ID A0A1A1Y6W4_9MYCO Unreviewed; 453 AA.
AC A0A1A1Y6W4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=A5724_03080 {ECO:0000313|EMBL:OBF27054.1};
OS Mycobacterium sp. ACS1612.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF27054.1, ECO:0000313|Proteomes:UP000092025};
RN [1] {ECO:0000313|Proteomes:UP000092025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA Musoke P., Ssengooba W., Joloba M.;
RL Submitted (JUN-2016) 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|ARBA:ARBA00011245, ECO:0000256|HAMAP-
CC 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:OBF27054.1}.
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DR EMBL; LZHZ01000067; OBF27054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A1Y6W4; -.
DR STRING; 1834117.A5724_03080; -.
DR OrthoDB; 9808813at2; -.
DR Proteomes; UP000092025; 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|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 Reference proteome {ECO:0000313|Proteomes:UP000092025};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01113}.
FT DOMAIN 5..187
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 412..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 453 AA; 48496 MW; 1488A4BE352EC31B CRC64;
MDRWVLHFDM DAFFASVEQL TRPTLRGRPV LVGGLGGRGV VAGASYESRV YGARSAMPMH
QARRLVGAAA VVLPPRGVVY GVASRRVFET VRTLVPVLEQ LSFDEAFGEP PELAGASADD
VEAFCRHLKA RIRDETGLVA SVGAGSGKQI AKIASDLAKP DGIRVVRRDE ETVLLHGLPV
RRLWGIGPVA EEKLHRLGIE TIGQLAALSD AEAANILGTA VGAALHRLAQ GIDDRPVAEN
APAKQISAES TFAEDLTTLD QLREALGPIG EHAHARLEKD GRGARTVTVK LKKSDMSILT
RSATLPYATT DASTLTAMAR RLLLDPLEIG PIRLVGVGFS GLTDVRQESL FPDLELAAED
VSNTSVGPTV TELAATGPAW RIGDDVVHTD YGHGWIQGAG HGVMTVRFET RGTGPGPART
FPDDEPRIAR ANPVDSLDWP DYVDELSRYQ SSP
//
