Reviewed, UniProtKB/Swiss-Prot P12927 (NTP2_VACCV)

Names and origin

Protein names

Recommended name:
    Nucleoside triphosphatase II
      Short name=NTPase II
    EC=3.6.1.15
Alternative name(s):
    Nucleoside triphosphate phosphohydrolase II
      Short name=NPH II
    RNA helicase I8

Gene names

Name:	NPH2
Ordered Locus Names:	VACWR077
ORF Names:	I8R

Organism

Vaccinia virus (strain Western Reserve / WR) (VACV)

Taxonomic identifier

10254 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Poxviridae › Chordopoxvirinae › Orthopoxvirus

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	676 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Essential for viral replication. Plays an important role during transcription of early mRNAs, presumably by preventing R-loop formation behind the elongating RNA polymerase. Acts as NTP-dependent helicase that catalyzes unidirectional unwinding of 3'tailed duplex RNAs. Might also play a role in the export of newly synthesized mRNA chains out of the core into the cytoplasm. Required for propagation of viral particles.
Catalytic activity	NTP + H(2)O = NDP + phosphate.
Sequence similarities	Belongs to the DEAD box helicase family. DEAH subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.

Ontologies

Keywords
Biological process	Transcription
Developmental stage	Early protein Late protein
Ligand	ATP-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
Gene Ontology (GO)
Biological process	transcription Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro nucleic acid 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 – 676	676	Nucleoside triphosphatase II		PRO_0000055185
Regions
	Domain	172 – 347	176	Helicase ATP-binding
	Domain	366 – 535	170	Helicase C-terminal
	Nucleotide binding	185 – 192	8	ATP By similarity
	Motif	296 – 299	4	DEXH box
Experimental info
	Mutagenesis	191	1	K → A: Inactivates ATPase and helicase activities
	Mutagenesis	192	1	T → A: Inactivates ATPase and helicase activities
	Mutagenesis	229	1	R → A: Inactivates ATPase and helicase activities
	Mutagenesis	296	1	D → A: Reduces strongly NTPase and helicase activities
	Mutagenesis	297	1	E → A: Reduces strongly NTPase and helicase activities
	Mutagenesis	299	1	H → A: Activates NTPase without need for a nucleic acid cofactor
	Mutagenesis	300	1	E → A: Inactivates ATPase and helicase activities
	Mutagenesis	326	1	T → A: Defect in RNA unwinding
	Mutagenesis	328	1	T → A: Defect in RNA unwinding
	Mutagenesis	491	1	Q → A: Defect in ATP hydrolysis and RNA unwinding
	Mutagenesis	492	1	R → A: Defect in ATP hydrolysis and RNA unwinding
	Mutagenesis	494	1	G → A: Defect in ATP hydrolysis and RNA unwinding
	Mutagenesis	495	1	R → A: Defect in ATP hydrolysis and RNA unwinding
	Mutagenesis	497	1	G → A: Defect in ATP hydrolysis and RNA unwinding
	Mutagenesis	498	1	R → A: Defect in ATP hydrolysis and RNA unwinding
	Mutagenesis	502	1	G → A: Defect in ATP hydrolysis and RNA unwinding

Sequences

	Sequence		Length	Mass (Da)
	P12927-1 [UniParc]. Last modified August 1, 1990. Version 2. Checksum: F341266D173EB61E	FASTA	676	77,600
	10 20 30 40 50 60 MEKNLPDIFF FPNCVNVFSY KYSQDEFSNM SKTERDSFSL AVFPVIKHRW HNAHVVKHKG 70 80 90 100 110 120 IYKVSTEARG KKVSPPSLGK PAHINLTAKQ YIYSEHTISF ECYSFLKCIT NTEINSFDEY 130 140 150 160 170 180 ILRGLLEAGN SLQIFSNSVG KRTDTIGVLG NKYPFSKIPL ASLTPKAQRE IFSAWISHRP 190 200 210 220 230 240 VVLTGGTGVG KTSQVPKLLL WFNYLFGGFS TLDKITNFHE RPVILSLPRI ALVRLHSNTI 250 260 270 280 290 300 LKSLGFKVLD GSPISLRYGS IPEELINKQP KKYGIVFSTH KLSLTKLFSY GTLIIDEVHE 310 320 330 340 350 360 HDQIGDIIIA VARKHHTKID SMFLMTATLE DDRERLKVFL PNPAFIHIPG DTLFKISEVF 370 380 390 400 410 420 IHNKINPSSR MAYIEEEKRN LVTAIQMYTP PDGSSGIVFV ASVAQCHEYK SYLEKRLPYD 430 440 450 460 470 480 MYIIHGKVLD IDEILEKVYS SPNVSIIIST PYLESSVTIR NVTHIYDMGK VFVPAPFGGS 490 500 510 520 530 540 QEFISKSMRD QRKGRVGRVN PGTYVYFYDL SYMKSIQRID SEFLHNYILY ANKFNLTLPE 550 560 570 580 590 600 DLFIIPTNLD ILWRTKEYID SFDISTETWN KLLSNYYMKM IEYAKLYVLS PILAEELDNF 610 620 630 640 650 660 ERTGELTSIV REAILSLNLR IKILNFKHKD DDTYIHFCKI LFGVYNGTNA TIYYHRPLTG 670 YMNMISDTIF VPVDNN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic and molecular biological characterization of a vaccinia virus temperature-sensitive complementation group affecting a virion component." Fathi Z., Condit R.C. Virology 181:258-272(1991) [PubMed: 1994576] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb." Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Sequence and transcriptional analysis of the vaccinia virus HindIII I fragment." Schmitt J.F.C., Stunnenberg H.G. J. Virol. 62:1889-1897(1988) [PubMed: 2835495] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99.
[4]	"Vaccinia virus encodes four putative DNA and/or RNA helicases distantly related to each other." Koonin E.V., Senkevich T.G. J. Gen. Virol. 73:989-993(1992) [PubMed: 1321883] [Abstract] Cited for: SIMILARITY TO HELICASES.
[5]	"Vaccinia virions lacking the RNA helicase nucleoside triphosphate phosphohydrolase II are defective in early transcription." Gross C.H., Shuman S. J. Virol. 70:8549-8557(1996) [PubMed: 8970979] [Abstract] Cited for: FUNCTION.
[6]	"The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication." Gross C.H., Shuman S. J. Virol. 72:4729-4736(1998) [PubMed: 9573237] [Abstract] Cited for: MUTAGENESIS OF LYS-191; THR-192; ARG-229; THR-326 AND THR-328.
[7]	"Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase II, a DExH box RNA helicase." Gross C.H., Shuman S. J. Virol. 69:4727-4736(1995) [PubMed: 7609038] [Abstract] Cited for: MUTAGENESIS OF ASP-296; GLU-297 AND HIS-299.
[8]	"The QRxGRxGRxxxG motif of the vaccinia virus DExH box RNA helicase NPH-II is required for ATP hydrolysis and RNA unwinding but not for RNA binding." Gross C.H., Shuman S. J. Virol. 70:1706-1713(1996) [PubMed: 8627691] [Abstract] Cited for: MUTAGENESIS OF GLN-491; ARG-492; GLY-494; ARG-495; GLY-497; ARG-498 AND GLY-502.

Web resources

The DExH/D protein family database

NPH2 entry

Cross-references

Sequence databases
EMBLGenBankDDBJ	J03399 Genomic DNA. Translation: AAB59810.1. AY243312 Genomic DNA. Translation: AAO89356.1.
PIR	WZVZI8. B38497.
RefSeq	YP_232959.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3707610.
Family and domain databases
InterPro	IPR014001. DEAD-like_N. IPR001650. DNA/RNA_helicase_C. IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. IPR002464. DNA/RNA_helicase_DEAH_CS. IPR014021. Helicase_SF1/SF2_ATP-bd. [Graphical view]
Pfam	PF00270. DEAD. 1 hit. PF00271. Helicase_C. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
PROSITE	PS00690. DEAH_ATP_HELICASE. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NTP2_VACCV

Accession

Primary (citable) accession number: P12927
Secondary accession number(s): Q76ZU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	August 1, 1990
Last modified:	November 25, 2008
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Virus (Virus annotation project)