ID   NTP1_MSEPV              Reviewed;         647 AA.
AC   Q9YW39;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-NOV-2008, entry version 43.
DE   RecName: Full=Nucleoside triphosphatase I;
DE            EC=3.6.1.15;
DE   AltName: Full=Nucleoside triphosphate phosphohydrolase I;
DE            Short=NPH I;
GN   Name=NPH1; OrderedLocusNames=MSV053;
OS   Melanoplus sanguinipes entomopoxvirus (MsEPV).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Entomopoxvirinae.
OX   NCBI_TaxID=83191;
OH   NCBI_TaxID=65742; Melanoplus sanguinipes (Migratory grasshopper).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Tucson;
RX   MEDLINE=99102612; PubMed=9847359;
RA   Afonso C.L., Tulman E.R., Lu Z., Oma E., Kutish G.F., Rock D.L.;
RT   "The genome of Melanoplus sanguinipes entomopoxvirus.";
RL   J. Virol. 73:533-552(1999).
CC   -!- FUNCTION: Serves two roles in transcription; it acts in concert
CC       with viral termination factor/capping enzyme to catalyze release
CC       of UUUUUNU-containing nascent RNA from the elongation complex, and
CC       it acts by itself as a polymerase elongation factor to facilitate
CC       readthrough of intrinsic pause sites (By similarity).
CC   -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
CC   -!- SIMILARITY: Belongs to the helicase family. NPH I subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR   EMBL; AF063866; AAC97824.1; -; Genomic_DNA.
DR   PIR; T28214; T28214.
DR   RefSeq; NP_048124.1; -.
DR   GeneID; 1449819; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR001650; DNA/RNA_helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR013676; NPHI_C.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08469; NPHI_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Nucleotide-binding; Transcription.
FT   CHAIN         1    647       Nucleoside triphosphatase I.
FT                                /FTId=PRO_0000099103.
FT   DOMAIN       48    213       Helicase ATP-binding.
FT   DOMAIN      377    540       Helicase C-terminal.
FT   NP_BIND      61     68       ATP (By similarity).
FT   MOTIF       150    153       DEXH box.
SQ   SEQUENCE   647 AA;  75135 MW;  E78C7F768235D51D CRC64;
     MHSIEHIVAR HFNYALEKTK DLPKSINNEI TNEIIILKDY QYLVSRIFIG LSELNSLLLF
     WDTGYGKTLT SVYIMKHLKL VFPQWFFVIF IKKSLYVDPW LNTLSKLGMK GQNIKFVLYD
     SSSSLKQFNV LYRTIISSIN TKNRILIIID EVHQVISRTI EKSSSTQRNF LSIFNKIVKL
     ANSENNKLLC MSATPITNNV LEFKYLINLL RPKIIEFKED FIVNNTLKNH EQLKNGLISI
     TSYQKISEAD SFTNTSYTEG FASKNIFYHN VTMTPEQSNI FNIADKHDKK SALGGLKTMR
     RLVSSFAFYD IKIKGSMSQI EYNKMVSEKL NEFKSIIGNF KFSNEFIDIF RNNDSFSNAK
     SSEIEIFDKI KQYSCKYIEA CKIILNSNGK VLLYEPLVSF EGISTLKIYF NIFNISYVEY
     SSKTESTRDY NIDIFNKYDN LYGNKIKVCI FSAAGSEGIS FSSINDIIIL DLPWKESDIK
     QIIGRSIRLN SHEELPIEKR YVNVHFIIAS TIDGKSVDKE IFDLIKSKQD KINVLNSFMK
     VISIEQIHSK YKYAEPVENE YIFNNIRHTK IDDVNENNVI TKIIVSPIYY CSEDNLNIIY
     NGYLDKKTGI IYSNNIPIAK LILDENNIYK FFIKDDKLVY ITKSIYE
//