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Database: UniProt
Entry: L0E265_THIND
LinkDB: L0E265_THIND
Original site: L0E265_THIND 
ID   L0E265_THIND            Unreviewed;       902 AA.
AC   L0E265;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 67.
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   OrderedLocusNames=TVNIR_3740 {ECO:0000313|EMBL:AGA35368.1};
OS   Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=1255043 {ECO:0000313|EMBL:AGA35368.1, ECO:0000313|Proteomes:UP000010809};
RN   [1] {ECO:0000313|Proteomes:UP000010809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14787 / UNIQEM 213 / ALEN2
RC   {ECO:0000313|Proteomes:UP000010809};
RA   Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., Sorokin D.Y.,
RA   Ravin N.V., Popov V.O.;
RT   "Complete sequence of Thioalkalivibrio nitratireducens.";
RL   Submitted (DEC-2012) 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; CP003989; AGA35368.1; -; Genomic_DNA.
DR   RefSeq; WP_015260460.1; NC_019902.2.
DR   AlphaFoldDB; L0E265; -.
DR   STRING; 1255043.TVNIR_3740; -.
DR   KEGG; tni:TVNIR_3740; -.
DR   PATRIC; fig|1255043.3.peg.3774; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_6; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000010809; 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:SF27; DNA POLYMERASE NU; 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|RuleBase:RU004460};
KW   DNA repair {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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          5..259
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          304..491
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          660..866
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   REGION          285..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   902 AA;  99836 MW;  7A2AF5247474A932 CRC64;
     MTENVPLVLV DGSSYLYRAF HALPPLTAPG GEPSGALYGV LGMLRKLRAD YGPQRMAVVF
     DAPGKTFRDD LYAEYKANRP SMPEELAVQI EPLHELVRAM GLPLLCIPGV EADDVIATLA
     AQAQARGEPV VISTGDKDLA QLVSDRVTLV NTMNGTVLDP PRVREKFGVD PERIVDLLTL
     VGDTVDNVPG VDKVGPKTAA KWLAEYGSLD AVIENADRIK GKVGENLRAA LERLPLSREL
     VTVRRDVDLG IDEHELALGK PDTTRLREMY GRFGFRRWLE ELEGNAGADS ADDPPPEEAQ
     RRDYSAIQDD RAFRDLLNRL EHAELVAFDT ETTSLDYMQA RIVGVSFSVE PGRGWYVPLA
     HEGPDAAPQL ERARTLERLR PWLESAERAK LGHHLKYDRN VLANHGITLR GIREDTMLES
     YVLDAGANRH DLDSLAERHL GHRMITYEDV AGKGAKQIPF AEVAVARATE YAAEDADICL
     RLHQALNPRL ADAEGPRAVY REIELPLVPV LSDMERTGVR VDAELLRAQS AELAKRMDEV
     SERAYSEAGA EFNLGSPKQI QEILFDRLGL PVLRRTPKGQ PSTAEDVLEQ MAAEYPLPRL
     ILEHRGLAKL RSTYTERLPE RIHPETGRVH TSYHQAVAAT GRLSSSDPNL QNIPVRTDEG
     RRIRQAFIAE PGQVLLAADY SQIELRIMAH LSRDRGLLEA FAAGEDIHRA TAAEVFGLEP
     ASVGPDQRRA AKAINFGLIY GMSAFGLARN LGIEQSQARE YIDRYFARYP GVKDYMERAK
     EQARDQGYVE TLFGRRLYLP EIGSRNPARR AQSERVAINA PMQGTAADII KRAMLKVAAR
     LEEGVLHARM IMQVHDELVL EVREDAVEAL RTAVVADMSG AAELAVDLVV DVGVGANWDA
     AH
//
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