ID A0A0B0KMX0_9GAMM Unreviewed; 921 AA.
AC A0A0B0KMX0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=PJ15_3107 {ECO:0000313|EMBL:KHF76353.1};
OS Acinetobacter sp. neg1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1561068 {ECO:0000313|EMBL:KHF76353.1, ECO:0000313|Proteomes:UP000030886};
RN [1] {ECO:0000313|EMBL:KHF76353.1, ECO:0000313|Proteomes:UP000030886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=neg1 {ECO:0000313|Proteomes:UP000030886};
RA Chiara M., Horner D.S., Pesole G., Mule' G., Logrieco A., Fanelli F.;
RT "Genome Sequencing of an Acinetobacter spp capable to degrade OTA.";
RL Submitted (NOV-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHF76353.1}.
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DR EMBL; JSZD01000017; KHF76353.1; -; Genomic_DNA.
DR RefSeq; WP_047431770.1; NZ_JSZD01000017.1.
DR AlphaFoldDB; A0A0B0KMX0; -.
DR PATRIC; fig|1561068.3.peg.2699; -.
DR Proteomes; UP000030886; 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 1..256
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 327..514
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 681..885
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
FT REGION 277..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 102865 MW; 90786020D169C57F CRC64;
MPPFVLVDGS YFLFRAFHAL PPLTTSTGLH TNAIRGAISA IQKLMRRTQP THMAVIFDTP
EPTFRHKLSP IYKGDRPSMP EELSQQIPYL HALIRAQGIP LYSLPGAEAD DIIGTLTKRA
LAEGHHVLIS TGDKDMAQLV NEHVKLEDSF KERVLDEAGV FEKFGVHPNQ IIDYLTLMGD
ASDGIMGVPG VGAKTAAKLL NEYGTLSNII ANADQLKSKI SQNIKDNVEN IKIDHQLASI
VCDLDLALDW HDLKLTNPNV DQLRNLYTEL EFRNQLQSLD HPNNPNSSAY QQTSQSIAKA
EQKTEQVVVE DHASLSSQDD QLGTATYHTV LSQQDWDALL QRMQQADHFA IDTETTNLDY
RFAELVGFSV AFDANDAYYV PVAHDYEGAP EQLNREQVLA QIKPILENEQ VKKIGHHLKY
DAHIFANHGI TIQGWYFDTM LASYVLNAAA TRHGMDDVAR LYLSHLTTTF EQIAGKGAKQ
KTFNQIELEV AAHYAAEDAH VTYRLYEVLA AKLKAHPELV NILHNIEMPV ARVLTGMEED
GIKLDHQFLD QLSVEFSETI QTLEAQAAEL AGEAFNVASP KQVGEVLFEK LGLKGGKKTA
TGQYSTSESI LEKIEHPLAE VILEHRSLAK LKNTYTDRLI VQSNDTTHRV HTSYHQALTA
TGRLSSTDPN LQNIPIRTPI GRQIRKAFIA PEGRVLLAAD YSQIELRLMA HFSQDDALVH
AFQQGQDVHR RTASEVLGID IEDVTNDQRR QAKAVNFGLL YGMSEFGLTR QLGFTREESR
SYIARYFQRY PGVLDYMERT RQIAREQGFV ETILGRRLYT PDIMATNKMI KQAAERAAIN
APLQGSAADI IKLAMIAVDK MLPKDQAKLL LQVHDELVFE ADAAIADELS KQIAEVMQSV
LQISVPFVVE VGQGLNWDAA H
//
