ID   NTP1_HAEPV              Reviewed;         646 AA.
AC   O37319;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 82.
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; ORFNames=F1L;
OS   Heliothis armigera entomopoxvirus (HaEPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Entomopoxvirinae; Betaentomopoxvirus.
OX   NCBI_TaxID=10290;
OH   NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9400959; DOI=10.1099/0022-1317-78-12-3115;
RA   Sriskantha A., Osborne R.J., Dall D.J.;
RT   "Mapping of the Heliothis armigera entomopoxvirus (HaEPV) genome, and
RT   analysis of genes encoding the HaEPV spheroidin and nucleoside triphosphate
RT   phosphohydrolase I proteins.";
RL   J. Gen. Virol. 78:3115-3123(1997).
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; AF019224; AAB96624.1; -; Genomic_DNA.
DR   SMR; O37319; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR013676; NPHI_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08469; NPHI_C; 1.
DR   Pfam; PF04851; ResIII; 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; Transcription;
KW   Virion.
FT   CHAIN           1..646
FT                   /note="Nucleoside triphosphatase I"
FT                   /id="PRO_0000099102"
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           151..154
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   646 AA;  75763 MW;  AA1B63287F8B8034 CRC64;
     MFTLDSIVGA HINYALDKTA HLPETITNNV SNVEITLKDY QYFVSRVFIG LKNLNSMLLF
     WDTGMGKTLT AVYIIKHIKE LFPRWIILIF IKKSLYIDPW LNTIRAFAPD ISNNIIFVYY
     DSSSSLDKFV NIYRSIENSL NKKNRLLIII DEVHKLISRS VKKDNSERNF TPTYKKLIKL
     ANYEGNKILC MSATPIYNNI DEFNNLIGLL RPNVMTFKEE YIINGKLINF KEIRDTLLGL
     CSYKRLIEAD SFTETNYVEG YAKKNVIYHN IIMSEEQSKL FNLAEKYDYK TELGGLKTMR
     RLVSSFAFYD LKIKGDLNNI EYNDMIKRKL AEFSEFTKTI NFSNNFIEKF KRDDLKNDIL
     LEDINNYNIL YQYSCKYIEA CRIILNSRGK VLLFEPLVNF EGIASLKYYF NCFNITYVEY
     SSKTLKTRDI EISEYNNYEN NDGKNIKVCI FSYAGSEGIS FKCVNDIIIL DMPWNESELK
     QIMGRSIRLN SHNDLPLENR YVNVHFIISY TNNRKSVDKE ILDIIKDKQS KINVVFDLLK
     SISIESIHNI HKYIEPVESE TIFDTIRKTR MREMNISNVI VKIKLYPIMY CKDYDRATIL
     KGLLNKENNI IYNEDTAVAK LTIENNKPVF IIVDDNLIYI ADDYYE