ID L8TVI5_9MICC Unreviewed; 243 AA.
AC L8TVI5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=G205_03361 {ECO:0000313|EMBL:ELT45746.1};
OS Arthrobacter nitrophenolicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=683150 {ECO:0000313|EMBL:ELT45746.1, ECO:0000313|Proteomes:UP000011189};
RN [1] {ECO:0000313|Proteomes:UP000011189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJCon {ECO:0000313|Proteomes:UP000011189};
RX PubMed=23516196; DOI=10.1128/genomeA.00058-13;
RA Vikram S., Kumar S., Vaidya B., Pinnaka A.K., Raghava G.P.;
RT "Draft Genome Sequence of the 2-Chloro-4-Nitrophenol-Degrading Bacterium
RT Arthrobacter sp. Strain SJCon.";
RL Genome Announc. 1:e0005813-e0005813(2013).
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}.
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};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family.
CC {ECO:0000256|ARBA:ARBA00010945}.
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:ELT45746.1}.
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DR EMBL; AOFD01000005; ELT45746.1; -; Genomic_DNA.
DR AlphaFoldDB; L8TVI5; -.
DR PATRIC; fig|683150.5.peg.679; -.
DR Proteomes; UP000011189; Unassembled WGS sequence.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:UniProt.
DR Gene3D; 3.30.70.270; -; 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 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; 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 Nucleotidyltransferase {ECO:0000313|EMBL:ELT45746.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011189};
KW Transferase {ECO:0000313|EMBL:ELT45746.1}.
FT DOMAIN 11..72
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
SQ SEQUENCE 243 AA; 26488 MW; 17B0C776A756530D CRC64;
MRTGDPDSYA RQLQQAVLAE TRLHCSVGIG DTLVRAKVAT TFGKPAGIFR LTEDNWLEVM
GSRPTIDLWG VGTKVSRRLA KLGIETVAQL AASNPDDLVP EFGPKMGPWY AQLGRGDGAR
EVDDTPWVAR GHSRETTFQQ DLTGPGQVDA AIRELAGHVL EDVAAEGRPV VGLTLKVRYA
PFITKTYARK IPETSDPAEV LARALDLVAK IEPDRPIRLL GLRAEMTMPG DSRQGHTPTR
SGW
//