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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-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) (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

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

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). Nuclease activity is inhibited by EDTA (PubMed:26841432).4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101For RuvC-like nuclease domain1 Publication
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
Active sitei840 – 8401Proton acceptor for HNH nuclease domain1 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

  • 3'-5' exonuclease activity Source: UniProtKB
  • DNA binding Source: UniProtKB
  • endodeoxyribonuclease activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-HAMAP
  • RNA binding Source: UniProtKB-HAMAP

GO - Biological processi

  • defense response to virus Source: UniProtKB-HAMAP
  • maintenance of CRISPR repeat elements Source: UniProtKB
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):
SpCas91 Publication
SpyCas91 Publication
Gene namesi
Name:cas91 PublicationUniRule annotation
Synonyms:csn11 Publication
Ordered Locus Names:SPy_1046
OrganismiStreptococcus pyogenes serotype M1
Taxonomic identifieri301447 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000750 Componenti: Chromosome

Pathology & Biotechi

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

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. 4 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
Mutagenesisi1333 – 13353RKR → AKA: Nearly complete loss of target DNA cleavage. 1 Publication
Mutagenesisi1333 – 13331R → A: Dramatically reduced target DNA binding, slightly decreased target cleavage. 1 Publication
Mutagenesisi1335 – 13351R → A: Dramatically reduced target DNA binding, slightly decreased target cleavage. 1 Publication

PTM / Processingi

Molecule processing

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

Proteomic databases

PaxDbiQ99ZW2.

Interactioni

Subunit structurei

Monomer. Binds crRNA and tracrRNA.UniRule annotation2 Publications

Protein-protein interaction databases

DIPiDIP-61504N.
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 strandi42 – 5211Combined sources
Helixi60 – 9334Combined sources
Helixi97 – 1026Combined sources
Turni103 – 1053Combined sources
Helixi108 – 1103Combined sources
Turni117 – 1193Combined sources
Helixi122 – 13110Combined sources
Helixi135 – 14410Combined sources
Helixi151 – 16313Combined sources
Helixi178 – 1803Combined sources
Helixi185 – 19511Combined sources
Turni196 – 1983Combined sources
Helixi208 – 2125Combined sources
Beta strandi214 – 2163Combined sources
Helixi218 – 22710Combined sources
Helixi237 – 24610Combined sources
Turni253 – 2575Combined sources
Beta strandi266 – 2683Combined sources
Helixi271 – 28212Combined sources
Helixi284 – 2863Combined sources
Helixi287 – 29913Combined sources
Turni300 – 3056Combined sources
Beta strandi310 – 3123Combined sources
Helixi316 – 34227Combined sources
Helixi345 – 3517Combined sources
Beta strandi356 – 3583Combined sources
Helixi359 – 3635Combined sources
Helixi369 – 38214Combined sources
Beta strandi383 – 3853Combined sources
Helixi387 – 3948Combined sources
Beta strandi402 – 4043Combined 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
Beta strandi505 – 5095Combined sources
Helixi513 – 52412Combined sources
Beta strandi528 – 5303Combined sources
Turni532 – 5343Combined 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 – 6368Combined sources
Helixi637 – 6426Combined sources
Helixi645 – 6528Combined sources
Beta strandi659 – 6635Combined sources
Helixi664 – 6685Combined sources
Turni673 – 6753Combined sources
Helixi679 – 6846Combined sources
Turni687 – 6893Combined sources
Helixi693 – 6986Combined 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
Turni771 – 7744Combined sources
Helixi777 – 79115Combined sources
Helixi795 – 7984Combined sources
Helixi805 – 8073Combined sources
Helixi809 – 8168Combined sources
Turni817 – 8193Combined sources
Beta strandi822 – 8276Combined 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 – 88715Combined sources
Turni888 – 8903Combined sources
Helixi894 – 9007Combined sources
Helixi902 – 9054Combined sources
Helixi910 – 92112Combined sources
Helixi926 – 93914Combined sources
Beta strandi945 – 9473Combined sources
Beta strandi953 – 9575Combined sources
Helixi960 – 96910Combined sources
Helixi976 – 9783Combined sources
Helixi981 – 100020Combined sources
Helixi1002 – 10043Combined sources
Helixi1005 – 10084Combined sources
Beta strandi1009 – 10113Combined sources
Helixi1018 – 10214Combined sources
Helixi1032 – 10409Combined sources
Helixi1042 – 10465Combined sources
Beta strandi1048 – 10514Combined sources
Beta strandi1053 – 10553Combined 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 strandi1105 – 11073Combined sources
Beta strandi1115 – 11173Combined sources
Beta strandi1120 – 11234Combined sources
Helixi1128 – 11314Combined sources
Beta strandi1134 – 11374Combined sources
Beta strandi1139 – 115113Combined sources
Turni1152 – 11554Combined sources
Beta strandi1156 – 116712Combined sources
Turni1168 – 11703Combined sources
Helixi1171 – 11766Combined sources
Helixi1178 – 11858Combined sources
Beta strandi1187 – 11893Combined sources
Helixi1192 – 11943Combined sources
Beta strandi1196 – 11983Combined sources
Beta strandi1203 – 12053Combined sources
Helixi1207 – 12093Combined sources
Beta strandi1211 – 12188Combined sources
Beta strandi1220 – 12223Combined sources
Helixi1230 – 124011Combined sources
Helixi1251 – 126111Combined sources
Turni1262 – 12643Combined sources
Helixi1265 – 128016Combined sources
Helixi1284 – 129613Combined sources
Turni1297 – 12993Combined sources
Helixi1302 – 131615Combined sources
Beta strandi1317 – 13204Combined sources
Beta strandi1324 – 13263Combined sources
Beta strandi1329 – 13313Combined sources
Helixi1340 – 13445Combined sources
Beta strandi1345 – 13506Combined sources
Beta strandi1352 – 13543Combined sources
Beta strandi1356 – 13616Combined sources
Helixi1362 – 13643Combined 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[»]
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[»]
ProteinModelPortaliQ99ZW2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini770 – 921152HNH Cas9-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6262RuvC-I1 PublicationAdd
BLAST
Regioni56 – 718663Recognition lobe1 PublicationAdd
BLAST
Regioni56 – 7318ARM1 PublicationAdd
BLAST
Regioni718 – 76548RuvC-II1 PublicationAdd
BLAST
Regioni925 – 1102178RuvC-III1 PublicationAdd
BLAST
Regioni1099 – 1368270PAM-interacting domain (PI)1 PublicationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1333 – 13353PAM substrate-binding1 Publication

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

Sequence similaritiesi

Contains 1 HNH Cas9-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3513. LUCA.
HOGENOMiHOG000071789.
KOiK09952.
OMAiTDRHSIK.

Family and domain databases

HAMAPiMF_01480. Cas9. 1 hit.
InterProiIPR028629. Cas9.
IPR032239. Cas9-BH.
IPR032237. Cas9_PI.
IPR032240. Cas9_REC.
IPR033114. HNH_CAS9.
IPR003615. HNH_nuc.
[Graphical view]
PfamiPF16593. Cas9-BH. 1 hit.
PF16595. Cas9_PI. 1 hit.
PF16592. Cas9_REC. 1 hit.
PF13395. HNH_4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01865. cas_Csn1. 1 hit.
PROSITEiPS51749. HNH_CAS9. 1 hit.
[Graphical view]

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_002737.2.

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.
RefSeqiNP_269215.1. NC_002737.2.

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[»]
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[»]
ProteinModelPortaliQ99ZW2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61504N.
STRINGi160490.SPy_1046.

Proteomic databases

PaxDbiQ99ZW2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG3513. LUCA.
HOGENOMiHOG000071789.
KOiK09952.
OMAiTDRHSIK.

Enzyme and pathway databases

BioCyciSPYO160490:GJ81-863-MONOMER.

Family and domain databases

HAMAPiMF_01480. Cas9. 1 hit.
InterProiIPR028629. Cas9.
IPR032239. Cas9-BH.
IPR032237. Cas9_PI.
IPR032240. Cas9_REC.
IPR033114. HNH_CAS9.
IPR003615. HNH_nuc.
[Graphical view]
PfamiPF16593. Cas9-BH. 1 hit.
PF16595. Cas9_PI. 1 hit.
PF16592. Cas9_REC. 1 hit.
PF13395. HNH_4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01865. cas_Csn1. 1 hit.
PROSITEiPS51749. HNH_CAS9. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 7, 2016
This is version 89 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.