ID   CAPS2_SUFV1             Reviewed;         199 AA.
AC   A0A346LU63;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2018, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Major capsid protein VP5 {ECO:0000303|PubMed:30135568};
GN   ORFNames=SFV1gp24 {ECO:0000312|EMBL:AXQ00106.1};
OS   Sulfolobus filamentous virus 1 (SFV1) (Sulfolobus virus SFV-1).
OC   Viruses; Adnaviria; Zilligvirae; Taleaviricota; Tokiviricetes;
OC   Ligamenvirales; Lipothrixviridae; Alphalipothrixvirus;
OC   Alphalipothrixvirus SFV1.
OX   NCBI_TaxID=2304198;
OH   NCBI_TaxID=2286; Saccharolobus shibatae (Sulfolobus shibatae).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], FUNCTION, STRUCTURE BY
RP   ELECTRON MICROSCOPY (3.70 ANGSTROMS), SUBUNIT, AND DOMAIN.
RC   STRAIN=S48 {ECO:0000312|EMBL:AXQ00106.1};
RX   PubMed=30135568; DOI=10.1038/s41467-018-05684-6;
RA   Liu Y., Osinski T., Wang F., Krupovic M., Schouten S., Kasson P.,
RA   Prangishvili D., Egelman E.H.;
RT   "Structural conservation in a membrane-enveloped filamentous virus
RT   infecting a hyperthermophilic acidophile.";
RL   Nat. Commun. 9:3360-3360(2018).
RN   [2]
RP   SUBUNIT, FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
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).
CC   -!- FUNCTION: Self-assembles to form a helical, filamentous nucleocapsid
CC       (Probable) (PubMed:30135568). Together with capsid protein 1, wraps
CC       arounds the DNA and maintains it in an A-form (Probable)
CC       (PubMed:30135568). Capsid proteins probably maintain the DNA in A-form
CC       by non-specific desolvation and specific coordination of the DNA
CC       phosphate groups by positively charged residues (Probable)
CC       (PubMed:30135568). This certainly protects the viral DNA under
CC       conditions such as the extreme desiccation of its host (Probable).
CC       {ECO:0000269|PubMed:30135568, ECO:0000305|PubMed:32759221}.
CC   -!- SUBUNIT: Heterodimer composed of major capsid protein VP4 and major
CC       capsid protein VP5. {ECO:0000269|PubMed:30135568,
CC       ECO:0000269|PubMed:32759221}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:32759221}.
CC   -!- DOMAIN: The N-terminus projects into a DNA groove.
CC       {ECO:0000269|PubMed:30135568, ECO:0000269|PubMed:32759221}.
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DR   EMBL; MH447526; AXQ00106.1; -; Genomic_DNA.
DR   PDB; 6D5F; EM; 3.70 A; A/B/C/D=2-140.
DR   PDBsum; 6D5F; -.
DR   SMR; A0A346LU63; -.
DR   Proteomes; UP000263690; 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; DNA-binding; Reference proteome; Virion.
FT   CHAIN           1..199
FT                   /note="Major capsid protein VP5"
FT                   /id="PRO_0000453808"
SQ   SEQUENCE   199 AA;  21998 MW;  C4BEE6B9AF7302DF CRC64;
     MARKRTSKND PLRMYLNYVR KLQTMGDAYD ESAKYRIANF ENGFKSLHMV ENEFKQYLAN
     VIDEAIKSGA SPQDLPYVNE IKLALMKIFT SWLKYSNEKL GANEIAINVA GTATMTLTEN
     LYGTRVSCEE AVSLINSIFA VWVGVEPFEA EEREGACLVT PRSPLPPVPI SSPTGFSAPI
     QEVLQAKSPE EIIGVKGGA