NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|71996090|ref|NP_001022949|]
View 

Putative polypeptide N-acetylgalactosaminyltransferase 11 [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
SCOP:  3000077

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
162-431 1.91e-144

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: 413.52  E-value: 1.91e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 162 SIVVCYFNESPSVLIRMVNSIFDRTKPEHLHEILLVDDSSEWSNATDEAIkyrEKHIIQWEKVKFLKTDKNEGLIRAKIF 241
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLE---EYYKKYLPKVKVLRLKKREGLIRARIA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 242 GARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVCPIIDIIDAITMKYVESPV-CTGGVNWAMTFKWDYPHRSYF 320
Cdd:cd02510  78 GARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGdARGGFDWSLHFKWLPLPEEER 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 321 eDPMNYVNPLKSPTMAGGLFAIDKEYFFEIGSYDEGMDVWGAENVEISVRIWTCGGELLIMPCSRVGHIFRRQR-PYGIK 399
Cdd:cd02510 158 -RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKRkPYTFP 236
                       250       260       270
                ....*....|....*....|....*....|....
gi 71996090 400 TDS--MGKNSVRLARVWLDEYLENFFEARPNYRT 431
Cdd:cd02510 237 GGSgtVLRNYKRVAEVWMDEYKEYFYKARPELRN 270
 
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 ...
162-431 1.91e-144

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: 413.52  E-value: 1.91e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 162 SIVVCYFNESPSVLIRMVNSIFDRTKPEHLHEILLVDDSSEWSNATDEAIkyrEKHIIQWEKVKFLKTDKNEGLIRAKIF 241
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLE---EYYKKYLPKVKVLRLKKREGLIRARIA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 242 GARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVCPIIDIIDAITMKYVESPV-CTGGVNWAMTFKWDYPHRSYF 320
Cdd:cd02510  78 GARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGdARGGFDWSLHFKWLPLPEEER 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 321 eDPMNYVNPLKSPTMAGGLFAIDKEYFFEIGSYDEGMDVWGAENVEISVRIWTCGGELLIMPCSRVGHIFRRQR-PYGIK 399
Cdd:cd02510 158 -RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKRkPYTFP 236
                       250       260       270
                ....*....|....*....|....*....|....
gi 71996090 400 TDS--MGKNSVRLARVWLDEYLENFFEARPNYRT 431
Cdd:cd02510 237 GGSgtVLRNYKRVAEVWMDEYKEYFYKARPELRN 270
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
162-345 1.84e-27

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: 107.10  E-value: 1.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090   162 SIVVCYFNEsPSVLIRMVNSIFDRTKPEHlhEILLVDDSSewsnaTDEAIKYREKHIIQWEKVKFLKTDKNEGLIRAKIF 241
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-----TDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090   242 GARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVCPIIDIIDaitmkyvespVCTGGVNWAMTFKWDYPHRSYFE 321
Cdd:pfam00535  73 GLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIF----------GETGEYRRASRITLSRLPFFLGL 142
                         170       180
                  ....*....|....*....|....
gi 71996090   322 DPMNYVNPLKSPTMAGGLFAIDKE 345
Cdd:pfam00535 143 RLLGLNLPFLIGGFALYRREALEE 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
155-394 2.64e-18

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: 85.18  E-value: 2.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 155 SDSLPAASIVVCYFNEsPSVLIRMVNSIFDRTKPEHLHEILLVDDSSewsnaTDEAIKYREKHIIQWEKVKFLKTDKNEG 234
Cdd:COG1215  25 PADLPRVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLEVIVVDDGS-----TDETAEIARELAAEYPRVRVIERPENGG 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 235 LIRAKIFGARRANGEVLVFLDSHCEVNEEWLpplldqikqnrRRVVcpiidiidaitmkyvespvctggvnwamtfkwdy 314
Cdd:COG1215  99 KAAALNAGLKAARGDIVVFLDADTVLDPDWL-----------RRLV---------------------------------- 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 315 phrSYFEDPmNYVnplksptMAGGLFAIDKEYFFEIGSYDEGMdvwGAENVEISVRIWTCGGELLIMPCSRVGHI----- 389
Cdd:COG1215 134 ---AAFADP-GVG-------ASGANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYEEapetl 199

                ....*..
gi 71996090 390 --FRRQR 394
Cdd:COG1215 200 raLFRQR 206
 
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 ...
162-431 1.91e-144

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: 413.52  E-value: 1.91e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 162 SIVVCYFNESPSVLIRMVNSIFDRTKPEHLHEILLVDDSSEWSNATDEAIkyrEKHIIQWEKVKFLKTDKNEGLIRAKIF 241
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLE---EYYKKYLPKVKVLRLKKREGLIRARIA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 242 GARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVCPIIDIIDAITMKYVESPV-CTGGVNWAMTFKWDYPHRSYF 320
Cdd:cd02510  78 GARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGdARGGFDWSLHFKWLPLPEEER 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 321 eDPMNYVNPLKSPTMAGGLFAIDKEYFFEIGSYDEGMDVWGAENVEISVRIWTCGGELLIMPCSRVGHIFRRQR-PYGIK 399
Cdd:cd02510 158 -RRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKRkPYTFP 236
                       250       260       270
                ....*....|....*....|....*....|....
gi 71996090 400 TDS--MGKNSVRLARVWLDEYLENFFEARPNYRT 431
Cdd:cd02510 237 GGSgtVLRNYKRVAEVWMDEYKEYFYKARPELRN 270
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
162-345 1.84e-27

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: 107.10  E-value: 1.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090   162 SIVVCYFNEsPSVLIRMVNSIFDRTKPEHlhEILLVDDSSewsnaTDEAIKYREKHIIQWEKVKFLKTDKNEGLIRAKIF 241
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-----TDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090   242 GARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVCPIIDIIDaitmkyvespVCTGGVNWAMTFKWDYPHRSYFE 321
Cdd:pfam00535  73 GLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIF----------GETGEYRRASRITLSRLPFFLGL 142
                         170       180
                  ....*....|....*....|....
gi 71996090   322 DPMNYVNPLKSPTMAGGLFAIDKE 345
Cdd:pfam00535 143 RLLGLNLPFLIGGFALYRREALEE 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
155-394 2.64e-18

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: 85.18  E-value: 2.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 155 SDSLPAASIVVCYFNEsPSVLIRMVNSIFDRTKPEHLHEILLVDDSSewsnaTDEAIKYREKHIIQWEKVKFLKTDKNEG 234
Cdd:COG1215  25 PADLPRVSVIIPAYNE-EAVIEETLRSLLAQDYPKEKLEVIVVDDGS-----TDETAEIARELAAEYPRVRVIERPENGG 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 235 LIRAKIFGARRANGEVLVFLDSHCEVNEEWLpplldqikqnrRRVVcpiidiidaitmkyvespvctggvnwamtfkwdy 314
Cdd:COG1215  99 KAAALNAGLKAARGDIVVFLDADTVLDPDWL-----------RRLV---------------------------------- 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 315 phrSYFEDPmNYVnplksptMAGGLFAIDKEYFFEIGSYDEGMdvwGAENVEISVRIWTCGGELLIMPCSRVGHI----- 389
Cdd:COG1215 134 ---AAFADP-GVG-------ASGANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYEEapetl 199

                ....*..
gi 71996090 390 --FRRQR 394
Cdd:COG1215 200 raLFRQR 206
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
159-416 6.87e-17

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 78.88  E-value: 6.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 159 PAASIVVCYFNeSPSVLIRMVNSIFDRTKPEHlhEILLVDDSSewsnaTDEAIKYREKHiiQWEKVKFLKTDKNEGLIRA 238
Cdd:COG1216   3 PKVSVVIPTYN-RPELLRRCLESLLAQTYPPF--EVIVVDNGS-----TDGTAELLAAL--AFPRVRVIRNPENLGFAAA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 239 KIFGARRANGEVLVFLDSHCEVNEEWLPPLLDqikqnrrrvvcpiidiidaitmkyvespvctggvnwamtfkwdyphrs 318
Cdd:COG1216  73 RNLGLRAAGGDYLLFLDDDTVVEPDWLERLLA------------------------------------------------ 104
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 319 yfedpmnyvnplksptmAGGLFaIDKEYFFEIGSYDEGMDVWGAEnVEISVRIWTCGGELLIMPCSRVGHIFRRQRPYGI 398
Cdd:COG1216 105 -----------------AACLL-IRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLL 165
                       250
                ....*....|....*...
gi 71996090 399 KTDSMGKNSVRLARVWLD 416
Cdd:COG1216 166 RAYYLGRNRLLFLRKHGP 183
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
162-357 8.81e-14

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 70.12  E-value: 8.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 162 SIVVCYFNEsPSVLIRMVNSIFDRTKPEHlhEILLVDDSSewsnaTDEAIKYREKHIIQWEKVKFLKTDKNEGLIRAKIF 241
Cdd:COG0463   5 SVVIPTYNE-EEYLEEALESLLAQTYPDF--EIIVVDDGS-----TDGTAEILRELAAKDPRIRVIRLERNRGKGAARNA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 242 GARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVCpiidiidaitmkyvespvctGGVNWAMTFKWDYPHRSYFE 321
Cdd:COG0463  77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY--------------------GSRLIREGESDLRRLGSRLF 136
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 71996090 322 DPMNYVNPLksPTMAGGLFAIDKEYFFEIGsYDEGM 357
Cdd:COG0463 137 NLVRLLTNL--PDSTSGFRLFRREVLEELG-FDEGF 169
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
163-281 1.12e-12

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: 65.61  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 163 IVVCYFNESPsVLIRMVNSIFDRTKPEHlhEILLVDDSSewsnaTDEAIKYREKHIIQWEKVKFLKTDKNEGLIRAKIFG 242
Cdd:cd00761   1 VIIPAYNEEP-YLERCLESLLAQTYPNF--EVIVVDDGS-----TDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAG 72
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 71996090 243 ARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVC 281
Cdd:cd00761  73 LKAARGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
163-388 5.61e-11

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: 60.65  E-value: 5.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 163 IVVCYFNeSPSVLIRMVNSIFDRTKPehLHEILLVDDSSewsnaTDEAIKYREKHiiqWEKVKFLKTDKNEGLIRAKIFG 242
Cdd:cd04186   1 IIIVNYN-SLEYLKACLDSLLAQTYP--DFEVIVVDNAS-----TDGSVELLREL---FPEVRLIRNGENLGFGAGNNQG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 243 ARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRrvvcpiidiidaitmkyvespvcTGGVnwamtfkwdyphrsyfed 322
Cdd:cd04186  70 IREAKGDYVLLLNPDTVVEPGALLELLDAAEQDPD-----------------------VGIV------------------ 108
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71996090 323 pmnyvnplkSPTMAGGLFAIDKEYFFEIGSYDEGMDVWGaENVEISVRIWTCGGELLIMPCSRVGH 388
Cdd:cd04186 109 ---------GPKVSGAFLLVRREVFEEVGGFDEDFFLYY-EDVDLCLRARLAGYRVLYVPQAVIYH 164
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
162-393 7.47e-08

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: 53.00  E-value: 7.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 162 SIVVCYFNESPSV--LIRmvnSIFDRTKPEHLHEILLVDDSSewSNATDEAIK-YREKHIiqweKVKFLKtdkNEGLIRA 238
Cdd:cd02525   3 SIIIPVRNEEKYIeeLLE---SLLNQSYPKDLIEIIVVDGGS--TDGTREIVQeYAAKDP----RIRLID---NPKRIQS 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 239 KIF--GARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVCPIIDIID------AITMKYvESPVCTGGVnwamtf 310
Cdd:cd02525  71 AGLniGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGeskfqkAIAVAQ-SSPLGSGGS------ 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 311 kwdyPHRSyfedpmNYVNPLKSPTMAGGLFaiDKEYFFEIGSYDEGMDVwgAENVEISVRIWTCGGELLIMPCSRVGHiF 390
Cdd:cd02525 144 ----AYRG------GAVKIGYVDTVHHGAY--RREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYY-Y 208

                ...
gi 71996090 391 RRQ 393
Cdd:cd02525 209 PRS 211
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
163-281 3.00e-07

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: 50.26  E-value: 3.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 163 IVVCYfNESPSvLIRMVNSIFDRTKPEHLHEILLVDDSSewSNATDEAIKyreKHIIQWEKVKFLKTDKNEGLIRAKIFG 242
Cdd:cd04179   2 VIPAY-NEEEN-IPELVERLLAVLEEGYDYEIIVVDDGS--TDGTAEIAR---ELAARVPRVRVIRLSRNFGKGAAVRAG 74
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 71996090 243 ARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVC 281
Cdd:cd04179  75 FKAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVI 113
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
316-390 1.17e-05

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: 43.37  E-value: 1.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71996090   316 HRSYFEDPMNYvnPLKSPTMAGGLFAIDKEYFFEIGSYDEGMDVWGAENVEISVRIWTCGGELLImPCSRVGHIF 390
Cdd:pfam02709   2 HLSVALDKFGY--KLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIER-PPGDIGRYY 73
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
159-256 2.16e-05

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: 45.27  E-value: 2.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 159 PAASIVVCYFNESPSVLIRMVNSIFDRTKPEHlhEILLVDDSSEWsnatDEAIKYREKHIIQWEKVKFLKTDKNEGLIRA 238
Cdd:cd04184   1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTD----PEVKRVLKKYAAQDPRIKVVFREENGGISAA 74
                        90
                ....*....|....*...
gi 71996090 239 KIFGARRANGEVLVFLDS 256
Cdd:cd04184  75 TNSALELATGEFVALLDH 92
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
163-281 3.74e-05

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: 44.48  E-value: 3.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 163 IVVCYFNESpSVLIRMVNSIFD--RTKPEHLHEILLVDDSSewSNATDE-AIKYREKHIiqwEKVKFLKTDKNEGLIRAK 239
Cdd:cd04188   1 VVIPAYNEE-KRLPPTLEEAVEylEERPSFSYEIIVVDDGS--KDGTAEvARKLARKNP---ALIRVLTLPKNRGKGGAV 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 71996090 240 IFGARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRRVVC 281
Cdd:cd04188  75 RAGMLAARGDYILFADADLATPFEELEKLEEALKTSGYDIAI 116
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
162-371 9.96e-05

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: 43.80  E-value: 9.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090   162 SIVVCYFN--ESPSVLIRMVNSifdRTKPEHLHEILLVDDSSewSNATDEAIKyrekHIIQWEKVKFLK--TDKNEGLIR 237
Cdd:pfam10111   1 SVVIPVYNgeKTHWIQERILNQ---TFQYDPEFELIIINDGS--TDKTLEEVS----SIKDHNLQVYYPnaPDTTYSLAA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090   238 AKIFGARRANGEVLVFLDSHCEVNEEWLPPLLDQIKQNRRR------VVCPIIDIIDAIT--MKYVESPVCTGGVnwamt 309
Cdd:pfam10111  72 SRNRGTSHAIGEYISFIDGDCLWSPDKFEKQLKIATSLALQeniqaaVVLPVTDLNDESSnfLRRGGDLTASGDV----- 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71996090   310 fkwdyphrsyFEDPMNYVNPL-KSPTMAGGLFAIDKEYFFEIGSYDEGMDVWGAENVEISVRI 371
Cdd:pfam10111 147 ----------LRDLLVFYSPLaIFFAPNSSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRL 199
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
163-265 1.39e-04

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: 43.05  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 163 IVVCYFNESPSVLiRMVNSIFDRTKPEHLHEILLVDDSSEwsNATDEAIKYREKH------IIQwEKVKFLKTDKNegli 236
Cdd:cd04192   1 VVIAARNEAENLP-RLLQSLSALDYPKEKFEVILVDDHST--DGTVQILEFAAAKpnfqlkILN-NSRVSISGKKN---- 72
                        90       100
                ....*....|....*....|....*....
gi 71996090 237 rAKIFGARRANGEVLVFLDSHCEVNEEWL 265
Cdd:cd04192  73 -ALTTAIKAAKGDWIVTTDADCVVPSNWL 100
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
156-255 7.17e-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: 41.03  E-value: 7.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 156 DSLPAASIVVCYFNESPsVLIRMVNSIFDRTKPEHLHEILLVDDSSewSNATDEAI-KYREKhiiqweKVKFLKTDKNEG 234
Cdd:cd06439  26 AYLPTVTIIIPAYNEEA-VIEAKLENLLALDYPRDRLEIIVVSDGS--TDGTAEIArEYADK------GVKLLRFPERRG 96
                        90       100
                ....*....|....*....|.
gi 71996090 235 LIRAKIFGARRANGEVLVFLD 255
Cdd:cd06439  97 KAAALNRALALATGEIVVFTD 117
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
163-274 8.29e-04

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: 40.59  E-value: 8.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71996090 163 IVVCYFNESPSvLIRMVNSIFDRTKPEHLhEILLVDDSSewsnaTDEAIKYREKHIIQWEKVKFLKTDKNEGLIRAKIFG 242
Cdd:cd06442   1 IIIPTYNEREN-IPELIERLDAALKGIDY-EIIVVDDNS-----PDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEG 73
                        90       100       110
                ....*....|....*....|....*....|....*
gi 71996090 243 ARRANGEVLVFLD---SHcevNEEWLPPLLDQIKQ 274
Cdd:cd06442  74 FKAARGDVIVVMDadlSH---PPEYIPELLEAQLE 105
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH