ID A0A496PN61_9MICC Unreviewed; 405 AA.
AC A0A496PN61;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=DWQ67_02120 {ECO:0000313|EMBL:RKW71973.1};
OS Galactobacter caseinivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Galactobacter.
OX NCBI_TaxID=2676123 {ECO:0000313|EMBL:RKW71973.1, ECO:0000313|Proteomes:UP000273119};
RN [1] {ECO:0000313|EMBL:RKW71973.1, ECO:0000313|Proteomes:UP000273119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JZ R-183 {ECO:0000313|EMBL:RKW71973.1,
RC ECO:0000313|Proteomes:UP000273119};
RA Hahne J., Isele D., Lipski A.;
RT "Arthrobacter sp. nov., isolated from raw cow's milk with high bacterial
RT count.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00025589, 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01113}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKW71973.1}.
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DR EMBL; QQXL01000001; RKW71973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A496PN61; -.
DR Proteomes; UP000273119; Unassembled WGS sequence.
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; 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 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 ECO:0000313|EMBL:RKW71973.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000273119};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01113, ECO:0000313|EMBL:RKW71973.1}.
FT DOMAIN 1..176
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 368..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 95
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT SITE 5
FT /note="Substrate discrimination"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
SQ SEQUENCE 405 AA; 43742 MW; A4035ED2B740CAA5 CRC64;
MDAFFVSVER KDAPELQGVP MIVAHDGERS VVLSASYDVR KLGVHSAQPV SQARRMAPHA
RLVEPRQGRY HQISGQIMEI FREFTPLVEP VSVDEAFLDL SGALRRWGTP ERVAQLIRER
IQEQLGLPAS VGLAANKFLA KMASGRAKPD GIFSIPPGRV REFLDPLPVG ELFGVGAATA
TTLRPAGFST AGDLAAADPA QVERLLGRGA LKLAALARGM DDREIVLERE EKSLSAEHTY
SVDVTDRETL ERTVLWLSHR VAERARRAGR VGEVVALKIR WEDFTTLTRQ RRLPRPSDAA
TEIDAAVREL MGALPRPLPP VRLIGVRLDG LAPHGAGLQL SLDQQVDARR DVEATMDQVN
ARFAGSLSPA SLLQPGAGRR AQPTPPAQGS SGHQPGSSPG AQGSG
//
