ID A0A183ID27_9BILA Unreviewed; 1374 AA.
AC A0A183ID27;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN ORFNames=SBAD_LOCUS1521 {ECO:0000313|EMBL:VDO94606.1};
OS Soboliphyme baturini.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Dioctophymatida; Dioctophymatoidea; Soboliphymatidae; Soboliphyme.
OX NCBI_TaxID=241478 {ECO:0000313|Proteomes:UP000050793, ECO:0000313|WBParaSite:SBAD_0000159201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SBAD_0000159201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO94606.1, ECO:0000313|Proteomes:UP000270296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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 ECO:0000256|RuleBase:RU369009};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU369009}.
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|RuleBase:RU369009}.
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DR EMBL; UZAM01006852; VDO94606.1; -; Genomic_DNA.
DR WBParaSite; SBAD_0000159201-mRNA-1; SBAD_0000159201-mRNA-1; SBAD_0000159201.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000050793; Unplaced.
DR Proteomes; UP000270296; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.720.50; -; 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; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS50918; WWE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000270296};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU369009}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1349..1369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 515..591
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT REGION 104..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1374 AA; 154159 MW; 6CF87CD45A26EDC4 CRC64;
MICLRKLGKR NLSVICYGRC AYLLDYLVSG YFIREMRFML VRILFAFDIT LRSSTDIRPF
RGAEFHISPV SGKQLQAHSS TSKRNTIGAA VAASSISSKK ADLQDMENRL MNRRRNRKSK
VPQKSDITAS STAGPAASPA VNDDVDKSSS RVPYPQLIPL NNLFINLGPR MQNMLHRYPF
SSSISRIEEL VQLLQKSQDP SVQLQSLIEL CNILVMINEE TTLGHNFPHQ DVVRALIRLI
QAENNFDIMN HACRALTYLM DASPRITPLA TEAIPYLLEK LQRVECIDVA EQALAALELL
SRRHAKHILN AGGINACLLY IDFLSLASQR SALQIVANCC LQLSSNDFNC VGDSLPMLSQ
RLNSQVIKSY IFSEEFLDKK SVEIACVAFT RMVENFLPVP DKLSRVCEYG LLESICQLVS
FTLLLMTPPI LGGSCTVAVI RMLHLLCRHC PMLATQLVRL NITNAISHFL VDDADQSSFN
NELSLRTSQE LHEVVLLISE LMPALPMDEQ FEVSSLLKPC SSSCTPPIWG WKDERGIWRP
YAADDNELIE EAYQAKHDEY SLSAWGQNFT LDFLNKVQIN DDTGQSSPIQ RKHSGRTSDA
AKASDDPRCD LIASKDLLFK ELVSVLFPLV YEIYSSTCGR SLRNECLRTM LRMLYHCDAK
LLNEVTQKIP ICSLIACKIG SGELTSVVPA LQLTKVLIDK LPNVFILHFQ REGVAHELQN
LAVKYADLRS LALSSLSSSG PLGSRAGSSL SSSTPPSTAT TSTALLPSSN VADXXXXXXX
RFVVYGSTRL LFLEFVSVIV ITCVTDRGQS RIRVSPSVRC RGALRSGTVK GRRKSSPDVN
GSTDLSSAVP RSSNSVCRQK ASSSSTYDNK VAMLYHHFPL HRHQSNHLTD SLLSSLPRWV
RCSSNASRGD DVRPLYVPEP PVRVLDSPLL LSNRSEPFAL SVKNHEKVVT WIGNFVQNLL
KNYFYNFDVN EAAIFGRGQS VLQKLCQTSD LLKKGQVGLV ETSAIRSLVE VLQSDITCFE
IMQSDLVGAM YNFLTKYESE DDKVKRLKTF CSQFYGVKVR VTSACVYLCG FAVTADKDGV
PTVHLNEVVT GKILIAKLIS CIGQLEQFPV STHDLAWSPQ GSLRGVSALR FLHSQQLKCH
PMRHPTDKSL RQWKRGTIKI DPLAQISTLE KYMVAKGYAR VKSGRQEDSS DDGDCDTTDE
EANYLAELPE GQHRIQFMMK DEVLPYDMTI YQAVRQYGVM PTTIRTDEAT LSEWVVPDIW
MHTHSIWYRA YREPRKPLYN WRSMDFTGKQ RGRNKLSDKQ PSSNSSDSEF CEPTSMLDEY
IHYELPEEIN DPSAGCLKLL RVLFGLCRYW WTLFQVLCVC VCVFLLVAYG KAKY
//
