ID DPOL_THEGO Reviewed; 773 AA. AC P56689; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 1. DT 13-SEP-2023, entry version 107. DE RecName: Full=DNA polymerase; DE EC=2.7.7.7; DE AltName: Full=TO POL; GN Name=pol; Synonyms=polA; OS Thermococcus gorgonarius. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=71997; RN [1] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=10097083; DOI=10.1073/pnas.96.7.3600; RA Hopfner K.-P., Eichinger A., Engh R.A., Laue F., Ankenbauer W., Huber R., RA Angerer B.; RT "Crystal structure of a thermostable type B DNA polymerase from RT Thermococcus gorgonarius."; RL Proc. Natl. Acad. Sci. U.S.A. 96:3600-3605(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=18614176; DOI=10.1016/j.jmb.2008.06.004; RA Firbank S.J., Wardle J., Heslop P., Lewis R.J., Connolly B.A.; RT "Uracil recognition in archaeal DNA polymerases captured by X-ray RT crystallography."; RL J. Mol. Biol. 381:529-539(2008). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS) OF 1-757, AND DISULFIDE BONDS. RX PubMed=20527806; DOI=10.1021/bi100421r; RA Killelea T., Ghosh S., Tan S.S., Heslop P., Firbank S.J., Kool E.T., RA Connolly B.A.; RT "Probing the interaction of archaeal DNA polymerases with deaminated bases RT using X-ray crystallography and non-hydrogen bonding isosteric base RT analogues."; RL Biochemistry 49:5772-5781(2010). CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase CC exhibits 3' to 5' exonuclease activity. 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 -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {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; 1TGO; X-ray; 2.50 A; A=1-773. DR PDB; 2VWJ; X-ray; 2.78 A; A=1-773. DR PDB; 2VWK; X-ray; 2.60 A; A=1-773. DR PDB; 2XHB; X-ray; 2.72 A; A=1-773. DR PDB; 7B06; X-ray; 2.35 A; A=1-773. DR PDB; 7B07; X-ray; 3.10 A; A=1-773. DR PDB; 7B08; X-ray; 2.39 A; A=1-773. DR PDB; 7B0F; X-ray; 2.80 A; A=1-773. DR PDB; 7B0G; X-ray; 3.00 A; A=1-773. DR PDB; 7B0H; X-ray; 3.15 A; E/F=1-773. DR PDBsum; 1TGO; -. DR PDBsum; 2VWJ; -. DR PDBsum; 2VWK; -. DR PDBsum; 2XHB; -. DR PDBsum; 7B06; -. DR PDBsum; 7B07; -. DR PDBsum; 7B08; -. DR PDBsum; 7B0F; -. DR PDBsum; 7B0G; -. DR PDBsum; 7B0H; -. DR AlphaFoldDB; P56689; -. DR SMR; P56689; -. DR OrthoDB; 323192at2157; -. DR BRENDA; 2.7.7.7; 13310. DR EvolutionaryTrace; P56689; -. 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: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; KW Multifunctional enzyme; Nuclease; Nucleotidyltransferase; Transferase. FT CHAIN 1..773 FT /note="DNA polymerase" FT /id="PRO_0000046488" FT DISULFID 428..442 FT /evidence="ECO:0000269|PubMed:10097083, FT ECO:0000269|PubMed:18614176, ECO:0007744|PDB:1TGO, FT ECO:0007744|PDB:2VWK" FT DISULFID 506..509 FT /evidence="ECO:0000269|PubMed:18614176, FT ECO:0000269|PubMed:20527806, ECO:0007744|PDB:2VWK, FT ECO:0007744|PDB:2XHB" FT STRAND 2..10 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 13..22 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 25..31 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 37..43 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 45..47 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 48..52 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 67..75 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 78..86 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 92..101 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 106..111 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 116..124 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 137..144 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:1TGO" FT STRAND 157..164 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 167..174 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 187..201 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 204..210 FT /evidence="ECO:0007829|PDB:7B06" FT TURN 211..214 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 215..226 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 233..236 FT /evidence="ECO:0007829|PDB:2XHB" FT STRAND 240..251 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 255..259 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 260..267 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 275..283 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 292..299 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 305..337 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 341..345 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 349..363 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 374..379 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 395..405 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 408..415 FT /evidence="ECO:0007829|PDB:7B06" FT TURN 420..422 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 431..433 FT /evidence="ECO:0007829|PDB:7B06" FT TURN 435..437 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 440..442 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 448..469 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 473..490 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 493..497 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 507..532 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 535..547 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 553..570 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 577..590 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 593..597 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 603..607 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 614..616 FT /evidence="ECO:0007829|PDB:7B08" FT HELIX 617..631 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 636..651 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 657..660 FT /evidence="ECO:0007829|PDB:7B08" FT STRAND 662..664 FT /evidence="ECO:0007829|PDB:7B08" FT HELIX 670..672 FT /evidence="ECO:0007829|PDB:1TGO" FT STRAND 675..677 FT /evidence="ECO:0007829|PDB:2VWK" FT HELIX 678..688 FT /evidence="ECO:0007829|PDB:7B08" FT STRAND 699..704 FT /evidence="ECO:0007829|PDB:7B08" FT STRAND 707..709 FT /evidence="ECO:0007829|PDB:1TGO" FT HELIX 710..713 FT /evidence="ECO:0007829|PDB:2XHB" FT STRAND 714..716 FT /evidence="ECO:0007829|PDB:7B08" FT HELIX 717..719 FT /evidence="ECO:0007829|PDB:7B08" FT TURN 722..724 FT /evidence="ECO:0007829|PDB:7B08" FT HELIX 729..734 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 737..745 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 746..748 FT /evidence="ECO:0007829|PDB:7B06" FT HELIX 752..754 FT /evidence="ECO:0007829|PDB:7B06" FT STRAND 758..760 FT /evidence="ECO:0007829|PDB:1TGO" FT HELIX 766..769 FT /evidence="ECO:0007829|PDB:2VWK" SQ SEQUENCE 773 AA; 89812 MW; F67AF04E875FBE44 CRC64; MILDTDYITE DGKPVIRIFK KENGEFKIDY DRNFEPYIYA LLKDDSAIED VKKITAERHG TTVRVVRAEK VKKKFLGRPI EVWKLYFTHP QDVPAIRDKI KEHPAVVDIY EYDIPFAKRY LIDKGLIPME GDEELKMLAF DIETLYHEGE EFAEGPILMI SYADEEGARV ITWKNIDLPY VDVVSTEKEM IKRFLKVVKE KDPDVLITYN GDNFDFAYLK KRSEKLGVKF ILGREGSEPK IQRMGDRFAV EVKGRIHFDL YPVIRRTINL PTYTLEAVYE AIFGQPKEKV YAEEIAQAWE TGEGLERVAR YSMEDAKVTY ELGKEFFPME AQLSRLVGQS LWDVSRSSTG NLVEWFLLRK AYERNELAPN KPDERELARR RESYAGGYVK EPERGLWENI VYLDFRSLYP SIIITHNVSP DTLNREGCEE YDVAPQVGHK FCKDFPGFIP SLLGDLLEER QKVKKKMKAT IDPIEKKLLD YRQRAIKILA NSFYGYYGYA KARWYCKECA ESVTAWGRQY IETTIREIEE KFGFKVLYAD TDGFFATIPG ADAETVKKKA KEFLDYINAK LPGLLELEYE GFYKRGFFVT KKKYAVIDEE DKITTRGLEI VRRDWSEIAK ETQARVLEAI LKHGDVEEAV RIVKEVTEKL SKYEVPPEKL VIYEQITRDL KDYKATGPHV AVAKRLAARG IKIRPGTVIS YIVLKGSGRI GDRAIPFDEF DPAKHKYDAE YYIENQVLPA VERILRAFGY RKEDLRYQKT RQVGLGAWLK PKT //