NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1237938342|ref|NP_001341413|]
View 

chondroitin sulfate N-acetylgalactosaminyltransferase 1 [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

 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;
70-507 8.91e-90

Chondroitin N-acetylgalactosaminyltransferase;


The actual alignment was detected with superfamily member pfam05679:

Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 284.15  E-value: 8.91e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342  70 NYVSSLK-----RQIAQLKEELQERSEQLRNGQYQASDAAGLGLDRSPPEKtqadllaflHSQVdkaevnagvklateya 144
Cdd:pfam05679  80 KYFLSLElqklrQEIIKLQREIKNMSELLPEGIDSLSWPLGIPPPLNRPKS---------RFDV---------------- 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 145 aVPFDSFTLQKVYQLETGLTRHPeekpVRKDKRDELVEAIESALETLNSpaeNSPNHRPytASDFIE---GIYRTERDKG 221
Cdd:pfam05679 135 -LRWDYFTETHLYSADDGQPRRR----LDGADKEDLDDVINTAMEEINR---NYRPRGR--VLEFKQllnGYRRFDPLRG 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 222 TLY----ELTFKGDHKHEF---KRLILFRPFGPIMKVKNEKlNMANTLINVIVPLAKRVDKFRQFMQNFREMCIEQDGRV 294
Cdd:pfam05679 205 MEYildlLLEYKKYRGRTVpvrRRVYLQRPFSKVEIIPMPY-VTESTRVHIILPLSGRYETFERFLENYERVCLETGENV 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 295 -HLTVVYFGKEE-----INEVKGILENTSKAANFRNFTFIQLNGEFSRGKGLDVGAR-FwkGSNVLLFFCDVDIYFTSEF 367
Cdd:pfam05679 284 vLLLVVLYDPDEgqndvFAEIKELIEELEKKYPKAKIPWISVKGEFSRGKALDLGAKkF--PPDSLLFFCDVDMVFTPEF 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 368 LNTCRLNTQPGKKVFYPVLFSQYNPGIIYgHHDAVPPLEQQLVIKKETGFWRDFGFGMTCQYRSDFINIGGFDLDIKGWG 447
Cdd:pfam05679 362 LNRCRMNTIQGKQVYFPIVFSQYDPEVVY-YDKPVPTSDDNFDISKDTGHWRRYGFGIVCFYKSDYMAVGGFRTSIQGWG 440
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 448 GEDVHLYRKYLHSNLIVVRTPVRGLFHLWHEKRCMDELTPEQYKMCMQSKAMNEASHGQL 507
Cdd:pfam05679 441 LEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHMCLGSKAEGLASRTQL 500
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
70-507 8.91e-90

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 284.15  E-value: 8.91e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342  70 NYVSSLK-----RQIAQLKEELQERSEQLRNGQYQASDAAGLGLDRSPPEKtqadllaflHSQVdkaevnagvklateya 144
Cdd:pfam05679  80 KYFLSLElqklrQEIIKLQREIKNMSELLPEGIDSLSWPLGIPPPLNRPKS---------RFDV---------------- 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 145 aVPFDSFTLQKVYQLETGLTRHPeekpVRKDKRDELVEAIESALETLNSpaeNSPNHRPytASDFIE---GIYRTERDKG 221
Cdd:pfam05679 135 -LRWDYFTETHLYSADDGQPRRR----LDGADKEDLDDVINTAMEEINR---NYRPRGR--VLEFKQllnGYRRFDPLRG 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 222 TLY----ELTFKGDHKHEF---KRLILFRPFGPIMKVKNEKlNMANTLINVIVPLAKRVDKFRQFMQNFREMCIEQDGRV 294
Cdd:pfam05679 205 MEYildlLLEYKKYRGRTVpvrRRVYLQRPFSKVEIIPMPY-VTESTRVHIILPLSGRYETFERFLENYERVCLETGENV 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 295 -HLTVVYFGKEE-----INEVKGILENTSKAANFRNFTFIQLNGEFSRGKGLDVGAR-FwkGSNVLLFFCDVDIYFTSEF 367
Cdd:pfam05679 284 vLLLVVLYDPDEgqndvFAEIKELIEELEKKYPKAKIPWISVKGEFSRGKALDLGAKkF--PPDSLLFFCDVDMVFTPEF 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 368 LNTCRLNTQPGKKVFYPVLFSQYNPGIIYgHHDAVPPLEQQLVIKKETGFWRDFGFGMTCQYRSDFINIGGFDLDIKGWG 447
Cdd:pfam05679 362 LNRCRMNTIQGKQVYFPIVFSQYDPEVVY-YDKPVPTSDDNFDISKDTGHWRRYGFGIVCFYKSDYMAVGGFRTSIQGWG 440
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 448 GEDVHLYRKYLHSNLIVVRTPVRGLFHLWHEKRCMDELTPEQYKMCMQSKAMNEASHGQL 507
Cdd:pfam05679 441 LEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHMCLGSKAEGLASRTQL 500
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
429-476 1.96e-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: 42.18  E-value: 1.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938342 429 YRSDFINIGGFDLDIKGWGGEDVHL-YRkyLHSNLIVVRTPVRG--LFHLW 476
Cdd:cd06420   134 WKKDLLAVNGFDEEFTGWGGEDSELvAR--LLNSGIKFRKLKFAaiVFHLW 182
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
70-507 8.91e-90

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 284.15  E-value: 8.91e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342  70 NYVSSLK-----RQIAQLKEELQERSEQLRNGQYQASDAAGLGLDRSPPEKtqadllaflHSQVdkaevnagvklateya 144
Cdd:pfam05679  80 KYFLSLElqklrQEIIKLQREIKNMSELLPEGIDSLSWPLGIPPPLNRPKS---------RFDV---------------- 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 145 aVPFDSFTLQKVYQLETGLTRHPeekpVRKDKRDELVEAIESALETLNSpaeNSPNHRPytASDFIE---GIYRTERDKG 221
Cdd:pfam05679 135 -LRWDYFTETHLYSADDGQPRRR----LDGADKEDLDDVINTAMEEINR---NYRPRGR--VLEFKQllnGYRRFDPLRG 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 222 TLY----ELTFKGDHKHEF---KRLILFRPFGPIMKVKNEKlNMANTLINVIVPLAKRVDKFRQFMQNFREMCIEQDGRV 294
Cdd:pfam05679 205 MEYildlLLEYKKYRGRTVpvrRRVYLQRPFSKVEIIPMPY-VTESTRVHIILPLSGRYETFERFLENYERVCLETGENV 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 295 -HLTVVYFGKEE-----INEVKGILENTSKAANFRNFTFIQLNGEFSRGKGLDVGAR-FwkGSNVLLFFCDVDIYFTSEF 367
Cdd:pfam05679 284 vLLLVVLYDPDEgqndvFAEIKELIEELEKKYPKAKIPWISVKGEFSRGKALDLGAKkF--PPDSLLFFCDVDMVFTPEF 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 368 LNTCRLNTQPGKKVFYPVLFSQYNPGIIYgHHDAVPPLEQQLVIKKETGFWRDFGFGMTCQYRSDFINIGGFDLDIKGWG 447
Cdd:pfam05679 362 LNRCRMNTIQGKQVYFPIVFSQYDPEVVY-YDKPVPTSDDNFDISKDTGHWRRYGFGIVCFYKSDYMAVGGFRTSIQGWG 440
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237938342 448 GEDVHLYRKYLHSNLIVVRTPVRGLFHLWHEKRCMDELTPEQYKMCMQSKAMNEASHGQL 507
Cdd:pfam05679 441 LEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHMCLGSKAEGLASRTQL 500
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
429-478 2.52e-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: 47.99  E-value: 2.52e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1237938342 429 YRSDFINIGGFDLDIKGWGGEDVHLYRKYLHSNLIVVRTP--VRGLFHLWHE 478
Cdd:pfam02709  27 SREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPgdIGRYYMLYHK 78
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
429-476 1.96e-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: 42.18  E-value: 1.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1237938342 429 YRSDFINIGGFDLDIKGWGGEDVHL-YRkyLHSNLIVVRTPVRG--LFHLW 476
Cdd:cd06420   134 WKKDLLAVNGFDEEFTGWGGEDSELvAR--LLNSGIKFRKLKFAaiVFHLW 182
Lzipper-MIP1 pfam14389
Leucine-zipper of ternary complex factor MIP1; This leucine-zipper is towards the N-terminus ...
67-120 5.68e-03

Leucine-zipper of ternary complex factor MIP1; This leucine-zipper is towards the N-terminus of MIP1 proteins. These proteins, here largely from plants, are subunits of the TORC2 (rictor-mTOR) protein complex controlling cell growth and proliferation. The leucine-zipper is likely to be the region that interacts with plant MADS-box factors,


Pssm-ID: 464163 [Multi-domain]  Cd Length: 82  Bit Score: 35.99  E-value: 5.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1237938342  67 QHRNYVSSLKRQIAQLKEELQErsEQ-----LRNGQYQASDAAGLGLDRSPPEKTQADL 120
Cdd:pfam14389   1 ALNEKRSSLEQEVEQLQEQLQD--EEdlrraLEKALSNSPDGSLPSLSSLLPPKAKELL 57
 
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