ID   RAD18_CANGA             Reviewed;         411 AA.
AC   Q6FPI4;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=CAGL0J03586g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380956; CAG60809.1; -; Genomic_DNA.
DR   RefSeq; XP_447860.1; XM_447860.1.
DR   AlphaFoldDB; Q6FPI4; -.
DR   SMR; Q6FPI4; -.
DR   STRING; 5478.XP_447860.1; -.
DR   EnsemblFungi; CAG60809; CAG60809; CAGL0J03586g.
DR   GeneID; 2889701; -.
DR   KEGG; cgr:CAGL0J03586g; -.
DR   CGD; CAL0133446; CAGL0J03586g.
DR   VEuPathDB; FungiDB:CAGL0J03586g; -.
DR   eggNOG; KOG0287; Eukaryota.
DR   HOGENOM; CLU_028491_2_0_1; -.
DR   InParanoid; Q6FPI4; -.
DR   OMA; ERTQGGH; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0097505; C:Rad6-Rad18 complex; IEA:EnsemblFungi.
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:0006513; P:protein monoubiquitination; IEA:EnsemblFungi.
DR   Gene3D; 1.10.720.30; -; 1.
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; IPR036361; SAP_dom_sf.
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..411
FT                   /note="Postreplication repair E3 ubiquitin-protein ligase
FT                   RAD18"
FT                   /id="PRO_0000056154"
FT   DOMAIN          256..290
FT                   /note="SAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT   ZN_FING         27..65
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         186..214
FT                   /note="UBZ4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   REGION          209..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          385..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   BINDING         205
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
SQ   SEQUENCE   411 AA;  46771 MW;  7F1772CE58665798 CRC64;
     MDVLTSAADF KKSKVPQLQE LDDLLRCHIC KDFLKNPVLT PCGHTFCSLC IRGYLSNEPK
     CPLCLHELRE SMLRSEYLVN EITETYKAAR QRLLDELNSL ETNQDNSVIE VVSDKEPSLL
     QIDDDVNENS NHITVNDTSD IIDEDNEIQI TGTKRTARTI LNGSRPTKAA KISDMFTTRK
     AKTEEKAPCP ICSQLFPIRY LERTHLDECL TKPPTSSPPI KQSRLSPKPS ESVSHVKRYL
     NSTNTSTQQR LPKLNFAKMT TSQLKQKLAS LSLPVSGTRA NMVARYNYYE MLWNSNFIDS
     INPVSESELR RQLMSWDASH NGNNNSSNGG TNTISQLMKM NSKNKGKEYE KLLKDFKKDS
     FDKKGWMLLH KNSFNRLLCD AKKTRRKTEN ETLMTSQSPR ESSTQTELSA T