(data stored in SCRATCH zone)

SWISSPROT: Q3KKA6_PSEPF

ID   Q3KKA6_PSEPF            Unreviewed;       935 AA.
AC   Q3KKA6;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 124.
DE   RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN   Name=polA {ECO:0000256|RuleBase:RU004460};
GN   OrderedLocusNames=Pfl01_0056 {ECO:0000313|EMBL:ABA71800.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA71800.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA71800.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA71800.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 5'-3' exonuclease activity.
CC       {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-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU004460};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|RuleBase:RU004460}.
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DR   EMBL; CP000094; ABA71800.1; -; Genomic_DNA.
DR   RefSeq; WP_011331779.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0056; -.
DR   EnsemblBacteria; ABA71800; ABA71800; Pfl01_0056.
DR   KEGG; pfo:Pfl01_0056; -.
DR   eggNOG; ENOG4105C2M; Bacteria.
DR   eggNOG; COG0258; LUCA.
DR   eggNOG; COG0749; LUCA.
DR   HOGENOM; HOG000020999; -.
DR   KO; K02335; -.
DR   OMA; ETGRVHT; -.
DR   BioCyc; PFLU205922:G1G4S-57-MONOMER; -.
DR   Proteomes; UP000002704; 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-dependent DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
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; 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   PANTHER; PTHR10133; PTHR10133; 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; 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;
DR   PRODOM; Q3KKA6.
DR   SWISS-2DPAGE; Q3KKA6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   DNA damage {ECO:0000256|RuleBase:RU004460};
KW   DNA repair {ECO:0000256|RuleBase:RU004460};
KW   DNA replication {ECO:0000256|RuleBase:RU004460};
KW   DNA-binding {ECO:0000256|RuleBase:RU004460,
KW   ECO:0000256|SAAS:SAAS00882656};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU004460};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00427537};
KW   Nuclease {ECO:0000256|SAAS:SAAS00427491};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU004460,
KW   ECO:0000313|EMBL:ABA71800.1};
KW   Transferase {ECO:0000256|RuleBase:RU004460,
KW   ECO:0000313|EMBL:ABA71800.1}.
FT   DOMAIN        4    266       53EXOc. {ECO:0000259|SMART:SM00475}.
FT   DOMAIN      328    523       3'-5' exonuclease. {ECO:0000259|SMART:
FT                                SM00474}.
FT   DOMAIN      693    899       POLAc. {ECO:0000259|SMART:SM00482}.
SQ   SEQUENCE   935 AA;  102210 MW;  FC33A41F2AA21E5D CRC64;
     MSQAPLVLVD GSSYLYRAFH ALPPLTTSKG LPTGAVKGVL NMLKSLRKQY PDSPFAVVFD
     AKGGTFRDEM YAEYKANRPS MPDDMRVQIE PLHQSVIALG FPLLCVEGVE ADDVIGTLAR
     SSAAADRPVI ISTGDKDMAQ LVDGHITLVN TMSGSSMDVD GVKEKFGVAP EQIIDYLALM
     GDSSDNIPGV PGIGPKTASG LLVGVNGGLT ELYAQLDIVP TLPIRGAKTL PAKLEEHKEM
     AFLSYQLATI KVDVPLDIGL DDLQMGPEDP AKLYELYTLL EFKSWLNDLD RDAKRQELSA
     AAEPVPAGDL FSAPAEEEAP AAPAEAAYET ILDQARFDVW LEKLKNAKLF AFDTETTGID
     AQQAQLVGLS FAVQANEAAY IPLTHSYIGV PEQLDRDTVL RALKPILEDP NKLKVGQHAK
     FDMNILANCA IGGDQNEGIT VRGIAFDTML ESYVLNSTAT RHDMDSLAQK YLDHTTVSFQ
     DIAGKGAKQL TFDQIALEQA GPYAAEDADV TLRLHQTLFD KLSAIPSLAS VLTDIEIPLV
     PVLARIERQG AFVDAELLGI QSIELGNKMI ALEREAFEIA GEEFNLGSPK QLGVILYEKL
     GLPVLKKTAK GQPSTAEEVL AKLAEDDHRL PKVLMEHRSM SKLKSTYTDR LPEQINPRTG
     RIHTSYHQAV ASTGRLSSSD PNLQNIPVRT AEGRRIRQAF VAPKGYKLLA ADYSQIELRI
     MAHLSRDEGL MNAFRNNLDV HTATAAEVFK VELNEVTSDQ RRGAKAINFG LIYGMGAQKL
     GKDIGVDTKT AKAYIDTYFA RYPGVREYMD RTRAQAADQG FVETIFGRRL YLPDINSNKP
     QERAAAERTA INAPMQGTAA DIIKKAMVAV DNWLCASGLD AKVILQVHDE LVLEVREDLV
     DQVREEIRVH MSEAAKLDVP LLVEVGVGNN WDEAH
//

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