ID   NPH2_RFVKA              Reviewed;         678 AA.
AC   Q9Q927;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 92.
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;
GN   Name=NPH2; OrderedLocusNames=s044R;
OS   Rabbit fibroma virus (strain Kasza) (RFV) (Shope fibroma virus (strain
OS   Kasza)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
OX   NCBI_TaxID=10272;
OH   NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10562495; DOI=10.1006/viro.1999.0002;
RA   Willer D.O., McFadden G., Evans D.H.;
RT   "The complete genome sequence of shope (Rabbit) fibroma virus.";
RL   Virology 264:319-343(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   -!- INDUCTION: Expressed both early and late in the viral replicative
CC       cycle.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF170722; AAF17926.1; -; Genomic_DNA.
DR   RefSeq; NP_051933.1; NC_001266.1.
DR   SMR; Q9Q927; -.
DR   PRIDE; Q9Q927; -.
DR   GeneID; 1486887; -.
DR   KEGG; vg:1486887; -.
DR   Proteomes; UP000000868; 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   2: Evidence at transcript level;
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_0000055191"
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;  78243 MW;  FDF8FDD5E5C58B1E CRC64;
     MENHLPNIFY FPNCVTTFPY RYTQKELDDM KPDERERFKY ATFPIIKHRW SHAYVVKDNH
     VFKLNVETSK RLRRATPPTL SVPVSMNTML REYITQDGTK ISFECYSYLT CKKATSLHDL
     DDNAIRGLVE GGNRLQLFTN SVGSVKDTVG IFGNPNPFMK VPLKSLHPSM QCKIFESWIH
     HVPVVLTGDT GVGKTSQVPK LLLWFNYLFG GFVNLSTITF DVQEKPIVLS LPRVALVKLH
     SETLLTSLGF NEIHKSPVSL KFGNMQEQFV NTRFRRYGIV FSTHKITLNT LFNYSTVILD
     EVHEHDQTGD IIIAVCRKYI RKLDSLFLMT ATLEDDRQRI EEFFTESVFV HIPGGTLFSI
     SEAYVKNSND SLNKFMYIEE EKRNLVNAIK TYTPPKQSSG IVFVSTVSQC DVYKQYLSER
     LPYKFYIIHG KIQNINDLLS DIYDNEGVSI IISTPYLESS VTVQNATHVY DTGRVYIPSP
     YGGREVFISK SMRDQRKGRV GRVKPGMYIY FYDVSELRPI KRIDFEFLHN YVLYSKVFDL
     QLPEDLFVKP TNMTRLRDVI EYIRSFNISD GVWTRLLSSY YIHILEYAKV YARGGQSAAA
     LDSFERTGNL TDDALDAIKS LNMRAKIISH RKASTHTYAL MCRLLFGVYA GKTFIAYHKR
     PLTGYITMIT EHSFIPEY