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Conserved domains on  [gi|459495020|gb|EMG88294|]
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hypothetical protein HMPREF1396_00145, partial [Helicobacter pylori GAM114Ai]

Protein Classification

O-fucosyltransferase family protein( domain architecture ID 94843)

O-fucosyltransferase family protein may be involved in glycan metabolism by O-fucosylation of protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
O-FucT_like super family cl16914
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like ...
3-135 1.49e-19

GDP-fucose protein O-fucosyltransferase and related proteins; 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.


The actual alignment was detected with superfamily member cd11301:

Pssm-ID: 450121  Cd Length: 265  Bit Score: 81.35  E-value: 1.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459495020   3 FKVVQIC-GGLGNQMFQYAFAKSLQKHLN-TPVLLDITSFDWSNRKMQLELFPIDLPYASEKEIAVAKMQHLPKLVRdal 80
Cdd:cd11301    1 MKIVSLLaGGLGNQLFQYAFLRALAKKLGrRKLFLDTSGYFERNLLKLLEFFNISLPILSRKEILLLKNLRLLNEDP--- 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 459495020  81 krmgfdrvsqeivfeYKPKLLKPSRLTYFYGYFQDPRYFDAISPLIKQTFTLPPP 135
Cdd:cd11301   78 ---------------VLKKLLRENYRHYLGRYYQFWKYFYSIKGEIRQEFKFFED 117
 
Name Accession Description Interval E-value
Fut1_Fut2_like cd11301
Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer ...
3-135 1.49e-19

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: 81.35  E-value: 1.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459495020   3 FKVVQIC-GGLGNQMFQYAFAKSLQKHLN-TPVLLDITSFDWSNRKMQLELFPIDLPYASEKEIAVAKMQHLPKLVRdal 80
Cdd:cd11301    1 MKIVSLLaGGLGNQLFQYAFLRALAKKLGrRKLFLDTSGYFERNLLKLLEFFNISLPILSRKEILLLKNLRLLNEDP--- 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 459495020  81 krmgfdrvsqeivfeYKPKLLKPSRLTYFYGYFQDPRYFDAISPLIKQTFTLPPP 135
Cdd:cd11301   78 ---------------VLKKLLRENYRHYLGRYYQFWKYFYSIKGEIRQEFKFFED 117
 
Name Accession Description Interval E-value
Fut1_Fut2_like cd11301
Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer ...
3-135 1.49e-19

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: 81.35  E-value: 1.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 459495020   3 FKVVQIC-GGLGNQMFQYAFAKSLQKHLN-TPVLLDITSFDWSNRKMQLELFPIDLPYASEKEIAVAKMQHLPKLVRdal 80
Cdd:cd11301    1 MKIVSLLaGGLGNQLFQYAFLRALAKKLGrRKLFLDTSGYFERNLLKLLEFFNISLPILSRKEILLLKNLRLLNEDP--- 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 459495020  81 krmgfdrvsqeivfeYKPKLLKPSRLTYFYGYFQDPRYFDAISPLIKQTFTLPPP 135
Cdd:cd11301   78 ---------------VLKKLLRENYRHYLGRYYQFWKYFYSIKGEIRQEFKFFED 117
 
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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