hypothetical protein [Lactobacillus delbrueckii]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| PGAP4-like super family | cl04660 | Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ... |
6-58 | 1.65e-03 | ||
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. This family also includes uncharacterized fungal proteins with similarity to PGAP4. The actual alignment was detected with superfamily member cd22190: Pssm-ID: 471077 Cd Length: 379 Bit Score: 37.20 E-value: 1.65e-03
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| Name | Accession | Description | Interval | E-value | ||
| PGAP4 | cd22190 | Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), ... |
6-58 | 1.65e-03 | ||
Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246), has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases (GTs), it contains three transmembrane domains. Structural modeling suggests that PGAP4 adopts a GT-A fold split by an insertion of tandem transmembrane domains. Pssm-ID: 409191 Cd Length: 379 Bit Score: 37.20 E-value: 1.65e-03
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| Name | Accession | Description | Interval | E-value | ||
| PGAP4 | cd22190 | Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), ... |
6-58 | 1.65e-03 | ||
Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246), has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases (GTs), it contains three transmembrane domains. Structural modeling suggests that PGAP4 adopts a GT-A fold split by an insertion of tandem transmembrane domains. Pssm-ID: 409191 Cd Length: 379 Bit Score: 37.20 E-value: 1.65e-03
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