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Database: UniProt
Entry: G9I7F9_9VIRU
LinkDB: G9I7F9_9VIRU
Original site: G9I7F9_9VIRU 
ID   G9I7F9_9VIRU            Unreviewed;      1054 AA.
AC   G9I7F9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   07-OCT-2020, entry version 33.
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   Espirito Santo virus.
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae.
OX   NCBI_TaxID=1127767 {ECO:0000313|EMBL:AEW87521.1, ECO:0000313|Proteomes:UP000175413};
RN   [1] {ECO:0000313|EMBL:AEW87521.1, ECO:0000313|Proteomes:UP000175413}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22171264; DOI=10.1128/JVI.06614-11;
RA   Vancini R., Paredes A., Ribeiro M., Blackburn K., Ferreira D.,
RA   Kononchik J.P.Jr., Hernandez R., Brown D.;
RT   "Espirito Santo Virus: A new Birnavirus that replicates in insect cells.";
RL   J. Virol. 0:0-0(2011).
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; JN589003; AEW87521.1; -; Genomic_RNA.
DR   RefSeq; YP_004956722.1; NC_016518.1.
DR   GeneID; 11493377; -.
DR   KEGG; vg:11493377; -.
DR   Proteomes; UP000175413; 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; 2.60.120.20; -; 1.
DR   InterPro; IPR002662; Birna_VP2.
DR   InterPro; IPR002663; Birna_VP3.
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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000175413};
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          501..724
FT                   /note="Peptidase S50"
FT                   /evidence="ECO:0000259|PROSITE:PS51548"
FT   COILED          841..861
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        628
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00881"
FT   ACT_SITE        671
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00881"
SQ   SEQUENCE   1054 AA;  115645 MW;  4AFBDFC6F9F8AB94 CRC64;
     MNTSNEYLKT LLDPAQFIAD IPDDIMIRHI NRAETITYNL KTGASGTGLI VFYPNTPSSV
     AGFHYRWDAE NSVWAFDQYI YTAQELKKSY DYGRLISGAV SVKSSSIPSG VYALTGTFNA
     VWFQGTLSEV SNLNYDRILS ITSNPLDKVG NVLVGDGLAV LSLPQGFNNP YVRLGDESPS
     SLTSVTHITN TSQNLGYGGA FAVPQTTVAG QGTFFKEFNI NVDSVGPIDV TWSGLMTMQD
     EWTVTANYQP LNLSGTLIQG SMRTIIWSNV GVSNGTHYMN LNEINVSFFH ENPPPEPVAA
     IKVHITFGNN TNGESSMNVD GSFTFHVVGG ATIGVNSPTV MIGYQGVASG STITLSGVNN
     YELVPNPALQ KNLPMSYGTC DPTDLNYVKY ILSNREKLGI RSVMTLAQYA KMKMQMNIMT
     DYHVGDREAS SFDFWHLLKQ IKKLVVPVAS TMLPQFAPII GAADNLANTV LGNSASGQPI
     GNSASGLPIS MTRRIKSAHS ADTPIGDSNW EPTRNPEFNK LDVIYDVSHS SMALFPVIMM
     DNDQVVPSDP EELFIAVSLT ESLRKQIPGI DTMPYYTIGG HRVYNAVSNG RVSTAPFLTS
     DYILLPCYQL FDGKLATSKT PNKVTGTSHQ LALYAAEGLQ KRGIMGKAPY AAFTGSVAGQ
     SVGEVFGISL KSQLTDSLGI PLFGNSQGLP IQNLHQLERL LDISGDVPRR TPRETPNHWT
     ASSASVPFSN TNPFLNGEVD QERNVQFLPT NTNPFLDAGQ DVGGVPPQQM ARIISDDTRN
     AFLEDGQSIP SSQEKIVTVH EFLLQNQELL EAMFGLISRG HEKALVNMVT KAAVNIKTQA
     KDLTEERLAR LEVKIQHLAR QGIVLDPENV KRAGRITQED TQAAIIRSKD HQMRNKLRRV
     FLNNVSIGRE YTEDEFVDFW IRQGFIPNGL QISAWLREED WSSPTPALSK RHYDSYLQML
     GPSPDQGLVE QVRSMVDSVY DENGNKGPSQ VQARALSSSV RRLISQSLVT RPQPVPKVPV
     RKIEPIATGQ GSNPERRAAL ERLQRARGGE SEMI
//
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