Q8IJK4 · MNMA_PLAF7

Function

function

Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s2U34 (By similarity).
Required for apicoplast maintenance (PubMed:37166116).

Features

Showing features for active site.

110841002003004005006007008009001,000
TypeIDPosition(s)Description
Active site538Nucleophile
Active site715Cysteine persulfide intermediate

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
Cellular Componentapicoplast
Cellular Componentmembrane
Molecular FunctionATP binding
Molecular FunctiontRNA (5-methylaminomethyl-2-thiouridylate)(34)-methyltransferase activity
Molecular FunctiontRNA binding
Biological ProcesstRNA processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Putative tRNA-specific 2-thiouridylase
  • EC number
  • Short names
    PfMnmA

Gene names

    • Name
      MNMA
    • ORF names
      PF3D7_1019800

Organism names

  • Taxonomic identifier
  • Strain
    • 3D7
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)

Accessions

  • Primary accession
    Q8IJK4

Proteomes

Organism-specific databases

Subcellular Location

Plastid, apicoplast
Membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane1-21Helical
Transmembrane32-52Helical
Transmembrane309-329Helical

Keywords

Phenotypes & Variants

Disruption phenotype

Parasites require exogenously provided mevalonate for survival (PubMed:37166116).
Apicoplast structure is disrupted (PubMed:37166116).

PTM/Processing

Features

Showing features for chain, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00004595871-1084Putative tRNA-specific 2-thiouridylase
Disulfide bond538↔715Alternate

Keywords

Proteomic databases

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the MnmA/TRMU family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,084
  • Mass (Da)
    130,518
  • Last updated
    2009-09-22 v2
  • Checksum
    DC871042759669AF
MLIFFFFFFFFKYIYNIFILTCFYITLSSYYFIISFIFSTLMFFYFCTFYVISLFFLYISSFCKSIKVTQLYDKKIKIKSFINNYLVSCRKKKYIYNNVDDKSNIGTFNLYHNIRDNNNNNNNNDNNNNLKKRDDVLFPLCNKNIINDVQKIYDEVNNIKDKEQKINYLMEQCSSLCKENYFPPILNLNKAYRNKRIDEFNKGNKNFYINEVGKNIWYKYVNRCDEILFMAIDIQIDEDEQRNNSIKDVHDVHDDNIKTCTLIKDDKHFEKYKDIHNDNILKNILPLDKKIDSIKNMLNHKYMKKKKCIITIDAYSNNLILYCFLYLILKHINKMYLYSFMNIQIKEITAKLKELFDLHFNVHHIIDYIHEYIYNFLMSYHIKRKKNKSKNMKEKDIKNVFANNIIISDEENKHISKESSDMYKKKTTITTTTTTKKKKNTMKLFTYPRIAHMLSGGVDSLMALHLLERKKFYVDNYFFNFTNADCSKNDIKYVKDICKNNKRNLFIININDEYFDEVLVPMLFFYADGKVPNPDIMCNQKIKYNFFLKVIKSIYKQKWNYRTKSKLCNYDFISTGHYAMIRTNDKNNPNNIFNNNLFIKKKKKKIKNIKNKKNIKNKNNIKNKNNNNNIYTYNIYNLHNDNIKTNYKKNNKYFYKLLVSNDKKKDQTFFLSSFNHIQLSKFIFPLSLYTKKDVKKYMNENNINNYNHKETKGLCLFGNIDMQTLLHKYFVNTEKDDIKNKQNEDNIFKENNILNLNNNFNQNEKKKKKEKKLLVDITTTSSHLKKFRETFIPKMNLHYKNYLINLDDQTILDINSDIHLYAIGQHKNVTNYLHNLYNKKMININGYKKKHVKNVISSFQWIVVYKKIKRDMSTNLIHNFIYLTKNYDQDLFTHIRTKCKLHNIKWIEGKLPACIKKQFKKYNKINKKKKKINNNNNKYKTNETFHVYNNIQESGKKKKKKKVKNIPHDEKTIFVKIRNSEQIKKAKIKFSLSNNTAYLKVKQKDTGFSPGQIITLYFPFIIKKNNKVTYITNLNKYNNLINTNKNTIYYHCLGSATISNQFLDYNLYQHIKNIHQINDLNMSK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LN999944
EMBL· GenBank· DDBJ
CZT98453.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp