UniProt: F4HEL1

Database: UniProt
Entry: F4HEL1_GALAU

LinkDB:  F4HEL1_GALAU 
Original site:  F4HEL1_GALAU

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (23)   
   InterPro (14)   
   Pfam (4)   
   PROSITE (1)   
   SMART (4)   
Literature (1)   
   PubMed (1)   
All databases (33)   

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ID   F4HEL1_GALAU            Unreviewed;       925 AA.
AC   F4HEL1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
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   OrderedLocusNames=UMN179_00831 {ECO:0000313|EMBL:AEC16861.1};
OS   Gallibacterium anatis (strain UMN179) (Pasteurella anatis).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Gallibacterium.
OX   NCBI_TaxID=1005058 {ECO:0000313|EMBL:AEC16861.1, ECO:0000313|Proteomes:UP000006908};
RN   [1] {ECO:0000313|EMBL:AEC16861.1, ECO:0000313|Proteomes:UP000006908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN179 {ECO:0000313|EMBL:AEC16861.1,
RC   ECO:0000313|Proteomes:UP000006908};
RX   PubMed=21602325; DOI=10.1128/JB.05177-11;
RA   Johnson T.J., Fernandez-Alarcon C., Bojesen A.M., Nolan L.K., Trampel D.W.,
RA   Seemann T.;
RT   "Complete genome sequence of Gallibacterium anatis strain UMN179, isolated
RT   from a laying hen with peritonitis.";
RL   J. Bacteriol. 193:3676-3677(2011).
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; CP002667; AEC16861.1; -; Genomic_DNA.
DR   RefSeq; WP_013745647.1; NC_015460.1.
DR   AlphaFoldDB; F4HEL1; -.
DR   STRING; 1005058.UMN179_00831; -.
DR   KEGG; gan:UMN179_00831; -.
DR   PATRIC; fig|1005058.3.peg.817; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_6; -.
DR   Proteomes; UP000006908; Chromosome.
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          7..270
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          329..515
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          684..889
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   925 AA;  104101 MW;  C8CD5F58D90BEC8D CRC64;
     MPQIAENPFV LVDGSSYLYR AYHANFRLGL SNSAGEPTGA MYGVLNMLKS LLKEVNPTHI
     AVVFDAKGKT FRDEMFEQYK SHRPPMPEDL RQQIQPLHQM IEALGLPLLI VEGVEADDVI
     GTLAKQASAA GREVLISTGD KDMAQLVDDK IMLINTMTNT LLDREGVIEK YEVPPELIID
     LLALMGDSSD NIPGVPSVGN KTAIALLQGL GGIADIYSQL DKVTDLPIRG AKKLADKLLA
     GKEDADLSYK LATIKTDVPL DVTFEQLTLQ PENRDQLIEY YARYEFKRWL NELLNENTVS
     TAQNSSTMVK ATPSREIQSS AIKVDRSRYQ TILTEEQLQQ WREKLSNASL FAIDTETNSL
     NYMQAKLVGL SFALENGEAA YLPLQHHYLD CPQQLSWKTV LAALKTVLED PNIKKVGQNL
     KYDLTILARH GVELQGVVYD TMLESYTLDS TGRHNMDDLA KRFLHHDTIH FEDLAGKGKG
     QLTFDQIEID KAAEYAAEDA DVTFKLHQVL WPQLNQTPSL VKLFTEVELP LSQVLARMER
     NGVLIDSDLL YQQSQEINAR LIQLEQQAHQ LAGQAFNLAS TKQLQEILFG KLGLPVLKKT
     PKGAPSTNEE VLEELAYEHE LPKLLVEHRG FSKLKSTYTD KLPQMIDPNT GRVHTSYHQA
     VTITGRLSSS DPNLQNIPTR SEEGRKIRQA FIAPQGFKVV AADYSQIELR IMAHLSADAG
     LAYAFSHGLD VHRSTAAEVF DVPLEQVTSQ QRYRAKAINF GLIYGMSAFG LARQLQIPRN
     EAQTYIDRYF HRYPGVKQFM NDIQEKAKQQ GYVETLLGRR LYLPELKSSN GMRRKAAERV
     AINAPMQGTA ADIIKKAMID IDRFIADKND IRMIMQVHDE LVFEVKEDKV EYYEKIIKDM
     MENAVKLSVP LIVEVNFGDN WDQAH
//

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