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   03-AUG-2022, entry version 91.
DE   RecName: Full=Nucleoside triphosphatase I;
DE            EC=3.6.1.15;
DE   AltName: Full=NPH-I;
DE   AltName: Full=Nucleoside triphosphate phosphohydrolase I;
DE            Short=NPH I;
GN   Name=NPH1; OrderedLocusNames=MSV053;
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: DNA-dependent ATPase required for providing the needed energy
CC       to achieve the termination of early transcripts. Acts in concert with
CC       the RAP94 subunit of the virion RNA polymerase and the capping
CC       enzyme/VTF to catalyze release of UUUUUNU-containing nascent RNA from
CC       the elongation complex. NPH-I must bind ssDNA in order to exhibit
CC       ATPase activity (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC   -!- SUBUNIT: Monomer. Interacts (via C-terminus) with RAP94 (via N-
CC       terminus). Interacts with the cap-specific mRNA (nucleoside-2'-O-)-
CC       methyltransferase (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Virion core enzyme.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. NPH I subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF063866; AAC97824.1; -; Genomic_DNA.
DR   PIR; T28214; T28214.
DR   RefSeq; NP_048124.1; NC_001993.1.
DR   SMR; Q9YW39; -.
DR   GeneID; 1449819; -.
DR   KEGG; vg:1449819; -.
DR   Proteomes; UP000172353; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR013676; NPHI_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08469; NPHI_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA-binding; Hydrolase; Nucleotide-binding;
KW   Reference proteome; Transcription; Virion.
FT   CHAIN           1..647
FT                   /note="Nucleoside triphosphatase I"
FT                   /id="PRO_0000099103"
FT   DOMAIN          48..213
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          377..540
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          466..532
FT                   /note="Binding to the cap-specific mRNA (nucleoside-2'-O-)-
FT                   methyltransferase"
FT                   /evidence="ECO:0000250"
FT   MOTIF           150..153
FT                   /note="DEXH box"
FT   BINDING         61..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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