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P19821

- DPO1_THEAQ

UniProt

P19821 - DPO1_THEAQ

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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:
EMBLi
GenBanki
DDBJi
Links Updated
J04639 Genomic DNA. Translation: AAA27507.1.
D32013 Genomic DNA. Translation: BAA06775.1.
PIRiA33530.
JX0359.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04639 Genomic DNA. Translation: AAA27507.1 .
D32013 Genomic DNA. Translation: BAA06775.1 .
PIRi A33530.
JX0359.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 111 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