[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=FP-9 / Isolate HP-440; Skinner M.A.; Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2177083 [NCBI, ExPASy, EBI, Israel, Japan] Binns M.M., Britton B.S., Mason C., Boursnell M.E.G.; "Analysis of the fowlpox virus genome region corresponding to the vaccinia virus D6 to A1 region: location of, and variation in, non-essential genes in poxviruses."; J. Gen. Virol. 71:2873-2881(1990).
[3]	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: 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 (By similarity).
CATALYTIC ACTIVITY: NTP + H₂O = NDP + phosphate.
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

AJ005163; CAA06401.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF198100; AAF44396.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S42251; S42251.

RefSeq

NP_039015.1; -.

3D structure databases

ModBase

O72907.

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).

Genome annotation databases

GeneID

1486600; -.

Other

ProtoNet

O72907.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 637`	`637`	`Nucleoside triphosphatase I.`	`PRO_0000099094`
`DOMAIN`	`43 205`	`163`	`Helicase ATP-binding.`
`DOMAIN`	`358 537`	`180`	`Helicase C-terminal.`
`NP_BIND`	`56 63`	`8`	`ATP (By similarity).`
`MOTIF`	`142 145`	`4`	`DEXH box.`

Sequence information

Length: 637 AA [This is the length of the unprocessed precursor]

Molecular weight: 73774 Da [This is the MW of the unprocessed precursor]

CRC64: 9F838D2E0519F0D8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNTYAAYIDY ALKKLDTFPV DMTGGNDNTV LLKDYQLFVA KVFLGLNSMN SILLFQETGV 

        70         80         90        100        110        120 
GKTITTVYML KNLKKIYSEW TIIILVKKAL IDDPWTHTIL DYAPEVMKDC IIMNYDDQNF 

       130        140        150        160        170        180 
HNKFFTNIKS INVKSRIFII IDECHNFISK SLTKEDNKKR NTKLVYNYIA KNLMQKNNKL 

       190        200        210        220        230        240 
ICLSATPIVN DVREFQMLVN LLRPGILTPD KSLFYNKKLI DEKEIISKLG CICSYIVNNE 

       250        260        270        280        290        300 
ASIFEDVENT TLFAKKTVHI KHVFMSKKQE ELYLKARYLE RKLGISVFKI YQRMASTFVF 

       310        320        330        340        350        360 
DDIPDKKKLT EEEYEKFVDS LSIDFKNTLY GKKISKQSLD ILSAGGTIND IKDVKDIELY 

       370        380        390        400        410        420 
NYLYEHSCKF TFVCVSIIQS KGKCLVFEPF IRSSGIEILL QYFNVFGITY IEFSSRTKDI 

       430        440        450        460        470        480 
RSKSVSDFNK VDNTDGEITK VCVFSQSGNE GISFLSINDI FILDMTWNEA SLKQIIGRAI 

       490        500        510        520        530        540 
RLNSHVNNPP ERRYVNVYFV VAKLSSGRSS VDDILLDIIQ SKSKEFSQLY KVFKHSSIEW 

       550        560        570        580        590        600 
IYSNYTDFQT VDDEKGFKKL ISRNIILDEN TITNKKKLTM GENIWYSFSS SLVSIHRGFK 

       610        620        630 
SMDNKIYDSE GFFITVLPDK PTIKIYEGKL IYILTVR

O72907 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