ID   NPH2_MYXVL              Reviewed;         678 AA.
AC   Q9Q8Q2;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=RNA helicase NPH-II;
DE            EC=3.6.4.13;
DE   AltName: Full=Nucleoside triphosphatase II;
DE            Short=NTPase II;
DE   AltName: Full=Nucleoside triphosphate phosphohydrolase II;
DE            Short=NPH II;
DE   AltName: Full=RNA helicase m44R;
GN   Name=NPH2; OrderedLocusNames=m044R;
OS   Myxoma virus (strain Lausanne) (MYXV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
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: NTP-dependent helicase that catalyzes unidirectional
CC       unwinding of 3'tailed duplex RNAs and plays an important role during
CC       transcription of early mRNAs, presumably by preventing R-loop formation
CC       behind the elongating RNA polymerase. Might also play a role in the
CC       export of newly synthesized mRNA chains out of the core into the
CC       cytoplasm. Required for replication and propagation of viral particles
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Virion. Note=Localizes to the virion core.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF170726; AAF14932.1; -; Genomic_DNA.
DR   RefSeq; NP_051758.1; NC_001132.2.
DR   SMR; Q9Q8Q2; -.
DR   GeneID; 932096; -.
DR   KEGG; vg:932096; -.
DR   Proteomes; UP000000867; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR021892; NPH-II.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF12011; NPH-II; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW   Transcription; Virion.
FT   CHAIN           1..678
FT                   /note="RNA helicase NPH-II"
FT                   /id="PRO_0000055190"
FT   DOMAIN          175..351
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          371..546
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           300..303
FT                   /note="DEXH box"
FT   BINDING         188..195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   678 AA;  77789 MW;  E30ED17F105A22F7 CRC64;
     MENHLPNIFY FPNCVTAFPY RYTQKELDDM KPVDRERFKY AVFPLIKHRW CRAYVVRDNH
     TFKLNVETSK RLRRVAYPTL VPLVGVNAAL REYVMEDGTK ISFECYSYLI CKRTTSLHDV
     DDSTIRGLVE GGNQLNIFTN SVGSVTNTVG IFGNPNPFAK VPLKSLHPSM QCKIFTSWAR
     RVPVVLTGDT GVGKTSQVPK LLLWFNYLFG GFTDLSTLTF EVQEKPIVLS LPRVALVKLH
     SETLLTSLGF EEIHGSPVSL KFGNMQERFV NTRFSRYGIV FSTHKITLNT LFKYSTVILD
     EVHEHDQTGD IIIAVCRKYI RKLDSLFLMT ATLEDDRRRI EEFFAESVFV HIPGGTLFSI
     SEAYVKNSND PLNRFMYIEE EKRNLANAIK TYTPPKQSSG IVFVSTVSQC EAYKQYLSER
     LPYKFYIIHG KVQNINDVLS DIYDNDGVSI IISTPYLESS VTVRNATHVY DTGRVYIPSP
     YGGCESFISK SMRDQRKGRV GRVNPGMYVY FYNVSELRPI KRIDFEFLHN YVLYAKVFDL
     QLPEDLFVKP TNVTRLHDVI EYIRSFDISD DVWTRLLSSY YIHILEYAKV YARGGSGALA
     LDSFERTGNL TDDALDAIKS LNMRAKILSH KKASAHTYAL RCKLLFGVYA GKVFTVYHKR
     PLTGYITMIA EHSFIPDY