DPO4_NITMS
ID DPO4_NITMS Reviewed; 364 AA.
AC A9A3A9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-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=Nmar_0642;
OS Nitrosopumilus maritimus (strain SCM1).
OC Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC Nitrosopumilus.
OX NCBI_TaxID=436308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCM1;
RX PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA Rosenzweig A.C., Manning G., Stahl D.A.;
RT "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT nitrification and autotrophy in globally distributed marine crenarchaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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; CP000866; ABX12538.1; -; Genomic_DNA.
DR AlphaFoldDB; A9A3A9; -.
DR SMR; A9A3A9; -.
DR STRING; 436308.Nmar_0642; -.
DR EnsemblBacteria; ABX12538; ABX12538; Nmar_0642.
DR KEGG; nmr:Nmar_0642; -.
DR eggNOG; arCOG04582; Archaea.
DR HOGENOM; CLU_012348_1_2_2; -.
DR OMA; CKPDGLL; -.
DR PhylomeDB; A9A3A9; -.
DR Proteomes; UP000000792; 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; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
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; IPR024728; PolY_HhH_motif.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF11798; IMS_HHH; 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; Reference proteome; Transferase.
FT CHAIN 1..364
FT /note="DNA polymerase IV"
FT /id="PRO_1000137144"
FT DOMAIN 6..194
FT /note="UmuC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT ACT_SITE 112
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
FT SITE 15
FT /note="Substrate discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01113"
SQ SEQUENCE 364 AA; 41636 MW; 1C75A957DD22A6D9 CRC64;
METRIVFHID FDYFYAQCEE IRSPELKSKP VCVCVFSDRG GDSGAIATAN YTARKYGAKS
GIPIVFAKKR LEERKDAVFL PVDFDYYSEM SEKAMKIMEE FSDVFEYVGR DEAYLDVTKR
TEGDFHKASH LAQQIKNSIR EKTKLSCSIG ISPNKLISKI ASDFQKPDGL TIVSPEKVEG
FLESLKIRDI PGIGKKTEQR FTEMNLETIG DVKRLDVFTL NKEFGRKSGT YIYNAVRGID
DELVKEREPS IQHGKIVTLK KDSKDYEFLL ENTLELCKEV HEIIQKKNQM FKSVGISFVQ
SDLSNKTKSK MLRNPTMSLE ELEKTVEQLL REALENQTAT IRRLGVKVSE LSESQGQRDI
TSYF
