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Conserved domains on  [gi|1516000573|gb|ROS71178|]
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glycosyl transferase family 2 [Vibrio crassostreae]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11421525)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  16037492|18518825

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-225 4.80e-37

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 131.36  E-value: 4.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   1 MAKVSVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASIHDD----RIVKLST-LGVGApqARNLGI 75
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKdpriRVIRLERnRGKGA--ARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  76 EKATGEFIAFLDADDFWFPEKVERQLEFHQRYP-DLAMSFTNYEHLTEDYQVIVDCFSYWSQfqdqeelfinienpleFI 154
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEGPaDLVYGSRLIREGESDLRRLGSRLFNLVR----------------LL 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1516000573 155 IENNVIGTSTVMVRADVFSqtgSFNADIKYGEDWELWLRMSENHQIGALNsvqVGYLMRASSVTQTENLKL 225
Cdd:COG0463   143 TNLPDSTSGFRLFRREVLE---ELGFDEGFLEDTELLRALRHGFRIAEVP---VRYRAGESKLNLRDLLRL 207
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-225 4.80e-37

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 131.36  E-value: 4.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   1 MAKVSVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASIHDD----RIVKLST-LGVGApqARNLGI 75
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKdpriRVIRLERnRGKGA--ARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  76 EKATGEFIAFLDADDFWFPEKVERQLEFHQRYP-DLAMSFTNYEHLTEDYQVIVDCFSYWSQfqdqeelfinienpleFI 154
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEGPaDLVYGSRLIREGESDLRRLGSRLFNLVR----------------LL 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1516000573 155 IENNVIGTSTVMVRADVFSqtgSFNADIKYGEDWELWLRMSENHQIGALNsvqVGYLMRASSVTQTENLKL 225
Cdd:COG0463   143 TNLPDSTSGFRLFRREVLE---ELGFDEGFLEDTELLRALRHGFRIAEVP---VRYRAGESKLNLRDLLRL 207
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
5-200 8.37e-34

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 122.65  E-value: 8.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   5 SVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASiHDDRIVKLstlgVGAP-----QARNLGIEKAT 79
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKK-YEDKITYW----ISEPdkgiyDAMNKGIALAT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  80 GEFIAFLDADDFWFPEKVERQLEFHQRYPDLAMSFTNYEHLTEDYQVIVDcfsywsqfqdqeelFINIENPLEFIIENNV 159
Cdd:cd06433    76 GDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGR--------------RRPPPFLDKFLLYGMP 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1516000573 160 IGTSTVMVRADVFSQTGSFNADIKYGEDWELWLRMSENHQI 200
Cdd:cd06433   142 ICHQATFFRRSLFEKYGGFDESYRIAADYDLLLRLLLAGKI 182
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-109 6.42e-32

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: 116.73  E-value: 6.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   5 SVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASIH--DDRI-VKLSTLGVGAPQARNLGIEKATGE 81
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAkkDPRVrVIRLPENRGKAGARNAGLRAATGD 80
                          90       100
                  ....*....|....*....|....*...
gi 1516000573  82 FIAFLDADDFWFPEKVERQLEFHQRYPD 109
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGA 108
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-102 4.60e-16

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 77.39  E-value: 4.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   3 KVSVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASI--HDDRIVKLSTLGVGAPQARNLGIEKATG 80
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYaeNYPHVRLLHQANAGVSVARNTGLAVATG 86
                          90       100
                  ....*....|....*....|..
gi 1516000573  81 EFIAFLDADDFWFPEKVERQLE 102
Cdd:PRK10073   87 KYVAFPDADDVVYPTMYETLMT 108
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-225 4.80e-37

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 131.36  E-value: 4.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   1 MAKVSVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASIHDD----RIVKLST-LGVGApqARNLGI 75
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKdpriRVIRLERnRGKGA--ARNAGL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  76 EKATGEFIAFLDADDFWFPEKVERQLEFHQRYP-DLAMSFTNYEHLTEDYQVIVDCFSYWSQfqdqeelfinienpleFI 154
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEGPaDLVYGSRLIREGESDLRRLGSRLFNLVR----------------LL 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1516000573 155 IENNVIGTSTVMVRADVFSqtgSFNADIKYGEDWELWLRMSENHQIGALNsvqVGYLMRASSVTQTENLKL 225
Cdd:COG0463   143 TNLPDSTSGFRLFRREVLE---ELGFDEGFLEDTELLRALRHGFRIAEVP---VRYRAGESKLNLRDLLRL 207
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
5-200 8.37e-34

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 122.65  E-value: 8.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   5 SVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASiHDDRIVKLstlgVGAP-----QARNLGIEKAT 79
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKK-YEDKITYW----ISEPdkgiyDAMNKGIALAT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  80 GEFIAFLDADDFWFPEKVERQLEFHQRYPDLAMSFTNYEHLTEDYQVIVDcfsywsqfqdqeelFINIENPLEFIIENNV 159
Cdd:cd06433    76 GDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGR--------------RRPPPFLDKFLLYGMP 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1516000573 160 IGTSTVMVRADVFSQTGSFNADIKYGEDWELWLRMSENHQI 200
Cdd:cd06433   142 ICHQATFFRRSLFEKYGGFDESYRIAADYDLLLRLLLAGKI 182
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-109 6.42e-32

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: 116.73  E-value: 6.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   5 SVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASIH--DDRI-VKLSTLGVGAPQARNLGIEKATGE 81
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAkkDPRVrVIRLPENRGKAGARNAGLRAATGD 80
                          90       100
                  ....*....|....*....|....*...
gi 1516000573  82 FIAFLDADDFWFPEKVERQLEFHQRYPD 109
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGA 108
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-116 3.22e-31

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: 114.53  E-value: 3.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   6 VVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYL---ASIHDDRIVKLSTLGVGAPQARNLGIEKATGEF 82
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILeeyAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1516000573  83 IAFLDADDFWFPEKVERQLEFHQRYPDLAMSFTN 116
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELLADPEADAVGGP 114
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-216 5.41e-29

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 110.08  E-value: 5.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   1 MAKVSVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASIHDDRIVKLST---LGVGApqARNLGIEK 77
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRVRVIRNpenLGFAA--ARNLGLRA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  78 ATGEFIAFLDADDFWFPEKVERQLEFHqrypdlamsftnyehltedyqvivdCFsywsqfqdqeelfinienplefiien 157
Cdd:COG1216    80 AGGDYLLFLDDDTVVEPDWLERLLAAA-------------------------CL-------------------------- 108
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1516000573 158 nvigtstvMVRADVFSQTGSFNADIK-YGEDWELWLRMSEN-HQIGALNSVQVGYLMRASS 216
Cdd:COG1216   109 --------LIRREVFEEVGGFDERFFlYGEDVDLCLRLRKAgYRIVYVPDAVVYHLGGASS 161
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-192 6.69e-25

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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 99.24  E-value: 6.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   5 SVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASI--HDDRIVKL----STLGVgapqARN--LGIE 76
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYidKDPFIIILirngKNLGV----ARNfeSLLQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  77 KATGEFIAFLDADDFWFPEKVERQLEFHQRYPDLAMSFTNYEHLTEDYQVIVDcfsywSQFQDQEelfINIENPLEFIIE 156
Cdd:cd04196    77 AADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELVDENGNPIGE-----SFFEYQK---IKPGTSFNNLLF 148
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1516000573 157 NNVIGTSTVMVRADVFSQTGSFNADIKYGEDWELWL 192
Cdd:cd04196   149 QNVVTGCTMAFNRELLELALPFPDADVIMHDWWLAL 184
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
3-206 2.29e-23

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 94.96  E-value: 2.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   3 KVSVVIPTYNC-LDYLPKAIGSVLKQTHQDIELIIIDDNS-NDGTSTYLASI--HDDRI-VKLSTLGVGAPQARNLGIEK 77
Cdd:cd04184     2 LISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDAStDPEVKRVLKKYaaQDPRIkVVFREENGGISAATNSALEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  78 ATGEFIAFLDADDFWFPEKVERQLEFHQRYPDLAMSFTNYEHLTEDYQVivdcfsywsqfqdQEELFINIENPlEFIIEN 157
Cdd:cd04184    82 ATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKR-------------SEPFFKPDWSP-DLLLSQ 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1516000573 158 NVIGTSTVmVRADVFSQTGSFNADIKYGEDWELWLRMSEN-HQIGALNSV 206
Cdd:cd04184   148 NYIGHLLV-YRRSLVRQVGGFREGFEGAQDYDLVLRVSEHtDRIAHIPRV 196
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-215 5.84e-21

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: 90.57  E-value: 5.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   1 MAKVSVVIPTYNCLDYLPKAIGSVLKQT--HQDIELIIIDDNSNDGTSTYLASIHDD----RIVKLSTLGvGAPQARNLG 74
Cdd:COG1215    28 LPRVSVIIPAYNEEAVIEETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEyprvRVIERPENG-GKAAALNAG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  75 IEKATGEFIAFLDADDFWFPEKVERQLEFHQRyPDLAMSftnyehltedyqvivdcfsywsqfqdqeelfinienplefi 154
Cdd:COG1215   107 LKAARGDIVVFLDADTVLDPDWLRRLVAAFAD-PGVGAS----------------------------------------- 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1516000573 155 iennvigTSTVMVRADVFSQTGSFNADiKYGEDWELWLRMSEN-HQIGALNSVQVGYLMRAS 215
Cdd:COG1215   145 -------GANLAFRREALEEVGGFDED-TLGEDLDLSLRLLRAgYRIVYVPDAVVYEEAPET 198
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
5-216 3.01e-17

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 80.01  E-value: 3.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   5 SVVIPTYNC--LDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASI----HDDRIVKLSTLGVGAPQARNLGIEKA 78
Cdd:pfam10111   1 SVVIPVYNGekTHWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIkdhnLQVYYPNAPDTTYSLAASRNRGTSHA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  79 TGEFIAFLDADDFWFPEKVERQLEFHQRY-----PDLAMSFTNYEHLTEDYQVIVDCFSYWSQFQDQEELFINIENPLEF 153
Cdd:pfam10111  81 IGEYISFIDGDCLWSPDKFEKQLKIATSLalqenIQAAVVLPVTDLNDESSNFLRRGGDLTASGDVLRDLLVFYSPLAIF 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1516000573 154 IIENnvigTSTVMVRADVFSQTGSFNADIKY--GEDWELWLRMSENHQIGALNSVQVGYLMRASS 216
Cdd:pfam10111 161 FAPN----SSNALINRQAFIEVGGFDESFRGhgAEDFDIFLRLAARYPFVAVMPPQLLYRLSAKS 221
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
6-187 4.32e-17

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 77.27  E-value: 4.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   6 VVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASI----HDDRIVKLSTLGVGAPQARNLGIEKATGE 81
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELaalyIRRVLVVRDKENGGKAGALNAGLRHAKGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  82 FIAFLDADDFWFPEKVERQLEFHQRYPDLAMSFTNyehltedYQVIVDCFSYWSQFQDQE-ELFINIENPLEFII-ENNV 159
Cdd:cd06423    81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGR-------VRVRNGSENLLTRLQAIEyLSIFRLGRRAQSALgGVLV 153
                         170       180
                  ....*....|....*....|....*...
gi 1516000573 160 IGTSTVMVRADVFSQTGSFNADIkYGED 187
Cdd:cd06423   154 LSGAFGAFRREALREVGGWDEDT-LTED 180
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-102 4.60e-16

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 77.39  E-value: 4.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   3 KVSVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASI--HDDRIVKLSTLGVGAPQARNLGIEKATG 80
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYaeNYPHVRLLHQANAGVSVARNTGLAVATG 86
                          90       100
                  ....*....|....*....|..
gi 1516000573  81 EFIAFLDADDFWFPEKVERQLE 102
Cdd:PRK10073   87 KYVAFPDADDVVYPTMYETLMT 108
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-194 2.75e-15

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: 72.21  E-value: 2.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   6 VVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASiHDDRIVKLST---LGVGApqARNLGIEKATGEF 82
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRE-LFPEVRLIRNgenLGFGA--GNNQGIREAKGDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  83 IAFLDADDFWFPEKVERQLEFHQRYPDLAmsftnyehltedyqvivdcfsywsqfqdqeelfinienplefIIENNVIGT 162
Cdd:cd04186    78 VLLLNPDTVVEPGALLELLDAAEQDPDVG------------------------------------------IVGPKVSGA 115
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1516000573 163 StVMVRADVFSQTGSFNADIK-YGEDWELWLRM 194
Cdd:cd04186   116 F-LLVRREVFEEVGGFDEDFFlYYEDVDLCLRA 147
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
3-197 1.53e-14

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: 71.88  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   3 KVSVVIPTYNCLDYLPKAIGSVLKQT--HQDIELIIIDDNSNDGTSTYLASI--HDDRIVKLSTLGVGAPQARNLGIEKA 78
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSypKDLIEIIVVDGGSTDGTREIVQEYaaKDPRIRLIDNPKRIQSAGLNIGIRNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  79 TGEFIAFLDADDFWFPEKVERQLEFHQRyPDLAMSFTNYEHLTEDYQVIVDCFSYWSQFQDQEELFINIENPLEFiienn 158
Cdd:cd02525    81 RGDIIIRVDAHAVYPKDYILELVEALKR-TGADNVGGPMETIGESKFQKAIAVAQSSPLGSGGSAYRGGAVKIGY----- 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1516000573 159 vigTSTV---MVRADVFSQTGSFNADIKYGEDWELWLRMSEN 197
Cdd:cd02525   155 ---VDTVhhgAYRREVFEKVGGFDESLVRNEDAELNYRLRKA 193
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
6-99 4.40e-13

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 66.44  E-value: 4.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   6 VVIPTYNCLDYLPKAIGSVLKQTHQDI--ELIIIDDNSNDGTS----TYLASIHDDRIVKLST-LGVGApqARNLGIEKA 78
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGYdyEIIVVDDGSTDGTAeiarELAARVPRVRVIRLSRnFGKGA--AVRAGFKAA 78
                          90       100
                  ....*....|....*....|.
gi 1516000573  79 TGEFIAFLDADDFWFPEKVER 99
Cdd:cd04179    79 RGDIVVTMDADLQHPPEDIPK 99
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
4-207 6.71e-13

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily 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: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 66.83  E-value: 6.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   4 VSVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTyLASIHDDRIVKlstlgvgAPQAR----NLGIEKAT 79
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVA-IARSAGVVVIS-------SPKGRarqmNAGAAAAR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  80 GEFIAFLDADDfWFPEKVERQLEFHQRypdlamsftnyehlteDYQVIVDCFSYwsQFQDQE------ELFINIENPLEF 153
Cdd:cd02522    73 GDWLLFLHADT-RLPPDWDAAIIETLR----------------ADGAVAGAFRL--RFDDPGprlrllELGANLRSRLFG 133
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1516000573 154 IIennvIGTSTVMVRADVFSQTGSFNaDIKYGEDWELWLRMsenHQIGALNSVQ 207
Cdd:cd02522   134 LP----YGDQGLFIRRELFEELGGFP-ELPLMEDVELVRRL---RRRGRPALLP 179
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
6-108 1.89e-12

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 65.56  E-value: 1.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   6 VVIPTYNCLDYLPKAIGSVLKQTH-QDIELIIIDDNSNDGTSTYLAS----IHDDRIVKL-------STLGVGApqARNL 73
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFeGTLELSVFNDASTDKSAEIIEKwrkkLEDSGVIVLvgshnspSPKGVGY--AKNQ 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1516000573  74 GIEKATGEFIAFLDADDFWFPEKVERQLEFHQRYP 108
Cdd:cd06913    79 AIAQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHP 113
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
6-89 1.97e-12

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 64.42  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   6 VVIPTYNCLDYLP---KAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASIHDD----RIVKLStlgvgapqaRNLG---- 74
Cdd:cd04187     1 IVVPVYNEEENLPelyERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARdprvKVIRLS---------RNFGqqaa 71
                          90
                  ....*....|....*....
gi 1516000573  75 ----IEKATGEFIAFLDAD 89
Cdd:cd04187    72 llagLDHARGDAVITMDAD 90
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
5-194 4.97e-12

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 63.87  E-value: 4.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   5 SVVIPTYNCLD--YLPKAIGSVLKQTHQDIELIIIDD----NSNDGTSTYLASIHDDRIVKL-STLGVGApqARNLGIEK 77
Cdd:cd04195     1 SVLMSVYIKEKpeFLREALESILKQTLPPDEVVLVKDgpvtQSLNEVLEEFKRKLPLKVVPLeKNRGLGK--ALNEGLKH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  78 ATGEFIAFLDADDFWFPEKVERQLEFHQRYPDlamsftnyehltedyqviVDCFSYWSQ-FQDQEELFINIENP------ 150
Cdd:cd04195    79 CTYDWVARMDTDDISLPDRFEKQLDFIEKNPE------------------IDIVGGGVLeFDSDGNDIGKRRLPtshddi 140
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1516000573 151 LEFIIENNVIGTSTVMVRADVFSQTGSFNaDIKYGEDWELWLRM 194
Cdd:cd04195   141 LKFARRRSPFNHPTVMFRKSKVLAVGGYQ-DLPLVEDYALWARM 183
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
4-194 6.74e-12

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 64.63  E-value: 6.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   4 VSVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSN--DGTSTYLASIHDDRIVKL-STLGVGAPQARNLGIEKATG 80
Cdd:PRK10018    7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCSTswEQLQQYVTALNDPRITYIhNDINSGACAVRNQAIMLAQG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  81 EFIAFLDADDFWFPEKVERQLEFHQRYPDLAMSFTNyehlteDYQVIVDCFSYWSQFqdqeELFINIENPLEFIIENNVI 160
Cdd:PRK10018   87 EYITGIDDDDEWTPNRLSVFLAHKQQLVTHAFLYAN------DYVCQGEVYSQPASL----PLYPKSPYSRRLFYKRNII 156
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1516000573 161 GtSTVMVRADVFSQTgSFNADIKYGEDWELWLRM 194
Cdd:PRK10018  157 G-NQVFTWAWRFKEC-LFDTELKAAQDYDIFLRM 188
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
4-197 6.83e-11

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 61.23  E-value: 6.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   4 VSVVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYL---ASIHDDRIVKLST----LGV-GAPQARNLGI 75
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAeeiAARFPDVRLRVIRnarlLGPtGKSRGLNHGF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  76 EKATGEFIAFLDADDFWFPEKVERQLEFHQ-------------RYPDLAMSFTNYEHLTEDYQvivdcfsywsqfqdQEE 142
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTLKKYVQYFDspkvgavgtpvfsLNRSTMLSALGALEFALRHL--------------RMM 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1516000573 143 LFINIENPLefiiennVIGTSTVMVRADVFSQTGSFNADIKYGEDWELWLRMSEN 197
Cdd:pfam13641 150 SLRLALGVL-------PLSGAGSAIRREVLKELGLFDPFFLLGDDKSLGRRLRRH 197
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
6-106 3.29e-10

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 58.36  E-value: 3.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   6 VVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASIHDDRIVKL-----STLGVGAPQARNLGIEKATG 80
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIkhvwqEDEGFRKAKIRNKAIAAAKG 80
                          90       100
                  ....*....|....*....|....*.
gi 1516000573  81 EFIAFLDADDFWFPEKVERQLEFHQR 106
Cdd:cd06420    81 DYLIFIDGDCIPHPDFIADHIELAEP 106
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-105 2.45e-09

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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 56.53  E-value: 2.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   6 VVIPTYNCLDYLPKAIGSVLKQT--HQDIELIIIDDNSNDGTSTYLASIHDDRIVKLSTL------GVGAPQARNLGIEK 77
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDypKEKFEVILVDDHSTDGTVQILEFAAAKPNFQLKILnnsrvsISGKKNALTTAIKA 80
                          90       100
                  ....*....|....*....|....*...
gi 1516000573  78 ATGEFIAFLDADDFWFPEKVERQLEFHQ 105
Cdd:cd04192    81 AKGDWIVTTDADCVVPSNWLLTFVAFIQ 108
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-112 3.03e-09

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: 55.72  E-value: 3.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   6 VVIPTYNCLDYLPKAIGSVLKQTHQDIELIIIDDNSNDGTSTYLASIHDDRIVKLSTLGVGAPQAR--NLGIEKATGE-- 81
Cdd:cd04185     1 AVVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLDNIVYLRLPENLGGAGgfYEGVRRAYELgy 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1516000573  82 -FIAFLDADDFWFPEKVERQLEfHQRYPDLAM 112
Cdd:cd04185    81 dWIWLMDDDAIPDPDALEKLLA-YADKDNPQF 111
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
3-89 6.92e-09

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 55.37  E-value: 6.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   3 KVSVVIPTYNCLDYLPKAIGSVlkQTHQDiELIIIDDNSNDGTstylASI---HDDRIVKLSTLGVGApqARNLGIEKAT 79
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESV--KWAVD-EIIVVDSGSTDRT----VEIakeYGAKVYQRWWDGFGA--QRNFALELAT 71
                          90
                  ....*....|
gi 1516000573  80 GEFIAFLDAD 89
Cdd:cd02511    72 NDWVLSLDAD 81
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
3-99 1.90e-08

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 54.13  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   3 KVSVVIPTYNCLDYLPKAIGSVLKQT--HQDIELIIIDDNSNDGTSTYLASIHDDRIVKLSTLG-VGAPQARNLGIEKAT 79
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAKLENLLALDypRDRLEIIVVSDGSTDGTAEIAREYADKGVKLLRFPErRGKAAALNRALALAT 109
                          90       100
                  ....*....|....*....|
gi 1516000573  80 GEFIAFLDADDFWFPEKVER 99
Cdd:cd06439   110 GEIVVFTDANALLDPDALRL 129
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
6-89 5.93e-08

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 52.54  E-value: 5.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   6 VVIPTYNCLDYLPKAIGSVLKQTHQ-DIELIIIDDNSNDGTSTY---LASIHDDRIVKLST--LGVGApqARNLGIEKAT 79
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGiDYEIIVVDDNSPDGTAEIvreLAKEYPRVRLIVRPgkRGLGS--AYIEGFKAAR 78
                          90
                  ....*....|
gi 1516000573  80 GEFIAFLDAD 89
Cdd:cd06442    79 GDVIVVMDAD 88
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
6-89 9.23e-08

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 51.80  E-value: 9.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   6 VVIPTYNCLDYLPKAIGSVL----KQTHQDIELIIIDDNSNDGTSTYLASI-----HDDRIVKLS-TLGVGApqARNLGI 75
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVeyleERPSFSYEIIVVDDGSKDGTAEVARKLarknpALIRVLTLPkNRGKGG--AVRAGM 78
                          90
                  ....*....|....
gi 1516000573  76 EKATGEFIAFLDAD 89
Cdd:cd04188    79 LAARGDYILFADAD 92
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-102 9.41e-08

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 52.01  E-value: 9.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   1 MAKVSVVIPTYNCLDYLPkAIGSVLKQTHQDI---ELIIIDDNSNDGTSTY---LASIHDDRIVKLST----LGVGApqA 70
Cdd:PLN02726    8 AMKYSIIVPTYNERLNIA-LIVYLIFKALQDVkdfEIIVVDDGSPDGTQDVvkqLQKVYGEDRILLRPrpgkLGLGT--A 84
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1516000573  71 RNLGIEKATGEFIAFLDAD----DFWFPEKVERQLE 102
Cdd:PLN02726   85 YIHGLKHASGDFVVIMDADlshhPKYLPSFIKKQRE 120
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
5-88 2.43e-07

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 51.05  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   5 SVVIPTYN-CLDYLPKAIGSVLKQT--HQDIELIIIDDNSNDGTST----YLASIHDD--RIVKLSTlGVGAPQARNLGI 75
Cdd:cd02510     1 SVIIIFHNeALSTLLRTVHSVINRTppELLKEIILVDDFSDKPELKllleEYYKKYLPkvKVLRLKK-REGLIRARIAGA 79
                          90
                  ....*....|...
gi 1516000573  76 EKATGEFIAFLDA 88
Cdd:cd02510    80 RAATGDVLVFLDS 92
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
3-99 4.10e-07

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 50.50  E-value: 4.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   3 KVSVVIPTYNCLDYLPKAIG---SVLKQTHQDIELIIIDDNSNDGTSTYL---ASIHDDRIVK-LSTLGVGAPQARNLGI 75
Cdd:PRK10714    7 KVSVVIPVYNEQESLPELIRrttAACESLGKEYEILLIDDGSSDNSAEMLveaAQAPDSHIVAiLLNRNYGQHSAIMAGF 86
                          90       100
                  ....*....|....*....|....
gi 1516000573  76 EKATGEFIAFLDADDFWFPEKVER 99
Cdd:PRK10714   87 SHVTGDLIITLDADLQNPPEEIPR 110
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
4-92 1.07e-06

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 48.79  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   4 VSVVIPTYN-CLDYLPKAIGSVLKQthQDIELII-IDDNSNDGTSTYLASIHDDRIVKLSTLGVGAPQARNLGIEKATGE 81
Cdd:cd06434     2 VTVIIPVYDeDPDVFRECLRSILRQ--KPLEIIVvTDGDDEPYLSILSQTVKYGGIFVITVPHPGKRRALAEGIRHVTTD 79
                          90
                  ....*....|.
gi 1516000573  82 FIAFLDADDFW 92
Cdd:cd06434    80 IVVLLDSDTVW 90
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
5-127 8.27e-05

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 43.60  E-value: 8.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   5 SVVIPTYNCLDYLPKAIGSVLKQTHQDI--------ELIIIDDNSNDGTST--------YLASIHDDRIVKLS-TLGVGA 67
Cdd:PTZ00260   73 SIVIPAYNEEDRLPKMLKETIKYLESRSrkdpkfkyEIIIVNDGSKDKTLKvakdfwrqNINPNIDIRLLSLLrNKGKGG 152
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1516000573  68 pqARNLGIEKATGEFIAFLDAD---DFWFPEKVERQLEfHQRYPDLAMSFTNYEHLTEDYQVI 127
Cdd:PTZ00260  153 --AVRIGMLASRGKYILMVDADgatDIDDFDKLEDIML-KIEQNGLGIVFGSRNHLVDSDVVA 212
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
3-89 1.06e-03

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 40.29  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   3 KVSVVIPTYNcldyLPKAIGSVLKQTHQDI------ELIIIDDNSNDGTSTYLAS-----IHDDRIvkLSTLGVGAPQAR 71
Cdd:PRK13915   32 TVSVVLPALN----EEETVGKVVDSIRPLLmeplvdELIVIDSGSTDATAERAAAagarvVSREEI--LPELPPRPGKGE 105
                          90       100
                  ....*....|....*....|
gi 1516000573  72 NL--GIEKATGEFIAFLDAD 89
Cdd:PRK13915  106 ALwrSLAATTGDIVVFVDAD 125
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
3-194 1.48e-03

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 39.48  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   3 KVSVVIPTYN-CLDYLPKAIGSVLKQTHQDIEL--IIIDDNSNDGTSTYLASIHDDRIVKLSTLG--VGApQARNL--GI 75
Cdd:cd06421     2 TVDVFIPTYNePLEIVRKTLRAALAIDYPHDKLrvYVLDDGRRPELRALAAELGVEYGYRYLTRPdnRHA-KAGNLnnAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573  76 EKATGEFIAFLDADDFWFPEKVERQLEFHQRYPDLAM-----SFTNYEHLTEDYQVIVdcfsywsqfQDQEELFINIENP 150
Cdd:cd06421    81 AHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALvqtpqFFYNPDPFDWLADGAP---------NEQELFYGVIQPG 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1516000573 151 LEFIIENNVIGTSTVMVRADVFS----QTGSFNadikygEDWELWLRM 194
Cdd:cd06421   152 RDRWGAAFCCGSGAVVRREALDEiggfPTDSVT------EDLATSLRL 193
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
4-127 4.41e-03

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 37.68  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516000573   4 VSVVIPTYNCLDYLPKAIGSV--LKQTHQDIELIIIDDnSNDGTSTYLASIhddrIVKLSTLGV---------------G 66
Cdd:cd06437     3 VTVQLPVFNEKYVVERLIEAAcaLDYPKDRLEIQVLDD-STDETVRLAREI----VEEYAAQGVnikhvrradrtgykaG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1516000573  67 APQArnlGIEKATGEFIAFLDAdDFWFPEKVERQLEFHQRYPDLAMSFTNYEHLTEDYQVI 127
Cdd:cd06437    78 ALAE---GMKVAKGEYVAIFDA-DFVPPPDFLQKTPPYFADPKLGFVQTRWGHINANYSLL 134
 
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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