NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|297850124|ref|XP_002892943|]
View 

uncharacterized protein LOC9329005 [Arabidopsis lyrata subsp. lyrata]

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 ...
392-550 1.65e-19

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: 87.09  E-value: 1.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297850124 392 NHKCKTLIEPSRLILVTAQRFIQTFL---GKNFISLHLRRHGFLKFCNAKSPS---CFYPIPQAADCISRMVERA----N 461
Cdd:cd11296   42 IRLVGKHLRFSPEIRKLADRFVRKLLglpGGPYLAVHLRRGDFEVECCHLAKWmgeYLEECLLSAEEIAEKIKELmaerK 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297850124 462 APVIYLSTDAAESETgLLQSLVVVNGKVVplvkrpprNSAEKWDSLLYRHGIEDDSQVDAMLDKTICAMSSVFIGASGST 541
Cdd:cd11296  122 LKVVYVATDEADREE-LREELRKAGIRVV--------TKDDLLEDAELLELEKLDNYLLSLVDQEICSRADVFIGTGFST 192

                 ....*....
gi 297850124 542 FTEDILRLR 550
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 ...
392-550 1.65e-19

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: 87.09  E-value: 1.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297850124 392 NHKCKTLIEPSRLILVTAQRFIQTFL---GKNFISLHLRRHGFLKFCNAKSPS---CFYPIPQAADCISRMVERA----N 461
Cdd:cd11296   42 IRLVGKHLRFSPEIRKLADRFVRKLLglpGGPYLAVHLRRGDFEVECCHLAKWmgeYLEECLLSAEEIAEKIKELmaerK 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297850124 462 APVIYLSTDAAESETgLLQSLVVVNGKVVplvkrpprNSAEKWDSLLYRHGIEDDSQVDAMLDKTICAMSSVFIGASGST 541
Cdd:cd11296  122 LKVVYVATDEADREE-LREELRKAGIRVV--------TKDDLLEDAELLELEKLDNYLLSLVDQEICSRADVFIGTGFST 192

                 ....*....
gi 297850124 542 FTEDILRLR 550
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 ...
392-550 1.65e-19

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: 87.09  E-value: 1.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297850124 392 NHKCKTLIEPSRLILVTAQRFIQTFL---GKNFISLHLRRHGFLKFCNAKSPS---CFYPIPQAADCISRMVERA----N 461
Cdd:cd11296   42 IRLVGKHLRFSPEIRKLADRFVRKLLglpGGPYLAVHLRRGDFEVECCHLAKWmgeYLEECLLSAEEIAEKIKELmaerK 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297850124 462 APVIYLSTDAAESETgLLQSLVVVNGKVVplvkrpprNSAEKWDSLLYRHGIEDDSQVDAMLDKTICAMSSVFIGASGST 541
Cdd:cd11296  122 LKVVYVATDEADREE-LREELRKAGIRVV--------TKDDLLEDAELLELEKLDNYLLSLVDQEICSRADVFIGTGFST 192

                 ....*....
gi 297850124 542 FTEDILRLR 550
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 ...
417-543 1.17e-10

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: 63.44  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297850124 417 LGKNFISLHLRRHGFLKFCNAKSPScfypIPQAADCISRMVERANAPVIYLSTDAAESETGLLQSLvVVNGKVVPLVkrP 496
Cdd:cd11298  242 LGGPYLAVHLRRGDFVYGRKKDVPS----LKGAAKQILNLMKKLKLKKVFIATDAKKEELEELKKL-LKKLKVVRYE--P 314
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 297850124 497 PRNSAEKWdsllyrhgieDDSQVdAMLDKTICAMSSVFIGASGSTFT 543
Cdd:cd11298  315 TLEELEKL----------KDGGV-AIIDQWICAHARYFIGTKESTFS 350
NodZ_like cd11548
Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ; Bradyrhizobium NodZ is an alpha 1, ...
353-551 1.81e-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 [Multi-domain]  Cd Length: 287  Bit Score: 46.98  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297850124 353 RTSKEVVEKFKSDDGVIAIGDVFYADMEQDLVMQPGGPINHKCKTLIEPSRLILVTAQRFIQTFLGKNFISLHLRRHGfL 432
Cdd:cd11548   99 RECDELTVLDVKGRKAVQAGYLPKLPRDADKLGRDRGIIKCYLYRLFTPKQEVRAAVRKLYAKLFGRPTIGVHIRTTD-H 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297850124 433 KFCNAKSPSCFYpipQAADCISRMVERANAPVIYLSTDAAESETGLLQslvvVNGKVVPLVKRPPRNSAEkwDSLLYRHG 512
Cdd:cd11548  178 KDSLFIKLSPLH---RVVDALRKKVALHKDATIFLATDSAEVKDELKR----LFPDVVVTPKEFPPHGER--SASDGLEG 248
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 297850124 513 IEddsqvDAMLDKTICAMSSVFIGASGSTFTEDILRLRK 551
Cdd:cd11548  249 AE-----DALIDMYLLARCDHLIGSRFSTFSRMASILGD 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