ID A0A444MNM7_9SPHI Unreviewed; 385 AA.
AC A0A444MNM7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 22-FEB-2023, entry version 16.
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=EPL05_14445 {ECO:0000313|EMBL:RWY51257.1};
OS Mucilaginibacter gilvus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=2305909 {ECO:0000313|EMBL:RWY51257.1, ECO:0000313|Proteomes:UP000286701};
RN [1] {ECO:0000313|EMBL:RWY51257.1, ECO:0000313|Proteomes:UP000286701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F01003 {ECO:0000313|EMBL:RWY51257.1,
RC ECO:0000313|Proteomes:UP000286701};
RA Yan Y.-Q., Du Z.-J.;
RT "Mucilaginibacter antarcticum sp. nov., isolated from antarctic soil.";
RL Submitted (JAN-2019) 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:RWY51257.1}.
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DR EMBL; SBIW01000006; RWY51257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444MNM7; -.
DR OrthoDB; 9808813at2; -.
DR Proteomes; UP000286701; 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; 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 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:RWY51257.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000286701};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01113, ECO:0000313|EMBL:RWY51257.1}.
FT DOMAIN 7..186
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT ACT_SITE 106
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 105
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 385 AA; 43364 MW; 662BF92514871B1E CRC64;
MNTDRQIIHM DQDAFFVSVE VRKNPALVGK PVIIGSLSDR GVVASCSYEA RKFGVHSAMP
ARLARRLCPH GIWIRGSMDE YSKASHEITE IIQGEVPLLE KASIDEHYID MTGMDKHYGT
LKCAKEIRSK VIKETGLPIS FGLSVNKTVS KMATNECKPN GELSIEKGIV QPFLNPLSIR
KIPGLGEKTF IKLSDMGIKK IHTLAQVHPE YMTSILGKNG LWLLQKAKGI DESPVIPYHE
QKTIGTQCTF KQDSIDVETI NHLLTSMVME LAFELRQKKK QTACITVTVR YSTFEDVTKQ
MRIPYTALDG VLITKTKELF KQLYQKRILI RLVGVRLSNL VSGFEQIDLY SESEEQYSLC
QAMDKIRRRF GPDSIKLASG IDLNL
//
