UniProt: R5QGN0

Database: UniProt
Entry: R5QGN0_9FIRM

LinkDB:  R5QGN0_9FIRM 
Original site:  R5QGN0_9FIRM

All links

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)   

Download RDF

ID   R5QGN0_9FIRM            Unreviewed;       878 AA.
AC   R5QGN0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
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=BN526_00225 {ECO:0000313|EMBL:CCZ27773.1};
OS   Firmicutes bacterium CAG:194.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263008 {ECO:0000313|EMBL:CCZ27773.1, ECO:0000313|Proteomes:UP000018384};
RN   [1] {ECO:0000313|EMBL:CCZ27773.1, ECO:0000313|Proteomes:UP000018384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:194 {ECO:0000313|Proteomes:UP000018384};
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:CCZ27773.1}.
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; CAZT010000016; CCZ27773.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5QGN0; -.
DR   Proteomes; UP000018384; 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:UP000018384};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          3..264
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          636..842
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   878 AA;  100041 MW;  6B939AE16F1104C4 CRC64;
     MSEKLVLIDG HSILNRAFYG VPDLTNTEGL HTNAIYGFLN IMFKIIEEED PTYLAVAFDL
     SAPTFRHKMY DAYKGTRKPM PQELREQVPV MKEVLSAMGI LTMEQEGFEA DDILGTMAKR
     AEKEGVLVAL VSGDRDLLQI ATDKIKIRIP KTKGARTEIE DYYAKDVEEK YHVNPQQFIE
     LKALMGDTAD NIPGVPKVGE KTATALMEQY GSIENIYAHL EEISKNSIRT SLAENRELAD
     LSKKLATIDI DAPIRYTLAD ARTGNFYTPE AYAYMKKLAF KNMLSRFDAQ DRQESDVREN
     LCITEMQKAE EIFALCEKAE KTAFYVLGES VLLSCGQENY YIPAQGFLTF AYLQGKLQEL
     FEACKKEGHL LLTFDVKKFY GLFTMERADV SCFFDTKLAA YLLNPLKSEY TLEDIAQEYR
     NVMLMDYKQQ FGKKSVAESM ETEEEMFTQY AGGLIQTIYD CYEKLADALS QTAMKELYDE
     IEMPLTYVLY AMEKEGVIVQ KEELKHYGGQ LAERIAVVEQ RIYDTVGEKF NINSPKQLGV
     ILFEKMQLKG GKKTKTGYST AADILEKLAP DYPVVNDILE YRGLTKLKST YADGLADCIA
     EDGRIHTNFN QMITATGRIS STEPNLQNIP MRMELGRLIR KVFVPKPGCV FMDADYSQIE
     LRILAHMSED EELIEAYRMS EDIHRITASK VFHTPFEEVT DLQRRNAKAV NFGIVYGISS
     FGLSQDLSIS RKEASAYIEQ YFETYPGVKR FLDNCIAKAK ETGESRTMYG RRRPIPELSS
     SNFMQRQFGE RVAMNAPIQG TAADIMKIAM IRVYDSLKRE GLKSRILLQV HDELLLEVWE
     DEVEKVREIL MRDMKGAAEL SVSLEIDVHT GKNWYEAK
//

DBGET integrated database retrieval system