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Protein

DNA polymerase

Gene

pol

Organism
Thermococcus gorgonarius
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

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

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase (EC:2.7.7.7)
Alternative name(s):
TO POL
Gene namesi
Name:pol
Synonyms:polA
OrganismiThermococcus gorgonarius
Taxonomic identifieri71997 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000464881 – 773DNA polymeraseAdd BLAST773

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi428 ↔ 442Combined sources2 Publications
Disulfide bondi506 ↔ 509Combined sources2 Publications

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 – 32Combined sources8
Beta strandi37 – 44Combined sources8
Helixi45 – 47Combined sources3
Helixi48 – 51Combined sources4
Beta strandi55 – 58Combined sources4
Beta strandi61 – 64Combined sources4
Beta strandi67 – 75Combined sources9
Beta strandi78 – 86Combined sources9
Helixi92 – 102Combined sources11
Beta strandi106 – 111Combined sources6
Helixi116 – 123Combined sources8
Beta strandi137 – 144Combined sources8
Beta strandi148 – 151Combined sources4
Beta strandi157 – 164Combined sources8
Beta strandi167 – 174Combined sources8
Beta strandi181 – 183Combined sources3
Helixi187 – 201Combined sources15
Beta strandi204 – 210Combined sources7
Helixi211 – 213Combined sources3
Helixi215 – 225Combined sources11
Beta strandi233 – 236Combined sources4
Beta strandi240 – 243Combined sources4
Beta strandi245 – 251Combined sources7
Beta strandi255 – 259Combined sources5
Helixi260 – 267Combined sources8
Helixi275 – 283Combined sources9
Helixi292 – 301Combined sources10
Helixi305 – 337Combined sources33
Helixi341 – 345Combined sources5
Helixi349 – 363Combined sources15
Helixi374 – 379Combined sources6
Beta strandi395 – 407Combined sources13
Helixi408 – 415Combined sources8
Turni420 – 422Combined sources3
Beta strandi429 – 433Combined sources5
Turni435 – 437Combined sources3
Beta strandi440 – 442Combined sources3
Helixi448 – 469Combined sources22
Helixi473 – 490Combined sources18
Helixi493 – 498Combined sources6
Helixi507 – 530Combined sources24
Beta strandi535 – 547Combined sources13
Helixi553 – 568Combined sources16
Beta strandi577 – 590Combined sources14
Beta strandi593 – 597Combined sources5
Beta strandi603 – 607Combined sources5
Beta strandi613 – 615Combined sources3
Helixi617 – 631Combined sources15
Helixi636 – 651Combined sources16
Helixi657 – 659Combined sources3
Beta strandi662 – 665Combined sources4
Helixi670 – 672Combined sources3
Beta strandi675 – 678Combined sources4
Helixi679 – 689Combined sources11
Beta strandi697 – 704Combined sources8
Beta strandi707 – 709Combined sources3
Helixi710 – 713Combined sources4
Beta strandi714 – 716Combined sources3
Helixi717 – 719Combined sources3
Turni722 – 724Combined sources3
Helixi729 – 735Combined sources7
Helixi738 – 740Combined sources3
Helixi742 – 746Combined sources5
Turni747 – 749Combined sources3
Helixi752 – 754Combined sources3
Beta strandi758 – 760Combined sources3
Helixi766 – 769Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TGOX-ray2.50A1-773[»]
2VWJX-ray2.78A1-773[»]
2VWKX-ray2.60A1-773[»]
2XHBX-ray2.72A1-757[»]
ProteinModelPortaliP56689.
SMRiP56689.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56689.

Family & Domainsi

Sequence similaritiesi

Belongs to the DNA polymerase type-B family.Curated

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.

P56689-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILDTDYITE DGKPVIRIFK KENGEFKIDY DRNFEPYIYA LLKDDSAIED
60 70 80 90 100
VKKITAERHG TTVRVVRAEK VKKKFLGRPI EVWKLYFTHP QDVPAIRDKI
110 120 130 140 150
KEHPAVVDIY EYDIPFAKRY LIDKGLIPME GDEELKMLAF DIETLYHEGE
160 170 180 190 200
EFAEGPILMI SYADEEGARV ITWKNIDLPY VDVVSTEKEM IKRFLKVVKE
210 220 230 240 250
KDPDVLITYN GDNFDFAYLK KRSEKLGVKF ILGREGSEPK IQRMGDRFAV
260 270 280 290 300
EVKGRIHFDL YPVIRRTINL PTYTLEAVYE AIFGQPKEKV YAEEIAQAWE
310 320 330 340 350
TGEGLERVAR YSMEDAKVTY ELGKEFFPME AQLSRLVGQS LWDVSRSSTG
360 370 380 390 400
NLVEWFLLRK AYERNELAPN KPDERELARR RESYAGGYVK EPERGLWENI
410 420 430 440 450
VYLDFRSLYP SIIITHNVSP DTLNREGCEE YDVAPQVGHK FCKDFPGFIP
460 470 480 490 500
SLLGDLLEER QKVKKKMKAT IDPIEKKLLD YRQRAIKILA NSFYGYYGYA
510 520 530 540 550
KARWYCKECA ESVTAWGRQY IETTIREIEE KFGFKVLYAD TDGFFATIPG
560 570 580 590 600
ADAETVKKKA KEFLDYINAK LPGLLELEYE GFYKRGFFVT KKKYAVIDEE
610 620 630 640 650
DKITTRGLEI VRRDWSEIAK ETQARVLEAI LKHGDVEEAV RIVKEVTEKL
660 670 680 690 700
SKYEVPPEKL VIYEQITRDL KDYKATGPHV AVAKRLAARG IKIRPGTVIS
710 720 730 740 750
YIVLKGSGRI GDRAIPFDEF DPAKHKYDAE YYIENQVLPA VERILRAFGY
760 770
RKEDLRYQKT RQVGLGAWLK PKT
Length:773
Mass (Da):89,812
Last modified:July 15, 1999 - v1
Checksum:iF67AF04E875FBE44
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TGOX-ray2.50A1-773[»]
2VWJX-ray2.78A1-773[»]
2VWKX-ray2.60A1-773[»]
2XHBX-ray2.72A1-757[»]
ProteinModelPortaliP56689.
SMRiP56689.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP56689.

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_THEGO
AccessioniPrimary (citable) accession number: P56689
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: November 2, 2016
This is version 87 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, 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.