ID A0A1M6N991_9BURK Unreviewed; 913 AA.
AC A0A1M6N991;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 ORFNames=SAMN05192548_1009150 {ECO:0000313|EMBL:SHJ92269.1};
OS Paraburkholderia terricola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=169427 {ECO:0000313|EMBL:SHJ92269.1, ECO:0000313|Proteomes:UP000184395};
RN [1] {ECO:0000313|EMBL:SHJ92269.1, ECO:0000313|Proteomes:UP000184395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20594 {ECO:0000313|EMBL:SHJ92269.1,
RC ECO:0000313|Proteomes:UP000184395};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FRAB01000009; SHJ92269.1; -; Genomic_DNA.
DR RefSeq; WP_073428626.1; NZ_FRAB01000009.1.
DR AlphaFoldDB; A0A1M6N991; -.
DR STRING; 169427.SAMN05192548_1009150; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000184395; Unassembled WGS sequence.
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 316..502
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 671..877
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 913 AA; 101512 MW; 7FAE25A2F642BD1B CRC64;
MPEERSLEGK TLLLVDGSSY LYRAYHAMPD LRGPEGGPTG ALYGMINMLR RMRKEVTAEY
SACVFDAKGK TFRDDWYADY KANRAAMPDD LSRQIEPIHV AVRALGWPLL MIDGVEADDV
IGTLSTEAEK RGMKVIVSTG DKDLAQLVSD HVTLINTMTN ETLDRAGVLA KFGVPPERIV
DYLSLIGDTV DNVPGVEKCG PKTALKWLAQ YETLDGIVAH ADEIKGAVGD NLRRALDFLP
MAKKLVTVER NCDLTDHIVS IEESLQSQPE SRAELREVFT RHGFKTWLRE VEIADAVEGP
ETDVSPALTV DHERHYEAVQ TWEQFDAWLE RLNAAELTSF DTETTSLDPM TAQIVGLSFA
VEAGRAAYVP LAHRGPDAPV QLPRDEVLGK LKPWLESAEH KKVGQHVKYD EQVLANYGIE
MRGIEHDTLL QSYVLESHRT HDMDSLALRH LGVKTIKYEE VAGKGAQQIG FDEVALDKAA
EYAAEDADIT LRLHQTLYPQ VAAEKTLEHV YRDIEVPTSR VLRKMERTGV LIDAEKLRQQ
SSEIATRLIQ LESEAYVLAG GEFNLGSPKQ IGQIFFEKLE LPVVKKTPSG APSTDEEVLQ
KLAEDYPLPK ILLEHRGLSK LKSTYTDKLP RMVNATTGRV HTNYAQAVAV TGRLASNDPN
LQNIPVRTGE GRRIREAFIA PPGHKLVSAD YSQIELRIMA HISGDESLLR AFSQGEDIHR
ATAAEIFSVT PLEVSNDQRR VAKVINFGLI YGMSSFGLAS NLGITRDAAK LYIDRYFARY
PGVARYMDET RVSAKAKGYV ETVFGRRLWL PEINGGNGPR RQAAERAAIN APMQGTAADL
IKLSMIAVQK WIEDSKIGTR MIMQVHDELI LEVPDEELSD VRKRLPELMC GVADLKVPLV
AEVGAGLNWE EAH
//
