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Entry: A0A1V2A910_9BACI
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ID   A0A1V2A910_9BACI        Unreviewed;       874 AA.
AC   A0A1V2A910;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=BTO28_05875 {ECO:0000313|EMBL:OMP67473.1};
OS   Domibacillus epiphyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX   NCBI_TaxID=1714355 {ECO:0000313|EMBL:OMP67473.1, ECO:0000313|Proteomes:UP000188613};
RN   [1] {ECO:0000313|EMBL:OMP67473.1, ECO:0000313|Proteomes:UP000188613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAB 38 {ECO:0000313|EMBL:OMP67473.1,
RC   ECO:0000313|Proteomes:UP000188613};
RA   Verma A., Ojha A.K., Krishnamurthi S.;
RT   "Domibacillus sp. SAB 38T whole genome sequencing.";
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, 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:OMP67473.1}.
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DR   EMBL; MSFI01000009; OMP67473.1; -; Genomic_DNA.
DR   RefSeq; WP_076764605.1; NZ_MSFI01000009.1.
DR   AlphaFoldDB; A0A1V2A910; -.
DR   STRING; 1714355.BTO28_05875; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000188613; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000188613};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          3..262
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          299..464
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          631..838
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   COILED          495..522
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   874 AA;  98685 MW;  818ED1ABD23C3154 CRC64;
     MNKKLVLIDG NSIAYRAFFA LPLLSNSKGI HTNAVYGFAM MLNKIVKDEQ PSHILVAFDA
     GKTTFRHETY KEYKGTRQKT PPELSEQFSY VRELLKAYGI PYYELENYEA DDIIGTLSLE
     AENNGFQVKV YSGDKDLTQL ATEKTTVCIT RKGITDIEEY TPEHVREKYG LTPDQIIDMK
     GLMGDSSDNI PGVPGIGEKT AVKLLKQFHS VEALLESIDD VSGAKLKEKL HDNKDMALLS
     KELATIMRNV PLDVTTDRLI YSGSNEDQLY DLFRELEFKT LIEGLNRTEQ VEETSDVLFN
     TITKPEPKHF ECAESLYVEM IDVNYHKSPV AAIAVSGSGM TYFMTGETAL ASDAFKNWAE
     EKSIRKTVFD AKRTVIALRR HGIELAGIDF DVFLASYLIN PSESPDDFAG VAKLHGETGI
     ASDEAVYGKG AKRAIPVEED FAKHVSAKAE ALSRLDDTCR RELSENSQNE LFDELELPLA
     LILADMESEG VRVDMDRLEE MGAELKKRLE EMERTIHELA GTEFNINSPK QLGVILFEKL
     GLPPLKKTKT GYSTSAEVLE KLAPSHEIVR HILDYRQIGK LQSTYIEGLL KVADPETNKI
     HTRFNQALTQ TGRLSSTEPN LQNIPIRLEE GRKIRQAFIP EKKDSVMFAA DYSQIELRVL
     AHICGDEKLM EAFRQDMDIH TATAMEVFHV GQEDVTSNMR RQAKAVNFGI VYGISDYGLS
     QNLGITRKEA AEFIERYLNT YPGVKEYMDD IIREAKEKGY VTTLLNRRRY IPEITSRNFN
     LRSFGERTAM NTPIQGSAAD IIKKAMIDVA ERIEKESLTS KLLLQVHDEL IFDVPKEEIA
     AMERIVPEVM EHAFELDVPL KVDYSFGPTW YDAK
//
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