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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)DescriptionActionsGraphical viewLength
Active sitei10For RuvC-like nuclease domain1 Publication1
Metal bindingi10Manganese 11 Publication1
Metal bindingi10Manganese 21 Publication1
Metal bindingi762Manganese 11 Publication1
Metal bindingi766Manganese 11 Publication1
Metal bindingi766Manganese 21 Publication1
Active sitei840Proton acceptor for HNH nuclease domain1 Publication1
Metal bindingi983Manganese 2; via pros nitrogen1 Publication1
Metal bindingi1297Manganese 3; via tele nitrogen1 Publication1
Metal bindingi1328Manganese 31 Publication1

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

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004184371 – 1368CRISPR-associated endonuclease Cas9/Csn1Add BLAST1368

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

11368
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 11Combined sources6
Beta strandi13 – 21Combined sources9
Beta strandi29 – 39Combined sources11
Beta strandi42 – 52Combined sources11
Helixi60 – 93Combined sources34
Helixi97 – 102Combined sources6
Turni103 – 105Combined sources3
Helixi108 – 110Combined sources3
Turni117 – 119Combined sources3
Helixi122 – 131Combined sources10
Helixi135 – 144Combined sources10
Helixi151 – 163Combined sources13
Helixi178 – 180Combined sources3
Helixi185 – 195Combined sources11
Turni196 – 198Combined sources3
Helixi208 – 212Combined sources5
Beta strandi214 – 216Combined sources3
Helixi218 – 227Combined sources10
Helixi237 – 246Combined sources10
Turni253 – 257Combined sources5
Beta strandi266 – 268Combined sources3
Helixi271 – 282Combined sources12
Helixi284 – 286Combined sources3
Helixi287 – 299Combined sources13
Turni300 – 305Combined sources6
Beta strandi310 – 312Combined sources3
Helixi316 – 342Combined sources27
Helixi345 – 351Combined sources7
Beta strandi356 – 358Combined sources3
Helixi359 – 363Combined sources5
Helixi369 – 382Combined sources14
Beta strandi383 – 385Combined sources3
Helixi387 – 394Combined sources8
Beta strandi402 – 404Combined sources3
Helixi405 – 409Combined sources5
Helixi412 – 426Combined sources15
Turni427 – 429Combined sources3
Helixi431 – 435Combined sources5
Helixi437 – 445Combined sources9
Turni450 – 452Combined sources3
Beta strandi467 – 471Combined sources5
Turni475 – 477Combined sources3
Helixi478 – 481Combined sources4
Helixi484 – 493Combined sources10
Beta strandi500 – 502Combined sources3
Beta strandi505 – 509Combined sources5
Helixi513 – 524Combined sources12
Beta strandi528 – 530Combined sources3
Turni532 – 534Combined sources3
Helixi542 – 551Combined sources10
Turni552 – 555Combined sources4
Beta strandi556 – 558Combined sources3
Helixi561 – 567Combined sources7
Turni568 – 573Combined sources6
Beta strandi579 – 582Combined sources4
Beta strandi584 – 586Combined sources3
Helixi592 – 601Combined sources10
Helixi604 – 608Combined sources5
Helixi610 – 612Combined sources3
Helixi613 – 625Combined sources13
Helixi629 – 636Combined sources8
Helixi637 – 642Combined sources6
Helixi645 – 652Combined sources8
Beta strandi659 – 663Combined sources5
Helixi664 – 668Combined sources5
Turni673 – 675Combined sources3
Helixi679 – 684Combined sources6
Turni687 – 689Combined sources3
Helixi693 – 698Combined sources6
Beta strandi700 – 703Combined sources4
Helixi704 – 711Combined sources8
Helixi720 – 725Combined sources6
Beta strandi727 – 729Combined sources3
Helixi731 – 750Combined sources20
Turni751 – 753Combined sources3
Beta strandi757 – 763Combined sources7
Turni771 – 774Combined sources4
Helixi777 – 791Combined sources15
Helixi795 – 798Combined sources4
Helixi805 – 807Combined sources3
Helixi809 – 816Combined sources8
Turni817 – 819Combined sources3
Beta strandi822 – 827Combined sources6
Helixi830 – 835Combined sources6
Beta strandi836 – 842Combined sources7
Turni844 – 846Combined sources3
Helixi852 – 854Combined sources3
Beta strandi855 – 859Combined sources5
Helixi861 – 864Combined sources4
Beta strandi867 – 871Combined sources5
Helixi873 – 887Combined sources15
Turni888 – 890Combined sources3
Helixi894 – 900Combined sources7
Helixi902 – 905Combined sources4
Helixi910 – 921Combined sources12
Helixi926 – 939Combined sources14
Beta strandi945 – 947Combined sources3
Beta strandi953 – 957Combined sources5
Helixi960 – 969Combined sources10
Helixi976 – 978Combined sources3
Helixi981 – 1000Combined sources20
Helixi1002 – 1004Combined sources3
Helixi1005 – 1008Combined sources4
Beta strandi1009 – 1011Combined sources3
Helixi1018 – 1021Combined sources4
Helixi1032 – 1040Combined sources9
Helixi1042 – 1046Combined sources5
Beta strandi1048 – 1051Combined sources4
Beta strandi1053 – 1055Combined sources3
Beta strandi1057 – 1059Combined sources3
Beta strandi1062 – 1065Combined sources4
Turni1067 – 1069Combined sources3
Beta strandi1072 – 1075Combined sources4
Turni1076 – 1078Combined sources3
Helixi1079 – 1087Combined sources9
Beta strandi1093 – 1096Combined sources4
Beta strandi1105 – 1107Combined sources3
Beta strandi1115 – 1117Combined sources3
Beta strandi1120 – 1123Combined sources4
Helixi1128 – 1131Combined sources4
Beta strandi1134 – 1137Combined sources4
Beta strandi1139 – 1151Combined sources13
Turni1152 – 1155Combined sources4
Beta strandi1156 – 1167Combined sources12
Turni1168 – 1170Combined sources3
Helixi1171 – 1176Combined sources6
Helixi1178 – 1185Combined sources8
Beta strandi1187 – 1189Combined sources3
Helixi1192 – 1194Combined sources3
Beta strandi1196 – 1198Combined sources3
Beta strandi1203 – 1205Combined sources3
Helixi1207 – 1209Combined sources3
Beta strandi1211 – 1218Combined sources8
Beta strandi1220 – 1222Combined sources3
Helixi1230 – 1240Combined sources11
Helixi1251 – 1261Combined sources11
Turni1262 – 1264Combined sources3
Helixi1265 – 1280Combined sources16
Helixi1284 – 1296Combined sources13
Turni1297 – 1299Combined sources3
Helixi1302 – 1316Combined sources15
Beta strandi1317 – 1320Combined sources4
Beta strandi1324 – 1326Combined sources3
Beta strandi1329 – 1331Combined sources3
Helixi1340 – 1344Combined sources5
Beta strandi1345 – 1350Combined sources6
Beta strandi1352 – 1354Combined sources3
Beta strandi1356 – 1361Combined sources6
Helixi1362 – 1364Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CMPX-ray2.62A/B1-1368[»]
4CMQX-ray3.09A/B1-1368[»]
4OO8X-ray2.50A/D1-1368[»]
4UN3X-ray2.59B1-1368[»]
4UN4X-ray2.37B1-1368[»]
4UN5X-ray2.40B1-1368[»]
4ZT0X-ray2.90A/C1-1368[»]
4ZT9X-ray3.10A/C1-1368[»]
5B2RX-ray2.00B1-1368[»]
5B2SX-ray2.20B1-1368[»]
5B2TX-ray2.20B1-1368[»]
5F9RX-ray3.40B1-1368[»]
5FQ5X-ray2.14B1-1368[»]
5FW1X-ray2.50B1-1368[»]
5FW2X-ray2.68B1-1368[»]
5FW3X-ray2.70B1-1368[»]
ProteinModelPortaliQ99ZW2.
SMRiQ99ZW2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini770 – 921HNH Cas9-typePROSITE-ProRule annotationAdd BLAST152

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 62RuvC-I1 PublicationAdd BLAST62
Regioni56 – 718Recognition lobe1 PublicationAdd BLAST663
Regioni56 – 73ARM1 PublicationAdd BLAST18
Regioni718 – 765RuvC-II1 PublicationAdd BLAST48
Regioni925 – 1102RuvC-III1 PublicationAdd BLAST178
Regioni1099 – 1368PAM-interacting domain (PI)1 PublicationAdd BLAST270

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1333 – 1335PAM substrate-binding1 Publication3

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CMPX-ray2.62A/B1-1368[»]
4CMQX-ray3.09A/B1-1368[»]
4OO8X-ray2.50A/D1-1368[»]
4UN3X-ray2.59B1-1368[»]
4UN4X-ray2.37B1-1368[»]
4UN5X-ray2.40B1-1368[»]
4ZT0X-ray2.90A/C1-1368[»]
4ZT9X-ray3.10A/C1-1368[»]
5B2RX-ray2.00B1-1368[»]
5B2SX-ray2.20B1-1368[»]
5B2TX-ray2.20B1-1368[»]
5F9RX-ray3.40B1-1368[»]
5FQ5X-ray2.14B1-1368[»]
5FW1X-ray2.50B1-1368[»]
5FW2X-ray2.68B1-1368[»]
5FW3X-ray2.70B1-1368[»]
ProteinModelPortaliQ99ZW2.
SMRiQ99ZW2.
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.

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: November 2, 2016
This is version 90 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.