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Conserved domains on  [gi|225441959|ref|XP_002264087|]
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O-fucosyltransferase 36 [Vitis vinifera]

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 ...
 374-534 1.02e-16

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: 79.00  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225441959 374 LAHKCQTLIEPSRLIMLTAQRFVQTFL---GKSFTALHFRRHGFLKFCNAK---EPSCFFPIPQAADCISRVVERA---- 443
Cdd:cd11296   41 PIRLVGKHLRFSPEIRKLADRFVRKLLglpGGPYLAVHLRRGDFEVECCHLakwMGEYLEECLLSAEEIAEKIKELmaer 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225441959 444 DTPVIYLSTDAAESETgLLQSLVVLNGKLVplIKRPTRNSAEKWDALLYrhgldgDSQVEAMLDKTICAMASVFIGAPGS 523
Cdd:cd11296  121 KLKVVYVATDEADREE-LREELRKAGIRVV--TKDDLLEDAELLELEKL------DNYLLSLVDQEICSRADVFIGTGFS 191

                        170
                 ....*....|.
gi 225441959 524 TFTEDILRLRR 534
Cdd:cd11296  192 TFSSNVALLRR 202
 
Name Accession Description Interval E-value
O-FucT_like cd11296
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like ...
 374-534 1.02e-16

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: 79.00  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225441959 374 LAHKCQTLIEPSRLIMLTAQRFVQTFL---GKSFTALHFRRHGFLKFCNAK---EPSCFFPIPQAADCISRVVERA---- 443
Cdd:cd11296   41 PIRLVGKHLRFSPEIRKLADRFVRKLLglpGGPYLAVHLRRGDFEVECCHLakwMGEYLEECLLSAEEIAEKIKELmaer 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225441959 444 DTPVIYLSTDAAESETgLLQSLVVLNGKLVplIKRPTRNSAEKWDALLYrhgldgDSQVEAMLDKTICAMASVFIGAPGS 523
Cdd:cd11296  121 KLKVVYVATDEADREE-LREELRKAGIRVV--TKDDLLEDAELLELEKL------DNYLLSLVDQEICSRADVFIGTGFS 191

                        170
                 ....*....|.
gi 225441959 524 TFTEDILRLRR 534
Cdd:cd11296  192 TFSSNVALLRR 202
 
Name Accession Description Interval E-value
O-FucT_like cd11296
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like ...
 374-534 1.02e-16

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: 79.00  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225441959 374 LAHKCQTLIEPSRLIMLTAQRFVQTFL---GKSFTALHFRRHGFLKFCNAK---EPSCFFPIPQAADCISRVVERA---- 443
Cdd:cd11296   41 PIRLVGKHLRFSPEIRKLADRFVRKLLglpGGPYLAVHLRRGDFEVECCHLakwMGEYLEECLLSAEEIAEKIKELmaer 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225441959 444 DTPVIYLSTDAAESETgLLQSLVVLNGKLVplIKRPTRNSAEKWDALLYrhgldgDSQVEAMLDKTICAMASVFIGAPGS 523
Cdd:cd11296  121 KLKVVYVATDEADREE-LREELRKAGIRVV--TKDDLLEDAELLELEKL------DNYLLSLVDQEICSRADVFIGTGFS 191

                        170
                 ....*....|.
gi 225441959 524 TFTEDILRLRR 534
Cdd:cd11296  192 TFSSNVALLRR 202
O-FucT-2 cd11298
GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 ...
 386-526 2.24e-07

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: 53.04  E-value: 2.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225441959 386 RLIMLTAQRFVQTFLGKSFTALHFRRHGFLKFCNAKEPScffpIPQAADCISRVVERADTPVIYLSTDAAESETGLLQSL 465
Cdd:cd11298  228 RPEWWRMKKKKGSALGGPYLAVHLRRGDFVYGRKKDVPS----LKGAAKQILNLMKKLKLKKVFIATDAKKEELEELKKL 303

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225441959 466 VvlnGKLVPLIKRPTRNSAEKWdallyrhgldGDSQVeAMLDKTICAMASVFIGAPGSTFT 526
Cdd:cd11298  304 L---KKLKVVRYEPTLEELEKL----------KDGGV-AIIDQWICAHARYFIGTKESTFS 350
 
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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