NS1_AADNV
ID NS1_AADNV Reviewed; 805 AA.
AC Q90185;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Aedes albopictus densovirus (isolate Boublik/1994) (AalDNV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Hamaparvovirinae; Brevihamaparvovirus;
OC Dipteran brevihamaparvovirus 1.
OX NCBI_TaxID=648330;
OH NCBI_TaxID=7160; Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8178459; DOI=10.1006/viro.1994.1239;
RA Boublik Y., Jousset F.X., Bergoin M.;
RT "Complete nucleotide sequence and genomic organization of the Aedes
RT albopictus parvovirus (AaPV) pathogenic for Aedes aegypti larvae.";
RL Virology 200:752-763(1994).
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; X74945; CAA52899.1; -; Genomic_DNA.
DR RefSeq; NP_694827.1; NC_004285.1.
DR GeneID; 955416; -.
DR KEGG; vg:955416; -.
DR Proteomes; UP000008472; 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; 2.
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..805
FT /note="Initiator protein NS1"
FT /id="PRO_0000222477"
FT DOMAIN 553..708
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT REGION 231..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 583..590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
SQ SEQUENCE 805 AA; 92645 MW; 36408B471CD476F4 CRC64;
STEYIRGINE GRVSSMESVC SEHSPCEHGN IECECIFCWE HDAQCKSRRR ELDLGEPTGS
ERGMANNYEQ SRNEDLYCTE TVPSSAALQA NTITERDIRE DFTDQTVDNI YPQLHSGSRA
SEQLEFAFPT IGTRSWEILI RQSYEHLKPD YKEEDFQSHI RRVRRQLFPE KTMDNNGSQA
STTQMLRDDI ERCGIESIAD SASEDNGDGV DGTCISTVDI QGNCIVNAHG NEQATGSKTR
KIRATTTPES SESKKHKGSN NQQNIQEQSS TTAIADGHDI VDGELDGRSE SNRETAYYTF
VLHKNNCKED WRYIATTRAK QAPSFITFDH GDHIHILFSS SNTGGNSTRV RTRITKFLSA
TSAGNAEATI TFSKVKFLRN YILYCIRYGI ETVNIYGNKI QQQLTEAMDT FKVLFENRDP
NDVILDAGCK LYHEEKKEYQ QKRCGQRKQQ NLTDIILDKI KEKKITTAQQ WENIIEPEFK
IQLMKEFGLN VDSYVQRIVR IERTRIQQII KSKTLTEIMV EILNEEYIKN FTPGEDNSKL
QNIIQWIEYM FKENNINIIH FLAWNEIIKP KRYKKINGMV LEGITNAGKS LILDNLLAMV
KPEEIPRERD NSGFHLDQLP GAGSVLFEEP MITPVNVGTW KLLLEGKTIK TDVKNKDKEP
IERTPTWITT ATPITNNVHM NETSQILQRI KLYIFKKSIQ HREDKYTINA QIQNKLISRP
PGLVEPIHMA IVFVKNFKEI YKLIEEEDNA HTVNEKAIRL SEEAKQEAEE WQTALQWNTM
EEEQKENEKQ TEDQDKESEK ETATQ
