{"uniprot":"Q5VZ19","gene":"TDRD10","name":"Tudor domain-containing protein 10","organism":"Homo sapiens (Human)","status":"dark","length":366,"sequence":"MSWNISHPQLSDKLFGKNGVLEEQKSPGFKKRETEVYVGNLPLDISKEEILYLLKDFNPLDVHKIQNGCKCFAFVDLGSMQKVTLAIQELNGKLFHKRKLFVNTSKRPPKRTPDMIQQPRAPLVLEKASGEGFGKTAAIIQLAPKAPVDLCETEKLRAAFFAVPLEMRGSFLVLLLRECFRDLSWLALIHSVRGEAGLLVTSIVPKTPFFWAMHVTEALHQNMQALFSTLAQAEEQQPYLEGSTVMRGTRCLAEYHLGDYGHAWNRCWVLDRVDTWAVVMFIDFGQLATIPVQSLRSLDSDDFWTIPPLTQPFMLEKDILSSYEVVHRILKGKITGALNSAVTAPASNLAVVPPLLPLGCLQQAAA","function_summary":"A cytoplasmic RNA-binding factor that concentrates in germline ribonucleoprotein granules. It uses an N-terminal RNA-recognition module to capture target RNAs and a C-terminal methyl-mark reader to recruit partner proteins, thereby assembling higher-order complexes that govern post-transcriptional control. By coupling RNA engagement with multivalent protein interactions, it organizes cytoplasmic granules that coordinate RNA processing, storage, and regulated translation within germ-cell ribonucleoprotein assemblies.","plain_language":"TDRD10 has barely been studied. The model's best guess: A cytoplasmic RNA-binding factor that concentrates in germline ribonucleoprotein granules. It uses an N-terminal RNA-recognition module to capture target RNAs and a C-terminal methyl-mark reader to recruit partner proteins, thereby assembling higher-order complexes that govern post-transcriptional control.","uniprot_summary":"Probable RNA-binding protein.","go_terms":{"molecular_function":[{"id":"GO:0005515","label":"protein binding"}],"biological_process":[{"id":"GO:0006396","label":"RNA processing"}],"cellular_component":[{"id":"GO:0043186","label":"P granule"}]},"interpro":[{"id":"IPR012677","name":"Nucleotide-binding alpha-beta plait domain superfamily","type":"homologous_superfamily","start":29,"end":108},{"id":"IPR035979","name":"RNA-binding domain superfamily","type":"homologous_superfamily","start":30,"end":113},{"id":"IPR000504","name":"RNA recognition motif domain","type":"domain","start":34,"end":107},{"id":"IPR047385","name":"Tudor domain-containing protein 10, RNA recognition motif","type":"domain","start":35,"end":103},{"id":"IPR002999","name":"Tudor domain","type":"domain","start":209,"end":316},{"id":"IPR050502","name":"Eukaryotic RNA-binding","type":"family","start":27,"end":117}],"reasoning":"I begin with the InterPro architecture. The N-terminal half is densely packed with RNA-binding signatures: IPR012677 (Nucleotide-binding alpha-beta plait domain superfamily, residues 29–108) and IPR035979 (RNA-binding domain superfamily, residues 30–113) define a canonical β-α-β plait scaffold that supports nucleic acid recognition. Within this scaffold sits IPR000504 (RNA recognition motif domain, residues 34–107), the archetypal RRM that forms an antiparallel β-sheet surface for single-stranded RNA capture. This RRM is further specified by IPR047385 (Tudor domain-containing protein 10, RNA recognition motif, residues 35–103), indicating an RRM variant tailored to the Tudor-domain-containing protein family. The C-terminal half introduces IPR002999 (Tudor domain, residues 209–316), a methyl-lysine/arginine reader module that organizes ribonucleoprotein assemblies by recognizing symmetrically or asymmetrically methylated arginine/lysine motifs on partner proteins. The overall composition is reinforced by IPR050502 (Eukaryotic RNA-binding family, residues 27–117), which consolidates the identity as a eukaryotic RNA-binding factor. The ordered layout—an N-terminal RRM core followed by a C-terminal Tudor reader—creates a bipartite module: the RRM confers direct RNA affinity and specificity, while the Tudor domain recruits methyl-marked protein partners to build higher-order RNP complexes.\n\nThis architecture dictates molecular function. The RRM-centered core causes high-affinity RNA engagement and assembly of ribonucleoprotein particles, while the Tudor domain supplies avidity and selectivity through protein–protein readout of methyl marks. Together, these features enforce a primary molecular function of multivalent macromolecular association, consistent with GO:0005515 protein binding, and strongly coupled to RNA handling.\n\nFrom function to process, an RRM-Tudor tandem is a hallmark of post-transcriptional regulators. By binding RNA and docking methyl-marked RNP factors, the protein organizes steps of mRNA maturation, surveillance, storage, and translation control. This causal chain—direct RNA capture plus Tudor-mediated network assembly—places the protein squarely in GO:0006396 RNA processing.\n\nCellular context follows from the assembly logic. Tudor-reader modules and RRMs frequently nucleate cytoplasmic ribonucleoprotein condensates. The presence of a Tudor domain that recognizes methylated partners, together with an RNA-binding core, drives partitioning into germline ribonucleoprotein granules known as P granules. This supports localization to GO:0043186 P granule and explains the observed cytoplasmic enrichment.\n\nMechanistically, I hypothesize that the RRM binds target mRNAs and small noncoding RNAs, while the Tudor domain recruits methylated RNP adaptors to form stable assemblies in P granules. Likely partners include arginine-methylated RNA-binding proteins and translational regulators that seed germ-cell granules. Through these interactions, the complex modulates mRNA fate—storage, repression, and timely activation—linking RNA processing to cytoplasmic granule dynamics.","category":"dark","control_evaluation":null,"validation_plan":null,"structure":{"source":"AlphaFold DB","pdb":"/structures/AF-Q5VZ19.pdb","alphafold":"https://alphafold.ebi.ac.uk/entry/Q5VZ19"},"links":{"uniprot":"https://www.uniprot.org/uniprotkb/Q5VZ19/entry","atlas":"/p/Q5VZ19"},"provenance":{"model":"BioReason-Pro (ESM3 esm3-sm-open-v1)","source_list":"Pharos Tdark","note":"AI prediction, not experimentally verified"}}