NS1_ADVG
ID NS1_ADVG Reviewed; 590 AA.
AC P24030;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 86.
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 Aleutian mink disease parvovirus (strain G) (ADV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Amdoparvovirus.
OX NCBI_TaxID=10783;
OH NCBI_TaxID=9665; Mustela.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2839709; DOI=10.1128/jvi.62.8.2903-2915.1988;
RA Bloom M.E., Alexandersen S., Perryman S., Lechner D., Wolfinbarger J.B.;
RT "Nucleotide sequence and genomic organization of Aleutian mink disease
RT parvovirus (ADV): sequence comparisons between a nonpathogenic and a
RT pathogenic strain of ADV.";
RL J. Virol. 62:2903-2915(1988).
RN [2]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-227 AND ASP-285.
RX PubMed=12692232; DOI=10.1128/jvi.77.9.5305-5312.2003;
RA Best S.M., Shelton J.F., Pompey J.M., Wolfinbarger J.B., Bloom M.E.;
RT "Caspase cleavage of the nonstructural protein NS1 mediates replication of
RT Aleutian mink disease parvovirus.";
RL J. Virol. 77:5305-5312(2003).
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:0000269|PubMed:12692232}.
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; M20036; AAA66612.1; -; Genomic_DNA.
DR PIR; A36760; UYPVAP.
DR RefSeq; NP_042872.1; NC_001662.1.
DR GeneID; 1494586; -.
DR KEGG; vg:1494586; -.
DR Proteomes; UP000008470; Genome.
DR GO; GO:0019034; C:viral replication complex; IDA:CACAO.
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; IPR020960; ADV_NS1-3.
DR InterPro; IPR014015; Helicase_SF3_DNA-vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001257; Parvovirus_NS1_helicase.
DR InterPro; IPR021076; Parvovirus_NS1_N.
DR Pfam; PF12475; Amdo_NSP; 2.
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 1: Evidence at protein level;
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..590
FT /note="Initiator protein NS1"
FT /id="PRO_0000222461"
FT DOMAIN 405..560
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT BINDING 432..439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 227..228
FT /note="Cleavage; by host caspase-3"
FT SITE 285..286
FT /note="Cleavage; by host caspase-3"
FT MUTAGEN 227
FT /note="D->E: Complete loss of viral replication competency,
FT when associated with E-285."
FT /evidence="ECO:0000269|PubMed:12692232"
FT MUTAGEN 227
FT /note="D->E: More than 99% loss of viral replication
FT efficiency."
FT /evidence="ECO:0000269|PubMed:12692232"
FT MUTAGEN 285
FT /note="D->E: Complete loss of viral replication efficiency,
FT when associated with E-227."
FT /evidence="ECO:0000269|PubMed:12692232"
FT MUTAGEN 285
FT /note="D->E: More than 99% loss of viral replication
FT efficiency."
FT /evidence="ECO:0000269|PubMed:12692232"
SQ SEQUENCE 590 AA; 67364 MW; 9898818AFD5343B0 CRC64;
MAQAQIDEQR RLQDLYVQLK KEINDGEGVA WLFQQKTYTD KDNKPTKATP PLRTTSSDLR
LAFDSIEENL TASNEHLTNN EINFCKLTLG KTLLLIDKHV KSHRWDSNKV NLIWQIEKGK
TQQFHIHCCL GYFDKNEDPK DVQKSLGWFM KRLNKDLAVI YSNHHCDIQD IKDPEDRAKN
LKVWIEDGPT KPYKYFNKQT KQDYNKPVHL RDYTFIYLFN KDKINTDSMD GYFAAGNGGI
VDNLTNKERK TLRKMYLDEQ SSDIMDANID WEDGQDAPKV TDQTDSATTK TGTSLIWKSC
ATKVTSKKEV ANPVQQPSKK LYSAQSTLDA LFNVGCFTPE DMIIKQSDKY LELSLEPNGP
QKINTLLHMN QVKTSTMITA FDCIIKFNEE EDDKPLLATI KDMGLNEQYL KKVLCTILTK
QGGKRGCIWF YGPGGTGKTL LASLICKATV NYGMVTTSNP NFPWTDCGNR NIIWAEECGN
FGNWVEDFKA ITGGGDVKVD TKNKQPQSIK GCVIVTSNTN ITKVTVGCVE TNAHAEPLKQ
RMIKIRCMKT INPKTKITPG MLKRWLNTWD RQPIQLSHEM PELYLGKCRW
