ID   NTP1_FOWPN              Reviewed;         637 AA.
AC   O72907;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=FPV052; ORFNames=FP-D11, FPD11;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FP-9 / Isolate HP-440;
RA   Skinner M.A.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2177083; DOI=10.1099/0022-1317-71-12-2873;
RA   Binns M.M., Britton B.S., Mason C., Boursnell M.E.G.;
RT   "Analysis of the fowlpox virus genome region corresponding to the vaccinia
RT   virus D6 to A1 region: location of, and variation in, non-essential genes
RT   in poxviruses.";
RL   J. Gen. Virol. 71:2873-2881(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(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 (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; AJ005163; CAA06401.1; -; Genomic_DNA.
DR   EMBL; AF198100; AAF44396.1; -; Genomic_DNA.
DR   PIR; S42251; S42251.
DR   RefSeq; NP_039015.1; NC_002188.1.
DR   SMR; O72907; -.
DR   GeneID; 1486600; -.
DR   KEGG; vg:1486600; -.
DR   Proteomes; UP000008597; 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..637
FT                   /note="Nucleoside triphosphatase I"
FT                   /id="PRO_0000099094"
FT   DOMAIN          43..205
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          358..537
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          459..526
FT                   /note="Binding to the cap-specific mRNA (nucleoside-2'-O-)-
FT                   methyltransferase"
FT                   /evidence="ECO:0000250"
FT   MOTIF           142..145
FT                   /note="DEXH box"
FT   BINDING         56..63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   637 AA;  73774 MW;  9F838D2E0519F0D8 CRC64;
     MNTYAAYIDY ALKKLDTFPV DMTGGNDNTV LLKDYQLFVA KVFLGLNSMN SILLFQETGV
     GKTITTVYML KNLKKIYSEW TIIILVKKAL IDDPWTHTIL DYAPEVMKDC IIMNYDDQNF
     HNKFFTNIKS INVKSRIFII IDECHNFISK SLTKEDNKKR NTKLVYNYIA KNLMQKNNKL
     ICLSATPIVN DVREFQMLVN LLRPGILTPD KSLFYNKKLI DEKEIISKLG CICSYIVNNE
     ASIFEDVENT TLFAKKTVHI KHVFMSKKQE ELYLKARYLE RKLGISVFKI YQRMASTFVF
     DDIPDKKKLT EEEYEKFVDS LSIDFKNTLY GKKISKQSLD ILSAGGTIND IKDVKDIELY
     NYLYEHSCKF TFVCVSIIQS KGKCLVFEPF IRSSGIEILL QYFNVFGITY IEFSSRTKDI
     RSKSVSDFNK VDNTDGEITK VCVFSQSGNE GISFLSINDI FILDMTWNEA SLKQIIGRAI
     RLNSHVNNPP ERRYVNVYFV VAKLSSGRSS VDDILLDIIQ SKSKEFSQLY KVFKHSSIEW
     IYSNYTDFQT VDDEKGFKKL ISRNIILDEN TITNKKKLTM GENIWYSFSS SLVSIHRGFK
     SMDNKIYDSE GFFITVLPDK PTIKIYEGKL IYILTVR