ID   NTP1_CBEPV              Reviewed;         648 AA.
AC   P24486;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 89.
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;
OS   Choristoneura biennis entomopoxvirus (CbEPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Entomopoxvirinae; Betaentomopoxvirus.
OX   NCBI_TaxID=10288;
OH   NCBI_TaxID=7141; Choristoneura fumiferana (Spruce budworm moth) (Archips fumiferana).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1850911; DOI=10.1016/0042-6822(91)90690-d;
RA   Yuen L., Noiseux M., Gomes M.;
RT   "DNA sequence of the nucleoside triphosphate phosphohydrolase I (NPH I) of
RT   the Choristoneura biennis entomopoxvirus.";
RL   Virology 182:403-406(1991).
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; M60400; AAA42886.1; -; Genomic_DNA.
DR   PIR; A39154; NPVZCP.
DR   SMR; P24486; -.
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..648
FT                   /note="Nucleoside triphosphatase I"
FT                   /id="PRO_0000099100"
FT   DOMAIN          48..213
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          379..542
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          468..534
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   648 AA;  76116 MW;  C61BA6EA5D36F892 CRC64;
     MFALDSIVGK HINYALDKTQ HLPNKINNSI TNTEITLQDY QYFASRIFIG LKNLNSMLLF
     WDTGTGKTLT AVYIIKYIKE LFPRWIILIF IKKSLYIDPW LNTISSYISD TSNIKFIYYD
     STSSLDKKFN NIYRSIESSL NKKNRLLIII DEVHKLISRS VKKDNNERNF TPIYRKLIKL
     ANYENNKILC MSATPITNNI AEFNNLIGLL RPNVMNIKEE YINNGKLINF KEVRETLLGI
     CSYKRLIEAD SLTDTNYIDG YAKKSIFYHN IIMSDEQSKL YNMAERYDYK TELGGLKTMR
     RLISSFAFYD LKIKGDLDNV EYNEMIKRKL AEFSEFTKNI NFSKAFINAF KNNEIKSKTD
     LLITDINNYN ILYQYSCKYI EACRIILNSR GKVLLFEPLV NFEGISSLKY YFNCFNISYI
     EYSSKTIKMR DNDLNEYNNY ENNDGNKIKV CIFSYAGSEG ISFKCINDII ILDMPWNESE
     LKQIIGRSIR LNSHEYLPIN YRYVNVHFII SYSNNRKSVD KEMLDIIKNK QGKINVVFDL
     LKASSIETIH NMHKYIEPVD NEIIFEIIRK TRMKEMNISN VIINLKLYPI TYCKDYDRAT
     ILKGFLNKDT NIIYDNDTPV AKLIVDNNNL PIFVIENDIL IYITNDYY