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Database: UniProt
Entry: Q2PBR5_9VIRU
LinkDB: Q2PBR5_9VIRU
Original site: Q2PBR5_9VIRU 
ID   Q2PBR5_9VIRU            Unreviewed;      1114 AA.
AC   Q2PBR5;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   07-OCT-2020, entry version 50.
DE   RecName: Full=Capsid protein VP2 {ECO:0000256|ARBA:ARBA00018985};
DE   AltName: Full=Capsid protein VP3 {ECO:0000256|ARBA:ARBA00018981};
DE   AltName: Full=Non-structural protein VP4 {ECO:0000256|ARBA:ARBA00017197};
DE   AltName: Full=Precursor of VP2 {ECO:0000256|ARBA:ARBA00015390};
DE   AltName: Full=Protease VP4 {ECO:0000256|ARBA:ARBA00018554};
DE   AltName: Full=Structural peptide 1 {ECO:0000256|ARBA:ARBA00022071};
DE   AltName: Full=Structural peptide 2 {ECO:0000256|ARBA:ARBA00022070};
DE   AltName: Full=Structural peptide 3 {ECO:0000256|ARBA:ARBA00022068};
DE   AltName: Full=Structural polyprotein {ECO:0000256|ARBA:ARBA00014555};
OS   Tellina virus 1.
OC   Viruses; Riboviria; Orthornavirae; Birnaviridae; Telnavirus.
OX   NCBI_TaxID=321302 {ECO:0000313|EMBL:CAI74981.1, ECO:0000313|Proteomes:UP000241576};
RN   [1] {ECO:0000313|EMBL:CAI74981.1, ECO:0000313|Proteomes:UP000241576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17976679; DOI=10.1016/j.virol.2007.09.022;
RA   Nobiron I., Galloux M., Henry C., Torhy C., Boudinot P., Lejal N.,
RA   Da Costa B., Delmas B.;
RT   "Genome and polypeptides characterization of Tellina virus 1 reveals a
RT   fifth genetic cluster in the Birnaviridae family.";
RL   Virology 371:350-361(2008).
RN   [2] {ECO:0000213|PDB:3P06}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 637-830.
RX   PubMed=21288899; DOI=10.1074/jbc.M110.198812;
RA   Chung I.Y., Paetzel M.;
RT   "Crystal structure of a viral protease intramolecular acyl-enzyme complex:
RT   insights into cis-cleavage at the VP4/VP3 junction of Tellina birnavirus.";
RL   J. Biol. Chem. 286:12475-12482(2011).
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}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC       cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Virion
CC       {ECO:0000256|ARBA:ARBA00004328}.
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DR   EMBL; AJ920335; CAI74981.1; -; Genomic_RNA.
DR   PDB; 3P06; X-ray; 2.10 A; A=637-830.
DR   PDBsum; 3P06; -.
DR   SMR; Q2PBR5; -.
DR   MEROPS; S69.001; -.
DR   BRENDA; 3.4.21.115; 12943.
DR   EvolutionaryTrace; Q2PBR5; -.
DR   Proteomes; UP000241576; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0000213|PDB:3P06};
KW   Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00881}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU00881}; Reference proteome {ECO:0000313|Proteomes:UP000241576};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU00881}; Virion {ECO:0000256|ARBA:ARBA00022844}.
FT   DOMAIN          619..839
FT                   /note="Peptidase S50"
FT                   /evidence="ECO:0000259|PROSITE:PS51548"
FT   REGION          860..882
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1076..1114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        862..879
FT                   /note="Pro-rich"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1079..1097
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        738
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00881"
FT   ACT_SITE        777
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00881"
SQ   SEQUENCE   1114 AA;  119739 MW;  658BB0EEDF059E42 CRC64;
     MASKQFSMLA TRKSPYIKSL LLPETGPASI PDDKIRRHVK RSESTTTNLT STTGKGMLIV
     YNNHPKNLVG SHYTYASDGK LRFDRNLYTA QDLSKNFNYG RKVSQLVTIK STQLPAGVYA
     MQGTMNGVCI DGAPSEVETA LKYETILSAS TNALDKVAGV LVNDGVGVLS LPTTFDNDYI
     RMGDPAPSSF TPGSAQLSKP THNPGLNSIV TAGTTGLTSG TKTISTTKTI ISTDVINVDS
     TEGLLLDLNI QLMRWGVPSG KTATVTVDVK TVDLAGAETD AEQREIKISG TNTGRDNVIT
     LSGLMMGLSG KKPLVAPTAA VVIEVSAISS ESMTLTHSGH INNYSLTSLC AGTPGTTNPI
     TIIIYTDLTP GGIMTVTAVS NFELIPNAEL RKNIPTDFGN SDPSEMDFIK RILGQRETLE
     LRTIWDMGMY DARRDVLSEF AHLDDNSLAM AWEWSDVLWW IKKIAGTIAP IAGAVFPAAA
     PLTSAISTMA NAASGRALAA SGKPLYRNMA LAGERPLSRQ ITRIARTAAR MTATALRSAA
     LTPCCLRNQD ACNLTADILM ELTGADSCPP GISSAARLVN ENNGCRCSNP SPDIKDAISA
     IEAGEAMDSI LTAEVAQAAD RPMIRTKRKA RKTRTANGVE LSAVGVLLPV LMDSGRRISG
     GAFMAVKGDL SEHIKNPKNT RIAQTVAGGT IYGLSEMVNI DEAEKLPIKG AITVLPVVQA
     TATSILVPDN QPQLAFNSWE AAACAADTLE SQQTPFLMVT GAVESGNLSP NLLAVQKQLL
     VAKPAGIGLA ANSDRALKVV TLEQLRQVVG DKPWRKPMVT FSSGKNVAQA STNPFTSNNP
     FNPFMNLGDE YEEAPINPFL NLLPEAPTPP VPAPRRRPTP SPRQIAVAER FEAAAEEAAA
     QSPDLSDALE VANWLMETGN IQMMLDFMKR DRRGDKLSRM LFVTTYPSMA PNPGNGPTPE
     QARWESAVRK AGNMAATYPD ITPEWVVANG YAGPDQAQAK YFSIHRRLPT AGETPIFSLG
     EKRKPGPDHA RRLLQRLLAS RDWNEEQIDA LTDYVEEHGT GPDEATMQYI AQLGHNRRER
     PSASSRNAMK EARDAARTTA KMSLNRYKNN SGML
//
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