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Conserved domains on  [gi|767951034|ref|XP_011542887|]
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chondroitin sulfate N-acetylgalactosaminyltransferase 1 isoform X2 [Homo sapiens]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

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
CHGN super family cl47930
Chondroitin N-acetylgalactosaminyltransferase;
12-259 1.71e-85

Chondroitin N-acetylgalactosaminyltransferase;


The actual alignment was detected with superfamily member pfam05679:

Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 264.51  E-value: 1.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951034   12 NTLINVIVPLAKRVDKFRQFMQNFREMCIEQDGRV-HLTVVYFGKEE-----INEVKGILENTSKAANFRNFTFIQLNGE 85
Cdd:pfam05679 249 STRVHIILPLSGRYETFERFLENYERVCLETGENVvLLLVVLYDPDEgqndvFAEIKELIEELEKKYPKAKIPWISVKGE 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951034   86 FSRGKGLDVGAR-FwkGSNVLLFFCDVDIYFTSEFLNTCRLNTQPGKKVFYPVLFSQYNPGIIYgHHDAVPPLEQQLVIK 164
Cdd:pfam05679 329 FSRGKALDLGAKkF--PPDSLLFFCDVDMVFTPEFLNRCRMNTIQGKQVYFPIVFSQYDPEVVY-YDKPVPTSDDNFDIS 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951034  165 KETGFWRDFGFGMTCQYRSDFINIGGFDLDIKGWGGEDVHLYRKYLHSNLIVVRTPVRGLFHLWHEKRCMDELTPEQYKM 244
Cdd:pfam05679 406 KDTGHWRRYGFGIVCFYKSDYMAVGGFRTSIQGWGLEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHM 485

                         250
                  ....*....|....*
gi 767951034  245 CMQSKAMNEASHGQL 259
Cdd:pfam05679 486 CLGSKAEGLASRTQL 500
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
12-259 1.71e-85

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 264.51  E-value: 1.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951034   12 NTLINVIVPLAKRVDKFRQFMQNFREMCIEQDGRV-HLTVVYFGKEE-----INEVKGILENTSKAANFRNFTFIQLNGE 85
Cdd:pfam05679 249 STRVHIILPLSGRYETFERFLENYERVCLETGENVvLLLVVLYDPDEgqndvFAEIKELIEELEKKYPKAKIPWISVKGE 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951034   86 FSRGKGLDVGAR-FwkGSNVLLFFCDVDIYFTSEFLNTCRLNTQPGKKVFYPVLFSQYNPGIIYgHHDAVPPLEQQLVIK 164
Cdd:pfam05679 329 FSRGKALDLGAKkF--PPDSLLFFCDVDMVFTPEFLNRCRMNTIQGKQVYFPIVFSQYDPEVVY-YDKPVPTSDDNFDIS 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951034  165 KETGFWRDFGFGMTCQYRSDFINIGGFDLDIKGWGGEDVHLYRKYLHSNLIVVRTPVRGLFHLWHEKRCMDELTPEQYKM 244
Cdd:pfam05679 406 KDTGHWRRYGFGIVCFYKSDYMAVGGFRTSIQGWGLEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHM 485

                         250
                  ....*....|....*
gi 767951034  245 CMQSKAMNEASHGQL 259
Cdd:pfam05679 486 CLGSKAEGLASRTQL 500
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 181-228 1.64e-04

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 41.41  E-value: 1.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767951034 181 YRSDFINIGGFDLDIKGWGGEDVHL-YRkyLHSNLIVVRTPVRG--LFHLW 228
Cdd:cd06420  134 WKKDLLAVNGFDEEFTGWGGEDSELvAR--LLNSGIKFRKLKFAaiVFHLW 182
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
12-259 1.71e-85

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 264.51  E-value: 1.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951034   12 NTLINVIVPLAKRVDKFRQFMQNFREMCIEQDGRV-HLTVVYFGKEE-----INEVKGILENTSKAANFRNFTFIQLNGE 85
Cdd:pfam05679 249 STRVHIILPLSGRYETFERFLENYERVCLETGENVvLLLVVLYDPDEgqndvFAEIKELIEELEKKYPKAKIPWISVKGE 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951034   86 FSRGKGLDVGAR-FwkGSNVLLFFCDVDIYFTSEFLNTCRLNTQPGKKVFYPVLFSQYNPGIIYgHHDAVPPLEQQLVIK 164
Cdd:pfam05679 329 FSRGKALDLGAKkF--PPDSLLFFCDVDMVFTPEFLNRCRMNTIQGKQVYFPIVFSQYDPEVVY-YDKPVPTSDDNFDIS 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951034  165 KETGFWRDFGFGMTCQYRSDFINIGGFDLDIKGWGGEDVHLYRKYLHSNLIVVRTPVRGLFHLWHEKRCMDELTPEQYKM 244
Cdd:pfam05679 406 KDTGHWRRYGFGIVCFYKSDYMAVGGFRTSIQGWGLEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHM 485

                         250
                  ....*....|....*
gi 767951034  245 CMQSKAMNEASHGQL 259
Cdd:pfam05679 486 CLGSKAEGLASRTQL 500
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 181-230 6.38e-07

N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 46.07  E-value: 6.38e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767951034  181 YRSDFINIGGFDLDIKGWGGEDVHLYRKYLHSNLIVVRTP--VRGLFHLWHE 230
Cdd:pfam02709  27 SREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPgdIGRYYMLYHK 78
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 181-228 1.64e-04

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 41.41  E-value: 1.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767951034 181 YRSDFINIGGFDLDIKGWGGEDVHL-YRkyLHSNLIVVRTPVRG--LFHLW 228
Cdd:cd06420  134 WKKDLLAVNGFDEEFTGWGGEDSELvAR--LLNSGIKFRKLKFAaiVFHLW 182
 
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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