RNM5_MYCPN
ID RNM5_MYCPN Reviewed; 178 AA.
AC P75045;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Ribonuclease M5 {ECO:0000255|HAMAP-Rule:MF_01469};
DE EC=3.1.26.8 {ECO:0000255|HAMAP-Rule:MF_01469};
DE AltName: Full=RNase M5 {ECO:0000255|HAMAP-Rule:MF_01469};
DE AltName: Full=Ribosomal RNA terminal maturase M5 {ECO:0000255|HAMAP-Rule:MF_01469};
GN Name=rnmV {ECO:0000255|HAMAP-Rule:MF_01469}; OrderedLocusNames=MPN_072;
GN ORFNames=D09_orf178, MP083;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
CC -!- FUNCTION: Required for correct processing of both the 5' and 3' ends of
CC 5S rRNA precursor. Cleaves both sides of a double-stranded region
CC yielding mature 5S rRNA in one step. {ECO:0000255|HAMAP-Rule:MF_01469}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 21 and 42
CC nucleotides, respectively, from the 5'- and 3'-termini of a 5S-rRNA
CC precursor.; EC=3.1.26.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01469};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01469};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_01469};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01469}.
CC -!- SIMILARITY: Belongs to the ribonuclease M5 family. {ECO:0000255|HAMAP-
CC Rule:MF_01469}.
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DR EMBL; U00089; AAB95731.1; -; Genomic_DNA.
DR PIR; S73409; S73409.
DR RefSeq; NP_109760.1; NC_000912.1.
DR RefSeq; WP_010874429.1; NC_000912.1.
DR AlphaFoldDB; P75045; -.
DR SMR; P75045; -.
DR IntAct; P75045; 3.
DR STRING; 272634.MPN_072; -.
DR PRIDE; P75045; -.
DR EnsemblBacteria; AAB95731; AAB95731; MPN_072.
DR GeneID; 66609286; -.
DR KEGG; mpn:MPN_072; -.
DR PATRIC; fig|272634.6.peg.73; -.
DR HOGENOM; CLU_109405_1_0_14; -.
DR OMA; RLQMFQI; -.
DR BioCyc; MPNE272634:G1GJ3-110-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043822; F:ribonuclease M5 activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR CDD; cd01027; TOPRIM_RNase_M5_like; 1.
DR HAMAP; MF_01469; RNase_M5; 1.
DR InterPro; IPR004466; RNase_M5.
DR InterPro; IPR025156; RNase_M5_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034141; TOPRIM_RNase_M5-like.
DR Pfam; PF13331; DUF4093; 1.
DR Pfam; PF01751; Toprim; 1.
DR SMART; SM00493; TOPRIM; 1.
DR TIGRFAMs; TIGR00334; 5S_RNA_mat_M5; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing;
KW rRNA-binding.
FT CHAIN 1..178
FT /note="Ribonuclease M5"
FT /id="PRO_0000210402"
FT DOMAIN 10..103
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 16
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
FT BINDING 64
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01469"
SQ SEQUENCE 178 AA; 20412 MW; 50A5129B163B86D6 CRC64;
MDKKTRLKLD GVIVCEGKTD QARLQQLFDV SVITTNGSAL NQRTINLIKA VAKKQPVILF
LDPDVAGQKI RRQLEQHLDK YESCFIARKD MKPNSTKIGV AEATDAALIQ ALQQRQVFTK
TTQPTLSWEQ YLELNLNSKS KRLALCNKLH LSYFNHKQLF RKLNLLQLTF DQVCQLLK
