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Database: UniProt
Entry: P29814
LinkDB: P29814
Original site: P29814 
ID   NTP1_AMEPV              Reviewed;         648 AA.
AC   P29814;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   05-JUN-2019, entry version 86.
DE   RecName: Full=Nucleoside triphosphatase I;
DE            EC=3.6.1.15;
DE   AltName: Full=NPH-I;
DE   AltName: Full=Nucleoside triphosphate phosphohydrolase I;
DE            Short=NPH I;
GN   Name=NPH1; OrderedLocusNames=AMV192; ORFNames=G6;
OS   Amsacta moorei entomopoxvirus (AmEPV).
OC   Viruses; Poxviridae; Entomopoxvirinae; Betaentomopoxvirus.
OX   NCBI_TaxID=28321;
OH   NCBI_TaxID=340055; Amsacta.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10936094; DOI=10.1006/viro.2000.0449;
RA   Bawden A.L., Glassberg K.J., Diggans J., Shaw R., Farmerie W.,
RA   Moyer R.W.;
RT   "Complete genomic sequence of the Amsacta moorei entomopoxvirus:
RT   analysis and comparison with other poxviruses.";
RL   Virology 274:120-139(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-486.
RX   PubMed=8517016; DOI=10.1006/viro.1993.1020;
RA   Hall R.L., Moyer R.W.;
RT   "Identification of an Amsacta spheroidin-like protein within the
RT   occlusion bodies of Choristoneura entomopoxviruses.";
RL   Virology 192:179-187(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 486-648.
RX   PubMed=1942245;
RA   Hall R.L., Moyer R.W.;
RT   "Identification, cloning, and sequencing of a fragment of Amsacta
RT   moorei entomopoxvirus DNA containing the spheroidin gene and three
RT   vaccinia virus-related open reading frames.";
RL   J. Virol. 65:6516-6527(1991).
CC   -!- FUNCTION: DNA-dependent ATPase required for providing the needed
CC       energy to achieve the termination of early transcripts. Acts in
CC       concert with the RAP94 subunit of the virion RNA polymerase and
CC       the capping enzyme/VTF to catalyze release of UUUUUNU-containing
CC       nascent RNA from the elongation complex. NPH-I must bind ssDNA in
CC       order to exhibit ATPase activity (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside
CC         5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC   -!- SUBUNIT: Monomer. Interacts (via C-terminus) with RAP94 (via N-
CC       terminus). Interacts with the cap-specific mRNA (nucleoside-2'-
CC       O-)-methyltransferase (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Virion core
CC       enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. NPH I subfamily.
CC       {ECO:0000305}.
DR   EMBL; AF250284; AAG02898.1; -; Genomic_DNA.
DR   EMBL; M77182; AAA42384.1; -; Genomic_DNA.
DR   PIR; F41561; NPVZAM.
DR   RefSeq; NP_064974.1; NC_002520.1.
DR   PRIDE; P29814; -.
DR   GeneID; 1494782; -.
DR   KEGG; vg:1494782; -.
DR   OrthoDB; 1206at10239; -.
DR   Proteomes; UP000000872; Genome.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR013676; NPHI_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08469; NPHI_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; DNA-binding; Hydrolase;
KW   Nucleotide-binding; Reference proteome; Transcription; Virion.
FT   CHAIN         1    648       Nucleoside triphosphatase I.
FT                                /FTId=PRO_0000099099.
FT   DOMAIN       48    212       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      378    541       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      61     68       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION      467    533       Binding to the cap-specific mRNA
FT                                (nucleoside-2'-O-)-methyltransferase.
FT                                {ECO:0000250}.
FT   MOTIF       150    153       DEXH box.
SQ   SEQUENCE   648 AA;  76109 MW;  25BE863C0B8728AA CRC64;
     MFALDSIVGK HINYALDKTQ HLPNKIMNNI TNTEITLQDY QYFVSRIFIG LKNLNSMLLF
     WDTGMGKTLT AVYIIKYIKE LFPRWIILIF IKKSLYIDPW LNTIRSYISD TSNIKFIYYD
     SSSSLDKFNN IYRSIESSLN KKSRLLIIID EVHKLISRTV KKDNNERNFT PIYKKLIKLA
     NFENNKILCM SATPVTNNIS EFNNLIGLLR PNVMNIKEEY INNGKLINFK ELRETLLAIC
     SYKRLIEADS LTETNYIDGY AKKNIFYHNI IMSDEQSKLY NMAEKYDYKT ELGGLKTMRR
     LISSFAFYDL KIKGDLDNIE YNDMIKRKLA EFSEFTKNIN FSESFIESFK NDNIKIKTNL
     PITDINNYNI LYQYSCKYIE TCKIILNSRG KVLIFEPLVN FEGISSLKCY FNCFNISYIE
     YSSKTLKTRD NELNEYNNYE NNNGKKVKVC IFSYAGSEGI SFKCINDIII LDMPWNESEL
     KQIIGRSIRL NSHKDLPQEY RYVNVHFLIS YTNNRKSVDK EILDIIKDKQ GKINVIFDLL
     KSSSIESIHN TYKYIEPAEN EIIFDTIRKT RMKEMNVSNV IINIKLYPIS YCKDYDRATI
     LKGLLNKDTN IVYKDNTAVA KLMIDKDNIP IFIIENDTLI YIADDYYE
//
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