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Protein

DNA polymerase

Gene

pol

Organism
Desulfurococcus sp. (strain Tok)
Status
Reviewed-Annotation score: Annotation score: 5 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)DescriptionActionsGraphical viewLength
Metal bindingi141Magnesium 11 Publication1
Metal bindingi141Magnesium 21 Publication1
Metal bindingi143Magnesium 21 Publication1
Metal bindingi315Magnesium 11 Publication1
Metal bindingi315Magnesium 21 Publication1

GO - Molecular functioni

GO - Biological processi

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

Enzyme and pathway databases

BRENDAi2.7.7.7. 1918.

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)DescriptionActionsGraphical viewLength
ChainiPRO_00002781461 – 773DNA polymeraseAdd BLAST773

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi428 ↔ 4421 Publication
Disulfide bondi506 ↔ 5091 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1773
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 10Combined sources9
Beta strandi13 – 22Combined sources10
Beta strandi25 – 31Combined sources7
Beta strandi37 – 44Combined sources8
Helixi45 – 47Combined sources3
Turni49 – 53Combined sources5
Beta strandi55 – 58Combined sources4
Beta strandi61 – 64Combined sources4
Beta strandi67 – 86Combined sources20
Helixi92 – 100Combined sources9
Beta strandi106 – 111Combined sources6
Helixi116 – 123Combined sources8
Beta strandi137 – 143Combined sources7
Beta strandi159 – 164Combined sources6
Beta strandi167 – 174Combined sources8
Beta strandi181 – 183Combined sources3
Helixi187 – 201Combined sources15
Beta strandi204 – 210Combined sources7
Turni211 – 214Combined sources4
Helixi215 – 224Combined sources10
Turni225 – 227Combined sources3
Beta strandi240 – 251Combined sources12
Beta strandi255 – 259Combined sources5
Helixi260 – 267Combined sources8
Helixi275 – 282Combined sources8
Helixi294 – 300Combined sources7
Helixi302 – 305Combined sources4
Helixi308 – 337Combined sources30
Helixi341 – 344Combined sources4
Helixi349 – 363Combined sources15
Helixi374 – 380Combined sources7
Beta strandi397 – 407Combined sources11
Helixi408 – 415Combined sources8
Helixi420 – 422Combined sources3
Beta strandi429 – 433Combined sources5
Turni435 – 437Combined sources3
Beta strandi440 – 442Combined sources3
Helixi448 – 469Combined sources22
Helixi473 – 490Combined sources18
Helixi493 – 497Combined sources5
Helixi507 – 532Combined sources26
Beta strandi535 – 539Combined sources5
Beta strandi541 – 547Combined sources7
Helixi553 – 567Combined sources15
Helixi568 – 570Combined sources3
Beta strandi576 – 590Combined sources15
Beta strandi593 – 597Combined sources5
Beta strandi603 – 607Combined sources5
Helixi617 – 631Combined sources15
Helixi636 – 650Combined sources15
Turni651 – 653Combined sources3
Helixi657 – 659Combined sources3
Beta strandi662 – 664Combined sources3
Helixi678 – 682Combined sources5
Turni687 – 690Combined sources4
Beta strandi699 – 702Combined sources4
Beta strandi709 – 711Combined sources3
Beta strandi717 – 719Combined sources3
Turni722 – 724Combined sources3
Turni729 – 732Combined sources4
Helixi733 – 737Combined sources5
Helixi738 – 746Combined sources9
Turni747 – 749Combined sources3
Helixi752 – 754Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ7SIG7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 131N-terminal domain1 PublicationAdd BLAST131
Regioni133 – 385Exonuclease domain1 PublicationAdd BLAST253
Regioni390 – 773Polymerase domain1 PublicationAdd BLAST384

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)DescriptionActionsGraphical viewLength
Sequence conflicti146 – 154YHEGEEFGE → AHAGAAAGA (PubMed:10545321).Curated9
Sequence conflicti287K → A (PubMed:10545321).Curated1
Sequence conflicti297R → E (PubMed:10545321).Curated1
Sequence conflicti300E → A (PubMed:10545321).Curated1
Sequence conflicti665 – 676QITRD…SYRAT → A (PubMed:10545321).CuratedAdd BLAST12
Sequence conflicti682 – 696VAKRL…KIRPG → AAA (PubMed:10545321).CuratedAdd BLAST15

Cross-referencesi

3D structure databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi2.7.7.7. 1918.

Miscellaneous databases

EvolutionaryTraceiQ7SIG7.

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]
ProtoNetiSearch...

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 2, 2016
This is version 70 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.