sec11

Summary: InterPro identifies Sec11 as a signal peptidase I/S26 serine-protease catalytic subunit, so the serine-type endopeptidase mapping is sound.

Reason: GO:0004252 records the conserved serine-protease chemistry of fungal Sec11, and A. fumigatus AfSec1/sec11 has target-specific support for signal peptidase activity on Gel1. The serine-endopeptidase and signal peptidase rows are therefore complementary rather than redundant.

Summary: The ER localization transferred from Saccharomyces cerevisiae Sec11 is consistent with fungal Sec11 acting in the ER membrane signal peptidase complex.

Reason: Sec11 is an ER signal peptidase complex subunit. Although ER membrane is more precise, the broader endoplasmic reticulum term remains biologically correct and informative as a compartment-level localization for this eukaryotic signal peptidase.

Summary: PAINT places signal peptidase complex membership at the eukaryotic PTN000086750 node, and A. fumigatus Sec11 sits in the fungal Sec11 subfamily that inherited this complex role.

Reason: PTN000086750 is scoped to Eukaryota for signal peptidase complex membership, matching the conserved ER signal peptidase complex in which Sec11 supplies the catalytic subunit. No A. fumigatus-specific loss or divergence is evident.

Summary: Transfer of signal peptidase complex membership from budding-yeast Sec11 is exact for the conserved fungal catalytic subunit.

Reason: A. fumigatus Sec11 and S. cerevisiae Sec11 are fungal members of PANTHER subfamily PTHR10806:SF6, and Sec11 is expected to be the catalytic subunit of the ER signal peptidase complex in both species.

Summary: UniProtKB-SubCell maps the curated endoplasmic-reticulum membrane localization of Sec11 to the correct GO cellular component.

Reason: The ER membrane is the expected site of the signal peptidase complex that cleaves signal peptides from proteins entering the secretory pathway, and is the precise membrane location for Sec11.

Summary: Manual similarity transfer from S. cerevisiae Sec11 supports ER membrane localization for A. fumigatus Sec11.

Reason: The fungal Sec11 orthologs are conserved ER membrane catalytic subunits of the signal peptidase complex; transferring ER membrane localization from the characterized S. cerevisiae protein is therefore appropriate.

Summary: The root PAINT node supports inherited peptidase activity, but the exact activity of A. fumigatus Sec11 is signal peptidase activity.

Reason: PTN000086749 places generic peptidase activity at the PTHR10806 root. This is true for A. fumigatus Sec11, but accepted GO:0009003 rows and the Gel1 processing experiment identify the precise Sec11 activity as signal peptidase activity.

Summary: UniProt's combined electronic peptidase call is true but generic relative to the accepted signal peptidase activity rows.

Reason: A. fumigatus Sec11 is a peptidase, but it is specifically an ER signal peptidase catalytic subunit. Retaining generic peptidase activity would duplicate the accepted signal peptidase activity annotation at lower specificity.

Summary: The EC/ARBA electronic annotation matches Sec11's experimentally supported signal peptidase activity.

Reason: AfSec1/sec11 promoter depletion caused accumulation of nonprocessed Gel1, while mature Gel1 was restored in wild-type and promoter-complemented strains, directly supporting signal peptide cleavage by A. fumigatus Sec11.

Summary: Manual similarity transfer from S. cerevisiae Sec11 is supported by conserved fungal Sec11 membership and target-specific A. fumigatus Gel1 processing data.

Reason: S. cerevisiae and A. fumigatus Sec11 are fungal PTHR10806:SF6 signal peptidase catalytic subunits, and the direct A. fumigatus promoter-deletion experiment confirms signal peptidase activity on Gel1.

Summary: Sec11 is membrane-associated, but endoplasmic reticulum membrane is the more specific accepted localization.

Reason: The InterPro membrane inference is correct for a type II ER membrane signal peptidase catalytic subunit, but accepted GO:0005789 rows already capture the specific membrane where Sec11 functions.

Summary: Protein targeting to ER is an upstream signal-recognition and targeting process, not the proteolytic signal-peptide removal catalyzed by Sec11.

Reason: Sec11 executes the post-targeting signal peptide cleavage step within the ER signal peptidase complex. Its substrate signal peptides direct precursors to the ER; Sec11 removes those peptides after targeting and translocation, so the EnsemblFungi transfer overstates Sec11's role.

Summary: PTN000086750 correctly places eukaryotic Sec11 signal-peptide cleavage in protein maturation, but the row can be refined to protein processing.

Reason: Signal peptide cleavage converts a secretory precursor into a mature protein, so the eukaryotic PTN000086750 IBD to GO:0051604 protein maturation captures the conserved Sec11 biological process at the right scope for A. fumigatus. GO:0016485 protein processing is the live process term for the proteolytic SPC reaction.

Proposed replacements: protein processing

Summary: UniProt's combined electronic protein-maturation annotation matches Sec11's role in signal peptide cleavage but is too broad for the specific proteolytic processing reaction.

Reason: Sec11 promotes maturation of secretory precursors by cleaving their N-terminal signal peptides, the same conserved function captured by the PAINT Eukaryota node. GO:0016485 protein processing is the live process term for the signal-peptide proteolysis carried out by Sec11.

Proposed replacements: protein processing