UniProt: R6SFZ6

Database: UniProt
Entry: R6SFZ6_9FIRM

LinkDB:  R6SFZ6_9FIRM 
Original site:  R6SFZ6_9FIRM

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (20)   
   InterPro (13)   
   Pfam (3)   
   PROSITE (1)   
   SMART (3)   
All databases (27)   

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ID   R6SFZ6_9FIRM            Unreviewed;       875 AA.
AC   R6SFZ6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN   Name=polA {ECO:0000256|RuleBase:RU004460};
GN   ORFNames=BN586_01146 {ECO:0000313|EMBL:CDC54351.1};
OS   Dorea formicigenerans CAG:28.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX   NCBI_TaxID=1263073 {ECO:0000313|EMBL:CDC54351.1, ECO:0000313|Proteomes:UP000018109};
RN   [1] {ECO:0000313|EMBL:CDC54351.1, ECO:0000313|Proteomes:UP000018109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:28 {ECO:0000313|Proteomes:UP000018109};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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|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:CDC54351.1}.
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DR   EMBL; CBFN010000033; CDC54351.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6SFZ6; -.
DR   Proteomes; UP000018109; Unassembled WGS sequence.
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:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
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; 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; 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};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018109};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          7..268
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          633..839
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   875 AA;  99180 MW;  2D954EDED62EB557 CRC64;
     MSENTNKKIV LIDGHSILNR AFFGLPDLTN SEGLHTNAIY GFLTIMFKIL DEEKPDYLTV
     AFDVHAPTFR HKMYDAYKGT RKPMADELRQ QVPVIKEVLC SMGIKTIECA GLEADDLLGT
     LSRRCEEKGM EVSVISGDRD LLQLATQHVK IRIPKTKQGR TEVEDYYAAD VKERYQVTPK
     EFIDLKALMG DTADNIPGVP SIGEKTATKI ITEYHSIENA YEHVSELKPP RASKALAEHW
     DMAVMSKTLA TIEVHADFPY ELSEAKLGNI FTEEAYAFFQ KLQFKNLLSK FDVTASANQV
     EDGFEQITDY KKAEKVLNQA KESTCVGAVI FQNTENVLPL FANEAAIGGI GLCFDEEHAY
     CIEVTEQITK EFLLEKLSKL NESCGRFVMF DIKEAMKWLP IKNQKHCFDA TVAAYLLNPL
     KNDYTYEDVA REQLNIVIEE KSEAYVKVCY EAYTAFKGSD LLYKKLEETQ MLHLFENIEM
     PLVFTLYDME RNGIRAEGEA LKVYSSQLGG RISELEKEIY EMAGESFNIN SPKQLGVILF
     EKLLLPGSKK TKSGYSTAAS VLDKLAPDYP IVSKVLEYRQ LTKLKSTYAD GLVNYIEEDG
     RIHSKFNQTI TATGRISSTE PNLQNIPVRV ELGRLIRKVF VPEDGYIFVD ADYSQIELRV
     LAHCSGDANL IEAYREEKDI HRITASQVFH IPFEEVTPLQ RRNAKAVNFG IVYGISSFGL
     SEDLSIGRKE AAKYIEDYFK TYPGIKTFLD DTVAHAKEMG YVVTLFGRRR PVPELSSSNF
     MQRSFGERVA MNAPIQGTAA DIMKIAMIGV NRRLKEQNLK SRLVLQVHDE LLIEAYRPEL
     PEVEKILREE MEQAASLDVP LEIDMHTGEN WYEAK
//

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