位置:首页 > 蛋白库 > NS1_BMDNV
NS1_BMDNV
ID   NS1_BMDNV               Reviewed;         885 AA.
AC   P05842;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   23-FEB-2022, entry version 68.
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;
OS   Bombyx mori densovirus (BmDNV) (Bombyx densonucleosis virus).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Quintoviricetes;
OC   Piccovirales; Parvoviridae; Densovirinae; Iteradensovirus.
OX   NCBI_TaxID=10809;
OH   NCBI_TaxID=7091; Bombyx mori (Silk moth).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate INA;
RX   PubMed=3027382; DOI=10.1128/jvi.61.2.553-560.1987;
RA   Bando H., Kusuda J., Gojobori T., Maruyama T., Kawase S.;
RT   "Organization and nucleotide sequence of a densovirus genome imply a host-
RT   dependent evolution of the parvoviruses.";
RL   J. Virol. 61:553-560(1987).
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). {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. {ECO:0000250|UniProtKB:P03134}.
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 (By similarity). The C-terminus probably
CC       contains a transactivation domain (By similarity).
CC       {ECO:0000250|UniProtKB:P03134, 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; M15123; AAA67698.1; -; Genomic_DNA.
DR   PIR; C26796; VCPVF2.
DR   SMR; P05842; -.
DR   PRIDE; P05842; -.
DR   Proteomes; UP000008471; 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; IPR016184; Capsid/spike_ssDNA_virus.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001257; Parvovirus_NS1_helicase.
DR   Pfam; PF01057; Parvo_NS1; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF88645; SSF88645; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Covalent protein-DNA linkage; DNA replication; DNA-binding;
KW   Endonuclease; Helicase; Host nucleus; Hydrolase; Magnesium; Metal-binding;
KW   Nuclease; Nucleotide-binding; Transcription; Transcription regulation;
KW   Viral DNA replication; Viral genome packaging;
KW   Viral release from host cell.
FT   CHAIN           1..885
FT                   /note="Initiator protein NS1"
FT                   /id="PRO_0000222481"
FT   REGION          404..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   885 AA;  100958 MW;  98430617C534D255 CRC64;
     MPIWGAISSN DLLNTYYTIE ESQQIVEELL DFQMHNDQLE YFDSIEDAKK RFITDLYEIL
     EKKHQKTNTF QIVSPPSAGK NFFIETVLAF YWNTGVIQNF NRYNNFPLME AVNRRVNYWD
     EPNFEPDATE TLKKLFAGTS LKATVKFQKE ANVQKTPVII TANYDKFTKE VWDDRIIKYY
     WYPCPKLKEY NKRLHPFAWV YLIDKYVTDL LILIKMYNHR VMGNKICNLI KMYKYRVMVI
     NIFSAFICLI LIFLTNNYLG PGLYTCKSID ETTLSEAVVI WPSDKVTNHK EVFQADKQAR
     DEFFTSFVHI GNVHSLIGGI GLGTKNLVEE HVLGKPLYGM GKRKSTEKDW AKIKRINRAR
     AARRENQENQ PDIREFGHVA GQNINADQEV NLADFPDFLQ DFDAEAGPSG TQPVETAQQS
     PPTMSEDIQP METVGATDTG GGAQVDPRTG GQAAGGSEMG AGGSANDGRE DIFSGAPQPN
     QHHTLVYGKS YHFTITKWFT EFRHLATTNS GYYAQQRFKH IHGIPWERLL MYVSEGELLR
     MFRDYTSLKV EEVVCEVYSL GVRLPFVTSA TTSSVANANA QYPIDVFHFD EAYETNYGIN
     NVADIINKAL GTEWKNATRP TAPVTTAWSE QFPNISASST SRDINNPVIV DYSLPYFENN
     VPKDVGIYDY VDIKNGTTAY GKCWEKRFKP TNGLLYAEST LKGNVVTPLA APTNIMTPIP
     GLENGYFMSN DQIRERRDLT TSVPPDALTA TKLNQSASNN LNAFVDYMGY NYFGEQKAPQ
     SMPKFMIGFV NIRNEDNSLL NAKWDILIKT RIRLTGLQST REWVARTDRI PPQYFTSQYT
     QFRYPNINDT PLLRSLGTFK LPTKRPGMDS RIALGELQKQ RKMNL
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024