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Conserved domains on  [gi|1039775359|ref|XP_017177147|]
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beta-1,4-N-acetylgalactosaminyltransferase 3 isoform X3 [Mus musculus]

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;
365-682 3.07e-25

Chondroitin N-acetylgalactosaminyltransferase;


The actual alignment was detected with superfamily member pfam05679:

Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 110.04  E-value: 3.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 365 PEQEALE-VTRVFLRKL--SQRTRGRY-QLQRIVNVEKRQDRLRGGRYFLELELldgqrlvrlsEYVSTRGWRggdhpgr 440
Cdd:pfam05679 160 ADKEDLDdVINTAMEEInrNYRPRGRVlEFKQLLNGYRRFDPLRGMEYILDLLL----------EYKKYRGRT------- 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 441 edtearnlqglvwSPRNRHRHVLnaqdpepklcwpQGFSWNH---------RAVVHFIVPVKNQARWVQQFIRDMESLSQ 511
Cdd:pfam05679 223 -------------VPVRRRVYLQ------------RPFSKVEiipmpyvteSTRVHIILPLSGRYETFERFLENYERVCL 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 512 VTGDAHFSIIITDYSSEDM--DVEMALKrSRLRSYQ---------YLKLSGNFERSAGLQAGIDLVkDPHSIIFLCDLHI 580
Cdd:pfam05679 278 ETGENVVLLLVVLYDPDEGqnDVFAEIK-ELIEELEkkypkakipWISVKGEFSRGKALDLGAKKF-PPDSLLFFCDVDM 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 581 HFPAGIIDTIRKHCVEGKMAFAPMV----------MRLHCGATPQWPE-----GYWEVNGFGLLGIYKSDLDKIGGMNTK 645
Cdd:pfam05679 356 VFTPEFLNRCRMNTIQGKQVYFPIVfsqydpevvyYDKPVPTSDDNFDiskdtGHWRRYGFGIVCFYKSDYMAVGGFRTS 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1039775359 646 eFRDrWGGEDWELLDRILQAGLEVERL---SLRNFFHHFH 682
Cdd:pfam05679 436 -IQG-WGLEDVDLYDKFVKSGLHVFRAvepGLVHRYHPRH 473
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
365-682 3.07e-25

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 110.04  E-value: 3.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 365 PEQEALE-VTRVFLRKL--SQRTRGRY-QLQRIVNVEKRQDRLRGGRYFLELELldgqrlvrlsEYVSTRGWRggdhpgr 440
Cdd:pfam05679 160 ADKEDLDdVINTAMEEInrNYRPRGRVlEFKQLLNGYRRFDPLRGMEYILDLLL----------EYKKYRGRT------- 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 441 edtearnlqglvwSPRNRHRHVLnaqdpepklcwpQGFSWNH---------RAVVHFIVPVKNQARWVQQFIRDMESLSQ 511
Cdd:pfam05679 223 -------------VPVRRRVYLQ------------RPFSKVEiipmpyvteSTRVHIILPLSGRYETFERFLENYERVCL 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 512 VTGDAHFSIIITDYSSEDM--DVEMALKrSRLRSYQ---------YLKLSGNFERSAGLQAGIDLVkDPHSIIFLCDLHI 580
Cdd:pfam05679 278 ETGENVVLLLVVLYDPDEGqnDVFAEIK-ELIEELEkkypkakipWISVKGEFSRGKALDLGAKKF-PPDSLLFFCDVDM 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 581 HFPAGIIDTIRKHCVEGKMAFAPMV----------MRLHCGATPQWPE-----GYWEVNGFGLLGIYKSDLDKIGGMNTK 645
Cdd:pfam05679 356 VFTPEFLNRCRMNTIQGKQVYFPIVfsqydpevvyYDKPVPTSDDNFDiskdtGHWRRYGFGIVCFYKSDYMAVGGFRTS 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1039775359 646 eFRDrWGGEDWELLDRILQAGLEVERL---SLRNFFHHFH 682
Cdd:pfam05679 436 -IQG-WGLEDVDLYDKFVKSGLHVFRAvepGLVHRYHPRH 473
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
486-693 6.71e-08

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 53.46  E-value: 6.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 486 VHFIVPVKNQARWVQQFIrdmESLSQVTGDaHFSIIITDYSSEDMDVEMaLKRSRLRSYQYLKLSGNFERSAGLQAGIDL 565
Cdd:COG1216     5 VSVVIPTYNRPELLRRCL---ESLLAQTYP-PFEVIVVDNGSTDGTAEL-LAALAFPRVRVIRNPENLGFAAARNLGLRA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 566 VKDPHsIIFLCDlhihfpagiiDTI-RKHCVEGKMAFAPMVMRlhcgatpqwpegywevngfgllgiyKSDLDKIGGMNT 644
Cdd:COG1216    80 AGGDY-LLFLDD----------DTVvEPDWLERLLAAACLLIR-------------------------REVFEEVGGFDE 123
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1039775359 645 KEFrdrWGGEDWELLDRILQAGLEVERLSLRNFFHHFHSKRGMWNRRQM 693
Cdd:COG1216   124 RFF---LYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYY 169
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
486-694 2.70e-04

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 42.99  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 486 VHFIVPVKNQARWVQQFIRDMesLSQVTGDAHFSIIITDYSSED--MDV--EMALKRSRLRSYQYLKLSgnfeRSAGLQA 561
Cdd:cd02525     2 VSIIIPVRNEEKYIEELLESL--LNQSYPKDLIEIIVVDGGSTDgtREIvqEYAAKDPRIRLIDNPKRI----QSAGLNI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 562 GIDLVKdpHSIIFLCDLHIHFPA-------------------GIIDTIRKHCVEGKMAFAPMVMRLHCGA---TPQWPEG 619
Cdd:cd02525    76 GIRNSR--GDIIIRVDAHAVYPKdyilelvealkrtgadnvgGPMETIGESKFQKAIAVAQSSPLGSGGSayrGGAVKIG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 620 YWEVNGFGLLgiYKSDLDKIGGMNTKEFRdrwgGEDWELLDRILQAGLEV-----------ERLSLRNFFHHFHsKRGMW 688
Cdd:cd02525   154 YVDTVHHGAY--RREVFEKVGGFDESLVR----NEDAELNYRLRKAGYKIwlspdirvyyyPRSTLKKLARQYF-RYGKW 226

                  ....*.
gi 1039775359 689 NRRQMK 694
Cdd:cd02525   227 RARTLR 232
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
365-682 3.07e-25

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 110.04  E-value: 3.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 365 PEQEALE-VTRVFLRKL--SQRTRGRY-QLQRIVNVEKRQDRLRGGRYFLELELldgqrlvrlsEYVSTRGWRggdhpgr 440
Cdd:pfam05679 160 ADKEDLDdVINTAMEEInrNYRPRGRVlEFKQLLNGYRRFDPLRGMEYILDLLL----------EYKKYRGRT------- 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 441 edtearnlqglvwSPRNRHRHVLnaqdpepklcwpQGFSWNH---------RAVVHFIVPVKNQARWVQQFIRDMESLSQ 511
Cdd:pfam05679 223 -------------VPVRRRVYLQ------------RPFSKVEiipmpyvteSTRVHIILPLSGRYETFERFLENYERVCL 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 512 VTGDAHFSIIITDYSSEDM--DVEMALKrSRLRSYQ---------YLKLSGNFERSAGLQAGIDLVkDPHSIIFLCDLHI 580
Cdd:pfam05679 278 ETGENVVLLLVVLYDPDEGqnDVFAEIK-ELIEELEkkypkakipWISVKGEFSRGKALDLGAKKF-PPDSLLFFCDVDM 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 581 HFPAGIIDTIRKHCVEGKMAFAPMV----------MRLHCGATPQWPE-----GYWEVNGFGLLGIYKSDLDKIGGMNTK 645
Cdd:pfam05679 356 VFTPEFLNRCRMNTIQGKQVYFPIVfsqydpevvyYDKPVPTSDDNFDiskdtGHWRRYGFGIVCFYKSDYMAVGGFRTS 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1039775359 646 eFRDrWGGEDWELLDRILQAGLEVERL---SLRNFFHHFH 682
Cdd:pfam05679 436 -IQG-WGLEDVDLYDKFVKSGLHVFRAvepGLVHRYHPRH 473
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
607-682 1.08e-12

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: 63.78  E-value: 1.08e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039775359 607 RLHCGATPQ-WPEGYWEVNGfGLLGIYKSDLDKIGGMNTKEFRdrWGGEDWELLDRILQAGLEVERLS--LRNFFHHFH 682
Cdd:pfam02709   2 HLSVALDKFgYKLPYKTYFG-GVLALSREDFERINGFSNGFWG--WGGEDDDLYNRLLLAGLEIERPPgdIGRYYMLYH 77
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
486-693 6.71e-08

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 53.46  E-value: 6.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 486 VHFIVPVKNQARWVQQFIrdmESLSQVTGDaHFSIIITDYSSEDMDVEMaLKRSRLRSYQYLKLSGNFERSAGLQAGIDL 565
Cdd:COG1216     5 VSVVIPTYNRPELLRRCL---ESLLAQTYP-PFEVIVVDNGSTDGTAEL-LAALAFPRVRVIRNPENLGFAAARNLGLRA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 566 VKDPHsIIFLCDlhihfpagiiDTI-RKHCVEGKMAFAPMVMRlhcgatpqwpegywevngfgllgiyKSDLDKIGGMNT 644
Cdd:COG1216    80 AGGDY-LLFLDD----------DTVvEPDWLERLLAAACLLIR-------------------------REVFEEVGGFDE 123
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1039775359 645 KEFrdrWGGEDWELLDRILQAGLEVERLSLRNFFHHFHSKRGMWNRRQM 693
Cdd:COG1216   124 RFF---LYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYY 169
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
486-694 2.70e-04

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 42.99  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 486 VHFIVPVKNQARWVQQFIRDMesLSQVTGDAHFSIIITDYSSED--MDV--EMALKRSRLRSYQYLKLSgnfeRSAGLQA 561
Cdd:cd02525     2 VSIIIPVRNEEKYIEELLESL--LNQSYPKDLIEIIVVDGGSTDgtREIvqEYAAKDPRIRLIDNPKRI----QSAGLNI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 562 GIDLVKdpHSIIFLCDLHIHFPA-------------------GIIDTIRKHCVEGKMAFAPMVMRLHCGA---TPQWPEG 619
Cdd:cd02525    76 GIRNSR--GDIIIRVDAHAVYPKdyilelvealkrtgadnvgGPMETIGESKFQKAIAVAQSSPLGSGGSayrGGAVKIG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 620 YWEVNGFGLLgiYKSDLDKIGGMNTKEFRdrwgGEDWELLDRILQAGLEV-----------ERLSLRNFFHHFHsKRGMW 688
Cdd:cd02525   154 YVDTVHHGAY--RREVFEKVGGFDESLVR----NEDAELNYRLRKAGYKIwlspdirvyyyPRSTLKKLARQYF-RYGKW 226

                  ....*.
gi 1039775359 689 NRRQMK 694
Cdd:cd02525   227 RARTLR 232
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
489-693 2.72e-04

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 42.77  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 489 IVPVKNQARWVQQFIrdmESLSQVTGdAHFSIIITDYSSED--MDV--EMALKRSRLRsyqYLKLSGNFERSAGLQAGID 564
Cdd:COG0463     7 VIPTYNEEEYLEEAL---ESLLAQTY-PDFEIIVVDDGSTDgtAEIlrELAAKDPRIR---VIRLERNRGKGAARNAGLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 565 LVKDPHsIIFL-CDLhIHFPAGI---IDTIRKHCVEgkMAFAPMVMRLHCGATPQWPEGYWEV---------NGFGLLGI 631
Cdd:COG0463    80 AARGDY-IAFLdADD-QLDPEKLeelVAALEEGPAD--LVYGSRLIREGESDLRRLGSRLFNLvrlltnlpdSTSGFRLF 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039775359 632 YKSDLDKIGgmntkeFRDRWgGEDWELLdRILQAGLEVERLSlrnffHHFHSKRGMWNRRQM 693
Cdd:COG0463   156 RREVLEELG------FDEGF-LEDTELL-RALRHGFRIAEVP-----VRYRAGESKLNLRDL 204
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
486-691 1.07e-03

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 41.65  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 486 VHFIVPVKNQARWVQQFIRDMesLSQVTGDAHFSIII-----TDYSSEDMDvEMALKRSRLRsyqYLKLSGNFERSAGLQ 560
Cdd:COG1215    31 VSVIIPAYNEEAVIEETLRSL--LAQDYPKEKLEVIVvddgsTDETAEIAR-ELAAEYPRVR---VIERPENGGKAAALN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039775359 561 AGIDLVKdpHSIIFLCDLHIHFPAGIIDTIRKHCVEGKMAFapmvmrlhCGATpqwpegywevngfglLGIYKSDLDKIG 640
Cdd:COG1215   105 AGLKAAR--GDIVVFLDADTVLDPDWLRRLVAAFADPGVGA--------SGAN---------------LAFRREALEEVG 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039775359 641 GmntkeFRDRWGGEDWELLDRILQAGLEVERLSLRNFFHHF-HSKRGMWNRR 691
Cdd:COG1215   160 G-----FDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEApETLRALFRQR 206
 
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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