[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1006/viro.2000.0449; PubMed=10936094 [NCBI, ExPASy, EBI, Israel, Japan] Bawden A.L., Glassberg K.J., Diggans J., Shaw R., Farmerie W., Moyer R.W.; "Complete genomic sequence of the Amsacta moorei entomopoxvirus: analysis and comparison with other poxviruses."; Virology 274:120-139(2000).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-486. DOI=10.1006/viro.1993.1020; PubMed=8517016 [NCBI, ExPASy, EBI, Israel, Japan] Hall R.L., Moyer R.W.; "Identification of an Amsacta spheroidin-like protein within the occlusion bodies of Choristoneura entomopoxviruses."; Virology 192:179-187(1993).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 486-648. PubMed=1942245 [NCBI, ExPASy, EBI, Israel, Japan] Hall R.L., Moyer R.W.; "Identification, cloning, and sequencing of a fragment of Amsacta moorei entomopoxvirus DNA containing the spheroidin gene and three vaccinia virus-related open reading frames."; J. Virol. 65:6516-6527(1991).

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

AF250284; AAG02898.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M77182; AAA42384.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F41561; NPVZAM.

RefSeq

NP_064974.1; -.

3D structure databases

ModBase

P29814.

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

1494782; -.

Other

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`	`1 648`	`648`	`Nucleoside triphosphatase I.`	`PRO_0000099099`
`DOMAIN`	`48 212`	`165`	`Helicase ATP-binding.`
`DOMAIN`	`378 541`	`164`	`Helicase C-terminal.`
`NP_BIND`	`61 68`	`8`	`ATP (By similarity).`
`MOTIF`	`150 153`	`4`	`DEXH box.`

Sequence information

Length: 648 AA [This is the length of the unprocessed precursor]

Molecular weight: 76109 Da [This is the MW of the unprocessed precursor]

CRC64: 25BE863C0B8728AA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFALDSIVGK HINYALDKTQ HLPNKIMNNI TNTEITLQDY QYFVSRIFIG LKNLNSMLLF 

        70         80         90        100        110        120 
WDTGMGKTLT AVYIIKYIKE LFPRWIILIF IKKSLYIDPW LNTIRSYISD TSNIKFIYYD 

       130        140        150        160        170        180 
SSSSLDKFNN IYRSIESSLN KKSRLLIIID EVHKLISRTV KKDNNERNFT PIYKKLIKLA 

       190        200        210        220        230        240 
NFENNKILCM SATPVTNNIS EFNNLIGLLR PNVMNIKEEY INNGKLINFK ELRETLLAIC 

       250        260        270        280        290        300 
SYKRLIEADS LTETNYIDGY AKKNIFYHNI IMSDEQSKLY NMAEKYDYKT ELGGLKTMRR 

       310        320        330        340        350        360 
LISSFAFYDL KIKGDLDNIE YNDMIKRKLA EFSEFTKNIN FSESFIESFK NDNIKIKTNL 

       370        380        390        400        410        420 
PITDINNYNI LYQYSCKYIE TCKIILNSRG KVLIFEPLVN FEGISSLKCY FNCFNISYIE 

       430        440        450        460        470        480 
YSSKTLKTRD NELNEYNNYE NNNGKKVKVC IFSYAGSEGI SFKCINDIII LDMPWNESEL 

       490        500        510        520        530        540 
KQIIGRSIRL NSHKDLPQEY RYVNVHFLIS YTNNRKSVDK EILDIIKDKQ GKINVIFDLL 

       550        560        570        580        590        600 
KSSSIESIHN TYKYIEPAEN EIIFDTIRKT RMKEMNVSNV IINIKLYPIS YCKDYDRATI 

       610        620        630        640 
LKGLLNKDTN IVYKDNTAVA KLMIDKDNIP IFIIENDTLI YIADDYYE

P29814 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