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Conserved domains on  [gi|767965823|ref|XP_011518373|]
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polypeptide N-acetylgalactosaminyltransferase 18 isoform X3 [Homo sapiens]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 157-365 4.29e-99

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.


The actual alignment was detected with superfamily member cd02510:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 299  Bit Score: 295.65  E-value: 4.29e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 157 SIVFIFVNEALSVLLRSIHSAMERTPPHLLKEIILVDDNSSNEELKEKLteyvDKVNSQKPGFIKVVRHSKQEGLIRSRV 236
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLL----EEYYKKYLPKVKVLRLKKREGLIRARI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 237 SGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFEIEEYPLAAQG-FDWELWCRYLNPPKAW 315
Cdd:cd02510   77 AGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGgFDWSLHFKWLPLPEEE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767965823 316 WKLENSTAPIRSPALIGC-FIVDRQYFQEIGLLDEGMEVYGGENVELGIRT 365
Cdd:cd02510  157 RRRESPTAPIRSPTMAGGlFAIDREWFLELGGYDEGMDIWGGENLELSFKV 207
 
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 ...
 157-365 4.29e-99

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: 295.65  E-value: 4.29e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 157 SIVFIFVNEALSVLLRSIHSAMERTPPHLLKEIILVDDNSSNEELKEKLteyvDKVNSQKPGFIKVVRHSKQEGLIRSRV 236
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLL----EEYYKKYLPKVKVLRLKKREGLIRARI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 237 SGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFEIEEYPLAAQG-FDWELWCRYLNPPKAW 315
Cdd:cd02510   77 AGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGgFDWSLHFKWLPLPEEE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767965823 316 WKLENSTAPIRSPALIGC-FIVDRQYFQEIGLLDEGMEVYGGENVELGIRT 365
Cdd:cd02510  157 RRRESPTAPIRSPTMAGGlFAIDREWFLELGGYDEGMDIWGGENLELSFKV 207
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 157-343 2.46e-22

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: 92.46  E-value: 2.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823  157 SIVFIFVNEAlSVLLRSIHSAMERTPPHLlkEIILVDDNSSnEELKEKLTEYVdkvnsQKPGFIKVVRHSKQEGLIRSRV 236
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGST-DGTVEIAEEYA-----KKDPRVRVIRLPENRGKAGARN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823  237 SGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFeieEYPLAAQGFDWELWCRYLNppkaww 316
Cdd:pfam00535  72 AGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETG---EYRRASRITLSRLPFFLGL------ 142

                         170       180
                  ....*....|....*....|....*..
gi 767965823  317 KLENSTAPIRSPaliGCFIVDRQYFQE 343
Cdd:pfam00535 143 RLLGLNLPFLIG---GFALYRREALEE 166
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 154-347 8.99e-11

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 60.87  E-value: 8.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 154 PEVSIVFIFVNEAlSVLLRSIHSAMERTPPHLlkEIILVDDNSSNEELkEKLTEYvdkvnSQKPGFIKVVRHSKQEGLIR 233
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTA-EILREL-----AAKDPRIRVIRLERNRGKGA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 234 SRVSGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFdniKYDNFEIEEYPLAAQGFDWELWCRYLNPPK 313
Cdd:COG0463   73 ARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSR---LIREGESDLRRLGSRLFNLVRLLTNLPDST 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767965823 314 AWWKLenstapIRSPALIGcFIVDRQYFQEIGLL 347
Cdd:COG0463  150 SGFRL------FRREVLEE-LGFDEGFLEDTELL 176
 
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 ...
 157-365 4.29e-99

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: 295.65  E-value: 4.29e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 157 SIVFIFVNEALSVLLRSIHSAMERTPPHLLKEIILVDDNSSNEELKEKLteyvDKVNSQKPGFIKVVRHSKQEGLIRSRV 236
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLL----EEYYKKYLPKVKVLRLKKREGLIRARI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 237 SGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFEIEEYPLAAQG-FDWELWCRYLNPPKAW 315
Cdd:cd02510   77 AGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGgFDWSLHFKWLPLPEEE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767965823 316 WKLENSTAPIRSPALIGC-FIVDRQYFQEIGLLDEGMEVYGGENVELGIRT 365
Cdd:cd02510  157 RRRESPTAPIRSPTMAGGlFAIDREWFLELGGYDEGMDIWGGENLELSFKV 207
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 157-343 2.46e-22

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: 92.46  E-value: 2.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823  157 SIVFIFVNEAlSVLLRSIHSAMERTPPHLlkEIILVDDNSSnEELKEKLTEYVdkvnsQKPGFIKVVRHSKQEGLIRSRV 236
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGST-DGTVEIAEEYA-----KKDPRVRVIRLPENRGKAGARN 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823  237 SGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFeieEYPLAAQGFDWELWCRYLNppkaww 316
Cdd:pfam00535  72 AGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETG---EYRRASRITLSRLPFFLGL------ 142

                         170       180
                  ....*....|....*....|....*..
gi 767965823  317 KLENSTAPIRSPaliGCFIVDRQYFQE 343
Cdd:pfam00535 143 RLLGLNLPFLIG---GFALYRREALEE 166
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 154-347 8.99e-11

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 60.87  E-value: 8.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 154 PEVSIVFIFVNEAlSVLLRSIHSAMERTPPHLlkEIILVDDNSSNEELkEKLTEYvdkvnSQKPGFIKVVRHSKQEGLIR 233
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTA-EILREL-----AAKDPRIRVIRLERNRGKGA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 234 SRVSGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFdniKYDNFEIEEYPLAAQGFDWELWCRYLNPPK 313
Cdd:COG0463   73 ARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSR---LIREGESDLRRLGSRLFNLVRLLTNLPDST 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767965823 314 AWWKLenstapIRSPALIGcFIVDRQYFQEIGLL 347
Cdd:COG0463  150 SGFRL------FRREVLEE-LGFDEGFLEDTELL 176
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 150-272 4.13e-10

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: 60.14  E-value: 4.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 150 PDSLPEVSIVFIFVNEALsVLLRSIHSAMERTPPHLLKEIILVDDNSSnEELKEKLTEYVDKVNsqkpgFIKVVRHSKQE 229
Cdd:COG1215   25 PADLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIARELAAEYP-----RVRVIERPENG 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767965823 230 GLIRSRVSGWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENR 272
Cdd:COG1215   98 GKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG 140
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
154-368 2.73e-09

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 56.54  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 154 PEVSIVFIFVNEAlSVLLRSIHSAMERTPPHLlkEIILVDDNSSNEElkeklteyVDKVNSQKPGFIKVVRHSKQEGLIR 233
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGT--------AELLAALAFPRVRVIRNPENLGFAA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 234 SRVSGWRAATAPVVALFDAHVEFNVGWAEPVLTRikenrkriispsfdnikydnfeieeyplaaqgfdwelwcrylnppk 313
Cdd:COG1216   72 ARNLGLRAAGGDYLLFLDDDTVVEPDWLERLLAA---------------------------------------------- 105

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767965823 314 awwklenstapirspaliGCFIVDRQYFQEIGLLDEGMEVYGGEnVELGIRTRKL 368
Cdd:COG1216  106 ------------------ACLLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKA 141
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 158-310 2.21e-08

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: 52.89  E-value: 2.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 158 IVFIFVNEAlSVLLRSIHSAMERTPPHLlkEIILVDDNSSnEELKEKLTEYVDKVNSqkpgfIKVVRHSKQEGLIRSRVS 237
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGST-DGTLEILEEYAKKDPR-----VIRVINEENQGLAAARNA 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767965823 238 GWRAATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPS-----FDNIKYDNFEIEEYPLAAQGFDWELWCRYLN 310
Cdd:cd00761   72 GLKAARGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGpgnllFRRELLEEIGGFDEALLSGEEDDDFLLRLLR 149
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 164-252 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: 50.65  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 164 NEA--LSVLLRSIHSAMERTPPHllkEIILVDDNSSNEELkEKLTEYVDKVNSqkpgfIKVVRHSKQEGLIRSRVSGWRA 241
Cdd:cd04179    7 NEEenIPELVERLLAVLEEGYDY---EIIVVDDGSTDGTA-EIARELAARVPR-----VRVIRLSRNFGKGAAVRAGFKA 77

                         90
                 ....*....|.
gi 767965823 242 ATAPVVALFDA 252
Cdd:cd04179   78 ARGDIVVTMDA 88
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 154-251 8.32e-05

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 42.96  E-value: 8.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 154 PEVSIVFIFVNEALSVLLRSIHSAMERTPPHLlkEIILVDDNSSNEELKEKLTEYvdkvnSQKPGFIKVVRHSKQEGLIR 233
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKY-----AAQDPRIKVVFREENGGISA 73

                         90
                 ....*....|....*...
gi 767965823 234 SRVSGWRAATAPVVALFD 251
Cdd:cd04184   74 ATNSALELATGEFVALLD 91
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 164-252 4.99e-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: 40.98  E-value: 4.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 164 NEA--LSVLLRSIHSAMErtPPHLlkEIILVDDNS---SNEELKEKLTEYvdkvnsqkpGFIKVVRHSKQEGLIRSRVSG 238
Cdd:cd06442    7 NERenIPELIERLDAALK--GIDY--EIIVVDDNSpdgTAEIVRELAKEY---------PRVRLIVRPGKRGLGSAYIEG 73

                         90
                 ....*....|....
gi 767965823 239 WRAATAPVVALFDA 252
Cdd:cd06442   74 FKAARGDVIVVMDA 87
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 164-252 8.21e-04

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: 39.90  E-value: 8.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767965823 164 NEAlSVLLRSIHSAMERTPPHLlkEIILVDDNSSNEELkEKLTEYVDKVNSQKpgfiKVVRHSKQEGLIRSRVSGWRAAT 243
Cdd:cd06423    7 NEE-AVIERTIESLLALDYPKL--EVIVVDDGSTDDTL-EILEELAALYIRRV----LVVRDKENGGKAGALNAGLRHAK 78


                 ....*....
gi 767965823 244 APVVALFDA 252
Cdd:cd06423   79 GDIVVVLDA 87
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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