ID   NTP1_AMEPV              Reviewed;         648 AA.
AC   P29814;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 92.
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=AMV192; ORFNames=G6;
OS   Amsacta moorei entomopoxvirus (AmEPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Entomopoxvirinae; Betaentomopoxvirus.
OX   NCBI_TaxID=28321;
OH   NCBI_TaxID=340055; Amsacta.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10936094; DOI=10.1006/viro.2000.0449;
RA   Bawden A.L., Glassberg K.J., Diggans J., Shaw R., Farmerie W., Moyer R.W.;
RT   "Complete genomic sequence of the Amsacta moorei entomopoxvirus: analysis
RT   and comparison with other poxviruses.";
RL   Virology 274:120-139(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-486.
RX   PubMed=8517016; DOI=10.1006/viro.1993.1020;
RA   Hall R.L., Moyer R.W.;
RT   "Identification of an Amsacta spheroidin-like protein within the occlusion
RT   bodies of Choristoneura entomopoxviruses.";
RL   Virology 192:179-187(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 486-648.
RX   PubMed=1942245; DOI=10.1128/jvi.65.12.6516-6527.1991;
RA   Hall R.L., Moyer R.W.;
RT   "Identification, cloning, and sequencing of a fragment of Amsacta moorei
RT   entomopoxvirus DNA containing the spheroidin gene and three vaccinia virus-
RT   related open reading frames.";
RL   J. Virol. 65:6516-6527(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; AF250284; AAG02898.1; -; Genomic_DNA.
DR   EMBL; M77182; AAA42384.1; -; Genomic_DNA.
DR   PIR; F41561; NPVZAM.
DR   RefSeq; NP_064974.1; NC_002520.1.
DR   SMR; P29814; -.
DR   GeneID; 1494782; -.
DR   KEGG; vg:1494782; -.
DR   Proteomes; UP000000872; Genome.
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;
KW   Reference proteome; Transcription; Virion.
FT   CHAIN           1..648
FT                   /note="Nucleoside triphosphatase I"
FT                   /id="PRO_0000099099"
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   648 AA;  76109 MW;  25BE863C0B8728AA CRC64;
     MFALDSIVGK HINYALDKTQ HLPNKIMNNI TNTEITLQDY QYFVSRIFIG LKNLNSMLLF
     WDTGMGKTLT AVYIIKYIKE LFPRWIILIF IKKSLYIDPW LNTIRSYISD TSNIKFIYYD
     SSSSLDKFNN IYRSIESSLN KKSRLLIIID EVHKLISRTV KKDNNERNFT PIYKKLIKLA
     NFENNKILCM SATPVTNNIS EFNNLIGLLR PNVMNIKEEY INNGKLINFK ELRETLLAIC
     SYKRLIEADS LTETNYIDGY AKKNIFYHNI IMSDEQSKLY NMAEKYDYKT ELGGLKTMRR
     LISSFAFYDL KIKGDLDNIE YNDMIKRKLA EFSEFTKNIN FSESFIESFK NDNIKIKTNL
     PITDINNYNI LYQYSCKYIE TCKIILNSRG KVLIFEPLVN FEGISSLKCY FNCFNISYIE
     YSSKTLKTRD NELNEYNNYE NNNGKKVKVC IFSYAGSEGI SFKCINDIII LDMPWNESEL
     KQIIGRSIRL NSHKDLPQEY RYVNVHFLIS YTNNRKSVDK EILDIIKDKQ GKINVIFDLL
     KSSSIESIHN TYKYIEPAEN EIIFDTIRKT RMKEMNVSNV IINIKLYPIS YCKDYDRATI
     LKGLLNKDTN IVYKDNTAVA KLMIDKDNIP IFIIENDTLI YIADDYYE