ID A0A0M3HSB0_ASCLU Unreviewed; 232 AA.
AC A0A0M3HSB0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367115};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367115};
OS Ascaris lumbricoides (Giant roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0000532801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ALUE_0000532801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase that specifically binds poly-ADP-
CC ribosylated proteins and mediates their ubiquitination and subsequent
CC degradation. {ECO:0000256|RuleBase:RU367115}.
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=2.3.2.27; Evidence={ECO:0000256|RuleBase:RU367115};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU367115}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|RuleBase:RU367115}.
CC -!- DOMAIN: The WWE domain mediates non-covalent poly(ADP-ribose)-binding.
CC {ECO:0000256|RuleBase:RU367115}.
CC -!- PTM: Ubiquitinated; autoubiquitinated. {ECO:0000256|RuleBase:RU367115}.
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DR AlphaFoldDB; A0A0M3HSB0; -.
DR WBParaSite; ALUE_0000532801-mRNA-1; ALUE_0000532801-mRNA-1; ALUE_0000532801.
DR Proteomes; UP000036681; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0072572; F:poly-ADP-D-ribose binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:InterPro.
DR Gene3D; 3.30.720.50; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR033509; RNF146.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR13417:SF2; E3 UBIQUITIN-PROTEIN LIGASE RNF146; 1.
DR PANTHER; PTHR13417; UNCHARACTERIZED; 1.
DR Pfam; PF02825; WWE; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS50918; WWE; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|RuleBase:RU367115};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367115};
KW Transferase {ECO:0000256|RuleBase:RU367115};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU367115};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367115};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 27..66
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 113..193
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 232 AA; 26208 MW; 88C673948B010547 CRC64;
MAMEPKPLRV KSSSAASKDE TNGSEDCSIC CQPYTFKATL PDCGHSFCFL CIKGVARRHG
VCPLCRKPIF AGIFRDPILT TEDNSAAEPS CSQAVLDKSS LKDCSIEEKE ESKEEVPQSD
EKSAARWFYQ ARHGGWWRYE QRQEHDIEKA FLKGDRQIEL LIAGYTYCIN FSDRCQYRKD
LGRSPHWERA VKRVEGDELD GEIRGIAGLR TPSNDVSTHQ ITASISKVQL HD
//
