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Conserved domains on  [gi|15240670|ref|NP_199853|]
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O-fucosyltransferase family protein [Arabidopsis thaliana]

Protein Classification

O-fucosyltransferase family protein( domain architecture ID 10181896)

O-fucosyltransferase family protein may be involved in glycan metabolism by O-fucosylation of protein substrates

Gene Ontology:  GO:0006004|GO:0016757
PubMed:  12966037|12868606

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
O-FucT_like cd11296
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like ...
 382-540 2.48e-18

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: 83.62  E-value: 2.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240670 382 NHKCKTLIEPSKLILLTAQRFIQTFL---GKNFIALHFRRHGFLKFCNAKSPS---CFYPIPQAAECIARIVERSNGA-- 453
Cdd:cd11296  42 IRLVGKHLRFSPEIRKLADRFVRKLLglpGGPYLAVHLRRGDFEVECCHLAKWmgeYLEECLLSAEEIAEKIKELMAErk 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240670 454 --VIYLSTDAAESETslLQSLVVVDGKIVpLVKRPPRNSAEKWDALLYRHGIEddsqvdAMLDKTICAMSSVFIGASGST 531
Cdd:cd11296 122 lkVVYVATDEADREE--LREELRKAGIRV-VTKDDLLEDAELLELEKLDNYLL------SLVDQEICSRADVFIGTGFST 192


                ....*....
gi 15240670 532 FTEDILRLR 540
Cdd:cd11296 193 FSSNVALLR 201
 
Name Accession Description Interval E-value
O-FucT_like cd11296
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like ...
 382-540 2.48e-18

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: 83.62  E-value: 2.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240670 382 NHKCKTLIEPSKLILLTAQRFIQTFL---GKNFIALHFRRHGFLKFCNAKSPS---CFYPIPQAAECIARIVERSNGA-- 453
Cdd:cd11296  42 IRLVGKHLRFSPEIRKLADRFVRKLLglpGGPYLAVHLRRGDFEVECCHLAKWmgeYLEECLLSAEEIAEKIKELMAErk 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240670 454 --VIYLSTDAAESETslLQSLVVVDGKIVpLVKRPPRNSAEKWDALLYRHGIEddsqvdAMLDKTICAMSSVFIGASGST 531
Cdd:cd11296 122 lkVVYVATDEADREE--LREELRKAGIRV-VTKDDLLEDAELLELEKLDNYLL------SLVDQEICSRADVFIGTGFST 192


                ....*....
gi 15240670 532 FTEDILRLR 540
Cdd:cd11296 193 FSSNVALLR 201
O-FucT pfam10250
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing ...
 392-540 7.52e-06

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: 47.68  E-value: 7.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240670   392 SKLILLTAQRFIQTFLGKNFIALHFRRHG-FLKFCN---------AKSPSCFYPIPQA-----AECIARIVER------- 449
Cdd:pfam10250  85 SPEIEELGDKLVDRLLKGPYLALHLRREKdMLAASGcaegggdeeAEEDPEERRRNGLcpltpEECLPSLVGIllqalgf 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240670   450 -SNGAVIYLSTDAAESETSL--LQSLvvvdgkIVPLVKRPPRNSAEKWDALlyrhgieDDSQVdAMLDKTICAMSSVFIG 526
Cdd:pfam10250 165 vKKLTRIYVATDEIYGGEELapLKSM------FPNLVTKESLASVEELEPF-------KDGSS-AALDYIICLHSDVFIG 230

                         170
                  ....*....|....
gi 15240670   527 ASGSTFTEDILRLR 540
Cdd:pfam10250 231 TCVSNFSAFVKGER 244
 
Name Accession Description Interval E-value
O-FucT_like cd11296
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like ...
 382-540 2.48e-18

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: 83.62  E-value: 2.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240670 382 NHKCKTLIEPSKLILLTAQRFIQTFL---GKNFIALHFRRHGFLKFCNAKSPS---CFYPIPQAAECIARIVERSNGA-- 453
Cdd:cd11296  42 IRLVGKHLRFSPEIRKLADRFVRKLLglpGGPYLAVHLRRGDFEVECCHLAKWmgeYLEECLLSAEEIAEKIKELMAErk 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240670 454 --VIYLSTDAAESETslLQSLVVVDGKIVpLVKRPPRNSAEKWDALLYRHGIEddsqvdAMLDKTICAMSSVFIGASGST 531
Cdd:cd11296 122 lkVVYVATDEADREE--LREELRKAGIRV-VTKDDLLEDAELLELEKLDNYLL------SLVDQEICSRADVFIGTGFST 192


                ....*....
gi 15240670 532 FTEDILRLR 540
Cdd:cd11296 193 FSSNVALLR 201
O-FucT-2 cd11298
GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 ...
 407-533 1.33e-09

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: 59.98  E-value: 1.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240670 407 LGKNFIALHFRRHGFLKFCNAKSPScfypIPQAAECIARIVERSNGAVIYLSTDAAESETSLLQSLVVvDGKIVPLVkrP 486
Cdd:cd11298 242 LGGPYLAVHLRRGDFVYGRKKDVPS----LKGAAKQILNLMKKLKLKKVFIATDAKKEELEELKKLLK-KLKVVRYE--P 314

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15240670 487 PRNSAEKWDallyrhgiedDSQVdAMLDKTICAMSSVFIGASGSTFT 533
Cdd:cd11298 315 TLEELEKLK----------DGGV-AIIDQWICAHARYFIGTKESTFS 350
NodZ_like cd11548
Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ; Bradyrhizobium NodZ is an alpha 1, ...
 347-541 4.87e-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: 48.52  E-value: 4.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240670 347 DVQMKFKSDDDVIAIGDVFYADMEQDWVMQPGGPINHKCKTLIEPSKLILLTAQRFIQTFLGKNFIALHFRRHGfLKFCN 426
Cdd:cd11548 103 ELTVLDVKGRKAVQAGYLPKLPRDADKLGRDRGIIKCYLYRLFTPKQEVRAAVRKLYAKLFGRPTIGVHIRTTD-HKDSL 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240670 427 AKSPSCFYpipQAAECIARIVERSNGAVIYLSTDAAESETSLLQ---SLVVVDgkivplvKRPPRNSAEkwDALLYRHGI 503
Cdd:cd11548 182 FIKLSPLH---RVVDALRKKVALHKDATIFLATDSAEVKDELKRlfpDVVVTP-------KEFPPHGER--SASDGLEGA 249

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15240670 504 EDdsqvdAMLDKTICAMSSVFIGASGSTFTEDILRLRK 541
Cdd:cd11548 250 ED-----ALIDMYLLARCDHLIGSRFSTFSRMASILGD 282
O-FucT pfam10250
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing ...
 392-540 7.52e-06

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: 47.68  E-value: 7.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240670   392 SKLILLTAQRFIQTFLGKNFIALHFRRHG-FLKFCN---------AKSPSCFYPIPQA-----AECIARIVER------- 449
Cdd:pfam10250  85 SPEIEELGDKLVDRLLKGPYLALHLRREKdMLAASGcaegggdeeAEEDPEERRRNGLcpltpEECLPSLVGIllqalgf 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240670   450 -SNGAVIYLSTDAAESETSL--LQSLvvvdgkIVPLVKRPPRNSAEKWDALlyrhgieDDSQVdAMLDKTICAMSSVFIG 526
Cdd:pfam10250 165 vKKLTRIYVATDEIYGGEELapLKSM------FPNLVTKESLASVEELEPF-------KDGSS-AALDYIICLHSDVFIG 230

                         170
                  ....*....|....
gi 15240670   527 ASGSTFTEDILRLR 540
Cdd:pfam10250 231 TCVSNFSAFVKGER 244
 
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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