NS1_HBOC2
ID NS1_HBOC2 Reviewed; 776 AA.
AC B9UYK5; C6KF52;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 2.
DT 03-AUG-2022, entry version 50.
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 2 (HBoV2) (Human bocavirus type 2).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Bocaparvovirus;
OC Primate bocaparvovirus 2.
OX NCBI_TaxID=573977;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM NS1-70).
RC STRAIN=PK-5510;
RX PubMed=19072716; DOI=10.1086/595831;
RA Kapoor A., Slikas E., Simmonds P., Chieochansin T., Naeem A., Shaukat S.,
RA Alam M.M., Sharif S., Angez M., Zaidi S., Delwart E.;
RT "A newly identified bocavirus species in human stool.";
RL J. Infect. Dis. 199:196-200(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM NS1-70).
RC STRAIN=KU1;
RX PubMed=20457462; DOI=10.1016/j.virol.2010.04.014;
RA Chen A.Y., Cheng F., Lou S., Luo Y., Liu Z., Delwart E., Pintel D., Qiu J.;
RT "Characterization of the gene expression profile of human bocavirus.";
RL Virology 403:145-154(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=B9UYK5-1; Sequence=Displayed;
CC Name=NS1-70;
CC IsoId=B9UYK5-2; Sequence=VSP_059928, VSP_059929;
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; FJ170278; ACJ38931.1; -; Genomic_DNA.
DR EMBL; GQ200737; ACS74733.1; -; Genomic_DNA.
DR RefSeq; YP_002586773.1; NC_012042.1.
DR SMR; B9UYK5; -.
DR GeneID; 7755626; -.
DR KEGG; vg:7755626; -.
DR Proteomes; UP000098880; Genome.
DR Proteomes; UP000150026; 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; Covalent protein-DNA linkage;
KW DNA replication; DNA-binding; Endonuclease; Helicase; Host nucleus;
KW Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotide-binding; Transcription; Transcription regulation;
KW Viral DNA replication.
FT CHAIN 1..776
FT /note="Initiator protein NS1"
FT /id="PRO_0000445634"
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..776
FT /note="Transactivation"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT REGION 628..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..688
FT /note="Polar 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..640
FT /note="NL -> RL (in isoform NS1-70)"
FT /id="VSP_059928"
FT VAR_SEQ 641..776
FT /note="Missing (in isoform NS1-70)"
FT /id="VSP_059929"
SQ SEQUENCE 776 AA; 87000 MW; 75010BA877798278 CRC64;
MAFSAPVIRA FSQPAFTYVV KFPYENWKEE EHLLWSLLAP GTERLMIQLR NCAPHPEDDP
VREDILCSLA DQHYGAIFAK ACYIATTTLM GQKQRTPFPR CDIICQSEIG SEHLHCHILV
GGAGLSKRNA KISRATLLGL VMAELTQRCK QLLALRPFEP AEANIFHLLK RIEREAWSGH
TGNWVQILQY KDKRGDLHAQ PIDPLRFLKH YILPKNRLIS PSSKPDVCTT PDNWFILADK
TYAHTIINGL PLLEHNRKAY LQELESEVIP GPSTMAFGGR GAWEQLPEVG EQRLITSNAS
TAYKANKKEK LMLNLLDKCD ELNLLVYEDL VSACPDLLLM LEGQPGGARL IEQVLGMHHI
KVCAKYTALT FLFHLHPDQL LTSNNKALKL LLIQGYNPLQ VGHAICCVLN KQMGKQNTIC
FYGPASTGKT NFAKAIVQGV RLYGCVNHLN KGFVFNDCRQ RLIIWWEECL MHQDWVEPAK
CILGGTECRI DVKHKDSVLL QQTPVIISTN HDIYSVVGGN TVSHVHAAPL KERVLQLNFM
KQLPQTFGEI SPVEIAELLQ WCFNEYECTL TGFKQKWNLD KVPNSFPLGD LCPTHSQDYT
LHENGFCTDC GGYLPHSADD FVYTDVASET TSGDCDPGNL GDTDGEDSKS EASEVDFRPS
KKRRVISATP PSSPVSGPSL STFLDTWQSQ PRDEDELRIY EEQASQLQKN TKSTPEREEA
QLGEPQEPQP EPDPTAWGEK LGVCSSQQPG EPPVVLYCFE DLRPSDEDEG ENIGGE
