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Conserved domains on  [gi|281485547|ref|NP_660335|]
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inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5 [Homo sapiens]

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 ...
 137-433 1.65e-154

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: 439.33  E-value: 1.65e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 137 SIVICFYNEECNALFQTMSSVTNLTPHYFLEEIILVDDMSKVDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLIGAS 216
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 217 HASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCPLIDVIDDRTLEYKPSP-LVRGTFDWNLQFKWDNVFSYEMDgP 295
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEERR-R 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 296 EGSTKPIRSPAMSGGIFAIRRHYFNEIGQYDKDMDFWGRENLELSLRIWMCGGQLFIIPCSRVGHISKKQtGKPSTI--- 372
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRK-RKPYTFpgg 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281485547 373 ISAMTHNYLRLVHVWLDEYKEQFFLRKPGLKYVTYGNIRERVELRKRLGCKSFQWYLDNVF 433
Cdd:cd02510  239 SGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 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 ...
 137-433 1.65e-154

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: 439.33  E-value: 1.65e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 137 SIVICFYNEECNALFQTMSSVTNLTPHYFLEEIILVDDMSKVDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLIGAS 216
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 217 HASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCPLIDVIDDRTLEYKPSP-LVRGTFDWNLQFKWDNVFSYEMDgP 295
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEERR-R 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 296 EGSTKPIRSPAMSGGIFAIRRHYFNEIGQYDKDMDFWGRENLELSLRIWMCGGQLFIIPCSRVGHISKKQtGKPSTI--- 372
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRK-RKPYTFpgg 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281485547 373 ISAMTHNYLRLVHVWLDEYKEQFFLRKPGLKYVTYGNIRERVELRKRLGCKSFQWYLDNVF 433
Cdd:cd02510  239 SGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 137-321 2.04e-30

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: 115.18  E-value: 2.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547  137 SIVICFYNEEcNALFQTMSSVTNLTphYFLEEIILVDDMSKvDDLKEKLDYHLETFrGKVKIIRNKKREGLIRARLIGAS 216
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGST-DGTVEIAEEYAKKD-PRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547  217 HASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCPLIDVIDDRTLEYKpsplvrgtfdWNLQFKWDNVFSYEMDGPE 296
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR----------RASRITLSRLPFFLGLRLL 145

                         170       180
                  ....*....|....*....|....*
gi 281485547  297 GSTKPIRspamSGGIFAIRRHYFNE 321
Cdd:pfam00535 146 GLNLPFL----IGGFALYRREALEE 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 123-360 1.02e-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: 86.33  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 123 MCLQKHYPARLPTASIVICFYNEECNaLFQTMSSVTNLTPHYFLEEIILVDDMSKvDDLKEKLDyHLETFRGKVKIIRNK 202
Cdd:COG1215   18 LARRRRAPADLPRVSVIIPAYNEEAV-IEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIAR-ELAAEYPRVRVIERP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 203 KREGLIRARLIGASHASGDVLVFLDSHCEVNRVWLEPLLHAIAkDPKMvvcplidviddrtleykpsplvrgtfdwnlqf 282
Cdd:COG1215   95 ENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGV-------------------------------- 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281485547 283 kwdnvfsyemdgpegstkpirspAMSGGIFAIRRHYFNEIGQYDKDMdfWGrENLELSLRIWMCGGQLFIIPCSRVGH 360
Cdd:COG1215  142 -----------------------GASGANLAFRREALEEVGGFDEDT--LG-EDLDLSLRLLRAGYRIVYVPDAVVYE 193
 
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 ...
 137-433 1.65e-154

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: 439.33  E-value: 1.65e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 137 SIVICFYNEECNALFQTMSSVTNLTPHYFLEEIILVDDMSKVDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLIGAS 216
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 217 HASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCPLIDVIDDRTLEYKPSP-LVRGTFDWNLQFKWDNVFSYEMDgP 295
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEERR-R 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 296 EGSTKPIRSPAMSGGIFAIRRHYFNEIGQYDKDMDFWGRENLELSLRIWMCGGQLFIIPCSRVGHISKKQtGKPSTI--- 372
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRK-RKPYTFpgg 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281485547 373 ISAMTHNYLRLVHVWLDEYKEQFFLRKPGLKYVTYGNIRERVELRKRLGCKSFQWYLDNVF 433
Cdd:cd02510  239 SGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 137-321 2.04e-30

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: 115.18  E-value: 2.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547  137 SIVICFYNEEcNALFQTMSSVTNLTphYFLEEIILVDDMSKvDDLKEKLDYHLETFrGKVKIIRNKKREGLIRARLIGAS 216
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGST-DGTVEIAEEYAKKD-PRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547  217 HASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCPLIDVIDDRTLEYKpsplvrgtfdWNLQFKWDNVFSYEMDGPE 296
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR----------RASRITLSRLPFFLGLRLL 145

                         170       180
                  ....*....|....*....|....*
gi 281485547  297 GSTKPIRspamSGGIFAIRRHYFNE 321
Cdd:pfam00535 146 GLNLPFL----IGGFALYRREALEE 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 123-360 1.02e-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: 86.33  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 123 MCLQKHYPARLPTASIVICFYNEECNaLFQTMSSVTNLTPHYFLEEIILVDDMSKvDDLKEKLDyHLETFRGKVKIIRNK 202
Cdd:COG1215   18 LARRRRAPADLPRVSVIIPAYNEEAV-IEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIAR-ELAAEYPRVRVIERP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 203 KREGLIRARLIGASHASGDVLVFLDSHCEVNRVWLEPLLHAIAkDPKMvvcplidviddrtleykpsplvrgtfdwnlqf 282
Cdd:COG1215   95 ENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGV-------------------------------- 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 281485547 283 kwdnvfsyemdgpegstkpirspAMSGGIFAIRRHYFNEIGQYDKDMdfWGrENLELSLRIWMCGGQLFIIPCSRVGH 360
Cdd:COG1215  142 -----------------------GASGANLAFRREALEEVGGFDEDT--LG-EDLDLSLRLLRAGYRIVYVPDAVVYE 193
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
134-389 1.68e-18

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 83.50  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 134 PTASIVICFYNEEcNALFQTMSSVTNLTPHYFleEIILVDDMSKvDDLKEKLDyhlETFRGKVKIIRNKKREGLIRARLI 213
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGST-DGTAELLA---ALAFPRVRVIRNPENLGFAAARNL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 214 GASHASGDVLVFLDSHCEVNRVWLEPLLHAiakdpkmvvcplidviddrtleykpsplvrgtfdwnlqfkwdnvfsyemd 293
Cdd:COG1216   76 GLRAAGGDYLLFLDDDTVVEPDWLERLLAA-------------------------------------------------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 294 gpegstkpirspamsgGIFAIRRHYFNEIGQYDKDMdFWGRENLELSLRIWMCGGQLFIIPCSRVGHISKKqTGKPSTII 373
Cdd:COG1216  106 ----------------ACLLIRREVFEEVGGFDERF-FLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGA-SSGPLLRA 167

                        250
                 ....*....|....*.
gi 281485547 374 SAMTHNYLRLVHVWLD 389
Cdd:COG1216  168 YYLGRNRLLFLRKHGP 183
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 138-253 2.34e-18

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: 81.78  E-value: 2.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 138 IVICFYNEECNaLFQTMSSVTNLTPHYFleEIILVDDMSKVDDLKEKLDYHLETFRgkVKIIRNKKREGLIRARLIGASH 217
Cdd:cd00761    1 VIIPAYNEEPY-LERCLESLLAQTYPNF--EVIVVDDGSTDGTLEILEEYAKKDPR--VIRVINEENQGLAAARNAGLKA 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 281485547 218 ASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVC 253
Cdd:cd00761   76 ARGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 134-363 7.74e-17

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 78.98  E-value: 7.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 134 PTASIVICFYNEECNaLFQTMSSVTNLTPHYFleEIILVDDMSKvDDLKEKLDYHLETFrGKVKIIRNKKREGLIRARLI 213
Cdd:COG0463    2 PLVSVVIPTYNEEEY-LEEALESLLAQTYPDF--EIIVVDDGST-DGTAEILRELAAKD-PRIRVIRLERNRGKGAARNA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 214 GASHASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVvcplidVIDDRTLEYKPSPLVRGTfdwNLQFKWDNVFSyemd 293
Cdd:COG0463   77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADL------VYGSRLIREGESDLRRLG---SRLFNLVRLLT---- 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 294 gpegstkpiRSPAMSGGIFAIRRHYFNEIGqYDKDMdfwgRENLELsLRIWMCGGQLFIIPCSRVGHISK 363
Cdd:COG0463  144 ---------NLPDSTSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVPVRYRAGESK 198
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 138-329 7.85e-11

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: 60.70  E-value: 7.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 138 IVICFYNEEcNALFQTMSSVTNLTphYFLEEIILVDDMSKvDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLIGASH 217
Cdd:cd06423    1 IIVPAYNEE-AVIERTIESLLALD--YPKLEVIVVDDGST-DDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 218 ASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMV-VCPLIDVIDDRTleykpSPLVRG-TFDWNLQFKWDNVFSYEMDGP 295
Cdd:cd06423   77 AKGDIVVVLDADTILEPDALKRLVVPFFADPKVGaVQGRVRVRNGSE-----NLLTRLqAIEYLSIFRLGRRAQSALGGV 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 281485547 296 egstkpirsPAMSGGIFAIRRHYFNEIGQYDKDM 329
Cdd:cd06423  152 ---------LVLSGAFGAFRREALREVGGWDEDT 176
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 135-382 9.43e-11

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: 61.86  E-value: 9.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 135 TASIVICFYNEEcNALFQTMSSVTNLTPHYFLEEIILVDDMSKvDDLKEKLDyHLETFRGKVKIIRNKKReglIR--ARL 212
Cdd:cd02525    1 FVSIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGST-DGTREIVQ-EYAAKDPRIRLIDNPKR---IQsaGLN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 213 IGASHASGDVLVFLDSHCEVNRVWLEPLLHAIAK-DPKMVVCPLIdviddrtleykpsPLVRGTFDWNLqfkwdnvfSYE 291
Cdd:cd02525   75 IGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRtGADNVGGPME-------------TIGESKFQKAI--------AVA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 292 MDGPEGSTK-PIRSPAMSGG----IF--AIRRHYFNEIGQYDKdmDFWGRENLELSLRIWMCGGQLFIIPCSRVGHiskk 364
Cdd:cd02525  134 QSSPLGSGGsAYRGGAVKIGyvdtVHhgAYRREVFEKVGGFDE--SLVRNEDAELNYRLRKAGYKIWLSPDIRVYY---- 207

                        250
                 ....*....|....*...
gi 281485547 365 qtgKPSTIISAMTHNYLR 382
Cdd:cd02525  208 ---YPRSTLKKLARQYFR 222
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 138-360 1.20e-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: 59.88  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 138 IVICFYNEECNaLFQTMSSVTNLTPHYFleEIILVDDMSKvDDLKEkldyHLETFRGKVKIIRNKKREGLIRARLIGASH 217
Cdd:cd04186    1 IIIVNYNSLEY-LKACLDSLLAQTYPDF--EVIVVDNAST-DGSVE----LLRELFPEVRLIRNGENLGFGAGNNQGIRE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 218 ASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCplidviddrtleykpSPLVRGTFdwnlqfkwdnvfsyemdgpeg 297
Cdd:cd04186   73 AKGDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIV---------------GPKVSGAF--------------------- 116

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281485547 298 stkpirspamsggiFAIRRHYFNEIGQYDKDMdFWGRENLELSLRIWMCGGQLFIIPCSRVGH 360
Cdd:cd04186  117 --------------LLVRREVFEEVGGFDEDF-FLYYEDVDLCLRARLAGYRVLYVPQAVIYH 164
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 138-341 1.56e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 60.77  E-value: 1.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 138 IVICFYNEECNaLFQTMSSVTNLTPHYFLEEIILVDDMSKvDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLI--GA 215
Cdd:cd04192    1 VVIAARNEAEN-LPRLLQSLSALDYPKEKFEVILVDDHST-DGTVQILEFAAAKPNFQLKILNNSRVSISGKKNALttAI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 216 SHASGDVLVFLDSHCEVNRVWLEPLLHAIAKD-PKMVVCPLIDVIDDRTLEYkpsplvRGTFDW-NLQFKWDNVFSYEMd 293
Cdd:cd04192   79 KAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEqIGLVAGPVIYFKGKSLLAK------FQRLDWlSLLGLIAGSFGLGK- 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 281485547 294 gpegstkpirsPAM-SGGIFAIRRHYFNEIGQYDKDMDFWgRENLELSL 341
Cdd:cd04192  152 -----------PFMcNGANMAYRKEAFFEVGGFEGNDHIA-SGDDELLL 188
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 137-343 2.92e-08

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: 54.59  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547  137 SIVICFYNEECNALFqtMSSVTNLTPHYFLE-EIILVDDMSKVDDLKEkldyhLETFRGKVKIIRNK----KREGLIRAR 211
Cdd:pfam10111   1 SVVIPVYNGEKTHWI--QERILNQTFQYDPEfELIIINDGSTDKTLEE-----VSSIKDHNLQVYYPnapdTTYSLAASR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547  212 LIGASHASGDVLVFLDSHCEVNRVWLEPLLhAIAKDPKM-------VVCPLIDVIDDRTLEYKPSplvrGTFDWNLQFKW 284
Cdd:pfam10111  74 NRGTSHAIGEYISFIDGDCLWSPDKFEKQL-KIATSLALqeniqaaVVLPVTDLNDESSNFLRRG----GDLTASGDVLR 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 281485547  285 DNVFSYemdgpegsTKPIRSPAMSGGIFAIRRHYFNEIGQYDKDMDFWGRENLELSLRI 343
Cdd:pfam10111 149 DLLVFY--------SPLAIFFAPNSSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRL 199
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 138-228 1.77e-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: 51.03  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 138 IVICFYNEECN--ALFQTMSSVTNLTPHYfleEIILVDDMSKvDDLKEKLDYHLETFrGKVKIIRNKKREGLIRARLIGA 215
Cdd:cd04179    1 VVIPAYNEEENipELVERLLAVLEEGYDY---EIIVVDDGST-DGTAEIARELAARV-PRVRVIRLSRNFGKGAAVRAGF 75

                         90
                 ....*....|...
gi 281485547 216 SHASGDVLVFLDS 228
Cdd:cd04179   76 KAARGDIVVTMDA 88
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 138-228 2.81e-07

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: 50.55  E-value: 2.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 138 IVICFYNEECN--ALFQTMSSV-TNLTPHYfleEIILVDDMSKvDDLKEKLDYHLETFrGKVKIIRNKKREGLIRARLIG 214
Cdd:cd04187    1 IVVPVYNEEENlpELYERLKAVlESLGYDY---EIIFVDDGST-DRTLEILRELAARD-PRVKVIRLSRNFGQQAALLAG 75

                         90
                 ....*....|....
gi 281485547 215 ASHASGDVLVFLDS 228
Cdd:cd04187   76 LDHARGDAVITMDA 89
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 130-319 8.69e-07

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: 49.89  E-value: 8.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 130 PARLPTASIVICFYNEECNALfQTMSSVTNLT-PHYFLeEIILVDDMSkVDDLKEKLDYHLEtfrGKVKIIRNKKREGLI 208
Cdd:cd06439   25 PAYLPTVTIIIPAYNEEAVIE-AKLENLLALDyPRDRL-EIIVVSDGS-TDGTAEIAREYAD---KGVKLLRFPERRGKA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 209 RARLIGASHASGDVLVFLDshceVNRVWLEPLLHAIAK---DPKM--VVCPLidVIDDRTleykpsplvRGTFDWNLQFK 283
Cdd:cd06439   99 AALNRALALATGEIVVFTD----ANALLDPDALRLLVRhfaDPSVgaVSGEL--VIVDGG---------GSGSGEGLYWK 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 281485547 284 WDNvFSYEMDGPEGSTkpirsPAMSGGIFAIRRHYF 319
Cdd:cd06439  164 YEN-WLKRAESRLGST-----VGANGAIYAIRRELF 193
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 138-227 4.99e-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: 44.10  E-value: 4.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 138 IVICFYNEEcNALFQTMSSVtnltpHYFLE-------EIILVDDMSKvDDLKEKLDYHLETFRGKVKIIRNKKREGLIRA 210
Cdd:cd04188    1 VVIPAYNEE-KRLPPTLEEA-----VEYLEerpsfsyEIIVVDDGSK-DGTAEVARKLARKNPALIRVLTLPKNRGKGGA 73

                         90
                 ....*....|....*..
gi 281485547 211 RLIGASHASGDVLVFLD 227
Cdd:cd04188   74 VRAGMLAARGDYILFAD 90
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 137-343 6.61e-05

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: 44.10  E-value: 6.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 137 SIVICFYNEEcNALFQTMSSVTNLTPHYFleEIILVDDMSKvDDLKEKLDyhletfRGKVKIIRNKKreGliRARLI--G 214
Cdd:cd02522    2 SIIIPTLNEA-ENLPRLLASLRRLNPLPL--EIIVVDGGST-DGTVAIAR------SAGVVVISSPK--G--RARQMnaG 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 215 ASHASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVC--PLIDviddrtleyKPSPLVRGTF-DWNLQFKWdnvfsye 291
Cdd:cd02522   68 AAAARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAfrLRFD---------DPGPRLRLLElGANLRSRL------- 131

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 281485547 292 mdgpegstkpIRSPAMSGGIFaIRRHYFNEIGQYDKD--MdfwgrENLELSLRI 343
Cdd:cd02522  132 ----------FGLPYGDQGLF-IRRELFEELGGFPELplM-----EDVELVRRL 169
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 137-250 1.31e-04

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: 43.40  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 137 SIVICFYNEECNALFQTMSSVTNLTPHyfleEIILVDDmskvDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLIGAS 216
Cdd:cd06434    3 TVIIPVYDEDPDVFRECLRSILRQKPL----EIIVVTD----GDDEPYLSILSQTVKYGGIFVITVPHPGKRRALAEGIR 74

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 281485547 217 HASGDVLVFLDSHCevnrVWLEPLLHAIAK---DPKM 250
Cdd:cd06434   75 HVTTDIVVLLDSDT----VWPPNALPEMLKpfeDPKV 107
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 134-363 3.40e-04

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: 41.80  E-value: 3.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 134 PTASIVICFYNEECNALFQTMSSVTNLT-PHYfleEIILVDDMSKVDDLKEKLDYHLETFRgKVKIIRNKKREGLIRARL 212
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAQTyPNW---ELCIADDASTDPEVKRVLKKYAAQDP-RIKVVFREENGGISAATN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 213 IGASHASGDVLVFLDSHCEvnrvwLEP--LLH---AIAKDPKmvvCPLI----DVIDDRTLEYKPsplvrgtfdwnlQFK 283
Cdd:cd04184   77 SALELATGEFVALLDHDDE-----LAPhaLYEvvkALNEHPD---ADLIysdeDKIDEGGKRSEP------------FFK 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 284 WDnvFSYEMdgpegstkpIRSPAMSGGIFAIRRHYFNEIGQYDKDMDfwGRENLELSLRiwmcggqlFIIPCSRVGHISK 363
Cdd:cd04184  137 PD--WSPDL---------LLSQNYIGHLLVYRRSLVRQVGGFREGFE--GAQDYDLVLR--------VSEHTDRIAHIPR 195
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 139-382 9.01e-04

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


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 40.73  E-value: 9.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 139 VICFYNEECNALFQTMSSVtnltpHYFLEEIILVDDMSKVDDLKEKLDYHletfrGKVKIIRNKKREGLIRARLIGASHA 218
Cdd:cd02526    2 VVVTYNPDLSKLKELLAAL-----AEQVDKVVVVDNSSGNDIELRLRLNS-----EKIELIHLGENLGIAKALNIGIKAA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 219 SG---DVLVFL--DSHCE---VNRVWLEpLLHAIAKDPKMVVCPLIdvIDDRTLEYKPSPLVRGTFDWNLqfkwdnvfsy 290
Cdd:cd02526   72 LEngaDYVLLFdqDSVPPpdmVEKLLAY-KILSDKNSNIGAVGPRI--IDRRTGENSPGVRKSGYKLRIQ---------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 291 emdgPEGSTKPIRSP-AMSGGIFaIRRHYFNEIGQYDKDM-----DFwgrenlELSLRIWMCGGQLFIIPCS----RVGH 360
Cdd:cd02526  139 ----KEGEEGLKEVDfLITSGSL-ISLEALEKVGGFDEDLfidyvDT------EWCLRARSKGYKIYVVPDAvlkhELGD 207

                        250       260
                 ....*....|....*....|..
gi 281485547 361 ISKKQTGkpstIISAMTHNYLR 382
Cdd:cd02526  208 KRVKRLG----GVSVPLHSPLR 225
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 138-229 9.98e-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: 9.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281485547 138 IVICFYNEECN------ALFQTMSSvtnltPHYfleEIILVDDMSK------VDDLKEKldyhletfRGKVKIIRNKKRE 205
Cdd:cd06442    1 IIIPTYNERENipelieRLDAALKG-----IDY---EIIVVDDNSPdgtaeiVRELAKE--------YPRVRLIVRPGKR 64

                         90       100
                 ....*....|....*....|....*..
gi 281485547 206 GLIRARLIGASHASGDVLVFLD---SH 229
Cdd:cd06442   65 GLGSAYIEGFKAARGDVIVVMDadlSH 91
 
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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