ID   NTP2_MSEPV              Reviewed;         717 AA.
AC   Q9YW06;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-NOV-2008, entry version 47.
DE   RecName: Full=Nucleoside triphosphatase II;
DE            Short=NTPase II;
DE            EC=3.6.1.15;
DE   AltName: Full=Nucleoside triphosphate phosphohydrolase II;
DE            Short=NPH II;
GN   Name=NPH2; OrderedLocusNames=MSV086;
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: Essential for viral replication. Plays an important role
CC       during transcription of early mRNAs, presumably by preventing R-
CC       loop formation behind the elongating RNA polymerase. Acts as NTP-
CC       dependent helicase that catalyzes unidirectional unwinding of
CC       3'tailed duplex RNAs. Might also play a role in the export of
CC       newly synthesized mRNA chains out of the core into the cytoplasm.
CC       Required for propagation of viral particles (By similarity).
CC   -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR   EMBL; AF063866; AAC97810.1; -; Genomic_DNA.
DR   PIR; T28247; T28247.
DR   RefSeq; NP_048157.1; -.
DR   GeneID; 1449805; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; AAA+_ATPase_core.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR001650; DNA/RNA_helicase_C.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; FALSE_NEG.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Transcription.
FT   CHAIN         1    717       Nucleoside triphosphatase II.
FT                                /FTId=PRO_0000055189.
FT   DOMAIN      193    384       Helicase ATP-binding.
FT   DOMAIN      406    566       Helicase C-terminal.
FT   NP_BIND     206    213       ATP (By similarity).
FT   MOTIF       331    334       DEXH box.
SQ   SEQUENCE   717 AA;  84726 MW;  E8FB04661F1EA863 CRC64;
     MDMQNITDLY KIDKKTTLYP NIINKYNYMA YLLFPNNATI FNSYITKKEV FEYPMQFAIA
     LYPVYKLYWH NINICLNNRF IYLSNEFKNN ISINTVYNLL YNNELKFEDD NIIINGKNLK
     ISYSAYSYVT IISQITINIS SLNKYQIYGI IESANYLGIL SSYKQNKYFD KNLFSFTKSE
     LRSTMIDVQL KIFEIFISKK NCIISGGTGI GKTTVIPKLF WWFNLLFDGY EFWNTSNENK
     NINDFIFKPN FEKNKTILSL PRKALIRQMG INYIKSLGFD NISGSPIILK YKDVKKEKEY
     YNNNPILYPF VLSVNRITIN NIKHSNSVII DEIHEHDKFG DIAIAIARTK KKKYNIRNIV
     LISATIESDI DNIRIYFKNI VEIYIPGVSL FPVKEIECED KDVISILKNY MPSVGKSVII
     FYETIKKINE YKEILESILI DKIYKIYTIH SKITNINAII NKLQNDKKHI HIILSTNYLE
     SSITITNATL VIDNGKMYQK KFLTGSTMYI TESMYIQRKG RVGRISKGTY IRTYSKDLLQ
     TTFKHINYQY LWEYILVFKY NNMDYYNDLF IKPDDPSRIE NTLNYLKNIN IDIDKYISLL
     YSKFNKYEIN MVEYLSIYIN NSTSDIILLN EFIDNIRNSD KYIFPYRLTE IFHKLNVRCR
     CINITETEEG NINCSFVILN NYDGDPFFKL SFEKSNLICR YNKIYYIVSM SPLYLID
//