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Database: UniProt/TrEMBL
Entry: B1Z156_BURA4
LinkDB: B1Z156_BURA4
Original site: B1Z156_BURA4 
ID   B1Z156_BURA4            Unreviewed;       917 AA.
AC   B1Z156;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 105.
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   OrderedLocusNames=BamMC406_3769 {ECO:0000313|EMBL:ACB66236.1};
OS   Burkholderia ambifaria (strain MC40-6).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=398577 {ECO:0000313|EMBL:ACB66236.1, ECO:0000313|Proteomes:UP000001680};
RN   [1] {ECO:0000313|Proteomes:UP000001680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC40-6 {ECO:0000313|Proteomes:UP000001680};
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA   Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia ambifaria MC40-6.";
RL   Submitted (APR-2008) 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}.
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; CP001026; ACB66236.1; -; Genomic_DNA.
DR   RefSeq; WP_012365627.1; NC_010552.1.
DR   AlphaFoldDB; B1Z156; -.
DR   KEGG; bac:BamMC406_3769; -.
DR   HOGENOM; CLU_004675_0_0_4; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000001680; 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-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR   CDD; cd06139; DNA_polA_I_Ecoli_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   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; 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   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          9..264
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          320..506
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          675..881
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   917 AA;  100869 MW;  864D46427AF48D36 CRC64;
     MPEERNLEGK TLLLVDGSSY LYRAYHAMPD LRGPGGEPTG ALYGIINMLR RMRKEVSAEY
     SACVFDAKGK TFRDDLYADY KANRPSMPPD LALQVEPIHG AVRALGWPLL MVEGVEADDV
     IGTLAREAER HGMNVIVSTG DKDLAQLVSD RVTLVNTMTN ETLDRDGVIA KFGVPPERII
     DYLALIGDTV DNVPGVEKCG PKTAVKWLSQ YDSLDGVIEH AGEIKGVVGD NLRRALDFLP
     LGRTLVTVET ACDLAPHLES IEASLRTDGE ARDLLRDIFA RYGFKTWLRE VESAPAEGGG
     ADAPEGDPAP VIAADIVREY DTIQTWAQFD AWFAKIDAAA LTAFDTETTA LDPMIARLVG
     LSFSIEPGKA AYLPVAHRGP DMPEQLPIDE VLARLKPWLE SADRKKVGQH LKYDAQVLAN
     YGIELNGIEH DTLLESYVLE SHRTHDMDSL ALRHLGVKTI KYEDVAGKGA KQIGFDEVAL
     EQAAAYAAED ADITLQLHQA LYPQVAREAG LERVYRDIEM PVSLVLRKME RTGVLIDDAL
     LQAQSTEIAT RLIELEGQAY ELAGGEFNLG SPKQIGQIFF EKLQLPVVKK TPSGAPSTDE
     EVLQKLAEDY PLPKLLLEHR GLSKLKSTYT DKLPRMVNPA TGRVHTNYAQ AVAVTGRLAS
     NDPNLQNIPV RTAEGRRIRE AFIASPGHRI VSADYSQIEL RIMAHISGDA SLLRAFAQGE
     DIHRATAAEV FGVTPLEVNS DQRRIAKVIN FGLIYGMSAF GLASNLGITR DAAKLYIDRY
     FTRYPGVAQY MEDTRTAAKD KGYVETVFGR RLWLPEINGG NGPRRQAAER AAINAPMQGT
     AADLIKLSMI AVDDWLTRDR LASRMIMQVH DELVLEVPDD ELSLVREKLP EMMCGVAKLK
     VPLVAEVGAG ANWEEAH
//
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