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Conserved domains on  [gi|1539298849|emb|VDZ62064|]
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Glycosyl transferase family 2 [Citrobacter freundii]

Protein Classification

glycosyltransferase family A protein( domain architecture ID 10091567)

Glycosyltransferase family A (GT-A) protein is part of a diverse family of glycosyl transferases with a common GT-A type structural fold

EC:  2.4.-.-
PubMed:  34850161|12691742

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-110 2.13e-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: 43.65  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539298849   6 LVVIYNKKLEVNVAVNSVKESqrTFENFDVIVWDNSDDEKILEQ-NQSYATNNNITYRTEKKNCPLSYVYNKIINENKLD 84
Cdd:cd00761     2 IIPAYNEEPYLERCLESLLAQ--TYPNFEVIVVDDGSTDGTLEIlEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGE 79

                          90       100
                  ....*....|....*....|....*.
gi 1539298849  85 FIIISDDDTVYNRVYFAELEQELQRD 110
Cdd:cd00761    80 YILFLDADDLLLPDWLERLVAELLAD 105
 
Name Accession Description Interval E-value
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-110 2.13e-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: 43.65  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539298849   6 LVVIYNKKLEVNVAVNSVKESqrTFENFDVIVWDNSDDEKILEQ-NQSYATNNNITYRTEKKNCPLSYVYNKIINENKLD 84
Cdd:cd00761     2 IIPAYNEEPYLERCLESLLAQ--TYPNFEVIVVDDGSTDGTLEIlEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGE 79

                          90       100
                  ....*....|....*....|....*.
gi 1539298849  85 FIIISDDDTVYNRVYFAELEQELQRD 110
Cdd:cd00761    80 YILFLDADDLLLPDWLERLVAELLAD 105
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-110 2.81e-04

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: 40.46  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539298849   5 LLVVIYNKKLEVNVAVNSVKEsqRTFENFDVIVWDNSDDEKILEQNQSYATNN-NITYRTEKKNCPLSYVYNKIINENKL 83
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLN--QTYPNFEIIVVDDGSTDGTVEIAEEYAKKDpRVRVIRLPENRGKAGARNAGLRAATG 79

                          90       100
                  ....*....|....*....|....*..
gi 1539298849  84 DFIIISDDDTVYNRVYFAELEQELQRD 110
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEED 106
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
4-194 4.91e-04

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 39.98  E-value: 4.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539298849   4 KLLVVI--YNKKLEVNVAVNSVKESqrTFENFDVIVWDNSDDEKILEQNQSYAtNNNITYRTEKKNCPLSYVYNKIINEN 81
Cdd:COG1216     4 KVSVVIptYNRPELLRRCLESLLAQ--TYPPFEVIVVDNGSTDGTAELLAALA-FPRVRVIRNPENLGFAAARNLGLRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539298849  82 KLDFIIISDDDTVynrvyfaeleqeLQRDYLvhipqiyvngalksparmgivvgkhlnsinpglhPKLLAiTSGMVINRk 161
Cdd:COG1216    81 GGDYLLFLDDDTV------------VEPDWL----------------------------------ERLLA-AACLLIRR- 112

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1539298849 162 lcDIFS--PLFDESLNLYGIDTDFFINLSKLNIPV 194
Cdd:COG1216   113 --EVFEevGGFDERFFLYGEDVDLCLRLRKAGYRI 145
 
Name Accession Description Interval E-value
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-110 2.13e-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: 43.65  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539298849   6 LVVIYNKKLEVNVAVNSVKESqrTFENFDVIVWDNSDDEKILEQ-NQSYATNNNITYRTEKKNCPLSYVYNKIINENKLD 84
Cdd:cd00761     2 IIPAYNEEPYLERCLESLLAQ--TYPNFEVIVVDDGSTDGTLEIlEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGE 79

                          90       100
                  ....*....|....*....|....*.
gi 1539298849  85 FIIISDDDTVYNRVYFAELEQELQRD 110
Cdd:cd00761    80 YILFLDADDLLLPDWLERLVAELLAD 105
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-110 2.81e-04

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: 40.46  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539298849   5 LLVVIYNKKLEVNVAVNSVKEsqRTFENFDVIVWDNSDDEKILEQNQSYATNN-NITYRTEKKNCPLSYVYNKIINENKL 83
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLN--QTYPNFEIIVVDDGSTDGTVEIAEEYAKKDpRVRVIRLPENRGKAGARNAGLRAATG 79

                          90       100
                  ....*....|....*....|....*..
gi 1539298849  84 DFIIISDDDTVYNRVYFAELEQELQRD 110
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEED 106
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
4-194 4.91e-04

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 39.98  E-value: 4.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539298849   4 KLLVVI--YNKKLEVNVAVNSVKESqrTFENFDVIVWDNSDDEKILEQNQSYAtNNNITYRTEKKNCPLSYVYNKIINEN 81
Cdd:COG1216     4 KVSVVIptYNRPELLRRCLESLLAQ--TYPPFEVIVVDNGSTDGTAELLAALA-FPRVRVIRNPENLGFAAARNLGLRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539298849  82 KLDFIIISDDDTVynrvyfaeleqeLQRDYLvhipqiyvngalksparmgivvgkhlnsinpglhPKLLAiTSGMVINRk 161
Cdd:COG1216    81 GGDYLLFLDDDTV------------VEPDWL----------------------------------ERLLA-AACLLIRR- 112

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1539298849 162 lcDIFS--PLFDESLNLYGIDTDFFINLSKLNIPV 194
Cdd:COG1216   113 --EVFEevGGFDERFFLYGEDVDLCLRLRKAGYRI 145
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 7-110 2.51e-03

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: 38.57  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1539298849   7 VVI--YNKKLEVNVAVNSVKESQRTFENFDVIV-WDNSDDE--KILEQNQsyATNNNITYRTEKKNCPLSYVYNKIINEN 81
Cdd:COG1215    33 VIIpaYNEEAVIEETLRSLLAQDYPKEKLEVIVvDDGSTDEtaEIARELA--AEYPRVRVIERPENGGKAAALNAGLKAA 110

                          90       100
                  ....*....|....*....|....*....
gi 1539298849  82 KLDFIIISDDDTVYNRVYFAELEQELQRD 110
Cdd:COG1215   111 RGDIVVFLDADTVLDPDWLRRLVAAFADP 139
 
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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