[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: Serves two roles in transcription; it acts in concert with viral termination factor/capping enzyme to catalyze release of UUUUUNU-containing nascent RNA from the elongation complex, and it acts by itself as a polymerase elongation factor to facilitate readthrough of intrinsic pause sites.
CATALYTIC ACTIVITY: NTP + H₂O = NDP + phosphate.
SUBUNIT: Monomer.
SIMILARITY: Belongs to the helicase family. NPH I 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

U94848; AAB96451.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY603355; AAT10506.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T37384; T37384.

3D structure databases

ModBase

O57214.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0004386;	Molecular function: helicase activity (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

IPR014001; DEAD-like_N.
IPR001650; DNA/RNA_helicase_C.
IPR014021; Helicase_SF1/SF2_ATP-bd.
IPR013676; NPHI_C.
IPR000330; SNF2_N.
Graphical view of domain structure.

Pfam

PF00271; Helicase_C; 1.
PF08469; NPHI_C; 1.
PF00176; SNF2_N; 1.
Pfam graphical view of domain structure.

SMART

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

PROSITE

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

Other

ProtoNet

O57214.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 631`	`631`	`Nucleoside triphosphatase I.`	`PRO_0000099090`
`DOMAIN`	`42 204`	`163`	`Helicase ATP-binding.`
`DOMAIN`	`367 532`	`166`	`Helicase C-terminal.`
`NP_BIND`	`55 62`	`8`	`ATP (By similarity).`
`MOTIF`	`141 144`	`4`	`DEXH box.`

Sequence information

Length: 631 AA [This is the length of the unprocessed precursor]

Molecular weight: 72381 Da [This is the MW of the unprocessed precursor]

CRC64: E7FE68BA105A1A35 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKSHAAYID YALRRTTNMP VEMMGTDVVR LKDYQHFVAR VFLGLDSMHS LLLFHETGVG 

        70         80         90        100        110        120 
KTMTTVYILK HLKDIYTNWA IILLVKKALI EDPWMNTILR YAPEITKDCI FINYDDQNFR 

       130        140        150        160        170        180 
NKFFTNIKTI NSKSRICVII DECHNFISKS LIKEDGKIRP TRSVYNFLSK TIALKNHKMI 

       190        200        210        220        230        240 
CLSATPIVNS VQEFTMLVNL LRPGSLQHQS LFENKRLVDE KELVSKLGGL CSYIVNNEFS 

       250        260        270        280        290        300 
IFDDVEGSAS FAKKTVLMRY VNMSKKQEEI YQKAKLAEIK TGISSFRILR RMATTFTFDS 

       310        320        330        340        350        360 
FPERQNRDPG EYAQEIATLY NDFKNSLRDR EFSKSALDTF KKGELLKGDA SAADISLFTE 

       370        380        390        400        410        420 
LKEKSVKFID VCLGILASHG KCLVFEPFVN QSGIEILLLY FKVFGISNIE FSSRTKDTRI 

       430        440        450        460        470        480 
KAVAEFNQES NTNGECIKTC VFSSSGGEGI SFFSINDIFI LDMTWNEASL RQIVGRAIRL 

       490        500        510        520        530        540 
NSHVLTPPER RYVNVHFIMA RLSNGMPTVD EDLFEIIQSK SKEFVQLFRV FKHTSLEWIH 

       550        560        570        580        590        600 
ANEKDFSPID NESGWKTLVS RAIDLSSKKN ITNKLIEGTN IWYSNSNRLM SINRGFKGVD 

       610        620        630 
GRVYDVDGNY LHDMPDNPVI KIHDGKLIYI F

O57214 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