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Conserved domains on  [gi|1215231134|gb|ASK72971|]
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glycosyltransferase family 2 protein [Klebsiella michiganensis]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10118607)

glycosyltransferase family 2 protein similar to Shigella flexneri dTDP rhamnosyl transferase, which adds rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
5-219 2.64e-64

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


:

Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 201.36  E-value: 2.64e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   5 VVLVTYNPNIDLVSRFVKHIDKYVDHIIVVDNSKINY-DLENLLSGKKNTIILNRSNRGIAEAQNQGIKYAIEIGMDNVF 83
Cdd:cd02526     1 AVVVTYNPDLSKLKELLAALAEQVDKVVVVDNSSGNDiELRLRLNSEKIELIHLGENLGIAKALNIGIKAALENGADYVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134  84 IFDQDTKINDAFVSKMIHAFNSMNFKERIACVGPNYEDMNNNTI-------------------DAIEKDFIIASGSLYNV 144
Cdd:cd02526    81 LFDQDSVPPPDMVEKLLAYKILSDKNSNIGAVGPRIIDRRTGENspgvrksgyklriqkegeeGLKEVDFLITSGSLISL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215231134 145 SIFDKVGYFKSEWFIDLIDVEWCHRAKKHGYKSYQIQNIKMEHNIDDNDYPTLFGKQVRIGSPVRQYYLIRNWIL 219
Cdd:cd02526   161 EALEKVGGFDEDLFIDYVDTEWCLRARSKGYKIYVVPDAVLKHELGDKRVKRLGGVSVPLHSPLRRYYLFRNAIY 235
 
Name Accession Description Interval E-value
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
5-219 2.64e-64

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 201.36  E-value: 2.64e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   5 VVLVTYNPNIDLVSRFVKHIDKYVDHIIVVDNSKINY-DLENLLSGKKNTIILNRSNRGIAEAQNQGIKYAIEIGMDNVF 83
Cdd:cd02526     1 AVVVTYNPDLSKLKELLAALAEQVDKVVVVDNSSGNDiELRLRLNSEKIELIHLGENLGIAKALNIGIKAALENGADYVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134  84 IFDQDTKINDAFVSKMIHAFNSMNFKERIACVGPNYEDMNNNTI-------------------DAIEKDFIIASGSLYNV 144
Cdd:cd02526    81 LFDQDSVPPPDMVEKLLAYKILSDKNSNIGAVGPRIIDRRTGENspgvrksgyklriqkegeeGLKEVDFLITSGSLISL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215231134 145 SIFDKVGYFKSEWFIDLIDVEWCHRAKKHGYKSYQIQNIKMEHNIDDNDYPTLFGKQVRIGSPVRQYYLIRNWIL 219
Cdd:cd02526   161 EALEKVGGFDEDLFIDYVDTEWCLRARSKGYKIYVVPDAVLKHELGDKRVKRLGGVSVPLHSPLRRYYLFRNAIY 235
rhamnosyltran TIGR01556
L-rhamnosyltransferase; This model subfamily is comprised of gamma proteobacteria whose ...
8-265 1.43e-49

L-rhamnosyltransferase; This model subfamily is comprised of gamma proteobacteria whose proteins function as L-rhamnosyltransferases in the synthesis of their respective surface polysaccharides. Rhamnolipids are glycolipids containing mono- or di- L-rhamnose molecules. Rhamnolipid synthesis occurs by sequential glycosyltransferase reactions involving two distinct rhamnosyltransferase enzymes. In P.aeruginosa, the synthesis of mono-rhamnolipids is catalyzed by rhamnosyltransferase 1, and proceeds by a glycosyltransfer reaction catalyzed by rhamnosyltransferase 2 to yield di-rhamnolipids. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130619 [Multi-domain]  Cd Length: 281  Bit Score: 164.97  E-value: 1.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   8 VTYNPNIDLVSRFVKHIDKYVDHIIVVDNSKI-NYDLENLLSGKKNTIILNRSNR-GIAEAQNQGIKYAIEIGMDNVFIF 85
Cdd:TIGR01556   1 VTFNPDLEHLGELITSLPKQVDRIIAVDNSPHsDQPLKNARLRGQKIALIHLGDNqGIAGAQNQGLDASFRRGVQGVLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134  86 DQDTKINDAFVSKMIHafNSMNFKERIACVGPNYEDMNNNT------IDAI--------------EKDFIIASGSLYNVS 145
Cdd:TIGR01556  81 DQDSRPGNAFLAAQWK--LLSAENGQACALGPRFFDRGTSRrlpaihLDGLllrqisldglttpqKTSFLISSGCLITRE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134 146 IFDKVGYFKSEWFIDLIDVEWCHRAKKHGYKSYQIQNIKMEHNIDDNDYPTLFG--KQVRIGSPVRQYYLIRNWILSLKS 223
Cdd:TIGR01556 159 VYQRLGMMDEELFIDHVDTEWSLRAQNYGIPLYIDPDIVLEHRIGDSKVRILGGlsLSIPNHSPLRRYYLFRNGILVLRR 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1215231134 224 NSFSLKFKIKTMYY-LCHKPIIFLLCSPRKTRFKYIIRGFKDG 265
Cdd:TIGR01556 239 YARSLPLKLRENLFtLIQFLAVMILEKNKLLKLRCLIKGLWDG 281
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-219 1.63e-22

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 91.98  E-value: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   1 MKVGVVLVTYNPnIDLVSRFVKHI---DKYVDHIIVVDNSKINYDLENLLSGKKN--TIILNRSNRGIAEAQNQGIKYAi 75
Cdd:COG1216     3 PKVSVVIPTYNR-PELLRRCLESLlaqTYPPFEVIVVDNGSTDGTAELLAALAFPrvRVIRNPENLGFAAARNLGLRAA- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134  76 eiGMDNVFIFDQDTKINDAFVSKMIHAFNSMnfkeriacvgpnyedmnnntidaiekdfiiasgslYNVSIFDKVGYFKS 155
Cdd:COG1216    81 --GGDYLLFLDDDTVVEPDWLERLLAAACLL-----------------------------------IRREVFEEVGGFDE 123
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215231134 156 EWFIDLIDVEWCHRAKKHGYKSYQIQNIKMEHNIDdndyptlfgkqVRIGSPVRQYYLIRNWIL 219
Cdd:COG1216   124 RFFLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGG-----------ASSGPLLRAYYLGRNRLL 176
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-103 1.82e-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: 41.23  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   5 VVLVTYN--PNIDLVSRFVKHIDKYVDHIIVVDNSKINYDLENLLS----GKKNTIILNRSNRGIAEAQNQGIKYAIEig 78
Cdd:pfam00535   2 VIIPTYNeeKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEyakkDPRVRVIRLPENRGKAGARNAGLRAATG-- 79
                          90       100
                  ....*....|....*....|....*
gi 1215231134  79 mDNVFIFDQDTKINDAFVSKMIHAF 103
Cdd:pfam00535  80 -DYIAFLDADDEVPPDWLEKLVEAL 103
 
Name Accession Description Interval E-value
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
5-219 2.64e-64

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 201.36  E-value: 2.64e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   5 VVLVTYNPNIDLVSRFVKHIDKYVDHIIVVDNSKINY-DLENLLSGKKNTIILNRSNRGIAEAQNQGIKYAIEIGMDNVF 83
Cdd:cd02526     1 AVVVTYNPDLSKLKELLAALAEQVDKVVVVDNSSGNDiELRLRLNSEKIELIHLGENLGIAKALNIGIKAALENGADYVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134  84 IFDQDTKINDAFVSKMIHAFNSMNFKERIACVGPNYEDMNNNTI-------------------DAIEKDFIIASGSLYNV 144
Cdd:cd02526    81 LFDQDSVPPPDMVEKLLAYKILSDKNSNIGAVGPRIIDRRTGENspgvrksgyklriqkegeeGLKEVDFLITSGSLISL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215231134 145 SIFDKVGYFKSEWFIDLIDVEWCHRAKKHGYKSYQIQNIKMEHNIDDNDYPTLFGKQVRIGSPVRQYYLIRNWIL 219
Cdd:cd02526   161 EALEKVGGFDEDLFIDYVDTEWCLRARSKGYKIYVVPDAVLKHELGDKRVKRLGGVSVPLHSPLRRYYLFRNAIY 235
rhamnosyltran TIGR01556
L-rhamnosyltransferase; This model subfamily is comprised of gamma proteobacteria whose ...
8-265 1.43e-49

L-rhamnosyltransferase; This model subfamily is comprised of gamma proteobacteria whose proteins function as L-rhamnosyltransferases in the synthesis of their respective surface polysaccharides. Rhamnolipids are glycolipids containing mono- or di- L-rhamnose molecules. Rhamnolipid synthesis occurs by sequential glycosyltransferase reactions involving two distinct rhamnosyltransferase enzymes. In P.aeruginosa, the synthesis of mono-rhamnolipids is catalyzed by rhamnosyltransferase 1, and proceeds by a glycosyltransfer reaction catalyzed by rhamnosyltransferase 2 to yield di-rhamnolipids. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130619 [Multi-domain]  Cd Length: 281  Bit Score: 164.97  E-value: 1.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   8 VTYNPNIDLVSRFVKHIDKYVDHIIVVDNSKI-NYDLENLLSGKKNTIILNRSNR-GIAEAQNQGIKYAIEIGMDNVFIF 85
Cdd:TIGR01556   1 VTFNPDLEHLGELITSLPKQVDRIIAVDNSPHsDQPLKNARLRGQKIALIHLGDNqGIAGAQNQGLDASFRRGVQGVLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134  86 DQDTKINDAFVSKMIHafNSMNFKERIACVGPNYEDMNNNT------IDAI--------------EKDFIIASGSLYNVS 145
Cdd:TIGR01556  81 DQDSRPGNAFLAAQWK--LLSAENGQACALGPRFFDRGTSRrlpaihLDGLllrqisldglttpqKTSFLISSGCLITRE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134 146 IFDKVGYFKSEWFIDLIDVEWCHRAKKHGYKSYQIQNIKMEHNIDDNDYPTLFG--KQVRIGSPVRQYYLIRNWILSLKS 223
Cdd:TIGR01556 159 VYQRLGMMDEELFIDHVDTEWSLRAQNYGIPLYIDPDIVLEHRIGDSKVRILGGlsLSIPNHSPLRRYYLFRNGILVLRR 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1215231134 224 NSFSLKFKIKTMYY-LCHKPIIFLLCSPRKTRFKYIIRGFKDG 265
Cdd:TIGR01556 239 YARSLPLKLRENLFtLIQFLAVMILEKNKLLKLRCLIKGLWDG 281
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-219 1.63e-22

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 91.98  E-value: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   1 MKVGVVLVTYNPnIDLVSRFVKHI---DKYVDHIIVVDNSKINYDLENLLSGKKN--TIILNRSNRGIAEAQNQGIKYAi 75
Cdd:COG1216     3 PKVSVVIPTYNR-PELLRRCLESLlaqTYPPFEVIVVDNGSTDGTAELLAALAFPrvRVIRNPENLGFAAARNLGLRAA- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134  76 eiGMDNVFIFDQDTKINDAFVSKMIHAFNSMnfkeriacvgpnyedmnnntidaiekdfiiasgslYNVSIFDKVGYFKS 155
Cdd:COG1216    81 --GGDYLLFLDDDTVVEPDWLERLLAAACLL-----------------------------------IRREVFEEVGGFDE 123
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215231134 156 EWFIDLIDVEWCHRAKKHGYKSYQIQNIKMEHNIDdndyptlfgkqVRIGSPVRQYYLIRNWIL 219
Cdd:COG1216   124 RFFLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGG-----------ASSGPLLRAYYLGRNRLL 176
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-187 1.33e-13

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 67.20  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   5 VVLVTYNpNIDLVSRFVKHI---DKYVDHIIVVDNSKINYDLENLLS-GKKNTIILNRSNRGIAEAQNQGIKYAieiGMD 80
Cdd:cd04186     1 IIIVNYN-SLEYLKACLDSLlaqTYPDFEVIVVDNASTDGSVELLRElFPEVRLIRNGENLGFGAGNNQGIREA---KGD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134  81 NVFIFDQDTKINDAFVSKMIHAfnsMNFKERIACVGPNyedmnnntidaiekdfiiASGS--LYNVSIFDKVGYFKSEWF 158
Cdd:cd04186    77 YVLLLNPDTVVEPGALLELLDA---AEQDPDVGIVGPK------------------VSGAflLVRREVFEEVGGFDEDFF 135
                         170       180
                  ....*....|....*....|....*....
gi 1215231134 159 IDLIDVEWCHRAKKHGYKSYQIQNIKMEH 187
Cdd:cd04186   136 LYYEDVDLCLRARLAGYRVLYVPQAVIYH 164
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-219 9.62e-12

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 62.65  E-value: 9.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   5 VVLVTYNpNIDLVSRFVKHIDKY---VDHIIVVDNSKINyDLENLLSGKKN----TIILNRSNRGIAEAQNQGIKYAIEI 77
Cdd:cd04185     1 AVVVTYN-RLDLLKECLDALLAQtrpPDHIIVIDNASTD-GTAEWLTSLGDldniVYLRLPENLGGAGGFYEGVRRAYEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134  78 GMDNVFIFDQDTKINDAFVSKMIHAFNSMNFkeriACVGPNYEDMNNNtidaiekdFIiasGSLYNVSIFDKVGYFKSEW 157
Cdd:cd04185    79 GYDWIWLMDDDAIPDPDALEKLLAYADKDNP----QFLAPLVLDPDGS--------FV---GVLISRRVVEKIGLPDKEF 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1215231134 158 FIDLIDVEWCHRAKKHGYKsYQIQNIKMEHnidDNDYPTLFGKQVRIGSPVRQYYLIRNWIL 219
Cdd:cd04185   144 FIWGDDTEYTLRASKAGPG-IYVPDAVVVH---KTAINKGSSAVVNIDPPWKLYYGVRNRIY 201
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-226 8.95e-10

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: 58.21  E-value: 8.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   1 MKVGVVLVTYN--PNI-DLVSRFVK-HIDKYVDHIIVV-DNSKINYD--LENLLSGKKN-TIILNRSNRGIAEAQNQGIK 72
Cdd:COG1215    29 PRVSVIIPAYNeeAVIeETLRSLLAqDYPKEKLEVIVVdDGSTDETAeiARELAAEYPRvRVIERPENGGKAAALNAGLK 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134  73 YA-IEIgmdnVFIFDQDTKINDAFVSKMIHAFNSmnfkERIACVGPNYedmnnntidaiekdfiiasgsLYNVSIFDKVG 151
Cdd:COG1215   109 AArGDI----VVFLDADTVLDPDWLRRLVAAFAD----PGVGASGANL---------------------AFRREALEEVG 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1215231134 152 YFKSEWFIDliDVEWCHRAKKHGYKSYQIQNIKMEHNIDDNdYPTLFGKQVRIGSPVRQYYLIRNWILSLKSNSF 226
Cdd:COG1215   160 GFDEDTLGE--DLDLSLRLLRAGYRIVYVPDAVVYEEAPET-LRALFRQRRRWARGGLQLLLKHRPLLRPRRLLL 231
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
5-178 1.86e-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: 44.03  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   5 VVLVTYN--PNID-LVSRFVKHIDKYVDHIIVVDNSK---INYDLENLLSGKKNTIILNRSNRGIAEAQNQGIKYAIEig 78
Cdd:cd00761     1 VIIPAYNeePYLErCLESLLAQTYPNFEVIVVDDGSTdgtLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARG-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134  79 mDNVFIFDQDTKINDAFVSKMIHAFnsmnfkeriacvgpnyedMNNNTIDAIekdfIIASGSLYNVSIFDKVGYFKSEWF 158
Cdd:cd00761    79 -EYILFLDADDLLLPDWLERLVAEL------------------LADPEADAV----GGPGNLLFRRELLEEIGGFDEALL 135
                         170       180
                  ....*....|....*....|
gi 1215231134 159 IDLIDVEWCHRAKKHGYKSY 178
Cdd:cd00761   136 SGEEDDDFLLRLLRGGKVAF 155
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
55-212 3.59e-05

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 44.14  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134  55 ILNRSNRGIAEAQNQGIKYAieiGMDNVFIFDQDTKINDAFVSKMIHAFnsmnFKERIACVG----PNYEDMNNNTIDAI 130
Cdd:cd02525    61 LIDNPKRIQSAGLNIGIRNS---RGDIIIRVDAHAVYPKDYILELVEAL----KRTGADNVGgpmeTIGESKFQKAIAVA 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134 131 EKDFIIASGSL------------------YNVSIFDKVGYFkSEWFIDLIDVEWCHRAKKHGYKSYQIQNIKMEHNIDDN 192
Cdd:cd02525   134 QSSPLGSGGSAyrggavkigyvdtvhhgaYRREVFEKVGGF-DESLVRNEDAELNYRLRKAGYKIWLSPDIRVYYYPRST 212
                         170       180
                  ....*....|....*....|
gi 1215231134 193 dYPTLFgkqvrigspvRQYY 212
Cdd:cd02525   213 -LKKLA----------RQYF 221
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-180 1.56e-04

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 42.00  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   1 MKVGVVLVTYN--PNI-DLVSRFVKHIDKYVDHIIVVDNSKinyD-----LENLLSGKKN-TIILNRSNRGIAEAQNQGI 71
Cdd:COG0463     2 PLVSVVIPTYNeeEYLeEALESLLAQTYPDFEIIVVDDGST---DgtaeiLRELAAKDPRiRVIRLERNRGKGAARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134  72 KYAieiGMDNVFIFDQDTKINDAFVSKMIHAF---------------NSMNFKERIACVGPNYEDMNNNTIDAIEKDFii 136
Cdd:COG0463    79 AAA---RGDYIAFLDADDQLDPEKLEELVAALeegpadlvygsrlirEGESDLRRLGSRLFNLVRLLTNLPDSTSGFR-- 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1215231134 137 asgsLYNVSIFDKVGYfkSEWFidLIDVEWChRAKKHGYKSYQI 180
Cdd:COG0463   154 ----LFRREVLEELGF--DEGF--LEDTELL-RALRHGFRIAEV 188
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-103 1.82e-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: 41.23  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215231134   5 VVLVTYN--PNIDLVSRFVKHIDKYVDHIIVVDNSKINYDLENLLS----GKKNTIILNRSNRGIAEAQNQGIKYAIEig 78
Cdd:pfam00535   2 VIIPTYNeeKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEyakkDPRVRVIRLPENRGKAGARNAGLRAATG-- 79
                          90       100
                  ....*....|....*....|....*
gi 1215231134  79 mDNVFIFDQDTKINDAFVSKMIHAF 103
Cdd:pfam00535  80 -DYIAFLDADDEVPPDWLEKLVEAL 103
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
28-96 6.52e-03

periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380523 [Multi-domain]  Cd Length: 302  Bit Score: 37.30  E-value: 6.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1215231134  28 VDHIIVV----DNSKINYDLENLLSGKKNTIILNRSNrgiAEAQNQGIKYAIEIGMDnVFIFDQDTKINDAFV 96
Cdd:cd06300    34 VKELIVAnsngDATEQIAQIRNLIDQGVDAIIINPSS---PTALNAVIEQAADAGIP-VVAFDGAVTSPDAYN 102
 
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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