ACL_RS00080


  Uniprot: A9NE78
Description: ribonuclease M5
EC number: 3.1.26.8
Annotation score: 2 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 21 and 42 nucleotides, respectively, from the 5'- and 3'-termini of a 5S-rRNA precursor. {ECO:0000256|HAMAP-Rule:MF_01469}.
Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_01469}; ; Note=Binds two Mg(2+) per subunit. {ECO:0000256|HAMAP-Rule:MF_01469}
Enzyme regulation: 
Function [CC]: FUNCTION: Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step. {ECO:0000256|HAMAP-Rule:MF_01469}.
Pathway: 
Active site: 
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: METAL 9 9 Magnesium 1; catalytic. {ECO:0000256|HAMAP-Rule:MF_01469}.; METAL 56 56 Magnesium 1; catalytic. {ECO:0000256|HAMAP-Rule:MF_01469}.; METAL 56 56 Magnesium 2. {ECO:0000256|HAMAP-Rule:MF_01469}.; METAL 58 58 Magnesium 2. {ECO:0000256|HAMAP-Rule:MF_01469}.
Nucleotide binding: 
Site: 
Gene names (primary): rnmV
Gene names (synonym): 
Mass: 20,599
Subunit structure [CC]: 
Gene ontology (GO): cytoplasm [GO:0005737]; magnesium ion binding [GO:0000287]; ribonuclease M5 activity [GO:0043822]; rRNA binding [GO:0019843]; rRNA processing [GO:0006364]
Gene ontology IDs: GO:0000287; GO:0005737; GO:0006364; GO:0019843; GO:0043822
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the ribonuclease M5 family. {ECO:0000256|HAMAP-Rule:MF_01469}.; SIMILARITY: Contains 1 Toprim domain. {ECO:0000256|HAMAP-Rule:MF_01469}.
Protein families: Ribonuclease M5 family
Coiled coil: 
Domain [FT]: DOMAIN 3 77 Toprim. {ECO:0000259|SMART:SM00493}.
Motif: 
Region: 
EMBL: CP000896
ProteinModelPortal: A9NE78
MEROPS: 
EnsemblBacteria KO: ABX80658
UniPathway: K05985
CDD: 
Gene3D: 
HAMAP: 
InterPro: MF_01469
PANTHER: IPR004466;IPR025156;IPR006171
PIRSF: 
PRINTS: 
PROSITE: 
Pfam: 
ProDom: PF13331
SMART: 
SUPFAM: SM00493
TIGRFAMs: 
18965-19505(+)

>nucleotide sequence
ATGAAACAAAAAATATATGTTGTTGAAGGCACACACGATGAAACGCTACTTAAACAAATA
GATCCAAATATTAGAACTGTTTCTGTTGGGGGATCACAAATCAAAGAAGATGTGATTCAG
TTTTTAAAAACCTATGAAGATAAATTTCAAATCATACTTTTATTAGATCCTGATTATACG
GGTGAACAAATAAGAAAAAGGATTGCTAAACATTTAACAAATCCTACACATATCTTTGTT
CAAAAACATAAAGCGATTAGTAAAAATAAAAAGAAGATAGGTGTTGAACACCTATCCTTA
GAAGATTTAAAGACCATGCTTCTCCATGAGGTACAAGAACTACCTAAAGTAGAGTCTATT
ACATTAGATAGTTTATATAAATTGGGACTTAGCGGTCAAACAGACTCTAAAGCCAAAAGA
GACTACTTAACCAGCAAATTAAACCTAACCTATAGTAACTCCAAGACACTGATACAAAGG
CTTAATTGGCTAGGGTTAAGTTATAAAGATTTAGAGGATATATTATATGCATCAAGCTAA


>protein sequence
MKQKIYVVEGTHDETLLKQIDPNIRTVSVGGSQIKEDVIQFLKTYEDKFQIILLLDPDYT
GEQIRKRIAKHLTNPTHIFVQKHKAISKNKKKIGVEHLSLEDLKTMLLHEVQELPKVESI
TLDSLYKLGLSGQTDSKAKRDYLTSKLNLTYSNSKTLIQRLNWLGLSYKDLEDILYASS






















© Fisunov Lab of Proteomics, 2016.