ID DPO4_THETN Reviewed; 384 AA. AC P58965; Q8RD00; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2002, sequence version 1. DT 15-DEC-2009, entry version 49. DE RecName: Full=DNA polymerase IV; DE Short=Pol IV; DE EC=2.7.7.7; GN Name=dinB; OrderedLocusNames=TTE0254; OS Thermoanaerobacter tengcongensis. OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=119072; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4; RX MEDLINE=21992816; PubMed=11997336; DOI=10.1101/gr.219302; RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., RA Chen Y., Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., RA Tan H., Chen R., Wang J., Yu J., Yang H.; RT "A complete sequence of the T. tengcongensis genome."; RL Genome Res. 12:689-700(2002). CC -!- FUNCTION: Poorly processive, error-prone DNA polymerase involved CC in untargeted mutagenesis. Copies undamaged DNA at stalled CC replication forks, which arise in vivo from mismatched or CC misaligned primer ends. These misaligned primers can be extended CC by polIV. Exhibits no 3'-5' exonuclease (proofreading) activity. CC May be involved in translesional synthesis, in conjunction with CC the beta clamp from polIII (By similarity). CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity). CC -!- SUBUNIT: Monomer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. CC -!- SIMILARITY: Contains 1 umuC domain. 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; AE008691; AAM23550.1; -; Genomic_DNA. DR RefSeq; NP_621946.1; -. DR GeneID; 996547; -. DR GenomeReviews; AE008691_GR; TTE0254. DR KEGG; tte:TTE0254; -. DR NMPDR; fig|273068.3.peg.1047; -. DR HOGENOM; HBG734504; -. DR OMA; LAKGDEH; -. DR BioCyc; TTEN273068:TTE0254-MON; -. DR BRENDA; 2.7.7.7; 276887. 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:HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:HAMAP. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:HAMAP. DR HAMAP; MF_01113; -; 1. DR InterPro; IPR017962; DNA_pol4/DinB_little_finger. DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger. DR InterPro; IPR001126; DNA_repair_prot_UmuC-like. DR InterPro; IPR017963; DNA_repair_prot_UmuC-like_N. DR Gene3D; G3DSA:3.30.1490.100; DNA_pol4/DinB_little_finger; 1. DR PANTHER; PTHR11076; UMUC_like; 1. DR Pfam; PF00817; IMS; 1. DR PROSITE; PS50173; UMUC; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA damage; DNA repair; DNA replication; KW DNA-binding; DNA-directed DNA polymerase; Magnesium; Metal-binding; KW Mutator protein; Nucleotidyltransferase; Transferase. FT CHAIN 1 384 DNA polymerase IV. FT /FTId=PRO_0000173960. FT DOMAIN 5 182 UmuC. FT ACT_SITE 104 104 By similarity. FT METAL 9 9 Magnesium (By similarity). FT METAL 103 103 Magnesium (By similarity). FT SITE 14 14 Substrate discrimination (By similarity). SQ SEQUENCE 384 AA; 43916 MW; 01C214516AD9AABB CRC64; MKRKIIHVDM DAFFASIEQQ DNPEYRGKPV IVGGLSGRGV VSTCSYEARK YGIHSAMPMY MAKKLCPQGI FLPVRRKRYE EVSEQIFRIL YDITPFVEPV SIDEAYLDVT HVDKNPEDIA LEIKKRVKDA TGLTVSVGIS YNKFLAKLAS DWNKPDGLMV ITEDMVPEIL KPLPVTKVHG IGEKSAEKLR SIGIETVEDL LKLPQENLIE LFGKTGVEIY NRIRGIDERP VETMREIKSI GKEKTLEKDT KNKELLIQHL KEFSEIVSEE LIKERLYCRT VTVKIKTADF AVHTKSKTVD KYIRFSEDIY EVAKGILEEW KLEQYVRLIG LSVSNLSPVK YEQLSFLDKR LVKVIKAGNL AEEINKRIGK KIIKKGSELL KDNK //