NS1_JDNVP
ID NS1_JDNVP Reviewed; 545 AA.
AC Q90054;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 61.
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=Non-structural protein 1;
DE AltName: Full=Non-structural protein NS1;
GN Name=NS1;
OS Junonia coenia densovirus (isolate pBRJ/1990) (JcDNV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Densovirinae; Ambidensovirus.
OX NCBI_TaxID=648250;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1413502; DOI=10.1016/0042-6822(92)90182-o;
RA Dumas B., Jourdan M., Pascaud A.M., Bergoin M.;
RT "Complete nucleotide sequence of the cloned infectious genome of Junonia
RT coenia densovirus reveals an organization unique among parvoviruses.";
RL Virology 191:202-222(1992).
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). {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. {ECO:0000250|UniProtKB:P03134}.
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 -!- SIMILARITY: Belongs to the parvoviruses initiator protein NS1 family.
CC {ECO:0000305}.
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DR EMBL; S47266; AAB23699.1; -; Genomic_DNA.
DR PIR; B44054; B44054.
DR RefSeq; NP_694824.1; NC_004284.1.
DR GeneID; 955411; -.
DR KEGG; vg:955411; -.
DR Proteomes; UP000008294; 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: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; IPR001257; Parvovirus_NS1_helicase.
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; Helicase; Host nucleus; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Nucleotide-binding; Reference proteome; Transcription;
KW Transcription regulation; Viral DNA replication; Viral genome packaging;
KW Viral release from host cell.
FT CHAIN 1..545
FT /note="Initiator protein NS1"
FT /id="PRO_0000222480"
FT DOMAIN 346..545
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 63462 MW; 97CD825268ABC6AE CRC64;
MNNGDTNRET DSTTRPNQDI IRESSGRTSP SEQCSMVANT SRKREWSHGG RGTMASIAKE
SQENFQYMAE ELEKMGSEFF GYVTGQSIKP SSAYISDVII LRDIQLRDQC LDVLREYGRS
RRNGLFGFSE EGDHIHVIHD CSYTNRSCRD IWISQVKPFG SVQKTGKPVK FIWEFKRTDW
YDVFIYFFVR KRGERAIYVR GESGKIPSND ECVRWTREFK EREMVSSSDC TDYYECEQQE
HKISRRSDAG SSNGRLYEKK AYSAGKFAYI RKKTKALLRK YYVSPVSAIC DVPEFRDDDL
LCDPKNRDYI QAACDDFGKD LNAMSLREIY NLLTEDYNFT DEQELNPYAL FISSMKYDNL
ENSLNIIIEL LKFQCNDDED LIVEFLTNLV NVLDRRIPKL NAFLIISPPS AGKNFFFDMI
FGLLLSYGQL GQANRHNLFA FQEAPNKRVL LWNEPNYESS LTDTIKMMFG GDPYTVRVKN
RMDAHVKRTP VIILTNNTVP FMYETAFSDR IIQYKWNAAP FLKDYELKPH PMTFFLLLSK
YNITF