ID A0A0M5J1J4_DROBS Unreviewed; 615 AA.
AC A0A0M5J1J4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367115};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367115};
GN ORFNames=Dbus_chr3Lg2302 {ECO:0000313|EMBL:ALC45136.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC45136.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC45136.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC45136.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU367115};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|RuleBase:RU367115}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514, 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 EMBL; CP012525; ALC45136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M5J1J4; -.
DR SMR; A0A0M5J1J4; -.
DR STRING; 30019.A0A0M5J1J4; -.
DR OMA; QSGDNHQ; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000494163; Chromosome 3l sequence.
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:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd16546; RING-HC_RNF146; 1.
DR Gene3D; 3.30.720.50; -; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR044110; RING-HC_RNF146.
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; 2.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00678; WWE; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF117839; WWE domain; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW Transferase {ECO:0000256|RuleBase:RU367115};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU367115};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687};
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 139..177
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 333..411
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 66835 MW; E175EFA65AB0F80E CRC64;
MSQQGDNASK TSKKNTSHGQ EDINAIINLD EDEDEEVQFV GVVRPPSVID LIDLSVSPST
SQAAAAAAAG GAGDSLKTPD SETDASESSS GVTALNPQVI VVDPTAVAPA EAAAAVPTAA
ATAASASAGA APVAPALECP ICLQTCIHPA RLPCGHIFCF LCVKGVAYKN RRCAMCRREI
PAEFLDHPQL VNGIDDICTT RATEDGYQWY YEGRNGGWWA YDARTNEDIE TAYQAYETHK
KTAPAAPVAA PNAVRQRPFC SCHLHMDISS ESDDELEVSS QEFNESELQD ITEGINMELE
GWSTDSSSDF ELEYGDNANE PGHLHQLICG QLYIINMIDM TQSPRSDPSR KRKIMRWWQY
DDRTSQDLEE AFKKGEHSCT ILVAGYVYIV DLELLIQQRQ NEPARCRRVK RDLATIAKKG
VAGLRIEGNQ VTCDTDFNRP PQNNTATVQR LINTFAARDA ALRIASDIIS STIAQADELS
LGLAASNISD SANDLSNGEQ SQTNPLQSTR QQTTGHGLGH STSRSLASSH SSSIQDLMLI
ATTDLLDSTE EIIENNQHTL DLFEQAINDF QALTASQRRR FADSSDEEDP PPGNARRGRQ
GGLEASEPDN ERLGF
//
