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Conserved domains on  [gi|18265338|dbj|BAB40929|]
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alpha 1,6-fucosyltransferase [Homo sapiens]

Protein Classification

FUT8_N_cat superfamily-containing protein( domain architecture ID 1912265)

FUT8_N_cat superfamily-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FUT8_N_cat super family cl45147
Alpha-(1,6)-fucosyltransferase N- and catalytic domains; This entry represents the N-terminal ...
 68-290 6.34e-122

Alpha-(1,6)-fucosyltransferase N- and catalytic domains; This entry represents the N-terminal coiled-coil and the catalytic domains of the Alpha-(1,6)-fucosyltransferase (FUT8), an enzyme that catalyzes the transfer of a fucose residue in alpha 1-6 linkage to the N-Acetylglucosamine (GlcNAc) residue in N-glycans. The catalytic domain comprises two structures, an open sheet alpha/beta structure, which contains five helices and three beta- strands at the N-terminal, and a Rossmann fold that contains five helices and five beta-strands at the C-terminal. The latter is conserved among the alpha1,2-, alpha1,6-, and protein O-fucosyltransferases and is similar to GT-B group glycosyltransferases.


The actual alignment was detected with superfamily member pfam19745:

Pssm-ID: 466170 [Multi-domain]  Cd Length: 431  Bit Score: 356.26  E-value: 6.34e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18265338    68 RIPEGPIDQGPAIGRVRVLEEQLVKAKEQIENYKKQTRNGLGKDHEILRRRIENGAKELWFFLQSELKKLKNLEGNE-LQ 146
Cdd:pfam19745   1 RLRRSEESKGIANGRLDSLEDQLVKAKQQIEDYKPSAANGPSLEHEVLRRRLENGIQELWYYLSSELKKLRKEIDREsLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18265338   147 RHADEFLLDLGHHERSIMTDLYYLSQTDGAGDWREKEAKDLTELVQRRITYLQNPKDCSKAKKLVCNINKGCGYGCQLHH 226
Cdd:pfam19745  81 NHINEILDLLAEHKRSLIADIEKLSKADGAEEWRKKELKDLSDLVQKRLDHLQNPEDCSKARKLICNLNKGCGFGCQLHH 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18265338   227 VVYCFMIAYGTQRTLILESQNWRYATGGWETVFRPVSETCTDRSGISTGHWSGTPIMNLLVITL 290
Cdd:pfam19745 161 VTYCFIVAYATNRTLILDSKGWRYSKGGWESVFKPLSDTCTERSGAGASPWPGEENSDAQVVEL 224
 
Name Accession Description Interval E-value
FUT8_N_cat pfam19745
Alpha-(1,6)-fucosyltransferase N- and catalytic domains; This entry represents the N-terminal ...
 68-290 6.34e-122

Alpha-(1,6)-fucosyltransferase N- and catalytic domains; This entry represents the N-terminal coiled-coil and the catalytic domains of the Alpha-(1,6)-fucosyltransferase (FUT8), an enzyme that catalyzes the transfer of a fucose residue in alpha 1-6 linkage to the N-Acetylglucosamine (GlcNAc) residue in N-glycans. The catalytic domain comprises two structures, an open sheet alpha/beta structure, which contains five helices and three beta- strands at the N-terminal, and a Rossmann fold that contains five helices and five beta-strands at the C-terminal. The latter is conserved among the alpha1,2-, alpha1,6-, and protein O-fucosyltransferases and is similar to GT-B group glycosyltransferases.


Pssm-ID: 466170 [Multi-domain]  Cd Length: 431  Bit Score: 356.26  E-value: 6.34e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18265338    68 RIPEGPIDQGPAIGRVRVLEEQLVKAKEQIENYKKQTRNGLGKDHEILRRRIENGAKELWFFLQSELKKLKNLEGNE-LQ 146
Cdd:pfam19745   1 RLRRSEESKGIANGRLDSLEDQLVKAKQQIEDYKPSAANGPSLEHEVLRRRLENGIQELWYYLSSELKKLRKEIDREsLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18265338   147 RHADEFLLDLGHHERSIMTDLYYLSQTDGAGDWREKEAKDLTELVQRRITYLQNPKDCSKAKKLVCNINKGCGYGCQLHH 226
Cdd:pfam19745  81 NHINEILDLLAEHKRSLIADIEKLSKADGAEEWRKKELKDLSDLVQKRLDHLQNPEDCSKARKLICNLNKGCGFGCQLHH 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18265338   227 VVYCFMIAYGTQRTLILESQNWRYATGGWETVFRPVSETCTDRSGISTGHWSGTPIMNLLVITL 290
Cdd:pfam19745 161 VTYCFIVAYATNRTLILDSKGWRYSKGGWESVFKPLSDTCTERSGAGASPWPGEENSDAQVVEL 224
Fut8_like cd11300
Alpha 1-6-fucosyltransferase; Alpha 1,6-fucosyltransferase (Fut8) transfers a fucose moiety ...
 174-281 1.72e-61

Alpha 1-6-fucosyltransferase; Alpha 1,6-fucosyltransferase (Fut8) transfers a fucose moiety from GDP-fucose to the reducing terminal N-acetylglucosamine of the core structure of Asn-linked oligosaccharides, in a process termed core fucosylation. Core fucosylation is essential for the function of growth factor receptors. 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: 211386 [Multi-domain]  Cd Length: 328  Bit Score: 198.24  E-value: 1.72e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18265338 174 DGAGDWREKEAKDLTELVQRRITYLQNPKDCSKAKKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLILESQNWRYATG 253
Cdd:cd11300   1 DGDSEWRRKELKKLSKLVQKRIHKLQNPKDCSKAKKLVCNLNKGCGFGCQLHHVVYCLIVAYGTNRTLILDSKGWRYSPG 80

                        90       100
                ....*....|....*....|....*...
gi 18265338 254 GWETVFRPVSETCTDRSGISTGHWSGTP 281
Cdd:cd11300  81 GWEKVFLPLSETCTDRSGDNTAVWWWEP 108
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
41-151 7.08e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 7.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18265338  41 RELSKILAKLERLKQQNEDLRRmaeslripegpidqgpaigRVRVLEEQLVKAKEQIENYKKQTRNGLGKDHEI--LRRR 118
Cdd:COG2433 413 EEIRRLEEQVERLEAEVEELEA-------------------ELEEKDERIERLERELSEARSEERREIRKDREIsrLDRE 473

                        90       100       110
                ....*....|....*....|....*....|...
gi 18265338 119 IENgakelwffLQSELKKLKNlEGNELQRHADE 151
Cdd:COG2433 474 IER--------LERELEEERE-RIEELKRKLER 497
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
40-142 4.00e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18265338   40 SRELSKILAKLERLKQQNEDLRRMAESLripEGPIDQGPAIGRVRVLEEQLVKAKEQIENYKKQTRNGLGKDHEILRRRI 119
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELREL---EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL 534

                         90       100
                 ....*....|....*....|...
gi 18265338  120 ENGAKELwFFLQSELKKLKNLEG 142
Cdd:PRK03918 535 IKLKGEI-KSLKKELEKLEELKK 556
 
Name Accession Description Interval E-value
FUT8_N_cat pfam19745
Alpha-(1,6)-fucosyltransferase N- and catalytic domains; This entry represents the N-terminal ...
 68-290 6.34e-122

Alpha-(1,6)-fucosyltransferase N- and catalytic domains; This entry represents the N-terminal coiled-coil and the catalytic domains of the Alpha-(1,6)-fucosyltransferase (FUT8), an enzyme that catalyzes the transfer of a fucose residue in alpha 1-6 linkage to the N-Acetylglucosamine (GlcNAc) residue in N-glycans. The catalytic domain comprises two structures, an open sheet alpha/beta structure, which contains five helices and three beta- strands at the N-terminal, and a Rossmann fold that contains five helices and five beta-strands at the C-terminal. The latter is conserved among the alpha1,2-, alpha1,6-, and protein O-fucosyltransferases and is similar to GT-B group glycosyltransferases.


Pssm-ID: 466170 [Multi-domain]  Cd Length: 431  Bit Score: 356.26  E-value: 6.34e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18265338    68 RIPEGPIDQGPAIGRVRVLEEQLVKAKEQIENYKKQTRNGLGKDHEILRRRIENGAKELWFFLQSELKKLKNLEGNE-LQ 146
Cdd:pfam19745   1 RLRRSEESKGIANGRLDSLEDQLVKAKQQIEDYKPSAANGPSLEHEVLRRRLENGIQELWYYLSSELKKLRKEIDREsLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18265338   147 RHADEFLLDLGHHERSIMTDLYYLSQTDGAGDWREKEAKDLTELVQRRITYLQNPKDCSKAKKLVCNINKGCGYGCQLHH 226
Cdd:pfam19745  81 NHINEILDLLAEHKRSLIADIEKLSKADGAEEWRKKELKDLSDLVQKRLDHLQNPEDCSKARKLICNLNKGCGFGCQLHH 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18265338   227 VVYCFMIAYGTQRTLILESQNWRYATGGWETVFRPVSETCTDRSGISTGHWSGTPIMNLLVITL 290
Cdd:pfam19745 161 VTYCFIVAYATNRTLILDSKGWRYSKGGWESVFKPLSDTCTERSGAGASPWPGEENSDAQVVEL 224
Fut8_like cd11300
Alpha 1-6-fucosyltransferase; Alpha 1,6-fucosyltransferase (Fut8) transfers a fucose moiety ...
 174-281 1.72e-61

Alpha 1-6-fucosyltransferase; Alpha 1,6-fucosyltransferase (Fut8) transfers a fucose moiety from GDP-fucose to the reducing terminal N-acetylglucosamine of the core structure of Asn-linked oligosaccharides, in a process termed core fucosylation. Core fucosylation is essential for the function of growth factor receptors. 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: 211386 [Multi-domain]  Cd Length: 328  Bit Score: 198.24  E-value: 1.72e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18265338 174 DGAGDWREKEAKDLTELVQRRITYLQNPKDCSKAKKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLILESQNWRYATG 253
Cdd:cd11300   1 DGDSEWRRKELKKLSKLVQKRIHKLQNPKDCSKAKKLVCNLNKGCGFGCQLHHVVYCLIVAYGTNRTLILDSKGWRYSPG 80

                        90       100
                ....*....|....*....|....*...
gi 18265338 254 GWETVFRPVSETCTDRSGISTGHWSGTP 281
Cdd:cd11300  81 GWEKVFLPLSETCTDRSGDNTAVWWWEP 108
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
41-151 7.08e-05

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 7.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18265338  41 RELSKILAKLERLKQQNEDLRRmaeslripegpidqgpaigRVRVLEEQLVKAKEQIENYKKQTRNGLGKDHEI--LRRR 118
Cdd:COG2433 413 EEIRRLEEQVERLEAEVEELEA-------------------ELEEKDERIERLERELSEARSEERREIRKDREIsrLDRE 473

                        90       100       110
                ....*....|....*....|....*....|...
gi 18265338 119 IENgakelwffLQSELKKLKNlEGNELQRHADE 151
Cdd:COG2433 474 IER--------LERELEEERE-RIEELKRKLER 497
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
40-142 4.00e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18265338   40 SRELSKILAKLERLKQQNEDLRRMAESLripEGPIDQGPAIGRVRVLEEQLVKAKEQIENYKKQTRNGLGKDHEILRRRI 119
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELREL---EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL 534

                         90       100
                 ....*....|....*....|...
gi 18265338  120 ENGAKELwFFLQSELKKLKNLEG 142
Cdd:PRK03918 535 IKLKGEI-KSLKKELEKLEELKK 556
 
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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