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Conserved domains on  [gi|768020476|ref|XP_011527811|]
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GDP-fucose protein O-fucosyltransferase 2 isoform X11 [Homo sapiens]

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 ...
 45-301 3.24e-107

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 cd11298:

Pssm-ID: 450121  Cd Length: 374  Bit Score: 316.52  E-value: 3.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020476  45 YLLYDVNPPEGFNLRRDVYIRIASLLKTLLK---TEEWVLVLPPWGRLYHWQSPDIHQVRIPWSEFFDLPSLNKNIPVIE 121
Cdd:cd11298    1 YLLYDVNPGEGFNLRRDVYIRVANLVKSLNKrgkEQDWVLVLPPWGRLYHWKSRDIKQSRLPWSLFFDLESLNRYIPVIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020476 122 YEQFIagrrtacgvcfvvsqcsardKESGGPFIDQVYVLQSYAEGWKEGTWEEKVDERPCIDQLLYSQDKHEYYrdgglv 201
Cdd:cd11298   81 YEEFL--------------------KETGPVSIDILYYLQHYAEGWEKGKWEDKLEERSCIIEPVYSKDCDGKY------ 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020476 202 spkcrlplkaltlpgllwkscqltasmcpvpgqlalkhgRGWFWGYEETRGLNVSCLSVQGSASIVAPLLLRNTSARSVM 281
Cdd:cd11298  135 ---------------------------------------RGWFWGYCEVTARKFSCLSFQGSASYLAPSLLENKFLRSIM 175

                        250       260
                 ....*....|....*....|
gi 768020476 282 LDRAENLLHDHYGGKEYWDL 301
Cdd:cd11298  176 IDRAEVLLHDHYGILDYWNA 195
 
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 ...
 45-301 3.24e-107

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: 316.52  E-value: 3.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020476  45 YLLYDVNPPEGFNLRRDVYIRIASLLKTLLK---TEEWVLVLPPWGRLYHWQSPDIHQVRIPWSEFFDLPSLNKNIPVIE 121
Cdd:cd11298    1 YLLYDVNPGEGFNLRRDVYIRVANLVKSLNKrgkEQDWVLVLPPWGRLYHWKSRDIKQSRLPWSLFFDLESLNRYIPVIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020476 122 YEQFIagrrtacgvcfvvsqcsardKESGGPFIDQVYVLQSYAEGWKEGTWEEKVDERPCIDQLLYSQDKHEYYrdgglv 201
Cdd:cd11298   81 YEEFL--------------------KETGPVSIDILYYLQHYAEGWEKGKWEDKLEERSCIIEPVYSKDCDGKY------ 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020476 202 spkcrlplkaltlpgllwkscqltasmcpvpgqlalkhgRGWFWGYEETRGLNVSCLSVQGSASIVAPLLLRNTSARSVM 281
Cdd:cd11298  135 ---------------------------------------RGWFWGYCEVTARKFSCLSFQGSASYLAPSLLENKFLRSIM 175

                        250       260
                 ....*....|....*....|
gi 768020476 282 LDRAENLLHDHYGGKEYWDL 301
Cdd:cd11298  176 IDRAEVLLHDHYGILDYWNA 195
O-FucT pfam10250
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing ...
 45-109 1.40e-14

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: 71.95  E-value: 1.40e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768020476   45 YLLYDvnPPEG-FNLRRDVYIRIASLLKTLLKTeewvLVLPPWGRLYHWQSPDIhqVRIPWSEFFD 109
Cdd:pfam10250   1 YLLYC--PCNGgFNQQRDHICDAVAFARLLNAT----LVLPPWDQLYHWRDPST--DQIPFSDIFD 58
 
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 ...
 45-301 3.24e-107

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: 316.52  E-value: 3.24e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020476  45 YLLYDVNPPEGFNLRRDVYIRIASLLKTLLK---TEEWVLVLPPWGRLYHWQSPDIHQVRIPWSEFFDLPSLNKNIPVIE 121
Cdd:cd11298    1 YLLYDVNPGEGFNLRRDVYIRVANLVKSLNKrgkEQDWVLVLPPWGRLYHWKSRDIKQSRLPWSLFFDLESLNRYIPVIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020476 122 YEQFIagrrtacgvcfvvsqcsardKESGGPFIDQVYVLQSYAEGWKEGTWEEKVDERPCIDQLLYSQDKHEYYrdgglv 201
Cdd:cd11298   81 YEEFL--------------------KETGPVSIDILYYLQHYAEGWEKGKWEDKLEERSCIIEPVYSKDCDGKY------ 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020476 202 spkcrlplkaltlpgllwkscqltasmcpvpgqlalkhgRGWFWGYEETRGLNVSCLSVQGSASIVAPLLLRNTSARSVM 281
Cdd:cd11298  135 ---------------------------------------RGWFWGYCEVTARKFSCLSFQGSASYLAPSLLENKFLRSIM 175

                        250       260
                 ....*....|....*....|
gi 768020476 282 LDRAENLLHDHYGGKEYWDL 301
Cdd:cd11298  176 IDRAEVLLHDHYGILDYWNA 195
O-FucT pfam10250
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing ...
 45-109 1.40e-14

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: 71.95  E-value: 1.40e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768020476   45 YLLYDvnPPEG-FNLRRDVYIRIASLLKTLLKTeewvLVLPPWGRLYHWQSPDIhqVRIPWSEFFD 109
Cdd:pfam10250   1 YLLYC--PCNGgFNQQRDHICDAVAFARLLNAT----LVLPPWDQLYHWRDPST--DQIPFSDIFD 58
O-FucT-1 cd11302
GDP-fucose protein O-fucosyltransferase 1; The protein O-fucosyltransferase 1 (Ofut1 or ...
 80-156 8.97e-04

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: 40.29  E-value: 8.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768020476  80 VLVLPPWGRLYHWQSPDIHqvrIPWSEFFDLPSLNKNIPVIEYEQFI---------AGRRTacGVCFVV------SQCSA 144
Cdd:cd11302   35 TLVLPPWIEYRHGPPPSVQ---IPFDDYFKVEPLQEYHRVITMEDFMeelaptiwpPGKRK--GYCYSPraspdsKDCPM 109

                         90
                 ....*....|..
gi 768020476 145 RDKESGGPFIDQ 156
Cdd:cd11302  110 KEGNPFGPFWDH 121
 
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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