ID E3VXA8_9DEIO Unreviewed; 358 AA. AC E3VXA8; DT 11-JAN-2011, integrated into UniProtKB/TrEMBL. DT 11-JAN-2011, sequence version 1. DT 21-MAR-2012, entry version 7. DE RecName: Full=DNA polymerase IV 1; DE Short=Pol IV 1; DE EC=2.7.7.7; GN Name=dinB; Synonyms=dinB1; OS Deinococcus ficus. OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; OC Deinococcaceae; Deinococcus. OX NCBI_TaxID=317577; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CC-FR2-10; 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] RP NUCLEOTIDE SEQUENCE. RC STRAIN=CC-FR2-10; RX PubMed=21459566; 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 RT evidenced by the existence of the imuB-dnaE2 gene cassette and RT generation of superior feather degrading bacteria."; RL Microbiol. Res. 167:40-47(2011). 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 (By similarity). 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; HQ328500; ADO33729.1; -; Genomic_DNA. 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; DNApol_IV; 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 InterPro; IPR022880; DNApol_IV. DR InterPro; IPR024728; PolY_HhH_motif. DR Gene3D; G3DSA:3.30.1490.100; DNA_pol4/DinB_little_finger; 1. DR Pfam; PF00817; IMS; 1. DR Pfam; PF11799; IMS_C; 1. DR Pfam; PF11798; IMS_HHH; 1. DR SUPFAM; SSF100879; DNA_pol_Y-fam_little_finger; 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; KW Mutator protein; Nucleotidyltransferase; Transferase. FT DOMAIN 6 187 UmuC (By similarity). FT ACT_SITE 105 105 By similarity. FT METAL 10 10 Magnesium (By similarity). FT METAL 104 104 Magnesium (By similarity). FT SITE 15 15 Substrate discrimination (By similarity). 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 //