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Q7SIG7

- DPOL_DESST

UniProt

Q7SIG7 - DPOL_DESST

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Protein

DNA polymerase

Gene

pol

Organism
Desulfurococcus sp. (strain Tok)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Thermostable DNA polymerase. In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 2 magnesium ions.1 Publication

Enzyme regulationi

DNA polymerase activity strongly inhibited by uracil-containing oligonucleotides.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi141 – 1411Magnesium 11 Publication
Metal bindingi141 – 1411Magnesium 21 Publication
Metal bindingi143 – 1431Magnesium 21 Publication
Metal bindingi315 – 3151Magnesium 11 Publication
Metal bindingi315 – 3151Magnesium 21 Publication

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. DNA-directed DNA polymerase activity Source: UniProtKB-KW
  3. exonuclease activity Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW
  5. nucleotide binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase (EC:2.7.7.7)
Alternative name(s):
D Tok Pol
Gene namesi
Name:pol
OrganismiDesulfurococcus sp. (strain Tok)
Taxonomic identifieri108142 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeDesulfurococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 773773DNA polymerasePRO_0000278146Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi428 ↔ 4421 Publication
Disulfide bondi506 ↔ 5091 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
773
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109Combined sources
Beta strandi13 – 2210Combined sources
Beta strandi25 – 317Combined sources
Beta strandi37 – 448Combined sources
Helixi45 – 473Combined sources
Turni49 – 535Combined sources
Beta strandi55 – 584Combined sources
Beta strandi61 – 644Combined sources
Beta strandi67 – 8620Combined sources
Helixi92 – 1009Combined sources
Beta strandi106 – 1116Combined sources
Helixi116 – 1238Combined sources
Beta strandi137 – 1437Combined sources
Beta strandi159 – 1646Combined sources
Beta strandi167 – 1748Combined sources
Beta strandi181 – 1833Combined sources
Helixi187 – 20115Combined sources
Beta strandi204 – 2107Combined sources
Turni211 – 2144Combined sources
Helixi215 – 22410Combined sources
Turni225 – 2273Combined sources
Beta strandi240 – 25112Combined sources
Beta strandi255 – 2595Combined sources
Helixi260 – 2678Combined sources
Helixi275 – 2828Combined sources
Helixi294 – 3007Combined sources
Helixi302 – 3054Combined sources
Helixi308 – 33730Combined sources
Helixi341 – 3444Combined sources
Helixi349 – 36315Combined sources
Helixi374 – 3807Combined sources
Beta strandi397 – 40711Combined sources
Helixi408 – 4158Combined sources
Helixi420 – 4223Combined sources
Beta strandi429 – 4335Combined sources
Turni435 – 4373Combined sources
Beta strandi440 – 4423Combined sources
Helixi448 – 46922Combined sources
Helixi473 – 49018Combined sources
Helixi493 – 4975Combined sources
Helixi507 – 53226Combined sources
Beta strandi535 – 5395Combined sources
Beta strandi541 – 5477Combined sources
Helixi553 – 56715Combined sources
Helixi568 – 5703Combined sources
Beta strandi576 – 59015Combined sources
Beta strandi593 – 5975Combined sources
Beta strandi603 – 6075Combined sources
Helixi617 – 63115Combined sources
Helixi636 – 65015Combined sources
Turni651 – 6533Combined sources
Helixi657 – 6593Combined sources
Beta strandi662 – 6643Combined sources
Helixi678 – 6825Combined sources
Turni687 – 6904Combined sources
Beta strandi699 – 7024Combined sources
Beta strandi709 – 7113Combined sources
Beta strandi717 – 7193Combined sources
Turni722 – 7243Combined sources
Turni729 – 7324Combined sources
Helixi733 – 7375Combined sources
Helixi738 – 7469Combined sources
Turni747 – 7493Combined sources
Helixi752 – 7543Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D5AX-ray2.40A1-756[»]
1QQCX-ray2.60A1-773[»]
ProteinModelPortaliQ7SIG7.
SMRiQ7SIG7. Positions 1-756.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SIG7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 131131N-terminal domain1 PublicationAdd
BLAST
Regioni133 – 385253Exonuclease domain1 PublicationAdd
BLAST
Regioni390 – 773384Polymerase domain1 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the DNA polymerase type-B family.Sequence Analysis

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProiIPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 2 hits.
[Graphical view]
PRINTSiPR00106. DNAPOLB.
SMARTiSM00486. POLBc. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
PROSITEiPS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7SIG7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MILDADYITE DGKPVIRVFK KEKGEFKIDY DRDFEPYIYA LLKDDSAIED
60 70 80 90 100
IKKITAERHG TTVRVTRAER VKKKFLGRPV EVWKLYFTHP QDVPAIRDKI
110 120 130 140 150
REHPAVVDIY EYDIPFAKRY LIDRGLIPME GDEELRMLAF DIETLYHEGE
160 170 180 190 200
EFGEGPILMI SYADEEGARV ITWKNIDLPY VESVSTEKEM IKRFLKVIQE
210 220 230 240 250
KDPDVLITYN GDNFDFAYLK KRSEMLGVKF ILGRDGSEPK IQRMGDRFAV
260 270 280 290 300
EVKGRIHFDL YPVIRRTINL PTYTLETVYE PVFGQPKEKV YAEEIARAWE
310 320 330 340 350
SGEGLERVAR YSMEDAKATY ELGKEFFPME AQLSRLVGQS LWDVSRSSTG
360 370 380 390 400
NLVEWFLLRK AYERNDVAPN KPDERELARR TESYAGGYVK EPEKGLWENI
410 420 430 440 450
VYLDYKSLYP SIIITHNVSP DTLNREGCRE YDVAPQVGHR FCKDFPGFIP
460 470 480 490 500
SLLGDLLEER QKVKKKMKAT VDPIERKLLD YRQRAIKILA NSYYGYYAYA
510 520 530 540 550
NARWYCRECA ESVTAWGRQY IETTMREIEE KFGFKVLYAD TDGFFATIPG
560 570 580 590 600
ADAETVKNKA KEFLNYINPR LPGLLELEYE GFYRRGFFVT KKKYAVIDEE
610 620 630 640 650
DKITTRGLEI VRRDWSEIAK ETQARVLEAI LKHGDVEEAV RIVKEVTEKL
660 670 680 690 700
SRHEVPPEKL VIYEQITRDL RSYRATGPHV AVAKRLAARG IKIRPGTVIS
710 720 730 740 750
YIVLKGPGRV GDRAIPFDEF DPAKHRYDAE YYIENQVLPA VERILRAFGY
760 770
RKEDLRYQKT KQAGLGAWLK PKT
Length:773
Mass (Da):89,989
Last modified:December 15, 2003 - v1
Checksum:i03F7377635283A44
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1549YHEGEEFGE → AHAGAAAGA(PubMed:10545321)Curated
Sequence conflicti287 – 2871K → A(PubMed:10545321)Curated
Sequence conflicti297 – 2971R → E(PubMed:10545321)Curated
Sequence conflicti300 – 3001E → A(PubMed:10545321)Curated
Sequence conflicti665 – 67612QITRD…SYRAT → A(PubMed:10545321)CuratedAdd
BLAST
Sequence conflicti682 – 69615VAKRL…KIRPG → AAA(PubMed:10545321)CuratedAdd
BLAST

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D5A X-ray 2.40 A 1-756 [» ]
1QQC X-ray 2.60 A 1-773 [» ]
ProteinModelPortali Q7SIG7.
SMRi Q7SIG7. Positions 1-756.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q7SIG7.

Family and domain databases

Gene3Di 3.30.420.10. 1 hit.
3.90.1600.10. 2 hits.
InterProi IPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
[Graphical view ]
Pfami PF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 2 hits.
[Graphical view ]
PRINTSi PR00106. DNAPOLB.
SMARTi SM00486. POLBc. 1 hit.
[Graphical view ]
SUPFAMi SSF53098. SSF53098. 1 hit.
PROSITEi PS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Archaebacterial DNA polymerases tightly bind uracil-containing DNA."
    Lasken R.S., Schuster D.M., Rashtchian A.
    J. Biol. Chem. 271:17692-17696(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  2. "Crystal structure of an archaebacterial DNA polymerase."
    Zhao Y., Jeruzalmi D., Moarefi I., Leighton L., Lasken R.S., Kuriyan J.
    Structure 7:1189-1199(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, COFACTOR, DISULFIDE BONDS.

Entry informationi

Entry nameiDPOL_DESST
AccessioniPrimary (citable) accession number: Q7SIG7
Secondary accession number(s): Q7SIG8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: December 15, 2003
Last modified: November 26, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

There are conflicts between the sequence shown here and that from PDB 1D5A.Curated

Keywords - Technical termi

3D-structure, Multifunctional enzyme

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