ID R6CZQ4_9FIRM Unreviewed; 118 AA.
AC R6CZQ4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Mini-ribonuclease 3 {ECO:0000256|HAMAP-Rule:MF_01468};
DE Short=Mini-3 {ECO:0000256|HAMAP-Rule:MF_01468};
DE Short=Mini-RNase 3 {ECO:0000256|HAMAP-Rule:MF_01468};
DE EC=3.1.26.- {ECO:0000256|HAMAP-Rule:MF_01468};
DE AltName: Full=Mini-RNase III {ECO:0000256|HAMAP-Rule:MF_01468};
DE Short=Mini-III {ECO:0000256|HAMAP-Rule:MF_01468};
GN Name=mrnC {ECO:0000256|HAMAP-Rule:MF_01468};
GN ORFNames=BN516_01035 {ECO:0000313|EMBL:CDA81005.1};
OS Firmicutes bacterium CAG:176.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263007 {ECO:0000313|EMBL:CDA81005.1, ECO:0000313|Proteomes:UP000017932};
RN [1] {ECO:0000313|EMBL:CDA81005.1, ECO:0000313|Proteomes:UP000017932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:176 {ECO:0000313|Proteomes:UP000017932};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01468}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01468};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01468}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01468}.
CC -!- SIMILARITY: Belongs to the MrnC RNase family. {ECO:0000256|HAMAP-
CC Rule:MF_01468}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDA81005.1}.
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DR EMBL; CBCO010000009; CDA81005.1; -; Genomic_DNA.
DR AlphaFoldDB; R6CZQ4; -.
DR Proteomes; UP000017932; Unassembled WGS sequence.
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; Ribonuclease III domain; 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 PANTHER; PTHR34276; MINI-RIBONUCLEASE 3; 1.
DR PANTHER; PTHR34276:SF1; MINI-RIBONUCLEASE 3; 1.
DR Pfam; PF00636; Ribonuclease_3; 1.
DR PIRSF; PIRSF005520; UCP005520; 1.
DR SUPFAM; SSF69065; RNase III domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01468};
KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_01468};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01468};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01468};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01468};
KW Reference proteome {ECO:0000313|Proteomes:UP000017932};
KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01468};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01468};
KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_01468};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01468}.
FT DOMAIN 5..102
FT /note="RNase III"
FT /evidence="ECO:0000259|Pfam:PF00636"
FT ACT_SITE 11
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01468"
SQ SEQUENCE 118 AA; 13070 MW; 5C55CE55110A3685 CRC64;
MSAIALAHMG DAVYETLVRT WLCVHGTATG KDLHRATIAL VCAPAQAEKM QKVLPLLTDE
EQAVYKRGRN ANVHTMSRSA TPAQYHSATG LECLMGYLYL KGDKNRAEEL FRAMMEET
//
