ID A0A0A7JQY4_9PSED Unreviewed; 915 AA.
AC A0A0A7JQY4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=DNA polymerase I {ECO:0000256|ARBA:ARBA00020311, ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU004460};
GN Name=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=NJ69_18565 {ECO:0000313|EMBL:AIZ34862.1};
OS Pseudomonas parafulva.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=157782 {ECO:0000313|EMBL:AIZ34862.1, ECO:0000313|Proteomes:UP000030632};
RN [1] {ECO:0000313|EMBL:AIZ34862.1, ECO:0000313|Proteomes:UP000030632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRS01-1 {ECO:0000313|EMBL:AIZ34862.1,
RC ECO:0000313|Proteomes:UP000030632};
RA Liu Q.;
RT "Genome sequence of Pseudomonas parafulva CRS01-1, an antagonistic
RT bacterium isolated from rice field.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
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 ECO:0000256|RuleBase:RU004460};
CC -!- SUBUNIT: Single-chain monomer with multiple functions.
CC {ECO:0000256|ARBA:ARBA00011541}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR EMBL; CP009747; AIZ34862.1; -; Genomic_DNA.
DR RefSeq; WP_039582051.1; NZ_CP009747.1.
DR AlphaFoldDB; A0A0A7JQY4; -.
DR KEGG; ppv:NJ69_18565; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR Proteomes; UP000030632; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; 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 CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR CDD; cd06139; DNA_polA_I_Ecoli_like_exo; 1.
DR CDD; cd09898; H3TH_53EXO; 1.
DR CDD; cd09859; PIN_53EXO; 1.
DR Gene3D; 3.30.70.370; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR020045; DNA_polI_H3TH.
DR InterPro; IPR018320; DNA_polymerase_1.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00593; pola; 1.
DR PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00474; 35EXOc; 1.
DR SMART; SM00475; 53EXOc; 1.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU004460};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU004460};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022839};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 4..266
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 314..503
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 673..879
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 915 AA; 99878 MW; C6E757B10FB9895D CRC64;
MSQAPLVLVD GSSYLYRAFH ALPPLTTSKG MPTGAVKGVL NMLKSLRRQY PDALFAVVFD
AKGGTFRDAM FAEYKANRPS MPDDLRVQVE PLHASVRALG YPLLCVEGVE ADDVIGTLAR
SSAAAGRPVI ISTGDKDMAQ LVDGHITLVN TMTGSVLDVA GVHEKFGVGP EHIIDFLALM
GDKVDNIPGV PGVGEKTAVG LLTGIGGGLR ELYENLDKVP SLAIRGAKSL PAKLEEHRDA
AFLSYELATI KIDVELDIAV DALVCGEPDR EALLALYTEM EFKSWIADVQ RDAAREGASI
EPVEAPAAKV EARYETVLDQ ARFDVWLDKL RQAPLFAFDT ETTGLDAQRA ELVGVSFAVE
PHEAAYVPLA HDYEGAPQQL DRDAVLLALK PLLEDPAKAK VGQNAKYDIN ILANCSQPIE
VRGVAYDTML ESYVLDSTAT RHDMDSLAQK YLDHRTIAFE DIAGRGAKQL TFNQIHLDKA
GPYAAEDADI TLRLHLALQA RLARTPSLQP VLMDIEMPLV PVLAKIERQG ALVDAALLKV
QSGELGVKMA ELERQAYELA GEPFNLGSPK QLGVILYDKL GMPVLSKTAK GQASTAEAVL
ADLAAEGYPL PTVLMEYRSL SKLKSTYTDK LPEQINPRTG RIHTSYQQAV AATGRLSSSD
PNLQNIPVRT LEGRRIRQAF VASPGYKLLA ADYSQIELRI MAHLAKDEGL LHAFRNDLDV
HRATAAEVFG VALEAVTHDQ RRSAKAINFG LIYGMSAFGL AKQIGVDRKQ AQDYIDRYFA
QYPGVLAYME RTRAQAAEQG FVETFFGRRL YLPDINAKNP ALRRGAERTA INAPMQGTAA
DIIKRAMVNV DHWLADSGLD ARVILQVHDE LVLEVREDLV EQVRNEIRPH MSNAAQLDVP
LLVEVGVGAN WDEAH
//
