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Conserved domains on  [gi|15862474|emb|CAC88636|]
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unnamed protein product [Homo sapiens]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
1-252 1.84e-123

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member cd03816:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 411  Bit Score: 358.51  E-value: 1.84e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474   1 MQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMWREPGAYIF 80
Cdd:cd03816  20 MQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPTKNKLPFLLFAPLKVLLQALSLLWLLYELRPADYIL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474  81 LQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDLA--DN 158
Cdd:cd03816 100 VQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMADAHLCVTKAMQRDLQqfEN 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474 159 WHIRAVTVYDKPASFFKETPLDLQHRLFMKLgsmhspfrarsepedpvtersaFTERDAGSGLVTRLRERPALLVSSTSW 238
Cdd:cd03816 180 WNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAEGAVSYKEGRPALLVSSTSW 237
                       250
                ....*....|....
gi 15862474 239 TEDEDFSILREALV 252
Cdd:cd03816 238 TPDEDFSILLDALK 251
 
Name Accession Description Interval E-value
GT33_ALG1-like cd03816
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ...
1-252 1.84e-123

chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.


Pssm-ID: 340843 [Multi-domain]  Cd Length: 411  Bit Score: 358.51  E-value: 1.84e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474   1 MQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMWREPGAYIF 80
Cdd:cd03816  20 MQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPTKNKLPFLLFAPLKVLLQALSLLWLLYELRPADYIL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474  81 LQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDLA--DN 158
Cdd:cd03816 100 VQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMADAHLCVTKAMQRDLQqfEN 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474 159 WHIRAVTVYDKPASFFKETPLDLQHRLFMKLgsmhspfrarsepedpvtersaFTERDAGSGLVTRLRERPALLVSSTSW 238
Cdd:cd03816 180 WNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAEGAVSYKEGRPALLVSSTSW 237
                       250
                ....*....|....
gi 15862474 239 TEDEDFSILREALV 252
Cdd:cd03816 238 TPDEDFSILLDALK 251
PLN02275 PLN02275
transferase, transferring glycosyl groups
1-255 6.32e-72

transferase, transferring glycosyl groups


Pssm-ID: 215155 [Multi-domain]  Cd Length: 371  Bit Score: 225.71  E-value: 6.32e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474    1 MQYHALSLAMH-GFSVTLLGFCNSKPHDELLQNNRIQI---VGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMWREPG 76
Cdd:PLN02275  21 MQYHALSLARQaSFQVDVVAYGGSEPIPALLNHPSIHIhlmVQPRLLQRLPRVLYALALLLKVAIQFLMLLWFLCVKIPR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474   77 AYIFL-QNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDL 155
Cdd:PLN02275 101 PDVFLvQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYERHYGKMADGHLCVTKAMQHEL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474  156 ADNWHIRAVTVYDKPASFFKETPldlqhrlfmklgsmhspfrarsepedpvtersafterdagsgLVTRLRE-RPALLVS 234
Cdd:PLN02275 181 DQNWGIRATVLYDQPPEFFRPAS------------------------------------------LEIRLRPnRPALVVS 218
                        250       260
                 ....*....|....*....|.
gi 15862474  235 STSWTEDEDFSILREALVGLD 255
Cdd:PLN02275 219 STSWTPDEDFGILLEAAVMYD 239
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
8-163 9.16e-03

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 36.36  E-value: 9.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474     8 LAMHGFSVTLlgFCNSKPHDELLQNNRIQIVGLTelqslavgPRVFQYGVKVVLQAMYLLWKLMWREPGAYIFLQNPPgl 87
Cdd:pfam13439  14 LARRGHEVTV--VTPGGPGPLAEEVVRVVRVPRV--------PLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSPF-- 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15862474    88 PSIAVCWFVGCLCGSKLVIDWHNyGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDLADNWHIRA 163
Cdd:pfam13439  82 PLGLAALAARLRLGIPLVVTYHG-LFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVPP 156
 
Name Accession Description Interval E-value
GT33_ALG1-like cd03816
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ...
1-252 1.84e-123

chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.


Pssm-ID: 340843 [Multi-domain]  Cd Length: 411  Bit Score: 358.51  E-value: 1.84e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474   1 MQYHALSLAMHGFSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMWREPGAYIF 80
Cdd:cd03816  20 MQYHALSLARHGWRVDLIGYLESPPHDELLSHPNITIHALPPPPTKNKLPFLLFAPLKVLLQALSLLWLLYELRPADYIL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474  81 LQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDLA--DN 158
Cdd:cd03816 100 VQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKTFGRMADAHLCVTKAMQRDLQqfEN 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474 159 WHIRAVTVYDKPASFFKETPLDLQHRLFMKLgsmhspfrarsepedpvtersaFTERDAGSGLVTRLRERPALLVSSTSW 238
Cdd:cd03816 180 WNIRATVLYDRPPSHFRPIPLEEKHELFLEL----------------------ALFRELAEGAVSYKEGRPALLVSSTSW 237
                       250
                ....*....|....
gi 15862474 239 TEDEDFSILREALV 252
Cdd:cd03816 238 TPDEDFSILLDALK 251
PLN02275 PLN02275
transferase, transferring glycosyl groups
1-255 6.32e-72

transferase, transferring glycosyl groups


Pssm-ID: 215155 [Multi-domain]  Cd Length: 371  Bit Score: 225.71  E-value: 6.32e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474    1 MQYHALSLAMH-GFSVTLLGFCNSKPHDELLQNNRIQI---VGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMWREPG 76
Cdd:PLN02275  21 MQYHALSLARQaSFQVDVVAYGGSEPIPALLNHPSIHIhlmVQPRLLQRLPRVLYALALLLKVAIQFLMLLWFLCVKIPR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474   77 AYIFL-QNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDL 155
Cdd:PLN02275 101 PDVFLvQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYERHYGKMADGHLCVTKAMQHEL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474  156 ADNWHIRAVTVYDKPASFFKETPldlqhrlfmklgsmhspfrarsepedpvtersafterdagsgLVTRLRE-RPALLVS 234
Cdd:PLN02275 181 DQNWGIRATVLYDQPPEFFRPAS------------------------------------------LEIRLRPnRPALVVS 218
                        250       260
                 ....*....|....*....|.
gi 15862474  235 STSWTEDEDFSILREALVGLD 255
Cdd:PLN02275 219 STSWTPDEDFGILLEAAVMYD 239
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
8-163 9.16e-03

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 36.36  E-value: 9.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15862474     8 LAMHGFSVTLlgFCNSKPHDELLQNNRIQIVGLTelqslavgPRVFQYGVKVVLQAMYLLWKLMWREPGAYIFLQNPPgl 87
Cdd:pfam13439  14 LARRGHEVTV--VTPGGPGPLAEEVVRVVRVPRV--------PLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSPF-- 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15862474    88 PSIAVCWFVGCLCGSKLVIDWHNyGYSIMGLVHGPNHPLVLLAKWYEKFFGRLSHLNLCVTNAMREDLADNWHIRA 163
Cdd:pfam13439  82 PLGLAALAARLRLGIPLVVTYHG-LFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVPP 156
 
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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