TRUL_CAEEL
ID TRUL_CAEEL Reviewed; 451 AA.
AC P90990;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=E3 ubiquitin-protein ligase trul-1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q6NRV0};
DE AltName: Full=Traip ubiquitin ligase 1 {ECO:0000303|PubMed:30849395, ECO:0000303|PubMed:31545170};
GN Name=trul-1 {ECO:0000303|PubMed:30849395, ECO:0000303|PubMed:31545170,
GN ECO:0000312|WormBase:B0432.13};
GN ORFNames=B0432.13 {ECO:0000312|WormBase:B0432.13};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=31545170; DOI=10.7554/elife.48686;
RA Sonneville R., Bhowmick R., Hoffmann S., Mailand N., Hickson I.D.,
RA Labib K.;
RT "TRAIP drives replisome disassembly and mitotic DNA repair synthesis at
RT sites of incomplete DNA replication.";
RL Elife 8:0-0(2019).
RN [3]
RP FUNCTION.
RX PubMed=30849395; DOI=10.1016/j.molcel.2018.12.021;
RA Deng L., Wu R.A., Sonneville R., Kochenova O.V., Labib K., Pellman D.,
RA Walter J.C.;
RT "Mitotic CDK Promotes replisome disassembly, fork breakage, and complex DNA
RT rearrangements.";
RL Mol. Cell 73:915-929(2019).
CC -!- FUNCTION: E3 ubiquitin ligase that acts as a key regulator of DNA
CC repair in response to replication stress (PubMed:31545170,
CC PubMed:30849395). Acts by mediating ubiquitination of the CMG helicase
CC complex, promoting the unloading of the CMG helicase complex by the p97
CC ATPase (cdc-48.1 or cdc-48.2) (PubMed:31545170, PubMed:30849395).
CC {ECO:0000269|PubMed:30849395, ECO:0000269|PubMed:31545170}.
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:0000250|UniProtKB:Q6NRV0};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q6NRV0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BWF2}.
CC Chromosome {ECO:0000250|UniProtKB:Q6NRV0}.
CC -!- SIMILARITY: Belongs to the TRAIP family. {ECO:0000305}.
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DR EMBL; BX284602; CCD61945.1; -; Genomic_DNA.
DR PIR; T25457; T25457.
DR RefSeq; NP_740965.2; NM_170969.4.
DR AlphaFoldDB; P90990; -.
DR SMR; P90990; -.
DR STRING; 6239.B0432.13.2; -.
DR EPD; P90990; -.
DR PaxDb; P90990; -.
DR EnsemblMetazoa; B0432.13.1; B0432.13.1; WBGene00015194.
DR EnsemblMetazoa; B0432.13.2; B0432.13.2; WBGene00015194.
DR GeneID; 173412; -.
DR UCSC; B0432.13.2; c. elegans.
DR CTD; 173412; -.
DR WormBase; B0432.13; CE40596; WBGene00015194; trul-1.
DR eggNOG; KOG0827; Eukaryota.
DR eggNOG; KOG3020; Eukaryota.
DR HOGENOM; CLU_025087_0_0_1; -.
DR InParanoid; P90990; -.
DR OMA; GHIYHHG; -.
DR OrthoDB; 761263at2759; -.
DR PhylomeDB; P90990; -.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00015194; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0090734; C:site of DNA damage; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0031297; P:replication fork processing; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromosome; Coiled coil; DNA damage; DNA repair; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..451
FT /note="E3 ubiquitin-protein ligase trul-1"
FT /id="PRO_0000451421"
FT ZN_FING 13..54
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 270..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 96..130
FT /evidence="ECO:0000255"
FT COILED 209..243
FT /evidence="ECO:0000255"
FT COMPBIAS 414..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 51444 MW; 4D09549CA851128A CRC64;
MTSQPTSSLQ GSCSICFEDL KQNDKISAIV CGHIYHHGCI SQWIATKRQC PSCRRTVPKN
GFVEKLFFDV QRMGGEAEKP PEIDYREEHY KLSTSLKVEQ EKLGTLNTEN KNLKDTVKSL
EKKIIREKDK YRQEIPKLQA TINHLTISSE ETAYLKRELQ ESKNRLKTCE FYKILTVHSS
EADKQLGEYL KKNGNLDTEK FFQLMKSTNK DLTDKRREAA KEIEQLKMEV QSLKRAAQED
AAIKKTLKKT VLDLRERANV DTPINNKRLR DVLETETPPP AKRKSMGFDE SSQMIDPDGE
LSFFKQNENR TPVTSVPSTS KAVLPFNFDD DEDDEYFKTP KIAEKKKKLP EAMAPVSEDS
FDFDIAVPQS IINRIPAKTT AQPAKKYPKI PNLSAKTSSK PTEAPKTENV LKIKSKSQEI
AQKPQKSTRI SSFFSRTTSS TSNLTEYVIL D
