NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|698580687|ref|XP_009777360|]
View 

PREDICTED: uncharacterized protein LOC104226946 [Nicotiana sylvestris]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 374-531 4.32e-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: 77.07  E-value: 4.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698580687 374 HKCKTLVEPSRLILLTAQRFIQTFL---GENFIALHFRRHGFLKFCNAKKPS---CFYPVPQAADCI----NRVVERANS 443
Cdd:cd11296   43 RLVGKHLRFSPEIRKLADRFVRKLLglpGGPYLAVHLRRGDFEVECCHLAKWmgeYLEECLLSAEEIaekiKELMAERKL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698580687 444 AVIYLSTDAAESETgLLQSLVVFNGKTVplvgrparNSAEKWDALLYRHGLEGDRQVEAMLDKTICSLSDVFIGSMGSTF 523
Cdd:cd11296  123 KVVYVATDEADREE-LREELRKAGIRVV--------TKDDLLEDAELLELEKLDNYLLSLVDQEICSRADVFIGTGFSTF 193


                 ....*...
gi 698580687 524 TEDILRLR 531
Cdd:cd11296  194 SSNVALLR 201
 
Name Accession Description Interval E-value
O-FucT_like cd11296
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like ...
 374-531 4.32e-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: 77.07  E-value: 4.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698580687 374 HKCKTLVEPSRLILLTAQRFIQTFL---GENFIALHFRRHGFLKFCNAKKPS---CFYPVPQAADCI----NRVVERANS 443
Cdd:cd11296   43 RLVGKHLRFSPEIRKLADRFVRKLLglpGGPYLAVHLRRGDFEVECCHLAKWmgeYLEECLLSAEEIaekiKELMAERKL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698580687 444 AVIYLSTDAAESETgLLQSLVVFNGKTVplvgrparNSAEKWDALLYRHGLEGDRQVEAMLDKTICSLSDVFIGSMGSTF 523
Cdd:cd11296  123 KVVYVATDEADREE-LREELRKAGIRVV--------TKDDLLEDAELLELEKLDNYLLSLVDQEICSRADVFIGTGFSTF 193


                 ....*...
gi 698580687 524 TEDILRLR 531
Cdd:cd11296  194 SSNVALLR 201
O-FucT pfam10250
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing ...
 386-531 2.33e-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: 49.22  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698580687  386 ILLTAQRFIQTFLGENFIALHFRRHG-FLKFCNakkpsCFYPVPQAADCINRVVERANSA-------------------- 444
Cdd:pfam10250  88 IEELGDKLVDRLLKGPYLALHLRREKdMLAASG-----CAEGGGDEEAEEDPEERRRNGLcpltpeeclpslvgillqal 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698580687  445 -------VIYLSTDaaesETGLLQSLVVFNGKTVPLVGRPARNSAEKWDaLLYRHGLegdrqveAMLDKTICSLSDVFIG 517
Cdd:pfam10250 163 gfvkkltRIYVATD----EIYGGEELAPLKSMFPNLVTKESLASVEELE-PFKDGSS-------AALDYIICLHSDVFIG 230

                         170
                  ....*....|....
gi 698580687  518 SMGSTFTEDILRLR 531
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 ...
 374-531 4.32e-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: 77.07  E-value: 4.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698580687 374 HKCKTLVEPSRLILLTAQRFIQTFL---GENFIALHFRRHGFLKFCNAKKPS---CFYPVPQAADCI----NRVVERANS 443
Cdd:cd11296   43 RLVGKHLRFSPEIRKLADRFVRKLLglpGGPYLAVHLRRGDFEVECCHLAKWmgeYLEECLLSAEEIaekiKELMAERKL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698580687 444 AVIYLSTDAAESETgLLQSLVVFNGKTVplvgrparNSAEKWDALLYRHGLEGDRQVEAMLDKTICSLSDVFIGSMGSTF 523
Cdd:cd11296  123 KVVYVATDEADREE-LREELRKAGIRVV--------TKDDLLEDAELLELEKLDNYLLSLVDQEICSRADVFIGTGFSTF 193


                 ....*...
gi 698580687 524 TEDILRLR 531
Cdd:cd11296  194 SSNVALLR 201
O-FucT pfam10250
GDP-fucose protein O-fucosyltransferase; This is a family of conserved proteins representing ...
 386-531 2.33e-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: 49.22  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698580687  386 ILLTAQRFIQTFLGENFIALHFRRHG-FLKFCNakkpsCFYPVPQAADCINRVVERANSA-------------------- 444
Cdd:pfam10250  88 IEELGDKLVDRLLKGPYLALHLRREKdMLAASG-----CAEGGGDEEAEEDPEERRRNGLcpltpeeclpslvgillqal 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698580687  445 -------VIYLSTDaaesETGLLQSLVVFNGKTVPLVGRPARNSAEKWDaLLYRHGLegdrqveAMLDKTICSLSDVFIG 517
Cdd:pfam10250 163 gfvkkltRIYVATD----EIYGGEELAPLKSMFPNLVTKESLASVEELE-PFKDGSS-------AALDYIICLHSDVFIG 230

                         170
                  ....*....|....
gi 698580687  518 SMGSTFTEDILRLR 531
Cdd:pfam10250 231 TCVSNFSAFVKGER 244
O-FucT-2 cd11298
GDP-fucose protein O-fucosyltransferase 2; O-FucT-2 adds O-fucose to thrombospondin type 1 ...
 398-524 3.10e-06

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: 49.58  E-value: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698580687 398 LGENFIALHFRRHGFLKFCNAKKPScfypVPQAADCINRVVERANSAVIYLSTDAAESETGLLQSLVvFNGKTVPLVgrP 477
Cdd:cd11298  242 LGGPYLAVHLRRGDFVYGRKKDVPS----LKGAAKQILNLMKKLKLKKVFIATDAKKEELEELKKLL-KKLKVVRYE--P 314

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 698580687 478 ARNSAEKWdallyrhgleGDRQVeAMLDKTICSLSDVFIGSMGSTFT 524
Cdd:cd11298  315 TLEELEKL----------KDGGV-AIIDQWICAHARYFIGTKESTFS 350
NodZ_like cd11548
Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ; Bradyrhizobium NodZ is an alpha 1, ...
 365-532 6.01e-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: 48.13  E-value: 6.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698580687 365 VMQPRGPISHKCKTLVEPSRLILLTAQRFIQTFLGENFIALHFRRHGfLKFCNAKKPSCFYPVpqaADCINRVVERANSA 444
Cdd:cd11548  130 LGRDRGIIKCYLYRLFTPKQEVRAAVRKLYAKLFGRPTIGVHIRTTD-HKDSLFIKLSPLHRV---VDALRKKVALHKDA 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 698580687 445 VIYLSTDAAESETGLLQ---SLVVFNGKTVPLVGRPARNsaekwdallYRHGLEgdrqvEAMLDKTICSLSDVFIGSMGS 521
Cdd:cd11548  206 TIFLATDSAEVKDELKRlfpDVVVTPKEFPPHGERSASD---------GLEGAE-----DALIDMYLLARCDHLIGSRFS 271

                        170
                 ....*....|.
gi 698580687 522 TFTEDILRLRK 532
Cdd:cd11548  272 TFSRMASILGD 282
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH