CAS6_PYRFU
ID CAS6_PYRFU Reviewed; 264 AA.
AC Q8U1S4;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=CRISPR-associated endoribonuclease Cas6;
DE EC=3.1.-.-;
GN Name=cas6; OrderedLocusNames=PF1131;
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 FUNCTION AS AN ENDORIBONUCLEASE, RNA-BINDING, COFACTOR, ACTIVE SITE, AND
RP MUTAGENESIS OF TYR-31; HIS-46 AND LYS-52.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=20884784; DOI=10.1261/rna.2230110;
RA Carte J., Pfister N.T., Compton M.M., Terns R.M., Terns M.P.;
RT "Binding and cleavage of CRISPR RNA by Cas6.";
RL RNA 16:2181-2188(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-264, FUNCTION AS AN
RP ENDORIBONUCLEASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND RNA-BINDING.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=19141480; DOI=10.1101/gad.1742908;
RA Carte J., Wang R., Li H., Terns R.M., Terns M.P.;
RT "Cas6 is an endoribonuclease that generates guide RNAs for invader defense
RT in prokaryotes.";
RL Genes Dev. 22:3489-3496(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 2-264 IN COMPLEX WITH RNA.
RX PubMed=21300293; DOI=10.1016/j.str.2010.11.014;
RA Wang R., Preamplume G., Terns M.P., Terns R.M., Li H.;
RT "Interaction of the Cas6 riboendonuclease with CRISPR RNAs: recognition and
RT cleavage.";
RL Structure 19:257-264(2011).
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. This protein
CC processes pre-crRNA into individual crRNA units, with an 8-nt 5'-repeat
CC DNA tag that may help other proteins recognize the crRNA. Further
CC processing occurs at their 3' termini in this organism. Generates a 5'-
CC hydroxy and 2',3'-cyclic phosphodiester. {ECO:0000269|PubMed:19141480,
CC ECO:0000269|PubMed:20884784}.
CC -!- COFACTOR:
CC Note=Does not require a metal cofactor. {ECO:0000269|PubMed:19141480,
CC ECO:0000269|PubMed:20884784};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.
CC {ECO:0000269|PubMed:19141480};
CC -!- SUBUNIT: Monomer, binds precursor but not mature crRNA; is not part of
CC the Cmr effector complex. {ECO:0000269|PubMed:21300293}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated protein Cas6/Cse3/CasE
CC family. {ECO:0000305}.
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DR EMBL; AE009950; AAL81255.1; -; Genomic_DNA.
DR RefSeq; WP_011012271.1; NC_003413.1.
DR PDB; 3I4H; X-ray; 2.25 A; X=2-264.
DR PDB; 3PKM; X-ray; 3.10 A; A/X=2-264.
DR PDBsum; 3I4H; -.
DR PDBsum; 3PKM; -.
DR AlphaFoldDB; Q8U1S4; -.
DR SMR; Q8U1S4; -.
DR STRING; 186497.PF1131; -.
DR EnsemblBacteria; AAL81255; AAL81255; PF1131.
DR GeneID; 1469000; -.
DR KEGG; pfu:PF1131; -.
DR PATRIC; fig|186497.12.peg.1192; -.
DR eggNOG; arCOG04342; Archaea.
DR HOGENOM; CLU_089858_1_1_2; -.
DR OMA; FGMVKVD; -.
DR OrthoDB; 59332at2157; -.
DR PhylomeDB; Q8U1S4; -.
DR EvolutionaryTrace; Q8U1S4; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0043571; P:maintenance of CRISPR repeat elements; IDA:CACAO.
DR Gene3D; 3.30.70.1890; -; 1.
DR InterPro; IPR010156; CRISPR-assoc_prot_Cas6.
DR InterPro; IPR045747; CRISPR-assoc_prot_Cas6_N_sf.
DR PANTHER; PTHR36984; PTHR36984; 1.
DR Pfam; PF01881; Cas_Cas6; 1.
DR PIRSF; PIRSF005054; PF1131; 1.
DR TIGRFAMs; TIGR01877; cas_cas6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Endonuclease; Hydrolase; Nuclease;
KW Reference proteome; RNA-binding.
FT CHAIN 1..264
FT /note="CRISPR-associated endoribonuclease Cas6"
FT /id="PRO_0000417970"
FT ACT_SITE 31
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:20884784"
FT ACT_SITE 46
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:20884784"
FT SITE 52
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:20884784"
FT MUTAGEN 31
FT /note="Y->A: No RNA cleavage, binds pre-crRNA normally."
FT /evidence="ECO:0000269|PubMed:20884784"
FT MUTAGEN 46
FT /note="H->A: No RNA cleavage, binds pre-crRNA normally."
FT /evidence="ECO:0000269|PubMed:20884784"
FT MUTAGEN 52
FT /note="K->A: 40-fold reduction in RNA cleavage, binds pre-
FT crRNA normally."
FT /evidence="ECO:0000269|PubMed:20884784"
FT STRAND 2..14
FT /evidence="ECO:0007829|PDB:3I4H"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:3I4H"
FT HELIX 23..37
FT /evidence="ECO:0007829|PDB:3I4H"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:3I4H"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:3I4H"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3I4H"
FT STRAND 71..86
FT /evidence="ECO:0007829|PDB:3I4H"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:3I4H"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3I4H"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:3I4H"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:3I4H"
FT HELIX 155..171
FT /evidence="ECO:0007829|PDB:3I4H"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:3I4H"
FT STRAND 180..191
FT /evidence="ECO:0007829|PDB:3I4H"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:3PKM"
FT STRAND 201..211
FT /evidence="ECO:0007829|PDB:3I4H"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:3I4H"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:3I4H"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3I4H"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:3I4H"
SQ SEQUENCE 264 AA; 30704 MW; 8FB43EB6BF649D1C CRC64;
MRFLIRLVPE DKDRAFKVPY NHQYYLQGLI YNAIKSSNPK LATYLHEVKG PKLFTYSLFM
AEKREHPKGL PYFLGYKKGF FYFSTCVPEI AEALVNGLLM NPEVRLWDER FYLHEIKVLR
EPKKFNGSTF VTLSPIAVTV VRKGKSYDVP PMEKEFYSII KDDLQDKYVM AYGDKPPSEF
EMEVLIAKPK RFRIKPGIYQ TAWHLVFRAY GNDDLLKVGY EVGFGEKNSL GFGMVKVEGN
KTTKEAEEQE KITFNSREEL KTGV
