DPOL_THELI
ID DPOL_THELI Reviewed; 1702 AA.
AC P30317;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=DNA polymerase;
DE EC=2.7.7.7;
DE AltName: Full=Vent DNA polymerase;
DE Contains:
DE RecName: Full=Endonuclease PI-TliII;
DE EC=3.1.-.-;
DE AltName: Full=IVPS2;
DE AltName: Full=Tli pol-1 intein;
DE Contains:
DE RecName: Full=Endonuclease PI-TliI;
DE EC=3.1.-.-;
DE AltName: Full=IVPS1;
DE AltName: Full=Tli pol-2 intein;
GN Name=pol;
OS Thermococcus litoralis.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=2265;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1608969; DOI=10.1073/pnas.89.12.5577;
RA Perler F.B., Comb D.G., Jack W.E., Moran L.S., Qiang B., Kucera R.B.,
RA Benner J., Slatko B.E., Nwankwo D.O., Hempstead S.K., Carlow C.K.S.,
RA Jannasch H.;
RT "Intervening sequences in an Archaea DNA polymerase gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:5577-5581(1992).
RN [2]
RP PROTEIN SPLICING.
RX PubMed=1475179; DOI=10.1093/nar/20.23.6153;
RA Hodges R.A., Perler F.B., Noren C.J., Jack W.E.;
RT "Protein splicing removes intervening sequences in an archaea DNA
RT polymerase.";
RL Nucleic Acids Res. 20:6153-6157(1992).
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 3' to 5' exonuclease activity.
CC -!- FUNCTION: Intein encoded endonucleases are thought to mediate intein
CC mobility by site-specific recombination initiated by endonuclease
CC cleavage at the 'homing site' in gene that lack the intein.
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 two intervening regions (inteins)
CC followed by peptide ligation.
CC -!- BIOTECHNOLOGY: Used in the PCR method because of its high
CC thermostability and low error rate. Sold by New England Biolabs.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR EMBL; M74198; AAA72100.1; -; Unassigned_DNA.
DR EMBL; M74198; AAA72101.1; -; Unassigned_DNA.
DR PIR; S42459; S42459.
DR RefSeq; WP_004067109.1; NC_022084.1.
DR AlphaFoldDB; P30317; -.
DR SMR; P30317; -.
DR GeneID; 16550440; -.
DR OMA; YAHNSYY; -.
DR BRENDA; 2.7.7.7; 6302.
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: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; Direct protein sequencing; DNA replication;
KW DNA-binding; DNA-directed DNA polymerase; Endonuclease; Hydrolase;
KW Intron homing; Nuclease; Nucleotidyltransferase; Protein splicing; Repeat;
KW Transferase.
FT CHAIN 1..494
FT /note="DNA polymerase, 1st part"
FT /id="PRO_0000007338"
FT CHAIN 495..1032
FT /note="Endonuclease PI-TliII"
FT /id="PRO_0000007339"
FT CHAIN 1033..1081
FT /note="DNA polymerase, 2nd part"
FT /id="PRO_0000007340"
FT CHAIN 1082..1471
FT /note="Endonuclease PI-TliI"
FT /id="PRO_0000007341"
FT CHAIN 1472..1702
FT /note="DNA polymerase, 3rd part"
FT /id="PRO_0000007342"
FT DOMAIN 776..909
FT /note="DOD-type homing endonuclease 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT DOMAIN 1229..1368
FT /note="DOD-type homing endonuclease 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
SQ SEQUENCE 1702 AA; 197294 MW; 21D6B98C75F53B20 CRC64;
MILDTDYITK DGKPIIRIFK KENGEFKIEL DPHFQPYIYA LLKDDSAIEE IKAIKGERHG
KTVRVLDAVK VRKKFLGREV EVWKLIFEHP QDVPAMRGKI REHPAVVDIY EYDIPFAKRY
LIDKGLIPME GDEELKLLAF DIETFYHEGD EFGKGEIIMI SYADEEEARV ITWKNIDLPY
VDVVSNEREM IKRFVQVVKE KDPDVIITYN GDNFDLPYLI KRAEKLGVRL VLGRDKEHPE
PKIQRMGDSF AVEIKGRIHF DLFPVVRRTI NLPTYTLEAV YEAVLGKTKS KLGAEEIAAI
WETEESMKKL AQYSMEDARA TYELGKEFFP MEAELAKLIG QSVWDVSRSS TGNLVEWYLL
RVAYARNELA PNKPDEEEYK RRLRTTYLGG YVKEPEKGLW ENIIYLDFRS LYPSIIVTHN
VSPDTLEKEG CKNYDVAPIV GYRFCKDFPG FIPSILGDLI AMRQDIKKKM KSTIDPIEKK
MLDYRQRAIK LLANSILPNE WLPIIENGEI KFVKIGEFIN SYMEKQKENV KTVENTEVLE
VNNLFAFSFN KKIKESEVKK VKALIRHKYK GKAYEIQLSS GRKINITAGH SLFTVRNGEI
KEVSGDGIKE GDLIVAPKKI KLNEKGVSIN IPELISDLSE EETADIVMTI SAKGRKNFFK
GMLRTLRWMF GEENRRIRTF NRYLFHLEKL GLIKLLPRGY EVTDWERLKK YKQLYEKLAG
SVKYNGNKRE YLVMFNEIKD FISYFPQKEL EEWKIGTLNG FRTNCILKVD EDFGKLLGYY
VSEGYAGAQK NKTGGISYSV KLYNEDPNVL ESMKNVAEKF FGKVRVDRNC VSISKKMAYL
VMKCLCGALA ENKRIPSVIL TSPEPVRWSF LEAYFTGDGD IHPSKRFRLS TKSELLANQL
VFLLNSLGIS SVKIGFDSGV YRVYINEDLQ FPQTSREKNT YYSNLIPKEI LRDVFGKEFQ
KNMTFKKFKE LVDSGKLNRE KAKLLEFFIN GDIVLDRVKS VKEKDYEGYV YDLSVEDNEN
FLVGFGLLYA HNSYYGYMGY PKARWYSKEC AESVTAWGRH YIEMTIREIE EKFGFKVLYA
DSVSGESEII IRQNGKIRFV KIKDLFSKVD YSIGEKEYCI LEGVEALTLD DDGKLVWKPV
PYVMRHRANK RMFRIWLTNS WYIDVTEDHS LIGYLNTSKT KTAKKIGERL KEVKPFELGK
AVKSLICPNA PLKDENTKTS EIAVKFWELV GLIVGDGNWG GDSRWAEYYL GLSTGKDAEE
IKQKLLEPLK TYGVISNYYP KNEKGDFNIL AKSLVKFMKR HFKDEKGRRK IPEFMYELPV
TYIEAFLRGL FSADGTVTIR KGVPEIRLTN IDADFLREVR KLLWIVGISN SIFAETTPNR
YNGVSTGTYS KHLRIKNKWR FAERIGFLIE RKQKRLLEHL KSARVKRNTI DFGFDLVHVK
KVEEIPYEGY VYDIEVEETH RFFANNILVH NTDGFYATIP GEKPELIKKK AKEFLNYINS
KLPGLLELEY EGFYLRGFFV TKKRYAVIDE EGRITTRGLE VVRRDWSEIA KETQAKVLEA
ILKEGSVEKA VEVVRDVVEK IAKYRVPLEK LVIHEQITRD LKDYKAIGPH VAIAKRLAAR
GIKVKPGTII SYIVLKGSGK ISDRVILLTE YDPRKHKYDP DYYIENQVLP AVLRILEAFG
YRKEDLRYQS SKQTGLDAWL KR
