ID   CAPSD_PVMG              Reviewed;         304 AA.
AC   Q01669;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   02-JUN-2021, entry version 68.
DE   RecName: Full=Capsid protein;
DE   AltName: Full=Coat protein;
DE            Short=CP;
OS   Potato virus M (strain German) (PVM).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Betaflexiviridae; Quinvirinae; Carlavirus.
OX   NCBI_TaxID=31710;
OH   NCBI_TaxID=4113; Solanum tuberosum (Potato).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2265707; DOI=10.1016/0014-5793(90)80500-i;
RA   Gramstat A., Courtpozanis A., Rohde W.;
RT   "The 12 kDa protein of potato virus M displays properties of a nucleic
RT   acid-binding regulatory protein.";
RL   FEBS Lett. 276:34-38(1990).
RN   [2]
RP   REVIEW.
RX   PubMed=15828680; DOI=10.1094/mpmi-18-0283;
RA   Verchot-Lubicz J.;
RT   "A new cell-to-cell transport model for Potexviruses.";
RL   Mol. Plant Microbe Interact. 18:283-290(2005).
CC   -!- FUNCTION: Required for genome encapsidation. Forms ribonucleoprotein
CC       complexes along with TGB1 helicase and viral RNA.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- MISCELLANEOUS: The N- and the C-terminus of this capsid protein may be
CC       exposed on the surface of the virus particle. The central core sequence
CC       may be important in maintaining correct tertiary structure of the
CC       capsid protein and/or play a role in interacting with the viral RNA.
CC   -!- SIMILARITY: Belongs to the potexviruses coat protein family.
CC       {ECO:0000305}.
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; X57440; CAA40688.1; -; Genomic_RNA.
DR   PIR; S12975; S12975.
DR   SMR; Q01669; -.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR013569; Carlavirus_coat_N.
DR   InterPro; IPR000052; Pltvir_coat.
DR   Pfam; PF00286; Flexi_CP; 1.
DR   Pfam; PF08358; Flexi_CP_N; 1.
DR   PRINTS; PR00232; POTXCARLCOAT.
DR   PROSITE; PS00418; POTEX_CARLAVIRUS_COAT; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Helical capsid protein; Ribonucleoprotein; Virion.
FT   CHAIN           1..304
FT                   /note="Capsid protein"
FT                   /id="PRO_0000222641"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   304 AA;  33927 MW;  E3B44FADE61D494F CRC64;
     MGDSTKKAET AKDVGTSQEK REARPLPTAA DFEGKDTSED TDGRAADADG EMSLERRLDS
     LREFLRERRG AIRVTNPGLE TGRPRLQLAE NMRPDPTNPY NRPSIEALSR IKPIAISNNM
     ATSEDMMRIY VNLEGLGVPT EHVQQVVIQA VLFCKDASSS VFLDPRGSFE WPRGAITADA
     VLAVLKKDAE TLRRVCRLYA PVTWNHMLTH NAPPAEWAAM GFQYEDRFAP FDCFDYVENT
     AAVQPLEGLI RRPTPREKVA HNTHKDIALR GANRNQVFSS LNAEVTGGMN GPELTRDYVK
     SNRK