P30317 (DPOL_THELI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase
EC=2.7.7.7

Alternative name(s):
Vent DNA polymerase

Cleaved into the following 2 chains:

1. Endonuclease PI-TliII
   EC=3.1.-.-
   Alternative name(s):
   IVPS2
   Tli pol-1 intein
2. Endonuclease PI-TliI
   EC=3.1.-.-
   Alternative name(s):
   IVPS1
   Tli pol-2 intein

Gene names

Name:

pol

Organism

Thermococcus litoralis

Taxonomic identifier

2265 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Thermococcus

Protein attributes

Sequence length	1702 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity. Intein encoded endonucleases are thought to mediate intein mobility by site-specific recombination initiated by endonuclease cleavage at the "homing site" in gene that lack the intein.
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Post-translational modification	This protein undergoes a protein self splicing that involves a post-translational excision of the two intervening regions (inteins) followed by peptide ligation.
Biotechnological use	Used in the PCR method because of its high thermostability and low error rate. Sold by New England Biolabs.
Sequence similarities	Belongs to the DNA polymerase type-B family. Contains 2 DOD-type homing endonuclease domains.

Ontologies

Keywords
Biological process	DNA replication Intron homing
Domain	Repeat
Ligand	DNA-binding
Molecular function	DNA-directed DNA polymerase Endonuclease Hydrolase Nuclease Nucleotidyltransferase Transferase
PTM	Autocatalytic cleavage Protein splicing
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW intein-mediated protein splicing Inferred from electronic annotation. Source: InterPro intron homing Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 494	494	DNA polymerase, 1st part		PRO_0000007338
	Chain	495 – 1032	538	Endonuclease PI-TliII		PRO_0000007339
	Chain	1033 – 1081	49	DNA polymerase, 2nd part		PRO_0000007340
	Chain	1082 – 1471	390	Endonuclease PI-TliI		PRO_0000007341
	Chain	1472 – 1702	231	DNA polymerase, 3rd part		PRO_0000007342
Regions
	Domain	776 – 909	134	DOD-type homing endonuclease 1
	Domain	1229 – 1368	140	DOD-type homing endonuclease 2

Sequences

	Sequence		Length	Mass (Da)
	P30317 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 21D6B98C75F53B20	FASTA	1,702	197,294
	10 20 30 40 50 60 MILDTDYITK DGKPIIRIFK KENGEFKIEL DPHFQPYIYA LLKDDSAIEE IKAIKGERHG 70 80 90 100 110 120 KTVRVLDAVK VRKKFLGREV EVWKLIFEHP QDVPAMRGKI REHPAVVDIY EYDIPFAKRY 130 140 150 160 170 180 LIDKGLIPME GDEELKLLAF DIETFYHEGD EFGKGEIIMI SYADEEEARV ITWKNIDLPY 190 200 210 220 230 240 VDVVSNEREM IKRFVQVVKE KDPDVIITYN GDNFDLPYLI KRAEKLGVRL VLGRDKEHPE 250 260 270 280 290 300 PKIQRMGDSF AVEIKGRIHF DLFPVVRRTI NLPTYTLEAV YEAVLGKTKS KLGAEEIAAI 310 320 330 340 350 360 WETEESMKKL AQYSMEDARA TYELGKEFFP MEAELAKLIG QSVWDVSRSS TGNLVEWYLL 370 380 390 400 410 420 RVAYARNELA PNKPDEEEYK RRLRTTYLGG YVKEPEKGLW ENIIYLDFRS LYPSIIVTHN 430 440 450 460 470 480 VSPDTLEKEG CKNYDVAPIV GYRFCKDFPG FIPSILGDLI AMRQDIKKKM KSTIDPIEKK 490 500 510 520 530 540 MLDYRQRAIK LLANSILPNE WLPIIENGEI KFVKIGEFIN SYMEKQKENV KTVENTEVLE 550 560 570 580 590 600 VNNLFAFSFN KKIKESEVKK VKALIRHKYK GKAYEIQLSS GRKINITAGH SLFTVRNGEI 610 620 630 640 650 660 KEVSGDGIKE GDLIVAPKKI KLNEKGVSIN IPELISDLSE EETADIVMTI SAKGRKNFFK 670 680 690 700 710 720 GMLRTLRWMF GEENRRIRTF NRYLFHLEKL GLIKLLPRGY EVTDWERLKK YKQLYEKLAG 730 740 750 760 770 780 SVKYNGNKRE YLVMFNEIKD FISYFPQKEL EEWKIGTLNG FRTNCILKVD EDFGKLLGYY 790 800 810 820 830 840 VSEGYAGAQK NKTGGISYSV KLYNEDPNVL ESMKNVAEKF FGKVRVDRNC VSISKKMAYL 850 860 870 880 890 900 VMKCLCGALA ENKRIPSVIL TSPEPVRWSF LEAYFTGDGD IHPSKRFRLS TKSELLANQL 910 920 930 940 950 960 VFLLNSLGIS SVKIGFDSGV YRVYINEDLQ FPQTSREKNT YYSNLIPKEI LRDVFGKEFQ 970 980 990 1000 1010 1020 KNMTFKKFKE LVDSGKLNRE KAKLLEFFIN GDIVLDRVKS VKEKDYEGYV YDLSVEDNEN 1030 1040 1050 1060 1070 1080 FLVGFGLLYA HNSYYGYMGY PKARWYSKEC AESVTAWGRH YIEMTIREIE EKFGFKVLYA 1090 1100 1110 1120 1130 1140 DSVSGESEII IRQNGKIRFV KIKDLFSKVD YSIGEKEYCI LEGVEALTLD DDGKLVWKPV 1150 1160 1170 1180 1190 1200 PYVMRHRANK RMFRIWLTNS WYIDVTEDHS LIGYLNTSKT KTAKKIGERL KEVKPFELGK 1210 1220 1230 1240 1250 1260 AVKSLICPNA PLKDENTKTS EIAVKFWELV GLIVGDGNWG GDSRWAEYYL GLSTGKDAEE 1270 1280 1290 1300 1310 1320 IKQKLLEPLK TYGVISNYYP KNEKGDFNIL AKSLVKFMKR HFKDEKGRRK IPEFMYELPV 1330 1340 1350 1360 1370 1380 TYIEAFLRGL FSADGTVTIR KGVPEIRLTN IDADFLREVR KLLWIVGISN SIFAETTPNR 1390 1400 1410 1420 1430 1440 YNGVSTGTYS KHLRIKNKWR FAERIGFLIE RKQKRLLEHL KSARVKRNTI DFGFDLVHVK 1450 1460 1470 1480 1490 1500 KVEEIPYEGY VYDIEVEETH RFFANNILVH NTDGFYATIP GEKPELIKKK AKEFLNYINS 1510 1520 1530 1540 1550 1560 KLPGLLELEY EGFYLRGFFV TKKRYAVIDE EGRITTRGLE VVRRDWSEIA KETQAKVLEA 1570 1580 1590 1600 1610 1620 ILKEGSVEKA VEVVRDVVEK IAKYRVPLEK LVIHEQITRD LKDYKAIGPH VAIAKRLAAR 1630 1640 1650 1660 1670 1680 GIKVKPGTII SYIVLKGSGK ISDRVILLTE YDPRKHKYDP DYYIENQVLP AVLRILEAFG 1690 1700 YRKEDLRYQS SKQTGLDAWL KR

References

[1]	"Intervening sequences in an Archaea DNA polymerase gene." Perler F.B., Comb D.G., Jack W.E., Moran L.S., Qiang B., Kucera R.B., Benner J., Slatko B.E., Nwankwo D.O., Hempstead S.K., Carlow C.K.S., Jannasch H. Proc. Natl. Acad. Sci. U.S.A. 89:5577-5581(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Protein splicing removes intervening sequences in an archaea DNA polymerase." Hodges R.A., Perler F.B., Noren C.J., Jack W.E. Nucleic Acids Res. 20:6153-6157(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SPLICING.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M74198 Unassigned DNA. Translation: AAA72100.1. M74198 Unassigned DNA. Translation: AAA72101.1.
PIR	S42459.
3D structure databases
ProteinModelPortal	P30317.
SMR	P30317. Positions 1-1082, 1456-1701.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR006172. DNA-dir_DNA_pol_B. IPR006133. DNA-dir_DNA_pol_B_exonuc. IPR006134. DNA-dir_DNA_pol_B_multi_dom. IPR004578. DNA-dir_DNA_pol_B_pol2. IPR003586. Hint_dom_C. IPR003587. Hint_dom_N. IPR006142. INTEIN. IPR004042. Intein_endonuc. IPR006141. Intein_splice_site. IPR012337. RNaseH-like_dom. [Graphical view]
Pfam	PF00136. DNA_pol_B. 3 hits. PF03104. DNA_pol_B_exo1. 2 hits. [Graphical view]
PRINTS	PR00379. INTEIN.
SMART	SM00305. HintC. 2 hits. SM00306. HintN. 2 hits. SM00486. POLBc. 1 hit. [Graphical view]
SUPFAM	SSF53098. RNaseH_fold. 1 hit.
TIGRFAMs	TIGR01443. intein_Cterm. 2 hits. TIGR01445. intein_Nterm. 2 hits. TIGR00592. pol2. 2 hits.
PROSITE	PS00116. DNA_POLYMERASE_B. False negative. PS50818. INTEIN_C_TER. 2 hits. PS50819. INTEIN_ENDONUCLEASE. 2 hits. PS50817. INTEIN_N_TER. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DPOL_THELI

Accession

Primary (citable) accession number: P30317

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	April 3, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program