ID B6VAJ2_9DEIN Unreviewed; 833 AA.
AC B6VAJ2;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN Name=polI {ECO:0000313|EMBL:ACJ07018.1};
GN Synonyms=polA {ECO:0000256|RuleBase:RU004460};
OS Thermus sp. Tok23.A1.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=570926 {ECO:0000313|EMBL:ACJ07018.1};
RN [1] {ECO:0000313|EMBL:ACJ07018.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tok23.A1 {ECO:0000313|EMBL:ACJ07018.1};
RX PubMed=19597696; DOI=10.1007/s00792-009-0269-8;
RA Gibbs M.D., Reeves R.A., Mandelman D., Mi Q., Lee J., Bergquist P.L.;
RT "Molecular diversity and catalytic activity of Thermus DNA polymerases.";
RL Extremophiles 13:817-826(2009).
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; FJ358545; ACJ07018.1; -; Genomic_DNA.
DR AlphaFoldDB; B6VAJ2; -.
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:0001882; F:nucleoside binding; IEA:InterPro.
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; 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; 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 InterPro; IPR015361; Taq_pol_thermo_exonuc.
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; PF09281; Taq-exonuc; 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.
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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 12..264
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 591..795
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 833 AA; 93864 MW; 1B92C1A6199CF14D CRC64;
MLPLFDLEEP PKRVLLVDGH HLAYRTFYAL SLTTSRGEPV QMVYGFARSL LKALKEDGQA
VVVVFDAKAP SFRHEAYEAY KAGRAPTPED FPRQLALVKR LVDLLGLVRL EAPGYEADDV
LGTLAKKAER EGMEVRILTG DRDFFQLLSE KVSVLLPDGT LVTPKDVQEK YGVPPERWVD
FRALTGDRSD NIPGVAGIGE KTALRLLAEW GSVENLLKNL DRVKPDSVRR KIEAHLEDLH
LSLDLARIRT DLPLEVDFKA LRRRTPDLEG LRAFLEELEF GSLLHEFGLL GGEKPREEAP
WPPPEGAFVG FLLSRKEPMW AELLALAAAA EGRVHRATSP VEALADLKEA RGFLAKDLAV
LALREGVALD PTDDPLLVAY LLDPANTNPE GVARRYGGEF TEDAAERALL SERLFQNLFP
RLSEKLLWLY QEVERPLSRV LAHMEARGVR LDVPLLEALS FELEKEMERL EGEIFRLAGH
PFNLNSRDQL ERVLFDELGL TPVGRTEKTG KRSTAQGALE ALRGAHPIVE LILQYRELSK
LKSTYLDPLP RLVHPRTGRL HTRFNQTATA TGRLSSSDPN LQNIPVRTPL GQRIRKAFVA
EEGWLLLAAD YSQIELRVLA HLSGDENLKR VFREGKDIHT ETAAWMFGLD PALVDPKMRR
AAKTVNFGVL YGMSAHRLSQ ELGIDYKEAE AFIERYFQSF PKVRAWIERT LEEGRTRGYV
ETLFGRRRYV PDLASRVRSV REAAERMAFN MPVQGTAADL MKIAMVKLFP RLKPLGAHLL
LQVHDELVLE VPEDRAEEAK ALVKEVMENA YPLDVPLEVE VGVGRDWLEA KQD
//
