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Database: UniProt
Entry: A9NE78_ACHLI
LinkDB: A9NE78_ACHLI
Original site: A9NE78_ACHLI 
ID   A9NE78_ACHLI            Unreviewed;       179 AA.
AC   A9NE78;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Ribonuclease M5 {ECO:0000256|HAMAP-Rule:MF_01469};
DE            EC=3.1.26.8 {ECO:0000256|HAMAP-Rule:MF_01469};
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; 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}.
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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; 66294179; -.
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: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   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_domain.
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
//
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