ID   CAPSD_SIRV2             Reviewed;         134 AA.
AC   Q8V9P2;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Major capsid protein;
OS   Sulfolobus islandicus rod-shaped virus 2 (SIRV2) (Sulfolobus virus SIRV-2).
OC   Viruses; Adnaviria; Zilligvirae; Taleaviricota; Tokiviricetes;
OC   Ligamenvirales; Rudiviridae; Icerudivirus; Icerudivirus SIRV2.
OX   NCBI_TaxID=157899;
OH   NCBI_TaxID=43080; Sulfolobus islandicus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HVE10/4 {ECO:0000312|EMBL:CAC87301.1};
RX   PubMed=11878892; DOI=10.1006/viro.2001.1190;
RA   Peng X., Blum H., She Q., Mallok S., Bruegger K., Garrett R.A., Zillig W.,
RA   Prangishvili D.;
RT   "Sequences and replication of genomes of the archaeal rudiviruses SIRV1 and
RT   SIRV2: relationships to the archaeal lipothrixvirus SIFV and some eukaryal
RT   viruses.";
RL   Virology 291:226-234(2001).
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:3J9X}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 7-134, FUNCTION,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=25999507; DOI=10.1126/science.aaa4181;
RA   DiMaio F., Yu X., Rensen E., Krupovic M., Prangishvili D., Egelman E.H.;
RT   "Virology. A virus that infects a hyperthermophile encapsidates A-form
RT   DNA.";
RL   Science 348:914-917(2015).
CC   -!- FUNCTION: Self-assembles to form a helical, filamentous nucleocapsid
CC       (PubMed:25999507). The capsid proteins wrap around the DNA and maintain
CC       it in an A-form by non-specific desolvation and specific coordination
CC       of the DNA phosphate groups by positively charged residues (Probable)
CC       (PubMed:25999507). This certainly protects the viral DNA under
CC       conditions such as the extreme desiccation of its host (Probable).
CC       {ECO:0000269|PubMed:25999507, ECO:0000305|PubMed:25999507,
CC       ECO:0000305|PubMed:32759221}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25999507,
CC       ECO:0000269|PubMed:32759221}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:25999507}.
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DR   EMBL; AJ344259; CAC87301.1; -; Genomic_DNA.
DR   RefSeq; NP_666560.1; NC_004086.1.
DR   PDB; 3J9X; EM; 3.80 A; 1/2/3/4/5/6/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=7-134.
DR   PDBsum; 3J9X; -.
DR   SMR; Q8V9P2; -.
DR   DIP; DIP-61651N; -.
DR   GeneID; 951446; -.
DR   KEGG; vg:951446; -.
DR   Proteomes; UP000002271; Genome.
DR   GO; GO:0019029; C:helical viral capsid; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   InterPro; IPR022014; Sulfobus_virus_coat_C.
DR   Pfam; PF12193; Sulf_coat_C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Reference proteome; Virion.
FT   CHAIN           1..134
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000453806"
SQ   SEQUENCE   134 AA;  14376 MW;  7F27088DE069CE63 CRC64;
     MAKGHTSRSY SQRYAKWQAK FNAFSNPTVA STILSNVSPV AQQNFQTNVP KFTSVNENVS
     AVLTQYGITG PNRAIYQGFG LKVARALNRI GSGPALVNMI NGLKGYYISA FNANPQVLDA
     VVNIITGSPT GYVS