NS1_HBOC1
ID NS1_HBOC1 Reviewed; 781 AA.
AC D0EZM8; A0A068B244; A0A1L2DWK9; A0A384KU82; H9CWJ3; J9RYC4; J9SK89; Q3YPH6;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 34.
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 Primate bocaparvovirus 1 (strain Human bocavirus 1 type 1) (HBoV1) (Human
OS bocavirus type 1).
OC Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC Piccovirales; Parvoviridae; Parvovirinae; Bocaparvovirus;
OC Primate bocaparvovirus 1.
OX NCBI_TaxID=689403;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM NS1-70).
RC STRAIN=St2;
RX PubMed=16118271; DOI=10.1073/pnas.0504666102;
RA Allander T., Tammi M.T., Eriksson M., Bjerkner A., Tiveljung-Lindell A.,
RA Andersson B.;
RT "Cloning of a human parvovirus by molecular screening of respiratory tract
RT samples.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12891-12896(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS NS1 AND NS1-70), SUBCELLULAR
RP LOCATION, AND ALTERNATIVE SPLICING.
RC STRAIN=KU2;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS NS1 AND NS1-70).
RC STRAIN=KU3, and Salvador1;
RX PubMed=22956907; DOI=10.1371/journal.ppat.1002899;
RA Huang Q., Deng X., Yan Z., Cheng F., Luo Y., Shen W., Lei-Butters D.C.,
RA Chen A.Y., Li Y., Tang L., Soderlund-Venermo M., Engelhardt J.F., Qiu J.;
RT "Establishment of a reverse genetics system for studying human bocavirus in
RT human airway epithelia.";
RL PLoS Pathog. 8:E1002899-E1002899(2012).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM NS1-70).
RC STRAIN=307AR09;
RA Cardozo Tomas A., Ghietto L.M., Insfran C., Adamo M.P.;
RT "Complete genome sequence of HBoV1 isolated form a child with pneumonia in
RT Cordoba, Argentina.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM NS1-70), AND ALTERNATIVE
RP SPLICING.
RC STRAIN=Eg/BSU-1;
RA Abdel-Moneim A.S., Kamel M.M., Hassan N.M.;
RT "Evolutionary and genetic analysis of human bocavirus genotype-1 strains
RT reveals an evidence of intragenomic recombination.";
RL J. Med. Microbiol. 0:0-0(2017).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-271, AND DOMAIN.
RX PubMed=23966383; DOI=10.1128/jvi.01770-13;
RA Tewary S.K., Zhao H., Shen W., Qiu J., Tang L.;
RT "Structure of the NS1 protein N-terminal origin recognition/nickase domain
RT from the emerging human bocavirus.";
RL J. Virol. 87:11487-11493(2013).
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:0000269|PubMed:20457462}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=NS1;
CC IsoId=D0EZM8-1; Sequence=Displayed;
CC Name=NS1-70;
CC IsoId=D0EZM8-2; Sequence=VSP_059926, VSP_059927;
CC Name=NS2;
CC IsoId=D0EZM8-3; Sequence=VSP_059925;
CC Name=NS3;
CC IsoId=D0EZM8-4; Sequence=VSP_059924;
CC Name=NS4;
CC IsoId=D0EZM8-5; Sequence=VSP_059924, VSP_059925;
CC -!- DOMAIN: In the N-terminus, the endonuclease region is involved in
CC binding to the origin of replication (PubMed:23966383). In the middle,
CC there are the ATPase and helicase activities (By similarity). The C-
CC terminus probably contains a transactivation domain (By similarity).
CC {ECO:0000250|UniProtKB:Q9PZT1, ECO:0000269|PubMed:23966383}.
CC -!- SIMILARITY: Belongs to the parvoviruses initiator protein NS1 family.
CC {ECO:0000305}.
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DR EMBL; DQ000496; AAY45700.1; -; Genomic_DNA.
DR EMBL; GQ925675; ACX50492.1; -; Genomic_DNA.
DR EMBL; GQ925675; ACX50493.1; -; Genomic_DNA.
DR EMBL; JQ411251; AFC37600.1; -; Genomic_DNA.
DR EMBL; JQ411251; AFC37603.1; -; Genomic_DNA.
DR EMBL; JQ923422; AFR53039.1; -; Genomic_DNA.
DR EMBL; JQ923422; AFR53040.1; -; Genomic_DNA.
DR EMBL; KU557404; AND46431.1; -; Genomic_DNA.
DR EMBL; KJ634207; AIC76457.1; -; Genomic_DNA.
DR RefSeq; YP_338086.1; NC_007455.1.
DR PDB; 4KW3; X-ray; 2.70 A; A/B=1-271.
DR PDBsum; 4KW3; -.
DR SMR; D0EZM8; -.
DR DNASU; 3711585; -.
DR GeneID; 3711585; -.
DR KEGG; vg:3711585; -.
DR Proteomes; UP000101074; Genome.
DR Proteomes; UP000114321; Genome.
DR Proteomes; UP000118311; Genome.
DR Proteomes; UP000128269; Genome.
DR Proteomes; UP000140113; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding;
KW Covalent protein-DNA linkage; DNA replication; DNA-binding; Endonuclease;
KW Helicase; Host nucleus; Hydrolase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nuclease; Nucleotide-binding; Reference proteome;
KW Transcription; Transcription regulation; Viral DNA replication.
FT CHAIN 1..781
FT /note="Initiator protein NS1"
FT /id="PRO_0000445633"
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..781
FT /note="Transactivation"
FT /evidence="ECO:0000250|UniProtKB:P03134"
FT REGION 621..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..781
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 1..274
FT /note="Missing (in isoform NS3 and isoform NS4)"
FT /id="VSP_059924"
FT VAR_SEQ 289..597
FT /note="Missing (in isoform NS2 and isoform NS4)"
FT /id="VSP_059925"
FT VAR_SEQ 639
FT /note="D -> K (in isoform NS1-70)"
FT /id="VSP_059926"
FT VAR_SEQ 640..781
FT /note="Missing (in isoform NS1-70)"
FT /id="VSP_059927"
FT VARIANT 384
FT /note="D -> N (in strain: Eg/BSU-1)"
FT /evidence="ECO:0000305"
FT VARIANT 398
FT /note="P -> L (in strain: Eg/BSU-1)"
FT /evidence="ECO:0000305"
FT VARIANT 536
FT /note="Q -> H (in strain: Eg/BSU-1)"
FT /evidence="ECO:0000305"
FT VARIANT 566
FT /note="Y -> H (in strain: Eg/BSU-1)"
FT /evidence="ECO:0000305"
FT VARIANT 639
FT /note="D -> K (in strain: Eg/BSU-1)"
FT /evidence="ECO:0000305"
FT VARIANT 649
FT /note="E -> K (in strain: KU3 and Salvator1)"
FT /evidence="ECO:0000305"
FT VARIANT 746
FT /note="F -> L (in strain: KU3 and Salvator1)"
FT /evidence="ECO:0000305"
FT STRAND 13..21
FT /evidence="ECO:0007829|PDB:4KW3"
FT TURN 25..30
FT /evidence="ECO:0007829|PDB:4KW3"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:4KW3"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:4KW3"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:4KW3"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:4KW3"
FT HELIX 74..94
FT /evidence="ECO:0007829|PDB:4KW3"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:4KW3"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:4KW3"
FT TURN 127..133
FT /evidence="ECO:0007829|PDB:4KW3"
FT HELIX 134..149
FT /evidence="ECO:0007829|PDB:4KW3"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:4KW3"
FT HELIX 160..177
FT /evidence="ECO:0007829|PDB:4KW3"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:4KW3"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:4KW3"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:4KW3"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:4KW3"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:4KW3"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:4KW3"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:4KW3"
SQ SEQUENCE 781 AA; 88180 MW; BF1D92C6BF0562DE CRC64;
MAFNPPVIRA FSQPAFTYVF KFPYPQWKEK EWLLHALLAH GTEQSMIQLR NCAPHPDEDI
IRDDLLISLE DRHFGAVLCK AVYMATTTLM SHKQRNMFPR CDIIVQSELG EKNLHCHIIV
GGEGLSKRNA KSSCAQFYGL ILAEIIQRCK SLLATRPFEP EEADIFHTLK KAEREAWGGV
TGGNMQILQY RDRRGDLHAQ TVDPLRFFKN YLLPKNRCIS SYSKPDVCTS PDNWFILAEK
TYSHTLINGL PLPEHYRKNY HATLDNEVIP GPQTMAYGGR GPWEHLPEVG DQRLAASSVS
TTYKPNKKEK LMLNLLDKCK ELNLLVYEDL VANCPELLLM LEGQPGGARL IEQVLGMHHI
NVCSNFTALT YLFHLHPVTS LDSDNKALQL LLIQGYNPLA VGHALCCVLN KQFGKQNTVC
FYGPASTGKT NMAKAIVQGI RLYGCVNHLN KGFVFNDCRQ RLVVWWEECL MHQDWVEPAK
CILGGTECRI DVKHRDSVLL TQTPVIISTN HDIYAVVGGN SVSHVHAAPL KERVIQLNFM
KQLPQTFGEI TATEIAALLQ WCFNEYDCTL TGFKQKWNLD KIPNSFPLGV LCPTHSQDFT
LHENGYCTDC GGYLPHSADN SMYTDRASET STGDITPSDL GDSDGEDTEP ETSQVDYCPP
KKRRLTAPAS PPNSPASSVS TITFFNTWHA QPRDEDELRE YERQASLLQK KRESRKRGEE
ETLADNSSQE QEPQPDPTQW GERLGFISSG TPNQPPIVLH CFEDLRPSDE DEGEYIGEKR
Q
