ID A7I5X9_METB6 Unreviewed; 365 AA.
AC A7I5X9;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=Mboo_0622 {ECO:0000313|EMBL:ABS55140.1};
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442 {ECO:0000313|EMBL:ABS55140.1, ECO:0000313|Proteomes:UP000002408};
RN [1] {ECO:0000313|Proteomes:UP000002408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8
RC {ECO:0000313|Proteomes:UP000002408};
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(2015).
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; CP000780; ABS55140.1; -; Genomic_DNA.
DR RefSeq; WP_012106161.1; NC_009712.1.
DR AlphaFoldDB; A7I5X9; -.
DR STRING; 456442.Mboo_0622; -.
DR GeneID; 5410187; -.
DR KEGG; mbn:Mboo_0622; -.
DR eggNOG; arCOG04582; Archaea.
DR HOGENOM; CLU_012348_1_1_2; -.
DR OrthoDB; 372207at2157; -.
DR Proteomes; UP000002408; 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; -; 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 ECO:0000313|EMBL:ABS55140.1}; 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:ABS55140.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002408};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01113, ECO:0000313|EMBL:ABS55140.1}.
FT DOMAIN 13..196
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT ACT_SITE 116
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT SITE 22
FT /note="Substrate discrimination"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
SQ SEQUENCE 365 AA; 39287 MW; C2634C3B94496C74 CRC64;
MDGQTGDAGQ RIVLHADMDC FYAAVEMHDH PEIAGKAVVV GADPQGGAGR GVVSTASYEA
RAFGVRSAMP ISQAYRLCPG AVYLRPDMAR YAAVSAEIMG IFKETGYRVQ QVSIDEAFLD
ISPVRSFDTA RDLAVRLKQT IRDRVGITCS LGVAPSKIVA KIASGHQKPD GMTVVTPDSA
RDFLAPLPIR KIPGIGGKTG AQIEALGITT IGNLATCDIQ VLVGAFGRSA GLLREAALGH
DNSEVVERDG VKSISKETTF ANDTEDPKEI AATMELLVRE VAQAIADEAL QFKTVTIRVR
YAGFVSKTKA RSLLHYHNDE AAIRAAAGEL LRELWDGKPI RRLGLRLSTL RHQDSRQQTL
FGSCR
//
