ID   DPO4_HALS3              Reviewed;         411 AA.
AC   B0R4P0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=DNA polymerase IV {ECO:0000255|HAMAP-Rule:MF_01113};
DE            Short=Pol IV {ECO:0000255|HAMAP-Rule:MF_01113};
DE            EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_01113};
GN   Name=dbh {ECO:0000255|HAMAP-Rule:MF_01113}; OrderedLocusNames=OE_2475F;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
CC   -!- FUNCTION: Poorly processive, error-prone DNA polymerase involved in
CC       untargeted mutagenesis. Copies undamaged DNA at stalled replication
CC       forks, which arise in vivo from mismatched or misaligned primer ends.
CC       These misaligned primers can be extended by PolIV. Exhibits no 3'-5'
CC       exonuclease (proofreading) activity. May be involved in translesional
CC       synthesis. {ECO:0000255|HAMAP-Rule:MF_01113}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01113};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01113};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01113};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01113}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01113}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC       {ECO:0000255|HAMAP-Rule:MF_01113}.
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DR   EMBL; AM774415; CAP13705.1; -; Genomic_DNA.
DR   RefSeq; WP_012289265.1; NC_010364.1.
DR   AlphaFoldDB; B0R4P0; -.
DR   SMR; B0R4P0; -.
DR   EnsemblBacteria; CAP13705; CAP13705; OE_2475F.
DR   GeneID; 5953908; -.
DR   KEGG; hsl:OE_2475F; -.
DR   HOGENOM; CLU_012348_1_2_2; -.
DR   OMA; KVRRYDF; -.
DR   PhylomeDB; B0R4P0; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR   Gene3D; 3.30.1490.100; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   HAMAP; MF_01113; DNApol_IV; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR   InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR   InterPro; IPR022880; DNApol_IV.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001126; UmuC.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   SUPFAM; SSF100879; SSF100879; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50173; UMUC; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Magnesium; Metal-binding; Mutator protein;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..411
FT                   /note="DNA polymerase IV"
FT                   /id="PRO_1000137136"
FT   DOMAIN          18..211
FT                   /note="UmuC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT   REGION          248..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT   BINDING         22
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT   BINDING         130
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT   SITE            27
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
SQ   SEQUENCE   411 AA;  43492 MW;  CA152C89EE8EAF81 CRC64;
     MPAGERLPGA PAREERIVVH VDMDCFYASC ERRREPALRG APVVVGMGYE PDQTVGAVAT
     ASYEAREYGV ESAQAISAAL ERLPRKADAP DASAAGYYRP VDMAYYESVS ESVSEILHGL
     GDPVREVSID EAYLDVTDRT AWDVAAGFGR HIKQRIARSV GVPASVGIAP DMSTAKLASD
     HEKPDGLVVV PPESVQSFLA PLDVADLHGV GPVHARALRE RGIETVGELA DADPYVLEAA
     FGERGREFHR RARGADSRPV EPRGKPKSLS RESSFDGATE SFDRVREQAA ALSGAVADRA
     SRTNASYRTI GVKVVTPPYD VQTRAESLPG PVDDPALLEA VSQSLLDEFE GAAVRKVGVR
     VSNLVFSERE QATLAGFSGD ETGDGGGHEG GACGGAGRGS CGGQTTLDEF T