ID R4SNC7_9PSEU Unreviewed; 438 AA.
AC R4SNC7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=DNA polymerase IV {ECO:0000256|HAMAP-Rule:MF_01113};
DE Short=Pol IV {ECO:0000256|HAMAP-Rule:MF_01113};
DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_01113};
GN Name=dinB {ECO:0000256|HAMAP-Rule:MF_01113,
GN ECO:0000313|EMBL:AGM04200.1};
GN ORFNames=AORI_1612 {ECO:0000313|EMBL:AGM04200.1};
OS Amycolatopsis keratiniphila.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis japonica group.
OX NCBI_TaxID=129921 {ECO:0000313|EMBL:AGM04200.1, ECO:0000313|Proteomes:UP000013968};
RN [1] {ECO:0000313|EMBL:AGM04200.1, ECO:0000313|Proteomes:UP000013968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HCCB10007 {ECO:0000313|EMBL:AGM04200.1,
RC ECO:0000313|Proteomes:UP000013968};
RX PubMed=23627759; DOI=10.1186/1471-2164-14-289;
RA Tang B., Wang Q., Yang M., Xie F., Zhu Y., Zhuo Y., Wang S., Gao H.,
RA Ding X., Zhang L., Zhao G., Zheng H.;
RT "ContigScape: a Cytoscape plugin facilitating microbial genome gap
RT closing.";
RL BMC Genomics 14:289-289(2013).
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, in conjunction with the beta clamp from PolIII.
CC {ECO:0000256|ARBA:ARBA00025589, ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00024632, ECO:0000256|HAMAP-
CC Rule:MF_01113};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01113};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01113};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01113}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01113}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC {ECO:0000256|ARBA:ARBA00010945, ECO:0000256|HAMAP-Rule:MF_01113}.
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DR EMBL; CP003410; AGM04200.1; -; Genomic_DNA.
DR RefSeq; WP_016332005.1; NC_021252.1.
DR AlphaFoldDB; R4SNC7; -.
DR KEGG; aoi:AORI_1612; -.
DR PATRIC; fig|1156913.3.peg.1649; -.
DR HOGENOM; CLU_012348_1_0_11; -.
DR Proteomes; UP000013968; 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 GO; GO:0009432; P:SOS response; IEA:UniProt.
DR CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.1170.60; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 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 PANTHER; PTHR11076:SF33; DNA POLYMERASE KAPPA; 1.
DR PANTHER; PTHR11076; DNA REPAIR POLYMERASE UMUC / TRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1.
DR PROSITE; PS50173; UMUC; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01113};
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01113};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01113};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_01113};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_01113};
KW DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_01113};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01113};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01113};
KW Mutator protein {ECO:0000256|HAMAP-Rule:MF_01113};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01113};
KW Reference proteome {ECO:0000313|Proteomes:UP000013968};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01113}.
FT DOMAIN 8..190
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT ACT_SITE 108
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT SITE 17
FT /note="Substrate discrimination"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
SQ SEQUENCE 438 AA; 47018 MW; 69836814C3EE0147 CRC64;
MGGHDRWVIH LDMDAFYASC EQLTRPTLAH RPVLVGGAGP RGVVAGASYQ AREHGIKSAM
PMSQARRLLP PNGVILPPRF KLYELLSTRV FDLVATYAPV LERISLDEAF AEPPSLVGAS
SEDVREFGAR LREHIRSDIG LVASIGAASG KQVAKVASDL AKPDGLLVVD QGTERDFLAP
LPTRVLWGIG PVAEGKLRAI GVRTLGQLTA LSDADAVSTL GSVVGRDLRR LATGVDDRPV
SDRAELKQVS AETTFDRDLI DLPSLRREVR DLAVHAHRRL VNAGRVARTV VVKLRHTDFS
TVTRSETMAS PTDEFDQLAA MAERLLIDPT EFGGVRLAGV ALSGLSVPHQ DPLFTLSVPA
PDVPVVERAP APVPVVASSW RPGDDVVHDE FGTGWVQGAG HGRVTVRFET RSSGPGVART
FTQEDPALRR GEPGDCLA
//
