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Links from Protein

Items: 10

1.

glycoside hydrolase family 95-like protein

Date:
2024-08-14
Family Accession:
NF045341.2
Method:
HMM
2.

Glycosyl hydrolase family 95 catalytic domain

Date:
2024-08-14
Family Accession:
NF046196.1
Method:
HMM
3.

glycoside hydrolase N-terminal domain-containing protein

This domain represents a domain found to the N-terminus of the glycosyl hydrolase 65 family catalytic domain. (from Pfam)

Date:
2024-08-14
Family Accession:
NF025851.5
Method:
HMM
4.

YSIRK-type signal peptide-containing protein

Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus. (from Pfam)

GO Terms:
Cellular Component:
membrane (GO:0016020)
Date:
2024-08-14
Family Accession:
NF016529.5
Method:
HMM
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.

YSIRK-type signal peptide-containing protein

The [YF]SIRKxxxGxxS type of signal peptide appears at the start of many proteins of Streptococcus, Staphylococcus, and Enterococcus, but not in other lineages such as Bacillus. Recent work in Staphylococcus aureus has shown that septal secretion (targeting to the crosswall in dividing cells) of the YSIRK-containing staphylococcal protein A depends on SecA, SecDF, and the lipoteichoic acid synthase LtaS, all of which co-purify when the motif is modified to YSIRKxxxGxxL to block processing.

Date:
2019-12-09
Family Accession:
TIGR01168.1
Method:
HMM
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