ID A0A0G3GXA8_9CORY Unreviewed; 466 AA.
AC A0A0G3GXA8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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:AKK03507.1};
GN ORFNames=CEPID_08285 {ECO:0000313|EMBL:AKK03507.1};
OS Corynebacterium epidermidicanis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK03507.1, ECO:0000313|Proteomes:UP000035368};
RN [1] {ECO:0000313|EMBL:AKK03507.1, ECO:0000313|Proteomes:UP000035368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK03507.1,
RC ECO:0000313|Proteomes:UP000035368};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium epidermidicanis DSM 45586,
RT isolated from the skin of a dog suffering from pruritus.";
RL Submitted (MAY-2015) 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}.
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DR EMBL; CP011541; AKK03507.1; -; Genomic_DNA.
DR RefSeq; WP_047240524.1; NZ_CP011541.1.
DR AlphaFoldDB; A0A0G3GXA8; -.
DR STRING; 1050174.CEPID_08285; -.
DR KEGG; cei:CEPID_08285; -.
DR PATRIC; fig|1050174.4.peg.1668; -.
DR OrthoDB; 9808813at2; -.
DR Proteomes; UP000035368; 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|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:AKK03507.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035368};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01113, ECO:0000313|EMBL:AKK03507.1}.
FT DOMAIN 5..187
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT ACT_SITE 105
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT SITE 14
FT /note="Substrate discrimination"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
SQ SEQUENCE 466 AA; 51149 MW; 1FC135B588C5F7B3 CRC64;
MQRWVLHIDM DAFFASVEQL TRPTLRGRPV LVGGLAGRGV VAGASYEARK FGARSAMPMF
QARALIGPRA TTVRPRFPVY SAASKRVFEI VRAQAGLVEQ LSIDEAFLEP SVLQGADPEK
VGQWCQQLRE SIRRETGLPA SLGAGPGKQA AKIGSGLAKP DGVFVIPVTD QVRLLHPLPV
RQLWGIGPIS EQKLKRLGID TIGDFAALEQ KEVEAALGKT VGPALWQIAQ GNDDRSVAPR
AEAKQVSAEH TYPKDLTTKA EVDEAVSRSM TDAYRRLKKD GRAARTISVK LKLADFTTET
RSLTLSYASD DLETLTAATR RLTRYPEQIG PIRLVGVSLS GLELERQDVM FPELDQQVTV
TEDVAGDFET GVRSSSHSEV ISLVNSPQLE ESRSGTWYST QDVFHPEYGH GWVQGCGHGV
VTVRFETRST AHGRTKSFAD DDPLLTEADP LASLDWDDWL SENYER
//
