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Database: UniProt
Entry: CAS6L_PYRFU
LinkDB: CAS6L_PYRFU
Original site: CAS6L_PYRFU 
ID   CAS6L_PYRFU             Reviewed;         241 AA.
AC   Q8U3R3;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Putative CRISPR-associated endoribonuclease-like protein Cas6;
GN   Name=cas6b; Synonyms=cas6-2, cas6-3; OrderedLocusNames=PF0393;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS), RNA-BINDING, AND LACK OF
RP   ENDONUCLEASE ACTIVITY.
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=22447673; DOI=10.1002/prot.24061;
RA   Park H.M., Shin M., Sun J., Kim G.S., Lee Y.C., Park J.H., Kim B.Y.,
RA   Kim J.S.;
RT   "Crystal structure of a Cas6 paralogous protein from Pyrococcus furiosus.";
RL   Proteins 80:1895-1900(2012).
CC   -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC       repeat), is an adaptive immune system that provides protection against
CC       mobile genetic elements (viruses, transposable elements and conjugative
CC       plasmids). CRISPR clusters contain sequences complementary to
CC       antecedent mobile elements and target invading nucleic acids. CRISPR
CC       clusters are transcribed and processed into CRISPR RNA (crRNA), also
CC       called psiRNA (prokaryotic silencing) in this organism (Potential).
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Binds crRNA.
CC   -!- SIMILARITY: Belongs to the CRISPR-associated protein Cas6/Cse3/CasE
CC       family. {ECO:0000305}.
CC   -!- CAUTION: No in vitro nuclease activity has been observed against crRNA
CC       for this protein. {ECO:0000305|PubMed:22447673}.
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DR   EMBL; AE009950; AAL80517.1; -; Genomic_DNA.
DR   RefSeq; WP_011011506.1; NZ_CP023154.1.
DR   PDB; 3UFC; X-ray; 2.03 A; X=1-241.
DR   PDBsum; 3UFC; -.
DR   AlphaFoldDB; Q8U3R3; -.
DR   SMR; Q8U3R3; -.
DR   STRING; 186497.PF0393; -.
DR   PaxDb; 186497-PF0393; -.
DR   GeneID; 41712190; -.
DR   KEGG; pfu:PF0393; -.
DR   PATRIC; fig|186497.12.peg.408; -.
DR   eggNOG; arCOG04342; Archaea.
DR   HOGENOM; CLU_089858_1_1_2; -.
DR   OrthoDB; 43942at2157; -.
DR   PhylomeDB; Q8U3R3; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.1890; -; 1.
DR   Gene3D; 3.30.70.1900; -; 1.
DR   InterPro; IPR049435; Cas_Cas6_C.
DR   InterPro; IPR010156; CRISPR-assoc_prot_Cas6.
DR   InterPro; IPR045747; CRISPR-assoc_prot_Cas6_N_sf.
DR   NCBIfam; TIGR01877; cas_cas6; 1.
DR   PANTHER; PTHR36984; CRISPR-ASSOCIATED ENDORIBONUCLEASE CAS6 1; 1.
DR   PANTHER; PTHR36984:SF1; CRISPR-ASSOCIATED ENDORIBONUCLEASE CAS6 1; 1.
DR   Pfam; PF21350; Cas6_I-A; 1.
DR   Pfam; PF01881; Cas_Cas6_C; 1.
DR   PIRSF; PIRSF005054; PF1131; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Reference proteome; RNA-binding.
FT   CHAIN           1..241
FT                   /note="Putative CRISPR-associated endoribonuclease-like
FT                   protein Cas6"
FT                   /id="PRO_0000417971"
FT   STRAND          1..13
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   HELIX           21..35
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   HELIX           40..44
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   STRAND          56..63
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   STRAND          67..70
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   STRAND          75..82
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   HELIX           84..96
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   STRAND          99..102
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   STRAND          105..114
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   STRAND          122..130
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   STRAND          132..140
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   STRAND          143..149
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   HELIX           156..172
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   STRAND          181..195
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   STRAND          198..211
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   HELIX           213..222
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   STRAND          224..226
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   HELIX           228..230
FT                   /evidence="ECO:0007829|PDB:3UFC"
FT   STRAND          235..237
FT                   /evidence="ECO:0007829|PDB:3UFC"
SQ   SEQUENCE   241 AA;  28046 MW;  A2C70BA1BC4BBD00 CRC64;
     MRIEIKLLPL QDNPVIPFNY NYELYSQIVE KAGAIEPRIV KLLESPHGYW TFSRIIIRKR
     EIIPEKGIKI LSDDISLYIS SSNKEIIKGI VEGIEKSPEF KIGDVGFLVA DIKALKSKEI
     KNVNIFSTLS PIVVRTVKFE GDKLKHWDLY PHDELFLDRL RKVMLLRYHE VMGDLPEDKD
     FRIELIKFKP TRLIVKDSYI RGSLMVFRYY GSKEIAKFGY ENGFGEKTNL GFGMVKIIEE
     Q
//
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