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 27-MAR-2024, entry version 97.
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; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; 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., Moyer R.W.;
RT "Complete genomic sequence of the Amsacta moorei entomopoxvirus: analysis
RT 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 occlusion
RT bodies of Choristoneura entomopoxviruses.";
RL Virology 192:179-187(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 486-648.
RX PubMed=1942245; DOI=10.1128/jvi.65.12.6516-6527.1991;
RA Hall R.L., Moyer R.W.;
RT "Identification, cloning, and sequencing of a fragment of Amsacta moorei
RT entomopoxvirus DNA containing the spheroidin gene and three vaccinia virus-
RT related open reading frames.";
RL J. Virol. 65:6516-6527(1991).
CC -!- FUNCTION: DNA-dependent ATPase required for providing the needed energy
CC to achieve the termination of early transcripts. Acts in concert with
CC the RAP94 subunit of the virion RNA polymerase and the capping
CC enzyme/VTF to catalyze release of UUUUUNU-containing nascent RNA from
CC the elongation complex. NPH-I must bind ssDNA in order to exhibit
CC ATPase activity (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC 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'-O-)-
CC methyltransferase (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Note=Virion core enzyme.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the helicase family. NPH I subfamily.
CC {ECO:0000305}.
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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 SMR; P29814; -.
DR GeneID; 1494782; -.
DR KEGG; vg:1494782; -.
DR OrthoDB; 1247at10239; -.
DR Proteomes; UP000000872; Genome.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR013676; NPHI_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45766:SF3; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A-LIKE PROTEIN 1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08469; NPHI_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome; Transcription; Virion.
FT CHAIN 1..648
FT /note="Nucleoside triphosphatase I"
FT /id="PRO_0000099099"
FT DOMAIN 48..212
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 378..541
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 467..533
FT /note="Binding to the cap-specific mRNA (nucleoside-2'-O-)-
FT methyltransferase"
FT /evidence="ECO:0000250"
FT MOTIF 150..153
FT /note="DEXH box"
FT BINDING 61..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
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
//
