NS1_MUMIM
ID NS1_MUMIM Reviewed; 672 AA.
AC P07300; P10837;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 91.
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 Murine minute virus (strain MVMi) (MVM) (Murine parvovirus).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Protoparvovirus.
OX NCBI_TaxID=10795;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3502703; DOI=10.1128/jvi.57.2.656-669.1986;
RA Astell C.R., Gardiner E.M., Tattersall P.;
RT "DNA sequence of the lymphotropic variant of minute virus of mice, MVM(i),
RT and comparison with the DNA sequence of the fibrotropic prototype strain.";
RL J. Virol. 57:656-669(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3855242; DOI=10.1093/nar/13.10.3617;
RA Sahli R., McMaster G.K., Hirt B.;
RT "DNA sequence comparison between two tissue-specific variants of the
RT autonomous parvovirus, minute virus of mice.";
RL Nucleic Acids Res. 13:3617-3633(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 of the tetranucleotide 5'TGGT3' within the origins of
CC replication (Ori), unwinds this hairpin region and nicks one DNA strand
CC thereby initiating the rolling circle replication (RCR). Cooperatively
CC binds Ori with host PIF and probably other host factors, which activate
CC the nickase function of NS1. Becomes covalently attached to the 5' end
CC of the nick and provides a 3'OH for priming DNA synthesis. The helicase
CC activity unwinds DNA in a 3'-5' direction on the longer strand.
CC Participates in the transcriptional regulation of several promoters
CC including the viral p38 promoter that regulates the expression of VP1
CC and VP2 transcripts. Inhibits the host cell cycle during the G1/S
CC transition, the S-phase, and the G2/M transition. These arrests may
CC provide essential cellular factors for viral DNA replication. Promotes
CC 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 (By similarity). Interacts
CC with human SYNCRIP. Interacts with host transcription factor SP1; this
CC interaction allows high levels of viral P38 promoter transactivation by
CC NS1 (By similarity). {ECO:0000250|UniProtKB:P03134,
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; X02481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M12032; AAA69567.1; -; Genomic_DNA.
DR SMR; P07300; -.
DR PRIDE; P07300; -.
DR Proteomes; UP000007783; Genome.
DR Proteomes; UP000104537; 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..672
FT /note="Initiator protein NS1"
FT /id="PRO_0000222465"
FT DOMAIN 373..528
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT REGION 1..276
FT /note="DNA-binding; interaction with SYNCRIP"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT REGION 191..195
FT /note="Ori-binding"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT REGION 543..672
FT /note="Transactivation"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT REGION 614..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..643
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"
FT CONFLICT 597
FT /note="I -> L (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 672 AA; 76140 MW; 25F025FE328B4DF0 CRC64;
MAGNAYSDEV LGTTNWLKEK SNQEVFSFVF KTEDVQLNGK DIGWNNYKKE LQEDELKSLQ
RGAETTWDQS EDMEWESTVD EMTKKQVFIY DSLVKKCLFE VLSTKNIAPA DVTWFVQHEW
GKDQGWHCHV LIGGKDFSQA QGKWWRRQLN VYWSRWLVTA CNVQLTPAER IKLREIAEDS
EWVTLLTYKH KQTKKDYTKC VLFGNMIAYY FLTKKKISTS PPRDGGYFLS SDSGWKTNFL
KEGERHLVSK LYTDDMRPET VETTVTTAQE TKRGRIQTKK EVSIKTTLKE LVHKRVTSPE
DWMMMQPDSY IEMMAQPGGE NLLKNTLEIC TLTLARTKTA FDLILEKAET SKLTNFSLPD
TRTCKIFAFH GWNYVKVCHA ICCVLNRQGG KRNTVLFHGP ASTGKSIIAQ AIAQAVGNVG
CYNAANVNFP FNDCTNKNLI WVEEAGNFGQ QVNQFKAICS GQTIRIDQKG KGSKQIEPTP
VIMTTNENIT VVRIGCEERP EHTQPIRDRM LNIHLTHTLP GDFGLVDKNE WPMICAWLVK
NGYQSTMASY CAKWGKVPDW SENWAEPKVP TPINSLGSAR SPFTTPKSTP LSQNYAITPL
ASDLEDLALE PWSTPNTPVA GTAETQNTGE AGSKACQDGQ LSPTWSEIEE DLRACFGAEP
LKRDFSEPLN LD
