ID A0A378AUX8_KLEPO Unreviewed; 861 AA.
AC A0A378AUX8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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_1 {ECO:0000313|EMBL:STV22060.1};
GN Synonyms=polA {ECO:0000256|RuleBase:RU004460};
GN ORFNames=NCTC5050_03372 {ECO:0000313|EMBL:STV22060.1};
OS Klebsiella pneumoniae subsp. ozaenae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=574 {ECO:0000313|EMBL:STV22060.1, ECO:0000313|Proteomes:UP000255382};
RN [1] {ECO:0000313|EMBL:STV22060.1, ECO:0000313|Proteomes:UP000255382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5050 {ECO:0000313|EMBL:STV22060.1,
RC ECO:0000313|Proteomes:UP000255382};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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; UGLZ01000005; STV22060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A378AUX8; -.
DR Proteomes; UP000255382; 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 Reference proteome {ECO:0000313|Proteomes:UP000255382};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 7..268
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 332..519
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 688..861
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 861 AA; 95347 MW; 3D33A6F47FF2D446 CRC64;
MVQIPENPLI LVDGSSYLYR AYHAFPPLTN SAGEPTGAMY GVLNMLRSLI LQYQPTHAVV
VFDAKGKTFR DELFEHYKSH RPPMPDDLRA QIEPLHKMVK AMGLPLMAVP GVEADDVIGT
LAREAERAGR PVLISTGDKD MAQLVTPGIT LINTMTNTIL GPDEVVTKYG VPPELIIDFL
ALMGDSSDNI PGVPGVGEKT AQALLQGLGG LDTLYAEPEK IAELSFRGAK TMAAKLEQNK
DVAYLSYQLA TIKTDVELEL TCEELEVQPP AADDLLALFR QYEFKRWTTD VEAGKWLQAK
GGKPAAKPAV PAAAAEAEEE VEAATALSAE HYVTILDEAT LLTWIDKLKQ APLFAFDTET
DSLDNISANM VGLSFAVEPG VAAYVPVAHD YLDAPDQIPR ERVLTLLKPL LEDEKVLKVG
QNLKYDRGIL ANYDIELRGI AFDTMLESYI LDSVAGRHDM DSLSDRWLKH KTITFEEIAG
KGKNQLTFNQ IALEEAGRYA AEDADVTLQL HLKMWPKLQQ HEGPLNIFQH IEMPLVPVLS
RVERNGVKID PAVLHAHSQE IAQRLVELEQ RAHEIAGEAF NLSSTKQLQT ILFEKQGIKP
LKKTPGGAPS TSEEVLEELA LDYPLPKVIL EYRGLAKLKS TYTDKLPLMI NPKTGRVHTS
YHQAVTATGR LSSTDPNLQN IPVRNEEGRR IRQAFIAPED YVIVSADYSQ IELRIMAHLS
RDKGLLTAFA EGKDIHRATA AEVFGLPLDS VSSEQRRSAK AINFGLIYGM SAFGLARQLN
IPRKEAQKYM DLYFERYPGV LEYMERTRAQ AKEQGYVETL DGRRLYLPDI KSSNGARRAG
AERAAINAPM QGRLRILSSG R
//
