ID A0A7W4V0F7_9MICO Unreviewed; 420 AA. AC A0A7W4V0F7; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-MAY-2024, entry version 11. 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 ORFNames=FHX49_000134 {ECO:0000313|EMBL:MBB2974593.1}; OS Microbacterium endophyticum. OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae; OC Microbacterium. OX NCBI_TaxID=1526412 {ECO:0000313|EMBL:MBB2974593.1, ECO:0000313|Proteomes:UP000529310}; RN [1] {ECO:0000313|EMBL:MBB2974593.1, ECO:0000313|Proteomes:UP000529310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 27099 {ECO:0000313|EMBL:MBB2974593.1, RC ECO:0000313|Proteomes:UP000529310}; RA Klenk H.-P.; RT "Sequencing the genomes of 1000 actinobacteria strains."; RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases. 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MBB2974593.1}. 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; JACHWQ010000001; MBB2974593.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7W4V0F7; -. DR Proteomes; UP000529310; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule. DR GO; GO:0042276; P:error-prone translesion synthesis; IEA:TreeGrafter. 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; IPR024728; PolY_HhH_motif. 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 Pfam; PF11798; IMS_HHH; 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 ECO:0000313|EMBL:MBB2974593.1}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01113, KW ECO:0000313|EMBL:MBB2974593.1}. FT DOMAIN 23..203 FT /note="UmuC" FT /evidence="ECO:0000259|PROSITE:PS50173" FT ACT_SITE 122 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113" FT BINDING 27 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113" FT BINDING 121 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113" FT SITE 32 FT /note="Substrate discrimination" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113" SQ SEQUENCE 420 AA; 45473 MW; 89E2D9F5FF81FA5C CRC64; MGKGDGRGRL TSPPDVDDTG AHVLHVDMDA FYPSVEILDN PSLRGKPIII GSTEGRSVVS SASYEARVYG VRSAMPVSQA LRLCPKAIVV PPHFARYSEL SRQVMAVFHE VTPLVEPLSI DEAFLDVSGS RRLWGRPREI AQMLRARVHE RTGLTCSVGA AATKHVAKMA STLSKPDGLL VVSAASTADF LSPLSVRNLW GVGPKSADVL EARGIRVVAD VLTTPIEVLQ RALGVSMGER VWQLARGIDT RTVQTERVEK SVGHEETFEV DVTDPDALRA ELRRLADRVG VRLRRHEWSA QTVSIKIRFA DFTTVTRGLT LAEPSNVSQR LGDVALDLFA QLHRGQPVRL VGVRAENLRP ASVQGGGLWD DDAEWRRVDG ALDGAATRFG VGAITRAALL GGRKSGSSLP SHPRPDADFS //