[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=India-1967 / Isolate Ind3; DOI=10.1016/0168-1702(93)90093-3; PubMed=8109158 [NCBI, ExPASy, EBI, Israel, Japan] Shchelkunov S.N., Blinov V.M., Resenchuk S.M., Totmenin A.V., Sandakhchiev L.S.; "Analysis of the nucleotide sequence of a 43 kbp segment of the genome of variola virus India-1967 strain."; Virus Res. 30:239-258(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=India-1967 / Isolate Ind3; DOI=10.1016/0168-1702(93)90110-9; PubMed=8383392 [NCBI, ExPASy, EBI, Israel, Japan] Shchelkunov S.N., Blinov V.M., Totmenin A.V., Marennikova S.S., Kolykhalov A.A., Frolov I.V., Chizhikov V.E., Gytorov V.V., Gashikov P.V., Belanov E.F., Belavin P.A., Resenchuk S.M., Andzhaparidze O.G., Sandakhchiev L.S.; "Nucleotide sequence analysis of variola virus HindIII M, L, I genome fragments."; Virus Res. 27:25-35(1993).
[3]	COMPLETE GENOME. STRAIN=India-1967 / Isolate Ind3; Blinov V.M.; Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Bangladesh-1975; DOI=10.1038/366748a0; PubMed=8264798 [NCBI, ExPASy, EBI, Israel, Japan] Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C., Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A., Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.; "Potential virulence determinants in terminal regions of variola smallpox virus genome."; Nature 366:748-751(1993).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Garcia-1966; DOI=10.1006/viro.1999.0086; PubMed=10639322 [NCBI, ExPASy, EBI, Israel, Japan] Shchelkunov S.N., Totmenin A.V., Loparev V.N., Safronov P.F., Gutorov V.V., Chizhikov V.E., Knight J.C., Parsons J.M., Massung R.F., Esposito J.J.; "Alastrim smallpox variola minor virus genome DNA sequences."; Virology 266:361-386(2000).

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.

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

X67119; CAA47562.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X69198; CAA49003.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L22579; AAA60810.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y16780; CAB54662.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X76267; CAA53867.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D72158; D72158.
F36843; F36843.
T28500; T28500.

RefSeq

NP_042106.1; -.

3D structure databases

ModBase

P33051.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0008026;	Molecular function: ATP-dependent helicase activity (inferred from electronic annotation from InterPro).
GO:0003676;	Molecular function: nucleic acid binding (inferred from electronic annotation from InterPro).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003593; AAA+_ATPase_core.
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

SM00382; AAA; 1.
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).

ProtoNet

P33051.

Genome annotation databases

GeneID

1486463; -.

Other

UniRef

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

Keywords

ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Transcription.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 676`	`676`	`Nucleoside triphosphatase II.`	`PRO_0000055186`
`DOMAIN`	`172 347`	`176`	`Helicase ATP-binding.`
`DOMAIN`	`366 542`	`177`	`Helicase C-terminal.`
`NP_BIND`	`185 192`	`8`	`ATP (By similarity).`
`MOTIF`	`296 299`	`4`	`DEXH box.`
`VARIANT`	`33 33`	`1`	`M -> T (in strain: Garcia-1966).`
`VARIANT`	`147 147`	`1`	`G -> A (in strain: Garcia-1966).`
`VARIANT`	`450 450`	`1`	`A -> T (in strain: Bangladesh-1975 and Garcia-1966).`
`VARIANT`	`595 595`	`1`	`E -> K (in strain: Garcia-1966).`
`VARIANT`	`632 632`	`1`	`D -> DNDNDND (in strain: Garcia-1966).`

Sequence information

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

Molecular weight: 77545 Da [This is the MW of the unprocessed precursor]

CRC64: 4D7589E5B012562F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEKNLPDIFF FPNCVNVFSY KYSQDEFSNM SNMERDSFSL AVFPVIKHRW HNAHVVKHKG 

        70         80         90        100        110        120 
IYKVSTEAHG KKVSPPSLGK PSHINLTAKQ YIYSEHTISF ECYSFLKCIT NAEINSFDEY 

       130        140        150        160        170        180 
ILRGLLEAGN SLQIFSNSVG KRTDTIGVLG NKYPFSKIPL ASLTPKAQRE IFSAWISHRP 

       190        200        210        220        230        240 
VVLTGGTGVG KTSQVPKLLL WFNYLFGGFS TLDKITDFHE 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 
MYIIHGKVLE IDKILEKVYS SPNVSIIISA PYLESSVTIH NVTHIYDMGR VFVPAPFGGS 

       490        500        510        520        530        540 
QQFISKSMRD QRKGRVGRVN PGTYVYFYDL SYMKSIQRIN SEFLHNYILY ANKFNLTLPE 

       550        560        570        580        590        600 
DLFIIPTNLD ILWRTKEYID SFDISTETWN KLLSNYYMKM IEYAKLYVLS PILAEELDNF 

       610        620        630        640        650        660 
ERTGELTSIV QEAILSLNLR IKILNFKHKD NDTYIHFCKI LFGVYNGTNA TIYYHRPLTG 

       670 
YMNMISDTIF VPVDNN

P33051 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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