ID   NPH2_FOWPN              Reviewed;         682 AA.
AC   O72904;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, 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; OrderedLocusNames=FPV082; ORFNames=FPI8R;
OS   Fowlpox virus (strain NVSL) (FPV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX   NCBI_TaxID=928301;
OH   NCBI_TaxID=7742; Vertebrata.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FP-9 / Isolate HP-440;
RX   PubMed=1326827; DOI=10.1016/0168-1702(92)90004-s;
RA   Binns M.M., Boursnell M.E.G., Skinner M.A.;
RT   "Gene translocations in poxviruses: the fowlpox virus thymidine kinase gene
RT   is flanked by 15 bp direct repeats and occupies the locus which in vaccinia
RT   virus is occupied by the ribonucleotide reductase large subunit gene.";
RL   Virus Res. 24:161-172(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA   Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT   "The genome of fowlpox virus.";
RL   J. Virol. 74:3815-3831(2000).
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; AJ223385; CAA11299.1; -; Genomic_DNA.
DR   EMBL; AF198100; AAF44426.1; -; Genomic_DNA.
DR   PIR; G48563; G48563.
DR   RefSeq; NP_039045.1; NC_002188.1.
DR   SMR; O72904; -.
DR   PRIDE; O72904; -.
DR   GeneID; 1486630; -.
DR   KEGG; vg:1486630; -.
DR   Proteomes; UP000008597; 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; 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; 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..682
FT                   /note="RNA helicase NPH-II"
FT                   /id="PRO_0000055187"
FT   DOMAIN          181..354
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          386..551
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           303..306
FT                   /note="DEXH box"
FT   BINDING         194..201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   682 AA;  79808 MW;  F394E69FD9745652 CRC64;
     MTTNDLFSIY AFSNMYDIFP RKYSQKELEE YHRKNPLFFS YTIFPVIKHR WSKAYICFQN
     NVYMLNIELD TSKPYDRVPI QHLIDIRPIS TDIKKEIYKI SDKTFITFEC YSYLKCKGYN
     SIYDITLDDK RGLLSAGNIL SIFSSNKQMP EKSSIGILKN PKPFTVIKFK SLSLITQLQI
     FELLRKRKQI VVTGSTGIGK TSQLPKVIMW YNYLFGGWDN LDRVRFDYIS RPIVLSLPRV
     ALVKSNGINF LQSLGFSDFE GSPVELRYGG KTEHTTRQHD GIVLSTNKLT SYSLSNYNII
     IVDEIHEHDR IADIIISVLR KNIDTIHSLV LMSATLEDDR DRLQEFLPDV EFYHIEGPVL
     YSIKEIYVKN KYSYDSKAYT EEEKKNISTT LNWCRPRNGM CGILFLASVS QCISYKKYLE
     KSNSDMDFII IHGKIPDITE VLNAVQRPGR ERPCILVSTP YLESSITIRT ATHVYDTGRV
     YVPKPFGGDQ LFISKSMMTQ RKGRVGRVSK GIYVYFYDMC LLKPIKSIDH EFLYEYIVYA
     KKFKLSLPND LLVIPSDKDM LKKSEEYIKS FNISFDRLFE IYVNYFVNMV EYVKIYNKGG
     KKAENLDMFE RNDILTGETL KDIKNLQLLV KINTTTRRKK MYCYKGEILF GPYMNTVIRL
     SSKQLYRNYV YMLTERSFTL YR