ID   CAPS1_PFV2              Reviewed;         129 AA.
AC   A0A6M3VZT9;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-OCT-2020, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=Major capsid protein 1 {ECO:0000303|PubMed:32368353};
DE   AltName: Full=MCP1 {ECO:0000303|PubMed:32368353};
DE   AltName: Full=Major capsid protein VP1 {ECO:0000250|UniProtKB:A0A140F3K6};
GN   ORFNames=PFV2_gp20 {ECO:0000312|EMBL:QJF12393.1};
OS   Pyrobaculum filamentous virus 2 (PFV2).
OC   Viruses; Adnaviria; Zilligvirae; Taleaviricota; Tokiviricetes;
OC   Primavirales; Tristromaviridae; Alphatristromavirus;
OC   Alphatristromavirus PFV2.
OX   NCBI_TaxID=2730621;
OH   NCBI_TaxID=121277; Pyrobaculum arsenaticum.
OH   NCBI_TaxID=99007; Pyrobaculum oguniense.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4;
RX   PubMed=32322010; DOI=10.1038/s41396-020-0653-z;
RA   Baquero D.P., Contursi P., Piochi M., Bartolucci S., Liu Y.,
RA   Cvirkaite-Krupovic V., Prangishvili D., Krupovic M.;
RT   "New virus isolates from Italian hydrothermal environments underscore the
RT   biogeographic pattern in archaeal virus communities.";
RL   ISME J. 14:1821-1833(2020).
RN   [2]
RP   SUBUNIT, AND FUNCTION.
RX   PubMed=32759221; DOI=10.1073/pnas.2011125117;
RA   Wang F., Baquero D.P., Beltran L.C., Su Z., Osinski T., Zheng W.,
RA   Prangishvili D., Krupovic M., Egelman E.H.;
RT   "Structures of filamentous viruses infecting hyperthermophilic archaea
RT   explain DNA stabilization in extreme environments.";
RL   Proc. Natl. Acad. Sci. U.S.A. 117:19643-19652(2020).
RN   [3] {ECO:0007744|PDB:6V7B}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION,
RP   AND FUNCTION.
RX   PubMed=32368353; DOI=10.1093/ve/veaa023;
RA   Wang F., Baquero D.P., Su Z., Osinski T., Prangishvili D., Egelman E.H.,
RA   Krupovic M.;
RT   "Structure of a filamentous virus uncovers familial ties within the
RT   archaeal virosphere.";
RL   Virus Evol. 6:veaa023-veaa023(2020).
CC   -!- FUNCTION: Self-assembles to form a helical, filamentous nucleocapsid
CC       mesuring 400 nm in length and 20 nm in width (Probable)
CC       (PubMed:32368353). Together with capsid protein 2, wraps arounds the
CC       DNA and maintains it in an A-form (Probable). Capsid proteins probably
CC       maintain the DNA in A-form by non-specific desolvation and specific
CC       coordination of the DNA phosphate groups by positively charged residues
CC       (Probable). This certainly protects the viral DNA under conditions such
CC       as the extreme desiccation of its host (Probable).
CC       {ECO:0000269|PubMed:32368353, ECO:0000305|PubMed:32759221}.
CC   -!- SUBUNIT: Heterodimer composed of major capsid protein 1 and major
CC       capsid protein 2. {ECO:0000269|PubMed:32759221}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:32368353}.
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DR   EMBL; MN876844; QJF12393.1; -; Genomic_DNA.
DR   PDB; 6V7B; EM; 3.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W=1-129.
DR   PDBsum; 6V7B; -.
DR   SMR; A0A6M3VZT9; -.
DR   Proteomes; UP000502572; Genome.
DR   GO; GO:0019029; C:helical viral capsid; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Virion.
FT   CHAIN           1..129
FT                   /note="Major capsid protein 1"
FT                   /id="PRO_0000453882"
SQ   SEQUENCE   129 AA;  14964 MW;  7250F8D0C5F890BB CRC64;
     MSVVTTRARI AETLTEKHTL GIEKVVATDS WRVGITSREK KLERINISAE ISRRIQDEAI
     AYARNKGIPY LPGINGIAWK LLRLKWLGYT DQINVVMRTV PAEWRDFLTQ IMENTQMESM
     YSELRKVRV