[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1006/viro.1998.9123; PubMed=9601507 [NCBI, ExPASy, EBI, Israel, Japan] Antoine G., Scheiflinger F., Dorner F., Falkner F.G.; "The complete genomic sequence of the modified vaccinia Ankara strain: comparison with other orthopoxviruses."; Virology 244:365-396(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Isolate Acambis 3000; Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J., Khristova M., Wohlhueter R.M.; Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.

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 (By similarity).
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

U94848; AAB96491.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY603355; AAT10467.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T37345; T37345.

3D structure databases

ModBase

O57193.

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).

Other

ProtoNet

O57193.

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_0000055182`
`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.`

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: FB4ABAAFF66AD9FC [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 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 
MYIIHGKVLD IDEILEKVYS SPNVSIIIST PYLESSVTIR NVTHIYDMGR 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 QEAILSLNLR IKILNFKHKD DDTYIHFCKI LFGVYNGTNA TIYYHRPLTG 

       670 
YMNMISDTIF VPVDNN

O57193 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