RNC_XYLFM
ID RNC_XYLFM Reviewed; 227 AA.
AC B0U3D8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Xfasm12_1444;
OS Xylella fastidiosa (strain M12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405440;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12;
RX PubMed=20601474; DOI=10.1128/jb.00651-10;
RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT causing almond leaf scorch disease in California.";
RL J. Bacteriol. 192:4534-4534(2010).
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). Processes some mRNAs, and tRNAs when
CC they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA
CC of type II CRISPR loci if present in the organism. {ECO:0000255|HAMAP-
CC Rule:MF_00104}.
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; CP000941; ACA12367.1; -; Genomic_DNA.
DR RefSeq; WP_004083431.1; NC_010513.1.
DR AlphaFoldDB; B0U3D8; -.
DR SMR; B0U3D8; -.
DR KEGG; xfm:Xfasm12_1444; -.
DR HOGENOM; CLU_000907_1_1_6; -.
DR OMA; LTHKSCK; -.
DR OrthoDB; 1890943at2; -.
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; cd00593; RIBOc; 1.
DR Gene3D; 1.10.1520.10; -; 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 PANTHER; PTHR11207; PTHR11207; 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; SSF69065; SSF69065; 1.
DR TIGRFAMs; TIGR02191; RNaseIII; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW mRNA processing; Nuclease; RNA-binding; rRNA processing; rRNA-binding;
KW tRNA processing.
FT CHAIN 1..227
FT /note="Ribonuclease 3"
FT /id="PRO_1000094143"
FT DOMAIN 6..128
FT /note="RNase III"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT DOMAIN 155..225
FT /note="DRBM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT REGION 203..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 45
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT ACT_SITE 117
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00104"
SQ SEQUENCE 227 AA; 25189 MW; F15E0E278CD3CDA0 CRC64;
MISSKASDYQ QRIGYVFTDP SLLLQALRHC SAGTPHNERL EFLGDSVVNL LIAEALFQRW
PRADEGALTR ARSELVRETS LASIARTMQL GEQLILGPGE LKSGGHRRDS ILADAVEAVI
AAIYLDADLA TCRTVVLPWF ETALTALPVG KPEKDPKTRL QEWLQARQWS LPVYELIFES
GDPHTKHFRV SCTLGELKLR TEGEGSSRRL AEQDAASHAI NQLDSNK
