ID   NTP1_VARV               Reviewed;         631 AA.
AC   P0DOQ4; P33066; Q9QNI4;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   03-AUG-2022, entry version 16.
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=D11L, N1L;
OS   Variola virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10255;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangladesh-1975;
RX   PubMed=8264798; DOI=10.1038/366748a0;
RA   Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA   Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA   Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT   "Potential virulence determinants in terminal regions of variola smallpox
RT   virus genome.";
RL   Nature 366:748-751(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Garcia-1966;
RX   PubMed=10639322; DOI=10.1006/viro.1999.0086;
RA   Shchelkunov S.N., Totmenin A.V., Loparev V.N., Safronov P.F., Gutorov V.V.,
RA   Chizhikov V.E., Knight J.C., Parsons J.M., Massung R.F., Esposito J.J.;
RT   "Alastrim smallpox variola minor virus genome DNA sequences.";
RL   Virology 266:361-386(2000).
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 J3 (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; L22579; AAA60849.1; -; Genomic_DNA.
DR   EMBL; Y16780; CAB54701.1; -; Genomic_DNA.
DR   PIR; T28539; T28539.
DR   RefSeq; NP_042145.1; NC_001611.1.
DR   SMR; P0DOQ4; -.
DR   GeneID; 1486475; -.
DR   KEGG; vg:1486475; -.
DR   Proteomes; UP000111493; Genome.
DR   Proteomes; UP000119805; 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; Late protein; Nucleotide-binding;
KW   Transcription; Virion.
FT   CHAIN           1..631
FT                   /note="Nucleoside triphosphatase I"
FT                   /id="PRO_0000448133"
FT   DOMAIN          42..204
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          367..532
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          457..524
FT                   /note="Binding to the cap-specific mRNA (nucleoside-2'-O-)-
FT                   methyltransferase"
FT                   /evidence="ECO:0000250"
FT   MOTIF           141..144
FT                   /note="DEXH box"
FT   BINDING         55..62
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   VARIANT         331
FT                   /note="E -> K (in strain: Garcia-1966)"
FT   VARIANT         577
FT                   /note="E -> K (in strain: Garcia-1966)"
SQ   SEQUENCE   631 AA;  72353 MW;  7C0BC2F82B534925 CRC64;
     MSKSHAAYID YALRRTTNMP VEMMGTDVVR LKDYQHFVAR VFLGLDSMHS LLLFHETGVG
     KTMTTVYILK HLKDIYTNWA IILLVKKALI EDPWMNTILR YAPEITKDCI FINYDDQNFR
     NKFFTNIKTI NSKSRICVII DECHNFISKS LIKEDGKIRP TRSVYNFLSK TIALKNHKMI
     CLSATPIVNS VQEFTMLVNL LRPGSLQHQS LFENKRLVNE KELVSKLGGL CSYIVNNEFS
     IFDDVEGSAS FAKKTVLMRY VNMSKKQEEI YQKAKLTEIK TGISSFRILR RMATTFTFDS
     FPERQNRDPG EYAQEIATLY NDFKRSLRDR EFSKSALDTF KKGELLGGDA SAADISLFTE
     LKEKSAKFID VCLGILASHG KCLVFEPFVN QSGIEILLLY FKVFGISNIE FSSRTKDTRI
     KAVAEFNQES NTNGECIKTC VFSSSGGEGI SFFSINDIFI LDMTWNEASL RQIVGRAIRL
     NSHVLTPPER RYVNVHFIMA RLSNGMPTVD EDLFEIIQSK SKEFVQLFRV FKHTSLEWIH
     ANEKDFSPID NESGWKTLVS RAIDLSSKKN ITNKLIEGTN IWYSNSNRLM SINRGFKGVD
     GRVYDVDGNY LHDMPDNPVI KIHDGKLIYI F