ID RNC_CAMJE Reviewed; 224 AA.
AC Q9PM40; Q0P7Z3;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Ribonuclease 3 {ECO:0000255|HAMAP-Rule:MF_00104};
DE EC=3.1.26.3 {ECO:0000255|HAMAP-Rule:MF_00104};
DE AltName: Full=Ribonuclease III {ECO:0000255|HAMAP-Rule:MF_00104};
DE Short=RNase III {ECO:0000255|HAMAP-Rule:MF_00104};
GN Name=rnc {ECO:0000255|HAMAP-Rule:MF_00104}; OrderedLocusNames=Cj1635c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 700819 / NCTC 11168;
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).
CC -!- FUNCTION: Digests double-stranded RNA. Involved in the processing of
CC primary rRNA transcript to yield the immediate precursors to the large
CC and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs
CC when they are encoded in the rRNA operon (By similarity).
CC {ECO:0000250}.
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 this
CC organism endogenous ribonuclease 3 and Cas9 are required for correct
CC coprocessing of pre-crRNA and the trans-encoded small RNA (tracrRNA).
CC Cas9, crRNA and tracrRNA are required for cleavage of invading DNA
CC (Probable). Complements pre-crRNA and tracrRNA coprocessing defects in
CC an rnc deletion in S.pyogenes strain 370 (PubMed:24270795).
CC {ECO:0000269|PubMed:24270795, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00104};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00104};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00104}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00104}.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000255|HAMAP-
CC Rule:MF_00104}.
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DR EMBL; AL111168; CAL35732.1; -; Genomic_DNA.
DR PIR; A81260; A81260.
DR RefSeq; WP_002851153.1; NZ_SZUC01000002.1.
DR RefSeq; YP_002345004.1; NC_002163.1.
DR PDB; 3N3W; X-ray; 2.21 A; A/B=1-224.
DR PDB; 3O2R; X-ray; 1.25 A; A/B/C/D=1-146.
DR PDBsum; 3N3W; -.
DR PDBsum; 3O2R; -.
DR AlphaFoldDB; Q9PM40; -.
DR SMR; Q9PM40; -.
DR IntAct; Q9PM40; 5.
DR STRING; 192222.Cj1635c; -.
DR PaxDb; 192222-Cj1635c; -.
DR EnsemblBacteria; CAL35732; CAL35732; Cj1635c.
DR GeneID; 905908; -.
DR KEGG; cje:Cj1635c; -.
DR PATRIC; fig|192222.6.peg.1611; -.
DR eggNOG; COG0571; Bacteria.
DR HOGENOM; CLU_000907_1_3_7; -.
DR OrthoDB; 9805026at2; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd10845; DSRM_RNAse_III_family; 1.
DR CDD; cd00593; RIBOc; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 1.10.1520.10; Ribonuclease III domain; 1.
DR HAMAP; MF_00104; RNase_III; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR011907; RNase_III.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR NCBIfam; TIGR02191; RNaseIII; 1.
DR PANTHER; PTHR14950; DICER-RELATED; 1.
DR PANTHER; PTHR14950:SF37; ENDORIBONUCLEASE DICER; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF14622; Ribonucleas_3_3; 1.
DR SMART; SM00358; DSRM; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF69065; RNase III domain-like; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW mRNA processing; Nuclease; Reference proteome; RNA-binding;
KW rRNA processing; rRNA-binding; tRNA processing.
FT CHAIN 1..224
FT /note="Ribonuclease 3"
FT /id="PRO_0000180383"
FT DOMAIN 4..127
FT /note="RNase III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT DOMAIN 154..223
FT /note="DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT ACT_SITE 44
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT ACT_SITE 116
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:3N3W"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:3N3W"
FT HELIX 37..58
FT /evidence="ECO:0007829|PDB:3N3W"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:3N3W"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:3N3W"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:3N3W"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3N3W"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:3N3W"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:3N3W"
FT HELIX 108..126
FT /evidence="ECO:0007829|PDB:3N3W"
FT HELIX 128..142
FT /evidence="ECO:0007829|PDB:3N3W"
SQ SEQUENCE 224 AA; 24964 MW; 4AB69FD394DB17CA CRC64;
MKNIEKLEQS LTYEFKDKNL LIHALTHKSF KKSYNNERLE FLGDAVLDLV VGEYLFHKFA
KDAEGDLSKL RAALVNEKSF AKIANSLNLG DFILMSVAEE NNGGKEKPSI LSDALEAIIG
AIHLEAGFEF AKTIALRLIE KNFPQIDAKI LIKDYKTKLQ EITQGKIGQT PQYETVRAFG
PDHLKQFEIA LMLDGKELAR AIAGSKKEAQ QMAAKIALEK LGAL
//
