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CRISPR type I-A cluster 1/Apern-associated protein Csa5-1

 CSA5A_SULSO             Reviewed;         162 AA.
Q97YC8;
16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 1.
05-DEC-2018, entry version 64.
RecName: Full=CRISPR type I-A cluster 1/Apern-associated protein Csa5-1;
Name=csa5; OrderedLocusNames=SSO1398;
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 /
P2).
Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
Saccharolobus.
NCBI_TaxID=273057;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
PubMed=11427726; DOI=10.1073/pnas.141222098;
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G.,
Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A.,
De Moors A., Erauso G., Fletcher C., Gordon P.M.K.,
Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X.,
Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N.,
Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
"The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
[2]
X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF
ASP-35.
PubMed=23846216; DOI=10.4161/rna.23854;
Reeks J., Graham S., Anderson L., Liu H., White M.F., Naismith J.H.;
"Structure of the archaeal Cascade subunit Csa5: relating the small
subunits of CRISPR effector complexes.";
RNA Biol. 10:762-769(2013).
-!- FUNCTION: CRISPR (clustered regularly interspaced short
palindromic repeat) is an adaptive immune system that provides
protection against mobile genetic elements (viruses, transposable
elements and conjugative plasmids). CRISPR clusters contain
spacers, sequences complementary to antecedent mobile elements,
and target invading nucleic acids. CRISPR clusters are transcribed
and processed into CRISPR RNA (crRNA). {ECO:0000305}.
-!- SUBUNIT: Oligomerizes as an infinite helical thread in crystal
structure; disrupting a potential salt bridge between Asp-35 and
Arg-55 leads to altered elution from a sizing column. By
immunoprecipitation Csa5 interacts weakly with a Cas5/Cas7
complex. There are 3 csa5, 3 cas5 and 2 cas7 genes in this
organism; the immunoprecipitation studies may not distinguish
between them. {ECO:0000269|PubMed:23846216}.
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EMBL; AE006641; AAK41633.1; -; Genomic_DNA.
PIR; B99297; B99297.
RefSeq; WP_009988390.1; NC_002754.1.
PDB; 3ZC4; X-ray; 2.72 A; A/B/C/D/E/F/G/H/I=1-162.
PDBsum; 3ZC4; -.
SMR; Q97YC8; -.
STRING; 273057.SSO1398; -.
EnsemblBacteria; AAK41633; AAK41633; SSO1398.
GeneID; 27427768; -.
KEGG; sso:SSO1398; -.
PATRIC; fig|273057.12.peg.1414; -.
eggNOG; arCOG03823; Archaea.
eggNOG; ENOG410YQTW; LUCA.
HOGENOM; HOG000108497; -.
OMA; VVHEIVD; -.
OrthoDB; POG093Z0CP6; -.
BioCyc; SSOL273057:G1FZF-1469-MONOMER; -.
Proteomes; UP000001974; Chromosome.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
1: Evidence at protein level;
3D-structure; Antiviral defense; Complete proteome;
Reference proteome.
CHAIN 1 162 CRISPR type I-A cluster 1/Apern-
associated protein Csa5-1.
/FTId=PRO_0000435656.
MUTAGEN 35 35 D->A: Altered protein oligomerization,
protein has a smaller radius of gyration,
elution from a sizing column is altered.
{ECO:0000269|PubMed:23846216}.
HELIX 7 14 {ECO:0000244|PDB:3ZC4}.
HELIX 16 27 {ECO:0000244|PDB:3ZC4}.
HELIX 31 33 {ECO:0000244|PDB:3ZC4}.
HELIX 35 39 {ECO:0000244|PDB:3ZC4}.
HELIX 43 63 {ECO:0000244|PDB:3ZC4}.
STRAND 65 72 {ECO:0000244|PDB:3ZC4}.
STRAND 75 77 {ECO:0000244|PDB:3ZC4}.
STRAND 79 89 {ECO:0000244|PDB:3ZC4}.
HELIX 91 93 {ECO:0000244|PDB:3ZC4}.
HELIX 98 101 {ECO:0000244|PDB:3ZC4}.
TURN 103 105 {ECO:0000244|PDB:3ZC4}.
STRAND 106 109 {ECO:0000244|PDB:3ZC4}.
STRAND 115 117 {ECO:0000244|PDB:3ZC4}.
STRAND 120 123 {ECO:0000244|PDB:3ZC4}.
STRAND 126 129 {ECO:0000244|PDB:3ZC4}.
HELIX 134 146 {ECO:0000244|PDB:3ZC4}.
HELIX 149 159 {ECO:0000244|PDB:3ZC4}.
STRAND 160 162 {ECO:0000244|PDB:3ZC4}.
SEQUENCE 162 AA; 18523 MW; 12622E57398E516B CRC64;
MEASEPVAET ISKRFWTLIK MLRFYVVLRR FGYIDPLIYS IDPKQIKDVL SEALREFVSY
TSSSSSRSIV IYDDPKNPVT AQAPCLVVAK RDEIPQNFPS IYRYTIYKID KSSEYCISPL
VVNDKYATLI TPNESVIKEF FDKLDSNIQY ARVLASLAVG GE


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