ID A9NE78_ACHLI Unreviewed; 179 AA. AC A9NE78; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 02-SEP-2026, entry version 93. DE RecName: Full=Ribonuclease M5 {ECO:0000256|HAMAP-Rule:MF_01469, ECO:0000256|NCBIfam:TIGR00334}; DE EC=3.1.26.8 {ECO:0000256|HAMAP-Rule:MF_01469, ECO:0000256|NCBIfam:TIGR00334}; DE AltName: Full=RNase M5 {ECO:0000256|HAMAP-Rule:MF_01469}; DE AltName: Full=Ribosomal RNA terminal maturase M5 {ECO:0000256|HAMAP-Rule:MF_01469}; GN Name=rnmV {ECO:0000256|HAMAP-Rule:MF_01469}; GN OrderedLocusNames=ACL_0015 {ECO:0000313|EMBL:ABX80658.1}; OS Acholeplasma laidlawii (strain PG-8A). OC Bacteria; Bacillati; Mycoplasmatota; Mollicutes; Acholeplasmatales; OC Acholeplasmataceae; Acholeplasma. OX NCBI_TaxID=441768 {ECO:0000313|EMBL:ABX80658.1, ECO:0000313|Proteomes:UP000008558}; RN [1] {ECO:0000313|EMBL:ABX80658.1, ECO:0000313|Proteomes:UP000008558} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PG-8A {ECO:0000313|EMBL:ABX80658.1, RC ECO:0000313|Proteomes:UP000008558}; RX PubMed=21784942; DOI=10.1128/JB.05059-11; RA Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A., RA Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D., RA Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A., RA Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G., RA Ladygina V.G., Govorun V.M.; RT "Complete genome and proteome of Acholeplasma laidlawii."; RL J. Bacteriol. 193:4943-4953(2011). 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:0000256|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:0000256|HAMAP-Rule:MF_01469}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01469}. CC -!- SIMILARITY: Belongs to the ribonuclease M5 family. {ECO:0000256|HAMAP- CC Rule:MF_01469}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000896; ABX80658.1; -; Genomic_DNA. DR RefSeq; WP_012241989.1; NC_010163.1. DR AlphaFoldDB; A9NE78; -. DR STRING; 441768.ACL_0015; -. DR GeneID; 41338219; -. DR KEGG; acl:ACL_0015; -. DR eggNOG; COG1658; Bacteria. DR HOGENOM; CLU_109405_0_0_14; -. DR OrthoDB; 9791329at2; -. DR Proteomes; UP000008558; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043822; F:ribonuclease M5 activity; IEA:UniProtKB-UniRule. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.1360.10; -; 1. DR HAMAP; MF_01469; RNase_M5; 1. DR InterPro; IPR004466; RNase_M5. DR InterPro; IPR025156; RNase_M5_C. DR InterPro; IPR006171; TOPRIM_dom. DR NCBIfam; TIGR00334; 5S_RNA_mat_M5; 1. DR PANTHER; PTHR39156; RIBONUCLEASE M5; 1. DR PANTHER; PTHR39156:SF1; RIBONUCLEASE M5; 1. DR Pfam; PF13331; DUF4093; 1. DR Pfam; PF01751; Toprim; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF110455; Toprim domain; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01469}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP- KW Rule:MF_01469}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01469}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01469}; KW Reference proteome {ECO:0000313|Proteomes:UP000008558}; KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP- KW Rule:MF_01469}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_01469}; KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP- KW Rule:MF_01469}; KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP- KW Rule:MF_01469}. FT DOMAIN 3..77 FT /note="Toprim" FT /evidence="ECO:0000259|SMART:SM00493" SQ SEQUENCE 179 AA; 20599 MW; D42A17D43ADC34B7 CRC64; MKQKIYVVEG THDETLLKQI DPNIRTVSVG GSQIKEDVIQ FLKTYEDKFQ IILLLDPDYT GEQIRKRIAK HLTNPTHIFV QKHKAISKNK KKIGVEHLSL EDLKTMLLHE VQELPKVESI TLDSLYKLGL SGQTDSKAKR DYLTSKLNLT YSNSKTLIQR LNWLGLSYKD LEDILYASS //