CAS2A_SACS2
ID CAS2A_SACS2 Reviewed; 101 AA.
AC Q97YC2;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=CRISPR-associated endoribonuclease Cas2 1;
DE EC=3.1.-.-;
DE AltName: Full=CAS2 endoribonuclease;
GN Name=cas21; OrderedLocusNames=SSO1404;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS), FUNCTION AS A SSRNA-SPECIFIC
RP ENDORIBONUCLEASE, SUBSTRATE SPECIFICITY, PH-DEPENDENCE, COFACTOR, SUBUNIT,
RP AND MUTAGENESIS OF TYR-9; ASP-10; ARG-17; ARG-19; ARG-31 AND PHE-37.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=18482976; DOI=10.1074/jbc.m803225200;
RA Beloglazova N., Brown G., Zimmerman M.D., Proudfoot M., Makarova K.S.,
RA Kudritska M., Kochinyan S., Wang S., Chruszcz M., Minor W., Koonin E.V.,
RA Edwards A.M., Savchenko A., Yakunin A.F.;
RT "A novel family of sequence-specific endoribonucleases associated with the
RT clustered regularly interspaced short palindromic repeats.";
RL J. Biol. Chem. 283:20361-20371(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 2-101.
RX PubMed=20419351; DOI=10.1007/s10969-010-9090-y;
RA Oke M., Carter L.G., Johnson K.A., Liu H., McMahon S.A., Yan X., Kerou M.,
RA Weikart N.D., Kadi N., Sheikh M.A., Schmelz S., Dorward M., Zawadzki M.,
RA Cozens C., Falconer H., Powers H., Overton I.M., van Niekerk C.A., Peng X.,
RA Patel P., Garrett R.A., Prangishvili D., Botting C.H., Coote P.J.,
RA Dryden D.T., Barton G.J., Schwarz-Linek U., Challis G.L., Taylor G.L.,
RA White M.F., Naismith J.H.;
RT "The Scottish Structural Proteomics Facility: targets, methods and
RT outputs.";
RL J. Struct. Funct. Genomics 11:167-180(2010).
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).
CC Involved in the integration of spacer DNA into the CRISPR cassette (By
CC similarity). Functions as a ssRNA-specific endoribonuclease, producing
CC a 5'-phosphomonoester and a 3'-hydroxy. Does not process pre-crRNA in
CC the manner expected if it were the CRISPR-processing endoribonuclease.
CC Prefers U-rich substrates and often cuts between adjacent U residues in
CC regions predicted to be single-stranded. RNAs as short as 10 residues
CC can serve as substrate. {ECO:0000250, ECO:0000269|PubMed:18482976}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18482976};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5-9.0.;
CC -!- SUBUNIT: Forms a heterotetramer with a Cas1 homodimer (By similarity).
CC Homodimer. {ECO:0000250, ECO:0000269|PubMed:18482976}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas2
CC protein family. {ECO:0000305}.
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DR EMBL; AE006641; AAK41639.1; -; Genomic_DNA.
DR PIR; H90297; H90297.
DR PDB; 2I8E; X-ray; 1.59 A; A=1-101.
DR PDB; 2IVY; X-ray; 1.40 A; A=2-101.
DR PDBsum; 2I8E; -.
DR PDBsum; 2IVY; -.
DR AlphaFoldDB; Q97YC2; -.
DR SMR; Q97YC2; -.
DR STRING; 273057.SSO1404; -.
DR EnsemblBacteria; AAK41639; AAK41639; SSO1404.
DR KEGG; sso:SSO1404; -.
DR PATRIC; fig|273057.12.peg.1420; -.
DR eggNOG; arCOG04194; Archaea.
DR HOGENOM; CLU_161124_2_0_2; -.
DR InParanoid; Q97YC2; -.
DR OMA; DEENVIW; -.
DR PhylomeDB; Q97YC2; -.
DR BRENDA; 3.1.26.12; 6163.
DR EvolutionaryTrace; Q97YC2; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-UniRule.
DR GO; GO:0043571; P:maintenance of CRISPR repeat elements; IEA:UniProtKB-UniRule.
DR CDD; cd09725; Cas2_I_II_III; 1.
DR HAMAP; MF_01471; Cas2; 1.
DR InterPro; IPR021127; CRISPR_associated_Cas2.
DR InterPro; IPR019199; Virulence_VapD/CRISPR_Cas2.
DR PANTHER; PTHR34405; PTHR34405; 1.
DR Pfam; PF09827; CRISPR_Cas2; 1.
DR TIGRFAMs; TIGR01573; cas2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..101
FT /note="CRISPR-associated endoribonuclease Cas2 1"
FT /id="PRO_0000416951"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT MUTAGEN 9
FT /note="Y->A: Considerable loss of RNase activity."
FT /evidence="ECO:0000269|PubMed:18482976"
FT MUTAGEN 10
FT /note="D->A: Loss of RNase activity."
FT /evidence="ECO:0000269|PubMed:18482976"
FT MUTAGEN 17
FT /note="R->A: Considerable loss of RNase activity."
FT /evidence="ECO:0000269|PubMed:18482976"
FT MUTAGEN 19
FT /note="R->A: Considerable loss of RNase activity."
FT /evidence="ECO:0000269|PubMed:18482976"
FT MUTAGEN 31
FT /note="R->A: Loss of RNase activity."
FT /evidence="ECO:0000269|PubMed:18482976"
FT MUTAGEN 37
FT /note="F->A: Loss of RNase activity."
FT /evidence="ECO:0000269|PubMed:18482976"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2IVY"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:2IVY"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:2IVY"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2IVY"
FT HELIX 43..56
FT /evidence="ECO:0007829|PDB:2IVY"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:2IVY"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:2IVY"
SQ SEQUENCE 101 AA; 11936 MW; A7C338AD76202E17 CRC64;
MAMLYLIFYD ITDDNLRNRV AEFLKKKGLD RIQYSVFMGD LNSSRLKDVE AGLKIIGNRK
KLQEDERFFI LIVPITENQF RERIVIGYSG SEREEKSNVV W
