(data stored in SCRATCH zone)

SWISSPROT: B1K3T6_BURCC

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}.
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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
//

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