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Conserved domains on  [gi|2217356087|ref|XP_047273235|]
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beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 4 isoform X1 [Homo sapiens]

Protein Classification

core-2/I-branching beta-1,6-N-acetylglucosaminyltransferase family protein( domain architecture ID 706199)

core-2/I-branching beta-1,6-N-acetylglucosaminyltransferase family protein similar to Homo sapiens xylosyltransferase 1 and Arabidopsis thaliana beta-glucuronosyltransferase GlcAT14A/B/C

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Branch super family cl27418
Core-2/I-Branching enzyme; This is a family of two different beta-1, ...
133-402 1.02e-54

Core-2/I-Branching enzyme; This is a family of two different beta-1,6-N-acetylglucosaminyltransferase enzymes, I-branching enzyme and core-2 branching enzyme. I-branching enzyme is responsible for the production of the blood group I-antigen during embryonic development. Core-2 branching enzyme forms crucial side-chain branches in O-glycans. This is a fmmily of glycosyl-transferases that are Type II membrane proteins that are found in the endoplasmic reticulum (ER) and Golgi apparatus.


The actual alignment was detected with superfamily member pfam02485:

Pssm-ID: 452742  Cd Length: 250  Bit Score: 182.87  E-value: 1.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217356087 133 IAYSLVVHKDAI-MVERLIHAIYNQHNIYCIHYDRKAPDTFKVAMNNLAKCFSNIFIASKLEAVEYAHISRLQADLNCLS 211
Cdd:pfam02485   1 IAFMFLTYKGDLpLLELWLRFFYHPENLYSIYVDSKAPSYFRERVRALASCFFNVRVIPKSESVDWGGPSMVAAELRLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217356087 212 DLLKSSIQWKYVINLCGQDFPLKSNFELVSELKKLNGANMLETVKPPNSKLERFTYHHELRRvPYEYVklpirTNISKEA 291
Cdd:pfam02485  81 NLLLLDPSWDYFILLSESDIPLKTFDELYQYLSSLNGNNSFIDSFSDPGWKGRGRYKPRILD-PMLPE-----IKKSKLF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217356087 292 PPHNIQIFVGSAYFVLSQAFVKYIFNNSIVQDFFAWSKDTYSPDEHFWATLIrvpGIPGEISRsaqdvSDLQSKTRLVKW 371
Cdd:pfam02485 155 LPTAFKWRKGSQWFVLSRAFAEYVVWDNLYYPLFKYYCDTCYPDEHYFPTLL---CMSGEFPN-----TCANRTLTYVDW 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2217356087 372 NYYEGffyPSCTGshlrSVCIYGAAELRWLI 402
Cdd:pfam02485 227 SRGGC---HPKTY----RPCILGPEDLKRIR 250
 
Name Accession Description Interval E-value
Branch pfam02485
Core-2/I-Branching enzyme; This is a family of two different beta-1, ...
133-402 1.02e-54

Core-2/I-Branching enzyme; This is a family of two different beta-1,6-N-acetylglucosaminyltransferase enzymes, I-branching enzyme and core-2 branching enzyme. I-branching enzyme is responsible for the production of the blood group I-antigen during embryonic development. Core-2 branching enzyme forms crucial side-chain branches in O-glycans. This is a fmmily of glycosyl-transferases that are Type II membrane proteins that are found in the endoplasmic reticulum (ER) and Golgi apparatus.


Pssm-ID: 426795  Cd Length: 250  Bit Score: 182.87  E-value: 1.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217356087 133 IAYSLVVHKDAI-MVERLIHAIYNQHNIYCIHYDRKAPDTFKVAMNNLAKCFSNIFIASKLEAVEYAHISRLQADLNCLS 211
Cdd:pfam02485   1 IAFMFLTYKGDLpLLELWLRFFYHPENLYSIYVDSKAPSYFRERVRALASCFFNVRVIPKSESVDWGGPSMVAAELRLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217356087 212 DLLKSSIQWKYVINLCGQDFPLKSNFELVSELKKLNGANMLETVKPPNSKLERFTYHHELRRvPYEYVklpirTNISKEA 291
Cdd:pfam02485  81 NLLLLDPSWDYFILLSESDIPLKTFDELYQYLSSLNGNNSFIDSFSDPGWKGRGRYKPRILD-PMLPE-----IKKSKLF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217356087 292 PPHNIQIFVGSAYFVLSQAFVKYIFNNSIVQDFFAWSKDTYSPDEHFWATLIrvpGIPGEISRsaqdvSDLQSKTRLVKW 371
Cdd:pfam02485 155 LPTAFKWRKGSQWFVLSRAFAEYVVWDNLYYPLFKYYCDTCYPDEHYFPTLL---CMSGEFPN-----TCANRTLTYVDW 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2217356087 372 NYYEGffyPSCTGshlrSVCIYGAAELRWLI 402
Cdd:pfam02485 227 SRGGC---HPKTY----RPCILGPEDLKRIR 250
PLN03183 PLN03183
acetylglucosaminyltransferase family protein; Provisional
112-315 2.75e-10

acetylglucosaminyltransferase family protein; Provisional


Pssm-ID: 178725  Cd Length: 421  Bit Score: 61.80  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217356087 112 IYQTLRGYAQKLVSKEEKSFPI-------AYSLVVHK-DAIMVERLIHAIYNQHNIYCIHYDRKAPDTFKVAMNNLAK-- 181
Cdd:PLN03183   52 TNQTRLEFAESKVNQSPHPPPVqdklprfAYLVSGSKgDLEKLWRTLRALYHPRNQYVVHLDLESPAEERLELASRVEnd 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217356087 182 -CFS---NIFIASKLEAVEYAHISRLQADLNCLSDLLKSSIQWKYVINLCGQDFPLKSNFELVSELKKLN-GANMLETvk 256
Cdd:PLN03183  132 pMFSkvgNVYMITKANLVTYRGPTMVANTLHACAILLKRSKDWDWFINLSASDYPLVTQDDLIHTFSTLDrNLNFIEH-- 209
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217356087 257 ppNSKLErftYHHELRRVP-------YEYVKLPIRTNISKEAPPHNIQIFVGSAYFVLSQAFVKYI 315
Cdd:PLN03183  210 --TSQLG---WKEEKRAMPliidpglYSTNKSDIYWVTPRRSLPTAFKLFTGSAWMVLSRSFVEYC 270
 
Name Accession Description Interval E-value
Branch pfam02485
Core-2/I-Branching enzyme; This is a family of two different beta-1, ...
133-402 1.02e-54

Core-2/I-Branching enzyme; This is a family of two different beta-1,6-N-acetylglucosaminyltransferase enzymes, I-branching enzyme and core-2 branching enzyme. I-branching enzyme is responsible for the production of the blood group I-antigen during embryonic development. Core-2 branching enzyme forms crucial side-chain branches in O-glycans. This is a fmmily of glycosyl-transferases that are Type II membrane proteins that are found in the endoplasmic reticulum (ER) and Golgi apparatus.


Pssm-ID: 426795  Cd Length: 250  Bit Score: 182.87  E-value: 1.02e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217356087 133 IAYSLVVHKDAI-MVERLIHAIYNQHNIYCIHYDRKAPDTFKVAMNNLAKCFSNIFIASKLEAVEYAHISRLQADLNCLS 211
Cdd:pfam02485   1 IAFMFLTYKGDLpLLELWLRFFYHPENLYSIYVDSKAPSYFRERVRALASCFFNVRVIPKSESVDWGGPSMVAAELRLLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217356087 212 DLLKSSIQWKYVINLCGQDFPLKSNFELVSELKKLNGANMLETVKPPNSKLERFTYHHELRRvPYEYVklpirTNISKEA 291
Cdd:pfam02485  81 NLLLLDPSWDYFILLSESDIPLKTFDELYQYLSSLNGNNSFIDSFSDPGWKGRGRYKPRILD-PMLPE-----IKKSKLF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217356087 292 PPHNIQIFVGSAYFVLSQAFVKYIFNNSIVQDFFAWSKDTYSPDEHFWATLIrvpGIPGEISRsaqdvSDLQSKTRLVKW 371
Cdd:pfam02485 155 LPTAFKWRKGSQWFVLSRAFAEYVVWDNLYYPLFKYYCDTCYPDEHYFPTLL---CMSGEFPN-----TCANRTLTYVDW 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2217356087 372 NYYEGffyPSCTGshlrSVCIYGAAELRWLI 402
Cdd:pfam02485 227 SRGGC---HPKTY----RPCILGPEDLKRIR 250
PLN03183 PLN03183
acetylglucosaminyltransferase family protein; Provisional
112-315 2.75e-10

acetylglucosaminyltransferase family protein; Provisional


Pssm-ID: 178725  Cd Length: 421  Bit Score: 61.80  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217356087 112 IYQTLRGYAQKLVSKEEKSFPI-------AYSLVVHK-DAIMVERLIHAIYNQHNIYCIHYDRKAPDTFKVAMNNLAK-- 181
Cdd:PLN03183   52 TNQTRLEFAESKVNQSPHPPPVqdklprfAYLVSGSKgDLEKLWRTLRALYHPRNQYVVHLDLESPAEERLELASRVEnd 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217356087 182 -CFS---NIFIASKLEAVEYAHISRLQADLNCLSDLLKSSIQWKYVINLCGQDFPLKSNFELVSELKKLN-GANMLETvk 256
Cdd:PLN03183  132 pMFSkvgNVYMITKANLVTYRGPTMVANTLHACAILLKRSKDWDWFINLSASDYPLVTQDDLIHTFSTLDrNLNFIEH-- 209
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217356087 257 ppNSKLErftYHHELRRVP-------YEYVKLPIRTNISKEAPPHNIQIFVGSAYFVLSQAFVKYI 315
Cdd:PLN03183  210 --TSQLG---WKEEKRAMPliidpglYSTNKSDIYWVTPRRSLPTAFKLFTGSAWMVLSRSFVEYC 270
 
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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