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Conserved domains on  [gi|329663910|ref|NP_001192582|]
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chondroitin sulfate N-acetylgalactosaminyltransferase 2 [Bos taurus]

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;
75-516 8.15e-90

Chondroitin N-acetylgalactosaminyltransferase;


The actual alignment was detected with superfamily member pfam05679:

Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 284.92  E-value: 8.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910   75 LKRQIAQLKQELQEMSEKMRSLQERKNVGANGISYQgnkeqapsdlleflhsqidkaevsIGAKLP-----SEYGVIPFE 149
Cdd:pfam05679  83 LSLELQKLRQEIIKLQREIKNMSELLPEGIDSLSWP------------------------LGIPPPlnrpkSRFDVLRWD 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910  150 SFTLMKVFqlemgltRHPEEKPVR---KDKRDELVEVIEAGLEVINNpdeddeqedEDGPLGEKLIFNEndFVEGYYRTE 226
Cdd:pfam05679 139 YFTETHLY-------SADDGQPRRrldGADKEDLDDVINTAMEEINR---------NYRPRGRVLEFKQ--LLNGYRRFD 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910  227 KDKGTQYEL-------FFKKADLMEYRHVTLFRPFGPLmKVKSEMIDITRSVINIIVPLAGRTEAFAQFMQNFRDVCIHQ 299
Cdd:pfam05679 201 PLRGMEYILdllleykKYRGRTVPVRRRVYLQRPFSKV-EIIPMPYVTESTRVHIILPLSGRYETFERFLENYERVCLET 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910  300 -DKRIHLTVVYFGKEGLS-----KVKSILESVASESNFHNYTLVSLNEEFNRGRGLNVGARAWDKGEvLMFFCDVDIYFS 373
Cdd:pfam05679 280 gENVVLLLVVLYDPDEGQndvfaEIKELIEELEKKYPKAKIPWISVKGEFSRGKALDLGAKKFPPDS-LLFFCDVDMVFT 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910  374 AEFLNSCRLNAEPGKKVFYPVVFSLYNPAIVYANLDVPPPVEQQLVHKkDSGFWRDFGFGMTCQYQSDFLTIGGFDMEVK 453
Cdd:pfam05679 359 PEFLNRCRMNTIQGKQVYFPIVFSQYDPEVVYYDKPVPTSDDNFDISK-DTGHWRRYGFGIVCFYKSDYMAVGGFRTSIQ 437
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 329663910  454 GWGGEDVHLYRKYLHSDLIVIRTPVPGLFHLWHEKRCADELTPEQYRMCIQSKAMNEASHSHL 516
Cdd:pfam05679 438 GWGLEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHMCLGSKAEGLASRTQL 500
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
75-516 8.15e-90

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 284.92  E-value: 8.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910   75 LKRQIAQLKQELQEMSEKMRSLQERKNVGANGISYQgnkeqapsdlleflhsqidkaevsIGAKLP-----SEYGVIPFE 149
Cdd:pfam05679  83 LSLELQKLRQEIIKLQREIKNMSELLPEGIDSLSWP------------------------LGIPPPlnrpkSRFDVLRWD 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910  150 SFTLMKVFqlemgltRHPEEKPVR---KDKRDELVEVIEAGLEVINNpdeddeqedEDGPLGEKLIFNEndFVEGYYRTE 226
Cdd:pfam05679 139 YFTETHLY-------SADDGQPRRrldGADKEDLDDVINTAMEEINR---------NYRPRGRVLEFKQ--LLNGYRRFD 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910  227 KDKGTQYEL-------FFKKADLMEYRHVTLFRPFGPLmKVKSEMIDITRSVINIIVPLAGRTEAFAQFMQNFRDVCIHQ 299
Cdd:pfam05679 201 PLRGMEYILdllleykKYRGRTVPVRRRVYLQRPFSKV-EIIPMPYVTESTRVHIILPLSGRYETFERFLENYERVCLET 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910  300 -DKRIHLTVVYFGKEGLS-----KVKSILESVASESNFHNYTLVSLNEEFNRGRGLNVGARAWDKGEvLMFFCDVDIYFS 373
Cdd:pfam05679 280 gENVVLLLVVLYDPDEGQndvfaEIKELIEELEKKYPKAKIPWISVKGEFSRGKALDLGAKKFPPDS-LLFFCDVDMVFT 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910  374 AEFLNSCRLNAEPGKKVFYPVVFSLYNPAIVYANLDVPPPVEQQLVHKkDSGFWRDFGFGMTCQYQSDFLTIGGFDMEVK 453
Cdd:pfam05679 359 PEFLNRCRMNTIQGKQVYFPIVFSQYDPEVVYYDKPVPTSDDNFDISK-DTGHWRRYGFGIVCFYKSDYMAVGGFRTSIQ 437
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 329663910  454 GWGGEDVHLYRKYLHSDLIVIRTPVPGLFHLWHEKRCADELTPEQYRMCIQSKAMNEASHSHL 516
Cdd:pfam05679 438 GWGLEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHMCLGSKAEGLASRTQL 500
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
343-485 6.87e-03

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: 37.94  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910 343 FNRGRGLNVGARAwDKGEVLMFFcDVDIYFSAEFLNSCRLNAEPGKKVFYPVVFslynpaivyanldVPPPVEQQLVHKK 422
Cdd:cd06420   65 FRKAKIRNKAIAA-AKGDYLIFI-DGDCIPHPDFIADHIELAEPGVFLSGSRVL-------------LNEKLTERGIRGC 129
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 329663910 423 DSGFWRdfgfgmtcqyqSDFLTIGGFDMEVKGWGGED----VHLYRKYLHSDLIVIRTPVpglFHLW 485
Cdd:cd06420  130 NMSFWK-----------KDLLAVNGFDEEFTGWGGEDselvARLLNSGIKFRKLKFAAIV---FHLW 182
PilN COG3166
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
56-128 7.54e-03

Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];


Pssm-ID: 442399 [Multi-domain]  Cd Length: 185  Bit Score: 37.64  E-value: 7.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 329663910  56 YYQALLQEQEEhyqtRATSLKRQIAQLKQELQEMSE---KMRSLQERKNVgangISYQGNKEQAPSDLLEFLHSQI 128
Cdd:COG3166   42 YLQGQIAQQQA----RNAALQQEIAKLDKQIAEIKElkkQKAELLARLQV----IEQLQQSRPPWVHLLDELARLL 109
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
75-516 8.15e-90

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 284.92  E-value: 8.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910   75 LKRQIAQLKQELQEMSEKMRSLQERKNVGANGISYQgnkeqapsdlleflhsqidkaevsIGAKLP-----SEYGVIPFE 149
Cdd:pfam05679  83 LSLELQKLRQEIIKLQREIKNMSELLPEGIDSLSWP------------------------LGIPPPlnrpkSRFDVLRWD 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910  150 SFTLMKVFqlemgltRHPEEKPVR---KDKRDELVEVIEAGLEVINNpdeddeqedEDGPLGEKLIFNEndFVEGYYRTE 226
Cdd:pfam05679 139 YFTETHLY-------SADDGQPRRrldGADKEDLDDVINTAMEEINR---------NYRPRGRVLEFKQ--LLNGYRRFD 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910  227 KDKGTQYEL-------FFKKADLMEYRHVTLFRPFGPLmKVKSEMIDITRSVINIIVPLAGRTEAFAQFMQNFRDVCIHQ 299
Cdd:pfam05679 201 PLRGMEYILdllleykKYRGRTVPVRRRVYLQRPFSKV-EIIPMPYVTESTRVHIILPLSGRYETFERFLENYERVCLET 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910  300 -DKRIHLTVVYFGKEGLS-----KVKSILESVASESNFHNYTLVSLNEEFNRGRGLNVGARAWDKGEvLMFFCDVDIYFS 373
Cdd:pfam05679 280 gENVVLLLVVLYDPDEGQndvfaEIKELIEELEKKYPKAKIPWISVKGEFSRGKALDLGAKKFPPDS-LLFFCDVDMVFT 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910  374 AEFLNSCRLNAEPGKKVFYPVVFSLYNPAIVYANLDVPPPVEQQLVHKkDSGFWRDFGFGMTCQYQSDFLTIGGFDMEVK 453
Cdd:pfam05679 359 PEFLNRCRMNTIQGKQVYFPIVFSQYDPEVVYYDKPVPTSDDNFDISK-DTGHWRRYGFGIVCFYKSDYMAVGGFRTSIQ 437
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 329663910  454 GWGGEDVHLYRKYLHSDLIVIRTPVPGLFHLWHEKRCADELTPEQYRMCIQSKAMNEASHSHL 516
Cdd:pfam05679 438 GWGLEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHMCLGSKAEGLASRTQL 500
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
438-487 1.21e-05

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: 43.37  E-value: 1.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 329663910  438 YQSDFLTIGGFDMEVKGWGGEDVHLYRKYLHSDLIVIRTP--VPGLFHLWHE 487
Cdd:pfam02709  27 SREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPgdIGRYYMLYHK 78
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
343-485 6.87e-03

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: 37.94  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329663910 343 FNRGRGLNVGARAwDKGEVLMFFcDVDIYFSAEFLNSCRLNAEPGKKVFYPVVFslynpaivyanldVPPPVEQQLVHKK 422
Cdd:cd06420   65 FRKAKIRNKAIAA-AKGDYLIFI-DGDCIPHPDFIADHIELAEPGVFLSGSRVL-------------LNEKLTERGIRGC 129
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 329663910 423 DSGFWRdfgfgmtcqyqSDFLTIGGFDMEVKGWGGED----VHLYRKYLHSDLIVIRTPVpglFHLW 485
Cdd:cd06420  130 NMSFWK-----------KDLLAVNGFDEEFTGWGGEDselvARLLNSGIKFRKLKFAAIV---FHLW 182
PilN COG3166
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
56-128 7.54e-03

Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];


Pssm-ID: 442399 [Multi-domain]  Cd Length: 185  Bit Score: 37.64  E-value: 7.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 329663910  56 YYQALLQEQEEhyqtRATSLKRQIAQLKQELQEMSE---KMRSLQERKNVgangISYQGNKEQAPSDLLEFLHSQI 128
Cdd:COG3166   42 YLQGQIAQQQA----RNAALQQEIAKLDKQIAEIKElkkQKAELLARLQV----IEQLQQSRPPWVHLLDELARLL 109
 
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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