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P19821

- DPO1_THEAQ

UniProt

P19821 - DPO1_THEAQ

Protein

DNA polymerase I, thermostable

Gene

polA

Organism
Thermus aquaticus
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. DNA-directed DNA polymerase activity Source: UniProtKB-KW
    3. nucleoside binding Source: InterPro

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair, DNA replication

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase I, thermostable (EC:2.7.7.7)
    Alternative name(s):
    Taq polymerase 1
    Gene namesi
    Name:polA
    Synonyms:pol1
    OrganismiThermus aquaticus
    Taxonomic identifieri271 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

    Pathology & Biotechi

    Biotechnological usei

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 832832DNA polymerase I, thermostablePRO_0000101256Add
    BLAST

    Interactioni

    Structurei

    Secondary structure

    1
    832
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 176
    Helixi22 – 254
    Helixi26 – 283
    Beta strandi36 – 383
    Beta strandi42 – 443
    Helixi47 – 537
    Helixi54 – 563
    Beta strandi60 – 656
    Beta strandi69 – 713
    Beta strandi73 – 753
    Helixi76 – 794
    Turni80 – 823
    Helixi95 – 973
    Helixi99 – 1057
    Beta strandi109 – 1113
    Beta strandi114 – 1163
    Helixi118 – 13215
    Beta strandi134 – 1396
    Helixi143 – 1486
    Beta strandi150 – 1567
    Beta strandi158 – 1603
    Helixi168 – 1714
    Helixi176 – 1783
    Turni179 – 1846
    Beta strandi189 – 1913
    Beta strandi199 – 2013
    Turni203 – 2075
    Helixi208 – 2103
    Beta strandi212 – 2143
    Beta strandi216 – 2205
    Turni226 – 2283
    Helixi230 – 2334
    Beta strandi236 – 2394
    Helixi242 – 2443
    Helixi266 – 2738
    Turni274 – 2774
    Helixi279 – 28810
    Beta strandi295 – 2973
    Beta strandi298 – 3003
    Beta strandi306 – 3149
    Turni316 – 3183
    Beta strandi321 – 3288
    Beta strandi331 – 3344
    Helixi338 – 3425
    Beta strandi346 – 3483
    Helixi353 – 36210
    Helixi373 – 3808
    Helixi387 – 3948
    Helixi402 – 41918
    Turni420 – 4223
    Helixi424 – 4329
    Helixi434 – 44714
    Beta strandi449 – 4513
    Helixi453 – 47826
    Helixi487 – 4959
    Turni507 – 5093
    Helixi513 – 5153
    Helixi516 – 5205
    Turni521 – 5255
    Helixi528 – 54417
    Turni545 – 5484
    Helixi549 – 5524
    Turni555 – 5573
    Beta strandi558 – 5603
    Beta strandi563 – 5675
    Beta strandi570 – 5723
    Beta strandi575 – 5795
    Helixi581 – 5833
    Beta strandi586 – 5883
    Helixi589 – 5957
    Beta strandi604 – 6118
    Helixi614 – 62310
    Helixi626 – 6338
    Helixi638 – 64710
    Helixi651 – 6533
    Helixi656 – 67015
    Helixi675 – 6806
    Turni681 – 6833
    Helixi686 – 69914
    Helixi701 – 71717
    Beta strandi718 – 7214
    Beta strandi723 – 7253
    Beta strandi727 – 7293
    Helixi731 – 7344
    Helixi738 – 77538
    Beta strandi778 – 7825
    Beta strandi784 – 7929
    Helixi793 – 7953
    Helixi796 – 80914
    Beta strandi819 – 8268
    Helixi829 – 8313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP19821.
    SMRiP19821. Positions 1-832.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19821.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni410 – 832423PolymeraseBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the DNA polymerase type-A family.Curated
    Contains 1 5'-3' exonuclease domain.Curated

    Family and domain databases

    Gene3Di3.30.420.10. 1 hit.
    3.40.50.1010. 1 hit.
    InterProiIPR020046. 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]
    PfamiPF01367. 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]
    PRINTSiPR00868. DNAPOLI.
    SMARTiSM00475. 53EXOc. 1 hit.
    SM00278. HhH1. 2 hits.
    SM00279. HhH2. 1 hit.
    SM00482. POLAc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47807. SSF47807. 1 hit.
    SSF53098. SSF53098. 1 hit.
    SSF88723. SSF88723. 1 hit.
    TIGRFAMsiTIGR00593. pola. 1 hit.
    PROSITEiPS00447. DNA_POLYMERASE_A. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19821-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRGMLPLFEP KGRVLLVDGH HLAYRTFHAL KGLTTSRGEP VQAVYGFAKS    50
    LLKALKEDGD AVIVVFDAKA PSFRHEAYGG YKAGRAPTPE DFPRQLALIK 100
    ELVDLLGLAR LEVPGYEADD VLASLAKKAE KEGYEVRILT ADKDLYQLLS 150
    DRIHVLHPEG YLITPAWLWE KYGLRPDQWA DYRALTGDES DNLPGVKGIG 200
    EKTARKLLEE WGSLEALLKN LDRLKPAIRE KILAHMDDLK LSWDLAKVRT 250
    DLPLEVDFAK RREPDRERLR AFLERLEFGS LLHEFGLLES PKALEEAPWP 300
    PPEGAFVGFV LSRKEPMWAD LLALAAARGG RVHRAPEPYK ALRDLKEARG 350
    LLAKDLSVLA LREGLGLPPG DDPMLLAYLL DPSNTTPEGV ARRYGGEWTE 400
    EAGERAALSE RLFANLWGRL EGEERLLWLY REVERPLSAV LAHMEATGVR 450
    LDVAYLRALS LEVAEEIARL EAEVFRLAGH PFNLNSRDQL ERVLFDELGL 500
    PAIGKTEKTG KRSTSAAVLE ALREAHPIVE KILQYRELTK LKSTYIDPLP 550
    DLIHPRTGRL HTRFNQTATA TGRLSSSDPN LQNIPVRTPL GQRIRRAFIA 600
    EEGWLLVALD YSQIELRVLA HLSGDENLIR VFQEGRDIHT ETASWMFGVP 650
    REAVDPLMRR AAKTINFGVL YGMSAHRLSQ ELAIPYEEAQ AFIERYFQSF 700
    PKVRAWIEKT LEEGRRRGYV ETLFGRRRYV PDLEARVKSV REAAERMAFN 750
    MPVQGTAADL MKLAMVKLFP RLEEMGARML LQVHDELVLE APKERAEAVA 800
    RLAKEVMEGV YPLAVPLEVE VGIGEDWLSA KE 832
    Length:832
    Mass (Da):93,910
    Last modified:February 1, 1991 - v1
    Checksum:iF1731055B5246F03
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti155 – 1551V → A in BAA06775. (PubMed:7896728)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04639 Genomic DNA. Translation: AAA27507.1.
    D32013 Genomic DNA. Translation: BAA06775.1.
    PIRiA33530.
    JX0359.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04639 Genomic DNA. Translation: AAA27507.1 .
    D32013 Genomic DNA. Translation: BAA06775.1 .
    PIRi A33530.
    JX0359.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BGX X-ray 2.30 T 1-832 [» ]
    1JXE X-ray 2.85 A 293-832 [» ]
    1KTQ X-ray 2.50 A 290-832 [» ]
    1QSS X-ray 2.30 A 293-831 [» ]
    1QSY X-ray 2.30 A 293-831 [» ]
    1QTM X-ray 2.30 A 293-831 [» ]
    1TAQ X-ray 2.40 A 1-832 [» ]
    1TAU X-ray 3.00 A 1-832 [» ]
    2KTQ X-ray 2.30 A 295-832 [» ]
    3KTQ X-ray 2.30 A 293-832 [» ]
    3LWL X-ray 2.25 A 293-832 [» ]
    3LWM X-ray 2.19 A 293-832 [» ]
    3M8R X-ray 2.00 A 293-832 [» ]
    3M8S X-ray 2.20 A 293-832 [» ]
    3OJS X-ray 1.90 A 293-832 [» ]
    3OJU X-ray 2.00 A 293-832 [» ]
    3PO4 X-ray 1.80 A 293-832 [» ]
    3PO5 X-ray 2.39 A 293-832 [» ]
    3PY8 X-ray 1.74 A 293-832 [» ]
    3RR7 X-ray 1.95 A 293-832 [» ]
    3RR8 X-ray 2.40 A 293-832 [» ]
    3RRG X-ray 2.30 A 293-832 [» ]
    3RRH X-ray 1.80 A 293-832 [» ]
    3RTV X-ray 1.90 A 293-832 [» ]
    3SV3 X-ray 2.10 A 293-832 [» ]
    3SV4 X-ray 1.99 A 293-832 [» ]
    3SYZ X-ray 1.95 A 293-832 [» ]
    3SZ2 X-ray 2.15 A 293-832 [» ]
    3T3F X-ray 1.90 A 293-832 [» ]
    4BWJ X-ray 1.55 A 293-832 [» ]
    4BWM X-ray 1.75 A 293-832 [» ]
    4C8K X-ray 2.17 A 293-832 [» ]
    4C8L X-ray 1.70 A 293-832 [» ]
    4C8M X-ray 1.57 A 293-832 [» ]
    4C8N X-ray 1.88 A 293-832 [» ]
    4C8O X-ray 1.75 A 293-832 [» ]
    4CCH X-ray 2.55 A 293-832 [» ]
    4DF4 X-ray 2.20 A 293-832 [» ]
    4DF8 X-ray 2.00 A 293-832 [» ]
    4DFJ X-ray 1.90 A 293-832 [» ]
    4DFK X-ray 1.65 A 293-832 [» ]
    4DFM X-ray 1.89 A 293-832 [» ]
    4DFP X-ray 2.00 A 293-832 [» ]
    4DLE X-ray 2.44 A 293-832 [» ]
    4DLG X-ray 1.89 A 293-832 [» ]
    4ELT X-ray 2.20 A 293-832 [» ]
    4ELU X-ray 1.80 A 293-832 [» ]
    4ELV X-ray 1.90 A 293-832 [» ]
    4KTQ X-ray 2.50 A 294-832 [» ]
    5KTQ X-ray 2.50 A 290-832 [» ]
    ProteinModelPortali P19821.
    SMRi P19821. Positions 1-832.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P19821.
    ChEMBLi CHEMBL3564.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P19821.

    Family and domain databases

    Gene3Di 3.30.420.10. 1 hit.
    3.40.50.1010. 1 hit.
    InterProi IPR020046. 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 ]
    Pfami PF01367. 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 ]
    PRINTSi PR00868. DNAPOLI.
    SMARTi SM00475. 53EXOc. 1 hit.
    SM00278. HhH1. 2 hits.
    SM00279. HhH2. 1 hit.
    SM00482. POLAc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47807. SSF47807. 1 hit.
    SSF53098. SSF53098. 1 hit.
    SSF88723. SSF88723. 1 hit.
    TIGRFAMsi TIGR00593. pola. 1 hit.
    PROSITEi PS00447. DNA_POLYMERASE_A. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiDPO1_THEAQ
    AccessioniPrimary (citable) accession number: P19821
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3