ID A0A183E349_9BILA Unreviewed; 479 AA.
AC A0A183E349;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN ORFNames=GPUH_LOCUS15390 {ECO:0000313|EMBL:VDN25908.1};
OS Gongylonema pulchrum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Spiruroidea; Gongylonematidae; Gongylonema.
OX NCBI_TaxID=637853 {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0001541101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:GPUH_0001541101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN25908.1, ECO:0000313|Proteomes:UP000271098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates.
CC {ECO:0000256|RuleBase:RU369009}.
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; UYRT01082375; VDN25908.1; -; Genomic_DNA.
DR WBParaSite; GPUH_0001541101-mRNA-1; GPUH_0001541101-mRNA-1; GPUH_0001541101.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000050760; Unplaced.
DR Proteomes; UP000271098; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
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; 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; 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 SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000271098};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU369009}.
FT DOMAIN 219..258
FT /note="WWE"
FT /evidence="ECO:0000259|Pfam:PF02825"
FT REGION 357..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 51788 MW; 1ABFF4A8190AE3BD CRC64;
MEGLRSSNEL SQAEAAAELA EMLLLGNEES LPNLPIKDII HALIALLQKE HNFELLKRIE
CIDVAEQSLM ALEVMSKRNG KTIMQAGGIA ATISHVDFFS VPSQRLAFQI AANCATYVTA
NDFPQVRDSL ADLTQRLLVE DKRCLESVCV LFCRLVDNMR NHVDKLREIA GQNHALLKNV
QQLLIVQPCA VGPNTFQALV RMLRTMASKC SDLAVALIAF NTSETDISLQ INGNVYKIDL
QRMVQQNQVT GKERPIQRRA PACYSNGPAL RYESLRVTLR MIYPAEVSIL KSILATLPLA
GPIASALACP RGKDLCVVAS ALQLTHILLN KFPDIYISLF RREGVAHEIE KLSRMKLESP
VSLPPVQSSP AVLSAEQDVA ASSSRTRGSP KTRTTSEQGA AATAAAPSIT KQSAVIAARS
RNNTQAAPAG SSSSSSSSSE AGPSSSSATR VIVSPSGGRH RRKASPESKG DRQQLETDD
//