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 04-NOV-2026, entry version 115. 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=OPG123; Synonyms=NPH1; ORFNames=D11L; OS Vaccinia virus (strain Copenhagen) (VACV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes; OC Chitovirales; 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 that acts as a 5' to 3' translocase on CC single-stranded DNA and thereby plays a role in transcription CC termination of viral early genes. Uses forward translocation in concert CC with the viral RNA polymerase RAP94/OPG109 subunit and the capping CC enzyme/VTF to catalyze release of UUUUUNU-containing nascent RNA from CC the elongation complex. In addition, acts as a positive elongation CC factor to assist transcription through problematic sequences. CC {ECO:0000250|UniProtKB:P05807}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- CC diphosphate + phosphate + H(+); 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 Evidence={ECO:0000250|UniProtKB:P05807}; CC -!- SUBUNIT: Monomer. Interacts (via C-terminus) with RAP94/OPG109 (via N- CC terminus). Interacts with the cap-specific mRNA (nucleoside-2'-O-)- CC methyltransferase OPG102. {ECO:0000250|UniProtKB:P05807}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P05807}. CC Note=Virion core enzyme. {ECO:0000250|UniProtKB:P05807}. CC -!- SIMILARITY: Belongs to the helicase family. NPH I subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M35027; AAA48110.1; -; Genomic_DNA. DR PDB; 8RQK; EM; 2.65 A; Y=1-631. DR PDB; 9FPY; EM; 2.40 A; Y=1-631. DR EMDB; EMD-19442; -. DR EMDB; EMD-50639; -. DR EMDB; EMD-50644; -. DR SMR; P20637; -. 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:ribonucleoside triphosphate phosphatase activity; ISS:UniProtKB. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR CDD; cd18785; SF2_C; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C-like. DR InterPro; IPR013676; NPHI_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000330; SNF2_N. DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; DNA-binding; Hydrolase; Late protein; KW Nucleotide-binding; Transcription; Virion. FT CHAIN 1..631 FT /note="Nucleoside triphosphatase I" FT /id="PRO_0000099091" FT DOMAIN 42..204 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 367..532 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 457..524 FT /note="Binding to the cap-specific mRNA (nucleoside-2'-O-)- FT methyltransferase" FT /evidence="ECO:0000250" FT MOTIF 141..144 FT /note="DEXH box" FT BINDING 55..62 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT HELIX 5..15 FT /evidence="ECO:0007829|PDB:9FPY" FT TURN 16..18 FT /evidence="ECO:0007829|PDB:8RQK" FT STRAND 21..30 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 33..44 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 50..55 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:8RQK" FT HELIX 61..70 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 71..74 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 79..85 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 91..95 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 96..101 FT /evidence="ECO:0007829|PDB:9FPY" FT TURN 106..108 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 110..116 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 119..128 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 135..142 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 143..151 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 155..157 FT /evidence="ECO:0007829|PDB:8RQK" FT HELIX 162..174 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 178..182 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 192..201 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 202..206 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 212..218 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 220..226 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 248..251 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 253..262 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 265..281 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 284..286 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 288..295 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 320..325 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 335..341 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 352..364 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 366..377 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 379..385 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 389..391 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 393..404 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 408..412 FT /evidence="ECO:0007829|PDB:8RQK" FT HELIX 419..426 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 434..436 FT /evidence="ECO:0007829|PDB:8RQK" FT STRAND 439..442 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 454..460 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 467..478 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 480..483 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 484..486 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 492..501 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 503..505 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 509..533 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 536..542 FT /evidence="ECO:0007829|PDB:9FPY" FT HELIX 555..559 FT /evidence="ECO:0007829|PDB:9FPY" FT STRAND 569..586 FT /evidence="ECO:0007829|PDB:8RQK" FT STRAND 593..598 FT /evidence="ECO:0007829|PDB:8RQK" FT STRAND 602..604 FT /evidence="ECO:0007829|PDB:8RQK" FT STRAND 606..613 FT /evidence="ECO:0007829|PDB:8RQK" FT STRAND 620..622 FT /evidence="ECO:0007829|PDB:8RQK" FT STRAND 624..626 FT /evidence="ECO:0007829|PDB:8RQK" FT STRAND 628..630 FT /evidence="ECO:0007829|PDB:8RQK" 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 //