ID A0RUK5_CENSY Unreviewed; 363 AA.
AC A0RUK5;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=dbh {ECO:0000256|HAMAP-Rule:MF_01113};
GN OrderedLocusNames=CENSYa_0386 {ECO:0000313|EMBL:ABK77022.1};
OS Cenarchaeum symbiosum (strain A).
OC Archaea; Nitrososphaerota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX NCBI_TaxID=414004 {ECO:0000313|EMBL:ABK77022.1, ECO:0000313|Proteomes:UP000000758};
RN [1] {ECO:0000313|EMBL:ABK77022.1, ECO:0000313|Proteomes:UP000000758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A {ECO:0000313|Proteomes:UP000000758};
RX PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT symbiosum.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
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. {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|HAMAP-Rule:MF_01113}.
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DR EMBL; DP000238; ABK77022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0RUK5; -.
DR STRING; 414004.CENSYa_0386; -.
DR EnsemblBacteria; ABK77022; ABK77022; CENSYa_0386.
DR KEGG; csy:CENSYa_0386; -.
DR PATRIC; fig|414004.10.peg.346; -.
DR HOGENOM; CLU_012348_1_2_2; -.
DR Proteomes; UP000000758; 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 CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR Gene3D; 3.30.70.270; -; 2.
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:ABK77022.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000758};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01113, ECO:0000313|EMBL:ABK77022.1}.
FT DOMAIN 5..193
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT ACT_SITE 111
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 110
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 363 AA; 40524 MW; 3B6C2A20FD5632BF CRC64;
MDRIVLHVDF DHFFAQCEEA RRPELRSGPV VVCVFSDRGG DSGAVATANY AARKFGVKSG
IPISHAKSRL HEVPDAVFLP ADFAYYSGIS QEAMDEMKGF ADVFEYVGKD EAYMDVTRRT
GGDYKKASYL AQQVKNAVRR KTRLTCSVGV TPNRLLSKIA SDYKKPDGLT VVPPGKVAEF
LEPLDIRDIP GIGGKTEKAL AEMGIRTVGQ MRSVDIFELQ QRFGRRSGTH MHNAARGIDD
EPVSEREPNV QHSRIVTLKR DSNEFGFLAE TLGELCRDLH SAVVKRRQRF KSVGIQLVQS
DLSQKTRSRM LRSPVSDLEV LEKSSVQLLR EALRDQEKPV RRLGVRISEL SEAGSQGVMD
SYF
//
