NS1_HBOC4
ID NS1_HBOC4 Reviewed; 776 AA.
AC C5IY43; C5IY44;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
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 4 (HBoV4) (Human bocavirus type 4).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Bocaparvovirus;
OC Primate bocaparvovirus 2.
OX NCBI_TaxID=1511883;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS NS1 AND NS1-70).
RC STRAIN=HBoV4-NI-385;
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=C5IY43-1; Sequence=Displayed;
CC Name=NS1-70;
CC IsoId=C5IY43-2; Sequence=VSP_059932, VSP_059933;
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}.
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; FJ973561; ACR15778.1; -; Genomic_DNA.
DR EMBL; FJ973561; ACR15779.1; -; Genomic_DNA.
DR RefSeq; YP_002916059.1; NC_012729.2. [C5IY43-1]
DR RefSeq; YP_002916060.1; NC_012729.2. [C5IY43-2]
DR SMR; C5IY43; -.
DR DNASU; 7922600; -.
DR GeneID; 7922600; -.
DR GeneID; 7922604; -.
DR KEGG; vg:7922600; -.
DR KEGG; vg:7922604; -.
DR Proteomes; UP000106086; 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_0000445636"
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 627..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..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_059932"
FT VAR_SEQ 641..776
FT /note="Missing (in isoform NS1-70)"
FT /id="VSP_059933"
SQ SEQUENCE 776 AA; 86782 MW; 9FD1A230343484DB CRC64;
MAFSAPVLRA FSQPTFTYVI KFPYNNWKED EHLLWSLLAP GTESLMIQLK NCAPHPEDDP
IREDILCSLA DLHYGAVFAK ACYIATSTLM GQKQRTLFPR CDIVCQSEIG SDFLHCHILV
GGAGLSKRNA KISRATLLGL VMAELTQRCK LLLAHRPFEP AEATIYHELK RIEREAWSGH
TGNWVQILQY KDKRGDLHAQ PIDPLRFLKH YILPKNRLIS PSSKPDVCTS PDNWFILADK
TYSHTIINGL PLLERNRKAY LQELESEVIP GPSAMAFGGR GAWEQLPEVG EQRLITSNTS
TAYKANKKEK LMLNLLDKCD ELNLLVYEDL VSACPDLLLM LEGQPGGARL IEQVLGMHHI
KVCAKHTALS FLFHLHPDQL LTSSNKALKL LLIQGYNPLQ VGHAICCVLN KQMGKQNTIC
FYGPASTGKT NFAKAIVQGV RLYGCVNHLN KGFVFNDCRQ RLIIWWEECL MHQDWVEPAK
CILGGTECRI DVKHKDSVLL QQTPVIISTN HDIYSVVGGN TVSHVHAAPL KERVLQLNFM
KQLPQTFGEI SPSEIAELLQ WCFNEYDCTL AGFKQKWNLD KVPNSFPIGD LCPTHSQDFT
LHENGFCSDC GGYLPHSADD SVYTDVASET TSGDYDPGNL GDTDGEDSKS EASEVDYCPP
KKRRVISATP PNSPVSGPSL STFLDTWQSQ PRDDDELRIY EEQASQFQKN TKSTSEREEA
QLGESQEPQP EPDPTAWGEK LGVCSSQQPG QPPIVLYCFE DLRPSDEDEG ENIGGD
