ID E3VXA8_9DEIO Unreviewed; 358 AA. AC E3VXA8; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 29-MAY-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:ADO33729.1}; OS Deinococcus ficus. OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=317577 {ECO:0000313|EMBL:ADO33729.1}; RN [1] {ECO:0000313|EMBL:ADO33729.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CC-FR2-10 {ECO:0000313|EMBL:ADO33729.1}; RA Lin C.H., Liu Y.M., Yang C.C., Wu K.M., Shu H.Y., Liu T.T., Kao Y.T., RA Chen Y.T., Lyu P.C., Chou S.H., Shen F.T., Young C.C., Tsai S.F.; RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADO33729.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CC-FR2-10 {ECO:0000313|EMBL:ADO33729.1}; RX PubMed=21459566; DOI=10.1016/j.micres.2011.02.008; RA Zeng Y.H., Shen F.T., Tan C.C., Huang C.C., Young C.C.; RT "The flexibility of UV-inducible mutation in Deinococcus ficus as evidenced RT by the existence of the imuB-dnaE2 gene cassette and generation of superior RT feather degrading bacteria."; RL Microbiol. Res. 167:40-47(2011). 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|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: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 --------------------------------------------------------------------------- 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; HQ328500; ADO33729.1; -; Genomic_DNA. DR AlphaFoldDB; E3VXA8; -. 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 Transferase {ECO:0000256|HAMAP-Rule:MF_01113}. FT DOMAIN 6..187 FT /note="UmuC" FT /evidence="ECO:0000259|PROSITE:PS50173" FT ACT_SITE 105 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113" FT BINDING 10 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113" FT BINDING 104 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113" FT SITE 15 FT /note="Substrate discrimination" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113" SQ SEQUENCE 358 AA; 39057 MW; 9849EBE987C65829 CRC64; MLMRKIVHVD ADAFFASVEL RDNPSLRGKA VAVAYHGPRS VVTTATYEAR QYGVRSALPL RTALARCPHL IVIEPRMDAY REASRLIHGV FTEFTDLIEP LSLDEAYLDV TRPKRGPGSA TRIAQEIRRL VRERTGGLTV SAGVSFNKML AKLGSGMNKP DGLTVILPQD ADALIARLPV GEFYGIGPVT AAKLERLGIR TGADLRARSL TELTAAFGRH GAHMYAIARG IDDRPVDPSD DRKSVGTEDT YDTDLRTLAD MHAKLPGLSE RTARRLARHG LAGRVVTVKV KFSNFEVISR QQSLPVPVQT AEEIGRVARR LLGADLVGTR AVRLLGVTVS HLVDPQGRDV VPPLFPLV //