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Conserved domains on  [gi|62510630|sp|Q866C9|]
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RecName: Full=Galactoside alpha-(1,2)-fucosyltransferase 1; AltName: Full=Alpha(1,2)FT 1; AltName: Full=Fucosyltransferase 1; AltName: Full=GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1; AltName: Full=Type 1 galactoside alpha-(1,2)-fucosyltransferase FUT1; AltName: Full=Type 2 galactoside alpha-(1,2)-fucosyltransferase FUT1

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_transf_11 pfam01531
Glycosyl transferase family 11; This family contains several fucosyl transferase enzymes.
38-354 1.30e-158

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


:

Pssm-ID: 250689  Cd Length: 298  Bit Score: 446.62  E-value: 1.30e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630    38 GLSVLCPDRRLVTHPVAIFCLPgtpmspntsspcPQHAASLSGTWTIYPDGRFGNQMGQYATLLALAQLNGRQAFILPAM 117
Cdd:pfam01531   1 MVSVLFHGNLGNQLFQAAWALK------------PQHLPSLIGMFTVNLNGRLGNQMGQYSTLIALAPLNGRLAFIPASM 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630   118 HAALAPvFRITLPVLAPEVDSRTPWRELRLHDWMSEEYADLGDPFLKLSGFPCSWTFFHH-LREQIRSEFTLHDHLREEA 196
Cdd:pfam01531  69 HSTLAP-FRITLPVLHSTTASRKPWQNYHLNDWMEEEYRHLRGEYVKFTGYPCSWTFYHHgLRQEILYEFTLHDHLREEI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630   197 QSVLRRLHLGrSGDRPRTFVGVHVRRGDYLQVMPQRWRGVVGNSAYLREAMDWFRARHEAPVFVVTSNGMEWCRENIDAS 276
Cdd:pfam01531 148 QNFLRGLQVN-LGSRPSTFVGVHIRRGDYVDVMPKVWKGVVADINYLIQALDWFRARYSSPVFVVFSDDMEWCKKNIDTS 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62510630   277 KGDVVFAGDGqeaSPWKDFALLTQCNHTIMTIGTFGFWAAYLAGGDTVYLANFTLPDSEFLkifKPEAAFLPEWVGIN 354
Cdd:pfam01531 227 CGDVYFAGDG---SPAEDFALLMQCNHTILSISTFSWWAAYLTGGDTIYLANFNLPDSEFL---KKEAAYLPEWVYIA 298
 
Name Accession Description Interval E-value
Glyco_transf_11 pfam01531
Glycosyl transferase family 11; This family contains several fucosyl transferase enzymes.
38-354 1.30e-158

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


Pssm-ID: 250689  Cd Length: 298  Bit Score: 446.62  E-value: 1.30e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630    38 GLSVLCPDRRLVTHPVAIFCLPgtpmspntsspcPQHAASLSGTWTIYPDGRFGNQMGQYATLLALAQLNGRQAFILPAM 117
Cdd:pfam01531   1 MVSVLFHGNLGNQLFQAAWALK------------PQHLPSLIGMFTVNLNGRLGNQMGQYSTLIALAPLNGRLAFIPASM 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630   118 HAALAPvFRITLPVLAPEVDSRTPWRELRLHDWMSEEYADLGDPFLKLSGFPCSWTFFHH-LREQIRSEFTLHDHLREEA 196
Cdd:pfam01531  69 HSTLAP-FRITLPVLHSTTASRKPWQNYHLNDWMEEEYRHLRGEYVKFTGYPCSWTFYHHgLRQEILYEFTLHDHLREEI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630   197 QSVLRRLHLGrSGDRPRTFVGVHVRRGDYLQVMPQRWRGVVGNSAYLREAMDWFRARHEAPVFVVTSNGMEWCRENIDAS 276
Cdd:pfam01531 148 QNFLRGLQVN-LGSRPSTFVGVHIRRGDYVDVMPKVWKGVVADINYLIQALDWFRARYSSPVFVVFSDDMEWCKKNIDTS 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62510630   277 KGDVVFAGDGqeaSPWKDFALLTQCNHTIMTIGTFGFWAAYLAGGDTVYLANFTLPDSEFLkifKPEAAFLPEWVGIN 354
Cdd:pfam01531 227 CGDVYFAGDG---SPAEDFALLMQCNHTILSISTFSWWAAYLTGGDTIYLANFNLPDSEFL---KKEAAYLPEWVYIA 298
Fut1_Fut2_like cd11301
Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer ...
88-342 3.93e-65

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: 207.70  E-value: 3.93e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630  88 GRFGNQMGQYATLLALAQ-LNGRQAFILPAMH-----AALAPVFRITLPVLAPEVDSRTPW-----RELRLHDWMSEEYA 156
Cdd:cd11301   9 GGLGNQLFQYAFLRALAKkLGRRKLFLDTSGYfernlLKLLEFFNISLPILSRKEILLLKNlrllnEDPVLKKLLRENYR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630 157 DLGDPFLKlsgfpcSWTFFHHLREQIRSEFTLHDHLREEAQSVLRRLhlgRSGDRPRTFVGVHVRRGDYLQVMPQRWRGV 236
Cdd:cd11301  89 HYLGRYYQ------FWKYFYSIKGEIRQEFKFFEDLEEENNKILKKL---KEELKNTNSVSVHIRRGDYLTNGNAKGYHG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630 237 VGNSAYLREAMDWFRARHEAPVFVVTSNGMEWCRENI-DASKGDVVFAgdGQEASPWKDFALLTQCNHTIMTIGTFGFWA 315
Cdd:cd11301 160 ICDLEYYKKAIEYIKEKVKNPVFFVFSDDIEWVKENLaLTSKENVYFV--DGNNSSYEDLYLMSLCKHVIISNSTFSWWG 237
                       250       260
                ....*....|....*....|....*..
gi 62510630 316 AYLAGGDTVYLANFTLPDSEFLKIFKP 342
Cdd:cd11301 238 AYLNKNPDKIVIIAPNPWFVKKKLFPP 264
 
Name Accession Description Interval E-value
Glyco_transf_11 pfam01531
Glycosyl transferase family 11; This family contains several fucosyl transferase enzymes.
38-354 1.30e-158

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


Pssm-ID: 250689  Cd Length: 298  Bit Score: 446.62  E-value: 1.30e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630    38 GLSVLCPDRRLVTHPVAIFCLPgtpmspntsspcPQHAASLSGTWTIYPDGRFGNQMGQYATLLALAQLNGRQAFILPAM 117
Cdd:pfam01531   1 MVSVLFHGNLGNQLFQAAWALK------------PQHLPSLIGMFTVNLNGRLGNQMGQYSTLIALAPLNGRLAFIPASM 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630   118 HAALAPvFRITLPVLAPEVDSRTPWRELRLHDWMSEEYADLGDPFLKLSGFPCSWTFFHH-LREQIRSEFTLHDHLREEA 196
Cdd:pfam01531  69 HSTLAP-FRITLPVLHSTTASRKPWQNYHLNDWMEEEYRHLRGEYVKFTGYPCSWTFYHHgLRQEILYEFTLHDHLREEI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630   197 QSVLRRLHLGrSGDRPRTFVGVHVRRGDYLQVMPQRWRGVVGNSAYLREAMDWFRARHEAPVFVVTSNGMEWCRENIDAS 276
Cdd:pfam01531 148 QNFLRGLQVN-LGSRPSTFVGVHIRRGDYVDVMPKVWKGVVADINYLIQALDWFRARYSSPVFVVFSDDMEWCKKNIDTS 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62510630   277 KGDVVFAGDGqeaSPWKDFALLTQCNHTIMTIGTFGFWAAYLAGGDTVYLANFTLPDSEFLkifKPEAAFLPEWVGIN 354
Cdd:pfam01531 227 CGDVYFAGDG---SPAEDFALLMQCNHTILSISTFSWWAAYLTGGDTIYLANFNLPDSEFL---KKEAAYLPEWVYIA 298
Fut1_Fut2_like cd11301
Alpha-1,2-fucosyltransferase; Alpha-1,2-fucosyltransferases (Fut1, Fut2) catalyze the transfer ...
88-342 3.93e-65

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: 207.70  E-value: 3.93e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630  88 GRFGNQMGQYATLLALAQ-LNGRQAFILPAMH-----AALAPVFRITLPVLAPEVDSRTPW-----RELRLHDWMSEEYA 156
Cdd:cd11301   9 GGLGNQLFQYAFLRALAKkLGRRKLFLDTSGYfernlLKLLEFFNISLPILSRKEILLLKNlrllnEDPVLKKLLRENYR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630 157 DLGDPFLKlsgfpcSWTFFHHLREQIRSEFTLHDHLREEAQSVLRRLhlgRSGDRPRTFVGVHVRRGDYLQVMPQRWRGV 236
Cdd:cd11301  89 HYLGRYYQ------FWKYFYSIKGEIRQEFKFFEDLEEENNKILKKL---KEELKNTNSVSVHIRRGDYLTNGNAKGYHG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630 237 VGNSAYLREAMDWFRARHEAPVFVVTSNGMEWCRENI-DASKGDVVFAgdGQEASPWKDFALLTQCNHTIMTIGTFGFWA 315
Cdd:cd11301 160 ICDLEYYKKAIEYIKEKVKNPVFFVFSDDIEWVKENLaLTSKENVYFV--DGNNSSYEDLYLMSLCKHVIISNSTFSWWG 237
                       250       260
                ....*....|....*....|....*..
gi 62510630 316 AYLAGGDTVYLANFTLPDSEFLKIFKP 342
Cdd:cd11301 238 AYLNKNPDKIVIIAPNPWFVKKKLFPP 264
O-FucT_like cd11296
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like ...
178-318 3.71e-09

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.


Pssm-ID: 211383  Cd Length: 206  Bit Score: 55.89  E-value: 3.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630 178 LREQIRSEFTLHDHLREEAQSVLRRLHlgrsGDRPRTFVGVHVRRGDYLQVMPQRWRGVVG--------NSAYLREAMDW 249
Cdd:cd11296  41 PIRLVGKHLRFSPEIRKLADRFVRKLL----GLPGGPYLAVHLRRGDFEVECCHLAKWMGEyleecllsAEEIAEKIKEL 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630 250 FRARHEAPVFVVTSNGM-EWCRENIDASKGDVVFAGDGQEASPWK-------------DFALLTQCNHTIMTIG-TFGFW 314
Cdd:cd11296 117 MAERKLKVVYVATDEADrEELREELRKAGIRVVTKDDLLEDAELLelekldnyllslvDQEICSRADVFIGTGFsTFSSN 196

                ....
gi 62510630 315 AAYL 318
Cdd:cd11296 197 VALL 200
O-FucT pfam10250
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing ...
88-226 4.32e-05

GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing the enzyme responsible for adding O-fucose to EGF (epidermal growth factor-like) repeats. Six highly conserved cysteines are present in O-FucT-1 as well as a DXD-like motif (ERD), conserved in mammals, Drosophila, and C. elegans. Both features are characteriztic of several glycosyltransferase families. The enzyme is a membrane-bound protein released by proteolysis and, as for most glycosyltransferases, is strongly activated by manganese.


Pssm-ID: 463023 [Multi-domain]  Cd Length: 247  Bit Score: 44.60  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630    88 GRFGNQMGQYATLLALAQLNGRqafilpamhaalapvfriTLpVLaPEVDSRTPWRElrlHDWMSEEYADLGDPFL---- 163
Cdd:pfam10250   9 GGFNQQRDHICDAVAFARLLNA------------------TL-VL-PPWDQLYHWRD---PSTDQIPFSDIFDEFIeslc 65
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62510630   164 --KLSGFPCSWTFFHHLReqirseFTlhDHLREEAQSVLRRLhlgrsgdRPRTFVGVHVRRG-DYL 226
Cdd:pfam10250  66 rsKQGNFGPFWVNFHALR------FS--PEIEELGDKLVDRL-------LKGPYLALHLRREkDML 116
NodZ_like cd11548
Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ; Bradyrhizobium NodZ is an alpha 1, ...
84-321 7.65e-03

Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ; Bradyrhizobium NodZ is an alpha 1,6-fucosyltransferase involved in the biosynthesis of the nodulation factor, a lipo-chitooligosaccharide formed by three-to-six beta-1,4-linked N-acetyl-d-glucosamine (GlcNAc) residues and a fatty acid acyl group attached to the nitrogen atom at the non-reducing end. NodZ transfers L-fucose from the GDP-beta-L-fucose donor to the reducing residue of the chitin oligosaccharide backbone, before the attachment of a fatty acid group. 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: 211389 [Multi-domain]  Cd Length: 287  Bit Score: 37.73  E-value: 7.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630  84 IYPDGRFGNQMGQYATLLALAQLNGRQAFI-------LPAMHAALaPVFRITL-PVLAPEVDSRTPWRELRLHdWMSEEY 155
Cdd:cd11548   4 FKGRGGLGNRMLALASALELARLTGRTLVIdwrdyeyAPRDENAF-PLLFDPIeDRSIDGLPDRDPRRGTQNI-KGYPQQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630 156 ADLGDPFLKLSG-----------------------------FPCSWTFFHHLREQI----RSEFTLHDHLREEAQSVLRR 202
Cdd:cd11548  82 WIRPTSDLSHRVpaqifrecdeltvldvkgrkavqagylpkLPRDADKLGRDRGIIkcylYRLFTPKQEVRAAVRKLYAK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62510630 203 LHlgrsgdrPRTFVGVHVRRGD--------------YLQVMPQRWRGVVGNSAYL----REAMDWFRARHEAPVFVVTSN 264
Cdd:cd11548 162 LF-------GRPTIGVHIRTTDhkdslfiklsplhrVVDALRKKVALHKDATIFLatdsAEVKDELKRLFPDVVVTPKEF 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62510630 265 GMEWCRENIDASKGdvvfagdGQEAspWKDFALLTQCNHTIMTIG-TFGFWAAYLAGG 321
Cdd:cd11548 235 PPHGERSASDGLEG-------AEDA--LIDMYLLARCDHLIGSRFsTFSRMASILGDF 283
 
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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