ID   NTP1_CFEPV              Reviewed;         647 AA.
AC   O91729;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 80.
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 fumiferana entomopoxvirus (CfEPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Entomopoxvirinae; Betaentomopoxvirus.
OX   NCBI_TaxID=28322;
OH   NCBI_TaxID=7141; Choristoneura fumiferana (Spruce budworm moth) (Archips fumiferana).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9784068; DOI=10.1016/s0168-1702(98)00061-6;
RA   Li X., Wallis J.L., Barrett J.W., Krell P.J., Arif B.M.;
RT   "Characterization of the nucleoside triphosphate phosphohydrolase I gene
RT   from the Choristoneura fumiferana entomopoxvirus.";
RL   Virus Res. 56:93-105(1998).
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; AF027657; AAC63435.1; -; Genomic_DNA.
DR   SMR; O91729; -.
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..647
FT                   /note="Nucleoside triphosphatase I"
FT                   /id="PRO_0000099101"
FT   DOMAIN          48..212
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          378..541
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          467..533
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;  76048 MW;  430815EC765CD1FD CRC64;
     MFALDSIVGK HINYALDKTQ HLPNKINNSI TNTEIILQDY QYFASRIFIG LKNLNSMLLF
     WDTGTGKTLT AVYIIKYIKE LFPRWIILIF IKKSLYVDPW LNTISSYISD TSNIKFIYYD
     STSSLDKFNN IYRSIESSLN KKNRLLIIID EVHKLISRSV KKDNSERNFT PIYRKLIKLA
     NYENNKILCM SATPITNNIA EFNNLIGLLR PNVMNIKEEY INNGKLINFK EIRETLLGIC
     SYKRLIEADS LTDTNYIDGY AKKSIFYHNI IMSDEQSKLY NMAERYDYKT ELGGLKTMRR
     LISSFAFYDL KIKGDLDNVE YNEMIKRKLA EFSEFTKNIN FSKEFINAFK NNEIKTKTDL
     LITDINNYNI LYQYSCKYIE ACRIILNSRG KVLLFEPLVN FEGISSLKYY FNCFNISYIE
     YSSKTIKMRD NDLNYYNNYE NNDGNKIKVC IFSYAGSEGI SFKCINDIII LDMPWNESEL
     KQIIGRSIRL NSHEYLPINY RYVNVHFIIS YSNNRKSVDK EILDIIKNKQ GKINVVFDLL
     KASPIEIIHN MYKYIEPVDN EIIFETIRKT RMKEMNISNV IINLKLYPIT YCKDYDRATI
     LKGLLNKDTN IIYDNDTPVA ILLVDNNNLP IFVIENDILI YITNDYY