ID NTP1_VACCA Reviewed; 631 AA. AC O57214; Q6J3C2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 16-JUN-2009, entry version 46. DE RecName: Full=Nucleoside triphosphatase I; DE EC=3.6.1.15; DE AltName: Full=Nucleoside triphosphate phosphohydrolase I; DE Short=NPH I; DE AltName: Full=Factor X; GN Name=NPH1; OrderedLocusNames=MVA108L, ACAM3000_MVA_108; 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: Serves two roles in transcription; it acts in concert CC with viral termination factor/capping enzyme to catalyze release CC of UUUUUNU-containing nascent RNA from the elongation complex, and CC it acts by itself as a polymerase elongation factor to facilitate CC readthrough of intrinsic pause sites. CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the helicase family. NPH I subfamily. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U94848; AAB96451.1; -; Genomic_DNA. DR EMBL; AY603355; AAT10506.1; -; Genomic_DNA. DR PIR; T37384; T37384. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004386; F:helicase activity; IEA:InterPro. DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW. DR InterPro; IPR014001; DEAD-like_N. DR InterPro; IPR001650; DNA/RNA_helicase_C. DR InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd. DR InterPro; IPR013676; NPHI_C. DR InterPro; IPR000330; SNF2_N. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF08469; NPHI_C; 1. DR Pfam; PF00176; SNF2_N; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Hydrolase; Late protein; Nucleotide-binding; KW Transcription. FT CHAIN 1 631 Nucleoside triphosphatase I. FT /FTId=PRO_0000099090. FT DOMAIN 42 204 Helicase ATP-binding. FT DOMAIN 367 532 Helicase C-terminal. FT NP_BIND 55 62 ATP (By similarity). FT MOTIF 141 144 DEXH box. SQ SEQUENCE 631 AA; 72381 MW; E7FE68BA105A1A35 CRC64; MSKSHAAYID YALRRTTNMP VEMMGTDVVR LKDYQHFVAR VFLGLDSMHS LLLFHETGVG KTMTTVYILK HLKDIYTNWA IILLVKKALI EDPWMNTILR YAPEITKDCI FINYDDQNFR NKFFTNIKTI NSKSRICVII DECHNFISKS LIKEDGKIRP TRSVYNFLSK TIALKNHKMI CLSATPIVNS VQEFTMLVNL LRPGSLQHQS LFENKRLVDE KELVSKLGGL CSYIVNNEFS IFDDVEGSAS FAKKTVLMRY VNMSKKQEEI YQKAKLAEIK TGISSFRILR RMATTFTFDS FPERQNRDPG EYAQEIATLY NDFKNSLRDR EFSKSALDTF KKGELLKGDA SAADISLFTE LKEKSVKFID VCLGILASHG KCLVFEPFVN QSGIEILLLY FKVFGISNIE FSSRTKDTRI KAVAEFNQES NTNGECIKTC VFSSSGGEGI SFFSINDIFI LDMTWNEASL RQIVGRAIRL NSHVLTPPER RYVNVHFIMA RLSNGMPTVD EDLFEIIQSK SKEFVQLFRV FKHTSLEWIH ANEKDFSPID NESGWKTLVS RAIDLSSKKN ITNKLIEGTN IWYSNSNRLM SINRGFKGVD GRVYDVDGNY LHDMPDNPVI KIHDGKLIYI F //