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Database: UniProt
Entry: A0A0R1XDK9_9LACO
LinkDB: A0A0R1XDK9_9LACO
Original site: A0A0R1XDK9_9LACO 
ID   A0A0R1XDK9_9LACO        Unreviewed;       886 AA.
AC   A0A0R1XDK9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 42.
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=FC91_GL002992 {ECO:0000313|EMBL:KRM26548.1};
OS   Schleiferilactobacillus harbinensis DSM 16991.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Schleiferilactobacillus.
OX   NCBI_TaxID=1122147 {ECO:0000313|EMBL:KRM26548.1, ECO:0000313|Proteomes:UP000050949};
RN   [1] {ECO:0000313|EMBL:KRM26548.1, ECO:0000313|Proteomes:UP000050949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16991 {ECO:0000313|EMBL:KRM26548.1,
RC   ECO:0000313|Proteomes:UP000050949};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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|RuleBase:RU004460}.
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:KRM26548.1}.
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DR   EMBL; AZFW01000071; KRM26548.1; -; Genomic_DNA.
DR   RefSeq; WP_027829238.1; NZ_AZFW01000071.1.
DR   AlphaFoldDB; A0A0R1XDK9; -.
DR   PATRIC; fig|1122147.4.peg.3081; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000050949; Unassembled WGS sequence.
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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000050949};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          5..268
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          642..850
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   886 AA;  99192 MW;  073DB3DE16D6BF99 CRC64;
     MPTTKKLLLV DGNSVAFRAF FAMHSALDSF INRDGLHTNA IFAFKRMLDN ILEQVDPTNV
     LVAFDAGKVT FRTKKFEEYK GTRAKMPGEL AEQLPFLHKL LDAYGIKWYE LKNYEADDII
     GTMAQEGAKA GMAVTVLSGD RDLTQLASDQ ITVQVTLKGV TELEAYTPAH FQEKLGITPK
     QLIDVKALMG DNSDNYPGVT KVGEKTALKL IQEYGSVENL YAHVADMKKS KMKENLINDK
     DMAFLSKDLA TIRTDAPITL GLADTVYPGP DNQALLALYQ ELDFNSFIKD LAPQEDDDAP
     VQKDLPVTAL TAANLPQALA GDAPKTFMIE MLGDNYHTEP VIAVGLGTPD QWYVATQDAI
     LREPALQTWL ADAQKVKYVF DAKRNYVAAH RFGATINGID FDMLLVSYLL NTVDNSNDLG
     SVAAQHGYTG VETDAAVYGT GKKRQVPDDQ AVFIQHIAHK LACVYNLQPQ LVKDLQAHEQ
     YTLYTDLERP LAIVLANMEI AGIKVLPDTL KAMGVSLKER LQDLENQIYT EAGHEFNINS
     TKQLGTVLFD EMKLPPIKKT KTGYSTSVAV LEKLQDESPI IQMILSYRQL AKIQSTYVEG
     LLSQIHPDGK IHTRYIQTLT QTGRLSSQDP NLQNIPMHQD EGKQIRKAFV PSHPGWQIFD
     SDYSQVELRV LAHVSGDRNM QEAFKENRDI HANTAMKIFH LTDPSQVTDN MRRQAKATNF
     GIVYGISDYG LSQNIGIPRE QAKAFIDAYF EQYPQVKDWT EQIVKTAREQ GYVETIMHRR
     RYLPDINAKN RNLRQFAERT AMNTPIQGSA ADIIKVAMIN MAQALKDQHL QATMLLQVHD
     ELLFEAPREE IPILEKLVPS IMDSAVKLAV PLKVDSSFGD TWYDVK
//
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