ID A0A1W7MBU9_9SPHN Unreviewed; 1058 AA.
AC A0A1W7MBU9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=NMD1_02085 {ECO:0000313|EMBL:GAO54982.1};
OS Novosphingobium sp. MD-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1630648 {ECO:0000313|EMBL:GAO54982.1, ECO:0000313|Proteomes:UP000266860};
RN [1] {ECO:0000313|EMBL:GAO54982.1, ECO:0000313|Proteomes:UP000266860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-1 {ECO:0000313|EMBL:GAO54982.1,
RC ECO:0000313|Proteomes:UP000266860};
RA Okano K.;
RT "Draft Genome Sequence of the microcystin-degrading bacterium
RT Novosphingobium sp. MD-1.";
RL Submitted (APR-2015) 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 -!- 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:GAO54982.1}.
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DR EMBL; BBXA01000027; GAO54982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W7MBU9; -.
DR OrthoDB; 9777169at2; -.
DR Proteomes; UP000266860; 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; 1.10.30.50; -; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
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};
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01480, ECO:0000256|PROSITE-
KW ProRule:PRU01085}; Reference proteome {ECO:0000313|Proteomes:UP000266860};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01480}.
FT DOMAIN 508..665
FT /note="HNH Cas9-type"
FT /evidence="ECO:0000259|PROSITE:PS51749"
FT ACT_SITE 9
FT /note="For RuvC-like nuclease domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
FT ACT_SITE 583
FT /note="Proton acceptor for HNH nuclease domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
SQ SEQUENCE 1058 AA; 119557 MW; E3C75C08D1277414 CRC64;
MNGLVFGIDL GIASCGWAAL RHPTSGDSSG EIVAMGSWMF DVPETDKERT PTNQVRRGNR
LLRRVIRRRA QRMAEIRRLF TQRGLLAGNE PDALKRAGLD PWELRARGLD KPLSPAEFAV
ALGHIAKRRG FKSARKGKEA NTAGDDQKML RALEATRERL GRYRTVGEMF GRDADFRDRK
RNRDGLFDRT QSRDDLIHEV GKLFEAQRRL GNDTASTALE AEFTAIAFRQ LEMQDSEKLV
GMCQFEPKEK RAARFAPSFE KFRLLGKLVN LRITTPEGER PLTPEEVRLA TGDLGKTAKL
SVKEVRKRIG LPADQRFTAF KPEEEAQDIA ARTGEAMHGT RKLRDALGEV LWVELQDKPE
QLDQIAHIIS FHETADKIGE ELRKLGLRAA AVDALLEDLA AFSRFKGAGH ISAKAARALI
PHLEAGLRYD QACEAVGYDH AASRWSKREQ VADKAGFNAL VKSMGDEIAN PVARKSLTEG
LKQLWAMRNR WGLPDAVHIE IARDVGNSLE KRNEIKRGID KNTAERERQR DEVRELLGIE
DVNGDTLLRY RLWKEQAGRC PYTDKAIPAT AIIATDNSHQ VDHILPWSRF GDDSYSNKVL
CTARANQEKK GQTPFEWIMS SQGEDAWNTF LARIEGNTAF RGAKKRNYVL KNAKEAEERF
RTRNLNDTRY ASRLLAEAVK LFYPEGDRQE KGGNRRVFTR PGGLTSALRH AWGVESLKKV
DGKRVEDARH HALDALVVAA IGEWEVQRLT RSYQEWEQKG LARPLRQVDP PWGDAASFRR
EVKEAYDSVF VARPERRRAR GEGHAATIRQ VKERDGALIV YERKAVIDLG MEKGKFSKAK
ALKQLSMLKD RERNLAVAEA IENWIERGRP VENPPLGLPV SKEPDAPRHP ILKVRLATEK
KPAVGVRGGV ADRGEFVRID VFTLPNKKGE DEFYLVPIYP HEVHSKTPPA AFMTTDGQEK
SLTSDHIFKM SIYNRSYVEI EKRDGRVVAG YVVSFDRSVA ALKIYEHHTL KPVEKSSGVK
TLKRFSKYNV DRFGVRSEVK SEVRTWHGVV CTSPIPPD
//
