ID   NTP1_CFEPV              Reviewed;         647 AA.
AC   O91729;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-JUN-2009, entry version 43.
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;
OS   Choristoneura fumiferana entomopoxvirus (CfEPV).
OC   Viruses; dsDNA viruses, no RNA stage; Poxviridae; Entomopoxvirinae;
OC   Betaentomopoxvirus.
OX   NCBI_TaxID=28322;
OH   NCBI_TaxID=7141; Choristoneura fumiferana (Spruce budworm).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98455389; PubMed=9784068; DOI=10.1016/S0168-1702(98)00061-6;
RA   Li X., Wallis J.L., Barrett J.W., Krell P.J., Arif B.M.;
RT   "Characterization of the nucleoside triphosphate phosphohydrolase I
RT   gene from the Choristoneura fumiferana entomopoxvirus.";
RL   Virus Res. 56:93-105(1998).
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.
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DR   EMBL; AF027657; AAC63435.1; -; Genomic_DNA.
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    647       Nucleoside triphosphatase I.
FT                                /FTId=PRO_0000099101.
FT   DOMAIN       48    212       Helicase ATP-binding.
FT   DOMAIN      378    541       Helicase C-terminal.
FT   NP_BIND      61     68       ATP (By similarity).
FT   MOTIF       150    153       DEXH box.
SQ   SEQUENCE   647 AA;  76048 MW;  430815EC765CD1FD CRC64;
     MFALDSIVGK HINYALDKTQ HLPNKINNSI TNTEIILQDY QYFASRIFIG LKNLNSMLLF
     WDTGTGKTLT AVYIIKYIKE LFPRWIILIF IKKSLYVDPW LNTISSYISD TSNIKFIYYD
     STSSLDKFNN IYRSIESSLN KKNRLLIIID EVHKLISRSV KKDNSERNFT PIYRKLIKLA
     NYENNKILCM SATPITNNIA EFNNLIGLLR PNVMNIKEEY INNGKLINFK EIRETLLGIC
     SYKRLIEADS LTDTNYIDGY AKKSIFYHNI IMSDEQSKLY NMAERYDYKT ELGGLKTMRR
     LISSFAFYDL KIKGDLDNVE YNEMIKRKLA EFSEFTKNIN FSKEFINAFK NNEIKTKTDL
     LITDINNYNI LYQYSCKYIE ACRIILNSRG KVLLFEPLVN FEGISSLKYY FNCFNISYIE
     YSSKTIKMRD NDLNYYNNYE NNDGNKIKVC IFSYAGSEGI SFKCINDIII LDMPWNESEL
     KQIIGRSIRL NSHEYLPINY RYVNVHFIIS YSNNRKSVDK EILDIIKNKQ GKINVVFDLL
     KASPIEIIHN MYKYIEPVDN EIIFETIRKT RMKEMNISNV IINLKLYPIT YCKDYDRATI
     LKGLLNKDTN IIYDNDTPVA ILLVDNNNLP IFVIENDILI YITNDYY
//