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Conserved domains on  [gi|1360981667|ref|WP_106191306|]
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glycosyltransferase family 32 protein [Alkalibacterium olivapovliticus]

Protein Classification

glycosyltransferase family 32 protein( domain architecture ID 11467330)

glycosyltransferase family 32 protein similar to initiation-specific alpha-1,6-mannosyltransferase that is involved in outer chain elongation of asparagine-linked oligosaccharides of the type Man(9)GlcNAc(2)

CAZY:  GT32
EC:  2.4.-.-
PubMed:  11231017

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OCH1 COG3774
Mannosyltransferase OCH1 or related enzyme [Cell wall/membrane/envelope biogenesis];
1-129 2.03e-50

Mannosyltransferase OCH1 or related enzyme [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442988 [Multi-domain]  Cd Length: 136  Bit Score: 159.67  E-value: 2.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360981667   1 MIPKIIHYAWFGGNPLGPLEEKCLASWKRYCPDWEIKRWDETNFNP--EDHG-EYTKQAYEREEWAFVSDVARLHALKEY 77
Cdd:COG3774     2 MIPKIIHQTWFGDKELPELVQRCIASWKKLNPDWEYRLWDDENFDDfiKEHGpEYLEAYYKLKKGAARADLFRLLLLYKY 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1360981667  78 GGVYCDTDMELIKPIDKFRKFPAFFS---FEIETEISTGIIGAEAHHPFIEELYK 129
Cdd:COG3774    82 GGIYLDIDVECLKPLDPLLDGDDLFLgyeDPPPGIISNGFIAAEPGHPFLKKALE 136
 
Name Accession Description Interval E-value
OCH1 COG3774
Mannosyltransferase OCH1 or related enzyme [Cell wall/membrane/envelope biogenesis];
1-129 2.03e-50

Mannosyltransferase OCH1 or related enzyme [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442988 [Multi-domain]  Cd Length: 136  Bit Score: 159.67  E-value: 2.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360981667   1 MIPKIIHYAWFGGNPLGPLEEKCLASWKRYCPDWEIKRWDETNFNP--EDHG-EYTKQAYEREEWAFVSDVARLHALKEY 77
Cdd:COG3774     2 MIPKIIHQTWFGDKELPELVQRCIASWKKLNPDWEYRLWDDENFDDfiKEHGpEYLEAYYKLKKGAARADLFRLLLLYKY 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1360981667  78 GGVYCDTDMELIKPIDKFRKFPAFFS---FEIETEISTGIIGAEAHHPFIEELYK 129
Cdd:COG3774    82 GGIYLDIDVECLKPLDPLLDGDDLFLgyeDPPPGIISNGFIAAEPGHPFLKKALE 136
Gly_transf_sug pfam04488
Glycosyltransferase sugar-binding region containing DXD motif; The DXD motif is a short ...
 17-102 3.83e-13

Glycosyltransferase sugar-binding region containing DXD motif; The DXD motif is a short conserved motif found in many families of glycosyltransferases, which add a range of different sugars to other sugars, phosphates and proteins. DXD-containing glycosyltransferases all use nucleoside diphosphate sugars as donors and require divalent cations, usually manganese. The DXD motif is expected to play a carbohydrate binding role in sugar-nucleoside diphosphate and manganese dependent glycosyltransferases.


Pssm-ID: 398274 [Multi-domain]  Cd Length: 93  Bit Score: 62.74  E-value: 3.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360981667  17 GPLEEKCLASWKRYCPDWEIKRWDETNFNPEDHGEYTK------QAYEREeWAFV--SDVARLHALKEYGGVYCDTDMEL 88
Cdd:pfam04488   1 PERVMKAIESLIKLHPDYCYVVLSDDLDFALDINFLKSdtpwflEAYSLL-PLFIakSDLLRYAILYKYGGIYLDTDVIP 79

                          90
                  ....*....|....
gi 1360981667  89 IKPIDKFRKFPAFF 102
Cdd:pfam04488  80 LKSLNSIGAQERFL 93
 
Name Accession Description Interval E-value
OCH1 COG3774
Mannosyltransferase OCH1 or related enzyme [Cell wall/membrane/envelope biogenesis];
1-129 2.03e-50

Mannosyltransferase OCH1 or related enzyme [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442988 [Multi-domain]  Cd Length: 136  Bit Score: 159.67  E-value: 2.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360981667   1 MIPKIIHYAWFGGNPLGPLEEKCLASWKRYCPDWEIKRWDETNFNP--EDHG-EYTKQAYEREEWAFVSDVARLHALKEY 77
Cdd:COG3774     2 MIPKIIHQTWFGDKELPELVQRCIASWKKLNPDWEYRLWDDENFDDfiKEHGpEYLEAYYKLKKGAARADLFRLLLLYKY 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1360981667  78 GGVYCDTDMELIKPIDKFRKFPAFFS---FEIETEISTGIIGAEAHHPFIEELYK 129
Cdd:COG3774    82 GGIYLDIDVECLKPLDPLLDGDDLFLgyeDPPPGIISNGFIAAEPGHPFLKKALE 136
Gly_transf_sug pfam04488
Glycosyltransferase sugar-binding region containing DXD motif; The DXD motif is a short ...
 17-102 3.83e-13

Glycosyltransferase sugar-binding region containing DXD motif; The DXD motif is a short conserved motif found in many families of glycosyltransferases, which add a range of different sugars to other sugars, phosphates and proteins. DXD-containing glycosyltransferases all use nucleoside diphosphate sugars as donors and require divalent cations, usually manganese. The DXD motif is expected to play a carbohydrate binding role in sugar-nucleoside diphosphate and manganese dependent glycosyltransferases.


Pssm-ID: 398274 [Multi-domain]  Cd Length: 93  Bit Score: 62.74  E-value: 3.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360981667  17 GPLEEKCLASWKRYCPDWEIKRWDETNFNPEDHGEYTK------QAYEREeWAFV--SDVARLHALKEYGGVYCDTDMEL 88
Cdd:pfam04488   1 PERVMKAIESLIKLHPDYCYVVLSDDLDFALDINFLKSdtpwflEAYSLL-PLFIakSDLLRYAILYKYGGIYLDTDVIP 79

                          90
                  ....*....|....
gi 1360981667  89 IKPIDKFRKFPAFF 102
Cdd:pfam04488  80 LKSLNSIGAQERFL 93
Caps_synth pfam05704
Capsular polysaccharide synthesis protein; This family consists of several capsular ...
 1-140 6.62e-07

Capsular polysaccharide synthesis protein; This family consists of several capsular polysaccharide proteins. Capsular polysaccharide (CPS) is a major virulence factor in Streptococcus pneumoniae.


Pssm-ID: 368570  Cd Length: 278  Bit Score: 48.43  E-value: 6.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1360981667   1 MIPKIIHYAWFGG-NPLGPLEEKCLASWKRYCPDWEIKRWDETNFnpEDHGEYTKQAYEREE-----WAFVSDVARLHAL 74
Cdd:pfam05704  45 QNNKIIWICWFQGiDNAPEIVKKCIDSVKKNAPDYEVVLLTKDNI--SEYVDIPDFIIEKFEkgkisRAHFSDILRLNLL 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1360981667  75 KEYGGVYCDTDMELIKPIDKFRKFPAFFSF------EIETEIS---TGIIGAEAHHPFI---EELYKDYDGREFILPD 140
Cdd:pfam05704 123 AKYGGVWIDATIYCTGDLPNELLDSDFFTFssseldSNKISISrwtGFFLAAKKNNPLLstlRDLLLEYWKKYNSLID 200
TcdA_TcdB pfam12919
TcdA/TcdB catalytic glycosyltransferase domain; This domain represents the N-terminal ...
 52-86 2.38e-05

TcdA/TcdB catalytic glycosyltransferase domain; This domain represents the N-terminal glycosyltransferase from a set of toxins found in some bacteria. This domain in TcdB glycosylates the host RhoA protein.


Pssm-ID: 372382 [Multi-domain]  Cd Length: 382  Bit Score: 44.06  E-value: 2.38e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1360981667  52 YTKQAYEREEWAFVSDVARLHALKEYGGVYCDTDM 86
Cdd:pfam12919 160 YEQELFLRGNLAAASDIVRLLALKELGGLYTDVDM 194
 
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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