ID   NPH2_MSEPV              Reviewed;         717 AA.
AC   Q9YW06;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=RNA helicase NPH-II;
DE            EC=3.6.4.13;
DE   AltName: Full=Nucleoside triphosphatase II;
DE            Short=NTPase II;
DE   AltName: Full=Nucleoside triphosphate phosphohydrolase II;
DE            Short=NPH II;
GN   Name=NPH2; OrderedLocusNames=MSV086;
OS   Melanoplus sanguinipes entomopoxvirus (MsEPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Entomopoxvirinae; Deltaentomopoxvirus.
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   PubMed=9847359; DOI=10.1128/jvi.73.1.533-552.1999;
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: NTP-dependent helicase that catalyzes unidirectional
CC       unwinding of 3'tailed duplex RNAs and plays an important role during
CC       transcription of early mRNAs, presumably by preventing R-loop formation
CC       behind the elongating RNA polymerase. Might also play a role in the
CC       export of newly synthesized mRNA chains out of the core into the
CC       cytoplasm. Required for replication and propagation of viral particles
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Virion. Note=Localizes to the virion core.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF063866; AAC97810.1; -; Genomic_DNA.
DR   PIR; T28247; T28247.
DR   RefSeq; NP_048157.1; NC_001993.1.
DR   SMR; Q9YW06; -.
DR   GeneID; 1449805; -.
DR   KEGG; vg:1449805; -.
DR   Proteomes; UP000172353; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR021892; NPH-II.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF12011; NPH-II; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
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; Reference proteome;
KW   Transcription; Virion.
FT   CHAIN           1..717
FT                   /note="RNA helicase NPH-II"
FT                   /id="PRO_0000055189"
FT   DOMAIN          193..384
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          406..566
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           331..334
FT                   /note="DEXH box"
FT   BINDING         206..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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