NS1_HBOC3
ID NS1_HBOC3 Reviewed; 780 AA.
AC C5IY48; C1IWT0;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 40.
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 Human bocavirus 3 (HBoV3) (Adelavirus W471).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Bocaparvovirus;
OC Primate bocaparvovirus 1.
OX NCBI_TaxID=638313;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM NS1-70).
RC STRAIN=W471;
RA Arthur J.L., Higgins G.D., Davidson G.P., Givney R.C., Ratcliff R.M.;
RT "A Novel Bocavirus Associated with Acute Gastroenteritis in Australian
RT Children.";
RL PLoS Pathog. 5:E1000391-E1000391(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM NS1).
RC STRAIN=HBoV3B-TU-A-210-07 {ECO:0000312|EMBL:ACR15784.1};
RX PubMed=20415538; DOI=10.1086/652416;
RA Kapoor A., Simmonds P., Slikas E., Li L., Bodhidatta L., Sethabutr O.,
RA Triki H., Bahri O., Oderinde B.S., Baba M.M., Bukbuk D.N., Besser J.,
RA Bartkus J., Delwart E.;
RT "Human bocaviruses are highly diverse, dispersed, recombination prone, and
RT prevalent in enteric infections.";
RL J. Infect. Dis. 201:1633-1643(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=NS1;
CC IsoId=C5IY48-1; Sequence=Displayed;
CC Name=NS1-70;
CC IsoId=C5IY48-2; Sequence=VSP_059930, VSP_059931;
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; FJ973562; ACR15784.1; -; Genomic_DNA.
DR EMBL; EU918736; ACH81927.1; -; Genomic_DNA.
DR RefSeq; YP_002808454.1; NC_012564.1. [C5IY48-2]
DR SMR; C5IY48; -.
DR GeneID; 7768240; -.
DR KEGG; vg:7768240; -.
DR Proteomes; UP000128541; Genome.
DR Proteomes; UP000143135; 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 Alternative splicing; ATP-binding; Coiled coil;
KW Covalent protein-DNA linkage; DNA replication; DNA-binding; Endonuclease;
KW Helicase; Host nucleus; Hydrolase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nuclease; Nucleotide-binding; Transcription;
KW Transcription regulation; Viral DNA replication.
FT CHAIN 1..780
FT /note="Initiator protein NS1"
FT /id="PRO_0000445635"
FT DOMAIN 397..552
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT REGION 193..197
FT /note="Ori-binding"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT REGION 606..780
FT /note="Transactivation"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT REGION 627..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..780
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /note="For nuclease activity"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 108
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 115
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 117
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT BINDING 423..430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT VAR_SEQ 639..661
FT /note="DLGDTDGEDSESEASEVGVRPSK -> KFTFSKHFIYILYTTLKHMFNYR
FT (in isoform NS1-70)"
FT /id="VSP_059930"
FT VAR_SEQ 662..780
FT /note="Missing (in isoform NS1-70)"
FT /id="VSP_059931"
SQ SEQUENCE 780 AA; 87867 MW; 0527F2F648AB001A CRC64;
MAFNPPVIRA FSSPAFTYVF KFPYPSWKEK EWLLHALLAH GTEQAMIQLR NCVPHPDEDI
IRDDLLLSLE DRHFGAILCK AVYMATTTFM SQKQRNMFPR CDIIVQSELG ETNLHCHIIV
GGEGLSKRNA KTSCPQLYGL ILGELIQRCK TLLATRPFEP EEAEIYHALK RAEREAWGGV
TSGNLQILQY RDRRGDLHAQ QVDALRFFKN YLLPKNRCIT SYSRPDVCTS PENWFVLAEK
TYCHTLVNGL PLPEHYRKHY HATLDNEVLP GPQTMAFGGR GPWEHLPEVG DQRLAASSVS
TTYKPNKKEK LMLNLLDKCS ELNLLVYEDL VANCPELLLM LEGQPGGARL IEQVLGMHHI
NVCSNFTALS YLFHLYPGTT LSSDNKALQL LLIQGYNPLM VGHALCCVLN KQFGKQNTVC
FYGPASTGKT NMAKAIVQGI RLYGCVNHLN KGFVFNDCRQ RLVVWWEECL MHQDWVEPAK
CILGGTECRI DVKHRDSVLL TQTPVIISTN HDIYAVVGGN SVSHVHAAPL KERVIQLNFM
KQLPQTFGEI TPEEIAALLQ WCFNEYECTL TGFKTKWSLD KIPNSFPLGV LCPTHSQDFI
LHENGYCTDC GGYLAHSADD SVYTDRASDT SKEAIDAGDL GDTDGEDSES EASEVGVRPS
KKRRITIPAT PPNSPGSSVS TSAFFDNWCA QPRDEDELRE YERQASRLQK KRESRERREE
TPMATSSQES ESEPNPTQWG DKLGVIPSGT PDQPPIVLHC FEDLRPSDED EGEYIGKERL
