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Q99ZW2

- CAS9_STRP1

UniProt

Q99ZW2 - CAS9_STRP1

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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

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

Mg2+2 PublicationsNote: Endonuclease activity on target dsDNA requires Mg(2+); the crystal was soaked in 20 mM MnCl(2+).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
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/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. 3 Publications
Mutagenesisi15 – 151S → A: Decreased DNA cleavage. 1 Publication
Mutagenesisi66 – 661R → A: Significantly decreased DNA cleavage. 1 Publication
Mutagenesisi70 – 701R → A: No DNA cleavage. 1 Publication
Mutagenesisi74 – 741R → A: Significantly decreased DNA cleavage. 1 Publication
Mutagenesisi78 – 781R → A: Moderately decreased DNA cleavage. 1 Publication
Mutagenesisi97 – 15054Missing: No nuclease activity. 1 PublicationAdd
BLAST
Mutagenesisi165 – 1651R → A: Moderately decreased DNA cleavage. 1 Publication
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. 2 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. 3 Publications
Mutagenesisi854 – 8541N → A: Decreased DNA cleavage. Processes guide RNAs correctly. In vivo, retains Cas9-mediated CRISPR interference in plasmid transformation. 2 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. 2 Publications
Mutagenesisi982 – 9832HH → AA: Processes guide RNAs correctly. 1 Publication
Mutagenesisi982 – 9821H → A: Decreased DNA cleavage. In vivo, loss of Cas9-mediated CRISPR interference in plasmid transformation. 1 Publication
Mutagenesisi983 – 9831H → A: Only cleaves 1 DNA strand, probably the noncomplementary strand. 1 Publication
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. 2 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. 1 Publication

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 – 116Combined sources
Beta strandi13 – 219Combined sources
Beta strandi29 – 3911Combined sources
Beta strandi41 – 5212Combined sources
Helixi60 – 9334Combined sources
Helixi97 – 1026Combined sources
Turni103 – 1053Combined sources
Turni108 – 1103Combined sources
Beta strandi117 – 1215Combined sources
Helixi122 – 13110Combined sources
Helixi135 – 14410Combined sources
Helixi151 – 16313Combined sources
Helixi178 – 1803Combined sources
Helixi181 – 19515Combined sources
Beta strandi197 – 1993Combined sources
Helixi208 – 2125Combined sources
Beta strandi214 – 2163Combined sources
Helixi218 – 22710Combined sources
Helixi237 – 24610Combined sources
Turni252 – 2576Combined sources
Beta strandi266 – 2683Combined sources
Helixi271 – 28212Combined sources
Helixi284 – 2863Combined sources
Helixi287 – 30519Combined sources
Turni310 – 3123Combined sources
Helixi316 – 34227Combined sources
Helixi344 – 3463Combined sources
Helixi347 – 3515Combined sources
Beta strandi356 – 3583Combined sources
Helixi359 – 3635Combined sources
Helixi369 – 38214Combined sources
Beta strandi383 – 3853Combined sources
Helixi387 – 3948Combined sources
Helixi405 – 4095Combined sources
Helixi412 – 42615Combined sources
Turni427 – 4293Combined sources
Helixi431 – 4355Combined sources
Helixi437 – 4459Combined sources
Turni450 – 4523Combined sources
Beta strandi467 – 4715Combined sources
Turni475 – 4773Combined sources
Helixi478 – 4814Combined sources
Helixi484 – 49310Combined sources
Beta strandi500 – 5023Combined sources
Helixi513 – 52412Combined sources
Beta strandi528 – 5303Combined sources
Helixi542 – 55110Combined sources
Turni552 – 5554Combined sources
Beta strandi556 – 5583Combined sources
Helixi561 – 5677Combined sources
Turni568 – 5736Combined sources
Beta strandi579 – 5824Combined sources
Beta strandi584 – 5863Combined sources
Helixi592 – 60110Combined sources
Helixi604 – 6085Combined sources
Helixi610 – 6123Combined sources
Helixi613 – 62513Combined sources
Helixi629 – 6357Combined sources
Helixi637 – 6393Combined sources
Turni640 – 6423Combined sources
Helixi645 – 6539Combined sources
Helixi664 – 6685Combined sources
Turni673 – 6753Combined sources
Helixi679 – 6846Combined sources
Turni687 – 6893Combined sources
Helixi693 – 6975Combined sources
Beta strandi700 – 7034Combined sources
Helixi704 – 7118Combined sources
Helixi720 – 7256Combined sources
Beta strandi727 – 7293Combined sources
Helixi731 – 75020Combined sources
Turni751 – 7533Combined sources
Beta strandi757 – 7637Combined sources
Helixi776 – 79116Combined sources
Helixi795 – 7984Combined sources
Helixi803 – 8075Combined sources
Helixi809 – 8168Combined sources
Turni817 – 8193Combined sources
Turni822 – 8243Combined sources
Beta strandi825 – 8273Combined sources
Helixi830 – 8356Combined sources
Beta strandi836 – 8427Combined sources
Turni844 – 8463Combined sources
Helixi852 – 8543Combined sources
Beta strandi855 – 8595Combined sources
Helixi861 – 8644Combined sources
Beta strandi867 – 8715Combined sources
Helixi873 – 88816Combined sources
Helixi894 – 9007Combined sources
Helixi903 – 9053Combined sources
Helixi910 – 91910Combined sources
Helixi926 – 93914Combined sources
Beta strandi953 – 9575Combined sources
Helixi960 – 96910Combined sources
Turni976 – 9783Combined sources
Helixi981 – 100020Combined sources
Helixi1002 – 10043Combined sources
Helixi1005 – 10084Combined sources
Beta strandi1009 – 10113Combined sources
Helixi1018 – 10214Combined sources
Helixi1031 – 104010Combined sources
Turni1041 – 10433Combined sources
Helixi1044 – 10463Combined sources
Beta strandi1048 – 10514Combined sources
Beta strandi1057 – 10593Combined sources
Beta strandi1062 – 10654Combined sources
Turni1067 – 10693Combined sources
Beta strandi1072 – 10754Combined sources
Turni1076 – 10783Combined sources
Helixi1079 – 10879Combined sources
Beta strandi1093 – 10964Combined sources
Beta strandi1115 – 11173Combined sources
Beta strandi1120 – 11234Combined sources
Helixi1128 – 11314Combined sources
Beta strandi1139 – 115113Combined sources
Turni1152 – 11554Combined sources
Beta strandi1156 – 116712Combined sources
Turni1168 – 11703Combined sources
Helixi1171 – 11766Combined sources
Helixi1178 – 11858Combined sources
Helixi1192 – 11943Combined sources
Beta strandi1196 – 11983Combined sources
Beta strandi1203 – 12053Combined sources
Beta strandi1207 – 12093Combined sources
Beta strandi1211 – 12188Combined sources
Beta strandi1220 – 12223Combined sources
Helixi1230 – 124011Combined sources
Helixi1252 – 126110Combined sources
Turni1262 – 12643Combined sources
Helixi1265 – 127915Combined sources
Helixi1284 – 129613Combined sources
Turni1297 – 12993Combined sources
Helixi1302 – 131211Combined sources
Turni1313 – 13164Combined sources
Beta strandi1317 – 13204Combined sources
Beta strandi1324 – 13285Combined sources
Beta strandi1329 – 13313Combined sources
Helixi1341 – 13444Combined sources
Beta strandi1345 – 13506Combined sources
Beta strandi1352 – 13543Combined sources
Beta strandi1356 – 13616Combined sources
Helixi1362 – 13654Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
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

        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
Checksum:i07D04F0B5965762F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AE004092 Genomic DNA. Translation: AAK33936.1 .
RefSeqi NP_269215.1. NC_002737.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 [» ]
4UN3 X-ray 2.59 B 1-1368 [» ]
4UN4 X-ray 2.37 B 1-1368 [» ]
4UN5 X-ray 2.40 B 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

« 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: November 26, 2014
This is version 76 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