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Conserved domains on  [gi|727290486|ref|WP_033748234|]
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alpha-(1,2)-fucosyltransferase FutC1 [Helicobacter pylori]

Protein Classification

alpha-1,2-fucosyltransferase( domain architecture ID 10181967)

alpha-1,2-fucosyltransferase plays a role in antigen synthesis, catalyzing the transfer of fucose from GDP-Fuc to N-linked type complex glycoproteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Fut1_Fut2_like cd11301
Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer ...
 3-118 2.11e-35

Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer of alpha-L-fucose to the terminal beta-D-galactose residue of glycoconjugates via an alpha-1,2-linkage, generating carbohydrate structures that exhibit H-antigenicity for blood-group carbohydrates. These structures also act as ligands for morphogenesis, the adhesion of microbes, and metastasizing cancer cells. Fut1 is responsible for producing the H antigen on red blood cells. Fut2 is expressed in epithelia of secretory tissues, and individuals termed "secretors" have at least one functional copy of the gene; they secrete H antigen which is further processed into A and/or B antigens depending on the ABO genotype. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.


:

Pssm-ID: 211387  Cd Length: 265  Bit Score: 122.96  E-value: 2.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727290486   3 LAAKNSVFAHIRRGDYV------GIGCQLGIDYQKKAVEYMAKRVPNMELFVFCEDLTFTQNLDLGYPFMDMTTRDKDEE 76
Cdd:cd11301  133 LKNTNSVSVHIRRGDYLtngnakGYHGICDLEYYKKAIEYIKEKVKNPVFFVFSDDIEWVKENLALTSKENVYFVDGNNS 212

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 727290486  77 AYWDMLLMQSCQHGIIANSTYSWWAAYLIENPEKI-IIGPKHW 118
Cdd:cd11301  213 SYEDLYLMSLCKHVIISNSTFSWWGAYLNKNPDKIvIIAPNPW 255
 
Name Accession Description Interval E-value
Fut1_Fut2_like cd11301
Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer ...
 3-118 2.11e-35

Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer of alpha-L-fucose to the terminal beta-D-galactose residue of glycoconjugates via an alpha-1,2-linkage, generating carbohydrate structures that exhibit H-antigenicity for blood-group carbohydrates. These structures also act as ligands for morphogenesis, the adhesion of microbes, and metastasizing cancer cells. Fut1 is responsible for producing the H antigen on red blood cells. Fut2 is expressed in epithelia of secretory tissues, and individuals termed "secretors" have at least one functional copy of the gene; they secrete H antigen which is further processed into A and/or B antigens depending on the ABO genotype. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.


Pssm-ID: 211387  Cd Length: 265  Bit Score: 122.96  E-value: 2.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727290486   3 LAAKNSVFAHIRRGDYV------GIGCQLGIDYQKKAVEYMAKRVPNMELFVFCEDLTFTQNLDLGYPFMDMTTRDKDEE 76
Cdd:cd11301  133 LKNTNSVSVHIRRGDYLtngnakGYHGICDLEYYKKAIEYIKEKVKNPVFFVFSDDIEWVKENLALTSKENVYFVDGNNS 212

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 727290486  77 AYWDMLLMQSCQHGIIANSTYSWWAAYLIENPEKI-IIGPKHW 118
Cdd:cd11301  213 SYEDLYLMSLCKHVIISNSTFSWWGAYLNKNPDKIvIIAPNPW 255
Glyco_transf_11 pfam01531
Glycosyl transferase family 11; This family contains several fucosyl transferase enzymes.
 8-134 3.70e-14

Glycosyl transferase family 11; This family contains several fucosyl transferase enzymes.


Pssm-ID: 250689  Cd Length: 298  Bit Score: 67.59  E-value: 3.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727290486    8 SVFAHIRRGDYV------GIGCQLGIDYQKKAVEYMAKRVPNMELFVFCEDLTFT-QNLDlgypfmdmTTRDKDEEAY-- 78
Cdd:pfam01531 165 FVGVHIRRGDYVdvmpkvWKGVVADINYLIQALDWFRARYSSPVFVVFSDDMEWCkKNID--------TSCGDVYFAGdg 236

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727290486   79 ---WDMLLMQSCQHGIIANSTYSWWAAYLIENpEKIIIGPKHW----LFGHENILCKEWVKIE 134
Cdd:pfam01531 237 spaEDFALLMQCNHTILSISTFSWWAAYLTGG-DTIYLANFNLpdseFLKKEAAYLPEWVYIA 298
 
Name Accession Description Interval E-value
Fut1_Fut2_like cd11301
Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer ...
 3-118 2.11e-35

Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer of alpha-L-fucose to the terminal beta-D-galactose residue of glycoconjugates via an alpha-1,2-linkage, generating carbohydrate structures that exhibit H-antigenicity for blood-group carbohydrates. These structures also act as ligands for morphogenesis, the adhesion of microbes, and metastasizing cancer cells. Fut1 is responsible for producing the H antigen on red blood cells. Fut2 is expressed in epithelia of secretory tissues, and individuals termed "secretors" have at least one functional copy of the gene; they secrete H antigen which is further processed into A and/or B antigens depending on the ABO genotype. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.


Pssm-ID: 211387  Cd Length: 265  Bit Score: 122.96  E-value: 2.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727290486   3 LAAKNSVFAHIRRGDYV------GIGCQLGIDYQKKAVEYMAKRVPNMELFVFCEDLTFTQNLDLGYPFMDMTTRDKDEE 76
Cdd:cd11301  133 LKNTNSVSVHIRRGDYLtngnakGYHGICDLEYYKKAIEYIKEKVKNPVFFVFSDDIEWVKENLALTSKENVYFVDGNNS 212

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 727290486  77 AYWDMLLMQSCQHGIIANSTYSWWAAYLIENPEKI-IIGPKHW 118
Cdd:cd11301  213 SYEDLYLMSLCKHVIISNSTFSWWGAYLNKNPDKIvIIAPNPW 255
Glyco_transf_11 pfam01531
Glycosyl transferase family 11; This family contains several fucosyl transferase enzymes.
 8-134 3.70e-14

Glycosyl transferase family 11; This family contains several fucosyl transferase enzymes.


Pssm-ID: 250689  Cd Length: 298  Bit Score: 67.59  E-value: 3.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727290486    8 SVFAHIRRGDYV------GIGCQLGIDYQKKAVEYMAKRVPNMELFVFCEDLTFT-QNLDlgypfmdmTTRDKDEEAY-- 78
Cdd:pfam01531 165 FVGVHIRRGDYVdvmpkvWKGVVADINYLIQALDWFRARYSSPVFVVFSDDMEWCkKNID--------TSCGDVYFAGdg 236

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727290486   79 ---WDMLLMQSCQHGIIANSTYSWWAAYLIENpEKIIIGPKHW----LFGHENILCKEWVKIE 134
Cdd:pfam01531 237 spaEDFALLMQCNHTILSISTFSWWAAYLTGG-DTIYLANFNLpdseFLKKEAAYLPEWVYIA 298
 
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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