ID A0A0F7N4R0_9ACTN Unreviewed; 904 AA.
AC A0A0F7N4R0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN Name=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=AA958_06015 {ECO:0000313|EMBL:AKH81832.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH81832.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH81832.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH81832.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-2015) 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 -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR EMBL; CP011492; AKH81832.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7N4R0; -.
DR STRING; 444103.AA958_06015; -.
DR KEGG; strc:AA958_06015; -.
DR PATRIC; fig|444103.5.peg.1257; -.
DR Proteomes; UP000034283; Chromosome.
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:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
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; cd06140; DNA_polA_I_Bacillus_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; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR002421; 5-3_exonuclease.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
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 PRINTS; PR00868; DNAPOLI.
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.
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|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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Reference proteome {ECO:0000313|Proteomes:UP000034283};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 9..271
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 660..867
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 904 AA; 98491 MW; D3E36ADF8A1D76AA CRC64;
MAENGSKTHR PRLMLLDGHS LAYRAFFALP AENFSTVGGQ VTNAIYGFTS MLSNTLRDEA
PTHLAVAFDV SRKTWRSAEF ADYKANRSST PDDFKGQVEL IGELLDAMNV PRFAVEGFEA
DDVIATLATQ AEAAGFEVLI VTGDRDSFQL VSDQVTVLYP TKGVSELTRF TPEKVEERYG
LTPAQYPDFA ALRGDPSDNL PGIPGVGEKT AAKWIKQFGS FAELAERAEE VKGKAGQNLR
DHLDAVKLNR RLTELDRAVE LPARPEELER KPYDRTALQV VMDALEFRNP NFRERLFNAD
PGAAEAVVEP EPGVQVDGRV LATGELAPWL AEHGSVPLGM ATVGTWQLGV GSVSEVALAT
AEGPAAWFDP ARLDAADEQA FAGWLADPGS AKTVHDAKSA MRVFAEHGWT VEGVAMDTAL
AAYLVTPGRR TFALDALSIA YLGRELEPPA ADGQLELGLD GAEGDQEAAE RDALMRTART
VLDLGEALSE KLAQVGAAEL LGDMELPVSA VLAGMERAGV AVDRAHLVAM EEQFAGAVQQ
AVREAHDAVG HEFNLGSPKQ LQEVFFGELD LPKTKKTKTG YTTDADALAW LATKTDHELP
VIMLRHREQA RLRSTVEGLI KTIAADGRIH TTFSQTVAAT GRLSSTDPNL QNVPIRTDEG
RAIRRGFVVG EGYESLLTAD YSQIELRVMA HLSEDEGLIE AFTSGEDLHD TVASQVFAVP
RTEVDAEMRR KIKAMSYGLA YGLSAFGLSQ QLGIEAAEAR KLMENYFERF GGVRDYLRHV
VDEARATGYT ETMFGRRRYL PDLNSDNRQR REMAERMALN APIQGTAADI VKLAMLRVDR
ALTAASLETR LLLQVHDEVV LEVAPGEREQ VEELVRREMA GAVSLRAPLD VAVGVGPDWE
SAAH
//
