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CAPSD_PMV
ID   CAPSD_PMV               Reviewed;         215 AA.
AC   P16596;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   02-JUN-2021, entry version 97.
DE   RecName: Full=Coat protein;
DE   AltName: Full=Capsid protein;
DE            Short=CP;
OS   Papaya mosaic potexvirus (PMV).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC   Tymovirales; Alphaflexiviridae; Potexvirus.
OX   NCBI_TaxID=12181;
OH   NCBI_TaxID=3649; Carica papaya (Papaya).
OH   NCBI_TaxID=108055; Ullucus tuberosus (Olluco).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2778435; DOI=10.1099/0022-1317-70-9-2325;
RA   Sit T.L., Abouhaidar M.G., Holy S.;
RT   "Nucleotide sequence of papaya mosaic virus RNA.";
RL   J. Gen. Virol. 70:2325-2331(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3335832; DOI=10.1099/0022-1317-69-1-219;
RA   Abouhaidar M.G.;
RT   "Nucleotide sequence of the capsid protein gene and 3' non-coding region of
RT   papaya mosaic virus RNA.";
RL   J. Gen. Virol. 69:219-226(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-215.
RX   PubMed=18640641; DOI=10.1016/0042-6822(86)90395-8;
RA   Short M.N., Turner D.S., March J.F., Pappin D.J., Parente A., Davies J.W.;
RT   "The primary structure of papaya mosaic virus coat protein.";
RL   Virology 152:280-283(1986).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-5, ACETYLATION AT SER-2, AND SEQUENCE REVISION TO
RP   214.
RX   PubMed=2624687; DOI=10.1007/bf01024903;
RA   Verde C., Malorni A., Parente A.;
RT   "The primary structure of papaya mosaic virus coat protein: a revision.";
RL   J. Protein Chem. 8:795-805(1989).
RN   [5]
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   -!- SIMILARITY: Belongs to the potexvirus capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; D00240; BAA00169.1; -; Genomic_RNA.
DR   EMBL; D13957; BAA03054.1; -; Genomic_RNA.
DR   PIR; JQ0100; VCWGPM.
DR   RefSeq; NP_044334.1; NC_001748.1.
DR   PDB; 4DOX; X-ray; 2.70 A; A/B=1-215.
DR   PDBsum; 4DOX; -.
DR   SMR; P16596; -.
DR   iPTMnet; P16596; -.
DR   GeneID; 1494025; -.
DR   KEGG; vg:1494025; -.
DR   Proteomes; UP000000477; Genome.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR000052; Pltvir_coat.
DR   Pfam; PF00286; Flexi_CP; 1.
DR   PRINTS; PR00232; POTXCARLCOAT.
DR   PROSITE; PS00418; POTEX_CARLAVIRUS_COAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Capsid protein; Direct protein sequencing;
KW   Helical capsid protein; Reference proteome; Ribonucleoprotein; Virion.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000269|PubMed:18640641,
FT                   ECO:0000269|PubMed:2624687"
FT   CHAIN           2..215
FT                   /note="Coat protein"
FT                   /id="PRO_0000222635"
FT   MOD_RES         2
FT                   /note="N-acetylserine; by host"
FT                   /evidence="ECO:0000269|PubMed:2624687"
FT   CONFLICT        11
FT                   /note="T -> I (in Ref. 1; BAA03054)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30
FT                   /note="S -> SN (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        77
FT                   /note="Missing (in Ref. 2; BAA00169)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        185
FT                   /note="Q -> E (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        190
FT                   /note="T -> A (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           18..23
FT                   /evidence="ECO:0007829|PDB:4DOX"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:4DOX"
FT   HELIX           36..48
FT                   /evidence="ECO:0007829|PDB:4DOX"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:4DOX"
FT   HELIX           56..70
FT                   /evidence="ECO:0007829|PDB:4DOX"
FT   HELIX           89..98
FT                   /evidence="ECO:0007829|PDB:4DOX"
FT   HELIX           103..108
FT                   /evidence="ECO:0007829|PDB:4DOX"
FT   HELIX           111..118
FT                   /evidence="ECO:0007829|PDB:4DOX"
FT   TURN            119..121
FT                   /evidence="ECO:0007829|PDB:4DOX"
FT   TURN            125..131
FT                   /evidence="ECO:0007829|PDB:4DOX"
FT   HELIX           134..139
FT                   /evidence="ECO:0007829|PDB:4DOX"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:4DOX"
FT   HELIX           165..172
FT                   /evidence="ECO:0007829|PDB:4DOX"
SQ   SEQUENCE   215 AA;  23033 MW;  605B94EE70B41323 CRC64;
     MSKSSMSTPN TAFPAITQEQ MSSIKVDPTS NLLPSQEQLK SVSTLMVAAK VPAASVTTVA
     LELVNFCYDN GSSAYTTVTG PSSIPEISLA QLASIVKASG TSLRKFCRYF APIIWNLRTD
     KMAPANWEAS GYKPSAKFAA FDFFDGVENP AAMQPPSGLI RSPTQEERIA NATNKQVHLF
     QAAAQDNNFT SNSAFITKGQ ISGSTPTIQF LPPPE
 
 
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