ID NTP1_YMTV5 Reviewed; 631 AA.
AC Q9QB93;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 08-NOV-2023, entry version 98.
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=88L; ORFNames=B5L;
OS Yaba monkey tumor virus (strain VR587) (YMTV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Yatapoxvirus;
OC Yaba monkey tumor virus.
OX NCBI_TaxID=928314;
OH NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9539; Macaca (macaques).
OH NCBI_TaxID=9557; Papio hamadryas (Hamadryas baboon).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14645589; DOI=10.1128/jvi.77.24.13335-13347.2003;
RA Brunetti C.R., Amano H., Ueda Y., Qin J., Miyamura T., Suzuki T., Li X.,
RA Barrett J.W., McFadden G.;
RT "Complete genomic sequence and comparative analysis of the tumorigenic
RT poxvirus Yaba monkey tumor virus.";
RL J. Virol. 77:13335-13347(2003).
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; AY386371; AAR07444.1; -; Genomic_DNA.
DR RefSeq; NP_938343.1; NC_005179.1.
DR SMR; Q9QB93; -.
DR GeneID; 2943701; -.
DR KEGG; vg:2943701; -.
DR Proteomes; UP000008596; Segment.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
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:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR10799:SF1009; HELICASE ATP-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 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..631
FT /note="Nucleoside triphosphatase I"
FT /id="PRO_0000099098"
FT DOMAIN 42..204
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 367..536
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 631 AA; 72579 MW; 06561CA08C729EFF CRC64;
MSRQHAAYID YALNRMKKMP IEMLGSDTIT LKPYQHFVAK VFLGLDTMHS ILLFHDTGVG
KTITTVFILK HLKDIYTNWT ILLLVKKALV EDPWMNTILK YSPEIIKNCI FINYDDKNFH
NKFFTNIKTI SSRSRVCVVL DECHNFISKS LIKEDGKQRP TKSVYNYLSK NISLNNNKMI
CLSATPIVNN VREFTMIVNL LRPKIIQFQS LFENKNLVNE KELIDKLGGI CSYIVNDEFS
IFDDVEGSQS FAKKTVYMHY VNMTKQQEII YQKAKIAEIK SGIASFRIYR RMAATFSFDS
FPDKKKKTID EITLELGALY KDFVNYVNKK SFSNNAIKLF KSGKGLTGDS NPLDISLLSE
LRQKSCKFTE VCLKILASPG KCLVFEPFIN QSGIEVLLVY FSVFCITSVE FSSRTKDTRI
KNVFEFNKES NTNGEQIKVC VFSISGGEGI SFFSINDIFI LDMTWNEASL KQIVGRAIRL
NSHANTPPNR RYVNVYFIIA RLSSGEPTVD EDLINIIKTK SKEFFQLFKV FKESSIEWIY
KNKKDFYPIN DESGWRALTS RVVDVNVKSK RTVQLAQGQN IWFSNSSRMV TIHKGFKTSD
GKIFDVDGNF IQNMPINPII KIHNDKLVYI I
//
