ID   DPOL_THEHY              Reviewed;        1668 AA.
AC   Q9HH05;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=DNA polymerase;
DE            EC=2.7.7.7;
DE   Contains:
DE     RecName: Full=Endonuclease PI-ThyII;
DE              EC=3.1.-.-;
DE     AltName: Full=Thy pol-1 intein;
DE   Contains:
DE     RecName: Full=Endonuclease PI-ThyI;
DE              EC=3.1.-.-;
DE     AltName: Full=Thy pol-2 intein;
DE   Flags: Fragment;
GN   Name=pol;
OS   Thermococcus hydrothermalis.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=46539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Querellou J.J.E., Cambon M.A., Lesongeur F.O., 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.
RN   [2]
RP   CHARACTERIZATION OF PI-THYI.
RX   PubMed=11058140; DOI=10.1093/nar/28.21.4391;
RA   Saves I., Eleaume H., Dietrich J., Masson J.-M.;
RT   "The Thy pol-2 intein of Thermococcus hydrothermalis is an isoschizomer of
RT   PI-TliI and PI-TfuII endonucleases.";
RL   Nucleic Acids Res. 28:4391-4396(2000).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 3' to 5' exonuclease activity. {ECO:0000250}.
CC   -!- FUNCTION: PI-ThyI and PI-ThyII are endonucleases. PI-ThyI cleaves the
CC       inteinless sequence of the Thy DNA pol gene. It requires a 21-bp
CC       minimal recognition sequence.
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. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; AJ245819; CAC18555.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HH05; -.
DR   SMR; Q9HH05; -.
DR   PRIDE; Q9HH05; -.
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   1: Evidence at protein level;
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..458
FT                   /note="DNA polymerase, 1st part"
FT                   /id="PRO_0000007333"
FT   CHAIN           459..995
FT                   /note="Endonuclease PI-ThyI"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007334"
FT   CHAIN           996..1044
FT                   /note="DNA polymerase, 2nd part"
FT                   /id="PRO_0000007335"
FT   CHAIN           1045..1433
FT                   /note="Endonuclease PI-ThyII"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000007336"
FT   CHAIN           1434..1668
FT                   /note="DNA polymerase, 3rd part"
FT                   /id="PRO_0000007337"
FT   DOMAIN          739..872
FT                   /note="DOD-type homing endonuclease 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT   DOMAIN          1191..1330
FT                   /note="DOD-type homing endonuclease 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT   NON_TER         1
SQ   SEQUENCE   1668 AA;  193321 MW;  5EEB805EFEDA71C8 CRC64;
     FEPYIYALLK DDSAIEEVKK ITAGRHGRVV KVKRAEKVKK KFLGRPIEVW KLYFTHPQDV
     PAIRDEIRRH SAVVDIYEYD IPFAKRYLID KGLIPMEGDE ELKMMSFDIE TLYHEGEEFG
     TGPILMISYA DEGEARVITW KKIDLPYVEV VSTEKEMIKR FLKVVKEKDP DVLITYNGDN
     FDFAYLKKRC EKIGIKFTLR RDGSEPKIQR MGDRFAVEVK GRIHFDLYPV IRRTINLPTY
     TLEAVYEAVF GTPKEKVYPE EITTAWETGE GLERVARYSM EDAKVTYELG REFFPMEAQL
     SRLIGQSLWD VSRSSTGNLV EWFLLRKAYE RNEIAPNKPD ERELARRRGG YAGGYVKEPE
     RGLWDNIVYL DFMSLYPSII ITHNVSPDTF NREGCKEYDT APQVGHKFCK DVQGFIPSLL
     GALLDERQKI KKRMKASIDP LEKKLLDYRQ KAIKILANSL LPEEWIPLVE NGKVRLHRIG
     EFVDKLMETD SELVKRNGDT EVLEVRGIRA LSFDRKSKKA RVMPVKAVIR HRYSGDVYEI
     VLGSGRRITV TEGHSLFAYG DGELREVTGG EIKAGDLLAV PRRVNLPEKK ERLNLVELLR
     RLPEEETGDI ILTIPVKGRK NFFKGMLRTL RWISGEEKRP RTARRYLEHL EGLGYVRLKK
     IGYEVTDREG LERYRKLYER LVEAVRYNGN KREYLVEFNA VRDVIALMPE EELRDWLVGT
     RNGFRMRPFV EIEEDFAKLL GYYVSEGNAR KWRNQKNGWS YTVKLYNENQ RVLDDMESLA
     ERFFGRVKRG KNYIEIPRKM AYIIFENLCG TLAENKRVPE AIFTSPESVR WAFIEGYFIG
     DGDVHPSKRV RLSTKSELLV NGLVLLLNSL GVSAIKIRHD SGVYRVYVNE ELPFTDYRKK
     KNAYYSHVIP KEILEETFGK VFQRSVSYEK FRELVKSEKL DGEKAKRIEW LLNGDVVLDK
     VLEVKKRPYE GYVYDLSVEE DENFLAGFGL LYAHNSYYGY YGYARARWYC KECAESVTAW
     GRDYIETTIH EIEERFGFKV LYADSVTGET EIIIKRNGKV EFVAIEELFQ RVDYRIGEKE
     YCVLEGVEAL TLDNRGRLVW KSVPYVMRHR TNKRIYRVWF TNSWYLDVTE DHSLIGYMNT
     SKVKPGKPLK ERLVEVKPGE LGESVKSLIT PNRAIAHGIR VNPIAVKLWE LIGLLVGDGN
     WGGQSNWAKY NVGLSLGLDK EEIEEKILKP LKNTGIISNY YDKSKKGDVS ILSKWLARFM
     VRYFKDESGS KRIPEFMFNL PREYIEAFLR GLFSADGTVS LRKGVPEVRL TSVNPELSSS
     VRKLLWLVGV SNSMFVETNP NRYLGKESGT HSVHVRIKDK HRFAERIGFL LDRKATKLSE
     NLGGHTSKKR AYKYDFDLVY PKKVEEIAYD GYVYDIEVEG THRFFANGIL VHNTDGFFAT
     IPGADAETVK KKAKEFLKYI NAKLPGLLEL EYEGFYVRGF FVTKKKYAVI DEEGKITTRG
     LEIVRRDWSE IAKETQARVL EAILRHGDVE EAVRIVKDVT EKLSKYEVPP EKLVIHEQIT
     RELKDYKATG PHVAIAKRLA ARGIKIRPGT VISYIVLKGS GRIGDRAIPF DEFDPTKHRY
     DAEYYIENQV LPAVERILKA FGYKKEELRY QKTRQVGLGA WLKLKGKK