NS1_FPV
ID NS1_FPV Reviewed; 392 AA.
AC P06431;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, 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;
DE Flags: Fragment;
GN Name=NS1;
OS Feline panleukopenia virus (FPV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX NCBI_TaxID=10786;
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].
RX PubMed=2991581; DOI=10.1128/jvi.55.3.574-582.1985;
RA Carlson J., Rushlow K., Maxwell I., Maxwell F., Winston S., Hahn W.;
RT "Cloning and sequence of DNA encoding structural proteins of the autonomous
RT parvovirus feline panleukopenia virus.";
RL J. Virol. 55:574-582(1985).
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; M10824; AAA47160.1; -; Genomic_DNA.
DR PIR; A03697; UYPV1F.
DR SMR; P06431; -.
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 Pfam; PF12117; NS1_C; 1.
DR Pfam; PF01057; Parvo_NS1; 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..392
FT /note="Initiator protein NS1"
FT /id="PRO_0000222462"
FT DOMAIN 91..253
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT BINDING 124..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT NON_TER 1
SQ SEQUENCE 392 AA; 43971 MW; B875ADDB4977F616 CRC64;
IQTKKEVSIK CTLRDLVSKR VTSPEDWMML QPDSYIEMMA QPGGENLLKN TLEICTLTLA
RTKTAFELIL EKANNTKLTN FDLANSRTCQ IFRMHGWNWI KVCHAIACVL NRQGGKRNTV
LFHGPASTGK SIIAQAIAQA VGNVGCYNAA NVNFPFNDCT NKNLIWIEEA GNFGQQVNQF
KAICSGQTIR IDQKGKGSKQ IEPTPVIMTT NENITIVRIG CEERPEHTQP IRDRMLNIKL
VCKLPGDFGL VDKEEWPLIC AWLVKHGYES TMANYTHHWG KVPEWDENWA EPKIQEGVNS
PGCKDLETQA ASNPQSQDHV LTPLTPDVVD LALEPWSTPD TPIAETANQQ SNQLGVTHKD
VQASPTWSEI EADLRAIFTS EQLEEDFRDD LD
