NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=FP-9 / Isolate HP-440;
DOI=10.1016/0168-1702(92)90004-S; PubMed=1326827 [NCBI, ExPASy, EBI, Israel, Japan]
Binns M.M., Boursnell M.E.G., Skinner M.A.;
"Gene translocations in poxviruses: the fowlpox virus thymidine kinase gene is flanked by 15 bp direct repeats and occupies the locus which in vaccinia virus is occupied by the ribonucleotide reductase large subunit gene.";
Virus Res. 24:161-172(1992).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JVI.74.8.3815-3831.2000; PubMed=10729156 [NCBI, ExPASy, EBI, Israel, Japan]
Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
"The genome of fowlpox virus.";
J. Virol. 74:3815-3831(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 (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.

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

AJ223385; CAA11299.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF198100; AAF44426.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

G48563; G48563.

RefSeq

NP_039045.1; -.

3D structure databases

ModBase

O72904.

Family and domain databases

InterPro

IPR014001; DEAD-like_N.
IPR001650; DNA/RNA_helicase_C.
IPR002464; DNA/RNA_helicase_DEAH_CS.
IPR014021; Helicase_SF1/SF2_ATP-bd.
Graphical view of domain structure.

Pfam

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

BLOCKS

O72904.

Genome annotation databases

GeneID

1486630; -.

Other

ProtoNet

O72904.

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`	`1 682`	`682`	`Nucleoside triphosphatase II.`	`PRO_0000055187`
`DOMAIN`	`181 354`	`174`	`Helicase ATP-binding.`
`DOMAIN`	`386 551`	`166`	`Helicase C-terminal.`
`NP_BIND`	`194 201`	`8`	`ATP (By similarity).`
`MOTIF`	`303 306`	`4`	`DEXH box.`

Sequence information

Length: 682 AA [This is the length of the unprocessed precursor]

Molecular weight: 79808 Da [This is the MW of the unprocessed precursor]

CRC64: F394E69FD9745652 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTTNDLFSIY AFSNMYDIFP RKYSQKELEE YHRKNPLFFS YTIFPVIKHR WSKAYICFQN 

        70         80         90        100        110        120 
NVYMLNIELD TSKPYDRVPI QHLIDIRPIS TDIKKEIYKI SDKTFITFEC YSYLKCKGYN 

       130        140        150        160        170        180 
SIYDITLDDK RGLLSAGNIL SIFSSNKQMP EKSSIGILKN PKPFTVIKFK SLSLITQLQI 

       190        200        210        220        230        240 
FELLRKRKQI VVTGSTGIGK TSQLPKVIMW YNYLFGGWDN LDRVRFDYIS RPIVLSLPRV 

       250        260        270        280        290        300 
ALVKSNGINF LQSLGFSDFE GSPVELRYGG KTEHTTRQHD GIVLSTNKLT SYSLSNYNII 

       310        320        330        340        350        360 
IVDEIHEHDR IADIIISVLR KNIDTIHSLV LMSATLEDDR DRLQEFLPDV EFYHIEGPVL 

       370        380        390        400        410        420 
YSIKEIYVKN KYSYDSKAYT EEEKKNISTT LNWCRPRNGM CGILFLASVS QCISYKKYLE 

       430        440        450        460        470        480 
KSNSDMDFII IHGKIPDITE VLNAVQRPGR ERPCILVSTP YLESSITIRT ATHVYDTGRV 

       490        500        510        520        530        540 
YVPKPFGGDQ LFISKSMMTQ RKGRVGRVSK GIYVYFYDMC LLKPIKSIDH EFLYEYIVYA 

       550        560        570        580        590        600 
KKFKLSLPND LLVIPSDKDM LKKSEEYIKS FNISFDRLFE IYVNYFVNMV EYVKIYNKGG 

       610        620        630        640        650        660 
KKAENLDMFE RNDILTGETL KDIKNLQLLV KINTTTRRKK MYCYKGEILF GPYMNTVIRL 

       670        680 
SSKQLYRNYV YMLTERSFTL YR

O72904 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