[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0042-6822(91)90491-S; PubMed=1994576 [NCBI, ExPASy, EBI, Israel, Japan] Fathi Z., Condit R.C.; "Genetic and molecular biological characterization of a vaccinia virus temperature-sensitive complementation group affecting a virion component."; Virology 181:258-272(1991).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R.; "Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb."; Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99. PubMed=2835495 [NCBI, ExPASy, EBI, Israel, Japan] Schmitt J.F.C., Stunnenberg H.G.; "Sequence and transcriptional analysis of the vaccinia virus HindIII I fragment."; J. Virol. 62:1889-1897(1988).
[4]	SIMILARITY TO HELICASES. PubMed=1321883 [NCBI, ExPASy, EBI, Israel, Japan] Koonin E.V., Senkevich T.G.; "Vaccinia virus encodes four putative DNA and/or RNA helicases distantly related to each other."; J. Gen. Virol. 73:989-993(1992).
[5]	FUNCTION. PubMed=8970979 [NCBI, ExPASy, EBI, Israel, Japan] Gross C.H., Shuman S.; "Vaccinia virions lacking the RNA helicase nucleoside triphosphate phosphohydrolase II are defective in early transcription."; J. Virol. 70:8549-8557(1996).
[6]	MUTAGENESIS OF LYS-191; THR-192; ARG-229; THR-326 AND THR-328. PubMed=9573237 [NCBI, ExPASy, EBI, Israel, Japan] Gross C.H., Shuman S.; "The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication."; J. Virol. 72:4729-4736(1998).
[7]	MUTAGENESIS OF ASP-296; GLU-297 AND HIS-299. PubMed=7609038 [NCBI, ExPASy, EBI, Israel, Japan] Gross C.H., Shuman S.; "Mutational analysis of vaccinia virus nucleoside triphosphate phosphohydrolase II, a DExH box RNA helicase."; J. Virol. 69:4727-4736(1995).
[8]	MUTAGENESIS OF GLN-491; ARG-492; GLY-494; ARG-495; GLY-497; ARG-498 AND GLY-502. PubMed=8627691 [NCBI, ExPASy, EBI, Israel, Japan] Gross C.H., Shuman S.; "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."; J. Virol. 70:1706-1713(1996).

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 + H₂O = NDP + phosphate.
SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
SIMILARITY: Contains 1 helicase ATP-binding domain.
SIMILARITY: Contains 1 helicase C-terminal domain.
WEB RESOURCE: Name=The DExH/D protein family database; Note=NPH2 entry; URL="http://www.helicase.net/dexhd/NPH2.htm";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J03399; AAB59810.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY243312; AAO89356.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B38497; WZVZI8.

RefSeq

YP_232959.1; -.

3D structure databases

ModBase

P12927.

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 of domain structure.

Pfam

PF00270; DEAD; 1.
PF00271; Helicase_C; 1.
Pfam graphical view of domain structure.

SMART

SM00487; DEXDc; 1.
SM00490; HELICc; 1.
SMART graphical view of domain structure.

PROSITE

PS00690; DEAH_ATP_HELICASE; 1.
PS51192; HELICASE_ATP_BIND_1; 1.
PS51194; HELICASE_CTER; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P12927.

Genome annotation databases

GeneID

3707610; -.

Other

ProtoNet

P12927.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Early protein; Helicase; Hydrolase; Late protein; Nucleotide-binding; Transcription.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 676`	`676`	`Nucleoside triphosphatase II.`	`PRO_0000055185`
`DOMAIN`	`172 347`	`176`	`Helicase ATP-binding.`
`DOMAIN`	`366 535`	`170`	`Helicase C-terminal.`
`NP_BIND`	`185 192`	`8`	`ATP (By similarity).`
`MOTIF`	`296 299`	`4`	`DEXH box.`
`MUTAGEN`	`191 191`		`K->A: Inactivates ATPase and helicase activities.`
`MUTAGEN`	`192 192`		`T->A: Inactivates ATPase and helicase activities.`
`MUTAGEN`	`229 229`		`R->A: Inactivates ATPase and helicase activities.`
`MUTAGEN`	`296 296`		`D->A: Reduces strongly NTPase and helicase activities.`
`MUTAGEN`	`297 297`		`E->A: Reduces strongly NTPase and helicase activities.`
`MUTAGEN`	`299 299`		`H->A: Activates NTPase without need for a nucleic acid cofactor.`
`MUTAGEN`	`300 300`		`E->A: Inactivates ATPase and helicase activities.`
`MUTAGEN`	`326 326`		`T->A: Defect in RNA unwinding.`
`MUTAGEN`	`328 328`		`T->A: Defect in RNA unwinding.`
`MUTAGEN`	`491 491`		`Q->A: Defect in ATP hydrolysis and RNA unwinding.`
`MUTAGEN`	`492 492`		`R->A: Defect in ATP hydrolysis and RNA unwinding.`
`MUTAGEN`	`494 494`		`G->A: Defect in ATP hydrolysis and RNA unwinding.`
`MUTAGEN`	`495 495`		`R->A: Defect in ATP hydrolysis and RNA unwinding.`
`MUTAGEN`	`497 497`		`G->A: Defect in ATP hydrolysis and RNA unwinding.`
`MUTAGEN`	`498 498`		`R->A: Defect in ATP hydrolysis and RNA unwinding.`
`MUTAGEN`	`502 502`		`G->A: Defect in ATP hydrolysis and RNA unwinding.`

Sequence information

Length: 676 AA [This is the length of the unprocessed precursor]

Molecular weight: 77600 Da [This is the MW of the unprocessed precursor]

CRC64: F341266D173EB61E [This is a checksum on the sequence]

        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

P12927 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools