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P1_TYYVF
ID   P1_TYYVF                Reviewed;         607 AA.
AC   P09506;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Protein P1;
DE   AltName: Full=66.2 kDa protein;
DE   AltName: Full=Genome-linked protein precursor;
DE   AltName: Full=Protein ORF1;
DE   Contains:
DE     RecName: Full=Serine protease;
DE              EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=VPg/P1-C25;
DE   Flags: Precursor;
GN   ORFNames=ORF1;
OS   Turnip yellows virus (isolate FL-1) (TuYV) (BWYV-FL1).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Sobelivirales; Solemoviridae; Polerovirus.
OX   NCBI_TaxID=12043;
OH   NCBI_TaxID=161934; Beta vulgaris (Sugar beet).
OH   NCBI_TaxID=3709; Brassica napus subsp. rapifera.
OH   NCBI_TaxID=138011; Brassica napus var. napus.
OH   NCBI_TaxID=3710; Brassica nigra (Black mustard) (Sinapis nigra).
OH   NCBI_TaxID=3715; Brassica oleracea var. botrytis (Cauliflower).
OH   NCBI_TaxID=3716; Brassica oleracea var. capitata (Cabbage).
OH   NCBI_TaxID=51350; Brassica rapa subsp. rapa (Turnip).
OH   NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
OH   NCBI_TaxID=3827; Cicer arietinum (Chickpea) (Garbanzo).
OH   NCBI_TaxID=3654; Citrullus lanatus (Watermelon) (Citrullus vulgaris).
OH   NCBI_TaxID=3721; Crambe hispanica subsp. abyssinica (Abyssinian kale) (Crambe abyssinica).
OH   NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH   NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
OH   NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH   NCBI_TaxID=4232; Helianthus annuus (Common sunflower).
OH   NCBI_TaxID=4236; Lactuca sativa (Garden lettuce).
OH   NCBI_TaxID=103529; Phlox drummondii (Annual phlox).
OH   NCBI_TaxID=3888; Pisum sativum (Garden pea).
OH   NCBI_TaxID=3726; Raphanus sativus (Radish) (Raphanus raphanistrum var. sativus).
OH   NCBI_TaxID=4081; Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OH   NCBI_TaxID=3562; Spinacia oleracea (Spinach).
OH   NCBI_TaxID=3900; Trifolium subterraneum (Subterranean clover).
OH   NCBI_TaxID=3906; Vicia faba (Broad bean) (Faba vulgaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3194229; DOI=10.1093/nar/16.21.9917;
RA   Veidt I., Lot H., Leiser M., Scheidecker D., Guilley H., Richards K.E.,
RA   Jonard G.;
RT   "Nucleotide sequence of beet western yellows virus RNA.";
RL   Nucleic Acids Res. 16:9917-9932(1988).
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: [Protein P1]: Membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=Protein P1;
CC         IsoId=P09506-1; Sequence=Displayed;
CC       Name=RNA-directed RNA polymerase;
CC         IsoId=P09507-1; Sequence=External;
CC   -!- DOMAIN: The C-terminus part of protein P1 and VPg/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; X13063; CAA31463.1; -; Genomic_RNA.
DR   PIR; S01939; S01939.
DR   RefSeq; NP_620486.1; NC_003743.1.
DR   SMR; P09506; -.
DR   MEROPS; S39.002; -.
DR   GeneID; 940483; -.
DR   KEGG; vg:940483; -.
DR   Proteomes; UP000007545; 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   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR018019; Luteovirus_Orf2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR000382; Peptidase_S39B_luteovirus.
DR   Pfam; PF02122; Peptidase_S39; 1.
DR   PRINTS; PR00913; LVIRUSORF2.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS51868; PEPTIDASE_S39; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Membrane; Protease; Reference proteome; Ribosomal frameshifting;
KW   RNA-binding; Serine protease; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..607
FT                   /note="Protein P1"
FT                   /id="PRO_0000222395"
FT   CHAIN           204..400
FT                   /note="Serine protease"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000390897"
FT   CHAIN           401..607
FT                   /note="VPg/P1-C25"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000390898"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          206..400
FT                   /note="Peptidase S39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   REGION          457..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..484
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..579
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        254
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   ACT_SITE        289
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   ACT_SITE        357
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT   SITE            203..204
FT                   /note="Cleavage; by viral serine protease"
FT                   /evidence="ECO:0000255"
FT   SITE            400..401
FT                   /note="Cleavage; by viral serine protease"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   607 AA;  66211 MW;  2A41F82911DEC84F CRC64;
     MYSKLMFFFA LCSISFLFTS EAASTMLLES SYLPLNQSYA PGFLYKRDML PPPLQAVLTY
     TCPEPRPLAE ESYNDLLRAI SQKSSSDFQN AYSLALSFSS DFYQHGLKTL KDVSFLAVEK
     FLWGLTRLWS SLILASFSAL WWLVSNFTTP VFCLALLYTV TKYMVKTVSF LFGGLPIWII
     SIAFSLLKKS FSALRSTPKC LYEKAIDGFK SFTIPQSPPK SCVIPITHAS GNHAGYASCI
     KLYNGENALM TATHVLRDCP NAVAVSAKGL KTRIPLAEFK TIAKSDKGDV TLLRGPPNWE
     GLLGCKAANV ITAANLAKCK ASIYSFDRDG WVSSYAEIVG SEGTDVMVLS HTEGGHSGSP
     YFNGKTILGV HSGASATGNY NLMAPIPSLP GLTSPTYVFE TTAPQGRVFA QEDIAEIEGL
     YAQVMKRVQQ AEDFKPKTGK YWGDMEDDED IFFESKEDLS GNGVRGTVRG TNGEGSSTPK
     TSNVDGKEMM EKIISSLVGK INLENIERKV IEEISAKAMK TPKSRRRRAP KKQPESSKDT
     SPRSTTGKYQ PPHVRSPASV TAANCPNTTT PSKKKNLAGG RPSSGTIPRW VRKQAASAGP
     SSAPKQN
 
 
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