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 08-NOV-2023, entry version 103.
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; Myxoma virus.
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; 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..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
//
