ID   NTP1_YMTV5              Reviewed;         631 AA.
AC   Q9QB93;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=88L; ORFNames=B5L;
OS   Yaba monkey tumor virus (strain VR587) (YMTV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Yatapoxvirus.
OX   NCBI_TaxID=928314;
OH   NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9539; Macaca (macaques).
OH   NCBI_TaxID=9557; Papio hamadryas (Hamadryas baboon).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14645589; DOI=10.1128/jvi.77.24.13335-13347.2003;
RA   Brunetti C.R., Amano H., Ueda Y., Qin J., Miyamura T., Suzuki T., Li X.,
RA   Barrett J.W., McFadden G.;
RT   "Complete genomic sequence and comparative analysis of the tumorigenic
RT   poxvirus Yaba monkey tumor virus.";
RL   J. Virol. 77:13335-13347(2003).
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; AY386371; AAR07444.1; -; Genomic_DNA.
DR   RefSeq; NP_938343.1; NC_005179.1.
DR   SMR; Q9QB93; -.
DR   GeneID; 2943701; -.
DR   KEGG; vg:2943701; -.
DR   Proteomes; UP000008596; 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; Nucleotide-binding;
KW   Reference proteome; Transcription; Virion.
FT   CHAIN           1..631
FT                   /note="Nucleoside triphosphatase I"
FT                   /id="PRO_0000099098"
FT   DOMAIN          42..204
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          367..536
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"
SQ   SEQUENCE   631 AA;  72579 MW;  06561CA08C729EFF CRC64;
     MSRQHAAYID YALNRMKKMP IEMLGSDTIT LKPYQHFVAK VFLGLDTMHS ILLFHDTGVG
     KTITTVFILK HLKDIYTNWT ILLLVKKALV EDPWMNTILK YSPEIIKNCI FINYDDKNFH
     NKFFTNIKTI SSRSRVCVVL DECHNFISKS LIKEDGKQRP TKSVYNYLSK NISLNNNKMI
     CLSATPIVNN VREFTMIVNL LRPKIIQFQS LFENKNLVNE KELIDKLGGI CSYIVNDEFS
     IFDDVEGSQS FAKKTVYMHY VNMTKQQEII YQKAKIAEIK SGIASFRIYR RMAATFSFDS
     FPDKKKKTID EITLELGALY KDFVNYVNKK SFSNNAIKLF KSGKGLTGDS NPLDISLLSE
     LRQKSCKFTE VCLKILASPG KCLVFEPFIN QSGIEVLLVY FSVFCITSVE FSSRTKDTRI
     KNVFEFNKES NTNGEQIKVC VFSISGGEGI SFFSINDIFI LDMTWNEASL KQIVGRAIRL
     NSHANTPPNR RYVNVYFIIA RLSSGEPTVD EDLINIIKTK SKEFFQLFKV FKESSIEWIY
     KNKKDFYPIN DESGWRALTS RVVDVNVKSK RTVQLAQGQN IWFSNSSRMV TIHKGFKTSD
     GKIFDVDGNF IQNMPINPII KIHNDKLVYI I