ID   NTP1_VACCA              Reviewed;         631 AA.
AC   O57214; Q6J3C2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Nucleoside triphosphatase I;
DE            EC=3.6.1.15;
DE   AltName: Full=Factor X;
DE   AltName: Full=Nucleoside triphosphate phosphohydrolase I;
DE            Short=NPH I;
GN   Name=NPH1; OrderedLocusNames=MVA108L, ACAM3000_MVA_108;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J.,
RA   Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serves two roles in transcription; it acts in concert with
CC       viral termination factor/capping enzyme to catalyze release of UUUUUNU-
CC       containing nascent RNA from the elongation complex, and it acts by
CC       itself as a polymerase elongation factor to facilitate readthrough of
CC       intrinsic pause sites.
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.
CC   -!- SIMILARITY: Belongs to the helicase family. NPH I subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U94848; AAB96451.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10506.1; -; Genomic_DNA.
DR   PIR; T37384; T37384.
DR   SMR; O57214; -.
DR   Proteomes; UP000159908; Genome.
DR   Proteomes; UP000172909; 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: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; Hydrolase; Late protein; Nucleotide-binding; Transcription.
FT   CHAIN           1..631
FT                   /note="Nucleoside triphosphatase I"
FT                   /id="PRO_0000099090"
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   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;  72381 MW;  E7FE68BA105A1A35 CRC64;
     MSKSHAAYID YALRRTTNMP VEMMGTDVVR LKDYQHFVAR VFLGLDSMHS LLLFHETGVG
     KTMTTVYILK HLKDIYTNWA IILLVKKALI EDPWMNTILR YAPEITKDCI FINYDDQNFR
     NKFFTNIKTI NSKSRICVII DECHNFISKS LIKEDGKIRP TRSVYNFLSK TIALKNHKMI
     CLSATPIVNS VQEFTMLVNL LRPGSLQHQS LFENKRLVDE KELVSKLGGL CSYIVNNEFS
     IFDDVEGSAS FAKKTVLMRY VNMSKKQEEI YQKAKLAEIK TGISSFRILR RMATTFTFDS
     FPERQNRDPG EYAQEIATLY NDFKNSLRDR EFSKSALDTF KKGELLKGDA SAADISLFTE
     LKEKSVKFID 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