ID A0A1H7X753_9RHOB Unreviewed; 499 AA.
AC A0A1H7X753;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=SAMN05443999_1197 {ECO:0000313|EMBL:SEM29646.1};
OS Roseovarius azorensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1287727 {ECO:0000313|EMBL:SEM29646.1, ECO:0000313|Proteomes:UP000199582};
RN [1] {ECO:0000313|EMBL:SEM29646.1, ECO:0000313|Proteomes:UP000199582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100674 {ECO:0000313|EMBL:SEM29646.1,
RC ECO:0000313|Proteomes:UP000199582};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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}.
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DR EMBL; FOAG01000019; SEM29646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7X753; -.
DR STRING; 1287727.SAMN05443999_1197; -.
DR OrthoDB; 9788640at2; -.
DR Proteomes; UP000199582; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000199582}.
FT DOMAIN 25..149
FT /note="UmuC"
FT /evidence="ECO:0000259|Pfam:PF00817"
FT DOMAIN 237..328
FT /note="DNA polymerase Y-family little finger"
FT /evidence="ECO:0000259|Pfam:PF11799"
SQ SEQUENCE 499 AA; 54704 MW; E5DC365E58258951 CRC64;
MARRLLSIWF PRLASDTSLR NRPVEGPFAL THRSGNSDHL HCLNTTATAR GLSRGMPLAD
ARAICPDLAT RPADLYREAA ALASLRRWAG RYAPMVALDG MDGLMADISG VPHLFDGEMD
LREDLQARLE RAGLHAVSAI AGTRGAAHAL ARHGGGIVAD GGLVEGIGHL PVRALRIDHD
TADALARVGL ARIADLVHLP RAPLVRRFGT GLVLRLDQAL GVQPEPVAAE PYAPHFGVRM
TLPEPIGLQS DVMSGLERLL DRLCARLALH QRGARRMRLE LRRVDRGTAQ IEIGLARPMR
DPVRIAALFA RGVGEVDAGF GIDALRVTAP LTEALAPEQI GGGATVRHED ALADLLSSIG
NRIGFDRVLR LSPATSLIPE RSFLLFPAAY SAPEPSPPRA GPMRPITLFP PEPATAVTGA
PPAGFRWRRM RFTTLRATGP ERITPEWWFD DPAWRNGLRD YWRIETREGP RLWLFTTPQK
RDWDGARGRQ DWYVQGEFP
//