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CRISPR-associated endonuclease Cas9 (EC 3.1.-.-) (AnaCas9)

 CAS9_ACTNH              Reviewed;        1101 AA.
J3F2B0;
03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 1.
28-FEB-2018, entry version 29.
RecName: Full=CRISPR-associated endonuclease Cas9;
EC=3.1.-.-;
AltName: Full=AnaCas9 {ECO:0000303|PubMed:24505130};
Name=cas9; ORFNames=HMPREF1129_2620;
Actinomyces naeslundii (strain ATCC 12104 / DSM 43013 / JCM 8349 /
NCTC 10301 / Howell 279).
Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
Actinomyces.
NCBI_TaxID=1115803;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 12104 / DSM 43013 / JCM 8349 / NCTC 10301 / Howell 279;
Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B.,
Sutton G., Nelson K.E.;
Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
[2]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH MAGNESIUM;
MANGANESE AND ZINC, FUNCTION, ACTIVE SITE, COFACTOR, DOMAIN, AND
POSSIBLE BIOTECHNOLOGY.
STRAIN=ATCC 12104 / DSM 43013 / JCM 8349 / NCTC 10301 / Howell 279;
PubMed=24505130; DOI=10.1126/science.1247997;
Jinek M., Jiang F., Taylor D.W., Sternberg S.H., Kaya E., Ma E.,
Anders C., Hauer M., Zhou K., Lin S., Kaplan M., Iavarone A.T.,
Charpentier E., Nogales E., Doudna J.A.;
"Structures of Cas9 endonucleases reveal RNA-mediated conformational
activation.";
Science 343:1247997-1247997(2014).
-!- FUNCTION: 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. 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). 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. PAM recognition is also required for catalytic activity (By
similarity). {ECO:0000250, ECO:0000269|PubMed:24505130}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:24505130};
Note=Binds 2 Mg(2+) per subunit. {ECO:0000269|PubMed:24505130};
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:24505130};
Note=Binds 2 Mn(2+) per subunit. {ECO:0000269|PubMed:24505130};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:24505130};
Note=Binds 1 Zn(2+) per subunit, which may stabilize the HNH Cas9
architecture. {ECO:0000269|PubMed:24505130};
-!- SUBUNIT: Monomer. Binds crRNA and tracrRNA (Probable).
{ECO:0000305|PubMed:24505130}.
-!- DOMAIN: Has 2 endonuclease domains. The discontinuous RuvC-like
domain cleaves the target DNA noncomplementary to crRNA while the
HNH nuclease domain cleaves the target DNA complementary to crRNA
(Probable). {ECO:0000305|PubMed:24505130}.
-!- BIOTECHNOLOGY: The simplicity of the Cas9-gRNAs RNA-directed DNA
endonuclease activity may be used to target and modify a DNA
sequence of interest.
-!- SIMILARITY: Belongs to the CRISPR-associated protein Cas9 family.
Subtype II-C subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; ALJK01000149; EJN84392.1; -; Genomic_DNA.
PDB; 4OGC; X-ray; 2.80 A; A=1-1101.
PDB; 4OGE; X-ray; 2.20 A; A=1-1101.
PDBsum; 4OGC; -.
PDBsum; 4OGE; -.
SMR; J3F2B0; -.
EnsemblBacteria; EJN84392; EJN84392; HMPREF1129_2620.
PATRIC; fig|1115803.3.peg.1655; -.
OrthoDB; POG091H0A03; -.
Proteomes; UP000007814; Unassembled WGS sequence.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
Gene3D; 3.30.420.10; -; 2.
InterPro; IPR002711; HNH.
InterPro; IPR033114; HNH_CAS9.
InterPro; IPR003615; HNH_nuc.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF01844; HNH; 1.
SMART; SM00507; HNHc; 1.
PROSITE; PS51749; HNH_CAS9; 1.
1: Evidence at protein level;
3D-structure; Antiviral defense; Complete proteome; DNA-binding;
Endonuclease; Hydrolase; Magnesium; Manganese; Metal-binding;
Nuclease; RNA-binding; Zinc.
CHAIN 1 1101 CRISPR-associated endonuclease Cas9.
/FTId=PRO_0000429982.
DOMAIN 513 675 HNH Cas9-type. {ECO:0000255|PROSITE-
ProRule:PRU01085}.
REGION 1 64 RuvC-I. {ECO:0000305|PubMed:24505130}.
REGION 64 468 Recognition lobe.
{ECO:0000305|PubMed:24505130}.
REGION 468 513 RuvC-II. {ECO:0000305|PubMed:24505130}.
REGION 674 822 RuvC-III. {ECO:0000305|PubMed:24505130}.
REGION 924 1101 PAM-interacting domain (PI).
{ECO:0000305|PubMed:24505130}.
ACT_SITE 17 17 For RuvC-like nuclease domain.
{ECO:0000250|UniProtKB:Q99ZW2}.
ACT_SITE 582 582 Proton acceptor for HNH nuclease domain.
{ECO:0000269|PubMed:24505130}.
METAL 17 17 Manganese 1.
{ECO:0000269|PubMed:24505130}.
METAL 17 17 Manganese 2.
{ECO:0000269|PubMed:24505130}.
METAL 505 505 Manganese 2.
{ECO:0000269|PubMed:24505130}.
METAL 566 566 Zinc. {ECO:0000269|PubMed:24505130}.
METAL 569 569 Zinc. {ECO:0000269|PubMed:24505130}.
METAL 581 581 Magnesium 1; catalytic.
{ECO:0000269|PubMed:24505130}.
METAL 586 586 Magnesium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:24505130}.
METAL 588 588 Magnesium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:24505130}.
METAL 590 590 Magnesium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:24505130}.
METAL 602 602 Zinc. {ECO:0000269|PubMed:24505130}.
METAL 605 605 Zinc. {ECO:0000269|PubMed:24505130}.
METAL 606 606 Magnesium 1; catalytic.
{ECO:0000269|PubMed:24505130}.
METAL 736 736 Manganese 1; via pros nitrogen.
{ECO:0000269|PubMed:24505130}.
STRAND 11 18 {ECO:0000244|PDB:4OGE}.
STRAND 20 30 {ECO:0000244|PDB:4OGE}.
STRAND 36 46 {ECO:0000244|PDB:4OGE}.
HELIX 66 91 {ECO:0000244|PDB:4OGE}.
TURN 92 94 {ECO:0000244|PDB:4OGE}.
HELIX 138 147 {ECO:0000244|PDB:4OGE}.
TURN 148 153 {ECO:0000244|PDB:4OGE}.
STRAND 227 230 {ECO:0000244|PDB:4OGE}.
HELIX 237 242 {ECO:0000244|PDB:4OGE}.
HELIX 243 246 {ECO:0000244|PDB:4OGE}.
TURN 247 249 {ECO:0000244|PDB:4OGE}.
STRAND 256 258 {ECO:0000244|PDB:4OGE}.
HELIX 278 290 {ECO:0000244|PDB:4OGE}.
STRAND 293 297 {ECO:0000244|PDB:4OGE}.
STRAND 301 303 {ECO:0000244|PDB:4OGE}.
HELIX 306 318 {ECO:0000244|PDB:4OGE}.
HELIX 326 333 {ECO:0000244|PDB:4OGE}.
HELIX 337 339 {ECO:0000244|PDB:4OGE}.
HELIX 361 368 {ECO:0000244|PDB:4OGE}.
HELIX 372 379 {ECO:0000244|PDB:4OGE}.
HELIX 384 394 {ECO:0000244|PDB:4OGE}.
HELIX 401 404 {ECO:0000244|PDB:4OGE}.
TURN 405 407 {ECO:0000244|PDB:4OGE}.
TURN 410 414 {ECO:0000244|PDB:4OGE}.
HELIX 415 418 {ECO:0000244|PDB:4OGE}.
HELIX 431 443 {ECO:0000244|PDB:4OGE}.
HELIX 448 456 {ECO:0000244|PDB:4OGE}.
HELIX 476 496 {ECO:0000244|PDB:4OGE}.
STRAND 500 505 {ECO:0000244|PDB:4OGE}.
HELIX 514 542 {ECO:0000244|PDB:4OGE}.
HELIX 550 561 {ECO:0000244|PDB:4OGE}.
TURN 567 569 {ECO:0000244|PDB:4OGE}.
TURN 575 577 {ECO:0000244|PDB:4OGE}.
STRAND 579 584 {ECO:0000244|PDB:4OGE}.
STRAND 586 590 {ECO:0000244|PDB:4OGE}.
HELIX 595 597 {ECO:0000244|PDB:4OGE}.
STRAND 598 601 {ECO:0000244|PDB:4OGE}.
HELIX 603 609 {ECO:0000244|PDB:4OGE}.
HELIX 614 621 {ECO:0000244|PDB:4OGE}.
HELIX 628 636 {ECO:0000244|PDB:4OGE}.
HELIX 647 662 {ECO:0000244|PDB:4OGE}.
TURN 672 675 {ECO:0000244|PDB:4OGE}.
HELIX 680 692 {ECO:0000244|PDB:4OGE}.
STRAND 696 701 {ECO:0000244|PDB:4OGE}.
HELIX 705 713 {ECO:0000244|PDB:4OGE}.
TURN 716 718 {ECO:0000244|PDB:4OGE}.
HELIX 735 745 {ECO:0000244|PDB:4OGE}.
HELIX 748 766 {ECO:0000244|PDB:4OGE}.
HELIX 773 775 {ECO:0000244|PDB:4OGE}.
HELIX 781 806 {ECO:0000244|PDB:4OGE}.
STRAND 810 813 {ECO:0000244|PDB:4OGE}.
STRAND 834 837 {ECO:0000244|PDB:4OGE}.
HELIX 838 840 {ECO:0000244|PDB:4OGE}.
HELIX 844 848 {ECO:0000244|PDB:4OGE}.
STRAND 850 852 {ECO:0000244|PDB:4OGE}.
HELIX 853 860 {ECO:0000244|PDB:4OGE}.
TURN 867 869 {ECO:0000244|PDB:4OGE}.
STRAND 878 881 {ECO:0000244|PDB:4OGE}.
STRAND 884 887 {ECO:0000244|PDB:4OGE}.
STRAND 890 894 {ECO:0000244|PDB:4OGE}.
STRAND 900 902 {ECO:0000244|PDB:4OGC}.
STRAND 911 915 {ECO:0000244|PDB:4OGE}.
STRAND 918 921 {ECO:0000244|PDB:4OGE}.
STRAND 926 934 {ECO:0000244|PDB:4OGE}.
STRAND 936 938 {ECO:0000244|PDB:4OGE}.
STRAND 940 947 {ECO:0000244|PDB:4OGE}.
HELIX 948 954 {ECO:0000244|PDB:4OGE}.
TURN 959 961 {ECO:0000244|PDB:4OGE}.
HELIX 969 972 {ECO:0000244|PDB:4OGE}.
HELIX 976 983 {ECO:0000244|PDB:4OGE}.
STRAND 987 993 {ECO:0000244|PDB:4OGE}.
STRAND 998 1000 {ECO:0000244|PDB:4OGE}.
HELIX 1009 1017 {ECO:0000244|PDB:4OGE}.
STRAND 1023 1031 {ECO:0000244|PDB:4OGE}.
STRAND 1034 1042 {ECO:0000244|PDB:4OGE}.
HELIX 1044 1046 {ECO:0000244|PDB:4OGE}.
HELIX 1052 1058 {ECO:0000244|PDB:4OGE}.
STRAND 1063 1066 {ECO:0000244|PDB:4OGE}.
HELIX 1067 1072 {ECO:0000244|PDB:4OGE}.
STRAND 1076 1078 {ECO:0000244|PDB:4OGE}.
SEQUENCE 1101 AA; 123754 MW; D93767E60402ACC2 CRC64;
MWYASLMSAH HLRVGIDVGT HSVGLATLRV DDHGTPIELL SALSHIHDSG VGKEGKKDHD
TRKKLSGIAR RARRLLHHRR TQLQQLDEVL RDLGFPIPTP GEFLDLNEQT DPYRVWRVRA
RLVEEKLPEE LRGPAISMAV RHIARHRGWR NPYSKVESLL SPAEESPFMK ALRERILATT
GEVLDDGITP GQAMAQVALT HNISMRGPEG ILGKLHQSDN ANEIRKICAR QGVSPDVCKQ
LLRAVFKADS PRGSAVSRVA PDPLPGQGSF RRAPKCDPEF QRFRIISIVA NLRISETKGE
NRPLTADERR HVVTFLTEDS QADLTWVDVA EKLGVHRRDL RGTAVHTDDG ERSAARPPID
ATDRIMRQTK ISSLKTWWEE ADSEQRGAMI RYLYEDPTDS ECAEIIAELP EEDQAKLDSL
HLPAGRAAYS RESLTALSDH MLATTDDLHE ARKRLFGVDD SWAPPAEAIN APVGNPSVDR
TLKIVGRYLS AVESMWGTPE VIHVEHVRDG FTSERMADER DKANRRRYND NQEAMKKIQR
DYGKEGYISR GDIVRLDALE LQGCACLYCG TTIGYHTCQL DHIVPQAGPG SNNRRGNLVA
VCERCNRSKS NTPFAVWAQK CGIPHVGVKE AIGRVRGWRK QTPNTSSEDL TRLKKEVIAR
LRRTQEDPEI DERSMESVAW MANELHHRIA AAYPETTVMV YRGSITAAAR KAAGIDSRIN
LIGEKGRKDR IDRRHHAVDA SVVALMEASV AKTLAERSSL RGEQRLTGKE QTWKQYTGST
VGAREHFEMW RGHMLHLTEL FNERLAEDKV YVTQNIRLRL SDGNAHTVNP SKLVSHRLGD
GLTVQQIDRA CTPALWCALT REKDFDEKNG LPAREDRAIR VHGHEIKSSD YIQVFSKRKK
TDSDRDETPF GAIAVRGGFV EIGPSIHHAR IYRVEGKKPV YAMLRVFTHD LLSQRHGDLF
SAVIPPQSIS MRCAEPKLRK AITTGNATYL GWVVVGDELE INVDSFTKYA IGRFLEDFPN
TTRWRICGYD TNSKLTLKPI VLAAEGLENP SSAVNEIVEL KGWRVAINVL TKVHPTVVRR
DALGRPRYSS RSNLPTSWTI E


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