F5RL11 · F5RL11_9FIRM

Function

Caution

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

Features

Showing features for active site.

112631002003004005006007008009001,0001,1001,200
TypeIDPosition(s)Description
Active site1103Nucleophile
Active site1233
Active site1235

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionmetal ion binding
Molecular Functionphosphoribosylformylglycinamidine synthase activity
Biological Processglutamine metabolic process
Biological Processpurine nucleotide biosynthetic process

Keywords

Names & Taxonomy

Protein names

  • Submitted names
    • Phosphoribosylformylglycinamidine synthase II
      (EC:6.3.5.3
      )

Gene names

    • Name
      purL
    • ORF names
      HMPREF9081_0946

Organism names

Accessions

  • Primary accession
    F5RL11

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain181-229Phosphoribosylformylglycinamidine synthase linker
Domain443-594PurM-like C-terminal
Region458-487Disordered
Compositional bias461-483Polar residues

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,263
  • Mass (Da)
    138,179
  • Last updated
    2011-07-27 v1
  • Checksum
    C4D52D5DA7E1224B
MAVKRIFVEKRQGFFDIPAQRLCSDLVETFRLTELRAVRIITRYDIEGLSDEEFARVRNIVFADPPVDTVYEDALPVFPDAHIFAIEPLPGQFDPTAAAAAECVQLVTQGERPDVRTARVIALIGKVETRVYEQIKAYLINTVESREASLAIPATLESRVAMPTDVEVLAQFNGFSRVELERFHAAHGFAMSEEDLEFVQQYFRDTEHRAPTITELRVIDTYWSDHCRHTTFTTAIDSVNIENGFFSMPIIESYQRYMDDRKVLYQGGKQRDMTLMDIAVIGMKALRAEGKLDDLDASEEINACSIRITVDVNGKDEDWLLMFKNETHNHPTEIEPFGGAATCLGGAIRDPLSGRSYVYQAMRVTGAFDPRVPIEDTLPGKLPQKKITLGAAEGYSSYGNQIGLATGQVHEIYHKGYLAKRMEIGAVIGAAPAAQVVRKRPVPGDVIVLLGGRTGRDGIGGATGSSKQHTESSLTTSGAEVQKGNPPTERKIQRLFRNPEVSCMIKRCNDFGAGGVAVAIGELADGLTINLDAVPKKYEGLDGTELAISESQERMAVVLAPKDVPAFLRHADAENLEATEVAVVTAEPHLVMKWRGQTIVHIARAFLATNGVRQHVRVIVDPPNERAPYLQQVPPAVKQVGRDLEDMWLTNLRDLNVCSQKGLGERFDSTFGAASVLMPFGGKYQLTPSEAMVAKIPVRHGQTNTASAMAFGFDPDLSTWSPFHGAVYAIVEAVAKIVAVGGEASKVRLTLQEYFERLGTESKKWGKPFAALLGALRAQHEMGIPAIGGKDSMSGTFENLNVPPTLVAFAVAVMHANEALSPEFKYPGNKVIMVPVPRDAQDLPVFSRLNTNFKKIHELIVEKKVFSAMSVGRGGIAATISKMCLGNNLGFKFTSFIQQDDLFKPLYGTMLLEVAPSFDTTANLVGTGAIEIGKTRDVPSIITDLDTIVLADVKDAYTEPLEKIFPTMIPQVVRQIDRPTYAPYTKGKIVGSSVKIAKPRVCIPVFPGTNCEYDSARAWERVGAIPEIFVVRNLTPKAVEETVSELAAALARSQILMLPGGFSGGDEPDGTGKFIAAMFRAPALTEAVQRLLRDQDGLILGICNGFQALLKLGLLPYGKITDLDENSPTLTYNNIGRHVSQTVRVRVASNLSPWLSGVSVGDTHTIAVSHGEGRFYTDAKTVANMRIRGQIATQYVNDKGEPTLEQPYNPNGSVNAIEGITSPDGRIYGRMAHAERIGTDICKNVPGEMNQMIFESGVSYFIR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias461-483Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AFHQ01000028
EMBL· GenBank· DDBJ
EGK60740.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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