ID   NTP1_RFVKA              Reviewed;         632 AA.
AC   Q9Q8Z2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=s086L;
OS   Rabbit fibroma virus (strain Kasza) (RFV) (Shope fibroma virus (strain
OS   Kasza)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
OX   NCBI_TaxID=10272;
OH   NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10562495; DOI=10.1006/viro.1999.0002;
RA   Willer D.O., McFadden G., Evans D.H.;
RT   "The complete genome sequence of shope (Rabbit) fibroma virus.";
RL   Virology 264:319-343(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-632.
RX   PubMed=1329373; DOI=10.1016/0168-1702(92)90104-h;
RA   Strayer D.S., Jerng H.H.;
RT   "Sequence and analysis of the BamHI 'D' fragment of Shope fibroma virus:
RT   comparison with similar regions of related poxviruses.";
RL   Virus Res. 25:117-132(1992).
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; AF170722; AAF17970.1; -; Genomic_DNA.
DR   RefSeq; NP_051975.1; NC_001266.1.
DR   SMR; Q9Q8Z2; -.
DR   PRIDE; Q9Q8Z2; -.
DR   GeneID; 1486931; -.
DR   KEGG; vg:1486931; -.
DR   Proteomes; UP000000868; 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..632
FT                   /note="Nucleoside triphosphatase I"
FT                   /id="PRO_0000099096"
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   CONFLICT        404
FT                   /note="F -> V (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        496
FT                   /note="H -> T (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   632 AA;  72883 MW;  2579BE4806A92F06 CRC64;
     MSVHHAAYID YALRVTENMT DVMTGSDTVT LKSYQHFVSR VFLGLDKMHS LLLFHETGVG
     KTITTVFILK HLKDVYTNWI IILLVKKALV EDPWTYSITK YAPEILKDCI FITYDDKNFH
     NKFFTNIKTI SSRSRLCIII DECHNFISKS IVKEDGKQRP TKSVYNYLLK NVALHHHKLI
     CLSATPIVNS VKEFIMLVNL LRPKILNNIS LFENKRLINE SELINKLGAI CSYIVTNEFS
     IFDDVEGSAT FAKKNVYFQY VNMTQKQEQV YQKAKSAELK AGTSSFRIYR RMAATFTFDT
     FLDKTDKTPE EIVNEQVTLY KDFEKFIKTK KFSDHALSHF KKGQSLNGTS SADDISFLNE
     LREHSCKFTD VCLRILASPG KCLVFEPFVN QSGINILLLY FSAFNISYIE FSSRTKNTRV
     QSVAEFNKRE NTNGDLIKTC VFSLSGGEGI SFFSINDIFI LDMTWNEASL RQIIGRAIRL
     NSHVLTPEHR RYVYVHFIIA RLSNGDPTVD EDLLDIIRNK SKEFTQLFKV FKHTSIEWIY
     EHQTNFSPVD DESGWGALIS RSIDENPTTK RVPRIARGQN IWYSHSNRMI TVYKGFKTDD
     GRLFDSDGNF IQTIQANPVI KIHNNKLVYV LD