ID A0A4R6UK41_9GAMM Unreviewed; 1024 AA.
AC A0A4R6UK41;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=CRISPR-associated endonuclease Cas9 {ECO:0000256|HAMAP-Rule:MF_01480};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01480};
GN Name=cas9 {ECO:0000256|HAMAP-Rule:MF_01480};
GN ORFNames=EV696_11762 {ECO:0000313|EMBL:TDQ45829.1};
OS Permianibacter aggregans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Permianibacter.
OX NCBI_TaxID=1510150 {ECO:0000313|EMBL:TDQ45829.1, ECO:0000313|Proteomes:UP000295375};
RN [1] {ECO:0000313|EMBL:TDQ45829.1, ECO:0000313|Proteomes:UP000295375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103792 {ECO:0000313|EMBL:TDQ45829.1,
RC ECO:0000313|Proteomes:UP000295375};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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. The tracrRNA serves as a guide for ribonuclease 3-aided
CC processing of pre-crRNA. Subsequently Cas9/crRNA/tracrRNA
CC endonucleolytically cleaves linear or circular dsDNA target
CC complementary to the spacer; Cas9 is inactive in the absence of the 2
CC guide RNAs (gRNA). Cas9 recognizes the protospacer adjacent motif (PAM)
CC in the CRISPR repeat sequences to help distinguish self versus nonself,
CC as targets within the bacterial CRISPR locus do not have PAMs. PAM
CC recognition is also required for catalytic activity.
CC {ECO:0000256|HAMAP-Rule:MF_01480}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01480};
CC -!- SUBUNIT: Monomer. Binds crRNA and tracrRNA. {ECO:0000256|HAMAP-
CC Rule:MF_01480}.
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:0000256|HAMAP-Rule:MF_01480}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated Cas9 family.
CC {ECO:0000256|HAMAP-Rule:MF_01480}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TDQ45829.1}.
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DR EMBL; SNYM01000017; TDQ45829.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R6UK41; -.
DR Proteomes; UP000295375; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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-UniRule.
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; Ribonuclease H-like superfamily/Ribonuclease H; 3.
DR HAMAP; MF_01480; Cas9; 1.
DR InterPro; IPR028629; Cas9.
DR InterPro; IPR040619; Cas9_alpha-helical_lobe.
DR InterPro; IPR033114; HNH_CAS9.
DR InterPro; IPR003615; HNH_nuc.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR041383; RuvC_III.
DR NCBIfam; TIGR01865; cas_Csn1; 1.
DR Pfam; PF18470; Cas9_a; 1.
DR Pfam; PF13395; HNH_4; 1.
DR Pfam; PF18541; RuvC_III; 1.
DR PROSITE; PS51749; HNH_CAS9; 1.
PE 3: Inferred from homology;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118, ECO:0000256|HAMAP-
KW Rule:MF_01480}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01480};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_01480, ECO:0000256|PROSITE-
KW ProRule:PRU01085};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01480};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01480};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01480};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01480, ECO:0000256|PROSITE-
KW ProRule:PRU01085}; Reference proteome {ECO:0000313|Proteomes:UP000295375};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01480}.
FT DOMAIN 533..696
FT /note="HNH Cas9-type"
FT /evidence="ECO:0000259|PROSITE:PS51749"
FT REGION 860..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 524..555
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 13
FT /note="For RuvC-like nuclease domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
FT ACT_SITE 613
FT /note="Proton acceptor for HNH nuclease domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
FT BINDING 525
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
FT BINDING 529
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
FT BINDING 529
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
FT BINDING 753
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
SQ SEQUENCE 1024 AA; 117457 MW; 7E58A8988BBBECFF CRC64;
MLDSKMPYRL ALDLGSSSLG WALIRLNAEN KPSAIIKAGV RIFPDGRNPK DGSSLAVTRR
EARAMRRRRD RLLKRKARMI TVLTELGFFP SDSLERKALE SLNPYRLRAE GLDRELQPDE
FARALFHLNQ RRGFKSNRKT DKKDNDSGAM KQALSKLRQN LDESSCRTVG EWLFQRQCAG
QSLRARYRET RQIHEDGRTR VEKSYDLYID RTMIEAEFDT LWRSQAARNP SRYTDEARRR
LKDVLLFQRP LKPVRPGRCT LLPDEERAPL ALPSTQRVRI YQELNNLRVL GDSLQEYALT
LQQRDQLAAA LDHRPKMSFD QIRRLLRLDG QTKFNLEDIK RQEIRGNATA ALLSKSDFFG
EQWHSFNSSL QDEIVQHLIA DEEEQALIDW LIANTGIDEA CAQRLADVSL PQGYGSLGRT
ALARILPALR QSVLPFSAAV QAAGFEHHSA LDHVQKTGEI LLELPYYGEY LTRHVGFGTG
NPDDVLEKRY GRIANPTVHI GLNQTRVVVN ALLKRYGPPQ EIIVEVAREL KQSREDRLAE
QKRQAENQRR NQRLREEVAA ILEIEEHAVK TADIQKMILW EELSPDPADR RCPYSGEQIS
KHRLLSEEVE IEHILPFSET LDDSLNNKTV AMRMANRVKG NRSPWQAFGE HPIAGFDYQE
ILARAERMPK GKRYRFAPDG YQRWLKDDAG FLARALNDTR YLSRIAREYL RLICPQGTRV
IPGQMTALLR AKFGLNDVLG LHGEKNRNDH RHHAVDACVI GVTDQGMLKK FSEAARSARE
KQLDRLVEHM PLPWPTYREH VKRAINAIWV SHRPDHNYQG PMHNDTAYGL LGDGRVVHHK
WLDGKRERVE KSLKVIEFKN PDVRNRSGQP RHGVTENGSP RPYKGYDGNS NYCIEIVRVE
NGRWQGEVIS TYTAYQTVKA QGEKRLRDPK LSLSGQPLIM RLMIDDAVRL EIDDHIRTMR
VAKISANGQI FMCDLHEANV DKRNRDKNEL FAYVSKTAGS LHAARGRRVT ISPSGELHDP
GFAD
//
