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 13-SEP-2023, entry version 91. 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; Thermoproteota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CDD; cd05780; DNA_polB_Kod1_like_exo; 1. DR CDD; cd05536; POLBc_B3; 1. DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1. DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1. DR Gene3D; 1.10.287.690; Helix hairpin bin; 1. DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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 NCBIfam; TIGR00592; pol2; 2. DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1. DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1. 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; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 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 //