A0A8B6BFL6

UniProt ID: A0A8B6BFL6
Organism: Mytilus galloprovincialis
Review Status: DRAFT
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Gene Description

A0A8B6BFL6 (ORF name MGAL_10B073878) is an uncharacterized 612-amino-acid protein from Mytilus galloprovincialis (Mediterranean mussel) that contains a reverse transcriptase domain (Pfam RVT_1/PF00078) and an RNase H domain of the DIRS1 type (CDD cd09275, RNase_HI_RT_DIRS1). This domain architecture indicates the protein is encoded by a DIRS1-class retrotransposon rather than a LINE-type element. DIRS1 retrotransposons replicate via an RNA intermediate, generating a cDNA copy through reverse transcription, and integrate into the host genome using a tyrosine recombinase-mediated mechanism acting on circular DNA intermediates at inverted terminal repeats. The protein is classified in PANTHER family PTHR33050 (Hepadnavirus polymerase/reverse transcriptase), subfamily SF7 (Ribonuclease H), and carries InterPro signatures for the RT domain superfamily (IPR000477, IPR043502, IPR043128) and Hepadnavirus pol/RT (IPR052055). The M. galloprovincialis genome is repeat-rich (43% repeat content, 1.28 Gb assembly) with extensive transposable element diversity, and bivalve genomes collectively harbor tens of thousands of RT-containing LINE and DIRS-type elements. No direct experimental characterization exists for this protein; functional inferences are based entirely on domain architecture and comparative genomics of bivalve retrotransposons.

Core Functions

The primary enzymatic activity of this protein is RNA-directed DNA polymerase (reverse transcriptase) activity, catalyzing the synthesis of complementary DNA from an RNA template using deoxyribonucleotide triphosphates. This activity is central to the retrotransposon replication cycle, enabling copy-and-paste propagation of the encoding DIRS1-type mobile element. The RT domain contains a conserved D..DD catalytic triad essential for phosphodiester bond formation.

Supporting Evidence:
  • file:MYTGA/A0A8B6BFL6/A0A8B6BFL6-uniprot.txt
    RecName: Full=Reverse transcriptase domain-containing protein {ECO:0000259|Pfam:PF00078}
  • file:MYTGA/A0A8B6BFL6/A0A8B6BFL6-deep-research-falcon.md
    The most likely primary molecular function is RNA-dependent DNA polymerase activity: synthesis of complementary DNA (cDNA) from an RNA template during retrotransposition.
  • file:MYTGA/A0A8B6BFL6/A0A8B6BFL6-protnlm-predictions-review.yaml
    ProtNLM2 correctly predicted DNA recombination and DNA integration, consistent with the DIRS1 tyrosine recombinase-mediated integration mechanism.

References

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Suggested Questions for Experts

Q: Is this protein encoded by an intact, potentially active DIRS1 retrotransposon, or is the element a degraded/inactive genomic fossil?

Q: What is the precise DIRS1 family classification of this element based on phylogenetic analysis of the full-length ORF including the tyrosine recombinase domain?

Q: Is there evidence of recent retrotransposition activity for this element in the M. galloprovincialis population, such as polymorphic insertions?

Suggested Experiments

Experiment: Express and purify the RT domain to test for RNA-dependent DNA polymerase activity in vitro using standard primer extension assays.

Experiment: Perform RNA-seq across tissues and developmental stages to determine whether the encoding retrotransposon is transcriptionally active.

Experiment: Conduct phylogenetic analysis of the complete protein sequence against classified DIRS1 elements from bivalve and other metazoan genomes to determine precise family membership.

External Prediction Reviews

These computational predictions are reviewed separately from the GOA annotation set used for this review. The assessments below are from this project and do not constitute official GO annotations or endorsement by GO/UniProt. They are not included in the existing annotation review above.

ProtNLM2 External predictions

View prediction review YAML Β· A0A8B6BFL6-protnlm-predictions-review.yaml Β· Review status: COMPLETE

The reverse-transcriptase domain supports broad DNA interaction. Recombination and integration require evidence for the mobile element and this protein's role within it.

Source documents: genes/MYTGA/A0A8B6BFL6/A0A8B6BFL6-uniprot.txt Β· genes/MYTGA/A0A8B6BFL6/A0A8B6BFL6-goa.tsv Β· publications/PMID_32170321.md

Review score: 2 = concordant with evidence; 1 = uncertain; 0 = discordant with evidence. This is an assessment score, not a model probability.

GO:0003677 DNA binding GO_MF
COR β€” Correct novel prediction Review score: 2/2
Prediction method: ProtNLM2 Β· Version: UniProt 2024_06 pilot
Review rationale: The target contains a reverse-transcriptase domain at residues 174–349 and a DNA/RNA polymerase fold assignment. Reverse transcription entails interaction with a DNA primer or nascent DNA product, providing a mechanistic basis for broad DNA binding. This inference does not specify a recognition sequence, chromosomal target, or recombinase activity. The cached GOA/UniProt record has no DNA-binding annotation, so this is a supported additional function.
Supporting Evidence:
GO:0006310 DNA recombination GO_BP
UNC β€” Uncertain Review score: 1/2
Prediction method: ProtNLM2 Β· Version: UniProt 2024_06 pilot
Review rationale: The sequence supports a reverse-transcriptase relationship but has no identified recombinase domain or documented complete mobile-element context. Experimental DIRS retrotransposition work distinguishes cDNA production from completion of an element's integration cycle (PMID:32170321); it does not establish that this mussel protein belongs to that element class. An RT can participate in a larger recombination pathway, so lack of its own recombinase domain is not a decisive refutation of the biological process. The process is absent from the cached annotations and requires verified element context or functional evidence.
Supporting Evidence:
GO:0015074 DNA integration GO_BP
UNC β€” Uncertain Review score: 1/2
Prediction method: ProtNLM2 Β· Version: UniProt 2024_06 pilot
Review rationale: A reverse-transcriptase domain establishes a plausible role in cDNA synthesis, not necessarily chromosomal integration. DIRS experiments demonstrate that productive retrotransposition depends on the element and its proteins together (PMID:32170321), but the target's element identity and integration machinery are not established in the inspected sources. The prediction is a biological process, so a protein could contribute without catalyzing integration itself. DNA integration is absent from the cached annotations and remains uncertain pending element-context evidence.
Supporting Evidence:

Deep Research

Falcon

(A0A8B6BFL6-deep-research-falcon.md)

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πŸ“„ View Raw YAML

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