ID A0A1N7S6H7_9BURK Unreviewed; 915 AA.
AC A0A1N7S6H7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ECO:0000313|EMBL:SIT43011.1};
GN ORFNames=BN2476_340022 {ECO:0000313|EMBL:SIT43011.1};
OS Paraburkholderia piptadeniae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1701573 {ECO:0000313|EMBL:SIT43011.1, ECO:0000313|Proteomes:UP000195569};
RN [1] {ECO:0000313|EMBL:SIT43011.1, ECO:0000313|Proteomes:UP000195569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 7183 {ECO:0000313|EMBL:SIT43011.1,
RC ECO:0000313|Proteomes:UP000195569};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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; CYGY02000034; SIT43011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7S6H7; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000195569; 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, ECO:0000313|EMBL:SIT43011.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000313|EMBL:SIT43011.1};
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 318..504
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 673..879
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 915 AA; 101431 MW; 4A8EED5ECE62DE05 CRC64;
MPEEQNLEGK TLLLVDGSSY LYRAYHAMPD LRGPDGGPTG ALYGIINMLR RMRKEVTAEY
SACVFDAKGK TFRDDWYPQY KAHRPSMPED LAKQIEPIHV AVRSLGWPLL MIEGVEADDV
IGTLARRAEQ RGMNVIVSTG DKDLAQLVTD HVTLINTMTN EKLDREGVVA KFGVPPERIV
DYLSLIGDTV DNVPGVEKCG PKTALKWLTQ FETLDGIVAH ADEIKGAVGD NLRRALDFLP
MAKKLVTVET DCDLTGHVNS FEETLATRPE AREELRDIFT RHGFKTWLRE VEIADAVEGP
ETDVPPAPTV DGENVREYDT VQTWEQLDAW LAKLDAADIT SFDTETTSLD PMIAQIVGIS
IAVEAGKAAY IPLAHRGPDA PVQLPRDEVL AKLKPWLESA DKKKVGQHVK YDEQVLANYG
IAMNGIEHDT LLQSYVLESH RPHDMDNLAL RHLGLTTIKY EDVAGKGASQ IGFDEVSLDK
ASEYAAEDAD ITLRLHHALF PQIAAEVPLD HVYRNIEVPT SRVLRKMERN GVLIDAEKLR
VQSNEIATRL VELEKEAYEL AGGEFNLGSP KQIGQIFFER LELPVIKKTP SGAPSTDEEV
LQKLAEDFPL PKILLEHRGL SKLKSTYTDK LPRMVNATTG RVHTNYAQAV AVTGRLASND
PNLQNIPVRT GEGRRIREAF IAPPGHKLVS ADYSQIELRI MAHISGDEAL LRAFKQGEDI
HRATASEVFS VTPLEVSNDQ RRIAKVINFG LIYGMSSFGL ASNLGITRDA AKLYIDRYFA
RYPGVAAYME NTRSSAKAKG YVETVFGRRL WLPEINGGNG PRRQAAERAA INAPMQGTAA
DLIKMSMIAV QKWIEESGIG TRMIMQVHDE LILEVPDAEL SYVRKRLPEL MCGVAQLKVP
LVAEVGAGAN WEEAH
//
