ID   DPOL_THEG8              Reviewed;        1699 AA.
AC   Q9HH84;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=DNA polymerase;
DE            EC=2.7.7.7;
DE   Contains:
DE     RecName: Full=Endonuclease PI-TspGE8I;
DE              EC=3.1.-.-;
DE     AltName: Full=Tsp-GE8 pol-1 intein;
DE   Contains:
DE     RecName: Full=Endonuclease PI-TspGE8II;
DE              EC=3.1.-.-;
DE     AltName: Full=Tsp-GE8 pol-2 intein;
GN   Name=pol; Synonyms=pol-1;
OS   Thermococcus sp. (strain GE8).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus; unclassified Thermococcus.
OX   NCBI_TaxID=105583;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Querellou J.J.E., Cambon M.A., Lesongeur F., Barbier G.;
RT   "Thermococcales taxonomy and phylogeny based on the comparative use of 16S
RT   rDNA, 16S-23S rDNA intergenic spacer and family B DNA polymerase genes.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 3' to 5' exonuclease activity. {ECO:0000250}.
CC   -!- FUNCTION: PI-TspGE8I and PI-TspGE8II are endonucleases. {ECO:0000305}.
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   -!- PTM: This protein undergoes a protein self splicing that involves a
CC       post-translational excision of the intervening region (intein) followed
CC       by peptide ligation.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; AJ250333; CAC12850.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HH84; -.
DR   SMR; Q9HH84; -.
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:0004519; F:endonuclease 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   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.10.28.10; -; 2.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 3.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
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; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR006142; INTEIN.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR004860; LAGLIDADG_2.
DR   InterPro; IPR041005; PI-TkoII_IV.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00136; DNA_pol_B; 3.
DR   Pfam; PF03104; DNA_pol_B_exo1; 2.
DR   Pfam; PF14528; LAGLIDADG_3; 2.
DR   Pfam; PF18714; PI-TkoII_IV; 1.
DR   PRINTS; PR00379; INTEIN.
DR   SMART; SM00305; HintC; 2.
DR   SMART; SM00306; HintN; 2.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF51294; SSF51294; 2.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF55608; SSF55608; 2.
DR   SUPFAM; SSF56672; SSF56672; 2.
DR   TIGRFAMs; TIGR01443; intein_Cterm; 2.
DR   TIGRFAMs; TIGR01445; intein_Nterm; 2.
DR   PROSITE; PS50818; INTEIN_C_TER; 2.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2.
DR   PROSITE; PS50817; INTEIN_N_TER; 2.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Endonuclease; Exonuclease; Hydrolase;
KW   Intron homing; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW   Protein splicing; Repeat; Transferase.
FT   CHAIN           1..491
FT                   /note="DNA polymerase, 1st part"
FT                   /id="PRO_0000007343"
FT   CHAIN           492..1026
FT                   /note="Endonuclease PI-TspGE8I"
FT                   /id="PRO_0000007344"
FT   CHAIN           1027..1075
FT                   /note="DNA polymerase, 2nd part"
FT                   /id="PRO_0000007345"
FT   CHAIN           1076..1464
FT                   /note="Endonuclease PI-TspGE8II"
FT                   /id="PRO_0000007346"
FT   CHAIN           1465..1699
FT                   /note="DNA polymerase, 3rd part"
FT                   /id="PRO_0000007347"
FT   DOMAIN          770..903
FT                   /note="DOD-type homing endonuclease 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT   DOMAIN          1222..1361
FT                   /note="DOD-type homing endonuclease 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
SQ   SEQUENCE   1699 AA;  197325 MW;  F389B4351F0B12D3 CRC64;
     MILDTDYITE DGKPVIRVFK KENGEFKIEY DRNFEPYFYA LLKDDSAIEE VKKITAKRHG
     TVVKVKRAEK VKKKFLGRPI EVWKLYFTHP QDVPAIRDKI REHPAVIDIY EYDIPFAKRY
     LIDKGLIPME GDEKLKMLAF DIETLYHEGE EFAEGPILMI SYADEEGARV ITWKKVDLPY
     VDVVSTEKEM IKRFLRVVKE KDPDVLITYN GDNFDFAYLK RRSEKLGVKF ILGRDGSEPK
     IQRMGDRFAV EVKGRIHFDL YPVIRRTINL PTYTLEAVYE AIFGKPKEKV YAEEIATAWE
     TGEGLERVAR YSMEDAKVTF ELGKEFFPME AQLSRLIGQS LWDVSRSSTG NLVEWFLLRK
     AYERNELAPN KPDERELARR RQSYAGGYVK EPERGLWNNI VYLDFRSLYP SIIITHNVSP
     DTLNREGCKE YDVAPQVGHK FCKDFPGFIP SLLGDLLEER QKIKRKMRAT IDPVEKKLLD
     YRQRAIKILA NSILPDEWLP LLVNGRLKLV RIGDFVDNTM KKGQPLENDG TEVLEVSGIE
     AISFNRKTKI AEIKPVKALI RHRYRGKVYD IKLSSGRNIK VTEGHSLFAF RDGELVEVTG
     GEIKPGDFIA VPRRVNLPER HERINLIEIL LGLPPEETSD IVLTIPVKGR KNFFKGMLRT
     LRWIFEEEQR PRTARRYLEH LQKLGYVKLM KRAYEIVNKE ALRNYRKLYE VLAERVKYNG
     NKREYLVHFN DLRNEIKFMP DEELEEWKVG TLNGFRMEPF IEVGEDFAKL LGYYVSEGYA
     RKQRNQKNGW SYSVKIYNND QRVLDDMEKL ASKFFGRVRR GKNYVEISRK MAYVLFESLC
     GTLAENKRVP EVIFTSPESV RWAFFEGYFI GDGDLHPSKR VRLSTKSEEL VNGLVVLLNS
     LGISAIKIRF DSGVYRVLVN EELPFLGNRK RKNAYYSHVI PKEILEETFG KQFQKNMSPA
     KLNEKVEKGE LDAGKARRIA WLLEGDIVLD RVEKVTVEDY EGYVYDLSVE ENENFLAGFG
     MLYAHNSYYG YYGYAKARWY CRECAESVTA WGRSYIETTI REIEEKFGFK VLYADSVAGN
     TEVIIRRNGK VEFVPIEKLF QRVDYRIGEK EYCALEGVEA LTLDNRGRLV WRKVPYIMRH
     KTNKKIYRVW FTNSWYLDVT EDHSLIGYLN TSKVKSEKPL KERLVEVKPR ELGEKVKSLI
     TLNRAIARSI KANPIAVRLW ELIGLLVGDG NWGGHSKWAK YYVGLSCGLD KAEIEEKVLR
     PLKEAGIISN YYGKSKKGDV SILSKWLAGF MVKYFKDENG NKRIPSFMFN LPREYIEAFL
     RGLFSADGTV SLRRGIPEIR LTSVNRELSN EVRKLLWLVG VSNSMFTETT PNKYLGNESG
     TRSIHVRIKN KHRFAKRIGF LLDRKATKLS DNLREHTNKK MAYRYDFDLV YPKKIEEINY
     DRYVYDIEVE GTHRFFANGI LVHNTDGFFA TIPGADAETV KKKAMEFLKY INAKLPGLLE
     LEYEGFYVRG FFVTKKKYAV IDEEGKITTR GLEIVRRDWS EIAKETQARV LEAILKHGDV
     EEAVRIVKEV TEKLSKYEVP PEKLVIHEQI TRDLKDYKAT GPHVAVAKRL AARGIKIRPG
     TVISYIVLKG SGRIGDRAIP FDEFDPAKHK YDAEYYIENQ VLPAVERILR AFGYRKEDLR
     YQKTKQVGLG AWLKVKGKK