RNC_MYCTU
ID RNC_MYCTU Reviewed; 240 AA.
AC P9WH03; L0TDT0; P66666; Q10962;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Ribonuclease 3;
DE EC=3.1.26.3;
DE AltName: Full=Ribonuclease III;
DE Short=RNase III;
GN Name=rnc; OrderedLocusNames=Rv2925c; ORFNames=MTCY338.14c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16155207; DOI=10.1110/ps.051665905;
RA Akey D.L., Berger J.M.;
RT "Structure of the nuclease domain of ribonuclease III from M. tuberculosis
RT at 2.1 A.";
RL Protein Sci. 14:2744-2750(2005).
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 (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16155207}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45728.1; -; Genomic_DNA.
DR PIR; E70748; E70748.
DR RefSeq; NP_217441.1; NC_000962.3.
DR RefSeq; WP_003414820.1; NZ_NVQJ01000006.1.
DR PDB; 2A11; X-ray; 2.10 A; A=1-240.
DR PDBsum; 2A11; -.
DR AlphaFoldDB; P9WH03; -.
DR SMR; P9WH03; -.
DR STRING; 83332.Rv2925c; -.
DR PaxDb; P9WH03; -.
DR DNASU; 887873; -.
DR GeneID; 45426913; -.
DR GeneID; 887873; -.
DR KEGG; mtu:Rv2925c; -.
DR TubercuList; Rv2925c; -.
DR eggNOG; COG0571; Bacteria.
DR OMA; LTHKSCK; -.
DR PhylomeDB; P9WH03; -.
DR BRENDA; 3.1.26.3; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
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 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; tRNA processing.
FT CHAIN 1..240
FT /note="Ribonuclease 3"
FT /id="PRO_0000180413"
FT DOMAIN 19..134
FT /note="RNase III"
FT DOMAIN 161..229
FT /note="DRBM"
FT ACT_SITE 48
FT /evidence="ECO:0000255"
FT ACT_SITE 123
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:2A11"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:2A11"
FT HELIX 28..33
FT /evidence="ECO:0007829|PDB:2A11"
FT HELIX 41..62
FT /evidence="ECO:0007829|PDB:2A11"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:2A11"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:2A11"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:2A11"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2A11"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:2A11"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2A11"
FT HELIX 115..133
FT /evidence="ECO:0007829|PDB:2A11"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:2A11"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:2A11"
SQ SEQUENCE 240 AA; 25399 MW; 64C8636742F161DC CRC64;
MIRSRQPLLD ALGVDLPDEL LSLALTHRSY AYENGGLPTN ERLEFLGDAV LGLTITDALF
HRHPDRSEGD LAKLRASVVN TQALADVARR LCAEGLGVHV LLGRGEANTG GADKSSILAD
GMESLLGAIY LQHGMEKARE VILRLFGPLL DAAPTLGAGL DWKTSLQELT AARGLGAPSY
LVTSTGPDHD KEFTAVVVVM DSEYGSGVGR SKKEAEQKAA AAAWKALEVL DNAMPGKTSA
