Gene Ontology annotation through association of InterPro records with GO terms

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000044

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

GO_REF:0000107

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

file:NEUCR/sec11/sec11-uniprot.txt

UniProtKB Q7RY44 signal peptidase complex catalytic subunit sec11 record

UniProtKB classifies Q7RY44 as a 172-residue reviewed fungal Sec11 signal peptidase complex catalytic subunit with one N-terminal signal-anchor transmembrane helix and conserved active-site residues at positions 49, 90, and 115.

"ID SEC11_NEUCR Reviewed; 172 AA. AC Q7RY44; ... ACT_SITE 49 ... ACT_SITE 90 ... ACT_SITE 115"
UniProtKB's curated homology notes place Q7RY44 in the ER signal peptidase complex and in the ER membrane.

"Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum"

file:interpro/panther/PTHR10806/PTHR10806-paint.tsv

PTHR10806 PAINT IBD export

PAINT placed the generic peptidase activity IBD at the PTHR10806 family root, while the ER signal peptidase complex and protein maturation IBDs are placed at the Eukaryota node PTN000086750.

"PTHR10806 PTN000086749 GO:0008233 F IBD false ... PTHR10806 PTN000086750 GO:0005787 C IBD false ... PTHR10806 PTN000086750 GO:0051604 P IBD false"

file:interpro/panther/PTHR10806/PTHR10806-entries.csv

PTHR10806 member export

The PANTHER export places Neurospora crassa Q7RY44 in PTHR10806:SF6, the fungal Sec11 subfamily that also contains budding yeast SEC11.

"Q7RY44,Signal peptidase complex catalytic subunit sec11,protein,367110 ... PTHR10806:SF6,SIGNAL PEPTIDASE COMPLEX CATALYTIC SUBUNIT SEC11"

PMID:12712197

The genome sequence of the filamentous fungus Neurospora crassa.

The Neurospora crassa OR74A genome project supplied the genomic sequence from which NCU04519/Q7RY44 was annotated.

PMID:3283143

SEC11 is required for signal peptide processing and yeast cell growth.

Budding yeast sec11 mutants accumulate signal-peptide-retaining secretory precursors, and a SEC11 null mutation is lethal.

PMID:1846444

Yeast signal peptidase contains a glycoprotein and the Sec11 gene product.

Biochemical purification of yeast signal peptidase recovered Sec11 as a component of the eukaryotic ER signal peptidase complex.

PMID:10206957

The catalytic mechanism of endoplasmic reticulum signal peptidase appears to be distinct from most eubacterial signal peptidases.

Mutational analysis of yeast Sec11 showed that conserved Ser, His, and Asp residues are important for eukaryotic ER signal peptidase activity.

PMID:34388369

Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage.

Cryo-EM structures of human SPC-A and SPC-C showed conserved SEC11A/C catalytic cores, a membrane-proximal active site, and a transmembrane window that helps discriminate signal peptides by hydrophobic-region length.

PMID:39565596

Spc2 modulates substrate- and cleavage site-selection in the yeast signal peptidase complex.

A yeast SPC AlphaFold2-Multimer model and in vivo signal-sequence cleavage assays supported the conserved ER-membrane architecture of fungal Sec11 within the heterotetrameric signal peptidase complex.

PMID:42173868

Structural basis of signal peptide recognition by the signal peptidase complex.

A human SPC-A structure bound to a model signal peptide directly visualized the signal peptide binding groove near SEC11A and the transmembrane window used by the catalytic subunit to engage substrates.

PMID:42586426

The Sec11 C-terminal short helix promotes productive engagement of internal signal sequences with the signal peptidase complex.

Recent yeast work showed that the Sec11 C-terminal short helix traverses the ER membrane and contributes selectively to productive engagement of internal signal sequences.