ID A0A263HDX9_9PAST Unreviewed; 959 AA.
AC A0A263HDX9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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:SUU37649.1};
GN ORFNames=NCTC10851_01667 {ECO:0000313|EMBL:SUU37649.1};
OS Actinobacillus seminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=722 {ECO:0000313|EMBL:SUU37649.1, ECO:0000313|Proteomes:UP000254507};
RN [1] {ECO:0000313|EMBL:SUU37649.1, ECO:0000313|Proteomes:UP000254507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10851 {ECO:0000313|EMBL:SUU37649.1,
RC ECO:0000313|Proteomes:UP000254507};
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; UFSB01000001; SUU37649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263HDX9; -.
DR InParanoid; A0A263HDX9; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000254507; 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:SF27; DNA POLYMERASE NU; 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|RuleBase:RU004460};
KW DNA repair {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}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU004460};
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 339..548
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 718..923
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 959 AA; 106223 MW; 12FBD572B3DE6788 CRC64;
MAQIAENPLV LVDGSSYLYR AFHAFPSLTN SLGEPTGAMY GVLNMLKSLI SQVQPTHIAV
VFDAKGKTFR DEMFEQYKSH RPPMPDELRS QILPLHNIIK ALGIPLLVVE GVEADDVIGT
LALQASKKGQ KVLISTGDKD MAQLVDDNIM LINTMNNTLL DRAGVIEKYG IPPELIIDYL
ALMGDSSDNI PGVAGVGEKT ALGLLQGIGS MAEIYANLDK VADLPIRGAK KLGEKLQAAK
ADADLSYLLA TIKTDVALAL TPDQLTLGQN DNDQLIEYFA RYEFKRWLNE VMSGESSLTN
GAEQRGLSIA YQATATLPQA EKTEKSAVKN VIKIDRTLYQ QIDTQEKLAA WIAKINAAKL
IAIDTETDCL DAMSANLVGI SIALEHGEAC YIPLAHVREV SVAQPQGDLF SEDKVAGEAC
FEQVLPQLSL EDCLAQLKPL LEDPQIRKVG QNLKYDLIVL ANYNVQLAGV AFDTMLESYV
LNSTGRHNMD DLAERYLGYQ TIAFETLAGK GKNQLTFDKI DLAQATEYAA EDADVTMKLH
QTLWQELSQM PELANLFNEI ELPLVKVLSR IERHGVLINP QTLLAQSEEI AQRLTALEQA
VHQEAGEVFN LASTKQLQEI LFEKLGLPVI AKTPKGAPST NEEVLEELAQ QGHVVPKLLI
EHRGLAKLKS TYTDKLPQMI NPRTGRVHTS YHQAVTITGR LSSSDPNLQN IPIRNEEGRR
IRQAFVAPQD FSIVAADYSQ IELRLMAHLS QDPNLIKAFV EGKDVHRSTA AEIFGLPMDS
VTNEQRRRAK AINFGLIYGM SAFGLARQLG IGRNEAQQYI NLYFQRYPGV QTFMTEIREK
AKAQGYVETL FGRRLYLPEI HSSKAMRRKG AERVAINAPM QGTAADIIKR AMIALDREIA
QDPDIRMIMQ VHDELVFEVR SNKVEKYRQL IKKTMENAAK LAVPLIVDVG VGVNWDEAH
//