NTP1_VACCW
ID NTP1_VACCW Reviewed; 631 AA.
AC P05807; P04313; P04317; Q76ZR6; Q84138;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Nucleoside triphosphatase I;
DE EC=3.6.1.15;
DE AltName: Full=Factor X;
DE AltName: Full=NPH-I;
DE AltName: Full=Nucleoside triphosphate phosphohydrolase I;
DE Short=NPH I;
GN Name=NPH1; OrderedLocusNames=VACWR116; ORFNames=D11L;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3025846; DOI=10.1073/pnas.83.24.9566;
RA Rodriguez J.F., Kahn J.S., Esteban M.;
RT "Molecular cloning, encoding sequence, and expression of vaccinia virus
RT nucleic acid-dependent nucleoside triphosphatase gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9566-9570(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3739227; DOI=10.1016/0042-6822(86)90011-5;
RA Niles E.G., Condit R.C., Caro P., Davidson K., Matusick L., Seto J.;
RT "Nucleotide sequence and genetic map of the 16-kb vaccinia virus HindIII D
RT fragment.";
RL Virology 153:96-112(1986).
RN [3]
RP SEQUENCE REVISION.
RA Niles E.G.;
RL Submitted (FEB-1988) to the PIR data bank.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-288.
RX PubMed=3008103; DOI=10.1093/nar/14.7.3003;
RA Weinrich S.L., Hruby D.E.;
RT "A tandemly-oriented late gene cluster within the vaccinia virus genome.";
RL Nucleic Acids Res. 14:3003-3016(1986).
RN [6]
RP CHARACTERIZATION, AND DNA-BINDING.
RX PubMed=9472022; DOI=10.1101/gad.12.4.538;
RA Deng L., Shuman S.;
RT "Vaccinia NPH-I, a DExH-box ATPase, is the energy coupling factor for mRNA
RT transcription termination.";
RL Genes Dev. 12:538-546(1998).
RN [7]
RP MUTAGENESIS OF LYS-61; THR-62; ASP-141; GLU-142; HIS-144; ASN-145; SER-183;
RP THR-185; GLN-472; ARG-476 AND ARG-479.
RX PubMed=9882335; DOI=10.1128/jvi.73.2.1302-1308.1999;
RA Martins A., Gross C.H., Shuman S.;
RT "Mutational analysis of vaccinia virus nucleoside triphosphate
RT phosphohydrolase I, a DNA-dependent ATPase of the DExH box family.";
RL J. Virol. 73:1302-1308(1999).
RN [8]
RP INTERACTION WITH RAP94.
RX PubMed=10833518; DOI=10.1074/jbc.m002250200;
RA Mohamed M.R., Niles E.G.;
RT "Interaction between nucleoside triphosphate phosphohydrolase I and the H4L
RT subunit of the viral RNA polymerase is required for vaccinia virus early
RT gene transcript release.";
RL J. Biol. Chem. 275:25798-25804(2000).
RN [9]
RP FUNCTION, AND INTERACTION WITH RAP94.
RX PubMed=11279216; DOI=10.1074/jbc.m101641200;
RA Mohamed M.R., Niles E.G.;
RT "The viral RNA polymerase H4L subunit is required for Vaccinia virus early
RT gene transcription termination.";
RL J. Biol. Chem. 276:20758-20765(2001).
RN [10]
RP INTERACTION WITH J3.
RX PubMed=11162828; DOI=10.1006/viro.2000.0749;
RA Mohamed M.R., Latner D.R., Condit R.C., Niles E.G.;
RT "Interaction between the J3R subunit of vaccinia virus poly(A) polymerase
RT and the H4L subunit of the viral RNA polymerase.";
RL Virology 280:143-152(2001).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=16474121; DOI=10.1128/jvi.80.5.2127-2140.2006;
RA Chung C.S., Chen C.H., Ho M.Y., Huang C.Y., Liao C.L., Chang W.;
RT "Vaccinia virus proteome: identification of proteins in vaccinia virus
RT intracellular mature virion particles.";
RL J. Virol. 80:2127-2140(2006).
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. {ECO:0000269|PubMed:11279216}.
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 J3. {ECO:0000269|PubMed:10833518,
CC ECO:0000269|PubMed:11162828, ECO:0000269|PubMed:11279216}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16474121}. Note=Virion
CC core enzyme.
CC -!- SIMILARITY: Belongs to the helicase family. NPH I subfamily.
CC {ECO:0000305}.
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DR EMBL; M14629; AAA48301.1; -; Genomic_DNA.
DR EMBL; M15058; AAA48267.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89395.1; -; Genomic_DNA.
DR EMBL; X03729; CAA27370.1; -; Genomic_DNA.
DR PIR; A94144; NPVZ17.
DR RefSeq; YP_232998.1; NC_006998.1.
DR SMR; P05807; -.
DR DNASU; 3707708; -.
DR GeneID; 3707708; -.
DR KEGG; vg:3707708; -.
DR BRENDA; 3.6.1.15; 6591.
DR Proteomes; UP000000344; 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 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Hydrolase; Late protein; Nucleotide-binding;
KW Reference proteome; Transcription; Virion.
FT CHAIN 1..631
FT /note="Nucleoside triphosphatase I"
FT /id="PRO_0000099092"
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 MOTIF 141..144
FT /note="DEXH box"
FT BINDING 55..62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 61
FT /note="K->A,R,Q: Almost complete loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 62
FT /note="T->A,V: Almost complete loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 62
FT /note="T->S: No loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 141
FT /note="D->A,N: Almost complete loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 141
FT /note="D->E: 50% loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 142
FT /note="E->A,D,Q: Almost complete loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 144
FT /note="H->A,D,N: Almost complete loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 144
FT /note="H->Q: 50% loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 145
FT /note="N->A,E: Almost complete loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 145
FT /note="N->D: 30% loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 145
FT /note="N->Q: No effect on ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 183
FT /note="S->A: 80% loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 185
FT /note="T->A: 50% loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 472
FT /note="Q->A,N: Almost complete loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 472
FT /note="Q->H: 80% loss of ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 476
FT /note="R->A,K: Loss ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
FT MUTAGEN 479
FT /note="R->A,K: Loss ATP hydrolysis."
FT /evidence="ECO:0000269|PubMed:9882335"
SQ SEQUENCE 631 AA; 72310 MW; 76DE4A45F0AF00D0 CRC64;
MSKSHAAYID YALRRTTNMP VEMMGSDVVR 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 KRGELLGGDA SAADISLFTE
LKEKSVKFID VCLGILASHG KCLVFEPFVN QSGIEILLLY FKVFGISNIE FSSRTKDTRI
KAVAEFNQES NTNGECIKTC VFSSSGGEGI SFFSINDIFI LDMTWNEASL RQIVGRAIRL
NSHVLTPPER RYVNVHFIMA RLSNGMPTVD EDLFEIIQSK SKEFVQLFRV FKHTSLEWIH
ANEKDFSPID NESGWKTLVS RAIDLSSNKN ITNKLIEGTN IWYSNSNRLM SINRGFKGVD
GRVYDVDGNY LHDMPDNPVI KIHDGKLIYI F
