ID A0A517TX54_9BACT Unreviewed; 1061 AA.
AC A0A517TX54;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-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_1 {ECO:0000313|EMBL:QDT72950.1};
GN Synonyms=cas9 {ECO:0000256|HAMAP-Rule:MF_01480};
GN ORFNames=I41_21370 {ECO:0000313|EMBL:QDT72950.1};
OS Lacipirellula limnantheis.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Lacipirellulaceae;
OC Lacipirellula.
OX NCBI_TaxID=2528024 {ECO:0000313|EMBL:QDT72950.1, ECO:0000313|Proteomes:UP000317909};
RN [1] {ECO:0000313|EMBL:QDT72950.1, ECO:0000313|Proteomes:UP000317909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I41 {ECO:0000313|EMBL:QDT72950.1,
RC ECO:0000313|Proteomes:UP000317909};
RA Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA Labrenz M., Spormann A.M., Op den Camp H., Overmann J., Amann R.,
RA Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT characterization uncovers novel biology.";
RL Submitted (FEB-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP036339; QDT72950.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A517TX54; -.
DR Proteomes; UP000317909; Chromosome.
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, 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:UP000317909};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01480}.
FT DOMAIN 537..690
FT /note="HNH Cas9-type"
FT /evidence="ECO:0000259|PROSITE:PS51749"
FT REGION 224..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 9
FT /note="For RuvC-like nuclease domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
FT ACT_SITE 608
FT /note="Proton acceptor for HNH nuclease domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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 533
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
FT BINDING 533
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
FT BINDING 763
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01480"
SQ SEQUENCE 1061 AA; 121662 MW; 4B448A145B46FB7C CRC64;
MANLVLGLDL GPNSIGWALL GDGAEGDSQL VDMGVRVFPE GVDAFDTAKE RSRNEDRRIN
RGMRRQIRRR ARRKRLLQAA LVESGLWPVD AAAQEEALAV DPYWLRAKGV SERLEPYEIG
RVFLHLNQRR GFLSNKKKDR GDKEVQGMLA EIKHNEELVA LGGFETVGQL LAEKCAALDH
TARQEDDEVR NRHLSRRQLV DEFHTIWSKQ ATFHPQLLTD KLRDGTVGGT MEPRKAVPKH
DPRRNKLSDL KAFGLFGLIF FQRRMYWPKS VVGLCELESK EKRCPKGDRR AERFRVLQEV
NNLRYIDTAE GDEQPLSEEQ RRLLIDYLSD REKATFDQIR KKLGFLESVK FNFERGKRTA
LKGFLIDWMI AKETDKSWYD RPEAQRDEIV RILLDNERDD ERILTTLIDK YGFSTVAAET
LLEIDFPPGY GSLSLKAIDK LLPSLERGLV YQSISDPEES ALHAAGYLRR DELQRRLFDK
LPNLARTRPA DCKLGDIPNP VVKRALVELR KVVNSIVVKY GKPSAVHVEM AREVQMGAER
RKEITARMRA REAEREKAAE AIRKMGYAAR RDSVTKYMLW QEQGHECVYC GKPISQTQLF
GGEIDVDHVL PYSRTLDNSQ GNKVVGHVKC NHLKGNRTPY EWLAAGDAVR YAEVCQRAAA
LLQKGMMPYG KYRKFLQKQL DLDKFIARQL TDTGYITRAT VEYLRLLFEK DHEVLGLKGQ
LTAELRWQWG LDKILEELPD SPAWIEKNDL RPGEKNRADH RHHAIDAIVV ALTNRKRLHK
LSELVRRGGA KKHGEILEEP WPDFRDTVVE RVKGLKVSHR VERKVRGALH EETLYGPTPT
EGEWVVRKPV ENLSPAEVER IRDAGIRTIV LESLRKRGID FGRGKKPDAK KMKEALSNLR
MPSGVPIKKV RILKQEQTIQ PLRDAPEHQA YVKPGSTHHL CIFEFEEKGK KKRKAIFVTM
LDAAKRQKRG EPIISRTHPE RPDAKFIMSL SSREMVLANW NGEQKLLVYK TAASTQGQIY
FAEHTDARRS SDQAKFVASA NSLDARKVTV DPLGRIRWAN D
//
