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Conserved domains on  [gi|392896416|ref|NP_001255069|]
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Uncharacterized protein CELE_K10G9.3 [Caenorhabditis elegans]

Protein Classification

O-FucT-2 domain-containing protein (domain architecture ID 10181941)

O-FucT-2 domain-containing protein

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 ...
43-411 0e+00

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: 551.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416  43 FLLYDVNFGEGFNLRRDVYMRVANTVRSLRDSG--ENYILVLPPWGRLHHWKRM---EVALSWRLFFDLESLNRFIPVIE 117
Cdd:cd11298    1 YLLYDVNPGEGFNLRRDVYIRVANLVKSLNKRGkeQDWVLVLPPWGRLYHWKSRdikQSRLPWSLFFDLESLNRYIPVIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 118 FEDFLDETENRPIDQVIYLQHYAEGW-GTEYVRKFEKRSCLPpaESHYKQVEEFKWKGWFYSYEDVYSRNFQCVSIQGDS 196
Cdd:cd11298   81 YEEFLKETGPVSIDILYYLQHYAEGWeKGKWEDKLEERSCII--EPVYSKDCDGKYRGWFWGYCEVTARKFSCLSFQGSA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 197 GTLKDLLKHSNFSesTSIMVDRAETILHEHYGEVDYWKARRSMRYSNDLVDVADAFRKKYLDSDDKRDKTKLVDDWTKEK 276
Cdd:cd11298  159 SYLAPSLLENKFL--RSIMIDRAEVLLHDHYGILDYWNARRSMRFAKHLRDIANEFRKEYLNSTDESDKTVRPEWWRMKK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 277 PRRTAIGGPYLGIHWRRRDFLYARRAQLPTIPGTAKILQDLCKKLDLQKIYLATDAPDQEVDELKALLnGELEVYRFTDT 356
Cdd:cd11298  237 KKGSALGGPYLAVHLRRGDFVYGRKKDVPSLKGAAKQILNLMKKLKLKKVFIATDAKKEELEELKKLL-KKLKVVRYEPT 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896416 357 ----QKLNDGQIAIIDQYLCAHAAYFIGSYESTFTFRIQEDREIIGFPISTTFNRLCPD 411
Cdd:cd11298  316 leelEKLKDGGVAIIDQWICAHARYFIGTKESTFSFRIQEEREILGFPPDTTFNRLCGD 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 ...
43-411 0e+00

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: 551.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416  43 FLLYDVNFGEGFNLRRDVYMRVANTVRSLRDSG--ENYILVLPPWGRLHHWKRM---EVALSWRLFFDLESLNRFIPVIE 117
Cdd:cd11298    1 YLLYDVNPGEGFNLRRDVYIRVANLVKSLNKRGkeQDWVLVLPPWGRLYHWKSRdikQSRLPWSLFFDLESLNRYIPVIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 118 FEDFLDETENRPIDQVIYLQHYAEGW-GTEYVRKFEKRSCLPpaESHYKQVEEFKWKGWFYSYEDVYSRNFQCVSIQGDS 196
Cdd:cd11298   81 YEEFLKETGPVSIDILYYLQHYAEGWeKGKWEDKLEERSCII--EPVYSKDCDGKYRGWFWGYCEVTARKFSCLSFQGSA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 197 GTLKDLLKHSNFSesTSIMVDRAETILHEHYGEVDYWKARRSMRYSNDLVDVADAFRKKYLDSDDKRDKTKLVDDWTKEK 276
Cdd:cd11298  159 SYLAPSLLENKFL--RSIMIDRAEVLLHDHYGILDYWNARRSMRFAKHLRDIANEFRKEYLNSTDESDKTVRPEWWRMKK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 277 PRRTAIGGPYLGIHWRRRDFLYARRAQLPTIPGTAKILQDLCKKLDLQKIYLATDAPDQEVDELKALLnGELEVYRFTDT 356
Cdd:cd11298  237 KKGSALGGPYLAVHLRRGDFVYGRKKDVPSLKGAAKQILNLMKKLKLKKVFIATDAKKEELEELKKLL-KKLKVVRYEPT 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896416 357 ----QKLNDGQIAIIDQYLCAHAAYFIGSYESTFTFRIQEDREIIGFPISTTFNRLCPD 411
Cdd:cd11298  316 leelEKLKDGGVAIIDQWICAHARYFIGTKESTFSFRIQEEREILGFPPDTTFNRLCGD 374
O-FucT pfam10250
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing ...
43-396 1.33e-31

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 characteristic 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: 313476  Cd Length: 251  Bit Score: 121.98  E-value: 1.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416   43 FLLYDVNfGeGFNLRRDVYMRVANTVRSLrdsgeNYILVLPPWGRLHHWKRMEVALSWRLFFDLESlnrFIPviefedfl 122
Cdd:pfam10250   1 YLLYPCN-G-GFNQQRDVICDAVAVARLL-----NATLVLPPWDKLYHWKDPSSFLPFSDIFDEDH---FIE-------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416  123 detenrpidqviYLQHyaegwgteyvrkfekrsclppaeshykqveefkwkgwfysyedvysrnFQCVSIQGDsgtlkdl 202
Cdd:pfam10250  63 ------------SLQR------------------------------------------------LRCRSKQGP------- 75
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416  203 lkhsnfsestsimvdraetilhehygevdYWKARRSMRYSNDLVDVADAFRKKYLDsddkrdktklvddwtkekprrtai 282
Cdd:pfam10250  76 -----------------------------FWVNFHALRFSPEIQELGDKLVRRLRK------------------------ 102
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416  283 GGPYLGIHWRR-RDFLYA-------------------------------RRAQLPTIPGTAKILQDLCKKldlQKIYLAT 330
Cdd:pfam10250 103 KGPYLALHLRReKDMLAFsgcaygggdeeaeelqidpeerrrnglcpltPEECLPSLVGLLLQALGFPKK---TSIYIAT 179
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896416  331 DAP--DQEVDELKALLngELEVYRFT-----DTQKLNDGQIAIIDQYLCAHAAYFIGSYESTFTFRIQEDREI 396
Cdd:pfam10250 180 DEIygGERLAPLKSLF--PNLVTKETlaspeELEPFKDGSSAALDYIVCLHSDVFIGTCVSNFSKFVQGERRY 250
 
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 ...
43-411 0e+00

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: 551.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416  43 FLLYDVNFGEGFNLRRDVYMRVANTVRSLRDSG--ENYILVLPPWGRLHHWKRM---EVALSWRLFFDLESLNRFIPVIE 117
Cdd:cd11298    1 YLLYDVNPGEGFNLRRDVYIRVANLVKSLNKRGkeQDWVLVLPPWGRLYHWKSRdikQSRLPWSLFFDLESLNRYIPVIE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 118 FEDFLDETENRPIDQVIYLQHYAEGW-GTEYVRKFEKRSCLPpaESHYKQVEEFKWKGWFYSYEDVYSRNFQCVSIQGDS 196
Cdd:cd11298   81 YEEFLKETGPVSIDILYYLQHYAEGWeKGKWEDKLEERSCII--EPVYSKDCDGKYRGWFWGYCEVTARKFSCLSFQGSA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 197 GTLKDLLKHSNFSesTSIMVDRAETILHEHYGEVDYWKARRSMRYSNDLVDVADAFRKKYLDSDDKRDKTKLVDDWTKEK 276
Cdd:cd11298  159 SYLAPSLLENKFL--RSIMIDRAEVLLHDHYGILDYWNARRSMRFAKHLRDIANEFRKEYLNSTDESDKTVRPEWWRMKK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 277 PRRTAIGGPYLGIHWRRRDFLYARRAQLPTIPGTAKILQDLCKKLDLQKIYLATDAPDQEVDELKALLnGELEVYRFTDT 356
Cdd:cd11298  237 KKGSALGGPYLAVHLRRGDFVYGRKKDVPSLKGAAKQILNLMKKLKLKKVFIATDAKKEELEELKKLL-KKLKVVRYEPT 315
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896416 357 ----QKLNDGQIAIIDQYLCAHAAYFIGSYESTFTFRIQEDREIIGFPISTTFNRLCPD 411
Cdd:cd11298  316 leelEKLKDGGVAIIDQWICAHARYFIGTKESTFSFRIQEEREILGFPPDTTFNRLCGD 374
O-FucT pfam10250
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing ...
43-396 1.33e-31

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 characteristic 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: 313476  Cd Length: 251  Bit Score: 121.98  E-value: 1.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416   43 FLLYDVNfGeGFNLRRDVYMRVANTVRSLrdsgeNYILVLPPWGRLHHWKRMEVALSWRLFFDLESlnrFIPviefedfl 122
Cdd:pfam10250   1 YLLYPCN-G-GFNQQRDVICDAVAVARLL-----NATLVLPPWDKLYHWKDPSSFLPFSDIFDEDH---FIE-------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416  123 detenrpidqviYLQHyaegwgteyvrkfekrsclppaeshykqveefkwkgwfysyedvysrnFQCVSIQGDsgtlkdl 202
Cdd:pfam10250  63 ------------SLQR------------------------------------------------LRCRSKQGP------- 75
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416  203 lkhsnfsestsimvdraetilhehygevdYWKARRSMRYSNDLVDVADAFRKKYLDsddkrdktklvddwtkekprrtai 282
Cdd:pfam10250  76 -----------------------------FWVNFHALRFSPEIQELGDKLVRRLRK------------------------ 102
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416  283 GGPYLGIHWRR-RDFLYA-------------------------------RRAQLPTIPGTAKILQDLCKKldlQKIYLAT 330
Cdd:pfam10250 103 KGPYLALHLRReKDMLAFsgcaygggdeeaeelqidpeerrrnglcpltPEECLPSLVGLLLQALGFPKK---TSIYIAT 179
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896416  331 DAP--DQEVDELKALLngELEVYRFT-----DTQKLNDGQIAIIDQYLCAHAAYFIGSYESTFTFRIQEDREI 396
Cdd:pfam10250 180 DEIygGERLAPLKSLF--PNLVTKETlaspeELEPFKDGSSAALDYIVCLHSDVFIGTCVSNFSKFVQGERRY 250
O-FucT_like cd11296
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like ...
222-399 8.75e-22

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: 92.87  E-value: 8.75e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 222 ILHEHYGEVdYWKARRSMRYSNDLVDVADAFRKKYLDSDdkrdktklvddwtkekprrtaiGGPYLGIHWRRRDFLYARR 301
Cdd:cd11296   33 VLPLCLACP-IRLVGKHLRFSPEIRKLADRFVRKLLGLP----------------------GGPYLAVHLRRGDFEVECC 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 302 AQ-----------LPTIPGTAKILQDLCKKLDLQKIYLATDapDQEVDELKALLNGELEVYRFTD----------TQKLN 360
Cdd:cd11296   90 HLakwmgeyleecLLSAEEIAEKIKELMAERKLKVVYVATD--EADREELREELRKAGIRVVTKDdlledaelleLEKLD 167
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 392896416 361 DGQIAIIDQYLCAHAAYFIGSYESTFTFRIQEDREIIGF 399
Cdd:cd11296  168 NYLLSLVDQEICSRADVFIGTGFSTFSSNVALLRRWRGK 206
NodZ_like cd11548
Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ; Bradyrhizobium NodZ is an alpha 1, ...
283-387 2.33e-05

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  Cd Length: 287  Bit Score: 45.82  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 283 GGPYLGIHWRRRDFLYARRAQLPTIpgtAKILQDLCKKLDLQK---IYLATDapDQEV-DELKALLNGELEVYRF----- 353
Cdd:cd11548  164 GRPTIGVHIRTTDHKDSLFIKLSPL---HRVVDALRKKVALHKdatIFLATD--SAEVkDELKRLFPDVVVTPKEfpphg 238
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 392896416 354 --TDTQKLNDGQIAIIDQYLCAHAAYFIGSYESTFT 387
Cdd:cd11548  239 erSASDGLEGAEDALIDMYLLARCDHLIGSRFSTFS 274
O-FucT-1 cd11302
GDP-fucose protein O-fucosyltransferase 1; The protein O-fucosyltransferase 1 (Ofut1 or ...
237-405 1.01e-03

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: 40.68  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 237 RSMRYSNDLVDVADAFRKKYLDsddkrdktklvddwtkekprrtaigGPYLGIH------WRR---------RDFL---- 297
Cdd:cd11302  180 KYLEWSDEIVKEADEFINENLP-------------------------RPFVGIHlrngidWKNacehvkgtsRNLMaspq 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896416 298 ---YARRAQLPT----IPGTAKILQDL---CKKLDLQKIYLATDApDQEVDELKALL-NGELEVYRFtdtqklnDGQIAI 366
Cdd:cd11302  235 clgYGNERGTLTkemcLPSKEEILKQVkraVKKIKAKSVFIATDN-DHMIEELKKALkSLKVKVVHL-------DPDEPQ 306
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 392896416 367 IDQYLCAHAAYFIGSYESTFTFRIQEDREIIGFPisTTF 405
Cdd:cd11302  307 IDLAILGKADHFIGNCVSSFSAFVKRERDVAGLP--SSF 343
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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