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Conserved domains on  [gi|767946958|ref|XP_011514155|]
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inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5 isoform X4 [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
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 ...
26-322 2.56e-156

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: 2.56e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  26 SIVICFYNEECNALFQTMSSVTNLTPHYFLEEIILVDDMSKVDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLIGAS 105
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 106 HASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCPLIDVIDDRTLEYKPSP-LVRGTFDWNLQFKWDNVFSYEMDgP 184
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEERR-R 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 185 EGSTKPIRSPAMSGGIFAIRRHYFNEIGQYDKDMDFWGRENLELSLRIWMCGGQLFIIPCSRVGHISKKQtGKPSTI--- 261
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRK-RKPYTFpgg 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767946958 262 ISAMTHNYLRLVHVWLDEYKEQFFLRKPGLKYVTYGNIRERVELRKRLGCKSFQWYLDNVF 322
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 ...
26-322 2.56e-156

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: 2.56e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  26 SIVICFYNEECNALFQTMSSVTNLTPHYFLEEIILVDDMSKVDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLIGAS 105
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 106 HASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCPLIDVIDDRTLEYKPSP-LVRGTFDWNLQFKWDNVFSYEMDgP 184
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEERR-R 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 185 EGSTKPIRSPAMSGGIFAIRRHYFNEIGQYDKDMDFWGRENLELSLRIWMCGGQLFIIPCSRVGHISKKQtGKPSTI--- 261
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRK-RKPYTFpgg 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767946958 262 ISAMTHNYLRLVHVWLDEYKEQFFLRKPGLKYVTYGNIRERVELRKRLGCKSFQWYLDNVF 322
Cdd:cd02510  239 SGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
26-210 9.40e-31

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: 114.03  E-value: 9.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958   26 SIVICFYNEEcNALFQTMSSVTNLTphYFLEEIILVDDMSKvDDLKEKLDYHLETFrGKVKIIRNKKREGLIRARLIGAS 105
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGST-DGTVEIAEEYAKKD-PRVRVIRLPENRGKAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  106 HASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCPLIDVIDDRTLEYKpsplvrgtfdWNLQFKWDNVFSYEMDGPE 185
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR----------RASRITLSRLPFFLGLRLL 145
                         170       180
                  ....*....|....*....|....*
gi 767946958  186 GSTKPIRSPAMsggiFAIRRHYFNE 210
Cdd:pfam00535 146 GLNLPFLIGGF----ALYRREALEE 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
16-249 2.50e-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: 83.64  E-value: 2.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  16 KHYPARLPTASIVICFYNEECNaLFQTMSSVTNLTPHYFLEEIILVDDMSKvDDLKEKLDyHLETFRGKVKIIRNKKREG 95
Cdd:COG1215   22 RRAPADLPRVSVIIPAYNEEAV-IEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIAR-ELAAEYPRVRVIERPENGG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  96 LIRARLIGASHASGDVLVFLDSHCEVNRVWLEPLLHAIAkDPKMvvcplidviddrtleykpsplvrgtfdwnlqfkwdn 175
Cdd:COG1215   99 KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGV------------------------------------ 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767946958 176 vfsyemdgpegstkpirspAMSGGIFAIRRHYFNEIGQYDKDMdfWGrENLELSLRIWMCGGQLFIIPCSRVGH 249
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 ...
26-322 2.56e-156

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: 2.56e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  26 SIVICFYNEECNALFQTMSSVTNLTPHYFLEEIILVDDMSKVDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLIGAS 105
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 106 HASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCPLIDVIDDRTLEYKPSP-LVRGTFDWNLQFKWDNVFSYEMDgP 184
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEERR-R 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 185 EGSTKPIRSPAMSGGIFAIRRHYFNEIGQYDKDMDFWGRENLELSLRIWMCGGQLFIIPCSRVGHISKKQtGKPSTI--- 261
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRK-RKPYTFpgg 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767946958 262 ISAMTHNYLRLVHVWLDEYKEQFFLRKPGLKYVTYGNIRERVELRKRLGCKSFQWYLDNVF 322
Cdd:cd02510  239 SGTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
26-210 9.40e-31

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: 114.03  E-value: 9.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958   26 SIVICFYNEEcNALFQTMSSVTNLTphYFLEEIILVDDMSKvDDLKEKLDYHLETFrGKVKIIRNKKREGLIRARLIGAS 105
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGST-DGTVEIAEEYAKKD-PRVRVIRLPENRGKAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  106 HASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCPLIDVIDDRTLEYKpsplvrgtfdWNLQFKWDNVFSYEMDGPE 185
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR----------RASRITLSRLPFFLGLRLL 145
                         170       180
                  ....*....|....*....|....*
gi 767946958  186 GSTKPIRSPAMsggiFAIRRHYFNE 210
Cdd:pfam00535 146 GLNLPFLIGGF----ALYRREALEE 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
16-249 2.50e-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: 83.64  E-value: 2.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  16 KHYPARLPTASIVICFYNEECNaLFQTMSSVTNLTPHYFLEEIILVDDMSKvDDLKEKLDyHLETFRGKVKIIRNKKREG 95
Cdd:COG1215   22 RRAPADLPRVSVIIPAYNEEAV-IEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIAR-ELAAEYPRVRVIERPENGG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  96 LIRARLIGASHASGDVLVFLDSHCEVNRVWLEPLLHAIAkDPKMvvcplidviddrtleykpsplvrgtfdwnlqfkwdn 175
Cdd:COG1215   99 KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGV------------------------------------ 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767946958 176 vfsyemdgpegstkpirspAMSGGIFAIRRHYFNEIGQYDKDMdfWGrENLELSLRIWMCGGQLFIIPCSRVGH 249
Cdd:COG1215  142 -------------------GASGANLAFRREALEEVGGFDEDT--LG-EDLDLSLRLLRAGYRIVYVPDAVVYE 193
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
27-142 2.73e-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: 80.63  E-value: 2.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  27 IVICFYNEECNaLFQTMSSVTNLTPHYFleEIILVDDMSKVDDLKEKLDYHLETFRgkVKIIRNKKREGLIRARLIGASH 106
Cdd:cd00761    1 VIIPAYNEEPY-LERCLESLLAQTYPNF--EVIVVDDGSTDGTLEILEEYAKKDPR--VIRVINEENQGLAAARNAGLKA 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767946958 107 ASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVC 142
Cdd:cd00761   76 ARGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
23-278 4.94e-18

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 80.81  E-value: 4.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  23 PTASIVICFYNEEcNALFQTMSSVTNLTPHYFleEIILVDDMSKvDDLKEKLDyhlETFRGKVKIIRNKKREGLIRARLI 102
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGST-DGTAELLA---ALAFPRVRVIRNPENLGFAAARNL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 103 GASHASGDVLVFLDSHCEVNRVWLEPLLHAiakdpkmvvcplidviddrtleykpsplvrgtfdwnlqfkwdnvfsyemd 182
Cdd:COG1216   76 GLRAAGGDYLLFLDDDTVVEPDWLERLLAA-------------------------------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 183 gpegstkpirspamsgGIFAIRRHYFNEIGQYDKDMdFWGRENLELSLRIWMCGGQLFIIPCSRVGHISKKqTGKPSTII 262
Cdd:COG1216  106 ----------------ACLLIRREVFEEVGGFDERF-FLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGA-SSGPLLRA 167
                        250
                 ....*....|....*.
gi 767946958 263 SAMTHNYLRLVHVWLD 278
Cdd:COG1216  168 YYLGRNRLLFLRKHGP 183
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
23-252 1.38e-16

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 77.05  E-value: 1.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  23 PTASIVICFYNEECNaLFQTMSSVTNLTPHYFleEIILVDDMSKvDDLKEKLDYHLETFrGKVKIIRNKKREGLIRARLI 102
Cdd:COG0463    2 PLVSVVIPTYNEEEY-LEEALESLLAQTYPDF--EIIVVDDGST-DGTAEILRELAAKD-PRIRVIRLERNRGKGAARNA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 103 GASHASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVvcplidVIDDRTLEYKPSPLVRGTfdwNLQFKWDNVFSyemd 182
Cdd:COG0463   77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADL------VYGSRLIREGESDLRRLG---SRLFNLVRLLT---- 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 183 gpegstkpiRSPAMSGGIFAIRRHYFNEIGqYDKDMdfwgRENLELsLRIWMCGGQLFIIPCSRVGHISK 252
Cdd:COG0463  144 ---------NLPDSTSGFRLFRREVLEELG-FDEGF----LEDTEL-LRALRHGFRIAEVPVRYRAGESK 198
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
27-230 6.38e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 61.54  E-value: 6.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  27 IVICFYNEECNaLFQTMSSVTNLTPHYFLEEIILVDDMSKvDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLI--GA 104
Cdd:cd04192    1 VVIAARNEAEN-LPRLLQSLSALDYPKEKFEVILVDDHST-DGTVQILEFAAAKPNFQLKILNNSRVSISGKKNALttAI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 105 SHASGDVLVFLDSHCEVNRVWLEPLLHAIAKD-PKMVVCPLIDVIDDRTLEYkpsplvRGTFDW-NLQFKWDNVFSYEMd 182
Cdd:cd04192   79 KAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEqIGLVAGPVIYFKGKSLLAK------FQRLDWlSLLGLIAGSFGLGK- 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767946958 183 gpegstkpirsPAM-SGGIFAIRRHYFNEIGQYDKDMDFWgRENLELSL 230
Cdd:cd04192  152 -----------PFMcNGANMAYRKEAFFEVGGFEGNDHIA-SGDDELLL 188
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
24-271 7.55e-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: 61.48  E-value: 7.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  24 TASIVICFYNEEcNALFQTMSSVTNLTPHYFLEEIILVDDMSKvDDLKEKLDyHLETFRGKVKIIRNKKReglIR--ARL 101
Cdd:cd02525    1 FVSIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGST-DGTREIVQ-EYAAKDPRIRLIDNPKR---IQsaGLN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 102 IGASHASGDVLVFLDSHCEVNRVWLEPLLHAIAK-DPKMVVCPLIdviddrtleykpsPLVRGTFDWNLqfkwdnvfSYE 180
Cdd:cd02525   75 IGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRtGADNVGGPME-------------TIGESKFQKAI--------AVA 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 181 MDGPEGSTK-PIRSPAMSGG----IF--AIRRHYFNEIGQYDKdmDFWGRENLELSLRIWMCGGQLFIIPCSRVGHiskk 253
Cdd:cd02525  134 QSSPLGSGGsAYRGGAVKIGyvdtVHhgAYRREVFEKVGGFDE--SLVRNEDAELNYRLRKAGYKIWLSPDIRVYY---- 207
                        250
                 ....*....|....*...
gi 767946958 254 qtgKPSTIISAMTHNYLR 271
Cdd:cd02525  208 ---YPRSTLKKLARQYFR 222
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
27-218 8.88e-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: 59.93  E-value: 8.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  27 IVICFYNEEcNALFQTMSSVTNLTphYFLEEIILVDDMSKvDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLIGASH 106
Cdd:cd06423    1 IIVPAYNEE-AVIERTIESLLALD--YPKLEVIVVDDGST-DDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 107 ASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMV-VCPLIDVIDDRTleykpSPLVRG-TFDWNLQFKWDNVFSYEMDGP 184
Cdd:cd06423   77 AKGDIVVVLDADTILEPDALKRLVVPFFADPKVGaVQGRVRVRNGSE-----NLLTRLqAIEYLSIFRLGRRAQSALGGV 151
                        170       180       190
                 ....*....|....*....|....*....|....
gi 767946958 185 egstkpirsPAMSGGIFAIRRHYFNEIGQYDKDM 218
Cdd:cd06423  152 ---------LVLSGAFGAFRREALREVGGWDEDT 176
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
27-249 2.79e-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: 58.34  E-value: 2.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  27 IVICFYNEECNaLFQTMSSVTNLTPHYFleEIILVDDMSKvDDLKEkldyHLETFRGKVKIIRNKKREGLIRARLIGASH 106
Cdd:cd04186    1 IIIVNYNSLEY-LKACLDSLLAQTYPDF--EVIVVDNAST-DGSVE----LLRELFPEVRLIRNGENLGFGAGNNQGIRE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 107 ASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVCplidviddrtleykpSPLVRGTFdwnlqfkwdnvfsyemdgpeg 186
Cdd:cd04186   73 AKGDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIV---------------GPKVSGAF--------------------- 116
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767946958 187 stkpirspamsggiFAIRRHYFNEIGQYDKDMdFWGRENLELSLRIWMCGGQLFIIPCSRVGH 249
Cdd:cd04186  117 --------------LLVRREVFEEVGGFDEDF-FLYYEDVDLCLRARLAGYRVLYVPQAVIYH 164
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
26-232 1.70e-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: 54.98  E-value: 1.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958   26 SIVICFYNEECNALFqtMSSVTNLTPHYFLE-EIILVDDMSKVDDLKEkldyhLETFRGKVKIIRNK----KREGLIRAR 100
Cdd:pfam10111   1 SVVIPVYNGEKTHWI--QERILNQTFQYDPEfELIIINDGSTDKTLEE-----VSSIKDHNLQVYYPnapdTTYSLAASR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  101 LIGASHASGDVLVFLDSHCEVNRVWLEPLLhAIAKDPKM-------VVCPLIDVIDDRTLEYKPSplvrGTFDWNLQFKW 173
Cdd:pfam10111  74 NRGTSHAIGEYISFIDGDCLWSPDKFEKQL-KIATSLALqeniqaaVVLPVTDLNDESSNFLRRG----GDLTASGDVLR 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767946958  174 DNVFSYemdgpegsTKPIRSPAMSGGIFAIRRHYFNEIGQYDKDMDFWGRENLELSLRI 232
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 ...
27-117 2.11e-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: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  27 IVICFYNEECN--ALFQTMSSVTNLTPHYfleEIILVDDMSKvDDLKEKLDYHLETFrGKVKIIRNKKREGLIRARLIGA 104
Cdd:cd04179    1 VVIPAYNEEENipELVERLLAVLEEGYDY---EIIVVDDGST-DGTAEIARELAARV-PRVRVIRLSRNFGKGAAVRAGF 75
                         90
                 ....*....|...
gi 767946958 105 SHASGDVLVFLDS 117
Cdd:cd04179   76 KAARGDIVVTMDA 88
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
27-117 3.27e-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: 49.78  E-value: 3.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  27 IVICFYNEECN--ALFQTMSSV-TNLTPHYfleEIILVDDMSKvDDLKEKLDYHLETFrGKVKIIRNKKREGLIRARLIG 103
Cdd:cd04187    1 IVVPVYNEEENlpELYERLKAVlESLGYDY---EIIFVDDGST-DRTLEILRELAARD-PRVKVIRLSRNFGQQAALLAG 75
                         90
                 ....*....|....
gi 767946958 104 ASHASGDVLVFLDS 117
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 ...
19-208 5.44e-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: 5.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  19 PARLPTASIVICFYNEECNALfQTMSSVTNLT-PHYFLeEIILVDDMSkVDDLKEKLDYHLEtfrGKVKIIRNKKREGLI 97
Cdd:cd06439   25 PAYLPTVTIIIPAYNEEAVIE-AKLENLLALDyPRDRL-EIIVVSDGS-TDGTAEIAREYAD---KGVKLLRFPERRGKA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  98 RARLIGASHASGDVLVFLDshceVNRVWLEPLLHAIAK---DPKM--VVCPLidVIDDRTleykpsplvRGTFDWNLQFK 172
Cdd:cd06439   99 AALNRALALATGEIVVFTD----ANALLDPDALRLLVRhfaDPSVgaVSGEL--VIVDGG---------GSGSGEGLYWK 163
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767946958 173 WDNvFSYEMDGPEGSTkpirsPAMSGGIFAIRRHYF 208
Cdd:cd06439  164 YEN-WLKRAESRLGST-----VGANGAIYAIRRELF 193
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
27-116 4.60e-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: 43.71  E-value: 4.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  27 IVICFYNEEcNALFQTMSSVtnltpHYFLE-------EIILVDDMSKvDDLKEKLDYHLETFRGKVKIIRNKKREGLIRA 99
Cdd:cd04188    1 VVIPAYNEE-KRLPPTLEEA-----VEYLEerpsfsyEIIVVDDGSK-DGTAEVARKLARKNPALIRVLTLPKNRGKGGA 73
                         90
                 ....*....|....*..
gi 767946958 100 RLIGASHASGDVLVFLD 116
Cdd:cd04188   74 VRAGMLAARGDYILFAD 90
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
26-232 7.47e-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: 43.33  E-value: 7.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  26 SIVICFYNEEcNALFQTMSSVTNLTPHYFleEIILVDDMSKvDDLKEKLDyhletfRGKVKIIRNKKreGliRARLI--G 103
Cdd:cd02522    2 SIIIPTLNEA-ENLPRLLASLRRLNPLPL--EIIVVDGGST-DGTVAIAR------SAGVVVISSPK--G--RARQMnaG 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 104 ASHASGDVLVFLDSHCEVNRVWLEPLLHAIAKDPKMVVC--PLIDviddrtleyKPSPLVRGTF-DWNLQFKWdnvfsye 180
Cdd:cd02522   68 AAAARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAfrLRFD---------DPGPRLRLLElGANLRSRL------- 131
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767946958 181 mdgpegstkpIRSPAMSGGIFaIRRHYFNEIGQYDKD--MdfwgrENLELSLRI 232
Cdd:cd02522  132 ----------FGLPYGDQGLF-IRRELFEELGGFPELplM-----EDVELVRRL 169
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
24-139 1.09e-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: 43.01  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  24 TASIVICFYNEECNALFQTMSSVTNLTPHyfleEIILVDDmskvDDLKEKLDYHLETFRGKVKIIRNKKREGLIRARLIG 103
Cdd:cd06434    1 DVTVIIPVYDEDPDVFRECLRSILRQKPL----EIIVVTD----GDDEPYLSILSQTVKYGGIFVITVPHPGKRRALAEG 72
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767946958 104 ASHASGDVLVFLDSHCevnrVWLEPLLHAIAK---DPKM 139
Cdd:cd06434   73 IRHVTTDIVVLLDSDT----VWPPNALPEMLKpfeDPKV 107
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
23-252 3.68e-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: 41.03  E-value: 3.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  23 PTASIVICFYNEECNALFQTMSSVTNLT-PHYfleEIILVDDMSKVDDLKEKLDYHLETFRgKVKIIRNKKREGLIRARL 101
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAQTyPNW---ELCIADDASTDPEVKRVLKKYAAQDP-RIKVVFREENGGISAATN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 102 IGASHASGDVLVFLDSHCEvnrvwLEP--LLH---AIAKDPKmvvCPLI----DVIDDRTLEYKPsplvrgtfdwnlQFK 172
Cdd:cd04184   77 SALELATGEFVALLDHDDE-----LAPhaLYEvvkALNEHPD---ADLIysdeDKIDEGGKRSEP------------FFK 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 173 WDnvFSYEMdgpegstkpIRSPAMSGGIFAIRRHYFNEIGQYDKDMDfwGRENLELSLRiwmcggqlFIIPCSRVGHISK 252
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 ...
28-271 8.00e-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: 40.34  E-value: 8.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  28 VICFYNEECNALFQTMSSVtnltpHYFLEEIILVDDMSKVDDLKEKLDYHletfrGKVKIIRNKKREGLIRARLIGASHA 107
Cdd:cd02526    2 VVVTYNPDLSKLKELLAAL-----AEQVDKVVVVDNSSGNDIELRLRLNS-----EKIELIHLGENLGIAKALNIGIKAA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 108 SG---DVLVFL--DSHCE---VNRVWLEpLLHAIAKDPKMVVCPLIdvIDDRTLEYKPSPLVRGTFDWNLqfkwdnvfsy 179
Cdd:cd02526   72 LEngaDYVLLFdqDSVPPpdmVEKLLAY-KILSDKNSNIGAVGPRI--IDRRTGENSPGVRKSGYKLRIQ---------- 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958 180 emdgPEGSTKPIRSP-AMSGGIFaIRRHYFNEIGQYDKDM-----DFwgrenlELSLRIWMCGGQLFIIPCS----RVGH 249
Cdd:cd02526  139 ----KEGEEGLKEVDfLITSGSL-ISLEALEKVGGFDEDLfidyvDT------EWCLRARSKGYKIYVVPDAvlkhELGD 207
                        250       260
                 ....*....|....*....|..
gi 767946958 250 ISKKQTGkpstIISAMTHNYLR 271
Cdd:cd02526  208 KRVKRLG----GVSVPLHSPLR 225
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
27-118 8.00e-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: 40.21  E-value: 8.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767946958  27 IVICFYNEECN------ALFQTMSSvtnltPHYfleEIILVDDMSK------VDDLKEKldyhletfRGKVKIIRNKKRE 94
Cdd:cd06442    1 IIIPTYNERENipelieRLDAALKG-----IDY---EIIVVDDNSPdgtaeiVRELAKE--------YPRVRLIVRPGKR 64
                         90       100
                 ....*....|....*....|....*..
gi 767946958  95 GLIRARLIGASHASGDVLVFLD---SH 118
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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