CSM3_METJA
ID CSM3_METJA Reviewed; 248 AA.
AC Q59063;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=CRISPR system Cms endoribonuclease Csm3;
DE EC=3.1.-.-;
DE AltName: Full=CRISPR type III A-associated RAMP protein Csm3;
GN Name=csm3; OrderedLocusNames=MJ1669;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2] {ECO:0007744|PDB:4QTS}
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH ZINC, SUBUNIT, AND
RP MUTAGENESIS OF 43-ASP--PHE-45; ARG-109; 214-TYR-TYR-215 AND GLU-216.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=25451598; DOI=10.1016/j.jmb.2014.09.029;
RA Numata T., Inanaga H., Sato C., Osawa T.;
RT "Crystal structure of the Csm3-Csm4 subcomplex in the type III-A CRISPR-Cas
RT interference complex.";
RL J. Mol. Biol. 427:259-273(2015).
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). The
CC type III-A Csm effector complex binds crRNA and acts as a crRNA-guided
CC RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA
CC cognate to the crRNA is required for all activities.
CC {ECO:0000250|UniProtKB:A0A0A7HIF0}.
CC -!- FUNCTION: This subunit has the target ssRNA endonuclease activity; it
CC cleaves multiple sites in the target RNA at 6 nucleotide intervals (By
CC similarity). The Csm3-Csm4 complex binds both crRNA and a non-specific
CC RNA; Csm3 alone was not seen to bind RNA (PubMed:25451598).
CC {ECO:0000250|UniProtKB:A0A0A7HIF0, ECO:0000269|PubMed:25451598}.
CC -!- SUBUNIT: Part of the Csm effector complex that includes Cas10, Csm2,
CC Csm3, Csm4 and Csm5 (By similarity). Stable Csm3-Csm4 (which
CC crystallizes as 2 heterodimers) and Cas10-Csm1-Csm3-Csm4 subcomplexes
CC can be isolated; Cas10 and Csm3 probably do not directly interact
CC (PubMed:25451598). {ECO:0000250|UniProtKB:A0A0A7HIF0,
CC ECO:0000269|PubMed:25451598}.
CC -!- MISCELLANEOUS: Encoded in a type III-A CRISPR locus. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated Csm3 family.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB99689.1; -; Genomic_DNA.
DR PIR; C64508; C64508.
DR RefSeq; WP_010871193.1; NC_000909.1.
DR PDB; 4QTS; X-ray; 3.10 A; C/D=1-248.
DR PDBsum; 4QTS; -.
DR AlphaFoldDB; Q59063; -.
DR SMR; Q59063; -.
DR STRING; 243232.MJ_1669; -.
DR EnsemblBacteria; AAB99689; AAB99689; MJ_1669.
DR GeneID; 1452578; -.
DR KEGG; mja:MJ_1669; -.
DR eggNOG; arCOG02658; Archaea.
DR HOGENOM; CLU_067743_0_0_2; -.
DR InParanoid; Q59063; -.
DR OMA; ICKIFGP; -.
DR OrthoDB; 98478at2157; -.
DR PhylomeDB; Q59063; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 CDD; cd09684; Csm3_III-A; 1.
DR InterPro; IPR013412; CRISPR-assoc_RAMP_Csm3.
DR InterPro; IPR005537; RAMP_III_fam.
DR Pfam; PF03787; RAMPs; 1.
DR TIGRFAMs; TIGR02582; cas7_TM1809; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Endonuclease; Hydrolase; Metal-binding;
KW Nuclease; Reference proteome; RNA-binding; Zinc.
FT CHAIN 1..248
FT /note="CRISPR system Cms endoribonuclease Csm3"
FT /id="PRO_0000107466"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25451598,
FT ECO:0007744|PDB:4QTS"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25451598,
FT ECO:0007744|PDB:4QTS"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25451598,
FT ECO:0007744|PDB:4QTS"
FT MUTAGEN 43..45
FT /note="DAF->AAA: Wild-type interaction with Csm4."
FT /evidence="ECO:0000269|PubMed:25451598"
FT MUTAGEN 109
FT /note="R->A: Wild-type interaction with Csm4."
FT /evidence="ECO:0000269|PubMed:25451598"
FT MUTAGEN 214..215
FT /note="YY->AA: No longer interacts with Csm4."
FT /evidence="ECO:0000269|PubMed:25451598"
FT MUTAGEN 216
FT /note="E->A: Wild-type interaction with Csm4."
FT /evidence="ECO:0000269|PubMed:25451598"
FT STRAND 8..20
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 52..65
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 156..165
FT /evidence="ECO:0007829|PDB:4QTS"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 200..211
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:4QTS"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:4QTS"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:4QTS"
SQ SEQUENCE 248 AA; 28159 MW; C68C09C5FC256BB1 CRC64;
MENLTLKGKV ILEGIIELET GMHIGGTKET LKIGGTDNPV IRDAFGRILI PGSSLKGKIR
ALLERKDGKY KEDGRGNYLP HDCGECEICK IFGPHDSKNI KEPVRVIVRD AYLQPEENKK
DYDYLEIKVE NTIDRLKGTT IKGGIRNMER VVAGSKFKFE VVFNIYKESD KELIKKFIEG
MKLLEDDYLG GSGSRGYGKI KFRDIKLICK PKEYYEGNEN SKKESDEVES LNELESELDK
IWGGINFN
