ID NTP1_FOWPV Reviewed; 637 AA. AC O72907; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 16-JUN-2009, entry version 51. DE RecName: Full=Nucleoside triphosphatase I; DE EC=3.6.1.15; DE AltName: Full=Nucleoside triphosphate phosphohydrolase I; DE Short=NPH I; GN Name=NPH1; OrderedLocusNames=FPV052; ORFNames=FP-D11, FPD11; OS Fowlpox virus (FPV). OC Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae; OC Avipoxvirus. OX NCBI_TaxID=10261; OH NCBI_TaxID=7742; Vertebrata. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=FP-9 / Isolate HP-440; RA Skinner M.A.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91108382; PubMed=2177083; RA Binns M.M., Britton B.S., Mason C., Boursnell M.E.G.; RT "Analysis of the fowlpox virus genome region corresponding to the RT vaccinia virus D6 to A1 region: location of, and variation in, non- RT essential genes in poxviruses."; RL J. Gen. Virol. 71:2873-2881(1990). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=20193820; PubMed=10729156; RX 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: 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 (By similarity). CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. 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; AJ005163; CAA06401.1; -; Genomic_DNA. DR EMBL; AF198100; AAF44396.1; -; Genomic_DNA. DR PIR; S42251; S42251. DR RefSeq; NP_039015.1; -. DR GeneID; 1486600; -. DR BRENDA; 3.6.1.15; 288568. 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; Nucleotide-binding; Transcription. FT CHAIN 1 637 Nucleoside triphosphatase I. FT /FTId=PRO_0000099094. FT DOMAIN 43 205 Helicase ATP-binding. FT DOMAIN 358 537 Helicase C-terminal. FT NP_BIND 56 63 ATP (By similarity). FT MOTIF 142 145 DEXH box. SQ SEQUENCE 637 AA; 73774 MW; 9F838D2E0519F0D8 CRC64; MNTYAAYIDY ALKKLDTFPV DMTGGNDNTV LLKDYQLFVA KVFLGLNSMN SILLFQETGV GKTITTVYML KNLKKIYSEW TIIILVKKAL IDDPWTHTIL DYAPEVMKDC IIMNYDDQNF HNKFFTNIKS INVKSRIFII IDECHNFISK SLTKEDNKKR NTKLVYNYIA KNLMQKNNKL ICLSATPIVN DVREFQMLVN LLRPGILTPD KSLFYNKKLI DEKEIISKLG CICSYIVNNE ASIFEDVENT TLFAKKTVHI KHVFMSKKQE ELYLKARYLE RKLGISVFKI YQRMASTFVF DDIPDKKKLT EEEYEKFVDS LSIDFKNTLY GKKISKQSLD ILSAGGTIND IKDVKDIELY NYLYEHSCKF TFVCVSIIQS KGKCLVFEPF IRSSGIEILL QYFNVFGITY IEFSSRTKDI RSKSVSDFNK VDNTDGEITK VCVFSQSGNE GISFLSINDI FILDMTWNEA SLKQIIGRAI RLNSHVNNPP ERRYVNVYFV VAKLSSGRSS VDDILLDIIQ SKSKEFSQLY KVFKHSSIEW IYSNYTDFQT VDDEKGFKKL ISRNIILDEN TITNKKKLTM GENIWYSFSS SLVSIHRGFK SMDNKIYDSE GFFITVLPDK PTIKIYEGKL IYILTVR //