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Database: UniProt
Entry: D0U495_9VIRU
LinkDB: D0U495_9VIRU
Original site: D0U495_9VIRU 
ID   D0U495_9VIRU            Unreviewed;       979 AA.
AC   D0U495;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   07-OCT-2020, entry version 27.
DE   RecName: Full=Structural polyprotein {ECO:0000256|RuleBase:RU363030};
DE            Short=PP {ECO:0000256|RuleBase:RU363030};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU363030};
OS   Drosophila melanogaster birnavirus SW-2009a.
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae.
OX   NCBI_TaxID=663281 {ECO:0000313|EMBL:ACU32790.1, ECO:0000313|Proteomes:UP000170672};
RN   [1] {ECO:0000313|EMBL:ACU32790.1, ECO:0000313|Proteomes:UP000170672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DBV {ECO:0000313|EMBL:ACU32790.1};
RX   PubMed=20080648; DOI=10.1073/pnas.0911353107;
RA   Wu Q., Luo Y., Lu R., Lau N., Lai E.C., Li W.X., Ding S.W.;
RT   "Virus discovery by deep sequencing and assembly of virus-derived small
RT   silencing RNAs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:1606-1611(2010).
CC   -!- FUNCTION: Capsid protein VP2 self assembles to form an icosahedral
CC       capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of
CC       260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also
CC       involved in attachment and entry into the host cell.
CC       {ECO:0000256|RuleBase:RU363030}.
CC   -!- FUNCTION: Capsid protein VP3 plays a key role in virion assembly by
CC       providing a scaffold for the capsid made of VP2. May self-assemble to
CC       form a T=4-like icosahedral inner-capsid composed of at least 180
CC       trimers. Plays a role in genomic RNA packaging by recruiting VP1 into
CC       the capsid and interacting with the dsRNA genome segments to form a
CC       ribonucleoprotein complex. Additionally, the interaction of the VP3 C-
CC       terminal tail with VP1 removes the inherent structural blockade of the
CC       polymerase active site. Thus, VP3 can also function as a
CC       transcriptional activator. {ECO:0000256|RuleBase:RU363030}.
CC   -!- FUNCTION: Protease VP4 is a serine protease that cleaves the
CC       polyprotein into its final products. Pre-VP2 is first partially
CC       cleaved, and may be completely processed by VP4 upon capsid maturation.
CC       {ECO:0000256|PROSITE-ProRule:PRU00881, ECO:0000256|RuleBase:RU363030}.
CC   -!- FUNCTION: Structural peptide 1 is a small peptide derived from pre-VP2
CC       C-terminus. It destabilizes and perforates cell membranes, suggesting a
CC       role during entry. {ECO:0000256|RuleBase:RU363030}.
CC   -!- FUNCTION: Structural peptide 2 is a small peptide derived from pre-VP2
CC       C-terminus. It is not essential for the virus viability, but viral
CC       growth is affected when missing. {ECO:0000256|RuleBase:RU363030}.
CC   -!- FUNCTION: Structural peptide 3 is a small peptide derived from pre-VP2
CC       C-terminus. It is not essential for the virus viability, but viral
CC       growth is affected when missing. {ECO:0000256|RuleBase:RU363030}.
CC   -!- FUNCTION: The precursor of VP2 plays an important role in capsid
CC       assembly. First, pre-VP2 and VP2 oligomers assemble to form a
CC       procapsid. Then, the pre-VP2 intermediates may be processed into VP2
CC       proteins by proteolytic cleavage mediated by VP4 to obtain the mature
CC       virion. The final capsid is composed of pentamers and hexamers but VP2
CC       has a natural tendency to assemble into all-pentameric structures.
CC       Therefore pre-VP2 may be required to allow formation of the hexameric
CC       structures. {ECO:0000256|ARBA:ARBA00002547,
CC       ECO:0000256|RuleBase:RU363030}.
CC   -!- SUBUNIT: Capsid protein VP2 is a homotrimer. A central divalent metal
CC       stabilizes the VP2 trimer. {ECO:0000256|RuleBase:RU363030}.
CC   -!- SUBUNIT: Capsid protein VP3 is a homodimer.
CC       {ECO:0000256|RuleBase:RU363030}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC       cytoplasm {ECO:0000256|ARBA:ARBA00004192,
CC       ECO:0000256|RuleBase:RU363030}. Virion {ECO:0000256|ARBA:ARBA00004328,
CC       ECO:0000256|RuleBase:RU363030}.
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DR   EMBL; GQ342962; ACU32790.1; -; Genomic_RNA.
DR   Proteomes; UP000170672; Genome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   Gene3D; 1.10.150.620; -; 1.
DR   Gene3D; 2.60.120.20; -; 1.
DR   InterPro; IPR002662; Birna_VP2.
DR   InterPro; IPR002663; Birna_VP3.
DR   InterPro; IPR043048; Birna_VP3_dom1.
DR   InterPro; IPR025775; Birna_VP4_Prtase_dom.
DR   InterPro; IPR029053; Viral_coat.
DR   Pfam; PF01766; Birna_VP2; 1.
DR   Pfam; PF01767; Birna_VP3; 1.
DR   Pfam; PF01768; Birna_VP4; 1.
DR   PROSITE; PS51548; BIRNAVIRUS_VP4_PRO; 1.
PE   4: Predicted;
KW   Capsid protein {ECO:0000256|ARBA:ARBA00022561,
KW   ECO:0000256|RuleBase:RU363030};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200,
KW   ECO:0000256|RuleBase:RU363030};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00881, ECO:0000256|RuleBase:RU363030};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU363030};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU00881, ECO:0000256|RuleBase:RU363030};
KW   Reference proteome {ECO:0000313|Proteomes:UP000170672};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU00881, ECO:0000256|RuleBase:RU363030};
KW   Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|RuleBase:RU363030}.
FT   DOMAIN          517..721
FT                   /note="Peptidase S50"
FT                   /evidence="ECO:0000259|PROSITE:PS51548"
FT   REGION          850..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        626
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00881"
FT   ACT_SITE        664
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00881"
SQ   SEQUENCE   979 AA;  106766 MW;  6770D91B25B6D63A CRC64;
     MSNEYLRSIL MPERGPSSIP DDNVRRHCVR QETITANIVV GSSGKGAFVL FPNNPSSLIG
     AHFKYDDQGK SYKYTQSLVV AQRLNESYNY GRKSAGVIYI RSSTLPSGVY NISGTINAAT
     YEGPPSEVGL PEYNKILSIT SNPMDKLGNV GVLEGVAVLT LPASYDIDYT RLADLSPSSA
     KNGCVVNDSG QSLIYTQYDE INYTGSQEKQ LLSFNIDSNI LVTTTATLDF YTTASDAQVT
     IKIKYLGIDG LVVSENEIIS RIDSLERTVS IDAFYPFPQV IKEGGQEPVA AVELYLTSDK
     STSITGTIRS ITTAHSAARP GITSPTTIVA YEGVQSGASI TVAGVSNYEL IPNPELARNM
     ETRYARTDPY GMIYTKYVLA NRDRLGIRSV WPTNDYKARF PLFEELGLMQ SDASITEAMA
     FGIHDVISWI RGLVPAASDW ANRMLPGSGD VIKGINRTAG HLLYGEAASG RLIAQSASGS
     LIGQLGHRDA LACDVDPTLM GHNAAQLICY NTALGVRSTG NRIYMIRLKT PKRNPRVTIF
     PALVFNTTPL GPEVSGTQLY AVIEGLYNQV PQSRFKVTGK NGRTIYGIKP GAYIPPGPNC
     TVVPISSITQ NEITTTATPP IPRGGSMEAA LALLQYIPPG VTPFAVTGNV IEGKIVPNKW
     ADLKREGMKG TGIPLVTDQD YKTIKDLAKA TEMLQRITTA QHPAVIGTIA SAMDYDDFPP
     PPPPVTDENI METLEDLLVA AADRDPRMAK LKDVVLWLAK IDNNNPGVLD TLHNFSRQDV
     EGEKMNRIVQ NSLTTAVHNR GPTQEVLQHQ KAVRIRENYL NQGVDLSIEW IKNNGFRGPS
     ADQMKTIKAG LEPPPDTTTK SPTPHNDTST PALVMKIIKN SLGIHYDNAS PETQKEINER
     ITTMVINNGN RGLNQYQAKE IVQDYGKTKK SAQMNLRYVG PRKIGYTPPS ANQVVDVPPP
     ENTRDVYRTT YSAGYPPMC
//
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