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Conserved domains on  [gi|578805077|ref|XP_006712882|]
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beta-1,3-galactosyltransferase 1 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
92-279 5.76e-72

Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose:2-acetamido-2-deoxy-D-glucose3beta-galactosyltransferase and UDP-Gal:beta-GlcNAc beta 1,3-galactosyltranferase. Specific galactosyltransferases transfer galactose to GlcNAc terminal chains in the synthesis of the lacto-series oligosaccharides types 1 and 2.


:

Pssm-ID: 426415 [Multi-domain]  Cd Length: 195  Bit Score: 221.04  E-value: 5.76e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077   92 DARQAIRETWGDENNFKGIKIATLFLLGKNADP--VLNQMVEQESQIFHDIIVEDFIDSYHNLTLKTLMGMRWVATFCSK 169
Cdd:pfam01762   1 ARRNAIRKTWMNQGNSEGGRIKSLFLVGLSADTdgKVADLVMEEAKLYGDIVVVDFEDTYENLTFKTLTGLLWAVSKCPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077  170 AKYVMKTDSDIFVNMDNLIYKLLKPSTKPRRRYFTGYVINGG-PIRDVRSKWYMPRDLYPDSNYPPFCSGTGYIFSADVA 248
Cdd:pfam01762  81 AKYIGKIDDDVYFFPDKLLSLLDNGNIDPSESSFYGYVMEEGpVIRNKKSKWYVSPSDYKCSRYPPYASGPFYVLSRDAA 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 578805077  249 ELIYKTSLHTRLLHLEDVYVGLCLRKLGIHP 279
Cdd:pfam01762 161 EKLLKASKHRRFLQIEDVYVGILANDLGISR 191
B3GALT2_N super family cl44771
Beta-1,3-galactosyltransferase 2 N-terminus; This family represents the N-terminal region of ...
57-81 2.45e-04

Beta-1,3-galactosyltransferase 2 N-terminus; This family represents the N-terminal region of the beta-1,3- galactosyltransferase 2 which contains a short cytosolic region, a transmembrane region which indicates that this protein has a type II transmembrane topology, typical for all mammalian glycosyltransferases and a stem region with two putative N-glycosylation sites. This enzyme catalyzes the synthesis of type 1 carbohydrate chains, which contain the Gal(beta 1-3) GlcNAc linkage.


The actual alignment was detected with superfamily member pfam19341:

Pssm-ID: 437173  Cd Length: 81  Bit Score: 39.27  E-value: 2.45e-04
                          10        20
                  ....*....|....*....|....*
gi 578805077   57 PINPHSFEFLINEPNKCEKNIPFLV 81
Cdd:pfam19341  57 TLTAQPYPYIINEPDKCRESTPFLV 81
 
Name Accession Description Interval E-value
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
92-279 5.76e-72

Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose:2-acetamido-2-deoxy-D-glucose3beta-galactosyltransferase and UDP-Gal:beta-GlcNAc beta 1,3-galactosyltranferase. Specific galactosyltransferases transfer galactose to GlcNAc terminal chains in the synthesis of the lacto-series oligosaccharides types 1 and 2.


Pssm-ID: 426415 [Multi-domain]  Cd Length: 195  Bit Score: 221.04  E-value: 5.76e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077   92 DARQAIRETWGDENNFKGIKIATLFLLGKNADP--VLNQMVEQESQIFHDIIVEDFIDSYHNLTLKTLMGMRWVATFCSK 169
Cdd:pfam01762   1 ARRNAIRKTWMNQGNSEGGRIKSLFLVGLSADTdgKVADLVMEEAKLYGDIVVVDFEDTYENLTFKTLTGLLWAVSKCPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077  170 AKYVMKTDSDIFVNMDNLIYKLLKPSTKPRRRYFTGYVINGG-PIRDVRSKWYMPRDLYPDSNYPPFCSGTGYIFSADVA 248
Cdd:pfam01762  81 AKYIGKIDDDVYFFPDKLLSLLDNGNIDPSESSFYGYVMEEGpVIRNKKSKWYVSPSDYKCSRYPPYASGPFYVLSRDAA 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 578805077  249 ELIYKTSLHTRLLHLEDVYVGLCLRKLGIHP 279
Cdd:pfam01762 161 EKLLKASKHRRFLQIEDVYVGILANDLGISR 191
PLN03133 PLN03133
beta-1,3-galactosyltransferase; Provisional
80-326 3.15e-31

beta-1,3-galactosyltransferase; Provisional


Pssm-ID: 215596 [Multi-domain]  Cd Length: 636  Bit Score: 123.37  E-value: 3.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077  80 LVILISTTHKEFDARQAIRETWGDENNFKGIKIATLFLLGKNADPVLNQMVEQESQIFHDIIVEDFIDSYHNLTLKTLMg 159
Cdd:PLN03133 387 LFIGVFSTANNFKRRMAVRRTWMQYDAVRSGAVAVRFFVGLHKNQMVNEELWNEARTYGDIQLMPFVDYYSLITWKTLA- 465
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077 160 mrwVATFCSK---AKYVMKTDSDIFVNMDNLIYKLLKpsTKPRRRYFTGYV-INGGPIRDVRSKWYMPRDLYPDSNYPPF 235
Cdd:PLN03133 466 ---ICIFGTEvvsAKYVMKTDDDAFVRVDEVLASLKR--TNVSHGLLYGLInSDSQPHRNPDSKWYISPEEWPEETYPPW 540
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077 236 CSGTGYIFSADVAELIYKTSLHTRL--LHLEDVYVGLCLRKLGIHPFQNSGFNHWKMAYSLCRYRRVITVHQiSPEEMHR 313
Cdd:PLN03133 541 AHGPGYVVSRDIAKEVYKRHKEGRLkmFKLEDVAMGIWIAEMKKEGLEVKYENDGRIYNEGCKDGYVVAHYQ-SPREMLC 619
                        250
                 ....*....|...
gi 578805077 314 IWNDMSSKKHLRC 326
Cdd:PLN03133 620 LWQKLQEGKRATC 632
B3GALT2_N pfam19341
Beta-1,3-galactosyltransferase 2 N-terminus; This family represents the N-terminal region of ...
57-81 2.45e-04

Beta-1,3-galactosyltransferase 2 N-terminus; This family represents the N-terminal region of the beta-1,3- galactosyltransferase 2 which contains a short cytosolic region, a transmembrane region which indicates that this protein has a type II transmembrane topology, typical for all mammalian glycosyltransferases and a stem region with two putative N-glycosylation sites. This enzyme catalyzes the synthesis of type 1 carbohydrate chains, which contain the Gal(beta 1-3) GlcNAc linkage.


Pssm-ID: 437173  Cd Length: 81  Bit Score: 39.27  E-value: 2.45e-04
                          10        20
                  ....*....|....*....|....*
gi 578805077   57 PINPHSFEFLINEPNKCEKNIPFLV 81
Cdd:pfam19341  57 TLTAQPYPYIINEPDKCRESTPFLV 81
 
Name Accession Description Interval E-value
Galactosyl_T pfam01762
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
92-279 5.76e-72

Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose:2-acetamido-2-deoxy-D-glucose3beta-galactosyltransferase and UDP-Gal:beta-GlcNAc beta 1,3-galactosyltranferase. Specific galactosyltransferases transfer galactose to GlcNAc terminal chains in the synthesis of the lacto-series oligosaccharides types 1 and 2.


Pssm-ID: 426415 [Multi-domain]  Cd Length: 195  Bit Score: 221.04  E-value: 5.76e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077   92 DARQAIRETWGDENNFKGIKIATLFLLGKNADP--VLNQMVEQESQIFHDIIVEDFIDSYHNLTLKTLMGMRWVATFCSK 169
Cdd:pfam01762   1 ARRNAIRKTWMNQGNSEGGRIKSLFLVGLSADTdgKVADLVMEEAKLYGDIVVVDFEDTYENLTFKTLTGLLWAVSKCPS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077  170 AKYVMKTDSDIFVNMDNLIYKLLKPSTKPRRRYFTGYVINGG-PIRDVRSKWYMPRDLYPDSNYPPFCSGTGYIFSADVA 248
Cdd:pfam01762  81 AKYIGKIDDDVYFFPDKLLSLLDNGNIDPSESSFYGYVMEEGpVIRNKKSKWYVSPSDYKCSRYPPYASGPFYVLSRDAA 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 578805077  249 ELIYKTSLHTRLLHLEDVYVGLCLRKLGIHP 279
Cdd:pfam01762 161 EKLLKASKHRRFLQIEDVYVGILANDLGISR 191
PLN03133 PLN03133
beta-1,3-galactosyltransferase; Provisional
80-326 3.15e-31

beta-1,3-galactosyltransferase; Provisional


Pssm-ID: 215596 [Multi-domain]  Cd Length: 636  Bit Score: 123.37  E-value: 3.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077  80 LVILISTTHKEFDARQAIRETWGDENNFKGIKIATLFLLGKNADPVLNQMVEQESQIFHDIIVEDFIDSYHNLTLKTLMg 159
Cdd:PLN03133 387 LFIGVFSTANNFKRRMAVRRTWMQYDAVRSGAVAVRFFVGLHKNQMVNEELWNEARTYGDIQLMPFVDYYSLITWKTLA- 465
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077 160 mrwVATFCSK---AKYVMKTDSDIFVNMDNLIYKLLKpsTKPRRRYFTGYV-INGGPIRDVRSKWYMPRDLYPDSNYPPF 235
Cdd:PLN03133 466 ---ICIFGTEvvsAKYVMKTDDDAFVRVDEVLASLKR--TNVSHGLLYGLInSDSQPHRNPDSKWYISPEEWPEETYPPW 540
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077 236 CSGTGYIFSADVAELIYKTSLHTRL--LHLEDVYVGLCLRKLGIHPFQNSGFNHWKMAYSLCRYRRVITVHQiSPEEMHR 313
Cdd:PLN03133 541 AHGPGYVVSRDIAKEVYKRHKEGRLkmFKLEDVAMGIWIAEMKKEGLEVKYENDGRIYNEGCKDGYVVAHYQ-SPREMLC 619
                        250
                 ....*....|...
gi 578805077 314 IWNDMSSKKHLRC 326
Cdd:PLN03133 620 LWQKLQEGKRATC 632
PLN03193 PLN03193
beta-1,3-galactosyltransferase; Provisional
79-269 3.91e-06

beta-1,3-galactosyltransferase; Provisional


Pssm-ID: 178735 [Multi-domain]  Cd Length: 408  Bit Score: 48.04  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077  79 FLVILISTTHKEFDARQAIRETW---GDE----NNFKGIKIAtlFLLGKNADP--VLNQMVEQESQIFHDIIVEDFIDSY 149
Cdd:PLN03193 140 LMVVGINTAFSSRKRRDSVRATWmpqGEKrkklEEEKGIIIR--FVIGHSATSggILDRAIEAEDRKHGDFLRLDHVEGY 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578805077 150 HNLTLKTLMgmrWVATFCSK--AKYVMKTDSDIFVNMDNLIYKLLKPSTKPrrRYFTGyVINGGPIRDVRSKWYMPRDLY 227
Cdd:PLN03193 218 LELSAKTKT---YFATAVAMwdADFYVKVDDDVHVNIATLGETLVRHRKKP--RVYIG-CMKSGPVLSQKGVRYHEPEYW 291
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 578805077 228 P----DSNYPPFCSGTGYIFSADVAELIyktSLHTRLLHL---EDVYVG 269
Cdd:PLN03193 292 KfgenGNKYFRHATGQLYAISKDLASYI---SINQHVLHKyanEDVSLG 337
B3GALT2_N pfam19341
Beta-1,3-galactosyltransferase 2 N-terminus; This family represents the N-terminal region of ...
57-81 2.45e-04

Beta-1,3-galactosyltransferase 2 N-terminus; This family represents the N-terminal region of the beta-1,3- galactosyltransferase 2 which contains a short cytosolic region, a transmembrane region which indicates that this protein has a type II transmembrane topology, typical for all mammalian glycosyltransferases and a stem region with two putative N-glycosylation sites. This enzyme catalyzes the synthesis of type 1 carbohydrate chains, which contain the Gal(beta 1-3) GlcNAc linkage.


Pssm-ID: 437173  Cd Length: 81  Bit Score: 39.27  E-value: 2.45e-04
                          10        20
                  ....*....|....*....|....*
gi 578805077   57 PINPHSFEFLINEPNKCEKNIPFLV 81
Cdd:pfam19341  57 TLTAQPYPYIINEPDKCRESTPFLV 81
 
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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