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Conserved domains on  [gi|1440915191|ref|WP_114703161|]
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glycosyltransferase [Thermosipho africanus]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

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
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 202-345 4.24e-04

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member cd03808:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 358  Bit Score: 42.20  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440915191 202 NNFSIIHAPSNKFI----------KGSKYVLKVFDKLKRKYPKIEFKLITNLKHEEAKKIYSGKGIAIDQINF------- 264
Cdd:cd03808   178 FQYSPESLPSEKVVflfvarllkdKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFlgfrsdv 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440915191 265 -----------------SIGLFSLESLYFGREVISTIHE--SE-FINGDPKLFAPIHSVyseQELEEKIEYLINNYSSTI 324
Cdd:cd03808   258 pellaesdvfvlpsyreGLPRSLLEAMAAGRPVITTDVPgcRElVIDGVNGFLVPPGDV---EALADAIEKLIEDPELRK 334

                         170       180
                  ....*....|....*....|....
gi 1440915191 325 ---NEKRKYVIENFSADKIAKLYK 345
Cdd:cd03808   335 emgEAARKRVEEKFDEEKVVNKLL 358
 
Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 202-345 4.24e-04

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 42.20  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440915191 202 NNFSIIHAPSNKFI----------KGSKYVLKVFDKLKRKYPKIEFKLITNLKHEEAKKIYSGKGIAIDQINF------- 264
Cdd:cd03808   178 FQYSPESLPSEKVVflfvarllkdKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFlgfrsdv 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440915191 265 -----------------SIGLFSLESLYFGREVISTIHE--SE-FINGDPKLFAPIHSVyseQELEEKIEYLINNYSSTI 324
Cdd:cd03808   258 pellaesdvfvlpsyreGLPRSLLEAMAAGRPVITTDVPgcRElVIDGVNGFLVPPGDV---EALADAIEKLIEDPELRK 334

                         170       180
                  ....*....|....*....|....
gi 1440915191 325 ---NEKRKYVIENFSADKIAKLYK 345
Cdd:cd03808   335 emgEAARKRVEEKFDEEKVVNKLL 358
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 271-352 4.34e-04

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 39.97  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440915191 271 LESLYFGREVISTIHE--SEFI-NGDPKLFAPIHSVyseQELEEKIEYLINNYS---STINEKRKYVIENFSADKIAKLY 344
Cdd:COG0438    38 LEAMAAGLPVIATDVGglPEVIeDGETGLLVPPGDP---EALAEAILRLLEDPElrrRLGEAARERAEERFSWEAIAERL 114


                  ....*...
gi 1440915191 345 KDLYQLLL 352
Cdd:COG0438   115 LALYEELL 122
 
Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 202-345 4.24e-04

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 42.20  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440915191 202 NNFSIIHAPSNKFI----------KGSKYVLKVFDKLKRKYPKIEFKLITNLKHEEAKKIYSGKGIAIDQINF------- 264
Cdd:cd03808   178 FQYSPESLPSEKVVflfvarllkdKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFlgfrsdv 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440915191 265 -----------------SIGLFSLESLYFGREVISTIHE--SE-FINGDPKLFAPIHSVyseQELEEKIEYLINNYSSTI 324
Cdd:cd03808   258 pellaesdvfvlpsyreGLPRSLLEAMAAGRPVITTDVPgcRElVIDGVNGFLVPPGDV---EALADAIEKLIEDPELRK 334

                         170       180
                  ....*....|....*....|....
gi 1440915191 325 ---NEKRKYVIENFSADKIAKLYK 345
Cdd:cd03808   335 emgEAARKRVEEKFDEEKVVNKLL 358
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 271-352 4.34e-04

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 39.97  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440915191 271 LESLYFGREVISTIHE--SEFI-NGDPKLFAPIHSVyseQELEEKIEYLINNYS---STINEKRKYVIENFSADKIAKLY 344
Cdd:COG0438    38 LEAMAAGLPVIATDVGglPEVIeDGETGLLVPPGDP---EALAEAILRLLEDPElrrRLGEAARERAEERFSWEAIAERL 114


                  ....*...
gi 1440915191 345 KDLYQLLL 352
Cdd:COG0438   115 LALYEELL 122
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 41-347 3.82e-03

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 39.36  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440915191  41 FKGDINLN---LDKYplperNKIVKKFFSENIDFFKKF--DIIHYHFFDTLTYGTSfggwnaypeknpyweLEYFKNLGK 115
Cdd:cd03799    37 NPGDLVKRhpdVEKY-----NVPSLNLLYAIVGLNKKGayDIIHCQFGPLGALGAL---------------LRRLKVLKG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440915191 116 KIVVSSWGSD----VRNNSKFVYYQLKFEGEKNLPYpplntyNQYFKiwefskySDAIVHG-DSEQLNHAPYGImipipf 190
Cdd:cd03799    97 KLVTSFRGYDismyVILEGNKVYPQLFAQGDLFLPN------CELFK-------HRLIALGcDEKKIIVHRSGI------ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440915191 191 DPESYqiteynnNFSIIHAPSNKFI-----------KGSKYVLKVFDKLKRKYPKIEF-------------KLITNL--- 243
Cdd:cd03799   158 DCNKF-------RFKPRYLPLDGKIriltvgrltekKGLEYAIEAVAKLAQKYPNIEYqiigdgdlkeqlqQLIQELnig 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440915191 244 ---------KHEEAKKIYSGKGIAI---------DQINFSIGLfsLESLYFGREVISTIHesefiNGDPKL--------F 297
Cdd:cd03799   231 dcvkllgwkPQEEIIEILDEADIFIapsvtaadgDQDGPPNTL--KEAMAMGLPVISTEH-----GGIPELvedgvsgfL 303

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1440915191 298 APIHSVyseQELEEKIEYLINN---YSSTINEKRKYVIENFSadkIAKLYKDL 347
Cdd:cd03799   304 VPERDA---EAIAEKLTYLIEHpaiWPEMGKAGRARVEEEYD---INKLNDEL 350
 
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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