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Q99ZW2

- CAS9_STRP1

UniProt

Q99ZW2 - CAS9_STRP1

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Protein
CRISPR-associated endonuclease Cas9/Csn1
Gene
cas9, csn1, SPy_1046
Organism
Streptococcus pyogenes serotype M1
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 (1 Publication). 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).2 Publications

Cofactori

Endonuclease activity on target dsDNA requires Mg2+; the crystal (1 Publication) was soaked in 20 mM MnCl2+.

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 (1 Publication). Also requires interaction with PAM to trigger catalytic activity (1 Publication).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi10 – 101Manganese 1
Metal bindingi10 – 101Manganese 2
Metal bindingi762 – 7621Manganese 1
Metal bindingi766 – 7661Manganese 1
Metal bindingi766 – 7661Manganese 2
Metal bindingi983 – 9831Manganese 2; via pros nitrogen
Metal bindingi1297 – 12971Manganese 3; via tele nitrogen
Metal bindingi1328 – 13281Manganese 3

GO - Molecular functioni

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

GO - Biological processi

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

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/Csn1 (EC:3.1.-.-)
Alternative name(s):
SpyCas9
Gene namesi
Name:cas9
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 (1 Publication, 1 Publication, 1 Publication). 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 (1 Publication). Microinjection of Cas9-encoding mRNA and a synthetic gRNA into zebrafish embryos induces targeted mutations (1 Publication). 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 (1 Publication).

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. 1 Publication
Mutagenesisi15 – 151S → A: Decreased DNA cleavage.
Mutagenesisi66 – 661R → A: Significantly decreased DNA cleavage.
Mutagenesisi70 – 701R → A: No DNA cleavage.
Mutagenesisi74 – 741R → A: Significantly decreased DNA cleavage.
Mutagenesisi78 – 781R → A: Moderately decreased DNA cleavage.
Mutagenesisi97 – 15054Missing: No nuclease activity.
Add
BLAST
Mutagenesisi165 – 1651R → A: Moderately decreased DNA cleavage.
Mutagenesisi175 – 307133Missing: About 50% nuclease activity.
Add
BLAST
Mutagenesisi312 – 40998Missing: No nuclease activity.
Add
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.
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.
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. 1 Publication
Mutagenesisi854 – 8541N → A: Decreased DNA cleavage. Processes guide RNAs correctly. In vivo, retains Cas9-mediated CRISPR interference in plasmid transformation.
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.
Mutagenesisi982 – 9832HH → AA: Processes guide RNAs correctly.
Mutagenesisi982 – 9821H → A: Decreased DNA cleavage. In vivo, loss of Cas9-mediated CRISPR interference in plasmid transformation.
Mutagenesisi983 – 9831H → A: Only cleaves 1 DNA strand, probably the noncomplementary strand.
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.
Mutagenesisi1099 – 1368270Missing: No nuclease activity.
Add
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.
Mutagenesisi1132 – 11321G → C: Probably inactivates protein. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13681368CRISPR-associated endonuclease Cas9/Csn1UniRule annotation
PRO_0000418437Add
BLAST

Interactioni

Subunit structurei

Monomer. Binds crRNA and tracrRNA.

Protein-protein interaction databases

STRINGi160490.SPy_1046.

Structurei

Secondary structure

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini810 – 87263HNH Cas9-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6262RuvC-I
Add
BLAST
Regioni60 – 718659Recognition lobe
Add
BLAST
Regioni475 – 4773PAM substrate binding Inferred
Regioni718 – 76548RuvC-II
Add
BLAST
Regioni925 – 1102178RuvC-III
Add
BLAST
Regioni1099 – 1368270PAM-interacting domain (PI)
Add
BLAST
Regioni1125 – 11273PAM substrate binding Inferred

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 (1 Publication, 1 Publication).
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 (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

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

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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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 73 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

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

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