ID A0A251XAN5_9GAMM Unreviewed; 896 AA.
AC A0A251XAN5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=TPSD3_04660 {ECO:0000313|EMBL:OUD14997.1};
OS Thioflexithrix psekupsensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thioflexithrix.
OX NCBI_TaxID=1570016 {ECO:0000313|EMBL:OUD14997.1, ECO:0000313|Proteomes:UP000194798};
RN [1] {ECO:0000313|EMBL:OUD14997.1, ECO:0000313|Proteomes:UP000194798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D3 {ECO:0000313|EMBL:OUD14997.1};
RA Fomenkov A., Vincze T., Grabovich M., Anton B.P., Dubinina G., Orlova M.,
RA Belousova E., Roberts R.J.;
RT "Thioflexothrix psekupsii D3 genome sequencing and assembly.";
RL Submitted (DEC-2016) 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}.
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:OUD14997.1}.
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DR EMBL; MSLT01000007; OUD14997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251XAN5; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000194798; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000194798};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 3..259
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 298..484
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 653..860
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 896 AA; 101599 MW; 55B1ADC0BA1A8D80 CRC64;
MNIEQTLILI DGSGYLYRAF HALPDLSNRQ GQATHAIYGV VSMLRRLLKT YQPHYAAVVF
DAKGRTFRHE LFADYKANRP AMPDELIQQI APLHGLIKAL GLPLLVEPNV EADDVIATLT
KQATEQAMQV LIFTSDKDFA QLVNPQVTLI NTLNETTLDE AGVFAKFGVM PHQIVDYLTL
IGDTVDNIPG VPKVGPKTAA KWLAQYGDLN HLLQHAHEIK GKVGEYLRQS QNQLPLSKQL
VQVKTDVTLD YAIHDLQIKT PDFSQLRHYY QQLDFNVWLA ELDSINPPVL EPKKTVNYHT
ILTQEQWQLW LARLQQADYF AFDTETTSLN ALDAEMVGFS FALTPHEAVY VPLMHRYLNA
PVQLDQQSIL NDLKPLLEDE QRLKIGQHLK YDAHILANYD INLRGIAFDT LLESYVLDSL
SRHDLDSLAE FYLNYKTVSF TDIAGKGKKQ LDFSEIPIEQ AAFYAAEDAD IALQLHQCLY
AKLTQNENLL NVYETIERPL IPVLMQMERT GVKIDAHLLA QHSGELQQRL TELEQQAHTL
AGHSFNLNST QQLQVVLFEE QGLPVLQKTP KGQASTAESV LQELAHSYPI AEVIMAHRSV
SKLKSTYTDA LPQQIRANTG RIHTSYQQSV TATGRLSSTD PNLQNIPIRT AEGRRIRQAF
IAESGFKIMS VDYSQIELRI MAHLSQDETL LNAFLTGIDV HQATAAEVFN VPLQAVSTEQ
RRSAKAINFG LIYGMSAYGL SKQLGIESPQ AQNYIDLYFE RYPKVKEYMD NIRQFARDQG
FVETVFGRRL YLPDINSRHY QKRQYAERTA INAPMQGTAA DIIKRAMIVI YNWLNQDLHD
HIKMILQVHD ELVFEVAVDY LPIAQQKIPE LMTQVVALKI PLEVQMGIAD NWDQAH
//
