CAS6B_SACS2
ID CAS6B_SACS2 Reviewed; 289 AA.
AC Q97WV8;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=CRISPR-associated endoribonuclease Cas6 2;
DE EC=3.1.-.-;
GN Name=cas6b; OrderedLocusNames=SSO2004;
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 FUNCTION AS AN ENDORIBONUCLEASE.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=21507944; DOI=10.1074/jbc.m111.238485;
RA Lintner N.G., Kerou M., Brumfield S.K., Graham S., Liu H., Naismith J.H.,
RA Sdano M., Peng N., She Q., Copie V., Young M.J., White M.F., Lawrence C.M.;
RT "Structural and functional characterization of an archaeal clustered
RT regularly interspaced short palindromic repeat (CRISPR)-associated complex
RT for antiviral defense (CASCADE).";
RL J. Biol. Chem. 286:21643-21656(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).
CC Functions as a ssRNA-specific endoribonuclease, generating an 8 base-
CC long tag known as the 5' handle. {ECO:0000269|PubMed:21507944}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBUNIT: Possibly part of the aCascade ribonucleoprotein complex.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas6
CC family. {ECO:0000305}.
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DR EMBL; AE006641; AAK42192.1; -; Genomic_DNA.
DR PIR; A99367; A99367.
DR RefSeq; WP_009992200.1; NC_002754.1.
DR PDB; 4ILL; X-ray; 2.48 A; A/B=1-289.
DR PDB; 4ILM; X-ray; 3.07 A; A/B/D/F/H/J/L/N=1-289.
DR PDB; 4ILR; X-ray; 3.09 A; A=1-289.
DR PDBsum; 4ILL; -.
DR PDBsum; 4ILM; -.
DR PDBsum; 4ILR; -.
DR AlphaFoldDB; Q97WV8; -.
DR SMR; Q97WV8; -.
DR DIP; DIP-60141N; -.
DR STRING; 273057.SSO2004; -.
DR EnsemblBacteria; AAK42192; AAK42192; SSO2004.
DR GeneID; 27428328; -.
DR KEGG; sso:SSO2004; -.
DR PATRIC; fig|273057.12.peg.2079; -.
DR eggNOG; arCOG01439; Archaea.
DR HOGENOM; CLU_929391_0_0_2; -.
DR InParanoid; Q97WV8; -.
DR OMA; KVRAFKF; -.
DR Proteomes; UP000001974; 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 InterPro; IPR041165; Cas6_N_arch.
DR InterPro; IPR019267; CRISPR-assoc_Cas6_C.
DR InterPro; IPR010156; CRISPR-assoc_prot_Cas6.
DR Pfam; PF17952; Cas6_N; 1.
DR Pfam; PF10040; CRISPR_Cas6; 1.
DR TIGRFAMs; TIGR01877; cas_cas6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Endonuclease; Hydrolase; Magnesium;
KW Nuclease; Reference proteome; RNA-binding.
FT CHAIN 1..289
FT /note="CRISPR-associated endoribonuclease Cas6 2"
FT /id="PRO_0000417884"
FT STRAND 3..15
FT /evidence="ECO:0007829|PDB:4ILL"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:4ILL"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:4ILL"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:4ILL"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:4ILL"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:4ILL"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4ILM"
FT TURN 94..98
FT /evidence="ECO:0007829|PDB:4ILL"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:4ILL"
FT STRAND 108..121
FT /evidence="ECO:0007829|PDB:4ILL"
FT HELIX 122..129
FT /evidence="ECO:0007829|PDB:4ILL"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4ILL"
FT STRAND 135..145
FT /evidence="ECO:0007829|PDB:4ILL"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:4ILL"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4ILL"
FT TURN 158..163
FT /evidence="ECO:0007829|PDB:4ILL"
FT HELIX 174..188
FT /evidence="ECO:0007829|PDB:4ILL"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:4ILL"
FT STRAND 210..223
FT /evidence="ECO:0007829|PDB:4ILL"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:4ILR"
FT STRAND 232..244
FT /evidence="ECO:0007829|PDB:4ILL"
FT HELIX 248..264
FT /evidence="ECO:0007829|PDB:4ILL"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:4ILM"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:4ILL"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4ILM"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:4ILL"
SQ SEQUENCE 289 AA; 32637 MW; 03ADDA6E415DDC83 CRC64;
MPLIFKIGYN VIPLQDVILP TPSSKVLKYL IQSGKLIPSL KDLITSRDKY KPIFISHLGF
NQRRIFQTNG NLKTITKGSR LSSIIAFSTQ ANVLSEVADE GIFETVYGKF HIMIESIEIV
EVEKLKEEVE KHMNDNIRVR FVSPTLLSSK VLLPPSLSER YKKIHAGYST LPSVGLIVAY
AYNVYCNLIG KKEVEVRAFK FGILSNALSR IIGYDLHPVT VAIGEDSKGN LRKARGVMGW
IEFDIPDERL KRRALNYLLT SSYLGIGRSR GIGFGEIRLE FRKIEEKEG
