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CAS9B_STRTD
ID   CAS9B_STRTD             Reviewed;        1388 AA.
AC   Q03JI6;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=CRISPR-associated endonuclease Cas9 2 {ECO:0000255|HAMAP-Rule:MF_01480};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01480};
DE   AltName: Full=Cas9*;
DE   AltName: Full=St3Cas9;
GN   Name=cas9-2 {ECO:0000255|HAMAP-Rule:MF_01480}; Synonyms=csn1;
GN   OrderedLocusNames=STER_1477;
OS   Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=322159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-491 / LMD-9;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
RN   [2]
RP   FUNCTION AS AN DNA ENDONUCLEASE, SUBUNIT, AND RNA-BINDING.
RC   STRAIN=ATCC BAA-491 / LMD-9;
RX   PubMed=22745249; DOI=10.1126/science.1225829;
RA   Jinek M., Chylinski K., Fonfara I., Hauer M., Doudna J.A., Charpentier E.;
RT   "A programmable dual-RNA-guided DNA endonuclease in adaptive bacterial
RT   immunity.";
RL   Science 337:816-821(2012).
RN   [3]
RP   BIOTECHNOLOGY.
RC   STRAIN=ATCC BAA-491 / LMD-9;
RX   PubMed=23287718; DOI=10.1126/science.1231143;
RA   Cong L., Ran F.A., Cox D., Lin S., Barretto R., Habib N., Hsu P.D., Wu X.,
RA   Jiang W., Marraffini L.A., Zhang F.;
RT   "Multiplex genome engineering using CRISPR/Cas systems.";
RL   Science 339:819-823(2013).
RN   [4]
RP   FUNCTION AS AN ENDONUCLEASE, AND FUNCTION IN GUIDE RNA PROCESSING.
RC   STRAIN=ATCC BAA-491 / LMD-9;
RX   PubMed=24270795; DOI=10.1093/nar/gkt1074;
RA   Fonfara I., Le Rhun A., Chylinski K., Makarova K.S., Lecrivain A.L.,
RA   Bzdrenga J., Koonin E.V., Charpentier E.;
RT   "Phylogeny of Cas9 determines functional exchangeability of dual-RNA and
RT   Cas9 among orthologous type II CRISPR-Cas systems.";
RL   Nucleic Acids Res. 42:2577-2590(2014).
RN   [5]
RP   FUNCTION, AND DOMAIN.
RX   PubMed=24505130; DOI=10.1126/science.1247997;
RA   Jinek M., Jiang F., Taylor D.W., Sternberg S.H., Kaya E., Ma E., Anders C.,
RA   Hauer M., Zhou K., Lin S., Kaplan M., Iavarone A.T., Charpentier E.,
RA   Nogales E., Doudna J.A.;
RT   "Structures of Cas9 endonucleases reveal RNA-mediated conformational
RT   activation.";
RL   Science 343:1247997-1247997(2014).
CC   -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC       repeat) is an adaptive immune system that provides protection against
CC       mobile genetic elements (viruses, transposable elements and conjugative
CC       plasmids). CRISPR clusters contain spacers, sequences complementary to
CC       antecedent mobile elements, and target invading nucleic acids. CRISPR
CC       clusters are transcribed and processed into CRISPR RNA (crRNA). In type
CC       II CRISPR systems correct processing of pre-crRNA requires a trans-
CC       encoded small RNA (tracrRNA), endogenous ribonuclease 3 (rnc) and this
CC       protein (By similarity). The tracrRNA serves as a guide for
CC       ribonuclease 3-aided processing of pre-crRNA. Subsequently
CC       Cas9/crRNA/tracrRNA endonucleolytically cleaves linear or circular
CC       dsDNA target complementary to the spacer yielding blunt ends; Cas9 is
CC       inactive in the absence of the 2 guide RNAs (gRNA). Cas9 recognizes a
CC       3'-G-rich protospacer adjacent motif (PAM, GGG in this organism) in the
CC       CRISPR repeat sequences to help distinguish self versus nonself, as
CC       targets within the bacterial CRISPR locus do not have PAMs. PAM
CC       recognition is also required for catalytic activity. Complements the
CC       gRNA coprocessing defect in a cas9 deletion in S.pyogenes strain 370,
CC       and cuts target DNA in Cas9:gRNAs mixing experiments with S.mutans
CC       strain UA159. {ECO:0000255|HAMAP-Rule:MF_01480,
CC       ECO:0000269|PubMed:22745249, ECO:0000269|PubMed:24270795,
CC       ECO:0000269|PubMed:24505130}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC       Note=Endonuclease activity on target dsDNA requires Mg(2+).
CC       {ECO:0000305};
CC   -!- SUBUNIT: Monomer (By similarity). Binds crRNA and tracrRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01480, ECO:0000269|PubMed:22745249}.
CC   -!- DOMAIN: Has 2 endonuclease domains. The discontinuous RuvC-like domain
CC       cleaves the target DNA noncomplementary to crRNA while the HNH nuclease
CC       domain cleaves the target DNA complementary to crRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01480}.
CC   -!- DOMAIN: The PAM-interacting domain (PI domain, approximately residues
CC       1102-1388) recognizes the PAM motif; swapping the PI domain of this
CC       enzyme with that from S.pyogenes Cas9 (AC Q99ZW2) prevents cleavage of
CC       DNA with the endogenous PAM site but confers the ability to cleave DNA
CC       with the PAM site specific for S.pyogenes CRISPRs.
CC       {ECO:0000269|PubMed:24505130}.
CC   -!- BIOTECHNOLOGY: Coexpression of Cas9 and both gRNAs in human cells has
CC       shown it is possible to use this system to target and modify a DNA
CC       sequence of interest in situ. {ECO:0000269|PubMed:23287718}.
CC   -!- SIMILARITY: Belongs to the CRISPR-associated protein Cas9 family.
CC       Subtype II-A subfamily. {ECO:0000255|HAMAP-Rule:MF_01480, ECO:0000305}.
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DR   EMBL; CP000419; ABJ66636.1; -; Genomic_DNA.
DR   RefSeq; WP_011681470.1; NC_008532.1.
DR   AlphaFoldDB; Q03JI6; -.
DR   SMR; Q03JI6; -.
DR   PRIDE; Q03JI6; -.
DR   KEGG; ste:STER_1477; -.
DR   HOGENOM; CLU_005604_0_0_9; -.
DR   OMA; TDRHSIK; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-UniRule.
DR   GO; GO:0043571; P:maintenance of CRISPR repeat elements; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_01480; Cas9; 1.
DR   InterPro; IPR028629; Cas9.
DR   InterPro; IPR032239; Cas9-BH.
DR   InterPro; IPR032237; Cas9_PI.
DR   InterPro; IPR032240; Cas9_REC.
DR   InterPro; IPR033114; HNH_CAS9.
DR   InterPro; IPR003615; HNH_nuc.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF16593; Cas9-BH; 1.
DR   Pfam; PF16595; Cas9_PI; 1.
DR   Pfam; PF16592; Cas9_REC; 1.
DR   Pfam; PF13395; HNH_4; 1.
DR   TIGRFAMs; TIGR01865; cas_Csn1; 1.
DR   PROSITE; PS51749; HNH_CAS9; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; DNA-binding; Endonuclease; Hydrolase; Magnesium;
KW   Manganese; Metal-binding; Nuclease; RNA-binding.
FT   CHAIN           1..1388
FT                   /note="CRISPR-associated endonuclease Cas9 2"
FT                   /id="PRO_0000421686"
FT   DOMAIN          771..928
FT                   /note="HNH Cas9-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01085"
FT   REGION          1100..1130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1102..1388
FT                   /note="PAM-interacting domain (PI)"
FT   ACT_SITE        10
FT                   /note="For RuvC-like nuclease domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01480"
FT   ACT_SITE        847
FT                   /note="Proton acceptor for HNH nuclease domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01480"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01480"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01480"
FT   BINDING         763
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01480"
FT   BINDING         767
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01480"
FT   BINDING         767
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01480"
FT   BINDING         990
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01480"
SQ   SEQUENCE   1388 AA;  161031 MW;  B97BC4C953090235 CRC64;
     MTKPYSIGLD IGTNSVGWAV TTDNYKVPSK KMKVLGNTSK KYIKKNLLGV LLFDSGITAE
     GRRLKRTARR RYTRRRNRIL YLQEIFSTEM ATLDDAFFQR LDDSFLVPDD KRDSKYPIFG
     NLVEEKAYHD EFPTIYHLRK YLADSTKKAD LRLVYLALAH MIKYRGHFLI EGEFNSKNND
     IQKNFQDFLD TYNAIFESDL SLENSKQLEE IVKDKISKLE KKDRILKLFP GEKNSGIFSE
     FLKLIVGNQA DFRKCFNLDE KASLHFSKES YDEDLETLLG YIGDDYSDVF LKAKKLYDAI
     LLSGFLTVTD NETEAPLSSA MIKRYNEHKE DLALLKEYIR NISLKTYNEV FKDDTKNGYA
     GYIDGKTNQE DFYVYLKKLL AEFEGADYFL EKIDREDFLR KQRTFDNGSI PYQIHLQEMR
     AILDKQAKFY PFLAKNKERI EKILTFRIPY YVGPLARGNS DFAWSIRKRN EKITPWNFED
     VIDKESSAEA FINRMTSFDL YLPEEKVLPK HSLLYETFNV YNELTKVRFI AESMRDYQFL
     DSKQKKDIVR LYFKDKRKVT DKDIIEYLHA IYGYDGIELK GIEKQFNSSL STYHDLLNII
     NDKEFLDDSS NEAIIEEIIH TLTIFEDREM IKQRLSKFEN IFDKSVLKKL SRRHYTGWGK
     LSAKLINGIR DEKSGNTILD YLIDDGISNR NFMQLIHDDA LSFKKKIQKA QIIGDEDKGN
     IKEVVKSLPG SPAIKKGILQ SIKIVDELVK VMGGRKPESI VVEMARENQY TNQGKSNSQQ
     RLKRLEKSLK ELGSKILKEN IPAKLSKIDN NALQNDRLYL YYLQNGKDMY TGDDLDIDRL
     SNYDIDHIIP QAFLKDNSID NKVLVSSASN RGKSDDVPSL EVVKKRKTFW YQLLKSKLIS
     QRKFDNLTKA ERGGLSPEDK AGFIQRQLVE TRQITKHVAR LLDEKFNNKK DENNRAVRTV
     KIITLKSTLV SQFRKDFELY KVREINDFHH AHDAYLNAVV ASALLKKYPK LEPEFVYGDY
     PKYNSFRERK SATEKVYFYS NIMNIFKKSI SLADGRVIER PLIEVNEETG ESVWNKESDL
     ATVRRVLSYP QVNVVKKVEE QNHGLDRGKP KGLFNANLSS KPKPNSNENL VGAKEYLDPK
     KYGGYAGISN SFTVLVKGTI EKGAKKKITN VLEFQGISIL DRINYRKDKL NFLLEKGYKD
     IELIIELPKY SLFELSDGSR RMLASILSTN NKRGEIHKGN QIFLSQKFVK LLYHAKRISN
     TINENHRKYV ENHKKEFEEL FYYILEFNEN YVGAKKNGKL LNSAFQSWQN HSIDELCSSF
     IGPTGSERKG LFELTSRGSA ADFEFLGVKI PRYRDYTPSS LLKDATLIHQ SVTGLYETRI
     DLAKLGEG
 
 
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