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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//