UniProt: A0A1J0A5M3

Database: UniProt
Entry: A0A1J0A5M3_9ENTE

LinkDB:  A0A1J0A5M3_9ENTE 
Original site:  A0A1J0A5M3_9ENTE

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (22)   
   InterPro (14)   
   Pfam (3)   
   PROSITE (1)   
   SMART (4)   
All databases (31)   

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ID   A0A1J0A5M3_9ENTE        Unreviewed;       883 AA.
AC   A0A1J0A5M3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=BHY08_04985 {ECO:0000313|EMBL:APB31237.1};
OS   Vagococcus teuberi.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX   NCBI_TaxID=519472 {ECO:0000313|EMBL:APB31237.1, ECO:0000313|Proteomes:UP000191200};
RN   [1] {ECO:0000313|EMBL:APB31237.1, ECO:0000313|Proteomes:UP000191200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21459 {ECO:0000313|EMBL:APB31237.1,
RC   ECO:0000313|Proteomes:UP000191200};
RA   Wullschleger S., Seifert C., Baumgartner S., Lacroix C., Bonfoh B.,
RA   Stevens M.J., Meile L.;
RT   "Vagococcus teuberi sp. nov., isolated from the Malian artisanal sour milk
RT   fene.";
RL   Submitted (SEP-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}.
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DR   EMBL; CP017267; APB31237.1; -; Genomic_DNA.
DR   RefSeq; WP_071456825.1; NZ_CP017267.1.
DR   AlphaFoldDB; A0A1J0A5M3; -.
DR   STRING; 519472.BHY08_04985; -.
DR   KEGG; vte:BHY08_04985; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000191200; 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:UP000191200};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          4..267
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          306..473
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          639..847
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   883 AA;  100470 MW;  4AF1A3A73618AF4E CRC64;
     MAKKKLLLVD GNSIAFRGFY ALYQSLERFK NNNGLHTNAL YAVNNMLENI LAKEEPTHVL
     VAFDAGKTTF RHAFYDDYKA GRAKTPSEFK EQMPYLRDLI EGLGMKHFEL DNYEADDIIG
     TLATKYGSQD VDVVVLSGDK DLTQLASEYT TVDVTVKGVS EIESYTPEHI MEKYGLTPPQ
     IVDMKGLAGD QSDNIPGVTK IGEKTAIKLL KEYGTVEGVY EYVDEMKKSK MKENLINEKD
     IAFLSKKLAT IDTNVPLDMT LDDLAYDGKN LEKLIPFYKE MDFNSFLAKL DTSNVESDLV
     EKVAIHYEVI SEITEDMFES DMSLYVEMLG ENYHTSPIVG VAFGNKEKVY VSDDIELLSH
     PLMIQWLEDN EKTKKVFDAK RQYVALNRYG IKLNDIKFDM LLAAYLADST NNSEDLAQIA
     HFYDYYDVDR DEVVYGKGAK KGLPESVDTL YQHLARKVVA IDVLYETIMT DLDDKNQSDL
     FYDIELPIAL ILADMEIEGI TVNASRLQEM KGEFAERLGE IEQTIYEIAG EEFNINSPKQ
     LGVILFEKMG LPVIKKTKTG YSTAVDVLEK LKGESPIIES ILSYRQLAKI QSTYVEGLLK
     VIFEDNKIHT RYIQTLTQTG RLSSVDPNLQ NIPIRLEEGR KIRQAFVPRE KGWKLFASDY
     SQIELRVLAA ISDDEHLKEA FIEGLDIHSS TAMRVFGIEK AEDVDSNMRR QAKAVNFGIV
     YGISDYGLSQ NLGITRKEAQ EFIDRYFTMY PGVKTYMEDI VREAKDKGYV ETLYHRRRYL
     PDINARNFNL RSFAERTAIN TPIQGSAADI LKIAMIKINK RLKEENMQAT MLLQVHDELV
     FEAPEEEIPA LQKLVEDTMN HAVDLSVPLR ADSSYGDTWY DAK
//

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