NTP1_SWPVK
ID NTP1_SWPVK Reviewed; 89 AA.
AC Q08513;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Nucleoside triphosphatase I;
DE EC=3.6.1.15;
DE AltName: Full=Nucleoside triphosphate phosphohydrolase I;
DE Short=NPH I;
DE Flags: Fragment;
GN Name=NPH1;
OS Swinepox virus (strain Kasza) (SWPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Suipoxvirus.
OX NCBI_TaxID=10277;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8249275; DOI=10.1006/viro.1993.1625;
RA Massung R.F., Jayarama V., Moyer R.W.;
RT "DNA sequence analysis of conserved and unique regions of swinepox virus:
RT identification of genetic elements supporting phenotypic observations
RT including a novel G protein-coupled receptor homologue.";
RL Virology 197:511-528(1993).
CC -!- FUNCTION: Serves two roles in transcription; it acts in concert with
CC viral termination factor/capping enzyme to catalyze release of UUUUUNU-
CC containing nascent RNA from the elongation complex, and it acts by
CC itself as a polymerase elongation factor to facilitate readthrough of
CC intrinsic pause sites. {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 -!- SIMILARITY: Belongs to the helicase family. NPH I subfamily.
CC {ECO:0000305}.
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DR EMBL; L22012; AAA16175.1; -; Unassigned_DNA.
DR SMR; Q08513; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:RHEA.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF04851; ResIII; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Nucleotide-binding; Transcription.
FT CHAIN 1..>89
FT /note="Nucleoside triphosphatase I"
FT /id="PRO_0000099097"
FT DOMAIN 42..>89
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 55..62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT NON_TER 89
SQ SEQUENCE 89 AA; 10240 MW; F550027F762EEDE6 CRC64;
MSSYHAAYID YELRVTESMT DTMGTDTEIT LKPYQHFVAS VFLGLDKMHS LLLFHDTGVG
KTITTTFIIK QLKNIYTNWS ILLLVKKHL