ID A0A7L8ACX7_9FLAO Unreviewed; 365 AA. AC A0A7L8ACX7; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 03-AUG-2022, entry version 4. 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:QOD59767.1}; GN ORFNames=H9I45_10430 {ECO:0000313|EMBL:QOD59767.1}; OS Polaribacter haliotis. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Polaribacter. OX NCBI_TaxID=1888915 {ECO:0000313|EMBL:QOD59767.1, ECO:0000313|Proteomes:UP000516764}; RN [1] {ECO:0000313|EMBL:QOD59767.1, ECO:0000313|Proteomes:UP000516764} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KCTC 52418 {ECO:0000313|EMBL:QOD59767.1, RC ECO:0000313|Proteomes:UP000516764}; RX PubMed=27902190; RA Kim Y.O., Park I.S., Park S., Nam B.H., Park J.M., Kim D.G., Yoon J.H.; RT "Polaribacter haliotis sp. nov., isolated from the gut of abalone Haliotis RT discus hannai."; RL Int. J. Syst. Evol. Microbiol. 66:5562-5567(2016). 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; 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 --------------------------------------------------------------------------- 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; CP061813; QOD59767.1; -; Genomic_DNA. DR KEGG; phal:H9I45_10430; -. DR Proteomes; UP000516764; 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; 3.30.1490.100; -; 1. DR Gene3D; 3.30.70.270; -; 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 Pfam; PF00817; IMS; 1. DR Pfam; PF11799; IMS_C; 1. DR Pfam; PF11798; IMS_HHH; 1. DR SUPFAM; SSF100879; SSF100879; 1. DR SUPFAM; SSF56672; SSF56672; 1. DR PROSITE; PS50173; UMUC; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01113}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_01113}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_01113}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP- KW Rule:MF_01113}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01113}; KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932, KW ECO:0000256|HAMAP-Rule:MF_01113}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01113}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01113}; KW Mutator protein {ECO:0000256|ARBA:ARBA00022457, ECO:0000256|HAMAP- KW Rule:MF_01113}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_01113}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01113}. FT DOMAIN 10..190 FT /note="UmuC" FT /evidence="ECO:0000259|PROSITE:PS50173" FT ACT_SITE 109 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113" FT BINDING 14 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113" FT BINDING 108 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113" FT SITE 19 FT /note="Substrate discrimination" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113" SQ SEQUENCE 365 AA; 41637 MW; 9A25E69F0D2B1F70 CRC64; MELQPPFRKI IHVDMDAFYA SVAQLDNPEL RGKAIAVGGN EIRGVVSAAS YEARKFGVKS AMSGFMAKKK CPHLIFVKSD FERYKELSAK IREIFYEYTD LVEPLSLDEA YLDVTENKKG NTSANDIARE IRARIFEVTG LRASAGISIN KFIAKVASDI NKPNGQKTVH PEEVIKFLEE LPVNKFYGVG KVTAAKMYNL GIFVGNDLKK KSLEELVTLF GKSGTHYYNI VRGIHNSAVK PNRIRKSLAA ERTFNENISS EIYMIEKLEK IADELERRML KNDTKGKTIT LKIKYSDFTQ QTRSKTKPHF MQTKKEFFPV VKELLFQDKL VNSVRLLGLS FGNLNTEIKE PVWVQLKFDF NTHRF //