NS1_FPV19
ID NS1_FPV19 Reviewed; 668 AA.
AC P24842;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Initiator protein NS1 {ECO:0000250|UniProtKB:P03134};
DE Short=NS1;
DE EC=3.1.21.- {ECO:0000250|UniProtKB:Q9PZT1};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q9PZT1};
DE AltName: Full=NCVP1;
DE AltName: Full=Non-capsid protein NS-1;
DE AltName: Full=Non-structural protein 1;
DE AltName: Full=Non-structural protein NS1;
GN Name=NS1;
OS Feline panleukopenia virus (strain 193) (FPV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX NCBI_TaxID=10787;
OH NCBI_TaxID=9681; Felidae (cat family).
OH NCBI_TaxID=9651; Nasua nasua (Ring-tailed coati).
OH NCBI_TaxID=9654; Procyon lotor (Raccoon).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=193/70;
RX PubMed=2174965; DOI=10.1099/0022-1317-71-11-2747;
RA Martyn J.C., Davidson B.E., Studdert M.J.;
RT "Nucleotide sequence of feline panleukopenia virus: comparison with canine
RT parvovirus identifies host-specific differences.";
RL J. Gen. Virol. 71:2747-2753(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CU-4;
RX PubMed=1647068; DOI=10.1016/0042-6822(91)90132-u;
RA Parrish C.R.;
RT "Mapping specific functions in the capsid structure of canine parvovirus
RT and feline panleukopenia virus using infectious plasmid clones.";
RL Virology 183:195-205(1991).
CC -!- FUNCTION: Multifunctional protein which displays endonuclease and
CC helicase activities required for initiating and directing viral DNA
CC replication. Also plays a role in viral packaging and transactivation
CC of several promoters. Binds site-specifically to 2-3 approximate tandem
CC copies within the origins of replication (Ori), unwinds this hairpin
CC region and nicks one DNA strand thereby initiating the rolling circle
CC replication (RCR). Cooperatively binds Ori with host PIF and probably
CC other host factors, which activate the nickase function of NS1. Becomes
CC covalently attached to the 5' end of the nick and provides a 3'OH for
CC priming DNA synthesis. The helicase activity unwinds DNA in a 3'-5'
CC direction on the longer strand. Inhibits the host cell cycle during the
CC G1/S transition, the S-phase, and the G2/M transition. These arrests
CC may provide essential cellular factors for viral DNA replication.
CC Promotes apoptosis in host cell. {ECO:0000250|UniProtKB:P03134}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:P03134};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P03134};
CC Note=The endonuclease active site can probably bind other divalent
CC cations. {ECO:0000250|UniProtKB:P03134};
CC -!- SUBUNIT: Homooligomer; when bound to DNA.
CC {ECO:0000250|UniProtKB:Q9PZT1}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:D0EZM8}.
CC -!- DOMAIN: In the N-terminus, the endonuclease region is involved in
CC binding to the origin of replication. In the middle, there are the
CC ATPase and helicase activities (By similarity). The C-terminus probably
CC contains a transactivation domain (By similarity).
CC {ECO:0000250|UniProtKB:P03134, ECO:0000250|UniProtKB:Q9PZT1}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:P03134}.
CC -!- SIMILARITY: Belongs to the parvoviruses initiator protein NS1 family.
CC {ECO:0000305}.
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DR EMBL; X55115; CAA38910.1; -; Genomic_DNA.
DR EMBL; M38246; AAC37927.1; -; Genomic_DNA.
DR PIR; A36608; UYPVFP.
DR SMR; P24842; -.
DR Proteomes; UP000002478; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0039645; P:modulation by virus of host G1/S transition checkpoint; IEA:UniProtKB-KW.
DR GO; GO:0039592; P:suppression by virus of G2/M transition of host mitotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014015; Helicase_SF3_DNA-vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR021972; Parvovirus_NS1_C.
DR InterPro; IPR001257; Parvovirus_NS1_helicase.
DR InterPro; IPR021076; Parvovirus_NS1_N.
DR Pfam; PF12117; NS1_C; 1.
DR Pfam; PF01057; Parvo_NS1; 1.
DR Pfam; PF12433; PV_NSP1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51206; SF3_HELICASE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding; Covalent protein-DNA linkage; DNA replication; DNA-binding;
KW Endonuclease; G1/S host cell cycle checkpoint dysregulation by virus;
KW Helicase; Host G2/M cell cycle arrest by virus; Host nucleus;
KW Host-virus interaction; Hydrolase; Magnesium; Metal-binding;
KW Modulation of host cell apoptosis by virus;
KW Modulation of host cell cycle by virus; Nuclease; Nucleotide-binding;
KW Transcription; Transcription regulation; Viral DNA replication;
KW Viral genome packaging; Viral release from host cell.
FT CHAIN 1..668
FT /note="Initiator protein NS1"
FT /id="PRO_0000222463"
FT DOMAIN 367..529
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT REGION 1..277
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT REGION 193..197
FT /note="Ori-binding"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT ACT_SITE 212
FT /note="For nuclease activity"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 121
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 129
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 131
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 400..407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT CONFLICT 23
FT /note="N -> D (in Ref. 2; AAC37927)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="I -> V (in Ref. 2; AAC37927)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="I -> N (in Ref. 2; AAC37927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 668 AA; 76768 MW; 4F8FEA3EE62D2AE7 CRC64;
MSGNQYTEEV MEGVNWLKKH AENEAFSFVF KCDNVQLNGK DVRWNNYTKP IQNEELTSLI
RGAQTAMDQT EEEEMDWESE VDSLAKKQVQ TFDALIKKCL FEVFVSKNIE PNECVWFIQH
EWGKDQGWHC HVLLHSKNLQ QATGKWLRRQ MNMYWSRWLV TLCSVNLTPT EKIKLREIAE
DSEWVTILTY RHKQTKKDYV KMVHFGNMIA YYFLTKKKIV HMTKESGYFL STDSGWKFNF
MKYQDRHTVS TLYTEQMKPE TVETTVTTAQ ETKRGRIQTK KEVSIKCTLR DLVSKRVTSP
EDWMMLQPDS YIEMMAQPGG ENLLKNTLEI CTLTLARTKT AFELILEKAD NTKLTNFDLA
NSRTCQIFRM HGWNWIKVCH AIACVLNRQG GKRNTVLFHG PASTGKSIIA QAIAQAVGNV
GCYNAANVNF PFNDCTNKNL IWIEEAGNFG QQVNQFKAIC SGQTIRIDQK GKGSKQIEPT
PVIMTTNENI TIVRIGCEER PEHTQPIRDR MLNIKLVCKL PGDFGLVDKE EWPLICAWLV
KHGYQSTMAN YTHHWGKVPE WDENWAEPKI QEGIISPGCK DLETQAASNP QSQDHVLTPL
TPDVVDLALE PWSTPDTPIA ETANQQSNQL GVTHKDVQAS PTWSEIEADL RAIFTSEQLE
EDFRDDLD
