NS1_AEDEV
ID NS1_AEDEV Reviewed; 849 AA.
AC P27454;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 71.
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 densonucleosis virus (strain GKV 002 002) (Aedes densovirus).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Hamaparvovirinae; Brevihamaparvovirus;
OC Dipteran brevihamaparvovirus 1.
OX NCBI_TaxID=10808;
OH NCBI_TaxID=7158; Aedes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1833875; DOI=10.1016/0042-6822(91)90780-f;
RA Afanasiev B.N., Galyov E.E., Buchatsky L.P., Kozlov Y.V.;
RT "Nucleotide sequence and genomic organization of Aedes densonucleosis
RT virus.";
RL Virology 185:323-336(1991).
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}.
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; M37899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A40784; UYPVAD.
DR PRIDE; P27454; -.
DR Proteomes; UP000008473; 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..849
FT /note="Initiator protein NS1"
FT /id="PRO_0000222478"
FT DOMAIN 594..749
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT REGION 270..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 624..631
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
SQ SEQUENCE 849 AA; 97543 MW; D4FA0980B08E152E CRC64;
MEYGLISKFY MDHWRWKIRE KHKVENNLLS TYKYILNFHY HMVHPYIRST KGGPNRVMNS
VCVEHSPCEH GNLFCECIYC WEHDGQCRGR KLDLGASTGI ERRLANDNQQ PGLSDLYCTE
TIHLATAIPE RRTIDRENYV KDFAGQTVGD LYPQLQGSTG ASEPIDFAFP TVGSGSWEIL
VRESHKHFEP NYTEEAYQSH IRSVRRRLFP EETMDNNGSQ ASTTEMLRDA VQRCGFEGPP
NSPSENNRDG IDGTCISTVD IQSNCIVNAH CPKQGTSNQT NKRKKSTDTT ESSGSKKNKS
SNYQQNLQEQ GSTSISDTID IVDGELDGST GSNRETAYYT FVLHKNNVKE DWRYIATTRA
KQAPSFITFD HGDHIHILFS SSNTGGNSTR VRTRITKFLS ATSAGSAEAT ITFSKVKFLR
NYILYCIRYG IETVNIYGNK IQQQLTEAMD TFKILFENRD PNDVILEAGC KLYHEEKKDN
KQKRCGQRKQ QNLTDIILEK IKEKKITTAQ QWENQIEPEF KIQLMKEFGL NVDSYVTRIV
RIERTRIQQL IKAKTLTEIM LEILNDEYIK HFTPGEDNSK TAKCIEWIEY LFKENNINII
HFLAWNEIIK TKRYKKINGM VLEGITNAGK SLILDNLLAM VKPEEIPRER DNSGFHLDQV
PGAGSILFEE PMITPVNVGT WKLLLEGKTI KTDVKNKDKE PIERTPTWIT TATPITNNID
MNETSQILQR IKLYILKKSI QHRDDKYTIN AQIQNKLISR PPTLIEPIHM AIVFIKNFTK
IYNLIAEEDK AHTVNEKAIQ INNEVKEEAE SWQTALQWTM TENNEEQNEN ETQALEDQVL
ELAKEQATT
