ID   DPOLB_RAT               Reviewed;         335 AA.
AC   P06766; Q4G081;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   24-JAN-2024, entry version 212.
DE   RecName: Full=DNA polymerase beta {ECO:0000250|UniProtKB:P06746};
DE            EC=2.7.7.7 {ECO:0000250|UniProtKB:P06746};
DE   AltName: Full=5'-deoxyribose-phosphate lyase {ECO:0000250|UniProtKB:P06746};
DE            Short=5'-dRP lyase {ECO:0000250|UniProtKB:P06746};
DE            EC=4.2.99.- {ECO:0000250|UniProtKB:P06746};
DE   AltName: Full=AP lyase {ECO:0000250|UniProtKB:P06746};
DE            EC=4.2.99.18 {ECO:0000250|UniProtKB:P06746};
GN   Name=Polb;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3597402; DOI=10.1016/s0021-9258(18)48029-5;
RA   Matsukage A., Nishikawa K., Ooi T., Seto Y., Yamaguchi M.;
RT   "Homology between mammalian DNA polymerase beta and terminal
RT   deoxynucleotidyltransferase.";
RL   J. Biol. Chem. 262:8960-8962(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RA   Konopinski R., Nowak R., Siedlecki J.A.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 18-335.
RX   PubMed=2873575; DOI=10.1073/pnas.83.14.5106;
RA   Zmudzka B.Z., Sengupta D., Matsukage A., Cobianchi F., Kumar P.,
RA   Wilson S.H.;
RT   "Structure of rat DNA polymerase beta revealed by partial amino acid
RT   sequencing and cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:5106-5110(1986).
RN   [5]
RP   PARTIAL PROTEIN SEQUENCE, AND SEQUENCE REVISION TO 228.
RX   PubMed=2404980; DOI=10.1016/s0021-9258(19)39949-1;
RA   Kumar P., Widen S.G., Williams K.R., Kedar P., Karpel R.L., Wilson S.H.;
RT   "Studies of the domain structure of mammalian DNA polymerase beta.
RT   Identification of a discrete template binding domain.";
RL   J. Biol. Chem. 265:2124-2131(1990).
RN   [6]
RP   IMPORTANCE OF ARG-183 IN PRIMER BINDING.
RX   PubMed=2198936; DOI=10.1021/bi00473a005;
RA   Date T., Yamamoto S., Tanihara K., Nishimoto Y., Liu N., Matsukage A.;
RT   "Site-directed mutagenesis of recombinant rat DNA polymerase beta:
RT   involvement of arginine-183 in primer recognition.";
RL   Biochemistry 29:5027-5034(1990).
RN   [7]
RP   MUTAGENESIS OF ASP-190 AND ASP-192, AND IMPORTANCE OF ASP-190 AND ASP-192
RP   IN PRIMER BINDING.
RX   PubMed=2036395; DOI=10.1021/bi00235a023;
RA   Date T., Yamamoto S., Tanihara K., Nishimoto Y., Matsukage A.;
RT   "Aspartic acid residues at positions 190 and 192 of rat DNA polymerase beta
RT   are involved in primer binding.";
RL   Biochemistry 30:5286-5292(1991).
RN   [8]
RP   DNA-BINDING REGION.
RX   PubMed=1420147; DOI=10.1021/bi00157a014;
RA   Casas-Finet J.R., Kumar A., Karpel R.L., Wilson S.H.;
RT   "Mammalian DNA polymerase beta: characterization of a 16-kDa transdomain
RT   fragment containing the nucleic acid-binding activities of the native
RT   enzyme.";
RL   Biochemistry 31:10272-10280(1992).
RN   [9]
RP   MUTAGENESIS OF ASP-246, AND IMPORTANCE OF ASP-246 IN FIDELITY.
RX   PubMed=14563842; DOI=10.1074/jbc.m309607200;
RA   Dalal S., Kosa J.L., Sweasy J.B.;
RT   "The D246V mutant of DNA polymerase beta misincorporates nucleotides:
RT   evidence for a role for the flexible loop in DNA positioning within the
RT   active site.";
RL   J. Biol. Chem. 279:577-584(2004).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=8137427; DOI=10.1016/0092-8674(94)90388-3;
RA   Davies J.F. II, Almassy R.J., Hostomska Z., Ferre R.A., Hostomsky Z.;
RT   "2.3-A crystal structure of the catalytic domain of DNA polymerase beta.";
RL   Cell 76:1123-1133(1994).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=7516581; DOI=10.1126/science.7516581;
RA   Sawaya M.R., Pelletier H., Kumar A., Wilson S.H., Kraut J.;
RT   "Crystal structure of rat DNA polymerase beta: evidence for a common
RT   polymerase mechanism.";
RL   Science 264:1930-1935(1994).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX   PubMed=8841120; DOI=10.1021/bi960790i;
RA   Pelletier H., Sawaya M.R.;
RT   "Characterization of the metal ion binding helix-hairpin-helix motifs in
RT   human DNA polymerase beta by X-ray structural analysis.";
RL   Biochemistry 35:12778-12787(1996).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   PubMed=11330999; DOI=10.1021/bi002176j;
RA   Arndt J.W., Gong W., Zhong X., Showalter A.K., Liu J., Dunlap C.A., Lin Z.,
RA   Paxson C., Tsai M.-D., Chan M.K.;
RT   "Insight into the catalytic mechanism of DNA polymerase beta: structures of
RT   intermediate complexes.";
RL   Biochemistry 40:5368-5375(2001).
RN   [14]
RP   STRUCTURE BY NMR OF 1-87.
RX   PubMed=8639559; DOI=10.1021/bi952656o;
RA   Liu D., Prasad R., Wilson S.H., DeRose E.F., Mullen G.P.;
RT   "Three-dimensional solution structure of the N-terminal domain of DNA
RT   polymerase beta and mapping of the ssDNA interaction interface.";
RL   Biochemistry 35:6188-6200(1996).
RN   [15]
RP   STRUCTURE BY NMR OF 1-87.
RX   PubMed=10656829; DOI=10.1006/jmbi.1999.3455;
RA   Maciejewski M.W., Liu D., Prasad R., Wilson S.H., Mullen G.P.;
RT   "Backbone dynamics and refined solution structure of the N-terminal domain
RT   of DNA polymerase beta. Correlation with DNA binding and dRP lyase
RT   activity.";
RL   J. Mol. Biol. 296:229-253(2000).
CC   -!- FUNCTION: Repair polymerase that plays a key role in base-excision
CC       repair. During this process, the damaged base is excised by specific
CC       DNA glycosylases, the DNA backbone is nicked at the abasic site by an
CC       apurinic/apyrimidic (AP) endonuclease, and POLB removes 5'-deoxyribose-
CC       phosphate from the preincised AP site acting as a 5'-deoxyribose-
CC       phosphate lyase (5'-dRP lyase); through its DNA polymerase activity, it
CC       adds one nucleotide to the 3' end of the arising single-nucleotide gap.
CC       Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion
CC       rather than in a processive fashion as for other DNA polymerases. It is
CC       also able to cleave sugar-phosphate bonds 3' to an intact AP site,
CC       acting as an AP lyase. {ECO:0000250|UniProtKB:P06746}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000250|UniProtKB:P06746};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end 2'-deoxyribose-2'-deoxyribonucleotide-DNA = (2E,4S)-
CC         4-hydroxypenten-2-al-5-phosphate + a 5'-end 5'-monophospho-2'-
CC         deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:76255, Rhea:RHEA-
CC         COMP:13180, Rhea:RHEA-COMP:18657, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:136412, ChEBI:CHEBI:195194, ChEBI:CHEBI:195195;
CC         Evidence={ECO:0000250|UniProtKB:P06746};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC         deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC         dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC         2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC         COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC         ChEBI:CHEBI:167181; EC=4.2.99.18;
CC         Evidence={ECO:0000250|UniProtKB:P06746};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P06746};
CC       Note=Binds 2 magnesium ions per subunit.
CC       {ECO:0000250|UniProtKB:P06746};
CC   -!- SUBUNIT: Monomer (By similarity). Binds single-stranded DNA (ssDNA) (By
CC       similarity). Interacts with APEX1, LIG1, LIG3, FEN1, PCNA and XRCC1 (By
CC       similarity). Interacts with HUWE1/ARF-BP1, STUB1/CHIP and USP47 (By
CC       similarity). Interacts with FAM168A (By similarity).
CC       {ECO:0000250|UniProtKB:P06746}.
CC   -!- INTERACTION:
CC       P06766; P18887: XRCC1; Xeno; NbExp=4; IntAct=EBI-15845002, EBI-947466;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P06746}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P06746}. Note=Cytoplasmic in normal conditions.
CC       Translocates to the nucleus following DNA damage.
CC       {ECO:0000250|UniProtKB:P06746}.
CC   -!- DOMAIN: Residues 239-252 form a flexible loop which appears to affect
CC       the polymerase fidelity.
CC   -!- PTM: Methylation by PRMT6 stimulates the polymerase activity by
CC       enhancing DNA binding and processivity. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated at Lys-41, Lys-61 and Lys-81: monoubiquitinated by
CC       HUWE1/ARF-BP1. Monoubiquitinated protein is then the target of
CC       STUB1/CHIP, which catalyzes polyubiquitination from monoubiquitin,
CC       leading to degradation by the proteasome. USP47 mediates the
CC       deubiquitination of monoubiquitinated protein, preventing
CC       polyubiquitination by STUB1/CHIP and its subsequent degradation (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; J02776; AAA41901.1; -; mRNA.
DR   EMBL; U38801; AAB00389.1; -; mRNA.
DR   EMBL; BC098668; AAH98668.1; -; mRNA.
DR   EMBL; M13961; AAA41900.1; -; mRNA.
DR   PIR; A27112; A27112.
DR   RefSeq; NP_058837.2; NM_017141.2.
DR   PDB; 1BNO; NMR; -; A=1-87.
DR   PDB; 1BNP; NMR; -; A=1-87.
DR   PDB; 1BPB; X-ray; 2.30 A; A=88-335.
DR   PDB; 1BPD; X-ray; 3.60 A; A=1-335.
DR   PDB; 1BPE; X-ray; 2.90 A; A=1-335.
DR   PDB; 1DK2; NMR; -; A=2-87.
DR   PDB; 1DK3; NMR; -; A=1-87.
DR   PDB; 1HUO; X-ray; 2.60 A; A/B=1-335.
DR   PDB; 1HUZ; X-ray; 2.60 A; A/B=1-335.
DR   PDB; 1JN3; X-ray; 2.35 A; A=85-335.
DR   PDB; 1NOM; X-ray; 3.00 A; A=88-335.
DR   PDB; 1RPL; X-ray; 2.30 A; A=85-335.
DR   PDB; 1ZQU; X-ray; 2.60 A; A=88-335.
DR   PDB; 1ZQV; X-ray; 2.70 A; A=88-335.
DR   PDB; 1ZQW; X-ray; 2.30 A; A=88-335.
DR   PDB; 1ZQX; X-ray; 2.50 A; A=88-335.
DR   PDB; 1ZQY; X-ray; 2.30 A; A=88-335.
DR   PDB; 1ZQZ; X-ray; 2.70 A; A=88-335.
DR   PDB; 2BPC; X-ray; 2.80 A; A=88-335.
DR   PDB; 2BPF; X-ray; 2.90 A; A=1-335.
DR   PDB; 2BPG; X-ray; 3.60 A; A/B=1-335.
DR   PDB; 2VAN; X-ray; 2.10 A; A=91-335.
DR   PDB; 3K75; X-ray; 2.95 A; D/E=91-335.
DR   PDB; 3LQC; X-ray; 2.35 A; B=142-335.
DR   PDB; 3UXN; X-ray; 2.50 A; A/B=1-335.
DR   PDB; 3UXO; X-ray; 2.10 A; A/B=1-335.
DR   PDB; 3UXP; X-ray; 2.72 A; A/B=1-335.
DR   PDB; 3V72; X-ray; 2.49 A; A=1-335.
DR   PDB; 3V7J; X-ray; 2.25 A; A=4-335.
DR   PDB; 3V7K; X-ray; 2.27 A; A=4-335.
DR   PDB; 3V7L; X-ray; 2.66 A; A=4-335.
DR   PDBsum; 1BNO; -.
DR   PDBsum; 1BNP; -.
DR   PDBsum; 1BPB; -.
DR   PDBsum; 1BPD; -.
DR   PDBsum; 1BPE; -.
DR   PDBsum; 1DK2; -.
DR   PDBsum; 1DK3; -.
DR   PDBsum; 1HUO; -.
DR   PDBsum; 1HUZ; -.
DR   PDBsum; 1JN3; -.
DR   PDBsum; 1NOM; -.
DR   PDBsum; 1RPL; -.
DR   PDBsum; 1ZQU; -.
DR   PDBsum; 1ZQV; -.
DR   PDBsum; 1ZQW; -.
DR   PDBsum; 1ZQX; -.
DR   PDBsum; 1ZQY; -.
DR   PDBsum; 1ZQZ; -.
DR   PDBsum; 2BPC; -.
DR   PDBsum; 2BPF; -.
DR   PDBsum; 2BPG; -.
DR   PDBsum; 2VAN; -.
DR   PDBsum; 3K75; -.
DR   PDBsum; 3LQC; -.
DR   PDBsum; 3UXN; -.
DR   PDBsum; 3UXO; -.
DR   PDBsum; 3UXP; -.
DR   PDBsum; 3V72; -.
DR   PDBsum; 3V7J; -.
DR   PDBsum; 3V7K; -.
DR   PDBsum; 3V7L; -.
DR   AlphaFoldDB; P06766; -.
DR   BMRB; P06766; -.
DR   SMR; P06766; -.
DR   DIP; DIP-44707N; -.
DR   IntAct; P06766; 1.
DR   STRING; 10116.ENSRNOP00000026039; -.
DR   BindingDB; P06766; -.
DR   ChEMBL; CHEMBL4343; -.
DR   iPTMnet; P06766; -.
DR   PhosphoSitePlus; P06766; -.
DR   jPOST; P06766; -.
DR   PaxDb; 10116-ENSRNOP00000026039; -.
DR   Ensembl; ENSRNOT00000113772.1; ENSRNOP00000094599.1; ENSRNOG00000019150.6.
DR   Ensembl; ENSRNOT00055012865; ENSRNOP00055010253; ENSRNOG00055007682.
DR   Ensembl; ENSRNOT00060048617; ENSRNOP00060040531; ENSRNOG00060027954.
DR   Ensembl; ENSRNOT00065013936; ENSRNOP00065010380; ENSRNOG00065008755.
DR   GeneID; 29240; -.
DR   KEGG; rno:29240; -.
DR   UCSC; RGD:3363; rat.
DR   AGR; RGD:3363; -.
DR   CTD; 5423; -.
DR   RGD; 3363; Polb.
DR   eggNOG; KOG2534; Eukaryota.
DR   GeneTree; ENSGT00940000156918; -.
DR   HOGENOM; CLU_008698_1_0_1; -.
DR   InParanoid; P06766; -.
DR   OMA; YKYNAYR; -.
DR   OrthoDB; 49764at2759; -.
DR   PhylomeDB; P06766; -.
DR   TreeFam; TF103002; -.
DR   Reactome; R-RNO-110362; POLB-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-RNO-110373; Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
DR   Reactome; R-RNO-110381; Resolution of AP sites via the single-nucleotide replacement pathway.
DR   Reactome; R-RNO-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
DR   Reactome; R-RNO-5651801; PCNA-Dependent Long Patch Base Excision Repair.
DR   Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR   Reactome; R-RNO-73930; Abasic sugar-phosphate removal via the single-nucleotide replacement pathway.
DR   EvolutionaryTrace; P06766; -.
DR   PRO; PR:P06766; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000019150; Expressed in testis and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0005876; C:spindle microtubule; ISO:RGD.
DR   GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISO:RGD.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; ISO:RGD.
DR   GO; GO:0003684; F:damaged DNA binding; IDA:RGD.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:RGD.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0016829; F:lyase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR   GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR   GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR   GO; GO:0006287; P:base-excision repair, gap-filling; IDA:RGD.
DR   GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR   GO; GO:0048872; P:homeostasis of number of cells; ISO:RGD.
DR   GO; GO:0071707; P:immunoglobulin heavy chain V-D-J recombination; ISO:RGD.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR   GO; GO:0048535; P:lymph node development; ISO:RGD.
DR   GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR   GO; GO:0006290; P:pyrimidine dimer repair; IDA:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0010332; P:response to gamma radiation; IEP:RGD.
DR   GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR   GO; GO:0007435; P:salivary gland morphogenesis; ISO:RGD.
DR   GO; GO:0016445; P:somatic diversification of immunoglobulins; ISO:RGD.
DR   GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; ISO:RGD.
DR   GO; GO:0048536; P:spleen development; ISO:RGD.
DR   CDD; cd00141; NT_POLXc; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR   Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1.
DR   InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR   InterPro; IPR019843; DNA_pol-X_BS.
DR   InterPro; IPR010996; DNA_pol_b-like_N.
DR   InterPro; IPR028207; DNA_pol_B_palm_palm.
DR   InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR   InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR   InterPro; IPR037160; DNA_Pol_thumb_sf.
DR   InterPro; IPR022312; DNA_pol_X.
DR   InterPro; IPR002008; DNA_pol_X_beta-like.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR029398; PolB_thumb.
DR   PANTHER; PTHR11276:SF42; DNA POLYMERASE BETA; 1.
DR   PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR   Pfam; PF14792; DNA_pol_B_palm; 1.
DR   Pfam; PF14791; DNA_pol_B_thumb; 1.
DR   Pfam; PF10391; DNA_pol_lambd_f; 1.
DR   Pfam; PF14716; HHH_8; 1.
DR   PRINTS; PR00869; DNAPOLX.
DR   PRINTS; PR00870; DNAPOLXBETA.
DR   SMART; SM00278; HhH1; 2.
DR   SMART; SM00483; POLXc; 1.
DR   SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81585; PsbU/PolX domain-like; 1.
DR   PROSITE; PS00522; DNA_POLYMERASE_X; 1.
DR   Genevisible; P06766; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   DNA damage; DNA repair; DNA replication; DNA synthesis; DNA-binding;
KW   DNA-directed DNA polymerase; Isopeptide bond; Lyase; Magnesium;
KW   Metal-binding; Methylation; Nucleotidyltransferase; Nucleus; Potassium;
KW   Reference proteome; Sodium; Transferase; Ubl conjugation.
FT   CHAIN           1..335
FT                   /note="DNA polymerase beta"
FT                   /id="PRO_0000218780"
FT   REGION          183..192
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   ACT_SITE        72
FT                   /note="Nucleophile; Schiff-base intermediate with DNA; for
FT                   5'-dRP lyase activity"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         60
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         60
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         62
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         62
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         65
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         65
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         101
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         101
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         103
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         103
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         106
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         106
FT                   /ligand="Na(+)"
FT                   /ligand_id="ChEBI:CHEBI:29101"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         149
FT                   /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61560"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         180
FT                   /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61560"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         183
FT                   /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61560"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         189
FT                   /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61560"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         190
FT                   /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT                   /ligand_id="ChEBI:CHEBI:61560"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         192
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   BINDING         256
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   MOD_RES         72
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K409"
FT   MOD_RES         83
FT                   /note="Omega-N-methylarginine; by PRMT6"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   MOD_RES         152
FT                   /note="Omega-N-methylarginine; by PRMT6"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   CROSSLNK        41
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   CROSSLNK        61
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   CROSSLNK        81
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P06746"
FT   MUTAGEN         190
FT                   /note="D->E,S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:2036395"
FT   MUTAGEN         191
FT                   /note="M->I: No loss of activity."
FT   MUTAGEN         191
FT                   /note="M->T: 50% loss of activity."
FT   MUTAGEN         192
FT                   /note="D->E,S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:2036395"
FT   MUTAGEN         246
FT                   /note="D->V: Misincorporates T nucleotide opposite G/C
FT                   template."
FT                   /evidence="ECO:0000269|PubMed:14563842"
FT   CONFLICT        228
FT                   /note="L -> R (in Ref. 1; AAA41901, 2; AAB00389 and 4;
FT                   AAA41900)"
FT                   /evidence="ECO:0000305"
FT   HELIX           13..28
FT                   /evidence="ECO:0007829|PDB:3UXO"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:1DK2"
FT   HELIX           33..48
FT                   /evidence="ECO:0007829|PDB:3UXO"
FT   HELIX           56..61
FT                   /evidence="ECO:0007829|PDB:3UXO"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:3V7L"
FT   HELIX           67..76
FT                   /evidence="ECO:0007829|PDB:3UXO"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:3UXO"
FT   HELIX           83..90
FT                   /evidence="ECO:0007829|PDB:3UXO"
FT   HELIX           92..100
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   TURN            101..104
FT                   /evidence="ECO:0007829|PDB:3V7L"
FT   HELIX           108..115
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   TURN            116..118
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   HELIX           122..126
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   HELIX           129..131
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   HELIX           134..141
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   TURN            142..144
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   HELIX           152..169
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   HELIX           179..182
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   STRAND          186..196
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   TURN            202..204
FT                   /evidence="ECO:0007829|PDB:1BPB"
FT   HELIX           208..220
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   STRAND          224..230
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   STRAND          232..239
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   STRAND          244..247
FT                   /evidence="ECO:0007829|PDB:3V7J"
FT   STRAND          253..259
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   HELIX           262..264
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   HELIX           265..273
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   HELIX           276..288
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   STRAND          291..293
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   STRAND          298..301
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   STRAND          303..305
FT                   /evidence="ECO:0007829|PDB:3UXO"
FT   HELIX           316..322
FT                   /evidence="ECO:0007829|PDB:2VAN"
FT   HELIX           330..332
FT                   /evidence="ECO:0007829|PDB:2VAN"
SQ   SEQUENCE   335 AA;  38327 MW;  BBF8498C0D3FBFC9 CRC64;
     MSKRKAPQET LNGGITDMLV ELANFEKNVS QAIHKYNAYR KAASVIAKYP HKIKSGAEAK
     KLPGVGTKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL TRVTGIGPSA ARKLVDEGIK
     TLEDLRKNED KLNHHQRIGL KYFEDFEKRI PREEMLQMQD IVLNEVKKLD PEYIATVCGS
     FRRGAESSGD MDVLLTHPNF TSESSKQPKL LHRVVEQLQK VRFITDTLSK GETKFMGVCQ
     LPSENDENEY PHRRIDIRLI PKDQYYCGVL YFTGSDIFNK NMRAHALEKG FTINEYTIRP
     LGVTGVAGEP LPVDSEQDIF DYIQWRYREP KDRSE
//