ID RAD18_KLULA Reviewed; 427 AA.
AC Q6CTZ8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 127.
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=KLLA0C08756g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382123; CAH01442.1; -; Genomic_DNA.
DR RefSeq; XP_452591.1; XM_452591.1.
DR AlphaFoldDB; Q6CTZ8; -.
DR SMR; Q6CTZ8; -.
DR STRING; 284590.Q6CTZ8; -.
DR PaxDb; 284590-Q6CTZ8; -.
DR GeneID; 2891860; -.
DR KEGG; kla:KLLA0_C08756g; -.
DR eggNOG; KOG0287; Eukaryota.
DR HOGENOM; CLU_028491_2_0_1; -.
DR InParanoid; Q6CTZ8; -.
DR OMA; IPNTGPR; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0006301; P:postreplication repair; IEA:InterPro.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:InterPro.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 NCBIfam; TIGR00599; rad18; 1.
DR PANTHER; PTHR14134; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR PANTHER; PTHR14134:SF2; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00734; ZnF_Rad18; 1.
DR SUPFAM; SSF57850; RING/U-box; 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..427
FT /note="Postreplication repair E3 ubiquitin-protein ligase
FT RAD18"
FT /id="PRO_0000056157"
FT DOMAIN 268..302
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 168..196
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 113..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
SQ SEQUENCE 427 AA; 48688 MW; 06E611DE2ECCE5B1 CRC64;
MKLSVPETIS NPRDFLHTSV PQLTDLDSLL RCHICKDFLK ASVLTPCGHS FCSICIRKYL
QKESKCPLCL SDLTESMLQK EFLVQEICSS YVKLRGSLQK HLTISSQEEE KDNEIIISDE
ADTSVGTKRG TPDSPSLSSV STKKRKHDGI TTLLMKKKTD HPQRQEKKAQ CPICSKHLPL
SELEGSHIDE CLNKGSSLER SDSFEILDER TPSPSMESSH QPLEEKTSLP SSHLLEVKEK
KDITYHNERY LNSGLLQQKE NRLPRLDFQS LSMTQLKQKL ASLALPSNGT KQQMVARYKH
YEMLWNSNFL DSIDPVDENE LKRRLSSWEA KHNTDHSSDS NSITNLLRGN KRTNAISAMI
KLFKSDRFDR KGWMRHHTST FKALKLEAQR SDKLAKMKKE ELSQKSDANS EVSSEPILKI
DQTSENN
//
