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Database: UniProt
Entry: RAD18_YARLI
LinkDB: RAD18_YARLI
Original site: RAD18_YARLI 
ID   RAD18_YARLI             Reviewed;         344 AA.
AC   Q6CHI1;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   11-DEC-2019, entry version 105.
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=YALI0A08580g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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}.
DR   EMBL; CR382127; CAG83807.1; -; Genomic_DNA.
DR   RefSeq; XP_499880.1; XM_499880.1.
DR   SMR; Q6CHI1; -.
DR   EnsemblFungi; CAG83807; CAG83807; YALI0_A08580g.
DR   GeneID; 2905883; -.
DR   KEGG; yli:YALI0A08580g; -.
DR   InParanoid; Q6CHI1; -.
DR   KO; K10627; -.
DR   OMA; NANCDSK; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001300; Chromosome A.
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:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR   GO; GO:0006513; P:protein monoubiquitination; IBA:GO_Central.
DR   GO; GO:0009411; P:response to UV; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR039577; Rad18.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR040539; Znf-WRNIP1_ubi.
DR   InterPro; IPR006642; Znf_Rad18_put.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR14134; PTHR14134; 2.
DR   Pfam; PF18279; zf-WRNIP1_ubi; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00734; ZnF_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..344
FT                   /note="Postreplication repair E3 ubiquitin-protein ligase
FT                   RAD18"
FT                   /id="PRO_0000056160"
FT   DOMAIN          197..231
FT                   /note="SAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT   ZN_FING         28..67
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         146..174
FT                   /note="UBZ4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
SQ   SEQUENCE   344 AA;  39535 MW;  AAB59CEEADF4D4F7 CRC64;
     MNSDIPDPSD WIDSKLSGLK DVDETLRCHI CKEFFTAPMI TGCGHTFCSL CIQRYLTNTS
     QRCPTCMQEQ QISQLRKNVT VETLVEHFSA QRATILRVVK EAAKQPIPEV VEPPSSPDLD
     DGRRRSGRKR TRTNYTETLV SSDDIQVECP VCQAMLPGAA INRHLDNNCN DTGANGGNWL
     GTKKKTKPLR KIQRVNQASE SVANVRRKLQ DEGLSTSGSK QTLFRRYDEW VTLWNANVDN
     KTPRSKSDIK DDLRRWETTV VANENAQPVK MTIKNIDDRQ WVQKHKEDYD YLIEQARKSI
     LKKKQEKEKE QQQQQEGHQK AVDRREDNEP DMKRSETEGY QVVS
//
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