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Database: UniProt
Entry: A0A1T0ATW6_9PAST
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ID   A0A1T0ATW6_9PAST        Unreviewed;       363 AA.
AC   A0A1T0ATW6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=B0187_03690 {ECO:0000313|EMBL:OOR99920.1};
OS   Haemophilus paracuniculus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=734 {ECO:0000313|EMBL:OOR99920.1, ECO:0000313|Proteomes:UP000190867};
RN   [1] {ECO:0000313|EMBL:OOR99920.1, ECO:0000313|Proteomes:UP000190867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 43573 {ECO:0000313|EMBL:OOR99920.1,
RC   ECO:0000313|Proteomes:UP000190867};
RA   Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA   Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT   "Draft genome sequence of Haemophilus paracuniculus CCUG 43573 type
RT   strain.";
RL   Submitted (FEB-2017) 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:OOR99920.1}.
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DR   EMBL; MUYA01000004; OOR99920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T0ATW6; -.
DR   STRING; 734.B0187_03690; -.
DR   OrthoDB; 9808813at2; -.
DR   Proteomes; UP000190867; 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}; Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190867};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01113}.
FT   DOMAIN          7..188
FT                   /note="UmuC"
FT                   /evidence="ECO:0000259|PROSITE:PS50173"
FT   REGION          344..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   BINDING         106
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
FT   SITE            16
FT                   /note="Substrate discrimination"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01113"
SQ   SEQUENCE   363 AA;  41203 MW;  978A1E36A10135B8 CRC64;
     MSEVRKIIHI DMDCFYAAVE IRDNPSLVGK PIAVGGSLDQ RGVLATCNYE ARKFGLHSAM
     SSAQALKRCP HLVLLPINMP LYKGISAQIH QIFRRYTDVI EPLSLDEAYL DVSNNPHCFG
     SATWIAQAIR QAIWDELKLT ASAGVAPLKF LAKIASDQNK PNGQFVIPPE NVADFVAKLP
     LKKIPGVGKV THEKLKQLGF HTCADIQRSD RATILHHFGK FGQRLWDFSH AIDERGVEVN
     RPRKSQAVEN TLLEDIDDLS EAEKFVEELF EKLRFRLERN WGDKPLSEFK KLGIKLKFDD
     FTQTTLEKTT EQGFEKAQFL ALLTQIWQRR DGRKVRLIGL NTHFPESKNP EKPNHGQLGL
     WND
//
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