NS1_PAVPK
ID NS1_PAVPK Reviewed; 662 AA.
AC P52502;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 75.
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 Porcine parvovirus (strain Kresse) (PPV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX NCBI_TaxID=73487;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8642680; DOI=10.1128/jvi.70.4.2508-2515.1996;
RA Bergeron J., Hebert B., Tijssen P.;
RT "Genome organization of the Kresse strain of porcine parvovirus:
RT identification of the allotropic determinant and comparison with those of
RT NADL-2 and field isolates.";
RL J. Virol. 70:2508-2515(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8212598; DOI=10.1006/viro.1993.1569;
RA Bergeron J., Menezes J., Tijssen P.;
RT "Genomic organization and mapping of transcription and translation products
RT of the NADL-2 strain of porcine parvovirus.";
RL Virology 197:86-98(1993).
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; U44978; AAC40229.1; -; Genomic_DNA.
DR EMBL; L23427; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR PIR; A36217; UYPVNA.
DR RefSeq; NP_757369.1; NC_001718.1.
DR SMR; P52502; -.
DR GeneID; 1489594; -.
DR KEGG; vg:1489594; -.
DR Proteomes; UP000000468; 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..662
FT /note="Initiator protein NS1"
FT /id="PRO_0000222472"
FT DOMAIN 372..527
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT REGION 2..275
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT REGION 192..196
FT /note="Ori-binding"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT ACT_SITE 211
FT /note="For nuclease activity"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 120
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 128
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 130
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 398..405
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
SQ SEQUENCE 662 AA; 75591 MW; B53F76D9F9FBD613 CRC64;
MAAGNTYSEE VLKATNWLQD NAQKEAFSYV FKTQKVNLNG KEIAWNNYNK DTTDAEMINL
QRGAETSWDQ ATDMEWESEI DSLTKRQVLI FDSLVKKCLF EGILQKNLSP SDCYWFIQHE
HGQDTGYHCH VLLGGKGLQQ AMGKWFRKQL NNLWSRWLIM QCKVPLTPVE RIKLRELAED
GEWVSLLTYT HKQTKKQYTK MTHFGNMIAY YFLNKKRKTT EREHGYYLSS DSGFMTNFLK
EGERHLVSHL FTEANKPETV ETTVTTAQEA KRGRIQTKKE VSIKCTIRDL VNKRCTSIED
WMMTDPDSYI EMMAQTGGEN LIKNTLEITT LTLARTKTAY DLILEKAKPS MLPTFNISNT
RTCKIFSMHN WNYIKVCHAI TCVLNRQGGK RNTILFHGPA STGKSIIAQH IANLVGNVGC
YNAANVNFPF NDCTNKNLIW IEEAGNFSNQ VNQFKAICSG QTIRIDQKGK GSKQIEPTPV
IMTTNEDITK VRIGCEERPE HTQPIRDRML NINLTRKLPG DFGLLEETEW PLICAWLVKK
GYQATMASYM HHWGNVPDWS EKWEEPKMQT PINTPTDSQI STSVKTSPAD NNYAATPIQE
DLDLALALEP WSEPTTPTFT NLHLTPTPPD SAIRTPSPTW SEIETDIRAC FGENCAPTTN
LE
