ID   NTP1_MYXVL              Reviewed;         632 AA.
AC   Q9Q8L4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Nucleoside triphosphatase I;
DE            EC=3.6.1.15;
DE   AltName: Full=M86L protein;
DE   AltName: Full=NPH-I;
DE   AltName: Full=Nucleoside triphosphate phosphohydrolase I;
DE            Short=NPH I;
GN   Name=NPH1; OrderedLocusNames=m086L;
OS   Myxoma virus (strain Lausanne) (MYXV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
OX   NCBI_TaxID=31530;
OH   NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10562494; DOI=10.1006/viro.1999.0001;
RA   Cameron C., Hota-Mitchell S., Chen L., Barrett J.W., Cao J.-X.,
RA   Macaulay C., Willer D.O., Evans D.H., McFadden G.;
RT   "The complete DNA sequence of myxoma virus.";
RL   Virology 264:298-318(1999).
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; AF170726; AAF14974.1; -; Genomic_DNA.
DR   RefSeq; NP_051800.1; NC_001132.2.
DR   SMR; Q9Q8L4; -.
DR   GeneID; 932112; -.
DR   KEGG; vg:932112; -.
DR   Proteomes; UP000000867; 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_0000099095"
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"
SQ   SEQUENCE   632 AA;  72623 MW;  9EED5BF143FAC0CD CRC64;
     MSVYHAAYID YALRVTENMT DVMTGSETVT LKSYQHFVSR VFLGLDKMHS LLLFHETGVG
     KTITTVFILK HLKDVYTNWI IILLVKKALV EDPWTYAITK YAPEILKDCI FITYDDKNFH
     NKFFTNIKTI SSRTRLCIII DECHNFISKS IIKEDGKQRP TKSVYNYLSK NVALHHHKLI
     CLSATPIVNS VKEFVMLVNL LRPKILSNVS LFENKRLVNE SELINKLGAI CSYIVTNEFS
     IFDDVAGSSA FARKTVYFQY VNMTQKQEQV YQKAKLAELK AGISSFRIYR RMAATFTFDA
     FLDKTDKTPE EVANEQITLY KDFETFIKTK KFSEHALSQF KRGQSLGGTS SADDISFLNE
     LRERSCKFTD VCLRILASPG KCLVFEPFVN QSGINILLLY FSAFNISYIE FSSRTKNTRV
     QSVAEFNKRE NTDGDLIKTC VFSLSGGEGI SFFSINDIFI LDMTWNEASL RQIIGRAIRL
     NSHVLTPEHR RYVNVHFIVA RLSNGDATVD EDLLDIIRTK SKEFTQLFKV FKHTSIEWIY
     EHQTDFSPVD NESGWSALIS RSIDENPTTK RVPHVVKGQN IWYSHSNRLI AVYKGFKTDD
     GRLFDSDGNF IQTIQDNPVI KIHNDKLVYV LD