MRNC_THEVB
ID MRNC_THEVB Reviewed; 151 AA.
AC Q8DLQ0;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Mini-ribonuclease 3 {ECO:0000255|HAMAP-Rule:MF_01468};
DE Short=Mini-3 {ECO:0000255|HAMAP-Rule:MF_01468};
DE Short=Mini-RNase 3 {ECO:0000255|HAMAP-Rule:MF_01468};
DE EC=3.1.26.- {ECO:0000255|HAMAP-Rule:MF_01468};
DE AltName: Full=Mini-RNase III {ECO:0000255|HAMAP-Rule:MF_01468};
DE Short=Mini-III {ECO:0000255|HAMAP-Rule:MF_01468};
GN Name=mrnC {ECO:0000255|HAMAP-Rule:MF_01468}; OrderedLocusNames=tlr0428;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
CC -!- FUNCTION: Involved in correct processing of both the 5' and 3' ends of
CC 23S rRNA precursor. Processes 30S rRNA precursor transcript even in
CC absence of ribonuclease 3 (Rnc); Rnc processes 30S rRNA into smaller
CC rRNA precursors. {ECO:0000255|HAMAP-Rule:MF_01468}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01468};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01468}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01468}.
CC -!- SIMILARITY: Belongs to the MrnC RNase family. {ECO:0000255|HAMAP-
CC Rule:MF_01468}.
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DR EMBL; BA000039; BAC07980.1; -; Genomic_DNA.
DR RefSeq; NP_681218.1; NC_004113.1.
DR RefSeq; WP_011056283.1; NC_004113.1.
DR AlphaFoldDB; Q8DLQ0; -.
DR SMR; Q8DLQ0; -.
DR STRING; 197221.22294149; -.
DR EnsemblBacteria; BAC07980; BAC07980; BAC07980.
DR KEGG; tel:tlr0428; -.
DR PATRIC; fig|197221.4.peg.452; -.
DR eggNOG; COG1939; Bacteria.
DR OMA; AYMGDAI; -.
DR OrthoDB; 1939897at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1520.10; -; 1.
DR HAMAP; MF_01468; RNase_Mini_III; 1.
DR InterPro; IPR008226; Mini3_fam.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR Pfam; PF00636; Ribonuclease_3; 1.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF69065; SSF69065; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Nuclease;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing;
KW rRNA-binding.
FT CHAIN 1..151
FT /note="Mini-ribonuclease 3"
FT /id="PRO_0000415996"
FT ACT_SITE 30
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01468"
SQ SEQUENCE 151 AA; 17261 MW; 0CA587F44CD001B2 CRC64;
MLDFGELLPL QPPTIPAHQL PPAALAYFGD AVYELFIRLL FLTPPQRINA YHRQVVAHVR
AESQARYMDF LWEYCTETER SIFRQGRNAA ADGPKRVAAK IYRQATGFEA LLGYLYLTNP
QRLQEIFQLL AGHIRSEVEN KTHAAESPSE M