ID   NPH2_MCV1               Reviewed;         684 AA.
AC   Q98218;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 101.
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; ORFNames=50R;
OS   Molluscum contagiosum virus subtype 1 (MOCV) (MCVI).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Molluscipoxvirus.
OX   NCBI_TaxID=10280;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8670425; DOI=10.1126/science.273.5276.813;
RA   Senkevich T.G., Bugert J.J., Sisler J.R., Koonin E.V., Darai G., Moss B.;
RT   "Genome sequence of a human tumorigenic poxvirus: prediction of specific
RT   host response-evasion genes.";
RL   Science 273:813-816(1996).
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; U60315; AAC55178.1; -; Genomic_DNA.
DR   PIR; T30652; T30652.
DR   RefSeq; NP_044001.1; NC_001731.1.
DR   SMR; Q98218; -.
DR   PRIDE; Q98218; -.
DR   GeneID; 1670235; -.
DR   KEGG; vg:1670235; -.
DR   Proteomes; UP000000869; 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..684
FT                   /note="RNA helicase NPH-II"
FT                   /id="PRO_0000055188"
FT   DOMAIN          184..359
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          392..563
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           308..311
FT                   /note="DEXH box"
FT   BINDING         197..204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   684 AA;  76557 MW;  51072B193CCC7284 CRC64;
     MKNLPGVFAF PDNETIFAHA YSQRELEAML PARAGAQPHA FAYAAWPLSK HRWRGAFVCR
     QRGVLKLNLE LDAGAFERVP RSEAERFEPE QSDARALMHR GADGTVMSFE CYSFLRCRPG
     LELREAGLAL LRGLVVGGNR MRIFSGVRRA GASAATSAGM LGNESPFERA PFASLRIDAQ
     AALFRAWAAR RPTVVTGGTG VGKTSQVPKL LLWFNYLFGG TEDLDVLAPA RERPVVLSLP
     RVALVRMNGH ALRRALGFDA LEGSPVELRY GDLAPADANS SRSPFRLVVS TNQLTLGALF
     AHGTVILDEV HEHDQMADIM LAVLRVHRAR VDSIVLMSAT LEDDRERLQE FFPDAEFVHI
     PGSTRFEIRG VYVRNSSDPR DARAYDEEER RNVSAALSAH RPRAGRCGIL FVASVAQCED
     YARLLTREHP ELGVYVVHGK TPNVDALLAE VYASARPCVL VSTPYLESSV TIRTVTHVYD
     TGRVFVPAPF GGRQMLISPA MRTQRRGRVG RVMPGTYVYF YDPARLAPIK RIDSEFLYNY
     IIYARHYGLV LPDDLYVQPS DLELLRRCEE YLDGFGLAPE RLFELASTRY LRMVEYAKIY
     ARGGARAEEL NRFERDGVVT EDVLASIRAL NLRARVLSAR ARRGQFLHTC EVAFGPYAGT
     RFLLANRRRL RGDIFMVTER SFVL