RNC_THEMA
ID RNC_THEMA Reviewed; 240 AA.
AC Q9X0I6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ribonuclease 3;
DE EC=3.1.26.3;
DE AltName: Full=Ribonuclease III;
DE Short=RNase III;
GN Name=rnc; OrderedLocusNames=TM_1102;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION AS AN RNASE, FUNCTION AS AN ENDONUCLEASE, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND RRNA-BINDING.
RX PubMed=20677811; DOI=10.1021/bi100930u;
RA Nathania L., Nicholson A.W.;
RT "Thermotoga maritima ribonuclease III. Characterization of thermostable
RT biochemical behavior and analysis of conserved base pairs that function as
RT reactivity epitopes for the Thermotoga 23S rRNA precursor.";
RL Biochemistry 49:7164-7178(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of ribonuclease III (TM1102) from Thermotoga maritima at
RT 2.0 A resolution.";
RL Submitted (FEB-2009) to the PDB data bank.
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. Probably processes pre-crRNA
CC and tracrRNA of type II CRISPR loci if present in the organism.
CC {ECO:0000269|PubMed:20677811}.
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;
CC Evidence={ECO:0000269|PubMed:20677811};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:20677811};
CC Temperature dependence:
CC Optimum temperature is 40-70 degrees Celsius.
CC {ECO:0000269|PubMed:20677811};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonuclease III family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36178.1; -; Genomic_DNA.
DR PIR; H72294; H72294.
DR RefSeq; NP_228908.1; NC_000853.1.
DR RefSeq; WP_004080335.1; NZ_CP011107.1.
DR PDB; 1O0W; X-ray; 2.00 A; A/B=1-240.
DR PDBsum; 1O0W; -.
DR AlphaFoldDB; Q9X0I6; -.
DR SMR; Q9X0I6; -.
DR STRING; 243274.THEMA_08835; -.
DR EnsemblBacteria; AAD36178; AAD36178; TM_1102.
DR KEGG; tma:TM1102; -.
DR eggNOG; COG0571; Bacteria.
DR InParanoid; Q9X0I6; -.
DR OMA; LTHKSCK; -.
DR OrthoDB; 1890943at2; -.
DR BRENDA; 3.1.26.3; 6331.
DR EvolutionaryTrace; Q9X0I6; -.
DR Proteomes; UP000008183; 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:0019843; F:rRNA binding; IEA:UniProtKB-KW.
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; rRNA-binding; tRNA processing.
FT CHAIN 1..240
FT /note="Ribonuclease 3"
FT /id="PRO_0000180448"
FT DOMAIN 9..141
FT /note="RNase III"
FT DOMAIN 168..237
FT /note="DRBM"
FT ACT_SITE 58
FT /evidence="ECO:0000255"
FT ACT_SITE 130
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:1O0W"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:1O0W"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:1O0W"
FT HELIX 51..72
FT /evidence="ECO:0007829|PDB:1O0W"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:1O0W"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:1O0W"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:1O0W"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:1O0W"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1O0W"
FT HELIX 122..140
FT /evidence="ECO:0007829|PDB:1O0W"
FT HELIX 142..161
FT /evidence="ECO:0007829|PDB:1O0W"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:1O0W"
FT STRAND 186..193
FT /evidence="ECO:0007829|PDB:1O0W"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:1O0W"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:1O0W"
FT HELIX 220..235
FT /evidence="ECO:0007829|PDB:1O0W"
SQ SEQUENCE 240 AA; 27530 MW; 94330E8898D48A0D CRC64;
MNESERKIVE EFQKETGINF KNEELLFRAL CHSSYANEQN QAGRKDVESN EKLEFLGDAV
LELFVCEILY KKYPEAEVGD LARVKSAAAS EEVLAMVSRK MNLGKFLFLG KGEEKTGGRD
RDSILADAFE ALLAAIYLDQ GYEKIKELFE QEFEFYIEKI MKGEMLFDYK TALQEIVQSE
HKVPPEYILV RTEKNDGDRI FVVEVRVNGK TIATGKGRTK KEAEKEAARI AYEKLLKERS
