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Protein

CRISPR-associated endonuclease Cas9/Csn1

Gene

cas9

Organism
Streptococcus pyogenes serotype M1
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) (PubMed:21455174). 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; Cas9 only stabilizes the pre-crRNA:tracrRNA interaction and has no catalytic function in RNA processing (PubMed:24270795). 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). The target strand not complementary to crRNA is first cut endonucleolytically, then trimmed 3'-5' exonucleolytically. DNA-binding requires protein and both gRNAs, as does nuclease activity. Cas9 recognizes the protospacer adjacent motif (PAM) in the CRISPR repeat sequences to help distinguish self versus nonself, as targets within the bacterial CRISPR locus do not have PAMs. DNA strand separation and heteroduplex formation starts at PAM sites; PAM recognition is required for catalytic activity (PubMed:24476820). Confers immunity against a plasmid with homology to the appropriate CRISPR spacer sequences (CRISPR interference) (PubMed:21455174).6 Publications

<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

Mg2+2 PublicationsNote: Endonuclease activity on target dsDNA requires Mg2+ (PubMed:22745249). The RuvC-like nuclease domain should have 2 divalent cations, while the HNH domain should have 1. Crystals are often soaked in MgCl(2) or MnCl2+.3 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Only has nuclease activity when bound to both gRNAs (crRNA plus tracrRNA), which results in conformational changes in the protein and formation of a central channel which binds target DNA (PubMed:24505130). Also requires interaction with PAM to trigger catalytic activity (PubMed:24476820). Nuclease activity is inhibited by EDTA (PubMed:26841432).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei10For RuvC-like nuclease domain1 Publication1
<p>This subsection of the ‘Function’ 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 bindingi10Manganese 11 Publication1
Metal bindingi10Manganese 21 Publication1
Metal bindingi762Manganese 11 Publication1
Metal bindingi766Manganese 11 Publication1
Metal bindingi766Manganese 21 Publication1
Active sitei840Proton acceptor for HNH nuclease domain1 Publication1
Metal bindingi983Manganese 2; via pros nitrogen1 Publication1
Metal bindingi1297Manganese 3; via tele nitrogen1 Publication1
Metal bindingi1328Manganese 31 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, Exonuclease, Hydrolase, Nuclease, RNA-binding
Biological processAntiviral defense
LigandMagnesium, Manganese, Metal-binding

<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_and_taxonomy_section">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/Csn1UniRule annotation (EC:3.1.-.-UniRule annotation)
Alternative name(s):
SpCas91 Publication
SpyCas91 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:cas91 PublicationUniRule annotation
Synonyms:csn11 Publication
Ordered Locus Names:SPy_1046
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiStreptococcus pyogenes serotype M1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri301447 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000750 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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

Coexpression of Cas9 with an artifical single guide RNA (sgRNA) which fuses the crRNA with the tracrRNA in human cells has shown it is possible to target and modify DNA sequences of interest (PubMed:23287722, PubMed:23360966, PubMed:23386978). Cas9 plus the 2 sgRNAs have also been expressed individually in human and mouse cells to achieve DNA targeting; cleavage efficiencies of the artificial sgRNA were lower that those for systems with the 2 sgRNAs expressed separately (PubMed:23287718). Microinjection of Cas9-encoding mRNA and a synthetic sgRNA into zebrafish embryos induces targeted mutations (PubMed:23360964). In all cases introduction of multiple sgRNAs leads to multiplexed editing of genomic loci; DNA has also been inserted into a mammalian locus of interest. In S.pneumoniae and E.coli it has been used to generate markerless mutations; mutiple changes can be made simultaneously (PubMed:23360965). Studies to make mutations that alter the PAM-specificity and thus recognition possibilities have been made, but are not annotated in this database (PubMed:26098369).7 Publications

<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

Loss of correct processing of pre-crRNA and tracrRNA. Loss of immunity against a plasmid with homology to CRISPR spacer sequences.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi10D → A: Target DNA noncomplementary to the crRNA is not cleaved; nickase activity. Processes guide RNAs. In vivo, loss of Cas9-mediated CRISPR interference in plasmid transformation. Able to bind guide RNAs and target DNA but not cleave DNA; when associated with A-840. 3 Publications1
Mutagenesisi15S → A: Decreased DNA cleavage. 1 Publication1
Mutagenesisi66R → A: Significantly decreased DNA cleavage. 1 Publication1
Mutagenesisi70R → A: No DNA cleavage. 1 Publication1
Mutagenesisi74R → A: Significantly decreased DNA cleavage. 1 Publication1
Mutagenesisi78R → A: Moderately decreased DNA cleavage. 1 Publication1
Mutagenesisi97 – 150Missing : No nuclease activity. 1 PublicationAdd BLAST54
Mutagenesisi165R → A: Moderately decreased DNA cleavage. 1 Publication1
Mutagenesisi175 – 307Missing : About 50% nuclease activity. 1 PublicationAdd BLAST133
Mutagenesisi312 – 409Missing : No nuclease activity. 1 PublicationAdd BLAST98
Mutagenesisi475 – 477PWN → AAA: Slight decrease in target DNA cleavage and DNA-binding. Almost complete loss of DNA cleavage and binding; when associated with 1125-A--A-1127. 1 Publication3
Mutagenesisi762E → A: Only cleaves 1 DNA strand, probably the noncomplementary strand. Processes guide RNAs correctly. In vivo, loss of Cas9-mediated CRISPR interference in plasmid transformation. 2 Publications1
Mutagenesisi840H → A: Target DNA complementary to the crRNA is not cleaved; nickase activity. In vivo, loss of Cas9-mediated CRISPR interference in plasmid transformation. Able to process and bind guide RNAs and target DNA but not cleave DNA; when associated with A-10. 4 Publications1
Mutagenesisi854N → A: Decreased DNA cleavage. Processes guide RNAs correctly. In vivo, retains Cas9-mediated CRISPR interference in plasmid transformation. 2 Publications1
Mutagenesisi863N → A: Only cleaves 1 DNA strand, probably the complementary strand. Processes guide RNAs correctly. In vivo, loss of Cas9-mediated CRISPR interference in plasmid transformation. 2 Publications1
Mutagenesisi982 – 983HH → AA: Processes guide RNAs correctly. 1 Publication2
Mutagenesisi982H → A: Decreased DNA cleavage. In vivo, loss of Cas9-mediated CRISPR interference in plasmid transformation. 1 Publication1
Mutagenesisi983H → A: Only cleaves 1 DNA strand, probably the noncomplementary strand. 1 Publication1
Mutagenesisi986D → A: Only cleaves 1 DNA strand, probably the noncomplementary strand. Processes guide RNAs correctly. In vivo, loss of Cas9-mediated CRISPR interference in plasmid transformation. 2 Publications1
Mutagenesisi1099 – 1368Missing : No nuclease activity. 1 PublicationAdd BLAST270
Mutagenesisi1125 – 1127DWD → AAA: No change in target DNA cleavage, slight decrease in DNA-binding. Almost complete loss of DNA cleavage and binding; when associated with 475-A--A-477. 1 Publication3
Mutagenesisi1132G → C: Probably inactivates protein. 1 Publication1
Mutagenesisi1333 – 1335RKR → AKA: Nearly complete loss of target DNA cleavage. 1 Publication3
Mutagenesisi1333R → A: Dramatically reduced target DNA binding, slightly decreased target cleavage. 1 Publication1
Mutagenesisi1335R → A: Dramatically reduced target DNA binding, slightly decreased target cleavage. 1 Publication1

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004184371 – 1368CRISPR-associated endonuclease Cas9/Csn1Add BLAST1368

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q99ZW2

PRoteomics IDEntifications database

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PRIDEi
Q99ZW2

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. Binds crRNA and tracrRNA.UniRule annotation2 Publications

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-61504N

Protein interaction database and analysis system

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IntActi
Q99ZW2, 3 interactors

STRING: functional protein association networks

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STRINGi
160490.SPy_1046

<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

11368
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q99ZW2

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

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SMRi
Q99ZW2

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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_and_domains_section">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>Domaini770 – 921HNH Cas9-typePROSITE-ProRule annotationAdd BLAST152

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 – 62RuvC-I1 PublicationAdd BLAST62
Regioni56 – 718Recognition lobe1 PublicationAdd BLAST663
Regioni56 – 73ARM1 PublicationAdd BLAST18
Regioni718 – 765RuvC-II1 PublicationAdd BLAST48
Regioni925 – 1102RuvC-III1 PublicationAdd BLAST178
Regioni1099 – 1368PAM-interacting domain (PI)1 PublicationAdd BLAST270

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>Motifi1333 – 1335PAM substrate-binding1 Publication3

<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

Has 2 endonuclease domains. The discontinuous RuvC-like domain (approximately residues 1-62, 718-765 and 925-1102) recognizes and cleaves the target DNA noncomplementary to crRNA while the HNH nuclease domain (residues 810-872) cleaves the target DNA complementary to crRNA (PubMed:22745249, PubMed:24529477).2 Publications
Has a bilobed architecture with a recognition lobe (REC, residues 60-718) and a discontinuous nuclease lobe (NUC, residues 1-59 and 719-1368) (PubMed:24529477, PubMed:24505130). The crRNA-target DNA lies in a channel between the 2 lobes (PubMed:24529477, PubMed:26841432). Binding of sgRNA induces large conformational changes further enhanced by target DNA binding (PubMed:26113724, PubMed:26841432). REC recognizes and binds differing regions of an artifical sgRNA in a sequence-independent manner. Deletions of parts of this lobe abolish nuclease activity (PubMed:24529477).4 Publications
The PAM-interacting domain (PI domain, approximately residues 1099-1368) recognizes the PAM motif; swapping the PI domain of this enzyme with that from S.thermophilus St3Cas9 (AC Q03JI6) prevents cleavage of DNA with the endogenous PAM site (5'-NGG-3') but confers the ability to cleave DNA with the PAM site specific for St3 CRISPRs.1 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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
COG3513 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000071789

KEGG Orthology (KO)

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KOi
K09952

Family and domain databases

HAMAP database of protein families

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HAMAPi
MF_01480 Cas9, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR028629 Cas9
IPR032239 Cas9-BH
IPR032237 Cas9_PI
IPR032240 Cas9_REC
IPR033114 HNH_CAS9
IPR003615 HNH_nuc

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16593 Cas9-BH, 1 hit
PF16595 Cas9_PI, 1 hit
PF16592 Cas9_REC, 1 hit
PF13395 HNH_4, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01865 cas_Csn1, 1 hit

PROSITE; a protein domain and family database

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

Q99ZW2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDKKYSIGLD IGTNSVGWAV ITDEYKVPSK KFKVLGNTDR HSIKKNLIGA
60 70 80 90 100
LLFDSGETAE ATRLKRTARR RYTRRKNRIC YLQEIFSNEM AKVDDSFFHR
110 120 130 140 150
LEESFLVEED KKHERHPIFG NIVDEVAYHE KYPTIYHLRK KLVDSTDKAD
160 170 180 190 200
LRLIYLALAH MIKFRGHFLI EGDLNPDNSD VDKLFIQLVQ TYNQLFEENP
210 220 230 240 250
INASGVDAKA ILSARLSKSR RLENLIAQLP GEKKNGLFGN LIALSLGLTP
260 270 280 290 300
NFKSNFDLAE DAKLQLSKDT YDDDLDNLLA QIGDQYADLF LAAKNLSDAI
310 320 330 340 350
LLSDILRVNT EITKAPLSAS MIKRYDEHHQ DLTLLKALVR QQLPEKYKEI
360 370 380 390 400
FFDQSKNGYA GYIDGGASQE EFYKFIKPIL EKMDGTEELL VKLNREDLLR
410 420 430 440 450
KQRTFDNGSI PHQIHLGELH AILRRQEDFY PFLKDNREKI EKILTFRIPY
460 470 480 490 500
YVGPLARGNS RFAWMTRKSE ETITPWNFEE VVDKGASAQS FIERMTNFDK
510 520 530 540 550
NLPNEKVLPK HSLLYEYFTV YNELTKVKYV TEGMRKPAFL SGEQKKAIVD
560 570 580 590 600
LLFKTNRKVT VKQLKEDYFK KIECFDSVEI SGVEDRFNAS LGTYHDLLKI
610 620 630 640 650
IKDKDFLDNE ENEDILEDIV LTLTLFEDRE MIEERLKTYA HLFDDKVMKQ
660 670 680 690 700
LKRRRYTGWG RLSRKLINGI RDKQSGKTIL DFLKSDGFAN RNFMQLIHDD
710 720 730 740 750
SLTFKEDIQK AQVSGQGDSL HEHIANLAGS PAIKKGILQT VKVVDELVKV
760 770 780 790 800
MGRHKPENIV IEMARENQTT QKGQKNSRER MKRIEEGIKE LGSQILKEHP
810 820 830 840 850
VENTQLQNEK LYLYYLQNGR DMYVDQELDI NRLSDYDVDH IVPQSFLKDD
860 870 880 890 900
SIDNKVLTRS DKNRGKSDNV PSEEVVKKMK NYWRQLLNAK LITQRKFDNL
910 920 930 940 950
TKAERGGLSE LDKAGFIKRQ LVETRQITKH VAQILDSRMN TKYDENDKLI
960 970 980 990 1000
REVKVITLKS KLVSDFRKDF QFYKVREINN YHHAHDAYLN AVVGTALIKK
1010 1020 1030 1040 1050
YPKLESEFVY GDYKVYDVRK MIAKSEQEIG KATAKYFFYS NIMNFFKTEI
1060 1070 1080 1090 1100
TLANGEIRKR PLIETNGETG EIVWDKGRDF ATVRKVLSMP QVNIVKKTEV
1110 1120 1130 1140 1150
QTGGFSKESI LPKRNSDKLI ARKKDWDPKK YGGFDSPTVA YSVLVVAKVE
1160 1170 1180 1190 1200
KGKSKKLKSV KELLGITIME RSSFEKNPID FLEAKGYKEV KKDLIIKLPK
1210 1220 1230 1240 1250
YSLFELENGR KRMLASAGEL QKGNELALPS KYVNFLYLAS HYEKLKGSPE
1260 1270 1280 1290 1300
DNEQKQLFVE QHKHYLDEII EQISEFSKRV ILADANLDKV LSAYNKHRDK
1310 1320 1330 1340 1350
PIREQAENII HLFTLTNLGA PAAFKYFDTT IDRKRYTSTK EVLDATLIHQ
1360
SITGLYETRI DLSQLGGD
Length:1,368
Mass (Da):158,441
Last modified:June 1, 2001 - 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:i07D04F0B5965762F
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

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DDBJi
Links Updated
AE004092 Genomic DNA Translation: AAK33936.1

NCBI Reference Sequences

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RefSeqi
NP_269215.1, NC_002737.2

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

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EnsemblBacteriai
AAK33936; AAK33936; SPy_1046

Database of genes from NCBI RefSeq genomes

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GeneIDi
901176

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
spy:SPy_1046

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|160490.10.peg.902

<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
AE004092 Genomic DNA Translation: AAK33936.1
RefSeqiNP_269215.1, NC_002737.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CMPX-ray2.62A/B1-1368[»]
4CMQX-ray3.09A/B1-1368[»]
4OO8X-ray2.50A/D1-1368[»]
4UN3X-ray2.59B1-1368[»]
4UN4X-ray2.37B1-1368[»]
4UN5X-ray2.40B1-1368[»]
4ZT0X-ray2.90A/C1-1368[»]
4ZT9X-ray3.10A/C1-1368[»]
5B2RX-ray2.00B1-1368[»]
5B2SX-ray2.20B1-1368[»]
5B2TX-ray2.20B1-1368[»]
5F9RX-ray3.40B1-1368[»]
5FQ5X-ray2.14B1-1368[»]
5FW1X-ray2.50B1-1368[»]
5FW2X-ray2.68B1-1368[»]
5FW3X-ray2.70B1-1368[»]
5VW1X-ray2.60A1-1368[»]
5VZLelectron microscopy3.90A1-1368[»]
5XBLX-ray3.05A1-1368[»]
5Y36electron microscopy5.20A1-1368[»]
ProteinModelPortaliQ99ZW2
SMRiQ99ZW2
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61504N
IntActiQ99ZW2, 3 interactors
STRINGi160490.SPy_1046

Proteomic databases

PaxDbiQ99ZW2
PRIDEiQ99ZW2

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK33936; AAK33936; SPy_1046
GeneIDi901176
KEGGispy:SPy_1046
PATRICifig|160490.10.peg.902

Phylogenomic databases

eggNOGiCOG3513 LUCA
HOGENOMiHOG000071789
KOiK09952

Family and domain databases

HAMAPiMF_01480 Cas9, 1 hit
InterProiView protein in InterPro
IPR028629 Cas9
IPR032239 Cas9-BH
IPR032237 Cas9_PI
IPR032240 Cas9_REC
IPR033114 HNH_CAS9
IPR003615 HNH_nuc
PfamiView protein in Pfam
PF16593 Cas9-BH, 1 hit
PF16595 Cas9_PI, 1 hit
PF16592 Cas9_REC, 1 hit
PF13395 HNH_4, 1 hit
TIGRFAMsiTIGR01865 cas_Csn1, 1 hit
PROSITEiView protein in PROSITE
PS51749 HNH_CAS9, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<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_STRP1
<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: Q99ZW2
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: June 1, 2001
Last modified: December 5, 2018
This is version 105 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, Complete proteome, Reference proteome

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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