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P19821 (DPO1_THEAQ) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA polymerase I, thermostable

EC=2.7.7.7
Alternative name(s):
Taq polymerase 1
Gene names
Name:polA
Synonyms:pol1
OrganismThermus aquaticus
Taxonomic identifier271 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length832 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

Biotechnological use

Used in the PCR method because of its high thermostability. Has a relatively high error rate because it lacks exonuclease proofreading functionality.

Sequence similarities

Belongs to the DNA polymerase type-A family.

Contains 1 5'-3' exonuclease domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 832832DNA polymerase I, thermostable
PRO_0000101256

Regions

Region410 – 832423Polymerase By similarity

Experimental info

Sequence conflict1551V → A in BAA06775. Ref.2

Secondary structure

.................................................................................................................................................................... 832
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19821 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: F1731055B5246F03

FASTA83293,910
        10         20         30         40         50         60 
MRGMLPLFEP KGRVLLVDGH HLAYRTFHAL KGLTTSRGEP VQAVYGFAKS LLKALKEDGD 

        70         80         90        100        110        120 
AVIVVFDAKA PSFRHEAYGG YKAGRAPTPE DFPRQLALIK ELVDLLGLAR LEVPGYEADD 

       130        140        150        160        170        180 
VLASLAKKAE KEGYEVRILT ADKDLYQLLS DRIHVLHPEG YLITPAWLWE KYGLRPDQWA 

       190        200        210        220        230        240 
DYRALTGDES DNLPGVKGIG EKTARKLLEE WGSLEALLKN LDRLKPAIRE KILAHMDDLK 

       250        260        270        280        290        300 
LSWDLAKVRT DLPLEVDFAK RREPDRERLR AFLERLEFGS LLHEFGLLES PKALEEAPWP 

       310        320        330        340        350        360 
PPEGAFVGFV LSRKEPMWAD LLALAAARGG RVHRAPEPYK ALRDLKEARG LLAKDLSVLA 

       370        380        390        400        410        420 
LREGLGLPPG DDPMLLAYLL DPSNTTPEGV ARRYGGEWTE EAGERAALSE RLFANLWGRL 

       430        440        450        460        470        480 
EGEERLLWLY REVERPLSAV LAHMEATGVR LDVAYLRALS LEVAEEIARL EAEVFRLAGH 

       490        500        510        520        530        540 
PFNLNSRDQL ERVLFDELGL PAIGKTEKTG KRSTSAAVLE ALREAHPIVE KILQYRELTK 

       550        560        570        580        590        600 
LKSTYIDPLP DLIHPRTGRL HTRFNQTATA TGRLSSSDPN LQNIPVRTPL GQRIRRAFIA 

       610        620        630        640        650        660 
EEGWLLVALD YSQIELRVLA HLSGDENLIR VFQEGRDIHT ETASWMFGVP REAVDPLMRR 

       670        680        690        700        710        720 
AAKTINFGVL YGMSAHRLSQ ELAIPYEEAQ AFIERYFQSF PKVRAWIEKT LEEGRRRGYV 

       730        740        750        760        770        780 
ETLFGRRRYV PDLEARVKSV REAAERMAFN MPVQGTAADL MKLAMVKLFP RLEEMGARML 

       790        800        810        820        830 
LQVHDELVLE APKERAEAVA RLAKEVMEGV YPLAVPLEVE VGIGEDWLSA KE 

« Hide

References

[1]"Isolation, characterization, and expression in Escherichia coli of the DNA polymerase gene from Thermus aquaticus."
Lawyer F.C., Stoffel S., Saiki R.K., Myambo K., Drummond R., Gelfand D.H.
J. Biol. Chem. 264:6427-6437(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Overproduction of Thermus aquaticus DNA polymerase and its structural analysis by ion-spray mass spectrometry."
Ishino Y., Ueno T., Miyagi M., Uemori T., Imamura M., Tsunasawa S., Kato I.
J. Biochem. 116:1019-1024(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: YT1.
[3]"Crystal structure of Thermus aquaticus DNA polymerase."
Kim Y., Eom S.H., Wang J., Lee D.-S., Suh S.W., Steitz T.A.
Nature 376:612-616(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[4]"Crystal structure of the large fragment of Thermus aquaticus DNA polymerase I at 2.5-A resolution: structural basis for thermostability."
Korolev S., Nayal M., Barnes W.M., di Cera E., Waksman G.
Proc. Natl. Acad. Sci. U.S.A. 92:9264-9268(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 290-832.
[5]"Structure of Taq polymerase with DNA at the polymerase active site."
Eom S.H., Wang J., Steitz T.A.
Nature 382:278-281(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[6]"Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation."
Li Y., Korolev S., Waksman G.
EMBO J. 17:7514-7525(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 295-832.
[7]"Crystal structures of the Klenow fragment of Thermus aquaticus DNA polymerase I complexed with deoxyribonucleoside triphosphates."
Li Y., Kong Y., Korolev S., Waksman G.
Protein Sci. 7:1116-1123(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 290-832.
[8]"Structure-based design of Taq DNA polymerases with improved properties of dideoxynucleotide incorporation."
Li Y., Mitaxov V., Waksman G.
Proc. Natl. Acad. Sci. U.S.A. 96:9491-9496(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 293-831.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04639 Genomic DNA. Translation: AAA27507.1.
D32013 Genomic DNA. Translation: BAA06775.1.
PIRA33530.
JX0359.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BGXX-ray2.30T1-832[»]
1JXEX-ray2.85A293-832[»]
1KTQX-ray2.50A290-832[»]
1QSSX-ray2.30A293-831[»]
1QSYX-ray2.30A293-831[»]
1QTMX-ray2.30A293-831[»]
1TAQX-ray2.40A1-832[»]
1TAUX-ray3.00A1-832[»]
2KTQX-ray2.30A295-832[»]
3KTQX-ray2.30A293-832[»]
3LWLX-ray2.25A293-832[»]
3LWMX-ray2.19A293-832[»]
3M8RX-ray2.00A293-832[»]
3M8SX-ray2.20A293-832[»]
3OJSX-ray1.90A293-832[»]
3OJUX-ray2.00A293-832[»]
3PO4X-ray1.80A293-832[»]
3PO5X-ray2.39A293-832[»]
3PY8X-ray1.74A293-832[»]
3RR7X-ray1.95A293-832[»]
3RR8X-ray2.40A293-832[»]
3RRGX-ray2.30A293-832[»]
3RRHX-ray1.80A293-832[»]
3RTVX-ray1.90A293-832[»]
3SV3X-ray2.10A293-832[»]
3SV4X-ray1.99A293-832[»]
3SYZX-ray1.95A293-832[»]
3SZ2X-ray2.15A293-832[»]
3T3FX-ray1.90A293-832[»]
4BWJX-ray1.55A293-832[»]
4BWMX-ray1.75A293-832[»]
4C8KX-ray2.17A293-832[»]
4C8LX-ray1.70A293-832[»]
4C8MX-ray1.57A293-832[»]
4C8NX-ray1.88A293-832[»]
4C8OX-ray1.75A293-832[»]
4CCHX-ray2.55A293-832[»]
4DF4X-ray2.20A293-832[»]
4DF8X-ray2.00A293-832[»]
4DFJX-ray1.90A293-832[»]
4DFKX-ray1.65A293-832[»]
4DFMX-ray1.89A293-832[»]
4DFPX-ray2.00A293-832[»]
4DLEX-ray2.44A293-832[»]
4DLGX-ray1.89A293-832[»]
4ELTX-ray2.20A293-832[»]
4ELUX-ray1.80A293-832[»]
4ELVX-ray1.90A293-832[»]
4KTQX-ray2.50A294-832[»]
5KTQX-ray2.50A290-832[»]
ProteinModelPortalP19821.
SMRP19821. Positions 1-832.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP19821.
ChEMBLCHEMBL3564.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.420.10. 1 hit.
3.40.50.1010. 1 hit.
InterProIPR020046. 5-3_exonucl_a-hlix_arch_N.
IPR020045. 5-3_exonuclease_C.
IPR002421. 5-3_exonuclease_N.
IPR019760. DNA-dir_DNA_pol_A_CS.
IPR001098. DNA-dir_DNA_pol_A_palm_dom.
IPR018320. DNA_polymerase_1.
IPR002298. DNA_polymerase_A.
IPR008918. HhH2.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR029060. PIN_domain-like.
IPR012337. RNaseH-like_dom.
IPR015361. Taq_pol_thermo_exonuc.
[Graphical view]
PfamPF01367. 5_3_exonuc. 1 hit.
PF02739. 5_3_exonuc_N. 1 hit.
PF00476. DNA_pol_A. 1 hit.
PF09281. Taq-exonuc. 1 hit.
[Graphical view]
PRINTSPR00868. DNAPOLI.
SMARTSM00475. 53EXOc. 1 hit.
SM00278. HhH1. 2 hits.
SM00279. HhH2. 1 hit.
SM00482. POLAc. 1 hit.
[Graphical view]
SUPFAMSSF47807. SSF47807. 1 hit.
SSF53098. SSF53098. 1 hit.
SSF88723. SSF88723. 1 hit.
TIGRFAMsTIGR00593. pola. 1 hit.
PROSITEPS00447. DNA_POLYMERASE_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19821.

Entry information

Entry nameDPO1_THEAQ
AccessionPrimary (citable) accession number: P19821
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references