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Database: UniProt
Entry: A0A2L0D6L8_9STRE
LinkDB: A0A2L0D6L8_9STRE
Original site: A0A2L0D6L8_9STRE 
ID   A0A2L0D6L8_9STRE        Unreviewed;       878 AA.
AC   A0A2L0D6L8;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
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   ECO:0000313|EMBL:AUW97493.1};
GN   ORFNames=C0J00_00980 {ECO:0000313|EMBL:AUW97493.1};
OS   Streptococcus pluranimalium.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=82348 {ECO:0000313|EMBL:AUW97493.1, ECO:0000313|Proteomes:UP000238956};
RN   [1] {ECO:0000313|EMBL:AUW97493.1, ECO:0000313|Proteomes:UP000238956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH11417 {ECO:0000313|EMBL:AUW97493.1,
RC   ECO:0000313|Proteomes:UP000238956};
RA   Hurst M.R.H.;
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AUW97493.1, ECO:0000313|Proteomes:UP000238956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH11417 {ECO:0000313|EMBL:AUW97493.1,
RC   ECO:0000313|Proteomes:UP000238956};
RA   Zhang J.-R., Hu G.-Z.;
RT   "Whole genome sequencing analysis of Streptococcus pluranimalium isolated
RT   from cattle infected mastitis in China.";
RL   Submitted (FEB-2018) 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, 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; CP025536; AUW97493.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2L0D6L8; -.
DR   KEGG; splr:C0J00_00980; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000238956; 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; 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; 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   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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238956};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          6..269
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          299..466
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          634..842
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   878 AA;  99266 MW;  915F2DCBE2B39634 CRC64;
     MTNAKNKLLL IDGSSVAFRA FFALYNQIDR FKNASGLHTN AIYGFHLMLD HLMERVQPTH
     ILVAFDAGKT TFRTEMYADY KAGRAKTPDE FREQFPYIRD MLAARGVPFY DLDNYEADDI
     IGTLDKMAEL DDFDVTIVSG DKDLIQLTDQ NTVVEISKKG VAEFEEFTPA YLMEKMGITP
     EQFIDLKALM GDKSDNIPGV TKIGEKTGLK LLLEHGSLEG IYNNIDGMKQ SKMKENLIKD
     KELAFLSKTL ATINTKAPIT IDLSDTVYMG PKVEELAKFY DEMGFTQFKN ALVGQAETPT
     FDTPFEEVST VTDKHFSDQD FFYFEMLNDN YHVEEIIGFA WGTKETIYAS TNLDLLQEPA
     FQEALAKPMQ TFDFKRVKVL LSHHGIDIPA PRFDSRLAKY LLSTVEDNQL STIARLYTAL
     PLENDEVVYG KGAKRAVPEK EVLLGHLAKK VQVLIESKEP MLAKLEENDQ IDLLFDMEQP
     LANVLAKMEI AGIKVNGGTL AEMALENQVS IDKLTQEIYE IAGQEFNINS PKQLGVLLFE
     TMGLPLEYTK KTKTGYSTAV DVLERLAPIS PIVSKILEYR QITKLQSTYL IGLQEYIRDD
     GKIHTRYVQD LTQTGRLSST DPNLQNIPIR LEQGRLIRKA FTPSTDKAVL LSSDYSQIEL
     RVLAHISGDE HLIDAFKHGA DIHTSTAMRV FGIEKPEDVT SNDRRNAKAV NFGIVYGISD
     FGLSNNLGIP RKLAKEYIET YFERYPGIKN YMETVVREAK DKGYVETLFK RRRELPDINS
     RNFNVRHFAE RTAINSPIQG SAADILKIAM INLDKALIDG NFKTKMLLQV HDEIVLEVPE
     DEIPAIQKLV KEVMEAAVEM TVPLLAEESY GQTWYEAK
//
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