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Conserved domains on  [gi|568913802|ref|XP_006498156|]
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polypeptide N-acetylgalactosaminyltransferase 13 isoform X5 [Mus musculus]

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 ...
 160-429 2.97e-167

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: 471.69  E-value: 2.97e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 160 SVVIVFHNEAWSTLLRTVYSVINRSPHYLLSEVILVDDASERDFLKLTLENYVKTLEVPVKIIRMEERSGLIRARLRGAA 239
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 240 ASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREmdRR 319
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 320 KGDRTLPVRTPTMAGGLFSIDRNYFEEIGTYDAGMDIWGGENLEMSFRIWQCGGSLEIVTCSHVGHVFR-KATPYTFPGG 398
Cdd:cd02510  159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238

                        250       260       270
                 ....*....|....*....|....*....|.
gi 568913802 399 TGhVINKNNRRLAEVWMDEFKDFFYIISPGL 429
Cdd:cd02510  239 SG-TVLRNYKRVAEVWMDEYKEYFYKARPEL 268
 
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 ...
 160-429 2.97e-167

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: 471.69  E-value: 2.97e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 160 SVVIVFHNEAWSTLLRTVYSVINRSPHYLLSEVILVDDASERDFLKLTLENYVKTLEVPVKIIRMEERSGLIRARLRGAA 239
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 240 ASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREmdRR 319
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 320 KGDRTLPVRTPTMAGGLFSIDRNYFEEIGTYDAGMDIWGGENLEMSFRIWQCGGSLEIVTCSHVGHVFR-KATPYTFPGG 398
Cdd:cd02510  159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238

                        250       260       270
                 ....*....|....*....|....*....|.
gi 568913802 399 TGhVINKNNRRLAEVWMDEFKDFFYIISPGL 429
Cdd:cd02510  239 SG-TVLRNYKRVAEVWMDEYKEYFYKARPEL 268
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 160-341 1.04e-37

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: 134.83  E-value: 1.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802  160 SVVIVFHNEaWSTLLRTVYSVINRSphYLLSEVILVDDASERDFLKLtLENYVKTLEvPVKIIRMEERSGLIRARLRGAA 239
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQT--YPNFEIIVVDDGSTDGTVEI-AEEYAKKDP-RVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802  240 ASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMagsdmtyggfnWKLNFRWYPVPQREMDRR 319
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR-----------RASRITLSRLPFFLGLRL 144

                         170       180
                  ....*....|....*....|..
gi 568913802  320 KGdRTLPVRTPTMAGGLFSIDR 341
Cdd:pfam00535 145 LG-LNLPFLIGGFALYRREALE 165
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 157-354 1.24e-15

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 75.51  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 157 PNTSVVIVFHNEAwSTLLRTVYSVINRSphYLLSEVILVDDASERDFLKLtLENYVKTLEvPVKIIRMEERSGLIRARLR 236
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQT--YPDFEIIVVDDGSTDGTAEI-LRELAAKDP-RIRVIRLERNRGKGAARNA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 237 GAAASKGQVITFLDAHCECTLGWLEPLLARIKEDrktvvcpiidvisddtfeymaGSDMTYGGFNWKLNFRWYPVPQREM 316
Cdd:COG0463   77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEG---------------------PADLVYGSRLIREGESDLRRLGSRL 135

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568913802 317 DRRkgdRTLPVRTPTMAGGLFSIDRNYFEEIGtYDAGM 354
Cdd:COG0463  136 FNL---VRLLTNLPDSTSGFRLFRREVLEELG-FDEGF 169
 
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 ...
 160-429 2.97e-167

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: 471.69  E-value: 2.97e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 160 SVVIVFHNEAWSTLLRTVYSVINRSPHYLLSEVILVDDASERDFLKLTLENYVKTLEVPVKIIRMEERSGLIRARLRGAA 239
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 240 ASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREmdRR 319
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWLPLPEEE--RR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 320 KGDRTLPVRTPTMAGGLFSIDRNYFEEIGTYDAGMDIWGGENLEMSFRIWQCGGSLEIVTCSHVGHVFR-KATPYTFPGG 398
Cdd:cd02510  159 RESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGG 238

                        250       260       270
                 ....*....|....*....|....*....|.
gi 568913802 399 TGhVINKNNRRLAEVWMDEFKDFFYIISPGL 429
Cdd:cd02510  239 SG-TVLRNYKRVAEVWMDEYKEYFYKARPEL 268
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 160-341 1.04e-37

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: 134.83  E-value: 1.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802  160 SVVIVFHNEaWSTLLRTVYSVINRSphYLLSEVILVDDASERDFLKLtLENYVKTLEvPVKIIRMEERSGLIRARLRGAA 239
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQT--YPNFEIIVVDDGSTDGTVEI-AEEYAKKDP-RVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802  240 ASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMagsdmtyggfnWKLNFRWYPVPQREMDRR 319
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR-----------RASRITLSRLPFFLGLRL 144

                         170       180
                  ....*....|....*....|..
gi 568913802  320 KGdRTLPVRTPTMAGGLFSIDR 341
Cdd:pfam00535 145 LG-LNLPFLIGGFALYRREALE 165
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 161-276 6.35e-17

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: 77.55  E-value: 6.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 161 VVIVFHNEAwSTLLRTVYSVINRSPHYLlsEVILVDDASERDFLKLtLENYVKTlEVPVKIIRMEERSGLIRARLRGAAA 240
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTLEI-LEEYAKK-DPRVIRVINEENQGLAAARNAGLKA 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568913802 241 SKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVC 276
Cdd:cd00761   76 ARGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 157-354 1.24e-15

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 75.51  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 157 PNTSVVIVFHNEAwSTLLRTVYSVINRSphYLLSEVILVDDASERDFLKLtLENYVKTLEvPVKIIRMEERSGLIRARLR 236
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQT--YPDFEIIVVDDGSTDGTAEI-LRELAAKDP-RIRVIRLERNRGKGAARNA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 237 GAAASKGQVITFLDAHCECTLGWLEPLLARIKEDrktvvcpiidvisddtfeymaGSDMTYGGFNWKLNFRWYPVPQREM 316
Cdd:COG0463   77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEG---------------------PADLVYGSRLIREGESDLRRLGSRL 135

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568913802 317 DRRkgdRTLPVRTPTMAGGLFSIDRNYFEEIGtYDAGM 354
Cdd:COG0463  136 FNL---VRLLTNLPDSTSGFRLFRREVLEELG-FDEGF 169
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
157-425 1.09e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 72.33  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 157 PNTSVVIVFHNEaWSTLLRTVYSVINRSphYLLSEVILVDDASERDFLkltleNYVKTLEVP-VKIIRMEERSGLIRARL 235
Cdd:COG1216    3 PKVSVVIPTYNR-PELLRRCLESLLAQT--YPPFEVIVVDNGSTDGTA-----ELLAALAFPrVRVIRNPENLGFAAARN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 236 RGAAASKGQVITFLDAHCECTLGWLEPLLArikedrktvvcpiidvisddtfeymagsdmtyggfnwklnfrwypvpqre 315
Cdd:COG1216   75 LGLRAAGGDYLLFLDDDTVVEPDWLERLLA-------------------------------------------------- 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 316 mdrrkgdrtlpvrtptmAGGLFsIDRNYFEEIGTYDAGMDIWGGEnLEMSFRIWQCGGSLEIVTCSHVGHVFRKAtpyTF 395
Cdd:COG1216  105 -----------------AACLL-IRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGAS---SG 162

                        250       260       270
                 ....*....|....*....|....*....|
gi 568913802 396 PGGTGHVINKNNRRLAEVWMDEFKDFFYII 425
Cdd:COG1216  163 PLLRAYYLGRNRLLFLRKHGPRPLLRLALL 192
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 148-271 5.30e-13

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 69.39  E-value: 5.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 148 KTKVYPDELPNTSVVIVFHNEAwSTLLRTVYSVIN-RSPHYLLsEVILVDDASERDFLKLtLENYvKTLEVPVKIIRMEE 226
Cdd:COG1215   20 RRRRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAqDYPKEKL-EVIVVDDGSTDETAEI-AREL-AAEYPRVRVIERPE 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568913802 227 RSGLIRARLRGAAASKGQVITFLDAHCECTLGWLEPLLARIKEDR 271
Cdd:COG1215   96 NGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG 140
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 160-375 5.83e-08

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 53.39  E-value: 5.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 160 SVVIVFHNEAwSTLLRTVYSVINRSPHYLLSEVILVDDASERDflklTLEnYVKTLEVPVKIIRMEERSGLIR--ARLRG 237
Cdd:cd02525    3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTDG----TRE-IVQEYAAKDPRIRLIDNPKRIQsaGLNIG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 238 AAASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEY---MAGSDMTYGGfnwKLNFRwypVPQR 314
Cdd:cd02525   77 IRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKaiaVAQSSPLGSG---GSAYR---GGAV 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568913802 315 EMdrrkgdrtlpVRTPTMAGGLFSIDRnyFEEIGTYDAGMDIwgGENLEMSFRIWQCGGSL 375
Cdd:cd02525  151 KI----------GYVDTVHHGAYRREV--FEKVGGFDESLVR--NEDAELNYRLRKAGYKI 197
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 161-360 1.46e-07

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 51.91  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 161 VVIVFHNEAwSTLLRTVYSVINRS-PHYLLsEVILVDDASERDFLKLtLENYVKTLEVPVKIIRMEER--SGLIRARLRG 237
Cdd:cd04192    1 VVIAARNEA-ENLPRLLQSLSALDyPKEKF-EVILVDDHSTDGTVQI-LEFAAAKPNFQLKILNNSRVsiSGKKNALTTA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 238 AAASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTF-------EYMAGSDMTYGGFNWKLnfrwyp 310
Cdd:cd04192   78 IKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFKGKSLlakfqrlDWLSLLGLIAGSFGLGK------ 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568913802 311 vpqremdrrkgdrtlpvrtPTMAGGL-FSIDRNYFEEIGTYDAGMDIWGGE 360
Cdd:cd04192  152 -------------------PFMCNGAnMAYRKEAFFEVGGFEGNDHIASGD 183
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 161-354 4.52e-07

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: 49.92  E-value: 4.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 161 VVIVFHNEAwSTLLRTVYSVinRSPHYLLSEVILVDDASERDFLKLtLENYVKTLEVPVKIIRMEERSGLIRARLRGAAA 240
Cdd:cd06423    1 IIVPAYNEE-AVIERTIESL--LALDYPKLEVIVVDDGSTDDTLEI-LEELAALYIRRVLVVRDKENGGKAGALNAGLRH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 241 SKGQVITFLDAHCECTLGWLEPLLARIKEDRKTV-VCPIIDVISDD--------TFEYMagsdmtyggfnwklnfRWYPV 311
Cdd:cd06423   77 AKGDIVVVLDADTILEPDALKRLVVPFFADPKVGaVQGRVRVRNGSenlltrlqAIEYL----------------SIFRL 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 568913802 312 PQREMDRRKGdrtlpvrTPTMAGGLFSIDRNYFEEIGTYDAGM 354
Cdd:cd06423  141 GRRAQSALGG-------VLVLSGAFGAFRREALREVGGWDEDT 176
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 161-279 2.03e-06

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: 47.55  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 161 VVIVFHNeAWSTLLRTVYSVINRSPHYLlsEVILVDDASERDflkltLENYVKTLEVPVKIIRMEERSGLIRARLRGAAA 240
Cdd:cd04186    1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVDNASTDG-----SVELLRELFPEVRLIRNGENLGFGAGNNQGIRE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568913802 241 SKGQVITFLDAHCECTLGWLEPLLARIKEDRKT-VVCPII 279
Cdd:cd04186   73 AKGDYVLLLNPDTVVEPGALLELLDAAEQDPDVgIVGPKV 112
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 157-250 4.68e-06

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: 47.20  E-value: 4.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 157 PNTSVVIVFHNEAWSTLLRTVYSVINRS-PHYllsEVILVDDASERDFLKLTLENYVKTlEVPVKIIRMEERSGLIRARL 235
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAQTyPNW---ELCIADDASTDPEVKRVLKKYAAQ-DPRIKVVFREENGGISAATN 76

                         90
                 ....*....|....*
gi 568913802 236 RGAAASKGQVITFLD 250
Cdd:cd04184   77 SALELATGEFVALLD 91
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 161-251 3.00e-05

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: 44.49  E-value: 3.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 161 VVIVFHNEAwSTLLRTVYSVINRSPHYLLSEVILVDDASeRDflkltlenyvKTLEV---------PVKIIRMEERSGLI 231
Cdd:cd04179    1 VVIPAYNEE-ENIPELVERLLAVLEEGYDYEIIVVDDGS-TD----------GTAEIarelaarvpRVRVIRLSRNFGKG 68

                         90       100
                 ....*....|....*....|
gi 568913802 232 RARLRGAAASKGQVITFLDA 251
Cdd:cd04179   69 AAVRAGFKAARGDIVVTMDA 88
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 161-276 2.70e-04

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 42.17  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 161 VVIVFHNEAwSTLLRTV-----YSVINRSPHYllsEVILVDDASERDFLKLtLENYVKTLEVPVKIIRMEERSGLIRARL 235
Cdd:cd04188    1 VVIPAYNEE-KRLPPTLeeaveYLEERPSFSY---EIIVVDDGSKDGTAEV-ARKLARKNPALIRVLTLPKNRGKGGAVR 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568913802 236 RGAAASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVC 276
Cdd:cd04188   76 AGMLAARGDYILFADADLATPFEELEKLEEALKTSGYDIAI 116
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 330-380 4.62e-04

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


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 38.75  E-value: 4.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 568913802  330 PTMAGGLFSIDRNYFEEIGTYDAGMDIWGGENLEMSFRIWQCGGSLEIVTC 380
Cdd:pfam02709  17 KTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG 67
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 191-368 8.64e-04

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: 41.11  E-value: 8.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802  191 EVILVDDASERDFLKlTLENyVKTLEVPVKIIRMEERS-GLIRARLRGAAASKGQVITFLDAHCECTLGWLEPLL--ARI 267
Cdd:pfam10111  31 ELIIINDGSTDKTLE-EVSS-IKDHNLQVYYPNAPDTTySLAASRNRGTSHAIGEYISFIDGDCLWSPDKFEKQLkiATS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802  268 KEDRKT----VVCPIIDVISDDTFEYMAGSDMTyggfnWKLNFRwypvpqremdrrkgdRTLPVRTPTMA------GGLF 337
Cdd:pfam10111 109 LALQENiqaaVVLPVTDLNDESSNFLRRGGDLT-----ASGDVL---------------RDLLVFYSPLAiffapnSSNA 168

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568913802  338 SIDRNYFEEIGTYDAGMDIWGGENLEMSFRI 368
Cdd:pfam10111 169 LINRQAFIEVGGFDESFRGHGAEDFDIFLRL 199
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 153-251 3.60e-03

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: 39.10  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568913802 153 PDELPNTSVVIVFHNEAwstllrtvySVINRSPHYLLS--------EVILVDDASERDflklTLENYVKTLEVPVKIIRM 224
Cdd:cd06439   25 PAYLPTVTIIIPAYNEE---------AVIEAKLENLLAldyprdrlEIIVVSDGSTDG----TAEIAREYADKGVKLLRF 91

                         90       100
                 ....*....|....*....|....*..
gi 568913802 225 EERSGLIRARLRGAAASKGQVITFLDA 251
Cdd:cd06439   92 PERRGKAAALNRALALATGEIVVFTDA 118
 
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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