Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P19821

- DPO1_THEAQ

UniProt

P19821 - DPO1_THEAQ

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

DNA polymerase I, thermostable

Gene

polA

Organism
Thermus aquaticus
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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

        10         20         30         40         50
MRGMLPLFEP KGRVLLVDGH HLAYRTFHAL KGLTTSRGEP VQAVYGFAKS
60 70 80 90 100
LLKALKEDGD AVIVVFDAKA PSFRHEAYGG YKAGRAPTPE DFPRQLALIK
110 120 130 140 150
ELVDLLGLAR LEVPGYEADD VLASLAKKAE KEGYEVRILT ADKDLYQLLS
160 170 180 190 200
DRIHVLHPEG YLITPAWLWE KYGLRPDQWA DYRALTGDES DNLPGVKGIG
210 220 230 240 250
EKTARKLLEE WGSLEALLKN LDRLKPAIRE KILAHMDDLK LSWDLAKVRT
260 270 280 290 300
DLPLEVDFAK RREPDRERLR AFLERLEFGS LLHEFGLLES PKALEEAPWP
310 320 330 340 350
PPEGAFVGFV LSRKEPMWAD LLALAAARGG RVHRAPEPYK ALRDLKEARG
360 370 380 390 400
LLAKDLSVLA LREGLGLPPG DDPMLLAYLL DPSNTTPEGV ARRYGGEWTE
410 420 430 440 450
EAGERAALSE RLFANLWGRL EGEERLLWLY REVERPLSAV LAHMEATGVR
460 470 480 490 500
LDVAYLRALS LEVAEEIARL EAEVFRLAGH PFNLNSRDQL ERVLFDELGL
510 520 530 540 550
PAIGKTEKTG KRSTSAAVLE ALREAHPIVE KILQYRELTK LKSTYIDPLP
560 570 580 590 600
DLIHPRTGRL HTRFNQTATA TGRLSSSDPN LQNIPVRTPL GQRIRRAFIA
610 620 630 640 650
EEGWLLVALD YSQIELRVLA HLSGDENLIR VFQEGRDIHT ETASWMFGVP
660 670 680 690 700
REAVDPLMRR AAKTINFGVL YGMSAHRLSQ ELAIPYEEAQ AFIERYFQSF
710 720 730 740 750
PKVRAWIEKT LEEGRRRGYV ETLFGRRRYV PDLEARVKSV REAAERMAFN
760 770 780 790 800
MPVQGTAADL MKLAMVKLFP RLEEMGARML LQVHDELVLE APKERAEAVA
810 820 830
RLAKEVMEGV YPLAVPLEVE VGIGEDWLSA KE
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