fukutin isoform X1 [Salmo salar]
List of domain hits
Name | Accession | Description | Interval | E-value | |||||
FKTN_N | pfam19737 | Fukutin N-terminal; This is the N-terminal domain of fukutin, which contains the transmembrane ... |
1-275 | 1.26e-178 | |||||
Fukutin N-terminal; This is the N-terminal domain of fukutin, which contains the transmembrane domain required for its localization to the Golgi and participates in the interaction with POMGnT1 for normal POMGnT1 location and activity. Fukutin is a ribitol-phosphate transferase that forms a complex with FKRP and TMEM5 which may contribute to specific biosynthesis of glycans required for dystroglycan function. : Pssm-ID: 466166 Cd Length: 278 Bit Score: 500.37 E-value: 1.26e-178
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LicD super family | cl01378 | LicD family; The LICD family of proteins show high sequence similarity and are involved in ... |
291-324 | 4.86e-05 | |||||
LicD family; The LICD family of proteins show high sequence similarity and are involved in phosphorylcholine metabolism. There is evidence to show that LicD2 mutants have a reduced ability to take up choline, have decreased ability to adhere to host cells and are less virulent. These proteins are part of the nucleotidyltransferase superfamily. The actual alignment was detected with superfamily member pfam04991: Pssm-ID: 470175 Cd Length: 228 Bit Score: 44.67 E-value: 4.86e-05
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Name | Accession | Description | Interval | E-value | |||||
FKTN_N | pfam19737 | Fukutin N-terminal; This is the N-terminal domain of fukutin, which contains the transmembrane ... |
1-275 | 1.26e-178 | |||||
Fukutin N-terminal; This is the N-terminal domain of fukutin, which contains the transmembrane domain required for its localization to the Golgi and participates in the interaction with POMGnT1 for normal POMGnT1 location and activity. Fukutin is a ribitol-phosphate transferase that forms a complex with FKRP and TMEM5 which may contribute to specific biosynthesis of glycans required for dystroglycan function. Pssm-ID: 466166 Cd Length: 278 Bit Score: 500.37 E-value: 1.26e-178
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LicD | pfam04991 | LicD family; The LICD family of proteins show high sequence similarity and are involved in ... |
291-324 | 4.86e-05 | |||||
LicD family; The LICD family of proteins show high sequence similarity and are involved in phosphorylcholine metabolism. There is evidence to show that LicD2 mutants have a reduced ability to take up choline, have decreased ability to adhere to host cells and are less virulent. These proteins are part of the nucleotidyltransferase superfamily. Pssm-ID: 428243 Cd Length: 228 Bit Score: 44.67 E-value: 4.86e-05
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Peptidase_C39B | cd02418 | A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
122-182 | 9.45e-04 | |||||
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family. Pssm-ID: 239099 [Multi-domain] Cd Length: 136 Bit Score: 39.50 E-value: 9.45e-04
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Name | Accession | Description | Interval | E-value | |||||
FKTN_N | pfam19737 | Fukutin N-terminal; This is the N-terminal domain of fukutin, which contains the transmembrane ... |
1-275 | 1.26e-178 | |||||
Fukutin N-terminal; This is the N-terminal domain of fukutin, which contains the transmembrane domain required for its localization to the Golgi and participates in the interaction with POMGnT1 for normal POMGnT1 location and activity. Fukutin is a ribitol-phosphate transferase that forms a complex with FKRP and TMEM5 which may contribute to specific biosynthesis of glycans required for dystroglycan function. Pssm-ID: 466166 Cd Length: 278 Bit Score: 500.37 E-value: 1.26e-178
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LicD | pfam04991 | LicD family; The LICD family of proteins show high sequence similarity and are involved in ... |
291-324 | 4.86e-05 | |||||
LicD family; The LICD family of proteins show high sequence similarity and are involved in phosphorylcholine metabolism. There is evidence to show that LicD2 mutants have a reduced ability to take up choline, have decreased ability to adhere to host cells and are less virulent. These proteins are part of the nucleotidyltransferase superfamily. Pssm-ID: 428243 Cd Length: 228 Bit Score: 44.67 E-value: 4.86e-05
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Peptidase_C39B | cd02418 | A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
122-182 | 9.45e-04 | |||||
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family. Pssm-ID: 239099 [Multi-domain] Cd Length: 136 Bit Score: 39.50 E-value: 9.45e-04
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Blast search parameters | ||||
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