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Entry version 70 (02 Jun 2021)
Sequence version 1 (09 Jan 2007)
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Protein

CRISPR-associated endonuclease Cas9

Gene

cas9

Organism
Francisella tularensis subsp. novicida (strain U112)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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). In type II CRISPR systems correct processing of pre-crRNA requires a trans-encoded small RNA (tracrRNA), endogenous ribonuclease 3 (rnc) and this protein. The tracrRNA serves as a guide for ribonuclease 3-aided processing of pre-crRNA. Subsequently Cas9/crRNA/tracrRNA endonucleolytically cleaves linear or circular dsDNA target complementary to the spacer; Cas9 is inactive in the absence of the 2 guide RNAs (gRNA). Cas9 recognizes a short motif in the CRISPR repeat sequences (the PAM or protospacer adjacent motif) to help distinguish self versus nonself, as targets within the bacterial CRISPR locus do not have PAMs. PAM recognition is also required for catalytic activity. Cuts target DNA when Cas9 and gRNAs are mixed (PubMed:24270795, PubMed:26875867).

By similarity2 Publications

Plays a role in repression of expression of endogenous bacterial lipoprotein FTN_1103. Cas9 plays a possibly non-enzymatic role in the degradation of FTN_1103 mRNA, which is dependent on formation of an RNA:RNA complex of tracrRNA and scaRNA (the latter is not found in all type II CRISPR-Cas systems).

1 Publication

Miscellaneous

Part of a type II CRISPR-Cas system.1 Publication

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei11For RuvC-like nuclease domain1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi11Manganese 1By similarity1
Metal bindingi11Manganese 2By similarity1
Metal bindingi460Zinc1 Publication1
Metal bindingi657Zinc1 Publication1
Metal bindingi814Zinc1 Publication1
Metal bindingi817Zinc1 Publication1
Metal bindingi876Magnesium 1By similarity1
Metal bindingi880Magnesium 1By similarity1
Metal bindingi880Magnesium 2By similarity1
Active sitei995Proton acceptor for HNH nuclease domain1 Publication1
Metal bindingi1162Manganese 2; via pros nitrogenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1556PAM RNA1 Publication1
Binding sitei1585PAM RNA1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Endonuclease, Hydrolase, Nuclease, RNA-binding
Biological processAntiviral defense, Virulence
LigandMagnesium, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
FTUL401614:G1G75-789-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
CRISPR-associated endonuclease Cas9 (EC:3.1.-.-)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cas9
Ordered Locus Names:FTN_0757
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiFrancisella tularensis subsp. novicida (strain U112)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri401614 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000762 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

The simplicity of the Cas9-gRNAs RNA-directed DNA endonuclease activity may be used to target and modify a DNA sequence of interest (PubMed:24270795). Pre-assembled Cas9, crRNA and tracRNA induces indel formation in targeted genes upon microinjection into mouse zygotes; mutations E1369R/E1449H/R1556A alter PAM recognition and thus enlarge the scope of this protein for genetic engineering, see PDB 5B2Q for the X-ray structure of this variant. The strain deleted for this gene might make a good vaccine candiate (PubMed:26875867).1 Publication1 Publication

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

100-fold increase in expression of bacterial lipoprotein FTN_1103, increased stimulation of interleukin-6 (Il6) production in a Tlr2-dependent fashion by C57BL/6 mouse bone marrow-derived macrophages. In mice nearly 104-fold less virulent than wild-type bacteria. A double cas9-FTN_1103 disruption significantly decreases Il6 production. Mice immunized with this gene deleted were protected against subsequent infection with wild-type bacteria.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi11D → A: Still represses expression of lipoprotein FTN_1103. 1 Publication1
Mutagenesisi59R → A: No longer represses expression of lipoprotein FTN_1103, Cas9 no longer binds mRNA for FTN_1103, tracrRNA or scaRNA. 1 Publication1
Mutagenesisi86E → A: Still represses expression of lipoprotein FTN_1103. 1 Publication1
Mutagenesisi102R → A: Still represses expression of lipoprotein FTN_1103. 1 Publication1
Mutagenesisi876D → A: Still represses expression of lipoprotein FTN_1103. 1 Publication1
Mutagenesisi969H → A: Still represses expression of lipoprotein FTN_1103. 1 Publication1
Mutagenesisi986N → A: Still represses expression of lipoprotein FTN_1103. 1 Publication1
Mutagenesisi995N → A: Target DNA not cleaved. 1 Publication1
Mutagenesisi1162H → A: Still represses expression of lipoprotein FTN_1103. 1 Publication1
Mutagenesisi1165D → A: Still represses expression of lipoprotein FTN_1103. 1 Publication1
Mutagenesisi1369E → R: Recognizes and cleaves altered PAM; when associated with H-1449 and A-1556. 1 Publication1
Mutagenesisi1449E → H: Recognizes and cleaves altered PAM; when associated with R-1369 and A-1556. 1 Publication1
Mutagenesisi1473S → A: Decreased target DNA cleavage. 1 Publication1
Mutagenesisi1474R → A: Target DNA not cleaved. 1 Publication1
Mutagenesisi1556R → A: Almost no target DNA cleavage, recognizes and partially cleaves altered PAM. Improved cleavage of altered PAM; when associated with R-1369 and H-1449. 1 Publication1
Mutagenesisi1585R → A: Target DNA not cleaved. 1 Publication1

Miscellaneous databases

Pathogen-Host Interaction database

More...
PHI-basei
PHI:3358

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004299841 – 1629CRISPR-associated endonuclease Cas9Add BLAST1629

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
A0Q5Y3

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

In culture expression is maximal at 3 hours during mid-log phase. During infection of mouse bone marrow-derived macrophages (BMDM) expression is maximal after 1 hour, when the bacteria is expected to be in the phagosome.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. Binds crRNA and tracrRNA.

1 Publication1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11629
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
A0Q5Y3

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini897 – 1046HNH Cas9-typePROSITE-ProRule annotationAdd BLAST150

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 51RuvC-I1 PublicationAdd BLAST51
Regioni55 – 73ARM1 PublicationAdd BLAST19
Regioni83 – 858Recognition domain (REC)1 PublicationAdd BLAST776
Regioni858 – 899RuvC-II1 PublicationAdd BLAST42
Regioni1088 – 1224RuvC-III1 PublicationAdd BLAST137
Regioni1476 – 1629PAM-interacting domain (PI)1 PublicationAdd BLAST154

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili555 – 582Sequence analysisAdd BLAST28

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1473 – 1474PAM-binding1 Publication2

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The arginine-rich motif (ARM, residues 55-73) plays a role in regulation of at least 1 endogenous gene (FTN_1103).1 Publication
Has a recognition domain (REC, residues 83-858) and a nuclease domain (NUC, residues 1-51 and 859-1629). The crRNA-target DNA twist through the domains in a different manner than in the S.pyogenes and S.aureus orthologs (PubMed:26875867). The NUC lobe has 2 endonuclease domains. The discontinuous RuvC-like domain in NUC cleaves the target DNA noncomplementary to crRNA while the HNH nuclease domain cleaves the target DNA complementary to crRNA (Probable).1 Publication1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

Identification of Orthologs from Complete Genome Data

More...
OMAi
LHHFVFA

Database of Orthologous Groups

More...
OrthoDBi
539526at2

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013492, CRISPR-assoc_Cas9/Csx12
IPR033114, HNH_CAS9

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03031, cas_csx12, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51749, HNH_CAS9, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

A0Q5Y3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNFKILPIAI DLGVKNTGVF SAFYQKGTSL ERLDNKNGKV YELSKDSYTL
60 70 80 90 100
LMNNRTARRH QRRGIDRKQL VKRLFKLIWT EQLNLEWDKD TQQAISFLFN
110 120 130 140 150
RRGFSFITDG YSPEYLNIVP EQVKAILMDI FDDYNGEDDL DSYLKLATEQ
160 170 180 190 200
ESKISEIYNK LMQKILEFKL MKLCTDIKDD KVSTKTLKEI TSYEFELLAD
210 220 230 240 250
YLANYSESLK TQKFSYTDKQ GNLKELSYYH HDKYNIQEFL KRHATINDRI
260 270 280 290 300
LDTLLTDDLD IWNFNFEKFD FDKNEEKLQN QEDKDHIQAH LHHFVFAVNK
310 320 330 340 350
IKSEMASGGR HRSQYFQEIT NVLDENNHQE GYLKNFCENL HNKKYSNLSV
360 370 380 390 400
KNLVNLIGNL SNLELKPLRK YFNDKIHAKA DHWDEQKFTE TYCHWILGEW
410 420 430 440 450
RVGVKDQDKK DGAKYSYKDL CNELKQKVTK AGLVDFLLEL DPCRTIPPYL
460 470 480 490 500
DNNNRKPPKC QSLILNPKFL DNQYPNWQQY LQELKKLQSI QNYLDSFETD
510 520 530 540 550
LKVLKSSKDQ PYFVEYKSSN QQIASGQRDY KDLDARILQF IFDRVKASDE
560 570 580 590 600
LLLNEIYFQA KKLKQKASSE LEKLESSKKL DEVIANSQLS QILKSQHTNG
610 620 630 640 650
IFEQGTFLHL VCKYYKQRQR ARDSRLYIMP EYRYDKKLHK YNNTGRFDDD
660 670 680 690 700
NQLLTYCNHK PRQKRYQLLN DLAGVLQVSP NFLKDKIGSD DDLFISKWLV
710 720 730 740 750
EHIRGFKKAC EDSLKIQKDN RGLLNHKINI ARNTKGKCEK EIFNLICKIE
760 770 780 790 800
GSEDKKGNYK HGLAYELGVL LFGEPNEASK PEFDRKIKKF NSIYSFAQIQ
810 820 830 840 850
QIAFAERKGN ANTCAVCSAD NAHRMQQIKI TEPVEDNKDK IILSAKAQRL
860 870 880 890 900
PAIPTRIVDG AVKKMATILA KNIVDDNWQN IKQVLSAKHQ LHIPIITESN
910 920 930 940 950
AFEFEPALAD VKGKSLKDRR KKALERISPE NIFKDKNNRI KEFAKGISAY
960 970 980 990 1000
SGANLTDGDF DGAKEELDHI IPRSHKKYGT LNDEANLICV TRGDNKNKGN
1010 1020 1030 1040 1050
RIFCLRDLAD NYKLKQFETT DDLEIEKKIA DTIWDANKKD FKFGNYRSFI
1060 1070 1080 1090 1100
NLTPQEQKAF RHALFLADEN PIKQAVIRAI NNRNRTFVNG TQRYFAEVLA
1110 1120 1130 1140 1150
NNIYLRAKKE NLNTDKISFD YFGIPTIGNG RGIAEIRQLY EKVDSDIQAY
1160 1170 1180 1190 1200
AKGDKPQASY SHLIDAMLAF CIAADEHRND GSIGLEIDKN YSLYPLDKNT
1210 1220 1230 1240 1250
GEVFTKDIFS QIKITDNEFS DKKLVRKKAI EGFNTHRQMT RDGIYAENYL
1260 1270 1280 1290 1300
PILIHKELNE VRKGYTWKNS EEIKIFKGKK YDIQQLNNLV YCLKFVDKPI
1310 1320 1330 1340 1350
SIDIQISTLE ELRNILTTNN IAATAEYYYI NLKTQKLHEY YIENYNTALG
1360 1370 1380 1390 1400
YKKYSKEMEF LRSLAYRSER VKIKSIDDVK QVLDKDSNFI IGKITLPFKK
1410 1420 1430 1440 1450
EWQRLYREWQ NTTIKDDYEF LKSFFNVKSI TKLHKKVRKD FSLPISTNEG
1460 1470 1480 1490 1500
KFLVKRKTWD NNFIYQILND SDSRADGTKP FIPAFDISKN EIVEAIIDSF
1510 1520 1530 1540 1550
TSKNIFWLPK NIELQKVDNK NIFAIDTSKW FEVETPSDLR DIGIATIQYK
1560 1570 1580 1590 1600
IDNNSRPKVR VKLDYVIDDD SKINYFMNHS LLKSRYPDKV LEILKQSTII
1610 1620
EFESSGFNKT IKEMLGMKLA GIYNETSNN
Length:1,629
Mass (Da):190,461
Last modified:January 9, 2007 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i254D6EB9C5C9E07B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CP000439 Genomic DNA Translation: ABK89648.1

NCBI Reference Sequences

More...
RefSeqi
WP_003038941.1, NZ_CP009633.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABK89648; ABK89648; FTN_0757

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ftn:FTN_0757

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000439 Genomic DNA Translation: ABK89648.1
RefSeqiWP_003038941.1, NZ_CP009633.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5B2OX-ray1.70A1-1629[»]
5B2PX-ray1.70A1-1629[»]
5B2QX-ray1.70A1-1629[»]
6J9LX-ray1.78E44-90[»]
SMRiA0Q5Y3
ModBaseiSearch...
PDBe-KBiSearch...

Proteomic databases

PRIDEiA0Q5Y3

Genome annotation databases

EnsemblBacteriaiABK89648; ABK89648; FTN_0757
KEGGiftn:FTN_0757

Phylogenomic databases

OMAiLHHFVFA
OrthoDBi539526at2

Enzyme and pathway databases

BioCyciFTUL401614:G1G75-789-MONOMER

Miscellaneous databases

PHI-baseiPHI:3358

Family and domain databases

InterProiView protein in InterPro
IPR013492, CRISPR-assoc_Cas9/Csx12
IPR033114, HNH_CAS9
TIGRFAMsiTIGR03031, cas_csx12, 1 hit
PROSITEiView protein in PROSITE
PS51749, HNH_CAS9, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCAS9_FRATN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A0Q5Y3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 3, 2014
Last sequence update: January 9, 2007
Last modified: June 2, 2021
This is version 70 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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