreviewed; 927 AA.
AC A0A0V1CHN1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=Wwp2 {ECO:0000313|EMBL:KRY48542.1};
GN ORFNames=T03_10401 {ECO:0000313|EMBL:KRY48542.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY48542.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY48542.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY48542.1};
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:KRY48542.1}.
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DR EMBL; JYDI01000204; KRY48542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CHN1; -.
DR STRING; 45882.A0A0V1CHN1; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 4.
DR Gene3D; 2.20.70.10; -; 3.
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; 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; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 4.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 4.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 4.
DR PROSITE; PS50020; WW_DOMAIN_2; 4.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 356..389
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 390..423
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 460..494
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 501..534
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 593..927
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 895
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 927 AA; 107676 MW; 0D05EA9C584E6273 CRC64;
MSAMAKPDVS AAIKHIFINS SMSTGNEFEK SKLSSKRNRK PKNTRIKPVR MKTLYHRHRI
IMVTSVVQII VADIKFNRIL LVSVVRLLFL IGIPTFLFLK RTFPVLIMDN SGYGWKCDAS
FVVHSGKLLE SNPPKRDTYL KVFIDDIRWF QSDICKQSSS PSWTLNFQSN DSKVRFRLIE
RRGEEEKIYG EGGIEISSLK SVVTNGKLKI SKMIVGIQKI GSMERIAEVK VSIRGNVVYI
YGKEDEGTCS KCEFGEEAPN ADGVRARGNA ESFSHSCRDR RLCCESYETP ALTTALDDCS
ALVTDLRVNE ELTEAPQRPW RRRQFHAAAT GQKAECESAD CTTDSSVHLV DEAVQQSLPA
GWEERLDGFG RRYYIDHNTM STTWERPINV PLPQGWELRY DPFGRVYYVD HNTRTTTWQR
PTQLMLQAHQ QWQSLRDEGH IRWQQRFLDS SHVNLLSNDA QLPEGWERRQ DPASGRFYYL
NHNTRTTQWE HPLQSNSLLS EALPPGWDTG YTSEGIQFFI DHNTRTTTYN DPRTGQPTPD
TFERINLSSQ SFSSKISRFR YKCMSNSLSN YVKISVSRDD VLEDSLSEVM RKNPIDLRRR
LFINFKGEEG LDYGGIAREW FFVLSHAILD PMYCLFEYSG KNKYNLEINP ASYVNPDHLK
YFKFVGRIVA MAFFHSKFIY NGFTMPFYKR MLGKRLTLED LESVDPEFYN SLKWIQENNV
DEADLGLYFT MDYNLLGEHL SDELKPGGKE IKLTEENKEE YLNLTVEWRF NRGIQEQTKA
FFDGFNEIFP IEWLKIFDER ELELLLCGIQ KIDIDDWERN TVYHHYTPAS KQIQWFWQFL
RSASNEQRAR MLQFVTGTCR VPVGGFAELM GSTGPQLFCI EKTGKEVWLP RSHTCFNRLD
LPPYRSYEQL CERLTRAIEE TEGFGND
//
