P2A_CFMVN
ID P2A_CFMVN Reviewed; 568 AA.
AC Q89504; Q0PW24; Q76PL5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Polyprotein P2A;
DE Contains:
DE RecName: Full=N-terminal protein;
DE Contains:
DE RecName: Full=Serine protease;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=VPg;
DE Contains:
DE RecName: Full=Putative protein p10;
DE Contains:
DE RecName: Full=Putative protein p8;
GN ORFNames=ORF2A;
OS Cocksfoot mottle virus (isolate Dactylis glomerata/Norway/CfMV-NO/1995)
OS (CfMV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Sobelivirales; Solemoviridae; Sobemovirus.
OX NCBI_TaxID=1005059;
OH NCBI_TaxID=4509; Dactylis glomerata (Orchard grass) (Cock's-foot grass).
OH NCBI_TaxID=4565; Triticum aestivum (Wheat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7595389; DOI=10.1099/0022-1317-76-11-2817;
RA Maekinen K., Tamm T., Naess V., Truve E., Puurand U., Munthe T., Saarma M.;
RT "Characterization of cocksfoot mottle sobemovirus genomic RNA and sequence
RT comparison with related viruses.";
RL J. Gen. Virol. 76:2817-2825(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16732485; DOI=10.1007/s11262-005-6917-x;
RA Meier M., Paves H., Olspert A., Tamm T., Truve E.;
RT "P1 protein of Cocksfoot mottle virus is indispensable for the systemic
RT spread of the virus.";
RL Virus Genes 32:321-326(2006).
RN [3]
RP PROTEIN SEQUENCE OF 320-336, PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND
RP CHARACTERIZATION OF VPG.
RX PubMed=11038392; DOI=10.1099/0022-1317-81-11-2783;
RA Maekinen K., Maekelaeinen K., Arshava N., Tamm T., Merits A., Truve E.,
RA Zavriev S., Saarma M.;
RT "Characterization of VPg and the polyprotein processing of cocksfoot mottle
RT virus (genus Sobemovirus).";
RL J. Gen. Virol. 81:2783-2789(2000).
RN [4]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND PHOSPHORYLATION AT THR-339 AND
RP SER-390.
RX PubMed=21068217; DOI=10.1099/vir.0.026476-0;
RA Olspert A., Peil L., Hebrard E., Fargette D., Truve E.;
RT "Protein-RNA linkage and post-translational modifications of two
RT sobemovirus VPgs.";
RL J. Gen. Virol. 92:445-452(2011).
CC -!- FUNCTION: [Serine protease]: Responsible for cleavages of polyprotein
CC P2A and replicase polyprotein P2AB.
CC -!- FUNCTION: [VPg]: Covalently attached to the 5' extremity of the genomic
CC and subgenomic RNAs. It may serve as a primer for the replicase.
CC -!- SUBCELLULAR LOCATION: [Polyprotein P2A]: Host membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [N-terminal protein]: Host membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=Polyprotein P2A;
CC IsoId=Q89504-1; Sequence=Displayed;
CC Name=Replicase polyprotein P2AB;
CC IsoId=Q0PW25-1; Sequence=External;
CC -!- MISCELLANEOUS: [Isoform Polyprotein P2A]: Produced by conventional
CC translation.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z36903; CAA85372.1; -; Genomic_RNA.
DR EMBL; Z48630; CAA88561.1; -; Genomic_RNA.
DR EMBL; DQ680848; ABG73618.1; -; Genomic_RNA.
DR RefSeq; NP_941376.1; NC_002618.2.
DR SMR; Q89504; -.
DR MEROPS; S39.001; -.
DR iPTMnet; Q89504; -.
DR GeneID; 2654592; -.
DR KEGG; vg:2654592; -.
DR Proteomes; UP000001461; Genome.
DR Proteomes; UP000008994; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0016032; P:viral process; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 2.
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 SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS51868; PEPTIDASE_S39; 1.
PE 1: Evidence at protein level;
KW Covalent protein-RNA linkage; Direct protein sequencing; Host membrane;
KW Hydrolase; Membrane; Phosphoprotein; Protease; Reference proteome;
KW Ribosomal frameshifting; Serine protease; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..568
FT /note="Polyprotein P2A"
FT /id="PRO_0000409851"
FT CHAIN 1..130
FT /note="N-terminal protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409852"
FT CHAIN 131..319
FT /note="Serine protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409853"
FT CHAIN 320..397
FT /note="VPg"
FT /evidence="ECO:0000255"
FT /id="PRO_0000409854"
FT CHAIN 398..499
FT /note="Putative protein p10"
FT /evidence="ECO:0000250"
FT /id="PRO_0000409855"
FT CHAIN 500..568
FT /note="Putative protein p8"
FT /evidence="ECO:0000250"
FT /id="PRO_0000409856"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 129..326
FT /note="Peptidase S39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT REGION 403..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT ACT_SITE 209
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT ACT_SITE 276
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01216"
FT SITE 130..131
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
FT SITE 319..320
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
FT SITE 324
FT /note="Interacts with viral RNA (covalent)"
FT SITE 397..398
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
FT SITE 499..500
FT /note="Cleavage; by viral serine protease"
FT /evidence="ECO:0000255"
FT MOD_RES 339
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000269|PubMed:21068217"
FT MOD_RES 390
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:21068217"
FT CONFLICT 27
FT /note="I -> V (in Ref. 1; CAA85372)"
FT /evidence="ECO:0000305"
FT CONFLICT 61..62
FT /note="CE -> WQ (in Ref. 1; CAA85372)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="T -> A (in Ref. 1; CAA85372)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="K -> R (in Ref. 1; CAA85372)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="L -> P (in Ref. 1; CAA85372)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="R -> Q (in Ref. 1; CAA85372)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="E -> A (in Ref. 1; CAA85372)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="K -> R (in Ref. 1; CAA85372)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="V -> A (in Ref. 1; CAA85372)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="V -> A (in Ref. 1; CAA85372)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="R -> K (in Ref. 1; CAA85372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 60947 MW; B42DED81F4077C57 CRC64;
MGCSVVGNCK SVMLMSRMSW SKLALLISVA MAAAMTDSPP TLICMGILVS VVLNWIVCAV
CEEASELILG VSLETTRPSP ARVIGEPVFD PRYGYVAPAI YDGKSFDVIL PISALSSAST
RKETVEMAVE NSRLQPLESS QTPKSLVALY SQDLLSGWGS RIKGPDGQEY LLTALHVWET
NISHLCKDGK KVPISGCPIV ASSADSDLDF VLVSVPKNAW SVLGVGVARL ELLKRRTVVT
VYGGLDSKTT YCATGVAELE NPFRIVTKVT TTGGWSGSPL YHKDAIVGLH LGARPSAGVN
RACNVAMAFR VVRKFVTVEN SELYPDQSSG PARELDAETY TERLEQGIAF TEYNISGITV
KTSDREWTTA EALRVARYKP LGGGKAWGDS DDEDTQETAI RPLNYQRAGS LRGSPPLANL
SSTRATSGVT KESSIPTACL SDPLESRVAG LEKLCAERFT EMFELLRQSS QNSKSSLGQA
ADRKQKSDRS SSKPEGLKES KRPPICNWQS LTSKPSTRGP DPAPVSAESP GVVKTSSQKS
KRSRTRGKST SRQVPASPSP KSGSATSK
