ID   NTP2_VACCA              Reviewed;         676 AA.
AC   O57193; Q6J3G1;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=Nucleoside triphosphatase II;
DE            Short=NTPase II;
DE            EC=3.6.1.15;
DE   AltName: Full=Nucleoside triphosphate phosphohydrolase II;
DE            Short=NPH II;
DE   AltName: Full=RNA helicase I8;
GN   Name=NPH2; OrderedLocusNames=MVA069R, ACAM3000_MVA_069;
OS   Vaccinia virus (strain Ankara) (VACV).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae;
OC   Orthopoxvirus.
OX   NCBI_TaxID=126794;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=98263813; PubMed=9601507; DOI=10.1006/viro.1998.9123;
RA   Antoine G., Scheiflinger F., Dorner F., Falkner F.G.;
RT   "The complete genomic sequence of the modified vaccinia Ankara strain:
RT   comparison with other orthopoxviruses.";
RL   Virology 244:365-396(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Acambis 3000;
RA   Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S.,
RA   Osborne J., Khristova M., Wohlhueter R.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential for viral replication. Plays an important role
CC       during transcription of early mRNAs, presumably by preventing R-
CC       loop formation behind the elongating RNA polymerase. Acts as NTP-
CC       dependent helicase that catalyzes unidirectional unwinding of
CC       3'tailed duplex RNAs. Might also play a role in the export of
CC       newly synthesized mRNA chains out of the core into the cytoplasm.
CC       Required for propagation of viral particles (By similarity).
CC   -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- WEB RESOURCE: Name=The DExH/D protein family database;
CC       Note=Poxviridae DExH proteins;
CC       URL="http://www.dexhd.org/viral_pox.htm";
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DR   EMBL; U94848; AAB96491.1; -; Genomic_DNA.
DR   EMBL; AY603355; AAT10467.1; -; Genomic_DNA.
DR   PIR; T37345; T37345.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR001650; DNA/RNA_helicase_C.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 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; Early protein; Helicase; Hydrolase; Late protein;
KW   Nucleotide-binding; Transcription.
FT   CHAIN         1    676       Nucleoside triphosphatase II.
FT                                /FTId=PRO_0000055182.
FT   DOMAIN      172    347       Helicase ATP-binding.
FT   DOMAIN      366    535       Helicase C-terminal.
FT   NP_BIND     185    192       ATP (By similarity).
FT   MOTIF       296    299       DEXH box.
SQ   SEQUENCE   676 AA;  77600 MW;  FB4ABAAFF66AD9FC 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 PYLESSVTIR NVTHIYDMGR VFVPAPFGGS
     QEFISKSMRD QRKGRVGRVN PGTYVYFYDL SYMKSIQRID SEFLHNYILY ANKFNLTLPE
     DLFIIPTNLD ILWRTKEYID SFDISTETWN KLLSNYYMKM IEYAKLYVLS PILAEELDNF
     ERTGELTSIV QEAILSLNLR IKILNFKHKD DDTYIHFCKI LFGVYNGTNA TIYYHRPLTG
     YMNMISDTIF VPVDNN
//