I checked for pre-existing SEC11-deep-research-*.md files in
genes/CANAL/SEC11 and none were present in this sparse worktree.
I attempted repository deep research with:
just deep-research CANAL SEC11 --provider perplexity
The wrapper found Q5A869 and launched the Perplexity provider, but no provider
API keys were configured:
ERROR - No research providers available. Please set API keys
No SEC11-deep-research-perplexity.md file was created.
SEC11 has a strong conserved-function case but little direct C. albicans
literature. The 2020 Candida secretory-pathway review summarizes the relevant
step as follows: "Following translocation into the ER, the N-terminal signal
peptide is cleaved by signal peptidase" and notes that "Spc3p, and Sec11p have
been identified as subunits in the signal peptidase complex", while adding that
SEC11's exact Candida function had not been characterized directly
PMID:32102426.
The primary Candida signal peptidase-complex paper is about SPC3, not SEC11.
It cloned CaSPC3, showed that it could rescue an S. cerevisiae spc3
phenotype, and found that conditional repression made CaSPC3 essential for
viability PMID:15300682. I therefore treated it as support for a conserved
Candida SPC, not as direct experimental evidence for Q5A869 catalytic activity.
The 2021 human cryo-EM paper resolved SEC11A- and SEC11C-containing SPC
paralogs and showed that the active site lies next to an ER-membrane window that
helps discriminate signal peptides by hydrophobic-region length
PMID:34388369. A 2026 S. cerevisiae paper then mapped the Sec11
C-terminal short helix and showed that it helps stabilize internal signal
sequences in the TM window PMID:42586426. These later papers are useful
mechanistic context for conserved Sec11 biology, but they do not change the
Candida-level annotation set.
PTHR10806-paint.tsv has only three IBD rows:
PTN000086749 at the family root for GO:0008233 peptidase activityPTN000086750 at taxon:2759 for GO:0005787 signal peptidase complexPTN000086750 at taxon:2759 for GO:0051604 protein maturationQ5A869 belongs to PTHR10806:SF6, the fungal
SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11 subfamily. The root
peptidase activity assertion is biologically right but deliberately generic,
so I refined the IBA and UniProt/InterPro peptidase rows to the already present
GO:0009003 signal peptidase activity term. The serine-type endopeptidase row
is retained because GO:0004252 and GO:0009003 are sibling terms that record
the catalytic mechanism and substrate class, respectively. I accepted the
eukaryotic PTN000086750 row for signal peptidase complex membership because
C. albicans SEC11 is inside that eukaryotic placement and there is no
Candida-specific loss evidence; its protein-maturation row is modified to
GO:0016485 protein processing, the live process term for SPC-catalyzed signal
peptide cleavage after obsoletion of GO:0006465 signal peptide processing.
The one biological-process row I removed is the EnsemblFungi transfer to
GO:0045047 protein targeting to ER. ER targeting is carried out by the signal
sequence, SRP/SRP receptor and the translocon; SEC11 acts afterward by cleaving
the signal peptide as the substrate enters the ER lumen. The old CGD ND row to
the biological_process root is no longer informative now that GOA has a
specific protein-maturation row.