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Conserved domains on  [gi|922581038|ref|NP_001300089|]
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L-Fucosyltransferase [Caenorhabditis elegans]

Protein Classification

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 ...
54-310 7.10e-44

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: 151.46  E-value: 7.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038  54 YLSSNLAspCQLGNHIFELASLYGLSKHLNRTPAFFIESGYHKNmldsirstmpGLIGKYAIFDGSVPTSLKETKFQKVC 133
Cdd:cd11301    2 KIVSLLA--GGLGNQLFQYAFLRALAKKLGRRKLFLDTSGYFER----------NLLKLLEFFNISLPILSRKEILLLKN 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038 134 C--VYENPWNLKRSQHEYLHLTGKFYQSWKYFPN----MREELISFLNTSVQNFGILPISNN---NTHVSCVHSRRGDFV 204
Cdd:cd11301   70 LrlLNEDPVLKKLLRENYRHYLGRYYQFWKYFYSikgeIRQEFKFFEDLEEENNKILKKLKEelkNTNSVSVHIRRGDYL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038 205 EMNFYA-----TDPKFMKNAVKFLKEKenysKKNQKIVLFGDDFKFMRNLFSEakvstdaHESVEYYISQ--NSAIDDFL 277
Cdd:cd11301  150 TNGNAKgyhgiCDLEYYKKAIEYIKEK----VKNPVFFVFSDDIEWVKENLAL-------TSKENVYFVDgnNSSYEDLY 218
                        250       260       270
                 ....*....|....*....|....*....|...
gi 922581038 278 YSAYnCDEVLITapRSTFGWWLGYFSKGDKVYY 310
Cdd:cd11301  219 LMSL-CKHVIIS--NSTFSWWGAYLNKNPDKIV 248
 
Name Accession Description Interval E-value
Fut1_Fut2_like cd11301
Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer ...
54-310 7.10e-44

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: 151.46  E-value: 7.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038  54 YLSSNLAspCQLGNHIFELASLYGLSKHLNRTPAFFIESGYHKNmldsirstmpGLIGKYAIFDGSVPTSLKETKFQKVC 133
Cdd:cd11301    2 KIVSLLA--GGLGNQLFQYAFLRALAKKLGRRKLFLDTSGYFER----------NLLKLLEFFNISLPILSRKEILLLKN 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038 134 C--VYENPWNLKRSQHEYLHLTGKFYQSWKYFPN----MREELISFLNTSVQNFGILPISNN---NTHVSCVHSRRGDFV 204
Cdd:cd11301   70 LrlLNEDPVLKKLLRENYRHYLGRYYQFWKYFYSikgeIRQEFKFFEDLEEENNKILKKLKEelkNTNSVSVHIRRGDYL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038 205 EMNFYA-----TDPKFMKNAVKFLKEKenysKKNQKIVLFGDDFKFMRNLFSEakvstdaHESVEYYISQ--NSAIDDFL 277
Cdd:cd11301  150 TNGNAKgyhgiCDLEYYKKAIEYIKEK----VKNPVFFVFSDDIEWVKENLAL-------TSKENVYFVDgnNSSYEDLY 218
                        250       260       270
                 ....*....|....*....|....*....|...
gi 922581038 278 YSAYnCDEVLITapRSTFGWWLGYFSKGDKVYY 310
Cdd:cd11301  219 LMSL-CKHVIIS--NSTFSWWGAYLNKNPDKIV 248
Glyco_transf_11 pfam01531
Glycosyl transferase family 11; This family contains several fucosyl transferase enzymes.
65-309 3.19e-11

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


Pssm-ID: 250689  Cd Length: 298  Bit Score: 62.97  E-value: 3.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038   65 LGNHIFELASLYGLSKhLNRTPAFfIESGYHKnMLDSIRSTMPGLIGKYAI----FDGSVPTSLKETKFQ-----KVCCV 135
Cdd:pfam01531  41 LGNQMGQYSTLIALAP-LNGRLAF-IPASMHS-TLAPFRITLPVLHSTTASrkpwQNYHLNDWMEEEYRHlrgeyVKFTG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038  136 YENPWNLkrsqheYLHltgKFYQSWKYFPNMREELISFLNTSVQNFGILPISNNNTHVsCVHSRRGDFVEMN-----FYA 210
Cdd:pfam01531 118 YPCSWTF------YHH---GLRQEILYEFTLHDHLREEIQNFLRGLQVNLGSRPSTFV-GVHIRRGDYVDVMpkvwkGVV 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038  211 TDPKFMKNAVKflKEKENYSkkNQKIVLFGDDFKFMRNlfseakvSTDAHESVEYYISQNSAIDDFLYSAyNCDEVLITA 290
Cdd:pfam01531 188 ADINYLIQALD--WFRARYS--SPVFVVFSDDMEWCKK-------NIDTSCGDVYFAGDGSPAEDFALLM-QCNHTILSI 255
                         250
                  ....*....|....*....
gi 922581038  291 prSTFGWWLGYFSKGDKVY 309
Cdd:pfam01531 256 --STFSWWAAYLTGGDTIY 272
 
Name Accession Description Interval E-value
Fut1_Fut2_like cd11301
Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer ...
54-310 7.10e-44

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: 151.46  E-value: 7.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038  54 YLSSNLAspCQLGNHIFELASLYGLSKHLNRTPAFFIESGYHKNmldsirstmpGLIGKYAIFDGSVPTSLKETKFQKVC 133
Cdd:cd11301    2 KIVSLLA--GGLGNQLFQYAFLRALAKKLGRRKLFLDTSGYFER----------NLLKLLEFFNISLPILSRKEILLLKN 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038 134 C--VYENPWNLKRSQHEYLHLTGKFYQSWKYFPN----MREELISFLNTSVQNFGILPISNN---NTHVSCVHSRRGDFV 204
Cdd:cd11301   70 LrlLNEDPVLKKLLRENYRHYLGRYYQFWKYFYSikgeIRQEFKFFEDLEEENNKILKKLKEelkNTNSVSVHIRRGDYL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038 205 EMNFYA-----TDPKFMKNAVKFLKEKenysKKNQKIVLFGDDFKFMRNLFSEakvstdaHESVEYYISQ--NSAIDDFL 277
Cdd:cd11301  150 TNGNAKgyhgiCDLEYYKKAIEYIKEK----VKNPVFFVFSDDIEWVKENLAL-------TSKENVYFVDgnNSSYEDLY 218
                        250       260       270
                 ....*....|....*....|....*....|...
gi 922581038 278 YSAYnCDEVLITapRSTFGWWLGYFSKGDKVYY 310
Cdd:cd11301  219 LMSL-CKHVIIS--NSTFSWWGAYLNKNPDKIV 248
Glyco_transf_11 pfam01531
Glycosyl transferase family 11; This family contains several fucosyl transferase enzymes.
65-309 3.19e-11

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


Pssm-ID: 250689  Cd Length: 298  Bit Score: 62.97  E-value: 3.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038   65 LGNHIFELASLYGLSKhLNRTPAFfIESGYHKnMLDSIRSTMPGLIGKYAI----FDGSVPTSLKETKFQ-----KVCCV 135
Cdd:pfam01531  41 LGNQMGQYSTLIALAP-LNGRLAF-IPASMHS-TLAPFRITLPVLHSTTASrkpwQNYHLNDWMEEEYRHlrgeyVKFTG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038  136 YENPWNLkrsqheYLHltgKFYQSWKYFPNMREELISFLNTSVQNFGILPISNNNTHVsCVHSRRGDFVEMN-----FYA 210
Cdd:pfam01531 118 YPCSWTF------YHH---GLRQEILYEFTLHDHLREEIQNFLRGLQVNLGSRPSTFV-GVHIRRGDYVDVMpkvwkGVV 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581038  211 TDPKFMKNAVKflKEKENYSkkNQKIVLFGDDFKFMRNlfseakvSTDAHESVEYYISQNSAIDDFLYSAyNCDEVLITA 290
Cdd:pfam01531 188 ADINYLIQALD--WFRARYS--SPVFVVFSDDMEWCKK-------NIDTSCGDVYFAGDGSPAEDFALLM-QCNHTILSI 255
                         250
                  ....*....|....*....
gi 922581038  291 prSTFGWWLGYFSKGDKVY 309
Cdd:pfam01531 256 --STFSWWAAYLTGGDTIY 272
 
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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