GenomeNet

Database: UniProt
Entry: A0A263HDX9_9PAST
LinkDB: A0A263HDX9_9PAST
Original site: A0A263HDX9_9PAST 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system