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Conserved domains on  [gi|545746399|ref|NP_001271163|]
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tRNA-queuosine alpha-mannosyltransferase isoform d [Homo sapiens]

Protein Classification

glycosyltransferase( domain architecture ID 10108132)

glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 158-270 2.66e-11

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.


:

Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 62.42  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399 158 VWPHRWEHDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHWGYLPSKDDYFQVLCMADVVIS 237
Cdd:cd01635  114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVL 193

                         90       100       110
                 ....*....|....*....|....*....|...
gi 545746399 238 TAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIF 270
Cdd:cd01635  194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
DUF3524 super family cl12034
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 1-35 6.72e-09

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


The actual alignment was detected with superfamily member pfam12038:

Pssm-ID: 432280  Cd Length: 165  Bit Score: 54.10  E-value: 6.72e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 545746399    1 MESFLTSMGKFMKLIPDHRPKDLESIIRPKCQVIY 35
Cdd:pfam12038 131 RDSFLEAIPALLKKMPDARPKGLVEKIRAKSRVLY 165
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 229-321 8.15e-04

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


:

Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 38.82  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399 229 LCMADVVISTAKHEFFGVAMLEAVYCGCYPLC-----PKDLVYPE----IFPAEylysTPEQLSKRLQNFCKRPDIIRKH 299
Cdd:COG0438   18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIAtdvggLPEVIEDGetglLVPPG----DPEALAEAILRLLEDPELRRRL 93

                         90       100
                 ....*....|....*....|....*
gi 545746399 300 LYKG-EIA--PFSWAALHGKFRSLL 321
Cdd:COG0438   94 GEAArERAeeRFSWEAIAERLLALY 118
 
Name Accession Description Interval E-value
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 158-270 2.66e-11

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.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 62.42  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399 158 VWPHRWEHDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHWGYLPSKDDYFQVLCMADVVIS 237
Cdd:cd01635  114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVL 193

                         90       100       110
                 ....*....|....*....|....*....|...
gi 545746399 238 TAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIF 270
Cdd:cd01635  194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 1-35 6.72e-09

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


Pssm-ID: 432280  Cd Length: 165  Bit Score: 54.10  E-value: 6.72e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 545746399    1 MESFLTSMGKFMKLIPDHRPKDLESIIRPKCQVIY 35
Cdd:pfam12038 131 RDSFLEAIPALLKKMPDARPKGLVEKIRAKSRVLY 165
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 157-329 1.63e-04

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 41.49  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399  157 IVWPHRWEHDKDPESFFKVLMHLKDLGLNFHVSVLGETfTDVPDIFSEAKKALGSSVLHW-GYLPSKD--DYFQvlcMAD 233
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDG-EEEKRLKKLAEKLGLGDNVIFlGFVSDEDlpELLK---IAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399  234 VVISTAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIFpaeylystpeqlskrlqnfckrpdiirKHLYKGE-IAPFSWAA 312
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV---------------------------KDGETGFlVKPNNAEA 133

                         170
                  ....*....|....*...
gi 545746399  313 LHGKFRSLLT-TEPREDL 329
Cdd:pfam00534 134 LAEAIDKLLEdEELRERL 151
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 229-321 8.15e-04

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 38.82  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399 229 LCMADVVISTAKHEFFGVAMLEAVYCGCYPLC-----PKDLVYPE----IFPAEylysTPEQLSKRLQNFCKRPDIIRKH 299
Cdd:COG0438   18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIAtdvggLPEVIEDGetglLVPPG----DPEALAEAILRLLEDPELRRRL 93

                         90       100
                 ....*....|....*....|....*
gi 545746399 300 LYKG-EIA--PFSWAALHGKFRSLL 321
Cdd:COG0438   94 GEAArERAeeRFSWEAIAERLLALY 118
 
Name Accession Description Interval E-value
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 158-270 2.66e-11

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.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 62.42  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399 158 VWPHRWEHDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHWGYLPSKDDYFQVLCMADVVIS 237
Cdd:cd01635  114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVL 193

                         90       100       110
                 ....*....|....*....|....*....|...
gi 545746399 238 TAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIF 270
Cdd:cd01635  194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 1-35 6.72e-09

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


Pssm-ID: 432280  Cd Length: 165  Bit Score: 54.10  E-value: 6.72e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 545746399    1 MESFLTSMGKFMKLIPDHRPKDLESIIRPKCQVIY 35
Cdd:pfam12038 131 RDSFLEAIPALLKKMPDARPKGLVEKIRAKSRVLY 165
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 159-312 7.23e-06

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 46.97  E-value: 7.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399 159 WPHrwehdKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHW-GYLPsKDDYFQVLCMADVVIS 237
Cdd:cd03809  202 EPR-----KNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEELLDLVKKLGLGGRVRFlGYVS-DEDLPALYRGARAFVF 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399 238 TAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIFPAEYLY---STPEQLSKRLQNFCKRPDIIRKHLYKG--EIAPFSWAA 312
Cdd:cd03809  276 PSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDAALYfdpLDPESIADAILRLLEDPSLREELIRKGleRAKKFSWEK 355
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 165-256 1.06e-05

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: 46.43  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399 165 HDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHWGYlpsKDDYFQVLCMADVVISTAKHEFF 244
Cdd:cd03808  200 KDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGF---RSDVPELLAESDVFVLPSYREGL 276

                         90
                 ....*....|..
gi 545746399 245 GVAMLEAVYCGC 256
Cdd:cd03808  277 PRSLLEAMAAGR 288
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 157-321 2.49e-05

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). 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. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the 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 members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 45.61  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399 157 IVWPHRWEHDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIfSEAKKALGSSVLHWGYLPsKDDYFQVLCMADVVI 236
Cdd:cd03801  195 LLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLRAEL-EELELGLGDRVRFLGFVP-DEELPALYAAADVFV 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399 237 STAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIFPAEYLY-----STPEQLSKRLQNFCKRPDI---IRKHLYKGEIAPF 308
Cdd:cd03801  273 LPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGlvvppDDVEALADALLRLLADPELrarLGRAARERVAERF 352

                        170
                 ....*....|...
gi 545746399 309 SWAALHGKFRSLL 321
Cdd:cd03801  353 SWERVAERLLDLY 365
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 157-329 1.63e-04

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 41.49  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399  157 IVWPHRWEHDKDPESFFKVLMHLKDLGLNFHVSVLGETfTDVPDIFSEAKKALGSSVLHW-GYLPSKD--DYFQvlcMAD 233
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDG-EEEKRLKKLAEKLGLGDNVIFlGFVSDEDlpELLK---IAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399  234 VVISTAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIFpaeylystpeqlskrlqnfckrpdiirKHLYKGE-IAPFSWAA 312
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV---------------------------KDGETGFlVKPNNAEA 133

                         170
                  ....*....|....*...
gi 545746399  313 LHGKFRSLLT-TEPREDL 329
Cdd:pfam00534 134 LAEAIDKLLEdEELRERL 151
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 229-321 8.15e-04

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 38.82  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545746399 229 LCMADVVISTAKHEFFGVAMLEAVYCGCYPLC-----PKDLVYPE----IFPAEylysTPEQLSKRLQNFCKRPDIIRKH 299
Cdd:COG0438   18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIAtdvggLPEVIEDGetglLVPPG----DPEALAEAILRLLEDPELRRRL 93

                         90       100
                 ....*....|....*....|....*
gi 545746399 300 LYKG-EIA--PFSWAALHGKFRSLL 321
Cdd:COG0438   94 GEAArERAeeRFSWEAIAERLLALY 118
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 218-255 9.80e-03

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. 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. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the 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 members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 37.33  E-value: 9.80e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 545746399 218 YLPSKDDYFQVLCMADVVISTAKHEFFGVAMLEAVYCG 255
Cdd:cd04962  256 FLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACG 293
 
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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