CSM6_THET8
ID CSM6_THET8 Reviewed; 464 AA.
AC Q53W17;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=CRISPR system endoribonuclease Csm6;
DE EC=3.1.-.- {ECO:0000269|PubMed:26763118, ECO:0000269|PubMed:28663439, ECO:0000269|PubMed:28722012};
DE AltName: Full=CRISPR type III-A associated protein Csm6 {ECO:0000305};
DE AltName: Full=TtCsm6 {ECO:0000303|PubMed:26763118};
GN Name=csm6 {ECO:0000303|PubMed:26763118}; OrderedLocusNames=TTHB152;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8; PLASMID=pTT27;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=28663439; DOI=10.1126/science.aao0100;
RA Kazlauskiene M., Kostiuk G., Venclovas C., Tamulaitis G., Siksnys V.;
RT "A cyclic oligonucleotide signaling pathway in type III CRISPR-Cas
RT systems.";
RL Science 357:605-609(2017).
RN [3]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=28722012; DOI=10.1038/nature23467;
RA Niewoehner O., Garcia-Doval C., Rostoel J.T., Berk C., Schwede F.,
RA Bigler L., Hall J., Marraffini L.A., Jinek M.;
RT "Type III CRISPR-Cas systems produce cyclic oligoadenylate second
RT messengers.";
RL Nature 548:543-548(2017).
RN [4] {ECO:0007744|PDB:5FSH}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), FUNCTION, COFACTOR, SUBUNIT,
RP DOMAIN, AND MUTAGENESIS OF 1-MET--ALA-190; THR-133; LYS-137; GLU-332;
RP ARG-415; ASN-416 AND HIS-422.
RC STRAIN=ATCC 27634 / DSM 579 / HB8; PLASMID=pTT27;
RX PubMed=26763118; DOI=10.1261/rna.054098.115;
RA Niewoehner O., Jinek M.;
RT "Structural basis for the endoribonuclease activity of the type III-A
RT CRISPR-associated protein Csm6.";
RL RNA 22:318-329(2016).
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 spacers, sequences complementary to
CC antecedent mobile elements, and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA)
CC (Probable). The type III-A Csm effector complex binds crRNA and acts as
CC a crRNA-guided RNase, DNase and cyclic oligoadenylate synthase; binding
CC of target RNA cognate to the crRNA is required for all activities. This
CC protein is not part of the Csm effector complex (Probable).
CC {ECO:0000305}.
CC -!- FUNCTION: A single-strand-specific endoribonuclease (ssRNase) producing
CC free 5'-OH (PubMed:26763118). Activity is approximately 1000-fold
CC stimulated by cyclic oligoadenylate (cOA); only cyclic tetraadenylate
CC (cA4) stimulates the ssRNase activity while linear oligoadenylates do
CC not activate the RNase (PubMed:28663439). Another study showed
CC stimulation by linear tetraadenylate at very high concentrations, but
CC did not examine stimulation by cA4 (PubMed:28722012).
CC {ECO:0000269|PubMed:26763118, ECO:0000269|PubMed:28663439,
CC ECO:0000269|PubMed:28722012}.
CC -!- COFACTOR:
CC Note=Does not require a metal cofactor. {ECO:0000269|PubMed:26763118};
CC -!- ACTIVITY REGULATION: Non-specific ssRNase activity is allosterically
CC activated about 1000-fold by cyclic tetraadenylate (cA4), which
CC probably binds to its CARF domain. {ECO:0000269|PubMed:28663439,
CC ECO:0000305|PubMed:28722012}.
CC -!- SUBUNIT: Homodimer. The protein forms a twisted, head-to-head dimer;
CC the composite ssRNase active site is formed at the dimer interface.
CC {ECO:0000269|PubMed:26763118}.
CC -!- DOMAIN: The N-terminal CRISPR-associated Rossman fold (CARF) probably
CC binds the cA4 effector. ssRNase activity resides in the C-terminal HEPN
CC domain. {ECO:0000269|PubMed:26763118}.
CC -!- MISCELLANEOUS: Probably encoded in a type III-A CRISPR locus.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated Csm6 family.
CC {ECO:0000305}.
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DR EMBL; AP008227; BAD71948.1; -; Genomic_DNA.
DR RefSeq; WP_011229148.1; NC_006462.1.
DR RefSeq; YP_145391.1; NC_006462.1.
DR PDB; 5FSH; X-ray; 2.30 A; A/B=1-464.
DR PDBsum; 5FSH; -.
DR AlphaFoldDB; Q53W17; -.
DR SMR; Q53W17; -.
DR EnsemblBacteria; BAD71948; BAD71948; BAD71948.
DR GeneID; 3169219; -.
DR KEGG; ttj:TTHB152; -.
DR PATRIC; fig|300852.9.peg.2100; -.
DR HOGENOM; CLU_589161_0_0_0; -.
DR OMA; TSGTKAM; -.
DR Proteomes; UP000000532; Plasmid pTT27.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Endonuclease; Hydrolase; Nuclease;
KW Plasmid; Reference proteome.
FT CHAIN 1..464
FT /note="CRISPR system endoribonuclease Csm6"
FT /id="PRO_0000446128"
FT REGION 1..190
FT /note="CARF domain"
FT /evidence="ECO:0000305|PubMed:26763118"
FT REGION 191..464
FT /note="HEPN domain"
FT /evidence="ECO:0000305|PubMed:26763118"
FT MUTAGEN 1..190
FT /note="Missing: Wild-type ssRNase activity."
FT /evidence="ECO:0000269|PubMed:26763118"
FT MUTAGEN 133
FT /note="T->A: Wild-type ssRNase activity."
FT /evidence="ECO:0000269|PubMed:26763118"
FT MUTAGEN 137
FT /note="K->A: Wild-type ssRNase activity."
FT /evidence="ECO:0000269|PubMed:26763118"
FT MUTAGEN 332
FT /note="E->A: No ssRNase activity."
FT /evidence="ECO:0000269|PubMed:26763118"
FT MUTAGEN 415
FT /note="R->A: No ssRNase activity."
FT /evidence="ECO:0000269|PubMed:26763118"
FT MUTAGEN 416
FT /note="N->A: No ssRNase activity."
FT /evidence="ECO:0000269|PubMed:26763118"
FT MUTAGEN 422
FT /note="H->A: No ssRNase activity."
FT /evidence="ECO:0000269|PubMed:26763118"
FT HELIX 1..17
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:5FSH"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:5FSH"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:5FSH"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 88..95
FT /evidence="ECO:0007829|PDB:5FSH"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:5FSH"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:5FSH"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:5FSH"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:5FSH"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:5FSH"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 208..222
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 226..241
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 245..260
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 273..292
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 298..315
FT /evidence="ECO:0007829|PDB:5FSH"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 320..341
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 353..366
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 382..391
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 402..412
FT /evidence="ECO:0007829|PDB:5FSH"
FT TURN 419..422
FT /evidence="ECO:0007829|PDB:5FSH"
FT HELIX 429..448
FT /evidence="ECO:0007829|PDB:5FSH"
SQ SEQUENCE 464 AA; 51121 MW; 98E516CEBF503083 CRC64;
MEDLDALWER YREAVRAGGN PQALYQEMVW PALLALWREK PRVYPFPQAF AVSVHTLGTS
PEATALAILG AGAERVYVLH TPESARFLPR LRQDTGKDLY PVEIGKSDVE AIYREVKRLL
EKHPEVPVAL DLTSGTKAMS AGLAAAGFFF QRFYPKVRVV YVDNEDYDPE LRRPRAGTEK
LRILPNPHEA LAEVDALFAK ELYGKGEFGQ AAAYFRGMVG RTGNQAYALY ALLAEMYRAW
RALDFGEALK AGRKLLGQLS QNVWLNHPLN ARREALEAQV ALLEAVDRFL KARDFALKEG
VYGLARTLLH LAQEAKEEAA VLAALYAYRA LELLLQERLA LLGRRAEAPG LSPEEAEALR
KALAELLGVL PEEVRLPAKL GLLDLLAFLR LKGDEALGRL SLAELRGLAG ALKGRNSALL
VHGFDVPSPK AVEGIARLAQ GLLQDLEART ALGPLSPEPV PLGF
