ID A0A0A1I125_9PSED Unreviewed; 353 AA.
AC A0A0A1I125;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=BN844_3355 {ECO:0000313|EMBL:CDF95979.1};
OS Pseudomonas sp. SHC52.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=984195 {ECO:0000313|EMBL:CDF95979.1, ECO:0000313|Proteomes:UP000031550};
RN [1] {ECO:0000313|EMBL:CDF95979.1, ECO:0000313|Proteomes:UP000031550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SHC52 {ECO:0000313|EMBL:CDF95979.1,
RC ECO:0000313|Proteomes:UP000031550};
RA Van der Voort M., Mendes R., Raaijmakers J.M.;
RT "Genome mining of the rhizosphere bacterium Pseudomonas sp. SH-C52.";
RL Submitted (MAY-2013) 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|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; Evidence={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: 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:CDF95979.1}.
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DR EMBL; CBLV010000300; CDF95979.1; -; Genomic_DNA.
DR RefSeq; WP_041023578.1; NZ_CBLV010000300.1.
DR AlphaFoldDB; A0A0A1I125; -.
DR OrthoDB; 9808813at2; -.
DR Proteomes; UP000031550; 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; 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|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|ARBA:ARBA00022932,
KW 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|ARBA:ARBA00022457, ECO:0000256|HAMAP-
KW Rule:MF_01113};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01113,
KW ECO:0000313|EMBL:CDF95979.1};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01113, ECO:0000313|EMBL:CDF95979.1}.
FT DOMAIN 6..187
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT ACT_SITE 106
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT SITE 15
FT /note="Substrate discrimination"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
SQ SEQUENCE 353 AA; 39343 MW; 53D632EB02D8E17E CRC64;
MTQRKIIHVD CDCFYAAIEM RDDPRLAGKP MAVGGSADRR GVIATCNYEA RAYGVRSAMS
SGHALKLCPD LIIVKPRMDA YREASKEIQG IFRDYTDLIE PLSLDEAYLD VSASAHFGGS
ATRIAQDIRR RVSNQLHITV SAGVAPNKFL AKIASDWKKP NGLFVITPDQ VEDFVSALPV
SKLHGVGKVT ADKLNRLGIV DCLQLRQWDK LALVREFGSF GERLWSLARG IDERLVHNDS
RRQSISVENT YDIDLPDLVS CLDKLPELME TLSGRMARID SSYRPGKPFV KVKFHDFTQT
TLEQAGAGRD LGSYQSLLTQ AFNRGAKPVR LLGIGVRLED LRGGFEQLEL FER
//
