NPH2_VACCT
ID NPH2_VACCT Reviewed; 676 AA.
AC Q9JFC3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=TI8R;
OS Vaccinia virus (strain Tian Tan) (VACV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX NCBI_TaxID=10253;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jin Q., Hou Y.D., Cheng N.H., Yao E.M., Cheng S.X., Yang X.K., Jing D.Y.,
RA Yu W.H., Yuan J.S., Ma X.J.;
RT "Complete genomic sequence of vaccinia virus (Tian Tan strain).";
RL Submitted (SEP-1998) 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; AF095689; AAF33937.1; -; Genomic_DNA.
DR SMR; Q9JFC3; -.
DR Proteomes; UP000163220; 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; Transcription; Virion.
FT CHAIN 1..676
FT /note="RNA helicase NPH-II"
FT /id="PRO_0000055184"
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"
SQ SEQUENCE 676 AA; 77572 MW; AF179FB67C97F430 CRC64;
MEKNLPDIFF FPNCVNVFSY KYSQDEFSNM SKTERDSFSL AVFPVIKHRW HNAHVVKHKG
IYKVSTEARG KKVSPPSLGK PAHINLTAKQ YIYSEHTISF ECYSFLKCIT NTEINSFDEY
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
MYIIHGKVLD IDEILEKVYS SPNVSIIIST PYLESSVTIH NVTHIYDMGR VFVPAPFGGS
QQFISKSMRD QRKGRVGRVN PGTYVYFYDL SYMKSIQRID SEFLHNYILY ANKFNLTLPE
DLFIIPTNLD ILWRTKEYID SFDISTETWN KLLSNYYMKM IEYAKLYVLS PILAEELDNF
ERTGELTSIV REAILSLNLR IKILNFKHKD DDTYIHFCKI LFGVYNGTNA TIYYHRPLTG
YINIISDTIF VPVDNN