DPOLB_XENLA
ID DPOLB_XENLA Reviewed; 334 AA.
AC O57383; Q3KQ91;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=DNA polymerase beta;
DE EC=2.7.7.7;
DE EC=4.2.99.-;
GN Name=polb;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=9492271; DOI=10.1046/j.1432-1327.1998.2510081.x;
RA Reichenberger S., Pfeiffer P.;
RT "Cloning, purification and characterization of DNA polymerase beta from
RT Xenopus laevis -- studies on its potential role in DNA-end joining.";
RL Eur. J. Biochem. 251:81-90(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Repair polymerase that plays a key role in base-excision
CC repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that
CC removes the 5' sugar phosphate and also acts as a DNA polymerase that
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 (By
CC similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Cytoplasmic in normal conditions. Translocates to the nucleus
CC following DNA damage (By similarity). {ECO:0000250}.
CC -!- PTM: Methylation by PRMT6 stimulates the polymerase activity by
CC enhancing DNA binding and processivity. {ECO:0000250}.
CC -!- PTM: Ubiquitinated: monoubiquitinated by huwe1/arf-bp1.
CC Monoubiquitinated protein is then the target of stub1/chip, which
CC catalyzes polyubiquitination from monoubiquitin, leading to degradation
CC by the proteasome. usp47 mediates the deubiquitination of
CC monoubiquitinated protein, preventing polyubiquitination by STUB1/CHIP
CC and its subsequent degradation (By 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; Y15732; CAA75741.1; -; mRNA.
DR EMBL; BC106329; AAI06330.1; -; mRNA.
DR RefSeq; NP_001081643.1; NM_001088174.1.
DR AlphaFoldDB; O57383; -.
DR SMR; O57383; -.
DR MaxQB; O57383; -.
DR PRIDE; O57383; -.
DR GeneID; 397973; -.
DR KEGG; xla:397973; -.
DR CTD; 397973; -.
DR Xenbase; XB-GENE-999702; polb.S.
DR OMA; ITDMLME; -.
DR OrthoDB; 1328151at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 397973; Expressed in blastula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 1.10.150.110; -; 1.
DR Gene3D; 3.30.210.10; -; 1.
DR Gene3D; 3.30.460.10; -; 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; PTHR11276; 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; SSF47802; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA damage; DNA repair; DNA replication; DNA synthesis;
KW DNA-binding; DNA-directed DNA polymerase; Lyase; Magnesium; Metal-binding;
KW Methylation; Nucleotidyltransferase; Nucleus; Reference proteome; Sodium;
KW Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..334
FT /note="DNA polymerase beta"
FT /id="PRO_0000218782"
FT REGION 183..192
FT /note="DNA-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 72
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 83
FT /note="Omega-N-methylarginine; by PRMT6"
FT /evidence="ECO:0000250"
FT MOD_RES 152
FT /note="Omega-N-methylarginine; by PRMT6"
FT /evidence="ECO:0000250"
SQ SEQUENCE 334 AA; 38294 MW; 33073FF0D0554458 CRC64;
MSKRKAPQES PNEGITDFLV ELANYERNVN RAIHKYNAYR KAASVIAKYP TKIKSGTEAK
KLDGVGAKIA EKIDEFLATG KLRKLEKIRQ DDTSSSINFL TRVTGIGPAA ARKFFDEGIK
TLDDLRNNEH KLNHHQKIGL KHFDDFEKRI PRKEMLQMQE IILDKVNNLD PEYIATVCGS
FRRGAESSGD MDILLTHPDF TSESAKQPRL LHQVVQCLED CNFITDTLVK GDTKFMGVCQ
LPCESDQDYP YRRIDIRLIP KDQYYCGVLY FTGSDIFNKN MRTHALEKGF TLNEYTLRPL
GVTGIAGEPL PIDSEKDIFD YIQWKYREPK DRSE
