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P1_PEMVW
ID   P1_PEMVW                Reviewed;         760 AA.
AC   Q84710;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Protein P1;
DE   AltName: Full=Genome-linked protein precursor;
DE   AltName: Full=ORF1 protein;
DE   Contains:
DE     RecName: Full=Serine protease;
DE              EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=VPg;
DE   Contains:
DE     RecName: Full=P1-C25;
DE   Flags: Precursor;
GN   ORFNames=ORF1;
OS   Pea enation mosaic virus-1 (strain WSG) (PEMV-1).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Sobelivirales; Solemoviridae; Enamovirus.
OX   NCBI_TaxID=693989;
OH   NCBI_TaxID=3827; Cicer arietinum (Chickpea) (Garbanzo).
OH   NCBI_TaxID=3859; Lathyrus odoratus (Sweet pea).
OH   NCBI_TaxID=3864; Lens culinaris (Lentil) (Cicer lens).
OH   NCBI_TaxID=70936; Medicago arabica.
OH   NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH   NCBI_TaxID=60916; Trifolium incarnatum (Crimson clover).
OH   NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
OH   NCBI_TaxID=3908; Vicia sativa (Spring vetch) (Tare).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1875194; DOI=10.1099/0022-1317-72-8-1819;
RA   Demler S.A., de Zoeten G.A.;
RT   "The nucleotide sequence and luteovirus-like nature of RNA 1 of an aphid
RT   non-transmissible strain of pea enation mosaic virus.";
RL   J. Gen. Virol. 72:1819-1834(1991).
RN   [2]
RP   CHARACTERIZATION OF VPG, AND PROTEIN SEQUENCE.
RX   PubMed=9714253; DOI=10.1099/0022-1317-79-8-2023;
RA   Wobus C.E., Skaf J.S., Schultz M.H., de Zoeten G.A.;
RT   "Sequencing, genomic localization and initial characterization of the VPg
RT   of pea enation mosaic enamovirus.";
RL   J. Gen. Virol. 79:2023-2025(1998).
CC   -!- FUNCTION: Precursor from which the VPg molecule is probably released at
CC       the onset of the RNA synthesis. Essential for virus replication (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Protein P1;
CC         IsoId=Q84710-1; Sequence=Displayed;
CC       Name=RNA-directed RNA polymerase;
CC         IsoId=P29154-1; Sequence=External;
CC   -!- DOMAIN: The C-terminus part of protein P1 and P1-C25 displays RNA-
CC       binding properties. {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC       protease probably cleaves itself and releases the VPg protein (By
CC       similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform Protein P1]: Produced by conventional
CC       translation.
CC   -!- SIMILARITY: Belongs to the peptidase S39B family. {ECO:0000305}.
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DR   EMBL; L04573; AAA72300.1; -; Genomic_RNA.
DR   PIR; JQ1383; JQ1383.
DR   RefSeq; NP_619736.1; NC_003629.1.
DR   GeneID; 940254; -.
DR   KEGG; vg:940254; -.
DR   Proteomes; UP000000519; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0016032; P:viral process; IEA:InterPro.
DR   InterPro; IPR018019; Luteovirus_Orf2.
DR   InterPro; IPR000382; Peptidase_S39B_luteovirus.
DR   Pfam; PF02122; Peptidase_S39; 1.
DR   PRINTS; PR00913; LVIRUSORF2.
DR   PROSITE; PS51868; PEPTIDASE_S39; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Membrane; Protease;
KW   Reference proteome; Ribosomal frameshifting; RNA-binding; Serine protease;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..760
FT                   /note="Protein P1"
FT                   /id="PRO_0000390915"
FT   CHAIN           316..515
FT                   /note="Serine protease"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000390916"
FT   CHAIN           516..543
FT                   /note="VPg"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000390917"
FT   CHAIN           544..760
FT                   /note="P1-C25"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000391318"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          318..515
FT                   /note="Peptidase S39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   REGION          572..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          684..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..729
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        366
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   ACT_SITE        396
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   ACT_SITE        465
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   SITE            315..316
FT                   /note="Cleavage; by viral serine protease"
FT                   /evidence="ECO:0000255"
FT   SITE            515..516
FT                   /note="Cleavage; by viral serine protease"
FT                   /evidence="ECO:0000255"
FT   SITE            543..544
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   760 AA;  84187 MW;  731B581AF51FFD14 CRC64;
     MASFLKPVNS QGLWLSLLLA ITYLFLLPSA GQSLDPSGIG LAAGCSQSQG GISSFAALPR
     PCNDSVCTLP DLGWSCQRTA QDTANQQQSP FNHTGHFLTT SGWTWPNWTC SPSQCQLLIH
     LPTWQIVKQD FLLLLKEWDL LTMCQRCSDL LTKTPGFILR FAGETLILVA NLIEFVLVSW
     SLWLCSVLVY VAQAVPGKFL LYMAAFCTTF WAWPRETASS LIRIVTTPLT LIGFLNKTGI
     GLISHCLALT WNMFMTWSLL PWVTLMKMMK ILITSSRVLT RSGRPKRTSS KSLKHKLKIS
     RAIQKKQGKK TPVEERTIPG VQIKKLREDP PKGVILRCTD QFGDHVGYAS AVKLEKGQTG
     IVLPIHVWTD TVYINGPNGK LKMADFTALY EVTNHDSLIM TSAMAGWGSI LGVRPRPLTT
     IDAVKLKNYS LFTERDGKWY VQAAKCIAPA EGMFRVVSDT RPGDSGLPLF DMKMNVVAVH
     RGTWPSERFP ENRAFAILPV PDLTSSSSPK FTGCETYSEA ETAYEMADNF SDGEEILIRT
     KGQSYRTFIG SNKVALLSIR KLEEELSRGP IGLWADDTED DESAPRRSGN GLFRSTPEKQ
     SQAKTPSPKV EESAAPPPAP RAEKVRHVRR SEMTPEQKRA DNLRRRKAKA AKKTPSTPPK
     KSKDKAPTLS QVAELVEKAV RAALTVQPRR SRASSKISIG GRNPGRKPQV SIQLDPVPSQ
     STSVPPKDSQ AGESAWLGPR RSYRPVQKST VGQKQEPRRN
 
 
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