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CRISPR-associated endonuclease Cas12a (EC 3.1.21.1) (EC 3.1.27.2) (CRISPR-associated endonuclease Cpf1) (FnCas12a) (FnCpf1)

 CS12A_FRATN             Reviewed;        1300 AA.
A0Q7Q2;
09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
09-JAN-2007, sequence version 1.
28-MAR-2018, entry version 51.
RecName: Full=CRISPR-associated endonuclease Cas12a {ECO:0000303|PubMed:28111461};
EC=3.1.21.1 {ECO:0000269|PubMed:28431230};
EC=3.1.27.2 {ECO:0000269|PubMed:28431230};
AltName: Full=CRISPR-associated endonuclease Cpf1 {ECO:0000303|PubMed:26422227};
AltName: Full=FnCas12a {ECO:0000303|PubMed:28431230};
AltName: Full=FnCpf1 {ECO:0000303|PubMed:26422227};
Name=cas12a {ECO:0000303|PubMed:28111461};
Synonyms=cpf1 {ECO:0000303|PubMed:26422227};
OrderedLocusNames=FTN_1397;
Francisella tularensis subsp. novicida (strain U112).
Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
Francisellaceae; Francisella.
NCBI_TaxID=401614;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=U112;
PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J.,
Radey M., Guina T., Svensson K., Hayden H.S., Jacobs M.,
Gallagher L.A., Manoil C., Ernst R.K., Drees B., Buckley D.,
Haugen E., Bovee D., Zhou Y., Chang J., Levy R., Lim R., Gillett W.,
Guenthener D., Kang A., Shaffer S.A., Taylor G., Chen J., Gallis B.,
D'Argenio D.A., Forsman M., Olson M.V., Goodlett D.R., Kaul R.,
Miller S.I., Brittnacher M.J.;
"Comparison of Francisella tularensis genomes reveals evolutionary
events associated with the emergence of human pathogenic strains.";
Genome Biol. 8:R102.1-R102.16(2007).
[2]
FUNCTION IN PLASMID RESISTANCE, FUNCTION IN CRRNA FORMATION, FUNCTION
AS AN ENDONUCLEASE, POSSIBLE ACTIVE SITE, COFACTOR, POSSIBLE SUBUNIT,
AND MUTAGENESIS OF ASP-917; GLU-1006 AND ASP-1255.
STRAIN=U112;
PubMed=26422227; DOI=10.1016/j.cell.2015.09.038;
Zetsche B., Gootenberg J.S., Abudayyeh O.O., Slaymaker I.M.,
Makarova K.S., Essletzbichler P., Volz S.E., Joung J.,
van der Oost J., Regev A., Koonin E.V., Zhang F.;
"Cpf1 is a single RNA-guided endonuclease of a class 2 CRISPR-Cas
system.";
Cell 163:759-771(2015).
[3]
DISCUSSION OF SEQUENCE.
PubMed=26593719; DOI=10.1016/j.molcel.2015.10.008;
Shmakov S., Abudayyeh O.O., Makarova K.S., Wolf Y.I., Gootenberg J.S.,
Semenova E., Minakhin L., Joung J., Konermann S., Severinov K.,
Zhang F., Koonin E.V.;
"Discovery and functional characterization of diverse class 2 CRISPR-
Cas systems.";
Mol. Cell 60:385-397(2015).
[4]
FUNCTION IN CRRNA PROCESSING, FUNCTION AS AN ENDORIBONUCLEASE,
FUNCTION AS AN ENDONUCLEASE, COFACTOR, SUBUNIT, MUTAGENESIS OF
HIS-843; LYS-852; LYS-869; PHE-873; ASP-917; GLU-920; HIS-922;
TYR-925; GLU-1006; TYR-1024; GLU-1028; ASP-1227 AND ASP-1255,
DNA-BINDING, AND RNA-BINDING.
STRAIN=U112;
PubMed=27096362; DOI=10.1038/nature17945;
Fonfara I., Richter H., Bratovic M., Le Rhun A., Charpentier E.;
"The CRISPR-associated DNA-cleaving enzyme Cpf1 also processes
precursor CRISPR RNA.";
Nature 532:517-521(2016).
[5]
BIOTECHNOLOGY.
PubMed=27905529; DOI=10.1038/srep38169;
Endo A., Masafumi M., Kaya H., Toki S.;
"Efficient targeted mutagenesis of rice and tobacco genomes using Cpf1
from Francisella novicida.";
Sci. Rep. 6:38169-38169(2016).
[6]
BIOTECHNOLOGY.
PubMed=27272384; DOI=10.1038/nbt.3609;
Kim D., Kim J., Hur J.K., Been K.W., Yoon S.H., Kim J.S.;
"Genome-wide analysis reveals specificities of Cpf1 endonucleases in
human cells.";
Nat. Biotechnol. 34:863-868(2016).
[7]
NOMENCLATURE.
PubMed=28111461; DOI=10.1038/nrmicro.2016.184;
Shmakov S., Smargon A., Scott D., Cox D., Pyzocha N., Yan W.,
Abudayyeh O.O., Gootenberg J.S., Makarova K.S., Wolf Y.I.,
Severinov K., Zhang F., Koonin E.V.;
"Diversity and evolution of class 2 CRISPR-Cas systems.";
Nat. Rev. Microbiol. 15:169-182(2017).
[8] {ECO:0000244|PDB:5NFV, ECO:0000244|PDB:5NG6}
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-1300 IN COMPLEX WITH GUIDE
RNA WITH AND WITHOUT TARGET DNA, FUNCTION IN CRRNA PROCESSING,
FUNCTION AS AN ENDONUCLEASE, ACTIVE SITE, CATALYTIC ACTIVITY, REACTION
MECHANISM, COFACTOR, SUBUNIT, DOMAIN, MUTAGENESIS OF ARG-692;
689-THR--SER-702; GLN-704; ASP-917; GLU-1006; ARG-1218 AND ASP-1255,
DNA-BINDING, AND RNA-BINDING.
STRAIN=U112;
PubMed=28431230; DOI=10.1016/j.molcel.2017.03.016;
Swarts D.C., van der Oost J., Jinek M.;
"Structural basis for guide RNA processing and seed-dependent DNA
targeting by CRISPR-Cas12a.";
Mol. Cell 66:221-233(2017).
[9] {ECO:0000244|PDB:5MGA}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH GUIDE RNA AND
PRODUCT DNA, FUNCTION AS AN ENDONUCLEASE, COFACTOR, DOMAIN,
MUTAGENESIS OF GLY-608; PRO-663; ASN-666; LYS-667; LYS-671; LYS-677;
ARG-692; HIS-694; GLU-1006; 1065-LYS-LYS-1066 AND ARG-1218,
DNA-BINDING, AND RNA-BINDING.
STRAIN=U112;
PubMed=28562584; DOI=10.1038/nature22398;
Stella S., Alcon P., Montoya G.;
"Structure of the Cpf1 endonuclease R-loop complex after target DNA
cleavage.";
Nature 546:559-563(2017).
[10]
ERRATUM.
PubMed=28678773; DOI=10.1038/nature23300;
Stella S., Alcon P., Montoya G.;
"Structure of the Cpf1 endonuclease R-loop complex after target DNA
cleavage.";
Nature 547:476-476(2017).
-!- 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
sequences complementary to antecedent mobile elements and target
invading nucleic acids. CRISPR clusters are transcribed and
processed into CRISPR RNA (crRNA). Has endonuclease activity on
pre-crRNA and dsDNA, using different active sites. A single-RNA
guided endonuclease that is also capable of guiding crRNA
processing; correct processing of pre-crRNA requires only this
protein and the CRISPR locus (PubMed:26422227, PubMed:27096362).
pre-crRNA processing proceeds by an intramolecular nucleophilic
attack on the scissile phosphate by the 2'-OH of the upstream
ribonucleotide, the divalent cation (which is bound by the crRNA)
is probably required for ordering the crRNA pseudoknot and/or
increasing RNA binding (PubMed:28431230). RNA mutagenesis studies
show pre-crRNA cleavage is highly sequence- and structure-specific
(PubMed:27096362). Forms a complex with crRNA and complementary
dsDNA, where the crRNA displaces the non-target DNA strand and
directs endonucleolytic cleavage of both strands of the DNA
(PubMed:26422227, PubMed:27096362, PubMed:28431230). Cleavage
results in staggered 5-base 5' overhangs 14-18 and 21-23 bases
downstream of the PAM (protospacer adjacent motif) on the non-
target and target strands respectively (PubMed:26422227,
PubMed:28431230, PubMed:28562584). Both target and non-target
strand DNA are probably independently cleaved in the same active
site (PubMed:28431230, PubMed:28562584). When this protein is
expressed in E.coli it prevents plasmids homologous to the first
CRISPR spacer from transforming, formally showing it is
responsible for plasmid immunity (PubMed:26422227).
{ECO:0000269|PubMed:26422227, ECO:0000269|PubMed:27096362,
ECO:0000269|PubMed:28431230, ECO:0000269|PubMed:28562584}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphodinucleotide and 5'-phosphooligonucleotide end-products.
{ECO:0000269|PubMed:28431230}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 2',3'-cyclic
nucleotides. {ECO:0000269|PubMed:28431230}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:26593719};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:26422227,
ECO:0000269|PubMed:26593719, ECO:0000269|PubMed:27096362,
ECO:0000269|PubMed:28562584};
Note=Cleavage of dsDNA requires Mg(2+) (PubMed:26422227,
PubMed:28562584). Another report shows DNA cleavage occurs equally
well in the presence of Ca(2+) or Mg(2+) (PubMed:27096362).
Processing of pre-crRNA requires a divalent cation, preferably
Mg(2+) which is bound by the crRNA (PubMed:26593719,
PubMed:28431230). {ECO:0000269|PubMed:26422227,
ECO:0000269|PubMed:26593719, ECO:0000269|PubMed:27096362,
ECO:0000269|PubMed:28431230, ECO:0000269|PubMed:28562584};
-!- SUBUNIT: Might be a homodimer (PubMed:26422227). Might be a
monomer (PubMed:27096362, PubMed:28431230).
{ECO:0000269|PubMed:26422227, ECO:0000269|PubMed:27096362,
ECO:0000269|PubMed:28431230}.
-!- DOMAIN: Has bilobed structure, with the REC lobe (residues 25-591)
connected to the NUC lobe (662-1300) by a discontinuous wedge
domain (PubMed:28431230, PubMed:28562584). The REC lobe binds the
(pre-)crRNA and the crRNA-target DNA heteroduplex
(PubMed:28431230, PubMed:28562584). The heteroduplex as well as
part of the DNA downstream of the heteroduplex is protected in the
central cavity formed by the NUC and REC lobes, which also
positions target and non-target DNA for cleavage after domain
rearrangement (PubMed:28431230, PubMed:28562584). The LKL region
(residues 662 to 679) inserts into target dsDNA initiating its
disruption to allow crRNA hybridization, is also involved in
determining the non-target strand cleavage site (PubMed:28562584).
A 'septum' formed by resdiues 197-204 and 1061-1070 separates the
2 DNA strands, preventing their reannealing, this region also
influences the non-target cleavage site (PubMed:28562584).
{ECO:0000269|PubMed:28431230, ECO:0000269|PubMed:28562584}.
-!- BIOTECHNOLOGY: This class of CRISPR enzymes recognize a 5' T-rich
protospacer adjacent motif (PAM, TTN for this specific enzyme),
unlike Cas9 enzymes which recognize 3' G-rich PAMs, thus this
enzyme increases the possibilites for genome editing
(PubMed:26422227). The simplicity of the Cas12a-crRNA directed DNA
endonuclease activity has been used to target and modify DNA
sequences in rice and tobacco (PubMed:27905529).
{ECO:0000269|PubMed:27272384, ECO:0000269|PubMed:27905529,
ECO:0000305|PubMed:26422227}.
-!- MISCELLANEOUS: Part of a type V-A CRISPR-Cas system.
{ECO:0000305|PubMed:26593719, ECO:0000305|PubMed:28111461}.
-!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas12a
family. {ECO:0000305|PubMed:28111461}.
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EMBL; CP000439; ABK90267.1; -; Genomic_DNA.
RefSeq; WP_003040289.1; NZ_CP009633.1.
PDB; 5MGA; X-ray; 3.00 A; A=1-1300.
PDB; 5NFV; X-ray; 2.50 A; A=2-1300.
PDB; 5NG6; X-ray; 3.34 A; A/C/E/G=2-1300.
PDBsum; 5MGA; -.
PDBsum; 5NFV; -.
PDBsum; 5NG6; -.
ProteinModelPortal; A0Q7Q2; -.
SMR; A0Q7Q2; -.
EnsemblBacteria; ABK90267; ABK90267; FTN_1397.
KEGG; ftn:FTN_1397; -.
KEGG; ftx:AW25_605; -.
HOGENOM; HOG000066230; -.
OMA; QIYNKDF; -.
BioCyc; FTUL401614:G1G75-1444-MONOMER; -.
Proteomes; UP000000762; Chromosome.
GO; GO:0033898; F:Bacillus subtilis ribonuclease activity; IEA:UniProtKB-EC.
GO; GO:0004530; F:deoxyribonuclease I activity; IEA:UniProtKB-EC.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
InterPro; IPR027620; Cas12a.
TIGRFAMs; TIGR04330; cas_Cpf1; 1.
1: Evidence at protein level;
3D-structure; Antiviral defense; Calcium; Complete proteome;
DNA-binding; Endonuclease; Hydrolase; Magnesium; Nuclease;
RNA-binding.
CHAIN 1 1300 CRISPR-associated endonuclease Cas12a.
/FTId=PRO_0000434902.
REGION 1 24 Wedge region 1.
{ECO:0000303|PubMed:28431230,
ECO:0000303|PubMed:28562584}.
REGION 25 339 Recognition domain 1.
{ECO:0000303|PubMed:28431230,
ECO:0000303|PubMed:28562584}.
REGION 47 51 Binds crRNA alone and in crRNA-target DNA
heteroduplex.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
REGION 182 186 Binds crRNA alone and in crRNA-target DNA
heteroduplex.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
REGION 301 305 Binds DNA in crRNA-target DNA
heteroduplex.
{ECO:0000269|PubMed:28431230}.
REGION 326 329 Binds crRNA in crRNA-target DNA
heteroduplex.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
REGION 340 591 Recognition domain 2.
{ECO:0000303|PubMed:28431230,
ECO:0000303|PubMed:28562584}.
REGION 538 541 Binds crRNA in crRNA-target DNA
heteroduplex.
{ECO:0000269|PubMed:28431230}.
REGION 591 595 Binds crRNA.
{ECO:0000269|PubMed:28431230}.
REGION 592 662 Wedge region 2.
{ECO:0000303|PubMed:28431230,
ECO:0000303|PubMed:28562584}.
REGION 662 679 LKL, important for PAM recognition and
DNA unwinding.
{ECO:0000305|PubMed:28562584}.
REGION 663 762 PAM-interacting domain (PI).
{ECO:0000303|PubMed:28431230,
ECO:0000303|PubMed:28562584}.
REGION 671 677 Binds DNA protospacer adjacent motif
(PAM) on target DNA.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
REGION 692 704 Binds single-strand non-target DNA.
{ECO:0000269|PubMed:28431230}.
REGION 763 892 Wedge region 3.
{ECO:0000303|PubMed:28431230,
ECO:0000303|PubMed:28562584}.
REGION 791 794 Binds crRNA.
{ECO:0000269|PubMed:28431230}.
REGION 803 804 Binds crRNA.
{ECO:0000269|PubMed:28431230}.
REGION 851 853 Binds crRNA.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
REGION 865 873 Binds crRNA.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
REGION 893 953 RuvC-I. {ECO:0000303|PubMed:28431230,
ECO:0000303|PubMed:28562584}.
REGION 954 971 Bridge helix.
{ECO:0000303|PubMed:28431230,
ECO:0000303|PubMed:28562584}.
REGION 972 1078 RuvC-II. {ECO:0000303|PubMed:28431230,
ECO:0000303|PubMed:28562584}.
REGION 1079 1254 Nuclease domain.
{ECO:0000303|PubMed:28431230,
ECO:0000303|PubMed:28562584}.
REGION 1255 1300 RuvC-III. {ECO:0000303|PubMed:28431230,
ECO:0000303|PubMed:28562584}.
ACT_SITE 843 843 For pre-crRNA processing.
{ECO:0000305|PubMed:28431230}.
ACT_SITE 852 852 For pre-crRNA processing.
{ECO:0000305|PubMed:28431230}.
ACT_SITE 869 869 For pre-crRNA processing.
{ECO:0000305|PubMed:28431230}.
ACT_SITE 917 917 For DNase activity of RuvC domain.
{ECO:0000305|PubMed:26422227}.
ACT_SITE 1006 1006 For DNase activity of RuvC domain.
{ECO:0000305|PubMed:26422227}.
ACT_SITE 1255 1255 For DNase activity of RuvC domain.
{ECO:0000305|PubMed:26422227}.
BINDING 16 16 crRNA alone and in crRNA-target DNA
heteroduplex.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
BINDING 131 131 Target strand DNA.
{ECO:0000269|PubMed:28431230}.
BINDING 295 295 crRNA in crRNA-target DNA heteroduplex.
{ECO:0000269|PubMed:28431230}.
BINDING 320 320 DNA in crRNA-target DNA heteroduplex.
{ECO:0000269|PubMed:28431230}.
BINDING 334 334 DNA in crRNA-target DNA heteroduplex.
{ECO:0000269|PubMed:28431230}.
BINDING 589 589 DNA in crRNA-target DNA heteroduplex.
{ECO:0000269|PubMed:28431230}.
BINDING 613 613 DNA protospacer adjacent motif (PAM).
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
BINDING 667 667 Target strand DNA.
{ECO:0000269|PubMed:28431230}.
BINDING 671 671 PAM. {ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
BINDING 677 677 Target strand DNA.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
BINDING 823 823 Target strand DNA.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
BINDING 826 826 Target strand DNA; via amide nitrogen.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
BINDING 833 833 crRNA. {ECO:0000269|PubMed:28431230}.
BINDING 1026 1026 DNA in crRNA-target DNA heteroduplex.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
BINDING 1063 1063 DNA in crRNA-target DNA heteroduplex.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
SITE 410 410 Caps the crRNA-target DNA heteroduplex.
{ECO:0000305|PubMed:28431230}.
SITE 852 852 Stabilizes transition state for pre-crRNA
processing.
{ECO:0000305|PubMed:28431230}.
MUTAGEN 608 608 G->A,E: 15% DNA cleavage.
{ECO:0000269|PubMed:28562584}.
MUTAGEN 663 663 P->A: 25% DNA cleavage, altered non-
target strand cleavage products.
{ECO:0000269|PubMed:28562584}.
MUTAGEN 666 666 N->A: 80% DNA cleavage, altered non-
target strand cleavage products.
{ECO:0000269|PubMed:28562584}.
MUTAGEN 667 667 K->A: 30% DNA cleavage.
{ECO:0000269|PubMed:28562584}.
MUTAGEN 671 671 K->A: 15% DNA cleavage.
{ECO:0000269|PubMed:28562584}.
MUTAGEN 677 677 K->A: 35% DNA cleavage, altered non-
target strand cleavage products.
{ECO:0000269|PubMed:28562584}.
MUTAGEN 692 692 R->A: Slight decrease in target DNA
cleavage, 30% DNA cleavage, altered non-
target strand cleavage products.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
MUTAGEN 694 694 H->A: Wild-type DNA cleavage, altered
non-target strand cleavage products.
{ECO:0000269|PubMed:28562584}.
MUTAGEN 698 702 TKNGS->AGGGG: Loss of target DNA
cleavage. {ECO:0000269|PubMed:28431230}.
MUTAGEN 704 704 Q->A: Significant decrease in target DNA
cleavage. {ECO:0000269|PubMed:28431230}.
MUTAGEN 843 843 H->A: Decreased pre-crRNA processing in
vitro, binds RNA, no change in DNA
cleavage. {ECO:0000269|PubMed:27096362}.
MUTAGEN 852 852 K->A: Decreased pre-crRNA processing in
vitro, binds RNA, no change in DNA
cleavage. {ECO:0000269|PubMed:27096362}.
MUTAGEN 869 869 K->A: Decreased pre-crRNA processing in
vitro, binds RNA, no change in DNA
cleavage. {ECO:0000269|PubMed:27096362}.
MUTAGEN 873 873 F->A: Decreased pre-crRNA processing in
vitro, no pre-crRNA processing in E.coli,
binds RNA, no change in DNA cleavage.
{ECO:0000269|PubMed:27096362}.
MUTAGEN 917 917 D->A: Loss of target and non-target
strand DNA cleavage, no change in DNA-
binding or pre-crRNA processing.
{ECO:0000269|PubMed:26422227,
ECO:0000269|PubMed:27096362,
ECO:0000269|PubMed:28431230}.
MUTAGEN 920 920 E->A: No longer cleaves DNA in presence
of Ca(2+). {ECO:0000269|PubMed:27096362}.
MUTAGEN 922 922 H->A: Decreased cleavage of target strand
in presence of Ca(2+), wild-type cleavage
of DNA in presence of Mg(2+).
{ECO:0000269|PubMed:27096362}.
MUTAGEN 925 925 Y->A: Decreased cleavage of target strand
in presence of Ca(2+), wild-type cleavage
of DNA in presence of Mg(2+).
{ECO:0000269|PubMed:27096362}.
MUTAGEN 1006 1006 E->A: Loss of target and non-target
strand DNA cleavage, no change in DNA-
binding or pre-crRNA processing.
{ECO:0000269|PubMed:26422227,
ECO:0000269|PubMed:27096362,
ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
MUTAGEN 1006 1006 E->Q: Complete loss of DNA cleavage,
still binds crRNA; when associated with
A-1218. {ECO:0000269|PubMed:28431230}.
MUTAGEN 1024 1024 Y->A: No longer cleaves DNA in presence
of Ca(2+). {ECO:0000269|PubMed:27096362}.
MUTAGEN 1028 1028 E->A: No longer cleaves DNA in presence
of Ca(2+), reduced cleavage of non-target
strand in presence of Mg(2+).
{ECO:0000269|PubMed:27096362}.
MUTAGEN 1065 1066 KK->AA: 67% DNA cleavage, altered non-
target strand cleavage products.
{ECO:0000269|PubMed:28562584}.
MUTAGEN 1218 1218 R->A: Cleaves both target and non-target
strand DNA. Complete loss of DNA
cleavage, still binds crRNA; when
associated with Q-1006.
{ECO:0000269|PubMed:28431230,
ECO:0000269|PubMed:28562584}.
MUTAGEN 1227 1227 D->A: No longer cleaves DNA in presence
of Ca(2+). {ECO:0000269|PubMed:27096362}.
MUTAGEN 1255 1255 D->A: Significant reduction to loss of
target and non-target strand DNA
cleavage, no change in DNA-binding or
pre-crRNA processing.
{ECO:0000269|PubMed:26422227,
ECO:0000269|PubMed:27096362,
ECO:0000269|PubMed:28431230}.
MUTAGEN 1255 1255 D->N: Significant reduction of target and
non-target strand DNA cleavage.
{ECO:0000269|PubMed:28431230}.
TURN 3 6 {ECO:0000244|PDB:5NFV}.
STRAND 13 23 {ECO:0000244|PDB:5NFV}.
HELIX 27 34 {ECO:0000244|PDB:5NFV}.
HELIX 36 68 {ECO:0000244|PDB:5NFV}.
HELIX 73 86 {ECO:0000244|PDB:5NFV}.
HELIX 92 114 {ECO:0000244|PDB:5NFV}.
HELIX 117 120 {ECO:0000244|PDB:5NFV}.
STRAND 122 124 {ECO:0000244|PDB:5NFV}.
HELIX 125 127 {ECO:0000244|PDB:5NFV}.
STRAND 132 134 {ECO:0000244|PDB:5MGA}.
HELIX 137 147 {ECO:0000244|PDB:5NFV}.
HELIX 153 155 {ECO:0000244|PDB:5NFV}.
HELIX 162 171 {ECO:0000244|PDB:5NFV}.
TURN 172 174 {ECO:0000244|PDB:5NFV}.
HELIX 176 179 {ECO:0000244|PDB:5NFV}.
HELIX 180 190 {ECO:0000244|PDB:5NFV}.
STRAND 192 194 {ECO:0000244|PDB:5MGA}.
STRAND 196 198 {ECO:0000244|PDB:5NG6}.
HELIX 199 204 {ECO:0000244|PDB:5NFV}.
HELIX 207 224 {ECO:0000244|PDB:5NFV}.
HELIX 226 228 {ECO:0000244|PDB:5NFV}.
HELIX 231 237 {ECO:0000244|PDB:5NFV}.
TURN 238 242 {ECO:0000244|PDB:5NFV}.
STRAND 243 245 {ECO:0000244|PDB:5NFV}.
TURN 248 251 {ECO:0000244|PDB:5NFV}.
STRAND 252 257 {ECO:0000244|PDB:5NG6}.
HELIX 260 263 {ECO:0000244|PDB:5NFV}.
HELIX 267 271 {ECO:0000244|PDB:5NFV}.
STRAND 272 274 {ECO:0000244|PDB:5NFV}.
HELIX 275 286 {ECO:0000244|PDB:5NFV}.
STRAND 291 293 {ECO:0000244|PDB:5MGA}.
STRAND 294 297 {ECO:0000244|PDB:5NG6}.
HELIX 300 311 {ECO:0000244|PDB:5NFV}.
HELIX 314 319 {ECO:0000244|PDB:5NFV}.
HELIX 345 361 {ECO:0000244|PDB:5NFV}.
HELIX 370 382 {ECO:0000244|PDB:5NFV}.
HELIX 388 390 {ECO:0000244|PDB:5NG6}.
STRAND 392 394 {ECO:0000244|PDB:5NFV}.
HELIX 397 406 {ECO:0000244|PDB:5NFV}.
HELIX 412 422 {ECO:0000244|PDB:5NFV}.
HELIX 438 442 {ECO:0000244|PDB:5MGA}.
TURN 445 447 {ECO:0000244|PDB:5NG6}.
STRAND 449 452 {ECO:0000244|PDB:5NFV}.
HELIX 453 465 {ECO:0000244|PDB:5NFV}.
STRAND 469 471 {ECO:0000244|PDB:5NFV}.
HELIX 475 484 {ECO:0000244|PDB:5NFV}.
HELIX 487 506 {ECO:0000244|PDB:5NFV}.
HELIX 513 515 {ECO:0000244|PDB:5NFV}.
HELIX 517 519 {ECO:0000244|PDB:5NFV}.
HELIX 520 541 {ECO:0000244|PDB:5NFV}.
HELIX 559 572 {ECO:0000244|PDB:5NFV}.
HELIX 575 586 {ECO:0000244|PDB:5NFV}.
STRAND 595 597 {ECO:0000244|PDB:5NFV}.
TURN 603 606 {ECO:0000244|PDB:5NFV}.
HELIX 611 613 {ECO:0000244|PDB:5NFV}.
HELIX 614 617 {ECO:0000244|PDB:5NFV}.
STRAND 619 624 {ECO:0000244|PDB:5NFV}.
STRAND 627 633 {ECO:0000244|PDB:5NFV}.
HELIX 635 637 {ECO:0000244|PDB:5MGA}.
TURN 638 641 {ECO:0000244|PDB:5MGA}.
HELIX 643 648 {ECO:0000244|PDB:5NFV}.
STRAND 650 661 {ECO:0000244|PDB:5NFV}.
HELIX 665 673 {ECO:0000244|PDB:5NFV}.
TURN 676 678 {ECO:0000244|PDB:5NFV}.
HELIX 679 682 {ECO:0000244|PDB:5NFV}.
HELIX 686 694 {ECO:0000244|PDB:5NFV}.
TURN 695 697 {ECO:0000244|PDB:5NFV}.
STRAND 706 708 {ECO:0000244|PDB:5MGA}.
HELIX 714 730 {ECO:0000244|PDB:5NFV}.
HELIX 734 737 {ECO:0000244|PDB:5NFV}.
HELIX 744 746 {ECO:0000244|PDB:5NFV}.
HELIX 750 760 {ECO:0000244|PDB:5NFV}.
STRAND 761 769 {ECO:0000244|PDB:5NFV}.
HELIX 771 779 {ECO:0000244|PDB:5NFV}.
STRAND 782 789 {ECO:0000244|PDB:5NFV}.
HELIX 791 793 {ECO:0000244|PDB:5NFV}.
HELIX 803 812 {ECO:0000244|PDB:5NFV}.
HELIX 814 818 {ECO:0000244|PDB:5NFV}.
STRAND 821 824 {ECO:0000244|PDB:5NFV}.
STRAND 829 833 {ECO:0000244|PDB:5NFV}.
STRAND 852 856 {ECO:0000244|PDB:5MGA}.
STRAND 857 861 {ECO:0000244|PDB:5NFV}.
HELIX 871 874 {ECO:0000244|PDB:5NFV}.
STRAND 877 887 {ECO:0000244|PDB:5NFV}.
HELIX 896 906 {ECO:0000244|PDB:5NFV}.
HELIX 908 910 {ECO:0000244|PDB:5NFV}.
STRAND 912 917 {ECO:0000244|PDB:5NFV}.
STRAND 923 929 {ECO:0000244|PDB:5NFV}.
STRAND 935 944 {ECO:0000244|PDB:5NFV}.
STRAND 950 952 {ECO:0000244|PDB:5NG6}.
HELIX 953 968 {ECO:0000244|PDB:5NFV}.
TURN 969 971 {ECO:0000244|PDB:5NFV}.
HELIX 977 999 {ECO:0000244|PDB:5NFV}.
STRAND 1001 1006 {ECO:0000244|PDB:5NFV}.
STRAND 1008 1011 {ECO:0000244|PDB:5NG6}.
HELIX 1019 1036 {ECO:0000244|PDB:5NFV}.
STRAND 1041 1043 {ECO:0000244|PDB:5MGA}.
STRAND 1045 1048 {ECO:0000244|PDB:5NG6}.
STRAND 1050 1053 {ECO:0000244|PDB:5NG6}.
HELIX 1065 1067 {ECO:0000244|PDB:5NFV}.
STRAND 1069 1071 {ECO:0000244|PDB:5MGA}.
STRAND 1074 1077 {ECO:0000244|PDB:5NFV}.
STRAND 1083 1085 {ECO:0000244|PDB:5NFV}.
TURN 1087 1089 {ECO:0000244|PDB:5NFV}.
HELIX 1102 1110 {ECO:0000244|PDB:5NFV}.
STRAND 1112 1118 {ECO:0000244|PDB:5NFV}.
TURN 1119 1122 {ECO:0000244|PDB:5NFV}.
STRAND 1123 1129 {ECO:0000244|PDB:5NFV}.
HELIX 1130 1132 {ECO:0000244|PDB:5NFV}.
STRAND 1141 1145 {ECO:0000244|PDB:5NFV}.
STRAND 1150 1153 {ECO:0000244|PDB:5NFV}.
STRAND 1165 1168 {ECO:0000244|PDB:5NFV}.
HELIX 1170 1180 {ECO:0000244|PDB:5NFV}.
HELIX 1192 1197 {ECO:0000244|PDB:5NFV}.
HELIX 1201 1214 {ECO:0000244|PDB:5NFV}.
STRAND 1218 1221 {ECO:0000244|PDB:5NG6}.
TURN 1222 1225 {ECO:0000244|PDB:5NG6}.
STRAND 1228 1230 {ECO:0000244|PDB:5NFV}.
TURN 1236 1238 {ECO:0000244|PDB:5MGA}.
STRAND 1242 1245 {ECO:0000244|PDB:5NFV}.
HELIX 1254 1275 {ECO:0000244|PDB:5NFV}.
STRAND 1278 1280 {ECO:0000244|PDB:5NG6}.
HELIX 1288 1297 {ECO:0000244|PDB:5NFV}.
SEQUENCE 1300 AA; 151915 MW; 601E903DE68C80DE CRC64;
MSIYQEFVNK YSLSKTLRFE LIPQGKTLEN IKARGLILDD EKRAKDYKKA KQIIDKYHQF
FIEEILSSVC ISEDLLQNYS DVYFKLKKSD DDNLQKDFKS AKDTIKKQIS EYIKDSEKFK
NLFNQNLIDA KKGQESDLIL WLKQSKDNGI ELFKANSDIT DIDEALEIIK SFKGWTTYFK
GFHENRKNVY SSNDIPTSII YRIVDDNLPK FLENKAKYES LKDKAPEAIN YEQIKKDLAE
ELTFDIDYKT SEVNQRVFSL DEVFEIANFN NYLNQSGITK FNTIIGGKFV NGENTKRKGI
NEYINLYSQQ INDKTLKKYK MSVLFKQILS DTESKSFVID KLEDDSDVVT TMQSFYEQIA
AFKTVEEKSI KETLSLLFDD LKAQKLDLSK IYFKNDKSLT DLSQQVFDDY SVIGTAVLEY
ITQQIAPKNL DNPSKKEQEL IAKKTEKAKY LSLETIKLAL EEFNKHRDID KQCRFEEILA
NFAAIPMIFD EIAQNKDNLA QISIKYQNQG KKDLLQASAE DDVKAIKDLL DQTNNLLHKL
KIFHISQSED KANILDKDEH FYLVFEECYF ELANIVPLYN KIRNYITQKP YSDEKFKLNF
ENSTLANGWD KNKEPDNTAI LFIKDDKYYL GVMNKKNNKI FDDKAIKENK GEGYKKIVYK
LLPGANKMLP KVFFSAKSIK FYNPSEDILR IRNHSTHTKN GSPQKGYEKF EFNIEDCRKF
IDFYKQSISK HPEWKDFGFR FSDTQRYNSI DEFYREVENQ GYKLTFENIS ESYIDSVVNQ
GKLYLFQIYN KDFSAYSKGR PNLHTLYWKA LFDERNLQDV VYKLNGEAEL FYRKQSIPKK
ITHPAKEAIA NKNKDNPKKE SVFEYDLIKD KRFTEDKFFF HCPITINFKS SGANKFNDEI
NLLLKEKAND VHILSIDRGE RHLAYYTLVD GKGNIIKQDT FNIIGNDRMK TNYHDKLAAI
EKDRDSARKD WKKINNIKEM KEGYLSQVVH EIAKLVIEYN AIVVFEDLNF GFKRGRFKVE
KQVYQKLEKM LIEKLNYLVF KDNEFDKTGG VLRAYQLTAP FETFKKMGKQ TGIIYYVPAG
FTSKICPVTG FVNQLYPKYE SVSKSQEFFS KFDKICYNLD KGYFEFSFDY KNFGDKAAKG
KWTIASFGSR LINFRNSDKN HNWDTREVYP TKELEKLLKD YSIEYGHGEC IKAAICGESD
KKFFAKLTSV LNTILQMRNS KTGTELDYLI SPVADVNGNF FDSRQAPKNM PQDADANGAY
HIGLKGLMLL GRIKNNQEGK KLNLVIKNEE YFEFVQNRNN


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