ID   A0A7L8ACX7_9FLAO        Unreviewed;       365 AA.
AC   A0A7L8ACX7;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   22-FEB-2023, entry version 6.
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; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
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}.
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DR   EMBL; CP061813; QOD59767.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7L8ACX7; -.
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; 3.30.70.270; -; 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|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
//