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Conserved domains on  [gi|25149506|ref|NP_498891|]
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Putative glycosyltransferase C06E1.7 [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 ...
71-343 5.47e-38

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: 136.82  E-value: 5.47e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506  71 TARLANHIFELVSVYGMAKSLNRKPAIFVEDSKYNLLITGVRKVLPGLLDEF--QIFEYPVHNKATKVPLSEKCCIFDNP 148
Cdd:cd11301   8 AGGLGNQLFQYAFLRALAKKLGRRKLFLDTSGYFERNLLKLLEFFNISLPILsrKEILLLKNLRLLNEDPVLKKLLRENY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506 149 DKFNNISSEYLHLT----GHFYQSWKYFDKYKEKVQSFVKPAIDFSPLPNSdssnfisrICIHIRRTDFV-----DGQHH 219
Cdd:cd11301  88 RHYLGRYYQFWKYFysikGEIRQEFKFFEDLEEENNKILKKLKEELKNTNS--------VSVHIRRGDYLtngnaKGYHG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506 220 SSNVSFIKPALEFIKEReqkdvNKKMLTVIMGDDPDFEAKMFegtvrakkeAKIEETTKYFVSENTPQ-DDLAYSHYsCD 298
Cdd:cd11301 160 ICDLEYYKKAIEYIKEK-----VKNPVFFVFSDDIEWVKENL---------ALTSKENVYFVDGNNSSyEDLYLMSL-CK 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 25149506 299 ATLITapSSTFGWWLGYLSKGQAVYYqdIRSTNDVNYKKGVLDPD 343
Cdd:cd11301 225 HVIIS--NSTFSWWGAYLNKNPDKIV--IIAPNPWFVKKKLFPPD 265
 
Name Accession Description Interval E-value
Fut1_Fut2_like cd11301
Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer ...
71-343 5.47e-38

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: 136.82  E-value: 5.47e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506  71 TARLANHIFELVSVYGMAKSLNRKPAIFVEDSKYNLLITGVRKVLPGLLDEF--QIFEYPVHNKATKVPLSEKCCIFDNP 148
Cdd:cd11301   8 AGGLGNQLFQYAFLRALAKKLGRRKLFLDTSGYFERNLLKLLEFFNISLPILsrKEILLLKNLRLLNEDPVLKKLLRENY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506 149 DKFNNISSEYLHLT----GHFYQSWKYFDKYKEKVQSFVKPAIDFSPLPNSdssnfisrICIHIRRTDFV-----DGQHH 219
Cdd:cd11301  88 RHYLGRYYQFWKYFysikGEIRQEFKFFEDLEEENNKILKKLKEELKNTNS--------VSVHIRRGDYLtngnaKGYHG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506 220 SSNVSFIKPALEFIKEReqkdvNKKMLTVIMGDDPDFEAKMFegtvrakkeAKIEETTKYFVSENTPQ-DDLAYSHYsCD 298
Cdd:cd11301 160 ICDLEYYKKAIEYIKEK-----VKNPVFFVFSDDIEWVKENL---------ALTSKENVYFVDGNNSSyEDLYLMSL-CK 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 25149506 299 ATLITapSSTFGWWLGYLSKGQAVYYqdIRSTNDVNYKKGVLDPD 343
Cdd:cd11301 225 HVIIS--NSTFSWWGAYLNKNPDKIV--IIAPNPWFVKKKLFPPD 265
Glyco_transf_11 pfam01531
Glycosyl transferase family 11; This family contains several fucosyl transferase enzymes.
73-338 9.46e-10

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


Pssm-ID: 250689  Cd Length: 298  Bit Score: 59.11  E-value: 9.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506    73 RLANHIFELVSVYGMAKSLNRKPAIFVEDSKYnllitgvrkvlpglLDEFQIFeYPVHNKATKV--PLSEKccifdnpdK 150
Cdd:pfam01531  40 RLGNQMGQYSTLIALAPLNGRLAFIPASMHST--------------LAPFRIT-LPVLHSTTASrkPWQNY--------H 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506   151 FNNISSE-YLHLTGHFYQ------SWKYF---------------DKYKEKVQSFVKPAIDFSPLPNSDSsnfisrICIHI 208
Cdd:pfam01531  97 LNDWMEEeYRHLRGEYVKftgypcSWTFYhhglrqeilyeftlhDHLREEIQNFLRGLQVNLGSRPSTF------VGVHI 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506   209 RRTDFVD-----GQHHSSNVSFIKPALEFIKEREQKDVnkkmlTVIMGDDPDFeakmfegtvrAKKEAKIEETTKYFVSE 283
Cdd:pfam01531 171 RRGDYVDvmpkvWKGVVADINYLIQALDWFRARYSSPV-----FVVFSDDMEW----------CKKNIDTSCGDVYFAGD 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25149506   284 NTPQDDLAYSHySCDATLITapSSTFGWWLGYLSKGQAVY------YQDIRSTNDVNYKKG 338
Cdd:pfam01531 236 GSPAEDFALLM-QCNHTILS--ISTFSWWAAYLTGGDTIYlanfnlPDSEFLKKEAAYLPE 293
 
Name Accession Description Interval E-value
Fut1_Fut2_like cd11301
Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer ...
71-343 5.47e-38

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: 136.82  E-value: 5.47e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506  71 TARLANHIFELVSVYGMAKSLNRKPAIFVEDSKYNLLITGVRKVLPGLLDEF--QIFEYPVHNKATKVPLSEKCCIFDNP 148
Cdd:cd11301   8 AGGLGNQLFQYAFLRALAKKLGRRKLFLDTSGYFERNLLKLLEFFNISLPILsrKEILLLKNLRLLNEDPVLKKLLRENY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506 149 DKFNNISSEYLHLT----GHFYQSWKYFDKYKEKVQSFVKPAIDFSPLPNSdssnfisrICIHIRRTDFV-----DGQHH 219
Cdd:cd11301  88 RHYLGRYYQFWKYFysikGEIRQEFKFFEDLEEENNKILKKLKEELKNTNS--------VSVHIRRGDYLtngnaKGYHG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506 220 SSNVSFIKPALEFIKEReqkdvNKKMLTVIMGDDPDFEAKMFegtvrakkeAKIEETTKYFVSENTPQ-DDLAYSHYsCD 298
Cdd:cd11301 160 ICDLEYYKKAIEYIKEK-----VKNPVFFVFSDDIEWVKENL---------ALTSKENVYFVDGNNSSyEDLYLMSL-CK 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 25149506 299 ATLITapSSTFGWWLGYLSKGQAVYYqdIRSTNDVNYKKGVLDPD 343
Cdd:cd11301 225 HVIIS--NSTFSWWGAYLNKNPDKIV--IIAPNPWFVKKKLFPPD 265
Glyco_transf_11 pfam01531
Glycosyl transferase family 11; This family contains several fucosyl transferase enzymes.
73-338 9.46e-10

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


Pssm-ID: 250689  Cd Length: 298  Bit Score: 59.11  E-value: 9.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506    73 RLANHIFELVSVYGMAKSLNRKPAIFVEDSKYnllitgvrkvlpglLDEFQIFeYPVHNKATKV--PLSEKccifdnpdK 150
Cdd:pfam01531  40 RLGNQMGQYSTLIALAPLNGRLAFIPASMHST--------------LAPFRIT-LPVLHSTTASrkPWQNY--------H 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506   151 FNNISSE-YLHLTGHFYQ------SWKYF---------------DKYKEKVQSFVKPAIDFSPLPNSDSsnfisrICIHI 208
Cdd:pfam01531  97 LNDWMEEeYRHLRGEYVKftgypcSWTFYhhglrqeilyeftlhDHLREEIQNFLRGLQVNLGSRPSTF------VGVHI 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25149506   209 RRTDFVD-----GQHHSSNVSFIKPALEFIKEREQKDVnkkmlTVIMGDDPDFeakmfegtvrAKKEAKIEETTKYFVSE 283
Cdd:pfam01531 171 RRGDYVDvmpkvWKGVVADINYLIQALDWFRARYSSPV-----FVVFSDDMEW----------CKKNIDTSCGDVYFAGD 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25149506   284 NTPQDDLAYSHySCDATLITapSSTFGWWLGYLSKGQAVY------YQDIRSTNDVNYKKG 338
Cdd:pfam01531 236 GSPAEDFALLM-QCNHTILS--ISTFSWWAAYLTGGDTIYlanfnlPDSEFLKKEAAYLPE 293
 
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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