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Conserved domains on  [gi|951046307|ref|XP_014464070|]
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beta-1,4 N-acetylgalactosaminyltransferase 1 isoform X1 [Alligator mississippiensis]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10455355)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  12691742|9445404
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 291-411 1.38e-14

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


:

Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 71.66  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307  291 TVATKTFLRYDKLRALIASVRR-FYPSITIVVADDSPQPE--------RLVGPHLEHYLMPFGKGWFAGRNLAISQVATK 361
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNqTYPNFEIIVVDDGSTDGtveiaeeyAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 951046307  362 YVLWVDDDFIFTPRtRLEKLVDVLEKTSLDLVGGAVREITGYSATYRHKI 411
Cdd:pfam00535  81 YIAFLDADDEVPPD-WLEKLVEALEEDGADVVVGSRYVIFGETGEYRRAS 129
 
Name Accession Description Interval E-value
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 291-411 1.38e-14

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 71.66  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307  291 TVATKTFLRYDKLRALIASVRR-FYPSITIVVADDSPQPE--------RLVGPHLEHYLMPFGKGWFAGRNLAISQVATK 361
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNqTYPNFEIIVVDDGSTDGtveiaeeyAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 951046307  362 YVLWVDDDFIFTPRtRLEKLVDVLEKTSLDLVGGAVREITGYSATYRHKI 411
Cdd:pfam00535  81 YIAFLDADDEVPPD-WLEKLVEALEEDGADVVVGSRYVIFGETGEYRRAS 129
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
287-395 1.91e-09

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 57.70  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307 287 SALVTVATKTFLRYDKLRALIASVRRF-YPSITIVVADDSPQP------ERLVGPHLEHYLMPFGKGWFAGRNLAISQVA 359
Cdd:COG1216    2 RPKVSVVIPTYNRPELLRRCLESLLAQtYPPFEVIVVDNGSTDgtaellAALAFPRVRVIRNPENLGFAAARNLGLRAAG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 951046307 360 TKYVLWVDDDFIFTPRTrLEKLVDV----LEKTSLDLVGG 395
Cdd:COG1216   82 GDYLLFLDDDTVVEPDW-LERLLAAacllIRREVFEEVGG 120
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
 299-387 7.12e-06

glycosyltransferase domain; This model describes a putative glycotransferase domain, related to the group 2 family glycosyltransferases of pfam00535.


Pssm-ID: 275233  Cd Length: 215  Bit Score: 47.29  E-value: 7.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307  299 RYDKLRALIASVRRFYPSITIVVADDSPQPERLV---------GPHLEHYLMPFGKGWFAGRNL-AISQVATKYVLWVDD 368
Cdd:TIGR04440  11 RPEYLKRWLRYYSDFGCDYRIIIADSSDEKFNENnlkvfknysNPNITYLHYPDLGVPFYEKLLdALEQVETPYVVICAD 90

                          90
                  ....*....|....*....
gi 951046307  369 DFIFTPRTrLEKLVDVLEK 387
Cdd:TIGR04440  91 DDFIIPSG-LTECLSFLEA 108
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 303-396 1.30e-05

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that 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. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 45.57  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307 303 LRALIASVRR-FYPSITIVVADD--SPQPERLV------GPHLEHYLMPFGKGWFAGRNLAISQVATKYVLWVDDDFIFT 373
Cdd:cd00761   12 LERCLESLLAqTYPNFEVIVVDDgsTDGTLEILeeyakkDPRVIRVINEENQGLAAARNAGLKAARGEYILFLDADDLLL 91

                         90       100
                 ....*....|....*....|....
gi 951046307 374 PrTRLEKLVDVLEK-TSLDLVGGA 396
Cdd:cd00761   92 P-DWLERLVAELLAdPEADAVGGP 114
 
Name Accession Description Interval E-value
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 291-411 1.38e-14

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 71.66  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307  291 TVATKTFLRYDKLRALIASVRR-FYPSITIVVADDSPQPE--------RLVGPHLEHYLMPFGKGWFAGRNLAISQVATK 361
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNqTYPNFEIIVVDDGSTDGtveiaeeyAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 951046307  362 YVLWVDDDFIFTPRtRLEKLVDVLEKTSLDLVGGAVREITGYSATYRHKI 411
Cdd:pfam00535  81 YIAFLDADDEVPPD-WLEKLVEALEEDGADVVVGSRYVIFGETGEYRRAS 129
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
287-395 1.91e-09

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 57.70  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307 287 SALVTVATKTFLRYDKLRALIASVRRF-YPSITIVVADDSPQP------ERLVGPHLEHYLMPFGKGWFAGRNLAISQVA 359
Cdd:COG1216    2 RPKVSVVIPTYNRPELLRRCLESLLAQtYPPFEVIVVDNGSTDgtaellAALAFPRVRVIRNPENLGFAAARNLGLRAAG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 951046307 360 TKYVLWVDDDFIFTPRTrLEKLVDV----LEKTSLDLVGG 395
Cdd:COG1216   82 GDYLLFLDDDTVVEPDW-LERLLAAacllIRREVFEEVGG 120
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 303-466 2.65e-09

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 57.40  E-value: 2.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307 303 LRALIASVRRF-YPSITIVVADD-SPQ--PERL-----VGPHLEHYLMPFGKGWFAGRNLAISQVATKYVLWVDDDFIFT 373
Cdd:COG0463   17 LEEALESLLAQtYPDFEIIVVDDgSTDgtAEILrelaaKDPRIRVIRLERNRGKGAARNAGLAAARGDYIAFLDADDQLD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307 374 PRtRLEKLVDVLEKTSLDLVGGaVREITGYSATYRHKISvepggPEGDCLRVVPGWHHPIAGfpgcvvadgvinFFLART 453
Cdd:COG0463   97 PE-KLEELVAALEEGPADLVYG-SRLIREGESDLRRLGS-----RLFNLVRLLTNLPDSTSG------------FRLFRR 157

                        170
                 ....*....|...
gi 951046307 454 DKVRQVGFDPRLS 466
Cdd:COG0463  158 EVLEELGFDEGFL 170
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
 299-387 7.12e-06

glycosyltransferase domain; This model describes a putative glycotransferase domain, related to the group 2 family glycosyltransferases of pfam00535.


Pssm-ID: 275233  Cd Length: 215  Bit Score: 47.29  E-value: 7.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307  299 RYDKLRALIASVRRFYPSITIVVADDSPQPERLV---------GPHLEHYLMPFGKGWFAGRNL-AISQVATKYVLWVDD 368
Cdd:TIGR04440  11 RPEYLKRWLRYYSDFGCDYRIIIADSSDEKFNENnlkvfknysNPNITYLHYPDLGVPFYEKLLdALEQVETPYVVICAD 90

                          90
                  ....*....|....*....
gi 951046307  369 DFIFTPRTrLEKLVDVLEK 387
Cdd:TIGR04440  91 DDFIIPSG-LTECLSFLEA 108
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 303-396 1.30e-05

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that 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. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 45.57  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307 303 LRALIASVRR-FYPSITIVVADD--SPQPERLV------GPHLEHYLMPFGKGWFAGRNLAISQVATKYVLWVDDDFIFT 373
Cdd:cd00761   12 LERCLESLLAqTYPNFEVIVVDDgsTDGTLEILeeyakkDPRVIRVINEENQGLAAARNAGLKAARGEYILFLDADDLLL 91

                         90       100
                 ....*....|....*....|....
gi 951046307 374 PrTRLEKLVDVLEK-TSLDLVGGA 396
Cdd:cd00761   92 P-DWLERLVAELLAdPEADAVGGP 114
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 303-405 2.08e-04

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: 43.58  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307 303 LRALIASVRRF-YPS--ITIVVADDSPQPE--------RLVGPHLEHYLMPF--GKGWfaGRNLAISQVATKYVLWVDDD 369
Cdd:COG1215   44 IEETLRSLLAQdYPKekLEVIVVDDGSTDEtaeiarelAAEYPRVRVIERPEngGKAA--ALNAGLKAARGDIVVFLDAD 121

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 951046307 370 FIFTPRTrLEKLVDVLEKTSLDLVGG-------AVREITGYSA 405
Cdd:COG1215  122 TVLDPDW-LRRLVAAFADPGVGASGAnlafrreALEEVGGFDE 163
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 299-387 8.53e-04

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 40.24  E-value: 8.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307 299 RYDKLRALIASVRRF-YPSITIVV-----ADDSPQPERLVGPHLEHYLMPFGKGWFAGRNLAISQVATKYVLWVDDDFIF 372
Cdd:cd04186    8 SLEYLKACLDSLLAQtYPDFEVIVvdnasTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDYVLLLNPDTVV 87

                         90
                 ....*....|....*
gi 951046307 373 TPRTrLEKLVDVLEK 387
Cdd:cd04186   88 EPGA-LLELLDAAEQ 101
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 301-473 4.13e-03

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: 39.14  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307 301 DKLRALIASVRRFYPSITIVvaddsPQPERLVGphlehylmpfgkgwfAGRNLAISQVATKYVLWVDDDFIFtPRTRLEK 380
Cdd:cd02525   43 DGTREIVQEYAAKDPRIRLI-----DNPKRIQS---------------AGLNIGIRNSRGDIIIRVDAHAVY-PKDYILE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307 381 LVDVLEKTSLDLVGGaVREITGYSATYR--HKISVEPGGpegdclrvVPGWHHPIAGFPGCVVADGvinFFLA-RTDKVR 457
Cdd:cd02525  102 LVEALKRTGADNVGG-PMETIGESKFQKaiAVAQSSPLG--------SGGSAYRGGAVKIGYVDTV---HHGAyRREVFE 169

                        170
                 ....*....|....*..
gi 951046307 458 QVG-FDPRLSRVAHIEF 473
Cdd:cd02525  170 KVGgFDESLVRNEDAEL 186
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 301-398 9.06e-03

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 38.00  E-value: 9.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951046307 301 DKLRALIASVRRFYPSITIVVADDSPQPERLVGPHLEHYLMPF-------GKgwfagRN---LAISQVATKYVLWVDDDF 370
Cdd:cd06434   14 DVFRECLRSILRQKPLEIIVVTDGDDEPYLSILSQTVKYGGIFvitvphpGK-----RRalaEGIRHVTTDIVVLLDSDT 88

                         90       100
                 ....*....|....*....|....*...
gi 951046307 371 IFTPRTrLEKLVDVLEKTSLDLVGGAVR 398
Cdd:cd06434   89 VWPPNA-LPEMLKPFEDPKVGGVGTNQR 115
 
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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