ID   NS1_PAVL3               Reviewed;         668 AA.
AC   P36311;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   04-NOV-2026, entry version 90.
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   Parvovirus LuIII.
OC   Viruses; Floreoviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC   Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus;
OC   Protoparvovirus rodent1.
OX   NCBI_TaxID=35339;
OH   NCBI_TaxID=9989; Rodentia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8517025; DOI=10.1006/viro.1993.1040;
RA   Diffoot N., Chen K.C., Bates R.C., Lederma M.;
RT   "The complete nucleotide sequence of parvovirus LuIII and localization of a
RT   unique sequence possibly responsible for its encapsidation pattern.";
RL   Virology 192:339-345(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 + phosphate + H(+); 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; M81888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A44276; A44276.
DR   SMR; P36311; -.
DR   GO; GO:0042025; C:host cell nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
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:0039592; P:symbiont-mediated arrest of host cell cycle during G2/M transition; IEA:UniProtKB-KW.
DR   GO; GO:0052150; P:symbiont-mediated perturbation of host apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0039645; P:symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   FunFam; 3.40.50.300:FF:003160; Initiator protein NS1; 1.
DR   Gene3D; 3.40.1310.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   InterPro; IPR049901; PV_NS1-NUC.
DR   Pfam; PF12117; NS1_C; 1.
DR   Pfam; PF01057; Parvo_NS1; 1.
DR   Pfam; PF12433; PV_NSP1; 1.
DR   SUPFAM; SSF55464; Origin of replication-binding domain, RBD-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS52022; PV_NS1_NUC; 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_0000222469"
FT   DOMAIN          21..259
FT                   /note="PV NS1-Nuc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01366"
FT   DOMAIN          373..528
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   REGION          1..276
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03134"
FT   REGION          191..195
FT                   /note="Ori-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P03134"
FT   REGION          543..668
FT                   /note="Transactivation"
FT                   /evidence="ECO:0000250|UniProtKB:P03134"
FT   REGION          571..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          605..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           127..129
FT                   /note="RCR-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01366"
FT   MOTIF           210..214
FT                   /note="RCR-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01366"
FT   COMPBIAS        571..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        210
FT                   /note="For nuclease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01366"
FT   BINDING         119
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01366"
FT   BINDING         127
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01366"
FT   BINDING         129
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01366"
FT   BINDING         399..406
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
SQ   SEQUENCE   668 AA;  75846 MW;  CAE69049F8F86B53 CRC64;
     MAGNAYSDEV LGTTNWLKDK SNQEVFSFVF KNEDVQLNGK NIGWNSYRKE LQEEELKSLQ
     RGAETTWDQS EDMEWESSVD ELTKKQVFIF DSLVKKCLFE VLSTKNIAPS DVTWFVQHEW
     GKDQGWHCHV LIGGKNFSQA QGKWWRRQLN VYWSRWLVTA CSVQLSPAER IKLREIAEDQ
     EWVTLLTYKH KQTKKDYTKC VCFGNMVAYY FLTKKKICTS PPRDGGYFLS SDSGWKTNFL
     KEGERHLVSK LYTDDMRPET VETTVTTAQE TKRGRIQTKK EVSIKTTLKE LVHKRVTSPE
     DWMMMQPDSY IEMMAQPGGE NLLKNTLEIC TLTLARTKTA FDLILEKAET SKLTNFLLAD
     TRTCRIFAFH GWNYIKVCHA ICCVLNRQGG KRNTVLFHGP ASTGKSIIAQ AIAQAVGNVG
     CYNAANVNFP FNDCTNKNLI WVEEAGNFGQ QVNQFKAICS GQTIRIDQKG KGSKQIEPTP
     VIMTTNENIT VVKIGCEERP EHTQPIRDRM LNIHLTHTLP GDFGLVDKNE WPMICAWLVK
     NGYQSTMASY CAKWGKVPDW TENWAEPKVT TEINSVGSTN SPSPKSTPLS QNYALTPSDL
     EDLALEPWST PSTPVVGTVK TPNTGETGST ACQEAQRSPT WSEIEEDLRA CFSSEHWKSD
     SEQLPNLD
//