NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|530379887|ref|XP_005272039|]
View 

chondroitin sulfate synthase 3 isoform X5 [Homo sapiens]

Protein Classification

glycosyltransferase family protein( domain architecture ID 229488)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CHGN super family cl47930
Chondroitin N-acetylgalactosaminyltransferase;
328-362 1.31e-15

Chondroitin N-acetylgalactosaminyltransferase;


The actual alignment was detected with superfamily member pfam05679:

Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 78.07  E-value: 1.31e-15
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 530379887  328 HIGECLREMYTTHEDVEVGRCVRRFGGTQCVWSYE 362
Cdd:pfam05679   1 HLDWCLKNLYSTHEDVELGRCIQKFAGIPCTWSYE 35
Galactosyl_T super family cl21608
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
 173-351 3.99e-13

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.


The actual alignment was detected with superfamily member pfam02434:

Pssm-ID: 473923  Cd Length: 248  Bit Score: 68.50  E-value: 3.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379887  173 LYVGVMTAQKYLGSRALAAQRTWARFIPGRVEFFSSQQPPNAGQPPPPLPVIalPGVDDSYPPQKKSFMM-IKYmhDHYL 251
Cdd:pfam02434   6 IFIAVKTTKKFHKTRLPLLLKTWISRAKHQTYIFTDGEDEGLPTRTGGHLIN--TNCSAGHCRKALSCKMaVEY--DRFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379887  252 -DKYEWFMRADDDVYIKGDKLEEFLRSLNSSKPLYLGQT---GLGNIEELGKLGLEPGENFCMGGPGMIFSREVLRRMVP 327
Cdd:pfam02434  82 eSGKKWFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyRPIEATERVKGNRKVGFWFATGGAGFCISRGLALKMSP 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 530379887  328 HIGEClrEMYTT------HEDVEVGRCVRR 351
Cdd:pfam02434 162 WASGG--RFMSTsekirlPDDCTLGYIIEN 189
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
328-362 1.31e-15

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 78.07  E-value: 1.31e-15
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 530379887  328 HIGECLREMYTTHEDVEVGRCVRRFGGTQCVWSYE 362
Cdd:pfam05679   1 HLDWCLKNLYSTHEDVELGRCIQKFAGIPCTWSYE 35
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 173-351 3.99e-13

Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls the response of the Notch receptor to specific ligands. FNG is localized to the Golgi apparatus (not secreted as previously thought). Modification of Notch occurs through glycosylation by FNG. The xenopus homolog, lunatic fringe, has been implicated in a variety of functions.


Pssm-ID: 367085  Cd Length: 248  Bit Score: 68.50  E-value: 3.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379887  173 LYVGVMTAQKYLGSRALAAQRTWARFIPGRVEFFSSQQPPNAGQPPPPLPVIalPGVDDSYPPQKKSFMM-IKYmhDHYL 251
Cdd:pfam02434   6 IFIAVKTTKKFHKTRLPLLLKTWISRAKHQTYIFTDGEDEGLPTRTGGHLIN--TNCSAGHCRKALSCKMaVEY--DRFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379887  252 -DKYEWFMRADDDVYIKGDKLEEFLRSLNSSKPLYLGQT---GLGNIEELGKLGLEPGENFCMGGPGMIFSREVLRRMVP 327
Cdd:pfam02434  82 eSGKKWFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyRPIEATERVKGNRKVGFWFATGGAGFCISRGLALKMSP 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 530379887  328 HIGEClrEMYTT------HEDVEVGRCVRR 351
Cdd:pfam02434 162 WASGG--RFMSTsekirlPDDCTLGYIIEN 189
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
328-362 1.31e-15

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 78.07  E-value: 1.31e-15
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 530379887  328 HIGECLREMYTTHEDVEVGRCVRRFGGTQCVWSYE 362
Cdd:pfam05679   1 HLDWCLKNLYSTHEDVELGRCIQKFAGIPCTWSYE 35
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
 173-351 3.99e-13

Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls the response of the Notch receptor to specific ligands. FNG is localized to the Golgi apparatus (not secreted as previously thought). Modification of Notch occurs through glycosylation by FNG. The xenopus homolog, lunatic fringe, has been implicated in a variety of functions.


Pssm-ID: 367085  Cd Length: 248  Bit Score: 68.50  E-value: 3.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379887  173 LYVGVMTAQKYLGSRALAAQRTWARFIPGRVEFFSSQQPPNAGQPPPPLPVIalPGVDDSYPPQKKSFMM-IKYmhDHYL 251
Cdd:pfam02434   6 IFIAVKTTKKFHKTRLPLLLKTWISRAKHQTYIFTDGEDEGLPTRTGGHLIN--TNCSAGHCRKALSCKMaVEY--DRFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530379887  252 -DKYEWFMRADDDVYIKGDKLEEFLRSLNSSKPLYLGQT---GLGNIEELGKLGLEPGENFCMGGPGMIFSREVLRRMVP 327
Cdd:pfam02434  82 eSGKKWFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyRPIEATERVKGNRKVGFWFATGGAGFCISRGLALKMSP 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 530379887  328 HIGEClrEMYTT------HEDVEVGRCVRR 351
Cdd:pfam02434 162 WASGG--RFMSTsekirlPDDCTLGYIIEN 189
 
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