NS1_PAVL3
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 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 Parvovirus LuIII.
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
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 + 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}.
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; M81888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A44276; A44276.
DR SMR; P36311; -.
DR Proteomes; UP000007898; 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_0000222469"
FT DOMAIN 373..528
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT REGION 1..276
FT /note="DNA-bindin"
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 COMPBIAS 611..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 210
FT /note="For nuclease activity"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 119
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 127
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 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
