ID DPOL_THES9 Reviewed; 775 AA.
AC Q56366;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 13-SEP-2023, entry version 108.
DE RecName: Full=DNA polymerase;
DE EC=2.7.7.7;
GN Name=pol; Synonyms=polA;
OS Thermococcus sp. (strain 9oN-7).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=103799;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8643567; DOI=10.1073/pnas.93.11.5281;
RA Southworth M.W., Kong H., Kucera R.B., Ware J., Jannasch H.W., Perler F.B.;
RT "Cloning of thermostable DNA polymerases from hyperthermophilic marine
RT Archaea with emphasis on Thermococcus sp. 9oN-7 and mutations affecting 3'-
RT 5' exonuclease activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5281-5285(1996).
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 EMBL; U47108; AAA88769.1; -; Genomic_DNA.
DR PIR; S67920; S67920.
DR PDB; 1QHT; X-ray; 2.10 A; A=1-775.
DR PDB; 4K8X; X-ray; 2.28 A; A=1-775.
DR PDB; 5OMQ; X-ray; 2.20 A; A=1-775.
DR PDB; 5OMV; X-ray; 2.00 A; A=1-775.
DR PDB; 6IS7; X-ray; 2.80 A; A/B=1-775.
DR PDB; 6ISF; X-ray; 2.80 A; A/B=1-775.
DR PDB; 6ISG; X-ray; 3.40 A; A=1-775.
DR PDB; 6ISH; X-ray; 3.30 A; A=1-775.
DR PDB; 6ISI; X-ray; 3.20 A; A=1-775.
DR PDBsum; 1QHT; -.
DR PDBsum; 4K8X; -.
DR PDBsum; 5OMQ; -.
DR PDBsum; 5OMV; -.
DR PDBsum; 6IS7; -.
DR PDBsum; 6ISF; -.
DR PDBsum; 6ISG; -.
DR PDBsum; 6ISH; -.
DR PDBsum; 6ISI; -.
DR AlphaFoldDB; Q56366; -.
DR SMR; Q56366; -.
DR EvolutionaryTrace; Q56366; -.
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: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; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..775
FT /note="DNA polymerase"
FT /id="PRO_0000046489"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:5OMV"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:6IS7"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 292..301
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:6ISH"
FT HELIX 305..337
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 349..364
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 374..379
FT /evidence="ECO:0007829|PDB:5OMV"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:1QHT"
FT STRAND 395..405
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 408..416
FT /evidence="ECO:0007829|PDB:5OMV"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:5OMV"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 448..469
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 473..497
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 507..531
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 535..540
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 543..547
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 553..567
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 568..570
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 577..590
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 593..598
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 603..608
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:6ISF"
FT HELIX 617..633
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 636..651
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 657..660
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 662..665
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 678..688
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 698..705
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:5OMV"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 717..719
FT /evidence="ECO:0007829|PDB:5OMV"
FT TURN 722..724
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 729..734
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 737..745
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 746..748
FT /evidence="ECO:0007829|PDB:5OMV"
FT HELIX 752..754
FT /evidence="ECO:0007829|PDB:5OMV"
SQ SEQUENCE 775 AA; 89781 MW; 71525D63C0C9CD9D CRC64;
MILDTDYITE NGKPVIRVFK KENGEFKIEY DRTFEPYFYA LLKDDSAIED VKKVTAKRHG
TVVKVKRAEK VQKKFLGRPI EVWKLYFNHP QDVPAIRDRI RAHPAVVDIY EYDIPFAKRY
LIDKGLIPME GDEELTMLAF DIETLYHEGE EFGTGPILMI SYADGSEARV ITWKKIDLPY
VDVVSTEKEM IKRFLRVVRE KDPDVLITYN GDNFDFAYLK KRCEELGIKF TLGRDGSEPK
IQRMGDRFAV EVKGRIHFDL YPVIRRTINL PTYTLEAVYE AVFGKPKEKV YAEEIAQAWE
SGEGLERVAR YSMEDAKVTY ELGREFFPME AQLSRLIGQS LWDVSRSSTG NLVEWFLLRK
AYKRNELAPN KPDERELARR RGGYAGGYVK EPERGLWDNI VYLDFRSLYP SIIITHNVSP
DTLNREGCKE YDVAPEVGHK FCKDFPGFIP SLLGDLLEER QKIKRKMKAT VDPLEKKLLD
YRQRAIKILA NSFYGYYGYA KARWYCKECA ESVTAWGREY IEMVIRELEE KFGFKVLYAD
TDGLHATIPG ADAETVKKKA KEFLKYINPK LPGLLELEYE GFYVRGFFVT KKKYAVIDEE
GKITTRGLEI VRRDWSEIAK ETQARVLEAI LKHGDVEEAV RIVKEVTEKL SKYEVPPEKL
VIHEQITRDL RDYKATGPHV AVAKRLAARG VKIRPGTVIS YIVLKGSGRI GDRAIPADEF
DPTKHRYDAE YYIENQVLPA VERILKAFGY RKEDLRYQKT KQVGLGAWLK VKGKK
//
