DPOL_THEAG
ID DPOL_THEAG Reviewed; 1829 AA.
AC O33845;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 29-SEP-2021, entry version 119.
DE RecName: Full=DNA polymerase;
DE EC=2.7.7.7;
DE AltName: Full=Pol Tfu;
DE Contains:
DE RecName: Full=Tag pol-1 intein;
DE AltName: Full=Intein I;
DE AltName: Full=Tsp-TY pol-1;
DE Contains:
DE RecName: Full=Tag pol-2 intein;
DE AltName: Full=Intein II;
DE AltName: Full=Tsp-TY pol-2;
DE Contains:
DE RecName: Full=Tag pol-3 intein;
DE AltName: Full=Intein III;
DE AltName: Full=Tsp-TY pol-3;
GN Name=pol;
OS Thermococcus aggregans.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=110163;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TY;
RX PubMed=9434178; DOI=10.1016/s0378-1119(97)00536-2;
RA Niehaus F., Frey B., Antranikian G.;
RT "Cloning and characterisation of a thermostable alpha-DNA polymerase from
RT the hyperthermophilic archaeon Thermococcus sp. TY.";
RL Gene 204:153-158(1997).
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 three intervening regions (inteins)
CC followed by peptide ligation.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y13030; CAA73475.1; -; Genomic_DNA.
DR PRIDE; O33845; -.
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 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; 3.
DR SMART; SM00306; HintN; 3.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF51294; SSF51294; 3.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF55608; SSF55608; 2.
DR SUPFAM; SSF56672; SSF56672; 3.
DR TIGRFAMs; TIGR01443; intein_Cterm; 3.
DR TIGRFAMs; TIGR01445; intein_Nterm; 2.
DR PROSITE; PS50818; INTEIN_C_TER; 3.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2.
DR PROSITE; PS50817; INTEIN_N_TER; 3.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Endonuclease; Hydrolase; Nuclease;
KW Nucleotidyltransferase; Protein splicing; Repeat; Transferase.
FT CHAIN 1..409
FT /note="DNA polymerase, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007353"
FT CHAIN 410..769
FT /note="Tag pol-1 intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007354"
FT CHAIN 770..855
FT /note="DNA polymerase, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007355"
FT CHAIN 856..1392
FT /note="Tag pol-2 intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007356"
FT CHAIN 1393..1441
FT /note="DNA polymerase, 3rd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007357"
FT CHAIN 1442..1598
FT /note="Tag pol-3 intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007358"
FT CHAIN 1599..1829
FT /note="DNA polymerase, 4th part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007359"
FT DOMAIN 527..668
FT /note="DOD-type homing endonuclease 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT DOMAIN 1136..1269
FT /note="DOD-type homing endonuclease 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
SQ SEQUENCE 1829 AA; 211879 MW; A113A8BC57EB9CB3 CRC64;
MILDTDYITK DGKPIIRIFK KENGEFKIEL DPHFQPYIYA LLKDDSAIDE IKAIKGERHG
KIVRVVDAVK VKKKFLGRDV EVWKLIFEHP QDVPALRGKI REHPAVIDIY EYDIPFAKRY
LIDKGLIPME GDEELKLMAF DIETFYHEGD EFGKGEIIMI SYADEEEARV ITWKNIDLPY
VDVVSNEREM IKRFVQIVRE KDPDVLITYN GDNFDLPYLI KRAEKLGVTL LLGRDKEHPE
PKIHRMGDSF AVEIKGRIHF DLFPVVRRTI NLPTYTLEAV YEAVLGKTKS KLGAEEIAAI
WETEESMKKL AQYSMEDARA TYELGKEFFP MEAELAKLIG QSVWDVSRSS TGNLVEWYLL
RVAYERNELA PNKPDEEEYR RRLRTTYLGG YVKEPERGLW ENIAYLDFRC HPADTKVIVK
GKGIVNISDV KEGDYILGID GWQRVKKVWK YHYEGKLINI NGLKCTPNHK VPVVTENDRQ
TRIRDSLAKS FLSGKVKGKI ITTKLFEKIA EFEKNKPSEE EILKGELSGI ILAEGTLLRK
DIEYFDSSRG KKRISHQYRV EITIGENEKE LLERILYIFD KLFGIRPSVK KKGDTNALKI
TTAKKAVYLQ IEELLKNIES LYAPAVLRGF FERDATVNKI RSTIVVTQGT NNKWKIDIVA
KLLDSLGIPY SRYEYKYIEN GKELTKHILE ITGRDGLILF QTLVGFISSE KNEALEKAIE
VREMNRLKNN SFYNLSTFEV SSEYYKGEVY DLTLEGNPYY FANGILTHNS LYPSIIVTHN
VSPDTLEREG CKNYDVAPIV GYKFCKDFPG FIPSILGELI TMRQEIKKKM KATIDPIEKK
MLDYRQRAVK LLANSILPNE WLPIIENGEV KFVKIGEFID RYMEEQKDKV RTVDNTEVLE
VDNIFAFSLN KESKKSEIKK VKALIRHKYK GEAYEVELNS GRKIHITRGH SLFTIRNGKI
KEIWGEEVKV GDLIIVPKKV KLNEKEAVIN IPELISKLPD EDTADVVMTT PVKGRKNFFK
GMLRTLKWIF GEESKRIRTF NRYLFHLEEL GFVKLLPRGY EVTDWEGLKR YRQLYEKLVK
NLRYNGNKRE YLVRFNDIKD SVSCFPRKEL EEWKIGTXKG FRXKCILKVD EDFGKFLGYY
VSEGYAGAQK NKTGGMSYSV KLYNENPNVL KDMKNIAEKF FGKVRVGKNC VDIPKKMAYL
LAKSLCGVTA ENKRIPSIIF DSSEPVRWAF LRAYFVGDGD IHPSKRLRLS TKSELLANQL
VFLLNSLGVS SIKIGFDSGV YRVYINEDLP FLQTSRQKNT YYPNLIPKEV LEEIFGRKFQ
KNITFEKFKE LADSGKLDKR KVKLLDFLLN GDIVLDRVKN VEKREYEGYV YDLSVEDNEN
FLVGFGLLYA HNSYYGYMGY PKARWYSKEC AESVTAWGRH YIEMTIKEIE EKFGFKVLYA
DSVTGDTEII VKRNGRIEFV PIEKLFERVD YRIGEKEYCI LEDVEALTLD NRGKLIWKKV
PYVMRHRAKK KVYRIWITNS WYIDVTEDHS LIVAEDGLKE ARPMEIEGKS LIATKDDLSG
VEYIKPHAIE EISYNGYVYD IEVEGTHRFF ANGILVHNTD GFYATIPGEK PETIKKKAKE
FLKYINSKLP GLLELEYEGF YLRGFFVAKK RYAVIDEEGR ITTRGLEVVR RDWSEIAKET
QAKVLEAILK EDSVEKAVEI VKDVVEEIAK YQVPLEKLVI HEQITKDLSE YKAIGPHVAI
AKRLAAKGIK VRPGTIISYI VLRGSGKISD RVILLSEYDP KKHKYDPDYY IENQVLPAVL
RILEAFGYRK EDLKYQSSKQ VGLDAWLKK
