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Conserved domains on  [gi|392923087|ref|NP_001256888|]
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polypeptide N-acetylgalactosaminyltransferase [Caenorhabditis elegans]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase family protein( domain architecture ID 10118411)

polypeptide N-acetylgalactosaminyltransferase family protein may catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor

CAZY:  GT2
Gene Ontology:  GO:0046872
PubMed:  10521532|12691742|9445404
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 154-449 0e+00

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: 513.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 154 TVIITYHNEARSSLLRTVFSVFNQSPEELLLEIVLVDDNSQDVEIGKEL-----AQIQRITVLRNNQREGLIRSRVKGAQ 228
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 229 VARAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVAPIIDVINVDNFNYVGASADLRGGFDWTLVFRWEFMNEQLRkeR 308
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER--R 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 309 HAHPTAPIRSPTMAGGLFAISKEWFNELGTYDLDMEVWGGENLEMSFRVWQCGGSLEIMPCSRVGHVFR-KKHPYTFPGG 387
Cdd:cd02510  159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392923087 388 SGNVfQKNTRRAAEVWMDEYKAIYLKNVPSARFVNFGDITDRLAIRDRLQCKSFKWYLENVY 449
Cdd:cd02510  239 SGTV-LRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 154-449 0e+00

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: 513.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 154 TVIITYHNEARSSLLRTVFSVFNQSPEELLLEIVLVDDNSQDVEIGKEL-----AQIQRITVLRNNQREGLIRSRVKGAQ 228
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 229 VARAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVAPIIDVINVDNFNYVGASADLRGGFDWTLVFRWEFMNEQLRkeR 308
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER--R 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 309 HAHPTAPIRSPTMAGGLFAISKEWFNELGTYDLDMEVWGGENLEMSFRVWQCGGSLEIMPCSRVGHVFR-KKHPYTFPGG 387
Cdd:cd02510  159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392923087 388 SGNVfQKNTRRAAEVWMDEYKAIYLKNVPSARFVNFGDITDRLAIRDRLQCKSFKWYLENVY 449
Cdd:cd02510  239 SGTV-LRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 154-331 2.39e-33

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: 123.66  E-value: 2.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087  154 TVIITYHNEArSSLLRTVFSVFNQSPEELllEIVLVDDNSQD--VEIGKELAQI-QRITVLRNNQREGLIRSRVKGAQVA 230
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGSTDgtVEIAEEYAKKdPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087  231 RAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVAPIIDVINVDNFNYVGASADLRGGFDWTLVFRWEFmneqlrkerha 310
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLG----------- 146

                         170       180
                  ....*....|....*....|.
gi 392923087  311 hPTAPIRSPTMAGGLFAISKE 331
Cdd:pfam00535 147 -LNLPFLIGGFALYRREALEE 166
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 154-337 5.17e-16

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 76.66  E-value: 5.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 154 TVIITYHNEARSsLLRTVFSVFNQSPEELllEIVLVDDNSQD--VEIGKELAQIQ-RITVLRNNQREGLIRSRVKGAQVA 230
Cdd:COG0463    5 SVVIPTYNEEEY-LEEALESLLAQTYPDF--EIIVVDDGSTDgtAEILRELAAKDpRIRVIRLERNRGKGAARNAGLAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 231 RAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVapiidvinvdnfnyVGASADLRGGFDWTLVFRWEFMNEQLRkerha 310
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLV--------------YGSRLIREGESDLRRLGSRLFNLVRLL----- 142

                        170       180
                 ....*....|....*....|....*..
gi 392923087 311 hptapIRSPTMAGGLFAISKEWFNELG 337
Cdd:COG0463  143 -----TNLPDSTSGFRLFRREVLEELG 164
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 154-449 0e+00

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: 513.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 154 TVIITYHNEARSSLLRTVFSVFNQSPEELLLEIVLVDDNSQDVEIGKEL-----AQIQRITVLRNNQREGLIRSRVKGAQ 228
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLeeyykKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 229 VARAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVAPIIDVINVDNFNYVGASADLRGGFDWTLVFRWEFMNEQLRkeR 308
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEER--R 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 309 HAHPTAPIRSPTMAGGLFAISKEWFNELGTYDLDMEVWGGENLEMSFRVWQCGGSLEIMPCSRVGHVFR-KKHPYTFPGG 387
Cdd:cd02510  159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392923087 388 SGNVfQKNTRRAAEVWMDEYKAIYLKNVPSARFVNFGDITDRLAIRDRLQCKSFKWYLENVY 449
Cdd:cd02510  239 SGTV-LRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 154-331 2.39e-33

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: 123.66  E-value: 2.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087  154 TVIITYHNEArSSLLRTVFSVFNQSPEELllEIVLVDDNSQD--VEIGKELAQI-QRITVLRNNQREGLIRSRVKGAQVA 230
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGSTDgtVEIAEEYAKKdPRVRVIRLPENRGKAGARNAGLRAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087  231 RAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVAPIIDVINVDNFNYVGASADLRGGFDWTLVFRWEFmneqlrkerha 310
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLG----------- 146

                         170       180
                  ....*....|....*....|.
gi 392923087  311 hPTAPIRSPTMAGGLFAISKE 331
Cdd:pfam00535 147 -LNLPFLIGGFALYRREALEE 166
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 154-337 5.17e-16

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 76.66  E-value: 5.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 154 TVIITYHNEARSsLLRTVFSVFNQSPEELllEIVLVDDNSQD--VEIGKELAQIQ-RITVLRNNQREGLIRSRVKGAQVA 230
Cdd:COG0463    5 SVVIPTYNEEEY-LEEALESLLAQTYPDF--EIIVVDDGSTDgtAEILRELAAKDpRIRVIRLERNRGKGAARNAGLAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 231 RAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVapiidvinvdnfnyVGASADLRGGFDWTLVFRWEFMNEQLRkerha 310
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADLV--------------YGSRLIREGESDLRRLGSRLFNLVRLL----- 142

                        170       180
                 ....*....|....*....|....*..
gi 392923087 311 hptapIRSPTMAGGLFAISKEWFNELG 337
Cdd:COG0463  143 -----TNLPDSTSGFRLFRREVLEELG 164
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 155-301 1.55e-14

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: 71.00  E-value: 1.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 155 VIITYHNEARSsLLRTVFSVFNQSPEELllEIVLVDDNSQD--VEIGKELAQIQ-RITVLRNNQREGLIRSRVKGAQVAR 231
Cdd:cd00761    1 VIIPAYNEEPY-LERCLESLLAQTYPNF--EVIVVDDGSTDgtLEILEEYAKKDpRVIRVINEENQGLAAARNAGLKAAR 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392923087 232 APVLTFLDSHIECNQKWLEPLLARIAENPK--AVVAPIIDVINVDNFNYVGASADLRGGFDWTLVFRWEFMN 301
Cdd:cd00761   78 GEYILFLDADDLLLPDWLERLVAELLADPEadAVGGPGNLLFRRELLEEIGGFDEALLSGEEDDDFLLRLLR 149
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 154-265 3.94e-13

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: 69.77  E-value: 3.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 154 TVIITYHNEARSsLLRTVFSVFNQSPEELLLEIVLVDDNSQD--VEIGKELA-QIQRITVLRNNQREGLIRSRVKGAQVA 230
Cdd:COG1215   32 SVIIPAYNEEAV-IEETLRSLLAQDYPKEKLEVIVVDDGSTDetAEIARELAaEYPRVRVIERPENGGKAAALNAGLKAA 110

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 392923087 231 RAPVLTFLDSHIECNQKWLEPLLARIaENPKAVVA 265
Cdd:COG1215  111 RGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGAS 144
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
150-378 6.45e-12

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 64.63  E-value: 6.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 150 MQPTT--VIITYHNEARssLLRTVFSVFNQSPEELllEIVLVDDNSQDvEIGKELAQIQ--RITVLRNNQREGLIRSRVK 225
Cdd:COG1216    1 MRPKVsvVIPTYNRPEL--LRRCLESLLAQTYPPF--EVIVVDNGSTD-GTAELLAALAfpRVRVIRNPENLGFAAARNL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 226 GAQVARAPVLTFLDSHIECNQKWLEPLLAriaenpkavvapiidvinvdnfnyvgasadlrggfdwtlvfrwefmneqlr 305
Cdd:COG1216   76 GLRAAGGDYLLFLDDDTVVEPDWLERLLA--------------------------------------------------- 104

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392923087 306 kerhahptapirsptmAGGLFaISKEWFNELGTYDLDMEVWGGEnLEMSFRVWQCGGSLEIMPCSRVGHVFRK 378
Cdd:COG1216  105 ----------------AACLL-IRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGA 159
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 155-374 7.74e-10

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: 57.57  E-value: 7.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 155 VIITYHNEARSsLLRTVFSVFNQSPEelLLEIVLVDDNSQDVEIGKELAQIQRITVLRNNQREGLIRSRVKGAQVARAPV 234
Cdd:cd04186    1 IIIVNYNSLEY-LKACLDSLLAQTYP--DFEVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 235 LTFLDSHIECNQKWLEPLLARIAENPKAVVApiidvinvdnfnyvgasadlrggfdwtlvfrwefmneqlrkerhahpta 314
Cdd:cd04186   78 VLLLNPDTVVEPGALLELLDAAEQDPDVGIV------------------------------------------------- 108

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 315 pirSPTMAGGLFAISKEWFNELGTYDLDMEVWgGENLEMSFRVWQCGGSLEIMPCSRVGH 374
Cdd:cd04186  109 ---GPKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYH 164
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 155-264 5.98e-08

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: 52.58  E-value: 5.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 155 VIITYHNEARS--SLLRTVFSVFNQSPEellLEIVLVDDNSQD--VEIGKELAQI-QRITVLRNNQREGLIRSRVKGAQV 229
Cdd:cd04179    1 VVIPAYNEEENipELVERLLAVLEEGYD---YEIIVVDDGSTDgtAEIARELAARvPRVRVIRLSRNFGKGAAVRAGFKA 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 392923087 230 ARAPVLTFLDS----HIECnqkwLEPLLARIAENPKAVV 264
Cdd:cd04179   78 ARGDIVVTMDAdlqhPPED----IPKLLEKLLEGGADVV 112
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 155-343 7.94e-08

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: 52.23  E-value: 7.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 155 VIITYHNEARSsLLRTVFSVFNQSPEELllEIVLVDDNSQD--VEIGKELA--QIQRITVLRNNQREGlirsrvK----- 225
Cdd:cd06423    1 IIVPAYNEEAV-IERTIESLLALDYPKL--EVIVVDDGSTDdtLEILEELAalYIRRVLVVRDKENGG------Kagaln 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 226 -GAQVARAPVLTFLD--SHIEcnQKWLEPLLARIAENPKAV-VAPIIDVINvDNFNYVGASADLRggfdWTLVFRWEFMN 301
Cdd:cd06423   72 aGLRHAKGDIVVVLDadTILE--PDALKRLVVPFFADPKVGaVQGRVRVRN-GSENLLTRLQAIE----YLSIFRLGRRA 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 392923087 302 EQLRKerhahptapiRSPTMAGGLFAISKEWFNELGTYDLDM 343
Cdd:cd06423  145 QSALG----------GVLVLSGAFGAFRREALREVGGWDEDT 176
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 153-379 3.92e-07

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: 50.83  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087  153 TTVIITYHNEArSSLLRTVFSVFNQspEELLLEIVLVDDNSQD--VEIGKELAQI---QRITVLRNNQREGL---IRSRV 224
Cdd:pfam13641   4 VSVVVPAFNED-SVLGRVLEAILAQ--PYPPVEVVVVVNPSDAetLDVAEEIAARfpdVRLRVIRNARLLGPtgkSRGLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087  225 KGAQVARAPVLTFLDShiEC-NQKWLEPLLARIAENPKavVAPIIDVINVDNFNYVgasadlrggfdWTLVFRWEFMNEQ 303
Cdd:pfam13641  81 HGFRAVKSDLVVLHDD--DSvLHPGTLKKYVQYFDSPK--VGAVGTPVFSLNRSTM-----------LSALGALEFALRH 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392923087  304 LRKERHAHPtapIRSPTMAGGLFAISKEWFNELGTYDLdmevWG--GENLEMSFRVWQCGGSLEIMPCSRVGHVFRKK 379
Cdd:pfam13641 146 LRMMSLRLA---LGVLPLSGAGSAIRREVLKELGLFDP----FFllGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTY 216
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 155-349 4.47e-07

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: 50.75  E-value: 4.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 155 VIITYHNEARSsLLRTVFSVFNQSPEELLLEIVLVDDNSQD--VEIGKELAQIQ--RITVLRNNQREGlirSRVK----- 225
Cdd:cd04192    1 VVIAARNEAEN-LPRLLQSLSALDYPKEKFEVILVDDHSTDgtVQILEFAAAKPnfQLKILNNSRVSI---SGKKnaltt 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 226 GAQVARAPVLTFLDSHIECNQKWLEPLLARIA-ENPKAVVAPII---------DVINVDNFNYVGASAdlrGGFDWTLvf 295
Cdd:cd04192   77 AIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQkEQIGLVAGPVIyfkgksllaKFQRLDWLSLLGLIA---GSFGLGK-- 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 392923087 296 rwefmneqlrkerhahptapirsPTMAGGL-FAISKEWFNELGTYDLDMEVWGGE 349
Cdd:cd04192  152 -----------------------PFMCNGAnMAYRKEAFFEVGGFEGNDHIASGD 183
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 155-241 6.90e-07

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: 50.22  E-value: 6.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 155 VII-TYhNEAR--SSLLRTVFSVFnqspEELLLEIVLVDDNSQD--VEIGKELAQIQ-RITVLRNNQREGLIRSRVKGAQ 228
Cdd:cd06442    1 IIIpTY-NEREniPELIERLDAAL----KGIDYEIIVVDDNSPDgtAEIVRELAKEYpRVRLIVRPGKRGLGSAYIEGFK 75

                         90
                 ....*....|....*.
gi 392923087 229 VARAPVLTFLD---SH 241
Cdd:cd06442   76 AARGDVIVVMDadlSH 91
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 315-381 7.83e-07

N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 46.84  E-value: 7.83e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392923087  315 PIRSPTMAGGLFAISKEWFNELGTYDLDMEVWGGENLEMSFRVWQCGGSLEImPCSRVGHVFRKKHP 381
Cdd:pfam02709  13 KLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIER-PPGDIGRYYMLYHK 78
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 154-364 8.02e-07

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: 50.31  E-value: 8.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 154 TVIITYHNEARSsLLRTVFSVFNQSPEELLLEIVLVDDNSQD--VEIGKELAQIQ-RITVLRNNQReglIRS--RVKGAQ 228
Cdd:cd02525    3 SIIIPVRNEEKY-IEELLESLLNQSYPKDLIEIIVVDGGSTDgtREIVQEYAAKDpRIRLIDNPKR---IQSagLNIGIR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 229 VARAPVLTFLDSHIECNQKWLEPLLARIAENPKAVVAPIIDVINVDNFN----YVGASADLRGGfdwtLVFRwefmneQL 304
Cdd:cd02525   79 NSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQkaiaVAQSSPLGSGG----SAYR------GG 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 305 RKERHAHPTAPirsptmaGGLFaiSKEWFNELGTYDLDMEVwgGENLEMSFRVWQCGGSL 364
Cdd:cd02525  149 AVKIGYVDTVH-------HGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKI 197
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 151-261 2.70e-04

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: 42.57  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 151 QPT-TVIITYHNEARSsLLRTVFSVFNQSPEELLLEIVLVDDNSQD--VEIGKELAQiQRITVLRNNQREGLIRSRVKGA 227
Cdd:cd06439   28 LPTvTIIIPAYNEEAV-IEAKLENLLALDYPRDRLEIIVVSDGSTDgtAEIAREYAD-KGVKLLRFPERRGKAAALNRAL 105

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 392923087 228 QVARAPVLTFLDShiecNQKWlEP----LLARIAENPK 261
Cdd:cd06439  106 ALATGEIVVFTDA----NALL-DPdalrLLVRHFADPS 138
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 155-265 3.82e-04

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: 41.78  E-value: 3.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392923087 155 VIITYHNEARSsLLRTVFSVFNQSPEELLL--EIVLVDDNSQD--VEIGKELA--QIQRITVLRNNQREGlirsrvKGAQ 228
Cdd:cd04188    1 VVIPAYNEEKR-LPPTLEEAVEYLEERPSFsyEIIVVDDGSKDgtAEVARKLArkNPALIRVLTLPKNRG------KGGA 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 392923087 229 V------ARAPVLTFLD----SHIECnqkwLEPLL-ARIAENPKAVVA 265
Cdd:cd04188   74 VragmlaARGDYILFADadlaTPFEE----LEKLEeALKTSGYDIAIG 117
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 155-214 4.06e-04

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: 41.31  E-value: 4.06e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392923087 155 VIITYHNEARS--SLLRTVFSVFNQSPEELllEIVLVDDNSQD--VEIGKELA-QIQRITVLRNN 214
Cdd:cd04187    1 IVVPVYNEEENlpELYERLKAVLESLGYDY--EIIFVDDGSTDrtLEILRELAaRDPRVKVIRLS 63
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 173-239 5.53e-03

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: 38.38  E-value: 5.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392923087 173 SVFNQSpeELLLEIVLVDDNSQD--VEIGKELAQI--QRITVLRNNQREGLIRSRVKGAQVARAPVLTFLD 239
Cdd:cd04196   19 SILAQT--YKNDELIISDDGSTDgtVEIIKEYIDKdpFIIILIRNGKNLGVARNFESLLQAADGDYVFFCD 87
 
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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