ID   NS1_DSDNV               Reviewed;         545 AA.
AC   O71153;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   23-FEB-2022, entry version 59.
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   Diatraea saccharalis densovirus (DsDNV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC   Piccovirales; Parvoviridae; Densovirinae; unclassified Densovirinae.
OX   NCBI_TaxID=72003;
OH   NCBI_TaxID=40085; Diatraea saccharalis (sugarcane borer).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Boublik Y., Kouassi K.N., Cavallaro C., Bergoin M.;
RT   "Complete nucleotide sequence and genome organization of an infectious
RT   clone of Diatraea saccharalis densovirus (DsDNV).";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
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; AF036333; AAC17999.1; -; Genomic_DNA.
DR   RefSeq; NP_046813.1; NC_001899.1.
DR   GeneID; 1449608; -.
DR   KEGG; vg:1449608; -.
DR   Proteomes; UP000007205; 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; Transcription; Transcription regulation;
KW   Viral DNA replication; Viral genome packaging;
KW   Viral release from host cell.
FT   CHAIN           1..545
FT                   /note="Initiator protein NS1"
FT                   /id="PRO_0000222479"
FT   DOMAIN          346..545
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..39
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  63476 MW;  810A0E440432E2B1 CRC64;
     MNNGDSNRET DSTTRSDQSN LRESPTRSPS SEQCSMVATT SRKREWAYGG RGTMASLAKE
     SQENFQYMAE ELEKMGNQFF GYVTGQSVKP SSAYISDVII LRDIQLRDQC LDVLREYGRS
     RRNGLFGFSE EGDHIHVIHD CSYTNRSCRD IWLGQVKPFG TVQKTGKPVK YIWEFKRTDW
     YDVFIYFFIR KRGERAIYIR GESGKIPSND ECVRWAREFK EREMVSSSDC TDYYECEQQE
     HKISRRSDAG STNGRLYEKK TYSAGKFAYI RQKTKALLRK YYVSPISAIC DVPEFRDDDL
     LCDPKNRDYI QAACEDFGKD LNAMSLREIY NLLTEDYNFT DDKELNPYAQ FISSMKYDNL
     EGSLNIVNEL LKYQCNDDED LIVEFLTNLV NVLDRRIPKL NAFLIISPPS GGKNFFFDMI
     FGLLLSYGQL GQANRHNLFA FQEAPNKRVL LWNEPNYESS LTDTIKMMFG GDPYTVRVKN
     RMDAHVKRTP VIILTNNTVP FMYELAFSDR IIQYKWNAAP FLKDYELKPH PMTFFLLLSK
     YNITF