ID A0A0P7W7V1_9RHOB Unreviewed; 477 AA.
AC A0A0P7W7V1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=imuB {ECO:0000313|EMBL:KPP86003.1};
GN ORFNames=HLUCCO07_04185 {ECO:0000313|EMBL:KPP86003.1};
OS Rhodobacteraceae bacterium HLUCCO07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666914 {ECO:0000313|EMBL:KPP86003.1, ECO:0000313|Proteomes:UP000050369};
RN [1] {ECO:0000313|EMBL:KPP86003.1, ECO:0000313|Proteomes:UP000050369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCO07 {ECO:0000313|EMBL:KPP86003.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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}.
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 -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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:KPP86003.1}.
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DR EMBL; LJSU01000018; KPP86003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7W7V1; -.
DR STRING; 1666914.HLUCCO07_04185; -.
DR PATRIC; fig|1666914.4.peg.1778; -.
DR Proteomes; UP000050369; Unassembled WGS sequence.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:UniProt.
DR CDD; cd03468; PolY_like; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.1170.60; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR PANTHER; PTHR35369:SF2; BLR3025 PROTEIN; 1.
DR PANTHER; PTHR35369; BLR3025 PROTEIN-RELATED; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
PE 3: Inferred from homology;
FT DOMAIN 6..132
FT /note="UmuC"
FT /evidence="ECO:0000259|Pfam:PF00817"
FT DOMAIN 220..310
FT /note="DNA polymerase Y-family little finger"
FT /evidence="ECO:0000259|Pfam:PF11799"
SQ SEQUENCE 477 AA; 52717 MW; 8F83D3B12CC655C0 CRC64;
MLRRRPAEGP FALVHRSRNT EHLHCLNEIA ERSGLHRGMT LADARAICPD LITRPADIVR
EAAALAALHR WMGRYAPMVA RDGSDGLIAD ITGVPHLFGG EQDLRADLHA RMARAGLSVV
SAIAGTRGAA HALARHGGGI IPEGRLVDKI GPLPVSALRI DTETTQALGR MGLTRIADLI
TQPRAPLARR FGSGLILRLD QALGHQPEPV AAETEAPHFG VRMTLPEPIG LQADVMAGLT
RLLERLCHTL GQHHMGARRL RLDLHRVDRE IARVEIGLAR PMRNPERIAA LFSKGIADVE
AGFGIEAMRL EAHVTESLPP EQIGGGQAMR HEDALADLFS RLGNRLGFER VLRLLPAEST
IPERSFLLAP AAYSEAAPPP PRTGPERPII IFPPEPVAIR GMDHPGHPPV RFRWRRMQFT
TMRATGPERI APEWWLIDPD WQSGLRDYWR IETREGPRLW LFHTPQSPAW SVQGEFA
//
