NS1_PAVBP
ID NS1_PAVBP Reviewed; 726 AA.
AC P07296;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Bovine parvovirus (isolate pAT153/1986) (BPV).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Bocaparvovirus.
OX NCBI_TaxID=648243;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3783814; DOI=10.1128/jvi.60.3.1085-1097.1986;
RA Chen K.C., Shull B.C., Moses E.A., Lederman M., Stout E.R., Bates R.C.;
RT "Complete nucleotide sequence and genome organization of bovine
RT parvovirus.";
RL J. Virol. 60:1085-1097(1986).
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). Becomes covalently attached to the 5' end of the
CC nick and provides a 3'OH for priming DNA synthesis. The helicase
CC activity unwinds DNA in a 3'-5' direction on the longer strand.
CC Participates in the transcriptional regulation of several promoters.
CC {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; when bound to DNA.
CC {ECO:0000250|UniProtKB:Q9PZT1}.
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. The C-terminus probably contains a
CC transactivation domain. {ECO:0000250|UniProtKB:Q9PZT1}.
CC -!- SIMILARITY: Belongs to the parvoviruses initiator protein NS1 family.
CC {ECO:0000305}.
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DR EMBL; M14363; AAB59845.1; -; Genomic_DNA.
DR PIR; C26104; UYPVS1.
DR RefSeq; NP_041402.1; NC_001540.1.
DR PRIDE; P07296; -.
DR GeneID; 1724585; -.
DR KEGG; vg:1724585; -.
DR Proteomes; UP000007022; 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; DNA replication; DNA-binding; Endonuclease; Helicase;
KW Host nucleus; Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme;
KW Nuclease; Nucleotide-binding; Reference proteome; Transcription;
KW Transcription regulation; Viral DNA replication.
FT CHAIN 1..726
FT /note="Initiator protein NS1"
FT /id="PRO_0000222471"
FT DOMAIN 284..439
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT REGION 67..71
FT /note="Ori-binding"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT REGION 495..724
FT /note="Transactivation"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT REGION 507..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 85
FT /note="For nuclease activity"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 310..317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
SQ SEQUENCE 726 AA; 81189 MW; 42659A611A3AF038 CRC64;
MQPSRGLYSA LHSFKHLLIT IRQRTHAPDT VLSRDELNAW NWLQKIAQRV MRGDMDDIVD
ILKCRKANGT LVAQAINGTE FITRYMLPKN RKVADTVLTR HTTPEQSYDS TWGKTYGFAV
CNGETVSEFT RKDLWKVLYN IYTAHPAENM LNSNPSVWGD LPRVSANRID ADDAEARSRP
IKLSRKQKIM AEVIQRATDG LLLTYNDLVV HLSDLMLMLE GMPGGSKTAE QLLTMIHIKL
CAKYNAYEFM LMKTPATQNM NPGAPHYDCQ GNLVFKLLNL QGYNPWQVGH WLVMMLSKKT
GKRNSTLFYG PASTGKTNLA KAICHAVGLY GCVNHNNKQF PFNDAPNKMI LWWEECIMTT
DYVEAAKCVL GGTHVRVDVK HKDSRELPQI PVLLSSNHDV YTVVGGNATF GVHAAPLKER
ITQMNFMKQL PNTFGEITPG MISNWLSHCA HIHQEHLSLE GFAIKWDVQS VGNSFPLQTL
CPGHSQNWTF SENGVCWHCG GFIQPTPESD TDSDGDPDPD GAVAGDSDTS ANSESTVSFS
SNDSGLGSVT SSAPSVPDRA EEIEEIPSEC LEWMREEVDR LSAHDINSLA HQATGFILDP
IPEEPEEGER DLAREDAEPE ASTSHTPATK RARVEEGEPW DGTQPITEGD WIDFESRQKR
RRLEREEKGG EDEDMEVQES DPSAWGEKLG IVEKPGEEPI VLYCFETLPE SDEEGDSDKE
NKTHTV
