DPOL_THEGO
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 25-MAY-2022, entry version 104.
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}.
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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 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 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;
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
