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Conserved domains on  [gi|768020478|ref|XP_011527812|]
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GDP-fucose protein O-fucosyltransferase 2 isoform X12 [Homo sapiens]

Protein Classification

GDP-fucose protein O-fucosyltransferase 2( domain architecture ID 10181941)

GDP-fucose protein O-fucosyltransferase 2 (POFUT2) catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively

CATH:  3.40.50.11350|3.40.50.11340
CAZY:  GT68
EC:  2.4.1.221
Gene Ontology:  GO:0016757|GO:0046922|GO:0036066|GO:1903334|GO:0006004

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
O-FucT-2 cd11298
GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 ...
 12-252 5.24e-149

GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 repeats (TSRs), and appears conserved in bilateria. The O-fucosylation of TSRs appears to play a role in regulating secretion of metalloproteases of the ADAMTS superfamily. 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: 211384  Cd Length: 374  Bit Score: 421.29  E-value: 5.24e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478  12 HGRGWFWGYEETRGLNVSCLSVQGSASIVAPLLLRNTSARSVMLDRAENLLHDHYGGKEYWDTRRSMVFARHLREVGDEF 91
Cdd:cd11298  133 KYRGWFWGYCEVTARKFSCLSFQGSASYLAPSLLENKFLRSIMIDRAEVLLHDHYGILDYWNARRSMRFAKHLRDIANEF 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478  92 RSRHLNSTDDADRIPFQEDWmKMKVKLGSALGGPYLGVHLRRKDFIWGHRQDVPSLEGAVRKIRSLMKTHRLDKVFVATD 171
Cdd:cd11298  213 RKEYLNSTDESDKTVRPEWW-RMKKKKGSALGGPYLAVHLRRGDFVYGRKKDVPSLKGAAKQILNLMKKLKLKKVFIATD 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478 172 AVRKEYEELKKLL--PEMVRFEPTWEELELYKDGGVAIIDQWICAHARFFIGTSVSTFSFRIHEEREILGLDPKTTYNRF 249
Cdd:cd11298  292 AKKEELEELKKLLkkLKVVRYEPTLEELEKLKDGGVAIIDQWICAHARYFIGTKESTFSFRIQEEREILGFPPDTTFNRL 371


                 ...
gi 768020478 250 CGD 252
Cdd:cd11298  372 CGD 374
 
Name Accession Description Interval E-value
O-FucT-2 cd11298
GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 ...
 12-252 5.24e-149

GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 repeats (TSRs), and appears conserved in bilateria. The O-fucosylation of TSRs appears to play a role in regulating secretion of metalloproteases of the ADAMTS superfamily. 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: 211384  Cd Length: 374  Bit Score: 421.29  E-value: 5.24e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478  12 HGRGWFWGYEETRGLNVSCLSVQGSASIVAPLLLRNTSARSVMLDRAENLLHDHYGGKEYWDTRRSMVFARHLREVGDEF 91
Cdd:cd11298  133 KYRGWFWGYCEVTARKFSCLSFQGSASYLAPSLLENKFLRSIMIDRAEVLLHDHYGILDYWNARRSMRFAKHLRDIANEF 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478  92 RSRHLNSTDDADRIPFQEDWmKMKVKLGSALGGPYLGVHLRRKDFIWGHRQDVPSLEGAVRKIRSLMKTHRLDKVFVATD 171
Cdd:cd11298  213 RKEYLNSTDESDKTVRPEWW-RMKKKKGSALGGPYLAVHLRRGDFVYGRKKDVPSLKGAAKQILNLMKKLKLKKVFIATD 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478 172 AVRKEYEELKKLL--PEMVRFEPTWEELELYKDGGVAIIDQWICAHARFFIGTSVSTFSFRIHEEREILGLDPKTTYNRF 249
Cdd:cd11298  292 AKKEELEELKKLLkkLKVVRYEPTLEELEKLKDGGVAIIDQWICAHARYFIGTKESTFSFRIQEEREILGFPPDTTFNRL 371


                 ...
gi 768020478 250 CGD 252
Cdd:cd11298  372 CGD 374
O-FucT pfam10250
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing ...
 71-238 7.08e-38

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: 133.19  E-value: 7.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478   71 YWDTRRSMVFARHLREVGDEFRSRHLNstddadripfqedwmkmkvklgsalgGPYLGVHLRR-KDFI--WGHRQD---- 143
Cdd:pfam10250  75 FWVNFHALRFSPEIEELGDKLVDRLLK--------------------------GPYLALHLRReKDMLaaSGCAEGggde 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478  144 ----------------------VPSLEGAVRKIRSLMKTHRldKVFVATDAVRKEYE--ELKKLLPEMVRFE--PTWEEL 197
Cdd:pfam10250 129 eaeedpeerrrnglcpltpeecLPSLVGILLQALGFVKKLT--RIYVATDEIYGGEElaPLKSMFPNLVTKEslASVEEL 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 768020478  198 ELYKDGGVAIIDQWICAHARFFIGTSVSTFSFRIHEEREIL 238
Cdd:pfam10250 207 EPFKDGSSAALDYIICLHSDVFIGTCVSNFSAFVKGERRYL 247
 
Name Accession Description Interval E-value
O-FucT-2 cd11298
GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 ...
 12-252 5.24e-149

GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 repeats (TSRs), and appears conserved in bilateria. The O-fucosylation of TSRs appears to play a role in regulating secretion of metalloproteases of the ADAMTS superfamily. 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: 211384  Cd Length: 374  Bit Score: 421.29  E-value: 5.24e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478  12 HGRGWFWGYEETRGLNVSCLSVQGSASIVAPLLLRNTSARSVMLDRAENLLHDHYGGKEYWDTRRSMVFARHLREVGDEF 91
Cdd:cd11298  133 KYRGWFWGYCEVTARKFSCLSFQGSASYLAPSLLENKFLRSIMIDRAEVLLHDHYGILDYWNARRSMRFAKHLRDIANEF 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478  92 RSRHLNSTDDADRIPFQEDWmKMKVKLGSALGGPYLGVHLRRKDFIWGHRQDVPSLEGAVRKIRSLMKTHRLDKVFVATD 171
Cdd:cd11298  213 RKEYLNSTDESDKTVRPEWW-RMKKKKGSALGGPYLAVHLRRGDFVYGRKKDVPSLKGAAKQILNLMKKLKLKKVFIATD 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478 172 AVRKEYEELKKLL--PEMVRFEPTWEELELYKDGGVAIIDQWICAHARFFIGTSVSTFSFRIHEEREILGLDPKTTYNRF 249
Cdd:cd11298  292 AKKEELEELKKLLkkLKVVRYEPTLEELEKLKDGGVAIIDQWICAHARYFIGTKESTFSFRIQEEREILGFPPDTTFNRL 371


                 ...
gi 768020478 250 CGD 252
Cdd:cd11298  372 CGD 374
O-FucT pfam10250
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing ...
 71-238 7.08e-38

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: 133.19  E-value: 7.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478   71 YWDTRRSMVFARHLREVGDEFRSRHLNstddadripfqedwmkmkvklgsalgGPYLGVHLRR-KDFI--WGHRQD---- 143
Cdd:pfam10250  75 FWVNFHALRFSPEIEELGDKLVDRLLK--------------------------GPYLALHLRReKDMLaaSGCAEGggde 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478  144 ----------------------VPSLEGAVRKIRSLMKTHRldKVFVATDAVRKEYE--ELKKLLPEMVRFE--PTWEEL 197
Cdd:pfam10250 129 eaeedpeerrrnglcpltpeecLPSLVGILLQALGFVKKLT--RIYVATDEIYGGEElaPLKSMFPNLVTKEslASVEEL 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 768020478  198 ELYKDGGVAIIDQWICAHARFFIGTSVSTFSFRIHEEREIL 238
Cdd:pfam10250 207 EPFKDGSSAALDYIICLHSDVFIGTCVSNFSAFVKGERRYL 247
O-FucT_like cd11296
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like ...
 71-240 3.20e-28

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: 107.12  E-value: 3.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478  71 YWDTRRSMVFARHLREVGDEFRSrhlnstddadripfqedwmkmkvKLGSALGGPYLGVHLRRKDFIWGHRQD------- 143
Cdd:cd11296   42 IRLVGKHLRFSPEIRKLADRFVR-----------------------KLLGLPGGPYLAVHLRRGDFEVECCHLakwmgey 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478 144 ----VPSLEGAVRKIRSLMKTHRLDKVFVATDAVRKEY--EELKKLLPEMVRFEPTWEELELYKD-----GGVAIIDQWI 212
Cdd:cd11296   99 leecLLSAEEIAEKIKELMAERKLKVVYVATDEADREElrEELRKAGIRVVTKDDLLEDAELLELekldnYLLSLVDQEI 178

                        170       180
                 ....*....|....*....|....*...
gi 768020478 213 CAHARFFIGTSVSTFSFRIHEEREILGL 240
Cdd:cd11296  179 CSRADVFIGTGFSTFSSNVALLRRWRGK 206
O-FucT-1 cd11302
GDP-fucose protein O-fucosyltransferase 1; The protein O-fucosyltransferase 1 (Ofut1 or ...
 122-240 1.66e-06

GDP-fucose protein O-fucosyltransferase 1; The protein O-fucosyltransferase 1 (Ofut1 or O-FucT-1) adds O-fucose to EGF (epidermal growth factor-like) repeats. The O-fucsosylation of the Notch receptor signaling protein is dependent on this enzyme, which requires GDP-fucose as a substrate. O-fucose residues added to the target of O-FucT-1 may be further elongated by other glycosyltransferases. On top of O-fucosylation, O-FucT-1 may have other functions such as the regulation of the Notch receptor exit from the ER. Six highly conserved cysteines are present in O-FucT-1, which is a soluble ER protein, as well as a DXD-like motif (ERD), conserved in mammals, Drosophila, and C. elegans. Both features are characteristic of several glycosyltransferase families. The membrane-bound pre-protein is released by proteolysis and, as for most glycosyltransferases, is strongly activated by manganese. O-FucT-1 is similar to family 1 glycosyltransferases (GT1).


Pssm-ID: 211388  Cd Length: 347  Bit Score: 48.38  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478 122 LGGPYLGVHLRR-----------KDFIW------------GHRQDV------PSLEGAVRKIRSLMKTHRLDKVFVATDA 172
Cdd:cd11302  200 LPRPFVGIHLRNgidwknacehvKGTSRnlmaspqclgygNERGTLtkemclPSKEEILKQVKRAVKKIKAKSVFIATDN 279

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768020478 173 VRKEyEELKKLLPemvrfeptWEELELYK-DGGVAIIDQWICAHARFFIGTSVSTFSFRIHEEREILGL 240
Cdd:cd11302  280 DHMI-EELKKALK--------SLKVKVVHlDPDEPQIDLAILGKADHFIGNCVSSFSAFVKRERDVAGL 339
NodZ_like cd11548
Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ; Bradyrhizobium NodZ is an alpha 1, ...
 123-228 9.05e-06

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: 45.82  E-value: 9.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020478 123 GGPYLGVHLRRKDfiwGHRQDVPSLEGAVRKIRSLMKTHRLDK---VFVATDAVRKEyEELKKLLPEMV----RFEPTWE 195
Cdd:cd11548  164 GRPTIGVHIRTTD---HKDSLFIKLSPLHRVVDALRKKVALHKdatIFLATDSAEVK-DELKRLFPDVVvtpkEFPPHGE 239

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 768020478 196 ELEL-YKDGGV-AIIDQWICAHARFFIGTSVSTFS 228
Cdd:cd11548  240 RSASdGLEGAEdALIDMYLLARCDHLIGSRFSTFS 274
 
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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