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DescriptionRecName: Full=DNA polymerase I; Short=POL I; EC=2.7.7.7;
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MyHits synonymsDPO1_SALTY , Q9F173 , FF887BF1039C160A
match map segment
ipfam:5_3_exonuc_N ismart:35EXOc ismart:HhH2 ismart:53EXOc ipfam:DNA_pol_A ipfam:DNA_pol_A_exo1 ipfam:5_3_exonuc ismart:POLAc ipat:DNA_POLYMERASE_A  
Legends: 1, CONFLICT G -> R (in Ref. 1; AAG43170). {ECO:0000305}; 2, CONFLICT M -> T (in Ref. 1; AAG43170). {ECO:0000305}; 3, CONFLICT L -> I (in Ref. 1; AAG43170). {ECO:0000305}; 4, ipfam:5_3_exonuc_N [T]; 5, ismart:HhH2 [T]; 6, ipfam:DNA_pol_A_exo1 [T]; 7, ipfam:5_3_exonuc [T]; 8, ipat:DNA_POLYMERASE_A [T].
ID   DPO1_SALTY              Reviewed;         928 AA.
AC   Q9F173;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   10-MAY-2017, entry version 117.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA; OrderedLocusNames=STM3999;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RA   Huang Y.P., Ito J.;
RT   "DNA polymerase I sequence from Salmonella typhimurium.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 3'-5' and 5'-3' exonuclease activity. It is able to
CC       utilize nicked circular duplex DNA as a template and can unwind
CC       the parental DNA strand from its template.
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1).
CC   -!- SUBUNIT: Single-chain monomer with multiple functions.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000305}.
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DR   EMBL; AF071212; AAG43170.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL22838.1; -; Genomic_DNA.
DR   RefSeq; NP_462879.1; NC_003197.2.
DR   RefSeq; WP_000249972.1; NC_003197.2.
DR   ProteinModelPortal; Q9F173; -.
DR   SMR; Q9F173; -.
DR   STRING; 99287.STM3999; -.
DR   PaxDb; Q9F173; -.
DR   PRIDE; Q9F173; -.
DR   EnsemblBacteria; AAL22838; AAL22838; STM3999.
DR   GeneID; 1255525; -.
DR   KEGG; stm:STM3999; -.
DR   PATRIC; 32386868; VBISalEnt20916_4214.
DR   eggNOG; ENOG4105C2M; Bacteria.
DR   eggNOG; COG0258; LUCA.
DR   eggNOG; COG0749; LUCA.
DR   HOGENOM; HOG000020999; -.
DR   KO; K02335; -.
DR   OMA; CFDTETT; -.
DR   PhylomeDB; Q9F173; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IBA:GO_Central.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.40.50.1010; -; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR020045; 5-3_exonuclease_C.
DR   InterPro; IPR002421; 5-3_exonuclease_N.
DR   InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR018320; DNA_polymerase_1.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN_domain-like.
DR   InterPro; IPR012337; RNaseH-like_dom.
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; SSF47807; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   TIGRFAMs; TIGR00593; pola; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   Complete proteome; DNA damage; DNA repair; DNA replication;
KW   DNA-binding; DNA-directed DNA polymerase; Exonuclease; Hydrolase;
KW   Nuclease; Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN         1    928       DNA polymerase I.
FT                                /FTId=PRO_0000101252.
FT   DOMAIN        1    323       5'-3' exonuclease.
FT   DOMAIN      324    517       3'-5' exonuclease.
FT   REGION      324    928       Klenow fragment.
FT   REGION      521    928       Polymerase.
FT   CONFLICT    751    751       G -> R (in Ref. 1; AAG43170).
FT                                {ECO:0000305}.
FT   CONFLICT    848    848       M -> T (in Ref. 1; AAG43170).
FT                                {ECO:0000305}.
FT   CONFLICT    867    867       L -> I (in Ref. 1; AAG43170).
FT                                {ECO:0000305}.
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CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         9    170       ipfam:5_3_exonuc_N [T]
FT   MYHIT       330    517       ismart:35EXOc [T]
FT   MYHIT       173    208       ismart:HhH2 [T]
FT   MYHIT         7    268       ismart:53EXOc [T]
FT   MYHIT       552    925       ipfam:DNA_pol_A [T]
FT   MYHIT       330    517       ipfam:DNA_pol_A_exo1 [T]
FT   MYHIT       171    270       ipfam:5_3_exonuc [T]
FT   MYHIT       686    892       ismart:POLAc [T]
FT   MYHIT       754    773       ipat:DNA_POLYMERASE_A [T]
SQ   SEQUENCE   928 AA;  103129 MW;  FF887BF1039C160A CRC64;
     MVQIPENPLI LVDGSSYLYR AYHAFPPLTN SAGEPTGAMY GVLNMLRSLI MQYQPTHAAV
     VFDAKGKTFR DELFEHYKSH RPPMPDDLRA QIEPLHAMVK AMGLPLLAVS GVEADDVIGT
     LAREAEKVGR PVLISTGDKD MAQLVTPNIT LINTMTNTIL GPDEVVNKYG VPPELIIDFL
     ALMGDSSDNI PGVPGVGEKT AQALLQGLGG LDTLYAEPEK IAGLTFRGAK TMAGKLAQNK
     DVAYLSYKLA TIKTDVELEL TCEQLEVQQP IADELLGLFK KYEFKRWTAD VESGKWLQAK
     GAKPAAKPQE TVVIDESPSE PAAALSYENY VTILDDVTLE SWIEKLKKAP VFAFDTETDS
     LDNIAANLVG LSFAIEPGVA AYVPVAHDYL DAPDQISRQR ALELLKPLLE DEKVRKVGQN
     LKYDRGVLQN YGIELRGIAF DTMLESYILN SVAGRHDMDS LSDRWLKHKT ITFEDIAGKG
     KNQLTFNQIA LEEAGRYAAE DADVTLQLHL KMWPELQQHK GPLNVFENIE MPLVPVLSRV
     ERNGVKIDPA VLHKHSEEIT LRLAELEKKA HDIAGEAFNL SSTKQLQTIL FEKQGIKPLK
     KTPGGAPSTS EEVLEELALD YPLPKVILEY RGLAKLKSTY TDKLPLMINP KTGRVHTSYH
     QAVTATGRLS STDPNLQNIP VRNEEGRRIR QAFIAPEDYL IVSADYSQIE LRIMAHLSRD
     KGLLTAFAEG KDIHRATAAE VFGLPLDSVT GEQRRSAKAI NFGLIYGMSA FGLSRQLNIP
     RKEAQKYMDL YFERYPGVLE YMERTRAQAK EQGYVETLEG RRLYLPDIKS SNAARRAGAE
     RAAINAPMQG TAADIIKRAM IAVDAWLQAE QPRVRMIMQV HDELVFEVHK DDLDAVAKRI
     HQLMENCTRI DVPLLVEVGS GENWDQAH
//