A0A2G6LB29 · A0A2G6LB29_9GAMM

Function

function

Endoribonuclease that plays a central role in RNA processing and decay. Required for the maturation of 5S and 16S rRNAs and the majority of tRNAs. Also involved in the degradation of most mRNAs.
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per homotetramer.

Pathway

Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site304Mg2+ (UniProtKB | ChEBI); catalytic
Binding site347Mg2+ (UniProtKB | ChEBI); catalytic
Binding site405Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners
Binding site408Zn2+ (UniProtKB | ChEBI); ligand shared between dimeric partners
Active site957Schiff-base intermediate with substrate

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytoplasmic side of plasma membrane
Molecular Functionmagnesium ion binding
Molecular Functionribonuclease E activity
Molecular FunctionRNA endonuclease activity
Molecular FunctionrRNA binding
Molecular Functiontransaldolase activity
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processcarbohydrate metabolic process
Biological ProcessmRNA catabolic process
Biological Processpentose-phosphate shunt
Biological ProcessrRNA processing
Biological ProcesstRNA processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Ribonuclease E
  • EC number
  • Short names
    RNase E
  • Recommended name
    Transaldolase
  • EC number

Gene names

    • Name
      tal
    • Synonyms
      rne
    • ORF names
      CSA45_04090

Organism names

Accessions

  • Primary accession
    A0A2G6LB29

Proteomes

Subcellular Location

Cytoplasm
Cell inner membrane
; Peripheral membrane protein

Keywords

Interaction

Subunit

Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Within the RNA degradosome, RNase E assembles into a homotetramer formed by a dimer of dimers.

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain39-121S1 motif
Region405-408Required for zinc-mediated homotetramerization and catalytic activity
Region568-761Disordered
Compositional bias571-599Basic and acidic residues
Compositional bias608-652Basic and acidic residues
Compositional bias654-669Polar residues
Compositional bias670-707Basic and acidic residues
Compositional bias740-761Basic and acidic residues

Sequence similarities

Belongs to the RNase E/G family. RNase E subfamily.
Belongs to the RNase E/G family. RNase G subfamily.
Belongs to the transaldolase family. Type 2 subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,182
  • Mass (Da)
    132,053
  • Last updated
    2018-01-31 v1
  • Checksum
    2F26D02E3AFAF374
MKRMLINATQREELRVALVDGQRLYDLDIEPINSKQKKANIYKGKITRVEPSLEAAFVDYGADRHGFLPIKEISKDYFSGSTAVGKNGRPDYKKLIREGQAVMVQVEKEERGNKGAALTTYIGLAGRYLVAMPNNPRGGGVSRRVQGTERRELRKALDEVSVPENVGVIVRTAGVGRNYEELQWDLDYQMQVWRAIVDAYEQAEVGSLLYQESNIIVRALRDYFRDDIAQIIIDDESVYRRAHGFMSLVMPDKLKRLQLYKDELPLFTRYQIEAQIDSAYGRSVRLPSGGELVIDYTEAMVSIDINSSRSTKGGDVEETALHTNLEAAEEIARQLRLRDIGGLIVVDFIDMYEAKHRRQVEEKIKESIRIDRARVQLARISKFGLLEMSRQRLRPSIDEASHSVCPRCKGQGSIRSIQSVALSVLRLIEEDANKDMTTKVIVQLPISVATFLLNEKRQAITDIEKNNQVSVLILANDTLETPNYDIQRVRHDNESFDGLSSYNMLRDFKASEEVEEQTSAPGGEVEVRQEAMVADISPSAPPPKPKAGFFKLIKRVLGIGDESLSLSTKKMKTAKTEDDAGKKADKADKEKYSRGEGHKKNGQRNRKKERPSGKNNKVSDGRKNTNKTIDKKTGKTTSNKKPPTEKQVKKTGSRNGHGKSGQSNQPVERTNKVDKADKTNKADKKVAKPFVNPYAKDKEKIRQGRPVSEDAIRGAGKADFAKQPDKASAQQVESTQENQKTKRPTTKDEGRKKAKKNYPDKGRVYVPRAVGDAVPALRMNDNLGIEESKTKVTKTEATRTVRPDNAEKSSADGVNNANNPIADLSAFGQSVWYDNISRDMIESGKLQRLIDEDDLRGITSNPAIFEKALASNHPGYLDYLKTLKGRVETPKEAFFALAIRDIVEACQAMRPVYDNSNGSDGMVSLEVSPDLAYDAEKTIDEALTLHQKLNQPNAMIKVPGTAQGLLAIEQLTYLGLNINVTLLFSIERYVEVFKAYMRGLQKRVDMALPVDKIRSVASFFISRIDSAADKVLENTNPEMKGKVAIANARLAYDAYLQLLDSEAWKQLEKAGAKPQRLLWASTSTKDPGYSDVLYMESLIGKDTVNTVPPVTYEAFKDHGKIAETITLDIPEAKALIELLPQYGVDLDLMTQTLERDGVIAFEKSFETLLAVLAEKMSSIESE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias571-599Basic and acidic residues
Compositional bias608-652Basic and acidic residues
Compositional bias654-669Polar residues
Compositional bias670-707Basic and acidic residues
Compositional bias740-761Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PDST01000039
EMBL· GenBank· DDBJ
PIE45087.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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