ID   NPH2_VAR67              Reviewed;         676 AA.
AC   P0DSU5; P33051; Q85378; Q89208; Q9QNJ4;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   03-AUG-2022, entry version 11.
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 I8;
GN   Name=NPH2; ORFNames=I8R;
OS   Variola virus (isolate Human/India/Ind3/1967) (VARV) (Smallpox virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=587200;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8109158; DOI=10.1016/0168-1702(93)90093-3;
RA   Shchelkunov S.N., Blinov V.M., Resenchuk S.M., Totmenin A.V.,
RA   Sandakhchiev L.S.;
RT   "Analysis of the nucleotide sequence of a 43 kbp segment of the genome of
RT   variola virus India-1967 strain.";
RL   Virus Res. 30:239-258(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8383392; DOI=10.1016/0168-1702(93)90110-9;
RA   Shchelkunov S.N., Blinov V.M., Totmenin A.V., Marennikova S.S.,
RA   Kolykhalov A.A., Frolov I.V., Chizhikov V.E., Gytorov V.V., Gashikov P.V.,
RA   Belanov E.F., Belavin P.A., Resenchuk S.M., Andzhaparidze O.G.,
RA   Sandakhchiev L.S.;
RT   "Nucleotide sequence analysis of variola virus HindIII M, L, I genome
RT   fragments.";
RL   Virus Res. 27:25-35(1993).
RN   [3]
RP   COMPLETE GENOME.
RA   Blinov V.M.;
RL   Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
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; X67119; CAA47562.1; -; Genomic_DNA.
DR   EMBL; X69198; CAA49003.1; -; Genomic_DNA.
DR   PIR; F36843; F36843.
DR   RefSeq; NP_042106.1; NC_001611.1.
DR   SMR; P0DSU5; -.
DR   GeneID; 1486463; -.
DR   KEGG; vg:1486463; -.
DR   Proteomes; UP000002060; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; PF00270; DEAD; 1.
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; Early protein; Helicase; Hydrolase; Late protein;
KW   Nucleotide-binding; Reference proteome; Transcription; Virion.
FT   CHAIN           1..676
FT                   /note="RNA helicase NPH-II"
FT                   /id="PRO_0000055186"
FT   DOMAIN          172..347
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          366..542
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           296..299
FT                   /note="DEXH box"
FT   BINDING         185..192
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   676 AA;  77545 MW;  4D7589E5B012562F CRC64;
     MEKNLPDIFF FPNCVNVFSY KYSQDEFSNM SNMERDSFSL AVFPVIKHRW HNAHVVKHKG
     IYKVSTEAHG KKVSPPSLGK PSHINLTAKQ YIYSEHTISF ECYSFLKCIT NAEINSFDEY
     ILRGLLEAGN SLQIFSNSVG KRTDTIGVLG NKYPFSKIPL ASLTPKAQRE IFSAWISHRP
     VVLTGGTGVG KTSQVPKLLL WFNYLFGGFS TLDKITDFHE RPVILSLPRI ALVRLHSNTI
     LKSLGFKVLD GSPISLRYGS IPEELINKQP KKYGIVFSTH KLSLTKLFSY GTLIIDEVHE
     HDQIGDIIIA VARKHHTKID SMFLMTATLE DDRERLKVFL PNPAFIHIPG DTLFKISEVF
     IHNKINPSSR MAYIEEEKRN LVTAIQMYTP PDGSSGIVFV ASVAQCHEYK SYLEKRLPYD
     MYIIHGKVLE IDKILEKVYS SPNVSIIISA PYLESSVTIH NVTHIYDMGR VFVPAPFGGS
     QQFISKSMRD QRKGRVGRVN PGTYVYFYDL SYMKSIQRIN SEFLHNYILY ANKFNLTLPE
     DLFIIPTNLD ILWRTKEYID SFDISTETWN KLLSNYYMKM IEYAKLYVLS PILAEELDNF
     ERTGELTSIV QEAILSLNLR IKILNFKHKD NDTYIHFCKI LFGVYNGTNA TIYYHRPLTG
     YMNMISDTIF VPVDNN