CAPS2_PFV2
ID CAPS2_PFV2 Reviewed; 145 AA.
AC A0A6M3VWZ7;
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 2 {ECO:0000303|PubMed:32368353};
DE AltName: Full=MCP2 {ECO:0000303|PubMed:32368353};
DE AltName: Full=Major capsid protein VP2 {ECO:0000250|UniProtKB:A0A140F3K7};
GN ORFNames=PFV2_gp21 {ECO:0000312|EMBL:QJF12394.1};
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] {ECO:0000312|EMBL:QJF12394.1, ECO:0000312|Proteomes:UP000502572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4 {ECO:0000312|EMBL:QJF12394.1};
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), DISULFIDE BONDS,
RP SUBCELLULAR LOCATION, 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 (Probable) (PubMed:32368353). Together with capsid protein 2, wraps
CC arounds the DNA and maintains it in an A-form (Probable). Capsid
CC proteins probably maintain the DNA in A-form by non-specific
CC desolvation and specific coordination of the DNA phosphate groups by
CC positively charged residues (Probable). This certainly protects the
CC viral DNA under conditions such as the extreme desiccation of its host
CC (Probable). {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; QJF12394.1; -; 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=1-145.
DR PDBsum; 6V7B; -.
DR SMR; A0A6M3VWZ7; -.
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; Disulfide bond; DNA-binding; Reference proteome; Virion.
FT CHAIN 1..145
FT /note="Major capsid protein 2"
FT /id="PRO_0000453883"
FT DISULFID 96..107
FT /evidence="ECO:0000269|PubMed:32368353"
SQ SEQUENCE 145 AA; 15307 MW; 065FB869E2FA126D CRC64;
MSVEVYRQKI EKGGYSAAYE ATRRYEREEI EVLSWSSRWE SAWSKFGEAV KALGKIEGAP
RALVIAKVQE ALAYMSKPLP NMKLAMAAAV QAVRACEQLP GMNRERCLDA VAGALGVAKD
WIRREMTGGG GGGGGGGGGG GGAVV
