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Database: UniProt
Entry: A0A150LZT3_9BACI
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ID   A0A150LZT3_9BACI        Unreviewed;       890 AA.
AC   A0A150LZT3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=B4135_2376 {ECO:0000313|EMBL:KYD17705.1};
OS   Caldibacillus debilis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX   NCBI_TaxID=301148 {ECO:0000313|EMBL:KYD17705.1, ECO:0000313|Proteomes:UP000075683};
RN   [1] {ECO:0000313|EMBL:KYD17705.1, ECO:0000313|Proteomes:UP000075683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4135 {ECO:0000313|EMBL:KYD17705.1,
RC   ECO:0000313|Proteomes:UP000075683};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA   Eijlander R.T., Kuipers O.P.;
RT   "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT   Foods.";
RL   Submitted (JAN-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:KYD17705.1}.
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DR   EMBL; LQYT01000053; KYD17705.1; -; Genomic_DNA.
DR   RefSeq; WP_061569093.1; NZ_LQYT01000053.1.
DR   AlphaFoldDB; A0A150LZT3; -.
DR   STRING; 301148.B4135_2376; -.
DR   PATRIC; fig|301148.3.peg.3881; -.
DR   Proteomes; UP000075683; 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   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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          17..276
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          315..480
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          647..854
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   890 AA;  100811 MW;  0D6A9E6F13A942FC CRC64;
     MRVFFFAETV GGIILANKLI LIDGNSIAYR AFFALPLLNN DKGIHTNAIY GFALMLSKIL
     EEEKPTHMLA AFDAGKTTFR HQTFKDYKGG RQKTPPELSE QFPFIRELLE AYGVATYELE
     LYEADDIIGT MARMAEQEGF ETIIVTGDRD LTQLVSGRTT VYVTKKGVTE MEKYTPEHIR
     EKYGLSVSQL VDMKGLMGDA SDNIPGVPGI GEKTAIKLLK EFSSVENLIR SIDRVGGKKL
     QETLAAYKDQ ALMSKELATI ERNAPVEISL SDIAYTGEKK EKMAALFKEL GFQSFLEKMD
     DIPAEKKEPL KNIEYAFLEE IDDSVLLNPS ALYMEMIEEN YHRAPILGFS LANASGNYFL
     PTETALRSPA FQKWLADEKK KKFVYDGKKM MVALKRHGLE INGIDFDLLL ASYLLNPSES
     LGDFADAAAV HGYTDVLSDD EFYGKGAKRT VPGERERAEH IVRKALAIYA LKDRLIRQLE
     ENKQDELFFR LEMPLSRILA EMEMTGVRVD TGRLIEMGKE FAGKLEEIEA EIHRLAGEPF
     NINSPKQLGT ILYEKLKLPV LKKTKTGYST SADTLEKLQH QHEIVDKILH YRQLGKLQST
     YIDGLLKVVN KETGKVHTRF NQALTQTGRL SSTDPNLQNI PIRLEEGRKI RQAFIPSEKD
     WLILSADYSQ IELRVLAHIS GDKNLIDAFL KDMDIHTSTA MNVFHVEKDQ VTPEMRRQAK
     AVNFGIVYGI SDYGLSQNLG ISRKEAAAFI ERYFQIYPGV KQFMEDIVKE AKQTGYVTTL
     LNRRRYIPEI TSRNYNLRSF AERTAMNTPI QGSAADIIKK AMIDMAERLK KEKLKARMLL
     QVHDELIFEA PKEEIGRLCQ IVPEVMEGAV ELKVPLKVDV AYGPTWYDAK
//
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