CAS6A_SACS2
ID CAS6A_SACS2 Reviewed; 287 AA.
AC Q97Y96;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=CRISPR-associated endoribonuclease Cas6 1;
DE EC=3.1.-.-;
GN Name=cas6a; OrderedLocusNames=SSO1437;
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 SUBUNIT.
RC STRAIN=ATCC 35091 / DSM 1616 / JCM 8930 / NBRC 15331 / P1;
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 spacers, sequences complementary to
CC antecedent mobile elements, and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA) (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the aCascade ribonucleoprotein complex, minimally
CC composed of Csa2 and Cas5a, which binds crRNA. Other possible
CC components of aCascade in strain P1 are Cas6b (SSO1437) and Csa5
CC (SSO1443), while SSO1399, Cas5b (SSO1400) and SSO1401 have sometimes
CC been seen weakly associated. Csa2 is probably the major RNA-binding
CC subunit. The Csa2-Cas5a-crRNA complex also binds target DNA homologous
CC to crRNA, probably forming an R-loop. Purified aCascade forms a
CC filament about 6 nm in width. {ECO:0000269|PubMed:21507944}.
CC -!- MISCELLANEOUS: The aCascade complex was purified from strain P1.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas6
CC family. {ECO:0000305}.
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DR EMBL; AE006641; AAK41670.1; -; Genomic_DNA.
DR PIR; G90301; G90301.
DR RefSeq; WP_010923402.1; NC_002754.1.
DR PDB; 3ZFV; X-ray; 2.80 A; A/B/C/D=2-287.
DR PDBsum; 3ZFV; -.
DR AlphaFoldDB; Q97Y96; -.
DR SMR; Q97Y96; -.
DR STRING; 273057.SSO1437; -.
DR EnsemblBacteria; AAK41670; AAK41670; SSO1437.
DR GeneID; 27427805; -.
DR KEGG; sso:SSO1437; -.
DR PATRIC; fig|273057.12.peg.1466; -.
DR eggNOG; arCOG01439; Archaea.
DR HOGENOM; CLU_929391_0_0_2; -.
DR InParanoid; Q97Y96; -.
DR OMA; KVINFRM; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; 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; Nuclease;
KW Reference proteome.
FT CHAIN 1..287
FT /note="CRISPR-associated endoribonuclease Cas6 1"
FT /id="PRO_0000417883"
FT STRAND 3..15
FT /evidence="ECO:0007829|PDB:3ZFV"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:3ZFV"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3ZFV"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3ZFV"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:3ZFV"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:3ZFV"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:3ZFV"
FT STRAND 107..120
FT /evidence="ECO:0007829|PDB:3ZFV"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:3ZFV"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:3ZFV"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:3ZFV"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:3ZFV"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3ZFV"
FT TURN 157..162
FT /evidence="ECO:0007829|PDB:3ZFV"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:3ZFV"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:3ZFV"
FT STRAND 209..221
FT /evidence="ECO:0007829|PDB:3ZFV"
FT STRAND 232..243
FT /evidence="ECO:0007829|PDB:3ZFV"
FT HELIX 247..263
FT /evidence="ECO:0007829|PDB:3ZFV"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:3ZFV"
FT STRAND 276..281
FT /evidence="ECO:0007829|PDB:3ZFV"
SQ SEQUENCE 287 AA; 32425 MW; 13E4FE6603783A94 CRC64;
MPLIFKIGYN VIPLQDVILP TPSSKVLKYL IQSGKLLPSL NNLITSRDKY KPIFISHLGL
NQRRIFQTNG NLKTISRGSK LSSTIAFSTQ VNVLPELDEG VFETIYGKFH ITIESVEIVE
VEKLKEEVEK HMNDNIRVRF ISPTLLSSKV LLPPSLSERY KRVNAGYSTL PSVGLIVAYA
YNVYCNLIGK KEVEVRAFKF GVISNALSRI IGYDLHPVTI VIGEDSKGNL RKARGVMGWI
EFDIPDEKLK RRALRYLLAS SYLGIGRSRG IGFGEIKLEF IKREENH
