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Conserved domains on  [gi|929062700|ref|XP_014002642|]
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fukutin isoform X1 [Salmo salar]

Protein Classification

Graphical summary

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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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929062700    1 MLRFNKTAVLALLIATSSVFLLFQLYHSRQPVSQ-NGPHIFGRTVHLSGKDAQ-WQVVKKFMGLVHKYNMPVFLVDTAAL 78
Cdd:pfam19737   1 MPRINKNVVLALLTLTSSVFLLFQLYYYKHYLSPkNGAHFSKVKGSLSGQDSTqWHVVKKFLGLVSKHNLPVFLIDPLVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929062700   79 GLLSQDSMLLRDSLVKE-PHCTFLCTNRDVLTFALLNNLWKYNAGLVAAAEEKGFELLEVRGKDPRLVSMDDLSGNEIPL 157
Cdd:pfam19737  81 GLISQDAEQLRDSSDGSsPECKYFCAPRDFTTFALLDKLWKNEAGLFRAAEEMGFQWLEIQGKDPRLEGMDDLSGTEIPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929062700  158 HFLFRLQGYVVHVVVLYERSGNYLWHGVLRLKPNMDRKFAPFRRLDYGRNAGAYDRPELVLTTLDGLDVRIPRNISGFLT 237
Cdd:pfam19737 161 HYIFRLAGHAVHLVVFYERSGNYLWHGQLRLKQNMDRKFVPFRKLDFGRYPGAYDRPELLLVSIDGLNVQIPKNPSRFLE 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 929062700  238 EYSQARFLECRYRDARSFFQLYPDDTSPEAMNFRMKAK 275
Cdd:pfam19737 241 EVSHSRFLECRYREARAFFQLYPDDTSLEAVEFRKKAK 278
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
                          10        20        30
                  ....*....|....*....|....*....|....
gi 929062700  291 PFWLSSGTCLGWFRQCGIIPYSKDVDLGIWIKDY 324
Cdd:pfam04991   7 IYWLSGGTLLGAVRHGGFIPWDDDIDIQMPRKDY 40
 
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929062700    1 MLRFNKTAVLALLIATSSVFLLFQLYHSRQPVSQ-NGPHIFGRTVHLSGKDAQ-WQVVKKFMGLVHKYNMPVFLVDTAAL 78
Cdd:pfam19737   1 MPRINKNVVLALLTLTSSVFLLFQLYYYKHYLSPkNGAHFSKVKGSLSGQDSTqWHVVKKFLGLVSKHNLPVFLIDPLVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929062700   79 GLLSQDSMLLRDSLVKE-PHCTFLCTNRDVLTFALLNNLWKYNAGLVAAAEEKGFELLEVRGKDPRLVSMDDLSGNEIPL 157
Cdd:pfam19737  81 GLISQDAEQLRDSSDGSsPECKYFCAPRDFTTFALLDKLWKNEAGLFRAAEEMGFQWLEIQGKDPRLEGMDDLSGTEIPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929062700  158 HFLFRLQGYVVHVVVLYERSGNYLWHGVLRLKPNMDRKFAPFRRLDYGRNAGAYDRPELVLTTLDGLDVRIPRNISGFLT 237
Cdd:pfam19737 161 HYIFRLAGHAVHLVVFYERSGNYLWHGQLRLKQNMDRKFVPFRKLDFGRYPGAYDRPELLLVSIDGLNVQIPKNPSRFLE 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 929062700  238 EYSQARFLECRYRDARSFFQLYPDDTSPEAMNFRMKAK 275
Cdd:pfam19737 241 EVSHSRFLECRYREARAFFQLYPDDTSLEAVEFRKKAK 278
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
                          10        20        30
                  ....*....|....*....|....*....|....
gi 929062700  291 PFWLSSGTCLGWFRQCGIIPYSKDVDLGIWIKDY 324
Cdd:pfam04991   7 IYWLSGGTLLGAVRHGGFIPWDDDIDIQMPRKDY 40
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
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 929062700 122 GLVAAAEEKGFELLEVRGkdprlvSMDDLSGNEIPL----HFLFRLQGYvvHVVVLYERSGNYLW 182
Cdd:cd02418   48 GLVKAAEKLGFETRAVKA------DMDLFELKDIPLpfiaHVIKEWKLN--HYVVVYKIKKKKIL 104
 
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929062700    1 MLRFNKTAVLALLIATSSVFLLFQLYHSRQPVSQ-NGPHIFGRTVHLSGKDAQ-WQVVKKFMGLVHKYNMPVFLVDTAAL 78
Cdd:pfam19737   1 MPRINKNVVLALLTLTSSVFLLFQLYYYKHYLSPkNGAHFSKVKGSLSGQDSTqWHVVKKFLGLVSKHNLPVFLIDPLVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929062700   79 GLLSQDSMLLRDSLVKE-PHCTFLCTNRDVLTFALLNNLWKYNAGLVAAAEEKGFELLEVRGKDPRLVSMDDLSGNEIPL 157
Cdd:pfam19737  81 GLISQDAEQLRDSSDGSsPECKYFCAPRDFTTFALLDKLWKNEAGLFRAAEEMGFQWLEIQGKDPRLEGMDDLSGTEIPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929062700  158 HFLFRLQGYVVHVVVLYERSGNYLWHGVLRLKPNMDRKFAPFRRLDYGRNAGAYDRPELVLTTLDGLDVRIPRNISGFLT 237
Cdd:pfam19737 161 HYIFRLAGHAVHLVVFYERSGNYLWHGQLRLKQNMDRKFVPFRKLDFGRYPGAYDRPELLLVSIDGLNVQIPKNPSRFLE 240

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 929062700  238 EYSQARFLECRYRDARSFFQLYPDDTSPEAMNFRMKAK 275
Cdd:pfam19737 241 EVSHSRFLECRYREARAFFQLYPDDTSLEAVEFRKKAK 278
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
                          10        20        30
                  ....*....|....*....|....*....|....
gi 929062700  291 PFWLSSGTCLGWFRQCGIIPYSKDVDLGIWIKDY 324
Cdd:pfam04991   7 IYWLSGGTLLGAVRHGGFIPWDDDIDIQMPRKDY 40
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
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 929062700 122 GLVAAAEEKGFELLEVRGkdprlvSMDDLSGNEIPL----HFLFRLQGYvvHVVVLYERSGNYLW 182
Cdd:cd02418   48 GLVKAAEKLGFETRAVKA------DMDLFELKDIPLpfiaHVIKEWKLN--HYVVVYKIKKKKIL 104
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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