P12927 (NPH2_VACCW) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RNA helicase NPH-II
EC=3.6.4.13

Alternative name(s):
Nucleoside triphosphatase II
Short name=NTPase II
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) (VACV) (Vaccinia virus (strain WR))

Taxonomic identifier

10254 [NCBI]

Taxonomic lineage

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

Virus host

Bos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length	676 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	NTP-dependent helicase that catalyzes unidirectional unwinding of 3'tailed duplex RNAs and plays an important role during transcription of early mRNAs, presumably by preventing R-loop formation behind the elongating RNA polymerase. Might also play a role in the export of newly synthesized mRNA chains out of the core into the cytoplasm. Required for replication and propagation of viral particles. Ref.6 Ref.7
Catalytic activity	ATP + H2O = ADP + phosphate. Ref.8
Subunit structure	Monomer. Ref.6
Subcellular location	Virion. Note: Localizes to the virion core. Ref.3
Induction	Expressed both early and late in the viral replicative cycle. Ref.1
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
Cellular component	Virion
Developmental stage	Early protein Late protein
Ligand	ATP-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	virion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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	RNA helicase NPH-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. Ref.8
	Mutagenesis	192	1	T → A: Inactivates ATPase and helicase activities. Ref.8
	Mutagenesis	229	1	R → A: Inactivates ATPase and helicase activities. Ref.8
	Mutagenesis	296	1	D → A: Reduces strongly NTPase and helicase activities. Ref.9
	Mutagenesis	297	1	E → A: Reduces strongly NTPase and helicase activities. Ref.9
	Mutagenesis	299	1	H → A: Activates NTPase without need for a nucleic acid cofactor. Ref.9
	Mutagenesis	300	1	E → A: Inactivates ATPase and helicase activities.
	Mutagenesis	326	1	T → A: Defect in RNA unwinding. Ref.8
	Mutagenesis	328	1	T → A: Defect in RNA unwinding. Ref.8
	Mutagenesis	491	1	Q → A: Defect in ATP hydrolysis and RNA unwinding. Ref.10
	Mutagenesis	492	1	R → A: Defect in ATP hydrolysis and RNA unwinding. Ref.10
	Mutagenesis	494	1	G → A: Defect in ATP hydrolysis and RNA unwinding. Ref.10
	Mutagenesis	495	1	R → A: Defect in ATP hydrolysis and RNA unwinding. Ref.10
	Mutagenesis	497	1	G → A: Defect in ATP hydrolysis and RNA unwinding. Ref.10
	Mutagenesis	498	1	R → A: Defect in ATP hydrolysis and RNA unwinding. Ref.10
	Mutagenesis	502	1	G → A: Defect in ATP hydrolysis and RNA unwinding. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P12927 [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], INDUCTION.
[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]	"Two nucleid acid-dependent nucleoside triphosphate phosphohydrolases from vaccinia virus. Purification and characterization." Paolette E., Rosemond-Hornbeak H., Moss B. J. Biol. Chem. 249:3273-3280(1974) [PubMed: 4364421] [Abstract] Cited for: SUBCELLULAR LOCATION.
[4]	"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.
[5]	"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.
[6]	"Vaccinia virus RNA helicase: an essential enzyme related to the DE-H family of RNA-dependent NTPases." Shuman S. Proc. Natl. Acad. Sci. U.S.A. 89:10935-10939(1992) [PubMed: 1332061] [Abstract] Cited for: FUNCTION, SUBUNIT.
[7]	"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.
[8]	"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: ENZYME ACTIVITY, MUTAGENESIS OF LYS-191; THR-192; ARG-229; THR-326 AND THR-328.
[9]	"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.
[10]	"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.
[11]	"The DExH protein NPH-II is a processive and directional motor for unwinding RNA." Jankowsky E., Gross C.H., Shuman S., Pyle A.M. Nature 403:447-451(2000) [PubMed: 10667799] [Abstract] Cited for: CHARACTERIZATION.
[12]	"The NPH-II helicase displays efficient DNA x RNA helicase activity and a pronounced purine sequence bias." Taylor S.D., Solem A., Kawaoka J., Pyle A.M. J. Biol. Chem. 285:11692-11703(2010) [PubMed: 20110368] [Abstract] Cited for: CHARACTERIZATION.

Web resources

The DExH/D protein family database

Poxviridae DExH proteins

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03399 Genomic DNA. Translation: AAB59810.1. AY243312 Genomic DNA. Translation: AAO89356.1.
PIR	WZVZI8. B38497.
RefSeq	YP_232959.1. NC_006998.1.
3D structure databases
ProteinModelPortal	P12927.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3707610.
Phylogenomic databases
ProtClustDB	PHA2653.
Family and domain databases
InterPro	IPR014001. DEAD-like_helicase. IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. IPR002464. DNA/RNA_helicase_DEAH_CS. IPR001650. Helicase_C. IPR021892. NPH-II. [Graphical view]
Pfam	PF00270. DEAD. 1 hit. PF12011. DUF3503. 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

NPH2_VACCW

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:	January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program