GenomeNet

Database: UniProt
Entry: A0A067QMT5_ZOONE
LinkDB: A0A067QMT5_ZOONE
Original site: A0A067QMT5_ZOONE 
ID   A0A067QMT5_ZOONE        Unreviewed;       295 AA.
AC   A0A067QMT5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367115};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU367115};
GN   ORFNames=L798_00852 {ECO:0000313|EMBL:KDR09510.1};
OS   Zootermopsis nevadensis (Dampwood termite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Termopsidae; Zootermopsis.
OX   NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR09510.1, ECO:0000313|Proteomes:UP000027135};
RN   [1] {ECO:0000313|EMBL:KDR09510.1, ECO:0000313|Proteomes:UP000027135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KDR09510.1};
RX   PubMed=24845553; DOI=10.1038/ncomms4636;
RA   Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA   Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA   Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA   Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA   Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA   Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA   Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA   Liebig J.;
RT   "Molecular traces of alternative social organization in a termite genome.";
RL   Nat. Commun. 5:3636-3636(2014).
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; KK853239; KDR09510.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067QMT5; -.
DR   STRING; 136037.A0A067QMT5; -.
DR   EnsemblMetazoa; KDR09510; KDR09510; L798_00852.
DR   eggNOG; KOG0824; Eukaryota.
DR   InParanoid; A0A067QMT5; -.
DR   OMA; WQYDQRT; -.
DR   OrthoDB; 2881299at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000027135; Unassembled WGS 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; -; 1.
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; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 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   Reference proteome {ECO:0000313|Proteomes:UP000027135};
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          29..67
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          85..161
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   REGION          203..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..271
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   295 AA;  32865 MW;  414067FE8865393A CRC64;
     MAESRPIEGN ESDKRTLGIE NIGSSILECA VCLQSCVHPA QLPCGHIFCF LCVKGVANQS
     KKCAMCRHEI PADYFEKPVL VAQNNTEKDI AELDDGYQWF YEGRNGWWQY DERTSRELEA
     AYKKGERMCE LLVAGLLYIA DFDAMLQIRR NDPSRRRRIK RDLSTIPKKG VAGLRFEGYQ
     QATEDQVEEE VRPKSPVLQV TADGAMTPTP VPPTNTPQTP AGGAVSGDTT PDRQESLHRA
     VEQIRSLSLR DDVSASDGSD EDERGSGDEH QELPDFSGVV PSPWVLTFSS DEDQL
//
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