DPOL_DESST
ID DPOL_DESST Reviewed; 773 AA.
AC Q7SIG7; Q7SIG8;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=DNA polymerase;
DE EC=2.7.7.7;
DE AltName: Full=D Tok Pol;
GN Name=pol;
OS Desulfurococcus sp. (strain Tok).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Desulfurococcus; unclassified Desulfurococcus.
OX NCBI_TaxID=108142;
RN [1] {ECO:0000305}
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=8663453; DOI=10.1074/jbc.271.30.17692;
RA Lasken R.S., Schuster D.M., Rashtchian A.;
RT "Archaebacterial DNA polymerases tightly bind uracil-containing DNA.";
RL J. Biol. Chem. 271:17692-17696(1996).
RN [2] {ECO:0000305, ECO:0000312|PDB:1QQC}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, COFACTOR,
RP AND DISULFIDE BONDS.
RX PubMed=10545321; DOI=10.1016/s0969-2126(00)80053-2;
RA Zhao Y., Jeruzalmi D., Moarefi I., Leighton L., Lasken R.S., Kuriyan J.;
RT "Crystal structure of an archaebacterial DNA polymerase.";
RL Structure 7:1189-1199(1999).
CC -!- FUNCTION: Thermostable DNA polymerase. In addition to polymerase
CC activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.
CC {ECO:0000269|PubMed:8663453}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000269|PubMed:8663453};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10545321};
CC Note=Binds 2 magnesium ions. {ECO:0000269|PubMed:10545321};
CC -!- ACTIVITY REGULATION: DNA polymerase activity strongly inhibited by
CC uracil-containing oligonucleotides. {ECO:0000269|PubMed:8663453}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000255}.
CC -!- CAUTION: There are conflicts between the sequence shown here and that
CC from PDB 1D5A. {ECO:0000305}.
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DR PDB; 1D5A; X-ray; 2.40 A; A=1-756.
DR PDB; 1QQC; X-ray; 2.60 A; A=1-773.
DR PDBsum; 1D5A; -.
DR PDBsum; 1QQC; -.
DR AlphaFoldDB; Q7SIG7; -.
DR SMR; Q7SIG7; -.
DR BRENDA; 2.7.7.7; 1918.
DR EvolutionaryTrace; Q7SIG7; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 2.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Exonuclease; Hydrolase; Magnesium;
KW Metal-binding; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW Transferase.
FT CHAIN 1..773
FT /note="DNA polymerase"
FT /id="PRO_0000278146"
FT REGION 1..131
FT /note="N-terminal domain"
FT /evidence="ECO:0000269|PubMed:10545321"
FT REGION 133..385
FT /note="Exonuclease domain"
FT /evidence="ECO:0000269|PubMed:10545321"
FT REGION 390..773
FT /note="Polymerase domain"
FT /evidence="ECO:0000269|PubMed:10545321"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10545321"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10545321"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10545321"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10545321"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10545321"
FT DISULFID 428..442
FT /evidence="ECO:0000269|PubMed:10545321"
FT DISULFID 506..509
FT /evidence="ECO:0000269|PubMed:10545321"
FT CONFLICT 146..154
FT /note="YHEGEEFGE -> AHAGAAAGA (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="K -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="R -> E (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="E -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 665..676
FT /note="QITRDLRSYRAT -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 682..696
FT /note="VAKRLAARGIKIRPG -> AAA (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1QQC"
FT TURN 49..53
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 67..86
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:1D5A"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:1D5A"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 240..251
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 308..337
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 349..363
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 397..407
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 408..415
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:1D5A"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 448..469
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 473..490
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 493..497
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 507..532
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 535..539
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 541..547
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 553..567
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 576..590
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 593..597
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 603..607
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 617..631
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 636..650
FT /evidence="ECO:0007829|PDB:1D5A"
FT TURN 651..653
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 657..659
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 662..664
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 678..682
FT /evidence="ECO:0007829|PDB:1QQC"
FT TURN 687..690
FT /evidence="ECO:0007829|PDB:1QQC"
FT STRAND 699..702
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 709..711
FT /evidence="ECO:0007829|PDB:1D5A"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:1D5A"
FT TURN 722..724
FT /evidence="ECO:0007829|PDB:1D5A"
FT TURN 729..732
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 733..737
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 738..746
FT /evidence="ECO:0007829|PDB:1D5A"
FT TURN 747..749
FT /evidence="ECO:0007829|PDB:1D5A"
FT HELIX 752..754
FT /evidence="ECO:0007829|PDB:1D5A"
SQ SEQUENCE 773 AA; 89989 MW; 03F7377635283A44 CRC64;
MILDADYITE DGKPVIRVFK KEKGEFKIDY DRDFEPYIYA LLKDDSAIED IKKITAERHG
TTVRVTRAER VKKKFLGRPV EVWKLYFTHP QDVPAIRDKI REHPAVVDIY EYDIPFAKRY
LIDRGLIPME GDEELRMLAF DIETLYHEGE EFGEGPILMI SYADEEGARV ITWKNIDLPY
VESVSTEKEM IKRFLKVIQE KDPDVLITYN GDNFDFAYLK KRSEMLGVKF ILGRDGSEPK
IQRMGDRFAV EVKGRIHFDL YPVIRRTINL PTYTLETVYE PVFGQPKEKV YAEEIARAWE
SGEGLERVAR YSMEDAKATY ELGKEFFPME AQLSRLVGQS LWDVSRSSTG NLVEWFLLRK
AYERNDVAPN KPDERELARR TESYAGGYVK EPEKGLWENI VYLDYKSLYP SIIITHNVSP
DTLNREGCRE YDVAPQVGHR FCKDFPGFIP SLLGDLLEER QKVKKKMKAT VDPIERKLLD
YRQRAIKILA NSYYGYYAYA NARWYCRECA ESVTAWGRQY IETTMREIEE KFGFKVLYAD
TDGFFATIPG ADAETVKNKA KEFLNYINPR LPGLLELEYE GFYRRGFFVT KKKYAVIDEE
DKITTRGLEI VRRDWSEIAK ETQARVLEAI LKHGDVEEAV RIVKEVTEKL SRHEVPPEKL
VIYEQITRDL RSYRATGPHV AVAKRLAARG IKIRPGTVIS YIVLKGPGRV GDRAIPFDEF
DPAKHRYDAE YYIENQVLPA VERILRAFGY RKEDLRYQKT KQAGLGAWLK PKT
