Back to PBIL home page
ID B1K3T6_BURCC Unreviewed; 917 AA.
AC B1K3T6;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 08-MAY-2019, entry version 82.
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 OrderedLocusNames=Bcenmc03_3655 {ECO:0000313|EMBL:ACA92807.1};
OS Burkholderia cenocepacia (strain MC0-3).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=406425 {ECO:0000313|EMBL:ACA92807.1, ECO:0000313|Proteomes:UP000002169};
RN [1] {ECO:0000313|Proteomes:UP000002169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC0-3 {ECO:0000313|Proteomes:UP000002169};
RA Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-
RT 3.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 5'-3' exonuclease activity.
CC {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-
CC COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC Evidence={ECO:0000256|RuleBase:RU004460};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000256|RuleBase:RU004460}.
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; CP000959; ACA92807.1; -; Genomic_DNA.
DR RefSeq; WP_011548155.1; NC_010515.1.
DR EnsemblBacteria; ACA92807; ACA92807; Bcenmc03_3655.
DR KEGG; bcm:Bcenmc03_3655; -.
DR HOGENOM; HOG000020999; -.
DR KO; K02335; -.
DR OMA; ETGRVHT; -.
DR BioCyc; BCEN406425:G1GBC-3882-MONOMER; -.
DR Proteomes; UP000002169; Chromosome 2.
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-dependent DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd09898; H3TH_53EXO; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR002421; 5-3_exonuclease_N.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
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 PANTHER; PTHR10133; PTHR10133; 1.
DR Pfam; PF01367; 5_3_exonuc; 1.
DR Pfam; PF02739; 5_3_exonuc_N; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR Pfam; PF01612; DNA_pol_A_exo1; 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; SSF47807; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
DR TIGRFAMs; TIGR00593; pola; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
DR PRODOM; B1K3T6.
DR SWISS-2DPAGE; B1K3T6.
KW Complete proteome {ECO:0000313|Proteomes:UP000002169};
KW DNA damage {ECO:0000256|RuleBase:RU004460};
KW DNA repair {ECO:0000256|RuleBase:RU004460};
KW DNA replication {ECO:0000256|RuleBase:RU004460};
KW DNA-binding {ECO:0000256|RuleBase:RU004460,
KW ECO:0000256|SAAS:SAAS00882656};
KW DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU004460};
KW Hydrolase {ECO:0000256|SAAS:SAAS00427537};
KW Nuclease {ECO:0000256|SAAS:SAAS00427491};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU004460,
KW ECO:0000313|EMBL:ACA92807.1};
KW Transferase {ECO:0000256|RuleBase:RU004460,
KW ECO:0000313|EMBL:ACA92807.1}.
FT DOMAIN 9 264 53EXOc. {ECO:0000259|SMART:SM00475}.
FT DOMAIN 320 506 3'-5' exonuclease. {ECO:0000259|SMART:
FT SM00474}.
FT DOMAIN 675 881 POLAc. {ECO:0000259|SMART:SM00482}.
SQ SEQUENCE 917 AA; 100960 MW; 763960D6E0959B0E CRC64;
MPEERNLEGK TLLLVDGSSY LYRAYHAMPD LRGPGGEPTG ALYGIINMLR RMRKEVSAEY
SACVFDAKGK TFRDDLYADY KANRPSMPPD LALQVEPIHG AVRALGWPLL MVEGVEADDV
IGTLAREAER HGMNVIVSTG DKDLAQLVTE RVTLVNTMTN ETLDRDGVIA KFGVPPERII
DYLALIGDTV DNVPGVEKCG PKTAVKWLTQ YDTLDGVIEH AADIKGVVGD NLRRALDFLP
LGRQLVTVDT SCDLTPHLES IEASLKSDGE ARDLLRDIFA RYGFKTWLRE VDSAPAEGGG
ADAPEGEPAP VIAADVVREY DTIQTWEQFD AWFAKIDAAA LTAFDTETTA LDPMLARLVG
LSFSVEPGKA AYLPVAHRGP DMPEQLPLDE VLARLKPWLE SADRKKVGQH LKYDAQVLAN
YDIALNGIEH DTLLESYVVE SHRTHDMDSL ALRHLGVKTI KYEDVAGKGA KQIGFDEVAL
AQAAEYAAED ADITLQLHHA LYPQVAREPG LERVYREIEM PVSLVLRKME RTGVLIDDAR
LHAQSTEIAT RLIELEGEAY ELAGGEFNLG SPKQIGQIFF EKLQLPVVKK TPSGAPSTDE
EVLQKLAEDY PLPKLLLEHR GLSKLKSTYT DKLPRMVNPT TGRVHTNYAQ AVAVTGRLAS
NDPNLQNIPV RTAEGRRIRE AFIASPGHRI VSADYSQIEL RIMAHISGDA SLLRAFSQGE
DIHRATAAEV FGVTPLEVNS DQRRIAKVIN FGLIYGMSAF GLASNLGITR DAAKLYIDRY
FARYPGVAQY MEDTRATAKE KGYVETVFGR RLWLPEINGG NGPRRQAAER AAINAPMQGT
AADLIKLSMI AVDGWLTRDQ LASRMIMQVH DELVLEVPEG ELSLVREKLP EMMCGVAKLK
VPLVAEVGAG ANWEEAH
//
Back to PBIL home page