NPH2_VACCW
ID NPH2_VACCW Reviewed; 676 AA.
AC P12927; Q76ZU5;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 123.
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; OrderedLocusNames=VACWR077; ORFNames=I8R;
OS Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS WR)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10254;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=1994576; DOI=10.1016/0042-6822(91)90491-s;
RA Fathi Z., Condit R.C.;
RT "Genetic and molecular biological characterization of a vaccinia virus
RT temperature-sensitive complementation group affecting a virion component.";
RL Virology 181:258-272(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA Wohlhueter R.;
RT "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT redundancy and an error rate of 0.16/10kb.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=4364421; DOI=10.1016/s0021-9258(19)42668-9;
RA Paolette E., Rosemond-Hornbeak H., Moss B.;
RT "Two nucleid acid-dependent nucleoside triphosphate phosphohydrolases from
RT vaccinia virus. Purification and characterization.";
RL J. Biol. Chem. 249:3273-3280(1974).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99.
RX PubMed=2835495; DOI=10.1128/jvi.62.6.1889-1897.1988;
RA Schmitt J.F.C., Stunnenberg H.G.;
RT "Sequence and transcriptional analysis of the vaccinia virus HindIII I
RT fragment.";
RL J. Virol. 62:1889-1897(1988).
RN [5]
RP SIMILARITY TO HELICASES.
RX PubMed=1321883; DOI=10.1099/0022-1317-73-4-989;
RA Koonin E.V., Senkevich T.G.;
RT "Vaccinia virus encodes four putative DNA and/or RNA helicases distantly
RT related to each other.";
RL J. Gen. Virol. 73:989-993(1992).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=1332061; DOI=10.1073/pnas.89.22.10935;
RA Shuman S.;
RT "Vaccinia virus RNA helicase: an essential enzyme related to the DE-H
RT family of RNA-dependent NTPases.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10935-10939(1992).
RN [7]
RP FUNCTION.
RX PubMed=8970979; DOI=10.1128/jvi.70.12.8549-8557.1996;
RA Gross C.H., Shuman S.;
RT "Vaccinia virions lacking the RNA helicase nucleoside triphosphate
RT phosphohydrolase II are defective in early transcription.";
RL J. Virol. 70:8549-8557(1996).
RN [8]
RP ENZYME ACTIVITY, AND MUTAGENESIS OF LYS-191; THR-192; ARG-229; THR-326 AND
RP THR-328.
RX PubMed=9573237; DOI=10.1128/jvi.72.6.4729-4736.1998;
RA Gross C.H., Shuman S.;
RT "The nucleoside triphosphatase and helicase activities of vaccinia virus
RT NPH-II are essential for virus replication.";
RL J. Virol. 72:4729-4736(1998).
RN [9]
RP MUTAGENESIS OF ASP-296; GLU-297 AND HIS-299.
RX PubMed=7609038; DOI=10.1128/jvi.69.8.4727-4736.1995;
RA Gross C.H., Shuman S.;
RT "Mutational analysis of vaccinia virus nucleoside triphosphate
RT phosphohydrolase II, a DExH box RNA helicase.";
RL J. Virol. 69:4727-4736(1995).
RN [10]
RP MUTAGENESIS OF GLN-491; ARG-492; GLY-494; ARG-495; GLY-497; ARG-498 AND
RP GLY-502.
RX PubMed=8627691; DOI=10.1128/jvi.70.3.1706-1713.1996;
RA Gross C.H., Shuman S.;
RT "The QRxGRxGRxxxG motif of the vaccinia virus DExH box RNA helicase NPH-II
RT is required for ATP hydrolysis and RNA unwinding but not for RNA binding.";
RL J. Virol. 70:1706-1713(1996).
RN [11]
RP CHARACTERIZATION.
RX PubMed=10667799; DOI=10.1038/35000239;
RA Jankowsky E., Gross C.H., Shuman S., Pyle A.M.;
RT "The DExH protein NPH-II is a processive and directional motor for
RT unwinding RNA.";
RL Nature 403:447-451(2000).
RN [12]
RP CHARACTERIZATION.
RX PubMed=20110368; DOI=10.1074/jbc.m109.088559;
RA Taylor S.D., Solem A., Kawaoka J., Pyle A.M.;
RT "The NPH-II helicase displays efficient DNA x RNA helicase activity and a
RT pronounced purine sequence bias.";
RL J. Biol. Chem. 285:11692-11703(2010).
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 {ECO:0000269|PubMed:1332061, ECO:0000269|PubMed:8970979}.
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 Evidence={ECO:0000269|PubMed:9573237};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1332061}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:4364421}.
CC Note=Localizes to the virion core.
CC -!- INDUCTION: Expressed both early and late in the viral replicative
CC cycle. {ECO:0000269|PubMed:1994576}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; J03399; AAB59810.1; -; Genomic_DNA.
DR EMBL; AY243312; AAO89356.1; -; Genomic_DNA.
DR PIR; B38497; WZVZI8.
DR RefSeq; YP_232959.1; NC_006998.1.
DR SMR; P12927; -.
DR DNASU; 3707610; -.
DR GeneID; 3707610; -.
DR KEGG; vg:3707610; -.
DR Proteomes; UP000000344; 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 1: Evidence at protein 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_0000055185"
FT DOMAIN 172..347
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 366..535
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"
FT MUTAGEN 191
FT /note="K->A: Inactivates ATPase and helicase activities."
FT /evidence="ECO:0000269|PubMed:9573237"
FT MUTAGEN 192
FT /note="T->A: Inactivates ATPase and helicase activities."
FT /evidence="ECO:0000269|PubMed:9573237"
FT MUTAGEN 229
FT /note="R->A: Inactivates ATPase and helicase activities."
FT /evidence="ECO:0000269|PubMed:9573237"
FT MUTAGEN 296
FT /note="D->A: Reduces strongly NTPase and helicase
FT activities."
FT /evidence="ECO:0000269|PubMed:7609038"
FT MUTAGEN 297
FT /note="E->A: Reduces strongly NTPase and helicase
FT activities."
FT /evidence="ECO:0000269|PubMed:7609038"
FT MUTAGEN 299
FT /note="H->A: Activates NTPase without need for a nucleic
FT acid cofactor."
FT /evidence="ECO:0000269|PubMed:7609038"
FT MUTAGEN 300
FT /note="E->A: Inactivates ATPase and helicase activities."
FT MUTAGEN 326
FT /note="T->A: Defect in RNA unwinding."
FT /evidence="ECO:0000269|PubMed:9573237"
FT MUTAGEN 328
FT /note="T->A: Defect in RNA unwinding."
FT /evidence="ECO:0000269|PubMed:9573237"
FT MUTAGEN 491
FT /note="Q->A: Defect in ATP hydrolysis and RNA unwinding."
FT /evidence="ECO:0000269|PubMed:8627691"
FT MUTAGEN 492
FT /note="R->A: Defect in ATP hydrolysis and RNA unwinding."
FT /evidence="ECO:0000269|PubMed:8627691"
FT MUTAGEN 494
FT /note="G->A: Defect in ATP hydrolysis and RNA unwinding."
FT /evidence="ECO:0000269|PubMed:8627691"
FT MUTAGEN 495
FT /note="R->A: Defect in ATP hydrolysis and RNA unwinding."
FT /evidence="ECO:0000269|PubMed:8627691"
FT MUTAGEN 497
FT /note="G->A: Defect in ATP hydrolysis and RNA unwinding."
FT /evidence="ECO:0000269|PubMed:8627691"
FT MUTAGEN 498
FT /note="R->A: Defect in ATP hydrolysis and RNA unwinding."
FT /evidence="ECO:0000269|PubMed:8627691"
FT MUTAGEN 502
FT /note="G->A: Defect in ATP hydrolysis and RNA unwinding."
FT /evidence="ECO:0000269|PubMed:8627691"
SQ SEQUENCE 676 AA; 77600 MW; F341266D173EB61E CRC64;
MEKNLPDIFF FPNCVNVFSY KYSQDEFSNM SKTERDSFSL AVFPVIKHRW HNAHVVKHKG
IYKVSTEARG KKVSPPSLGK PAHINLTAKQ YIYSEHTISF ECYSFLKCIT NTEINSFDEY
ILRGLLEAGN SLQIFSNSVG KRTDTIGVLG NKYPFSKIPL ASLTPKAQRE IFSAWISHRP
VVLTGGTGVG KTSQVPKLLL WFNYLFGGFS TLDKITNFHE RPVILSLPRI ALVRLHSNTI
LKSLGFKVLD GSPISLRYGS IPEELINKQP KKYGIVFSTH KLSLTKLFSY GTLIIDEVHE
HDQIGDIIIA VARKHHTKID SMFLMTATLE DDRERLKVFL PNPAFIHIPG DTLFKISEVF
IHNKINPSSR MAYIEEEKRN LVTAIQMYTP PDGSSGIVFV ASVAQCHEYK SYLEKRLPYD
MYIIHGKVLD IDEILEKVYS SPNVSIIIST PYLESSVTIR NVTHIYDMGK VFVPAPFGGS
QEFISKSMRD QRKGRVGRVN PGTYVYFYDL SYMKSIQRID SEFLHNYILY ANKFNLTLPE
DLFIIPTNLD ILWRTKEYID SFDISTETWN KLLSNYYMKM IEYAKLYVLS PILAEELDNF
ERTGELTSIV REAILSLNLR IKILNFKHKD DDTYIHFCKI LFGVYNGTNA TIYYHRPLTG
YMNMISDTIF VPVDNN
