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Conserved domains on  [gi|2003412964|emb|CAE6258945|]
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unnamed protein product, partial [Karlodinium veneficum]

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
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
229-588 3.46e-11

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.


The actual alignment was detected with superfamily member cd02537:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 240  Bit Score: 63.43  E-value: 3.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 229 EAWATTVAipsnkasveGKAWIQAVRVLHASVRRHEPSwhrRPFLVGVEAGLDATFARHLQSDGMVLKVLDPIIIPEHlA 308
Cdd:cd02537     1 EAYVTLLT---------NDDYLPGALVLGYSLRKVGSS---YDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDS-A 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 309 ECPSVQRRAEGL-RFRLFGLIEYERIIYIDADAIVVGPLAFLFETPRGvffVATVNSTRWLYprgvgeqsgwerppsidi 387
Cdd:cd02537    68 NLLKRPRFKDTYtKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLPGE---FAAAPDCGWPD------------------ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 388 trgprdsaltgvpMVNTGVMVITPWEG-FE--LAFVEplgasacsvrggwthcDQPPFEKGEnlgasqllhtgpgifaay 464
Cdd:cd02537   127 -------------LFNSGVFVLKPSEEtFNdlLDALQ----------------DTPSFDGGD------------------ 159
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 465 ctQGLIDAVFVTLS--RRLghavwtgsgefqgcqippdgsgesgirmpePWMHhctldesfnlQVTRPHLDWHfdfleqs 542
Cdd:cd02537   160 --QGLLNSYFSDRGiwKRL------------------------------PFTY----------NALKPLRYLH------- 190
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2003412964 543 rasSLANGEQPSLHVVHWPGRPKPWKLGLGQRSVW-------ERHWWQIHGEL 588
Cdd:cd02537   191 ---PEALWFGDEIKVVHFIGGDKPWSWWRDPETKEkddynelHQWWWDIYDEL 240
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
229-588 3.46e-11

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.


Pssm-ID: 133018 [Multi-domain]  Cd Length: 240  Bit Score: 63.43  E-value: 3.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 229 EAWATTVAipsnkasveGKAWIQAVRVLHASVRRHEPSwhrRPFLVGVEAGLDATFARHLQSDGMVLKVLDPIIIPEHlA 308
Cdd:cd02537     1 EAYVTLLT---------NDDYLPGALVLGYSLRKVGSS---YDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDS-A 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 309 ECPSVQRRAEGL-RFRLFGLIEYERIIYIDADAIVVGPLAFLFETPRGvffVATVNSTRWLYprgvgeqsgwerppsidi 387
Cdd:cd02537    68 NLLKRPRFKDTYtKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLPGE---FAAAPDCGWPD------------------ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 388 trgprdsaltgvpMVNTGVMVITPWEG-FE--LAFVEplgasacsvrggwthcDQPPFEKGEnlgasqllhtgpgifaay 464
Cdd:cd02537   127 -------------LFNSGVFVLKPSEEtFNdlLDALQ----------------DTPSFDGGD------------------ 159
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 465 ctQGLIDAVFVTLS--RRLghavwtgsgefqgcqippdgsgesgirmpePWMHhctldesfnlQVTRPHLDWHfdfleqs 542
Cdd:cd02537   160 --QGLLNSYFSDRGiwKRL------------------------------PFTY----------NALKPLRYLH------- 190
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2003412964 543 rasSLANGEQPSLHVVHWPGRPKPWKLGLGQRSVW-------ERHWWQIHGEL 588
Cdd:cd02537   191 ---PEALWFGDEIKVVHFIGGDKPWSWWRDPETKEkddynelHQWWWDIYDEL 240
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
320-442 1.06e-06

Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.


Pssm-ID: 279798 [Multi-domain]  Cd Length: 252  Bit Score: 50.40  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 320 LRFRLFGLI-EYERIIYIDADAIVVGPLAFLFETPRGVFFVATVNSTR-WLYPrgvgeqsgWERPPSIDITRGPRDsalt 397
Cdd:pfam01501  88 LRLYLPDLFpKLDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDNYfQRYP--------NFSEPIILENFGPPA---- 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2003412964 398 gvPMVNTGVMVI--TPW--EGFELAFVEPLGASAcsVRGGWTHCDQPPF 442
Cdd:pfam01501 156 --CYFNAGMLLFdlDAWrkENITERYIKWLNLNE--NRTLWKLGDQDPL 200
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
321-360 2.16e-04

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 43.42  E-value: 2.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2003412964 321 RFRLFGLI--EYERIIYIDADAIVVGPLAFLFETPRGVFFVA 360
Cdd:COG1442    90 RLLIPELLpdDYDKVLYLDADTLVLGDLSELWDIDLGGNLLA 131
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
229-588 3.46e-11

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.


Pssm-ID: 133018 [Multi-domain]  Cd Length: 240  Bit Score: 63.43  E-value: 3.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 229 EAWATTVAipsnkasveGKAWIQAVRVLHASVRRHEPSwhrRPFLVGVEAGLDATFARHLQSDGMVLKVLDPIIIPEHlA 308
Cdd:cd02537     1 EAYVTLLT---------NDDYLPGALVLGYSLRKVGSS---YDLVVLVTPGVSEESREALEEVGWIVREVEPIDPPDS-A 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 309 ECPSVQRRAEGL-RFRLFGLIEYERIIYIDADAIVVGPLAFLFETPRGvffVATVNSTRWLYprgvgeqsgwerppsidi 387
Cdd:cd02537    68 NLLKRPRFKDTYtKLRLWNLTEYDKVVFLDADTLVLRNIDELFDLPGE---FAAAPDCGWPD------------------ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 388 trgprdsaltgvpMVNTGVMVITPWEG-FE--LAFVEplgasacsvrggwthcDQPPFEKGEnlgasqllhtgpgifaay 464
Cdd:cd02537   127 -------------LFNSGVFVLKPSEEtFNdlLDALQ----------------DTPSFDGGD------------------ 159
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 465 ctQGLIDAVFVTLS--RRLghavwtgsgefqgcqippdgsgesgirmpePWMHhctldesfnlQVTRPHLDWHfdfleqs 542
Cdd:cd02537   160 --QGLLNSYFSDRGiwKRL------------------------------PFTY----------NALKPLRYLH------- 190
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2003412964 543 rasSLANGEQPSLHVVHWPGRPKPWKLGLGQRSVW-------ERHWWQIHGEL 588
Cdd:cd02537   191 ---PEALWFGDEIKVVHFIGGDKPWSWWRDPETKEkddynelHQWWWDIYDEL 240
GT8_GNT1 cd06914
GNT1 is a fungal enzyme that belongs to the GT 8 family; N-acetylglucosaminyltransferase is a ...
283-360 9.60e-07

GNT1 is a fungal enzyme that belongs to the GT 8 family; N-acetylglucosaminyltransferase is a fungal enzyme that catalyzes the addition of N-acetyl-D-glucosamine to mannotetraose side chains by an alpha 1-2 linkage during the synthesis of mannan. The N-acetyl-D-glucosamine moiety in mannan plays a role in the attachment of mannan to asparagine residues in proteins. The mannotetraose and its N-acetyl-D-glucosamine derivative side chains of mannan are the principle immunochemical determinants on the cell surface. N-acetylglucosaminyltransferase is a member of glycosyltransferase family 8, which are, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed, retaining glycosyltransferases.


Pssm-ID: 133064  Cd Length: 278  Bit Score: 50.89  E-value: 9.60e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2003412964 283 TFARHLQSDGMVLKVLDPIIIPEHLAECpsvqrrAEGL-RFRLFGLIEYERIIYIDADAIVVGPLAFLFETPRGVFFVA 360
Cdd:cd06914    50 RRDLLLARDKVIVKLIPVIIASGGDAYW------AKSLtKLRAFNQTEYDRIIYFDSDSIIRHPMDELFFLPNYIKFAA 122
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
320-442 1.06e-06

Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.


Pssm-ID: 279798 [Multi-domain]  Cd Length: 252  Bit Score: 50.40  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 320 LRFRLFGLI-EYERIIYIDADAIVVGPLAFLFETPRGVFFVATVNSTR-WLYPrgvgeqsgWERPPSIDITRGPRDsalt 397
Cdd:pfam01501  88 LRLYLPDLFpKLDKILYLDADIVVQGDLSPLWDIDLGGKVLAAVEDNYfQRYP--------NFSEPIILENFGPPA---- 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2003412964 398 gvPMVNTGVMVI--TPW--EGFELAFVEPLGASAcsVRGGWTHCDQPPF 442
Cdd:pfam01501 156 --CYFNAGMLLFdlDAWrkENITERYIKWLNLNE--NRTLWKLGDQDPL 200
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
322-409 1.49e-04

A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.


Pssm-ID: 133037 [Multi-domain]  Cd Length: 248  Bit Score: 43.74  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 322 FRLFG---LIEYERIIYIDADAIVVGPLAFLFETPRGVFFVAtvnstrwlyprGVGEQSGWERPPSIDITRGPRDSaltg 398
Cdd:cd04194    85 YRLLIpdlLPDYDKVLYLDADIIVLGDLSELFDIDLGDNLLA-----------AVRDPFIEQEKKRKRRLGGYDDG---- 149
                          90
                  ....*....|.
gi 2003412964 399 vPMVNTGVMVI 409
Cdd:cd04194   150 -SYFNSGVLLI 159
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
321-360 2.16e-04

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 43.42  E-value: 2.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2003412964 321 RFRLFGLI--EYERIIYIDADAIVVGPLAFLFETPRGVFFVA 360
Cdd:COG1442    90 RLLIPELLpdDYDKVLYLDADTLVLGDLSELWDIDLGGNLLA 131
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
253-411 2.67e-03

Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis; Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.


Pssm-ID: 132996 [Multi-domain]  Cd Length: 246  Bit Score: 39.73  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 253 VRVLHASVRRHEPSWHRRPFLVGVEAGLDATFARHLQSDGMVLKVLDPIIIPEHL-AECPSVQRRAEGL-RFRLFGLI-E 329
Cdd:cd00505    16 AIVLMKSVLRHRTKPLRFHVLTNPLSDTFKAALDNLRKLYNFNYELIPVDILDSVdSEHLKRPIKIVTLtKLHLPNLVpD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2003412964 330 YERIIYIDADAIVVGPLAFLFETPRGvffvatvnsTRWLyprGVGEQSGWERppsidITRGPRDSA--LTGVPMVNTGVM 407
Cdd:cd00505    96 YDKILYVDADILVLTDIDELWDTPLG---------GQEL---AAAPDPGDRR-----EGKYYRQKRshLAGPDYFNSGVF 158

                  ....
gi 2003412964 408 VITP 411
Cdd:cd00505   159 VVNL 162
 
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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