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Q99ZW2

- CAS9_STRP1

UniProt

Q99ZW2 - CAS9_STRP1

Protein

CRISPR-associated endonuclease Cas9/Csn1

Gene

cas9

Organism
Streptococcus pyogenes serotype M1
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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; 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. Confers immunity against a plasmid with homology to the appropriate CRISPR spacer sequences (CRISPR interference).6 Publications

    Cofactori

    Endonuclease activity on target dsDNA requires Mg2+; the crystal was soaked in 20 mM MnCl2+.2 Publications

    Enzyme 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).3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi10 – 101Manganese 11 Publication
    Metal bindingi10 – 101Manganese 21 Publication
    Metal bindingi762 – 7621Manganese 11 Publication
    Metal bindingi766 – 7661Manganese 11 Publication
    Metal bindingi766 – 7661Manganese 21 Publication
    Metal bindingi983 – 9831Manganese 2; via pros nitrogen1 Publication
    Metal bindingi1297 – 12971Manganese 3; via tele nitrogen1 Publication
    Metal bindingi1328 – 13281Manganese 31 Publication

    GO - Molecular functioni

    1. 3'-5' exonuclease activity Source: UniProtKB
    2. DNA binding Source: UniProtKB
    3. endodeoxyribonuclease activity Source: UniProtKB
    4. metal ion binding Source: UniProtKB-HAMAP
    5. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. defense response to virus Source: UniProtKB-HAMAP
    2. DNA catabolic process, endonucleolytic Source: GOC
    3. maintenance of CRISPR repeat elements Source: UniProtKB
    4. nucleic acid phosphodiester bond hydrolysis Source: GOC

    Keywords - Molecular functioni

    Endonuclease, Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    Antiviral defense

    Keywords - Ligandi

    DNA-binding, Magnesium, Manganese, Metal-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciSPYO160490:GJ81-863-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CRISPR-associated endonuclease Cas9/Csn1UniRule annotation (EC:3.1.-.-UniRule annotation)
    Alternative name(s):
    SpyCas9
    Gene namesi
    Name:cas9UniRule annotation
    Synonyms:csn1
    Ordered Locus Names:SPy_1046
    OrganismiStreptococcus pyogenes serotype M1
    Taxonomic identifieri301447 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
    ProteomesiUP000000750: Chromosome

    Pathology & Biotechi

    Biotechnological usei

    Coexpression of Cas9 with an artifical gRNA 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 gRNAs have also been expressed individually in human and mouse cells to achieve DNA targeting; cleavage efficiencies of the artificial gRNA were lower that those for systems with the 2 gRNAs expressed separately (PubMed:23287718). Microinjection of Cas9-encoding mRNA and a synthetic gRNA into zebrafish embryos induces targeted mutations (PubMed:23360964). In all cases introduction of multiple gRNAs 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).6 Publications

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101D → 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. 4 Publications
    Mutagenesisi15 – 151S → A: Decreased DNA cleavage. 2 Publications
    Mutagenesisi66 – 661R → A: Significantly decreased DNA cleavage. 2 Publications
    Mutagenesisi70 – 701R → A: No DNA cleavage. 2 Publications
    Mutagenesisi74 – 741R → A: Significantly decreased DNA cleavage. 2 Publications
    Mutagenesisi78 – 781R → A: Moderately decreased DNA cleavage. 2 Publications
    Mutagenesisi97 – 15054Missing: No nuclease activity. 1 PublicationAdd
    BLAST
    Mutagenesisi165 – 1651R → A: Moderately decreased DNA cleavage. 2 Publications
    Mutagenesisi175 – 307133Missing: About 50% nuclease activity. 1 PublicationAdd
    BLAST
    Mutagenesisi312 – 40998Missing: No nuclease activity. 1 PublicationAdd
    BLAST
    Mutagenesisi475 – 4773PWN → 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 Publication
    Mutagenesisi762 – 7621E → 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. 3 Publications
    Mutagenesisi840 – 8401H → 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 Publications
    Mutagenesisi854 – 8541N → A: Decreased DNA cleavage. Processes guide RNAs correctly. In vivo, retains Cas9-mediated CRISPR interference in plasmid transformation. 3 Publications
    Mutagenesisi863 – 8631N → 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. 3 Publications
    Mutagenesisi982 – 9832HH → AA: Processes guide RNAs correctly. 2 Publications
    Mutagenesisi982 – 9821H → A: Decreased DNA cleavage. In vivo, loss of Cas9-mediated CRISPR interference in plasmid transformation. 2 Publications
    Mutagenesisi983 – 9831H → A: Only cleaves 1 DNA strand, probably the noncomplementary strand. 2 Publications
    Mutagenesisi986 – 9861D → 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. 3 Publications
    Mutagenesisi1099 – 1368270Missing: No nuclease activity. 1 PublicationAdd
    BLAST
    Mutagenesisi1125 – 11273DWD → 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 Publication
    Mutagenesisi1132 – 11321G → C: Probably inactivates protein. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13681368CRISPR-associated endonuclease Cas9/Csn1PRO_0000418437Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer. Binds crRNA and tracrRNA.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    STRINGi160490.SPy_1046.

    Structurei

    Secondary structure

    1
    1368
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 116
    Beta strandi13 – 219
    Beta strandi29 – 3911
    Beta strandi42 – 5211
    Helixi60 – 9334
    Helixi97 – 1015
    Turni102 – 1054
    Turni108 – 1103
    Turni117 – 1193
    Helixi122 – 13110
    Helixi135 – 14410
    Helixi151 – 16313
    Helixi176 – 1794
    Helixi181 – 19515
    Beta strandi197 – 1993
    Helixi208 – 2125
    Beta strandi214 – 2163
    Helixi218 – 22710
    Helixi237 – 24610
    Turni252 – 2576
    Helixi271 – 28212
    Helixi284 – 2863
    Helixi287 – 30519
    Helixi316 – 34227
    Helixi344 – 3463
    Helixi347 – 3515
    Beta strandi356 – 3583
    Helixi359 – 3635
    Helixi369 – 38214
    Beta strandi383 – 3853
    Helixi387 – 3948
    Helixi407 – 4093
    Helixi412 – 42514
    Turni426 – 4294
    Helixi431 – 4355
    Helixi437 – 4459
    Turni450 – 4523
    Beta strandi467 – 4715
    Beta strandi475 – 4773
    Helixi478 – 4814
    Helixi484 – 49310
    Beta strandi500 – 5023
    Helixi513 – 52412
    Beta strandi528 – 5303
    Helixi542 – 55110
    Turni552 – 5554
    Beta strandi556 – 5583
    Helixi561 – 5666
    Turni567 – 5726
    Beta strandi579 – 5824
    Helixi592 – 60110
    Helixi604 – 6085
    Helixi610 – 6123
    Helixi613 – 62513
    Helixi629 – 6357
    Helixi636 – 6394
    Turni640 – 6423
    Helixi645 – 6539
    Helixi664 – 6685
    Turni673 – 6753
    Helixi679 – 6846
    Turni687 – 6893
    Helixi693 – 6986
    Beta strandi700 – 7034
    Helixi704 – 7096
    Helixi720 – 7267
    Beta strandi727 – 7293
    Helixi731 – 75020
    Turni751 – 7533
    Beta strandi757 – 7637
    Helixi776 – 79116
    Helixi804 – 8074
    Helixi809 – 8168
    Turni817 – 8193
    Beta strandi822 – 8276
    Turni832 – 8354
    Beta strandi836 – 8394
    Turni844 – 8463
    Helixi852 – 8543
    Beta strandi856 – 8594
    Helixi862 – 8643
    Beta strandi868 – 8725
    Helixi873 – 88816
    Helixi894 – 9007
    Helixi902 – 9054
    Helixi910 – 9189
    Turni919 – 9213
    Helixi926 – 93914
    Beta strandi954 – 9585
    Helixi961 – 9699
    Turni976 – 9783
    Helixi981 – 100020
    Beta strandi1004 – 10074
    Beta strandi1009 – 10113
    Helixi1018 – 10214
    Helixi1031 – 10399
    Helixi1041 – 10444
    Beta strandi1048 – 10514
    Beta strandi1057 – 10593
    Beta strandi1064 – 10663
    Turni1067 – 10693
    Beta strandi1072 – 10754
    Turni1076 – 10783
    Helixi1079 – 10868
    Beta strandi1093 – 10964
    Beta strandi1115 – 11173
    Beta strandi1119 – 11257
    Helixi1128 – 11314
    Beta strandi1139 – 115113
    Turni1152 – 11554
    Beta strandi1156 – 116712
    Turni1168 – 11703
    Helixi1171 – 11766
    Helixi1178 – 11836
    Turni1184 – 11863
    Helixi1192 – 11943
    Beta strandi1196 – 11983
    Beta strandi1203 – 12053
    Helixi1207 – 12093
    Beta strandi1211 – 12188
    Beta strandi1220 – 12223
    Helixi1230 – 124112
    Helixi1250 – 12534
    Helixi1255 – 12628
    Helixi1266 – 127914
    Helixi1284 – 129613
    Beta strandi1298 – 13003
    Helixi1302 – 13098
    Helixi1310 – 13145
    Beta strandi1318 – 13203
    Beta strandi1324 – 13263
    Beta strandi1329 – 13313
    Helixi1341 – 13444
    Beta strandi1345 – 13506
    Beta strandi1354 – 13618
    Helixi1362 – 13654

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4CMPX-ray2.62A/B1-1368[»]
    4CMQX-ray3.09A/B1-1368[»]
    4OO8X-ray2.50A/D1-1368[»]
    ProteinModelPortaliQ99ZW2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini810 – 87263HNH Cas9-typeUniRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 6262RuvC-IAdd
    BLAST
    Regioni60 – 718659Recognition lobeAdd
    BLAST
    Regioni475 – 4773PAM substrate bindingCurated
    Regioni718 – 76548RuvC-IIAdd
    BLAST
    Regioni925 – 1102178RuvC-IIIAdd
    BLAST
    Regioni1099 – 1368270PAM-interacting domain (PI)Add
    BLAST
    Regioni1125 – 11273PAM substrate bindingCurated

    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
    The recognition lobe (approximately residues 60-718) recognizes and binds differing regions of an artifical gRNA in a sequence-independent manner. Deletions of parts of this lobe abolish nuclease activity (PubMed:24529477).1 Publication
    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

    Sequence similaritiesi

    Contains 1 HNH Cas9-type domain.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000071789.
    KOiK09952.
    OMAiIPHQIHL.
    OrthoDBiEOG6MH57S.

    Family and domain databases

    HAMAPiMF_01480. Cas9.
    InterProiIPR028629. Cas9/Csn1_fam.
    IPR025978. CRISPR-rel_HNH_dom.
    IPR003615. HNH_nuc.
    [Graphical view]
    PfamiPF13395. HNH_4. 1 hit.
    [Graphical view]
    SMARTiSM00507. HNHc. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01865. cas_Csn1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q99ZW2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDKKYSIGLD IGTNSVGWAV ITDEYKVPSK KFKVLGNTDR HSIKKNLIGA     50
    LLFDSGETAE ATRLKRTARR RYTRRKNRIC YLQEIFSNEM AKVDDSFFHR 100
    LEESFLVEED KKHERHPIFG NIVDEVAYHE KYPTIYHLRK KLVDSTDKAD 150
    LRLIYLALAH MIKFRGHFLI EGDLNPDNSD VDKLFIQLVQ TYNQLFEENP 200
    INASGVDAKA ILSARLSKSR RLENLIAQLP GEKKNGLFGN LIALSLGLTP 250
    NFKSNFDLAE DAKLQLSKDT YDDDLDNLLA QIGDQYADLF LAAKNLSDAI 300
    LLSDILRVNT EITKAPLSAS MIKRYDEHHQ DLTLLKALVR QQLPEKYKEI 350
    FFDQSKNGYA GYIDGGASQE EFYKFIKPIL EKMDGTEELL VKLNREDLLR 400
    KQRTFDNGSI PHQIHLGELH AILRRQEDFY PFLKDNREKI EKILTFRIPY 450
    YVGPLARGNS RFAWMTRKSE ETITPWNFEE VVDKGASAQS FIERMTNFDK 500
    NLPNEKVLPK HSLLYEYFTV YNELTKVKYV TEGMRKPAFL SGEQKKAIVD 550
    LLFKTNRKVT VKQLKEDYFK KIECFDSVEI SGVEDRFNAS LGTYHDLLKI 600
    IKDKDFLDNE ENEDILEDIV LTLTLFEDRE MIEERLKTYA HLFDDKVMKQ 650
    LKRRRYTGWG RLSRKLINGI RDKQSGKTIL DFLKSDGFAN RNFMQLIHDD 700
    SLTFKEDIQK AQVSGQGDSL HEHIANLAGS PAIKKGILQT VKVVDELVKV 750
    MGRHKPENIV IEMARENQTT QKGQKNSRER MKRIEEGIKE LGSQILKEHP 800
    VENTQLQNEK LYLYYLQNGR DMYVDQELDI NRLSDYDVDH IVPQSFLKDD 850
    SIDNKVLTRS DKNRGKSDNV PSEEVVKKMK NYWRQLLNAK LITQRKFDNL 900
    TKAERGGLSE LDKAGFIKRQ LVETRQITKH VAQILDSRMN TKYDENDKLI 950
    REVKVITLKS KLVSDFRKDF QFYKVREINN YHHAHDAYLN AVVGTALIKK 1000
    YPKLESEFVY GDYKVYDVRK MIAKSEQEIG KATAKYFFYS NIMNFFKTEI 1050
    TLANGEIRKR PLIETNGETG EIVWDKGRDF ATVRKVLSMP QVNIVKKTEV 1100
    QTGGFSKESI LPKRNSDKLI ARKKDWDPKK YGGFDSPTVA YSVLVVAKVE 1150
    KGKSKKLKSV KELLGITIME RSSFEKNPID FLEAKGYKEV KKDLIIKLPK 1200
    YSLFELENGR KRMLASAGEL QKGNELALPS KYVNFLYLAS HYEKLKGSPE 1250
    DNEQKQLFVE QHKHYLDEII EQISEFSKRV ILADANLDKV LSAYNKHRDK 1300
    PIREQAENII HLFTLTNLGA PAAFKYFDTT IDRKRYTSTK EVLDATLIHQ 1350
    SITGLYETRI DLSQLGGD 1368
    Length:1,368
    Mass (Da):158,441
    Last modified:June 1, 2001 - v1
    Checksum:i07D04F0B5965762F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004092 Genomic DNA. Translation: AAK33936.1.
    RefSeqiNP_269215.1. NC_002737.1.

    Genome annotation databases

    EnsemblBacteriaiAAK33936; AAK33936; SPy_1046.
    GeneIDi901176.
    KEGGispy:SPy_1046.
    PATRICi19715675. VBIStrPyo79812_0902.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE004092 Genomic DNA. Translation: AAK33936.1 .
    RefSeqi NP_269215.1. NC_002737.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4CMP X-ray 2.62 A/B 1-1368 [» ]
    4CMQ X-ray 3.09 A/B 1-1368 [» ]
    4OO8 X-ray 2.50 A/D 1-1368 [» ]
    ProteinModelPortali Q99ZW2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 160490.SPy_1046.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK33936 ; AAK33936 ; SPy_1046 .
    GeneIDi 901176.
    KEGGi spy:SPy_1046.
    PATRICi 19715675. VBIStrPyo79812_0902.

    Phylogenomic databases

    HOGENOMi HOG000071789.
    KOi K09952.
    OMAi IPHQIHL.
    OrthoDBi EOG6MH57S.

    Enzyme and pathway databases

    BioCyci SPYO160490:GJ81-863-MONOMER.

    Family and domain databases

    HAMAPi MF_01480. Cas9.
    InterProi IPR028629. Cas9/Csn1_fam.
    IPR025978. CRISPR-rel_HNH_dom.
    IPR003615. HNH_nuc.
    [Graphical view ]
    Pfami PF13395. HNH_4. 1 hit.
    [Graphical view ]
    SMARTi SM00507. HNHc. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01865. cas_Csn1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700294 / SF370 / Serotype M1.
    2. "CRISPR RNA maturation by trans-encoded small RNA and host factor RNase III."
      Deltcheva E., Chylinski K., Sharma C.M., Gonzales K., Chao Y., Pirzada Z.A., Eckert M.R., Vogel J., Charpentier E.
      Nature 471:602-607(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CRISPR-MEDIATED PLASMID DEFENSE, DISRUPTION PHENOTYPE.
      Strain: ATCC 700294 / SF370 / Serotype M1.
    3. "A programmable dual-RNA-guided DNA endonuclease in adaptive bacterial immunity."
      Jinek M., Chylinski K., Fonfara I., Hauer M., Doudna J.A., Charpentier E.
      Science 337:816-821(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A DNA ENDONUCLEASE, FUNCTION AS AN EXONUCLEASE, COFACTOR, ENZYME REGULATION, DNA-BINDING, POSSIBLE BIOTECHNOLOGY, MUTAGENESIS OF ASP-10 AND HIS-840.
      Strain: ATCC 700294 / SF370 / Serotype M1.
    4. Cited for: BIOTECHNOLOGY IN HUMAN AND MOUSE CELLS.
      Strain: ATCC 700294 / SF370 / Serotype M1.
    5. Cited for: BIOTECHNOLOGY IN HUMAN CELLS.
    6. Cited for: BIOTECHNOLOGY IN ZEBRAFISH EMBRYOS.
    7. "RNA-guided editing of bacterial genomes using CRISPR-Cas systems."
      Jiang W., Bikard D., Cox D., Zhang F., Marraffini L.A.
      Nat. Biotechnol. 31:233-239(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOTECHNOLOGY IN BACTERIA, MUTAGENESIS OF GLY-1132.
      Strain: ATCC 700294 / SF370 / Serotype M1.
    8. "Targeted genome engineering in human cells with the Cas9 RNA-guided endonuclease."
      Cho S.W., Kim S., Kim J.M., Kim J.S.
      Nat. Biotechnol. 31:230-232(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOTECHNOLOGY IN HUMAN CELLS.
      Strain: ATCC 700294 / SF370 / Serotype M1.
    9. "RNA-programmed genome editing in human cells."
      Jinek M., East A., Cheng A., Lin S., Ma E., Doudna J.
      Elife 2:E00471-E00471(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOTECHNOLOGY IN HUMAN CELLS.
    10. "DNA interrogation by the CRISPR RNA-guided endonuclease Cas9."
      Sternberg S.H., Redding S., Jinek M., Greene E.C., Doudna J.A.
      Nature 507:62-67(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, IMPORTANCE OF PAM SEQUENCES.
    11. "Phylogeny of Cas9 determines functional exchangeability of dual-RNA and Cas9 among orthologous type II CRISPR-Cas systems."
      Fonfara I., Le Rhun A., Chylinski K., Makarova K.S., Lecrivain A.L., Bzdrenga J., Koonin E.V., Charpentier E.
      Nucleic Acids Res. 42:2577-2590(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CRISPR-MEDIATED PLASMID DEFENSE, FUNCTION AS AN ENDONUCLEASE, MUTAGENESIS OF ASP-10; GLU-762; HIS-840; ASN-854; ASN-863; 982-HIS-HIS-983 AND ASP-986.
      Strain: ATCC 700294 / SF370 / Serotype M1.
    12. "Crystal structure of Cas9 in complex with guide RNA and target DNA."
      Nishimasu H., Ran F.A., Hsu P.D., Konermann S., Shehata S.I., Dohmae N., Ishitani R., Zhang F., Nureki O.
      Cell 156:935-949(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SYNTHETIC GUIDE RNA AND DNA, FUNCTION, SUBUNIT, DOMAIN, DNA-BINDING; RNA-BINDING, MUTAGENESIS OF ASP-10; SER-15; ARG-66; ARG-70; ARG-74; ARG-78; 97-PHE--ASP-150; ARG-165; 175-ASN--ARG-307; 312-ILE--SER-409; GLU-762; HIS-840; ASN-854; ASN-863; HIS-982; HIS-983; ASP-986 AND 1099-GLU--ASP-1368.
    13. Cited for: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) IN COMPLEX WITH MANGANESE, STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH GUIDE RNAS AND DNA OR GUIDE RNAS ALONE, FUNCTION, COFACTOR, ENZYME REGULATION, SUBUNIT, DOMAIN, DNA-BINDING, MUTAGENESIS OF 475-PRO--ASN-477 AND 1125-ASP--ASP-1127.
      Strain: ATCC 700294 / SF370 / Serotype M1.

    Entry informationi

    Entry nameiCAS9_STRP1
    AccessioniPrimary (citable) accession number: Q99ZW2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2012
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    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

    External Data

    Dasty 3