RAD18_ASHGO
ID RAD18_ASHGO Reviewed; 443 AA.
AC Q75EN0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Postreplication repair E3 ubiquitin-protein ligase RAD18;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase RAD18 {ECO:0000305};
GN Name=RAD18; OrderedLocusNames=AAR049C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: E3 RING-finger protein, member of the UBC2/RAD6 epistasis
CC group. Associates to the E2 ubiquitin conjugating enzyme UBC2/RAD6 to
CC form the UBC2-RAD18 ubiquitin ligase complex involved in
CC postreplicative repair (PRR) of damaged DNA. {ECO:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with E2 UBC2, forming a complex with ubiquitin
CC ligase activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RAD18 family. {ECO:0000305}.
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DR EMBL; AE016814; AAS50414.1; -; Genomic_DNA.
DR RefSeq; NP_982590.1; NM_207943.1.
DR AlphaFoldDB; Q75EN0; -.
DR SMR; Q75EN0; -.
DR STRING; 33169.AAS50414; -.
DR EnsemblFungi; AAS50414; AAS50414; AGOS_AAR049C.
DR GeneID; 4618439; -.
DR KEGG; ago:AGOS_AAR049C; -.
DR eggNOG; KOG0287; Eukaryota.
DR HOGENOM; CLU_028491_2_0_1; -.
DR InParanoid; Q75EN0; -.
DR OMA; ERTQGGH; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000591; Chromosome I.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097505; C:Rad6-Rad18 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:EnsemblFungi.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:EnsemblFungi.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0042275; P:error-free postreplication DNA repair; IEA:EnsemblFungi.
DR GO; GO:0070987; P:error-free translesion synthesis; IEA:EnsemblFungi.
DR GO; GO:0042276; P:error-prone translesion synthesis; IEA:EnsemblFungi.
DR GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR GO; GO:0006513; P:protein monoubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039577; Rad18.
DR InterPro; IPR004580; Rad18_fungi.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14134; PTHR14134; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR TIGRFAMs; TIGR00599; rad18; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..443
FT /note="Postreplication repair E3 ubiquitin-protein ligase
FT RAD18"
FT /id="PRO_0000056151"
FT DOMAIN 270..304
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT ZN_FING 32..70
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 178..206
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 410..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
SQ SEQUENCE 443 AA; 49688 MW; C6FDA02392291ABC CRC64;
MSIQPGQVVT DPSDFAGTTI PELADLDSLL RCHICKDMLQ TPVLTQCGHT FCSLCIREYL
NKESRCPLCL AELRQNMLQK EFLVGELAAC YMELRARLLE TVRIPPKKVA EVVQNNSPIE
LDSDGEVEII ESCTGAVPGS KRGSPQVEEV EAAAKRQRTK QNGIQYMLQK KPKAVGEKVP
CPICNRLYNK EFLERVHLDE CLMMGTLRES GESDITVIEQ QSYTAEPDSK NSHVAERRGE
SPVDEVVTHK ESYLGSGLRV TKSRLPKLHF TSLSTSQLKQ KLSELGLPTA GSRQQMINRY
NHYELLWNSN FLDSIQPVGE GELRRSLLSW EATRNTDTPI SSGVSSSITN MLKTNNSAST
LLKSFKTDKF DKSAWSRLHG KEFRRLIRAA KKSMLEQDRG EAITAQNNEL STKASVDMES
TSFRNDTNDT IDTVTDEVHE DLK
