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Database: UniProt
Entry: P20637
LinkDB: P20637
Original site: P20637 
ID   NTP1_VACCC              Reviewed;         631 AA.
AC   P20637;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   18-SEP-2019, entry version 89.
DE   RecName: Full=Nucleoside triphosphatase I;
DE            EC=3.6.1.15;
DE   AltName: Full=Factor X;
DE   AltName: Full=NPH-I;
DE   AltName: Full=Nucleoside triphosphate phosphohydrolase I;
DE            Short=NPH I;
GN   Name=NPH1; ORFNames=D11L;
OS   Vaccinia virus (strain Copenhagen) (VACV).
OC   Viruses; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10249;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2219722; DOI=10.1016/0042-6822(90)90294-2;
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "The complete DNA sequence of vaccinia virus.";
RL   Virology 179:247-266(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Goebel S.J., Johnson G.P., Perkus M.E., Davis S.W., Winslow J.P.,
RA   Paoletti E.;
RT   "Appendix to 'The complete DNA sequence of vaccinia virus'.";
RL   Virology 179:517-563(1990).
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 J3 (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; M35027; AAA48110.1; -; Genomic_DNA.
DR   Proteomes; UP000008269; 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; 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   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   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; Late protein;
KW   Nucleotide-binding; Transcription; Virion.
FT   CHAIN         1    631       Nucleoside triphosphatase I.
FT                                /FTId=PRO_0000099091.
FT   DOMAIN       42    204       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      367    532       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND      55     62       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION      457    524       Binding to the cap-specific mRNA
FT                                (nucleoside-2'-O-)-methyltransferase.
FT                                {ECO:0000250}.
FT   MOTIF       141    144       DEXH box.
SQ   SEQUENCE   631 AA;  72366 MW;  3DD5980D16E91553 CRC64;
     MSKSHAAYID YALRRTTNMP VEMMGSDVVR LKDYQHFVAR VFLGLDSMHS LLLFHETGVG
     KTMTTVYILK HLKDIYTNWA IILLVKKALI EDPWMNTILR YAPEITKDCI FINYDDQNFR
     NKFFTNIKTI NSKSRICVII DECHNFISKS LIKEDGKIRP TRSVYNFLSK TIALKNHKMI
     CLSATPIVNS VQEFTMLVNL LRPGSLQHQS LFENKRLVDE KELVSKLGGL CSYIVNNEFS
     IFDDVEGSAS FAKKTVLMRY VNMSKKQEEI YQKAKLAEIK TGISSFRILR RMATTFTFDS
     FPERQNRDPG EYAQEIATLY NDFKNSLRNR EFSKSALDTF KKGELLKGDA SAADISLFTE
     LKEKSVKFID VCLGILASHG KCLVFEPFVN QSGIEILLLY FKVFGISNIE FSSRTKDTRI
     KAVAEFNQES NTNGECIKTC VFSSSGGEGI SFFSINDIFI LDMTWNEASL RQIVGRAIRL
     NSHVLTPPER RYVNVHFIMA RLSNGMPTVD EDLFEIIQSK SKEFVQLFRV FKHTSLEWIH
     ANEKDFSPID NESGWKTLVS RAIDLSSKKN ITNKLIEGTN IWYSNSNRLM SINRGFKGVD
     GRVYDVDGNY LHDMPDNPVI KIHDGKLIYI F
//
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