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Conserved domains on  [gi|1907189560|ref|XP_036009969|]
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polypeptide N-acetylgalactosaminyltransferase-like 6 isoform X3 [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 ...
 237-532 7.11e-180

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: 508.28  E-value: 7.11e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 237 SIIIPFHNEGWTSLLRTIHSIINRTPESLIAEIILVDDFSDREHLKDKLED-YMARFSKVRIVRTKKREGLIRTRLLGAS 315
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEyYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 316 VARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVCPMIDVIDHNHFGYEAQAGDAmRGAFDWEMYYKRIPIPPELQRA 395
Cdd:cd02510    81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDA-RGGFDWSLHFKWLPLPEEERRR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 396 -DPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGEMFDVPCSRVGHIYR-KYVPYKVPSGT 473
Cdd:cd02510   160 eSPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 474 S-LARNLKRVAETWMDEFAEYIYQRRPEYRHLSTGDISAQKELRKRLKCKDFKWFMAAVA 532
Cdd:cd02510   240 GtVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 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 ...
 237-532 7.11e-180

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: 508.28  E-value: 7.11e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 237 SIIIPFHNEGWTSLLRTIHSIINRTPESLIAEIILVDDFSDREHLKDKLED-YMARFSKVRIVRTKKREGLIRTRLLGAS 315
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEyYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 316 VARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVCPMIDVIDHNHFGYEAQAGDAmRGAFDWEMYYKRIPIPPELQRA 395
Cdd:cd02510    81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDA-RGGFDWSLHFKWLPLPEEERRR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 396 -DPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGEMFDVPCSRVGHIYR-KYVPYKVPSGT 473
Cdd:cd02510   160 eSPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 474 S-LARNLKRVAETWMDEFAEYIYQRRPEYRHLSTGDISAQKELRKRLKCKDFKWFMAAVA 532
Cdd:cd02510   240 GtVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 237-420 4.85e-32

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: 121.35  E-value: 4.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 237 SIIIPFHNEgWTSLLRTIHSIINRTPESLiaEIILVDDFSdREHLKDKLEDYMARFSKVRIVRTKKREGLIRTRLLGASV 316
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 317 ARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVCPMIDVIDhnhfgyeaqagdamRGAFDWEMYYKRIPIPPELQRAD 396
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIF--------------GETGEYRRASRITLSRLPFFLGL 142

                         170       180
                  ....*....|....*....|....
gi 1907189560 397 PSDPFESPVMAGGLFAVDRKWFWE 420
Cdd:pfam00535 143 RLLGLNLPFLIGGFALYRREALEE 166
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 234-352 5.36e-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: 5.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 234 PNTSIIIPFHNEGwTSLLRTIHSIINRTPESLiaEIILVDDFSdREHLKDKLEDYMARFSKVRIVRTKKREGLIRTRLLG 313
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGS-TDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907189560 314 ASVARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVC 352
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY 116
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 234-326 9.89e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 50.81  E-value: 9.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 234 PNTSIIIPFHNEGwTSLLRTIHSIINRTPESLiaEIILVDDFSDrEHLKDKLEDYMARFSKVRIVrTKKREGLIRTRLLG 313
Cdd:PRK10073    6 PKLSIIIPLYNAG-KDFRAFMESLIAQTWTAL--EIIIVNDGST-DNSVEIAKHYAENYPHVRLL-HQANAGVSVARNTG 80

                          90
                  ....*....|...
gi 1907189560 314 ASVARGEVLTFLD 326
Cdd:PRK10073   81 LAVATGKYVAFPD 93
 
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 ...
 237-532 7.11e-180

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: 508.28  E-value: 7.11e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 237 SIIIPFHNEGWTSLLRTIHSIINRTPESLIAEIILVDDFSDREHLKDKLED-YMARFSKVRIVRTKKREGLIRTRLLGAS 315
Cdd:cd02510     1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEyYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 316 VARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVCPMIDVIDHNHFGYEAQAGDAmRGAFDWEMYYKRIPIPPELQRA 395
Cdd:cd02510    81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDA-RGGFDWSLHFKWLPLPEEERRR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 396 -DPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGEMFDVPCSRVGHIYR-KYVPYKVPSGT 473
Cdd:cd02510   160 eSPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRrKRKPYTFPGGS 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 474 S-LARNLKRVAETWMDEFAEYIYQRRPEYRHLSTGDISAQKELRKRLKCKDFKWFMAAVA 532
Cdd:cd02510   240 GtVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 237-420 4.85e-32

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: 121.35  E-value: 4.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 237 SIIIPFHNEgWTSLLRTIHSIINRTPESLiaEIILVDDFSdREHLKDKLEDYMARFSKVRIVRTKKREGLIRTRLLGASV 316
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 317 ARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVCPMIDVIDhnhfgyeaqagdamRGAFDWEMYYKRIPIPPELQRAD 396
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIF--------------GETGEYRRASRITLSRLPFFLGL 142

                         170       180
                  ....*....|....*....|....
gi 1907189560 397 PSDPFESPVMAGGLFAVDRKWFWE 420
Cdd:pfam00535 143 RLLGLNLPFLIGGFALYRREALEE 166
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 238-352 2.54e-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: 79.09  E-value: 2.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 238 IIIPFHNEGwTSLLRTIHSIINRTPESLiaEIILVDDFSDREHLkDKLEDYMARFSKVRIVRTKKREGLIRTRLLGASVA 317
Cdd:cd00761     1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTL-EILEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907189560 318 RGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVC 352
Cdd:cd00761    77 RGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 234-352 5.36e-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: 5.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 234 PNTSIIIPFHNEGwTSLLRTIHSIINRTPESLiaEIILVDDFSdREHLKDKLEDYMARFSKVRIVRTKKREGLIRTRLLG 313
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGS-TDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907189560 314 ASVARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVC 352
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY 116
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 231-504 3.02e-14

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: 73.62  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 231 ERLPNTSIIIPFHNEGwTSLLRTIHSIINRTPESLIAEIILVDDfSDREHLKDKLEDYMARFSKVRIVRTKKREGLIRTR 310
Cdd:COG1215    26 ADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDD-GSTDETAEIARELAAEYPRVRVIERPENGGKAAAL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 311 LLGASVARGEVLTFLDSHCEVNVNWLPPLLnqialnhktivcpmidvidhnhfgyeaqagdamrgafdwemyykripipp 390
Cdd:COG1215   104 NAGLKAARGDIVVFLDADTVLDPDWLRRLV-------------------------------------------------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 391 elqradpsDPFESP--VMAGGLFAVDRKWFWELGGYDPGLeiwGGEQYEISFKVWMCGGemfdvpcsRVGHIYRKYVPYK 468
Cdd:COG1215   134 --------AAFADPgvGASGANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGY--------RIVYVPDAVVYEE 194

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907189560 469 VPSG-TSLARNLKRVAETWMDEFAEYIYQRRPEYRHL 504
Cdd:COG1215   195 APETlRALFRQRRRWARGGLQLLLKHRPLLRPRRLLL 231
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
234-463 2.33e-13

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 68.87  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 234 PNTSIIIPFHNeGWTSLLRTIHSIINRTPESLiaEIILVDDFSDrEHLKDKLEDYmaRFSKVRIVRTKKREGLIRTRLLG 313
Cdd:COG1216     3 PKVSVVIPTYN-RPELLRRCLESLLAQTYPPF--EVIVVDNGST-DGTAELLAAL--AFPRVRVIRNPENLGFAAARNLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 314 ASVARGEVLTFLDSHCEVNVNWLPPLLnqialnhktivcpmidvidhnhfgyeAQAGdamrgafdwemyykripippelq 393
Cdd:COG1216    77 LRAAGGDYLLFLDDDTVVEPDWLERLL--------------------------AAAC----------------------- 107

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 394 radpsdpfespvmagglFAVDRKWFWELGGYDPGLEIWGGEqYEISFKVWMCGGEMFDVPCSRVGHIYRK 463
Cdd:COG1216   108 -----------------LLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGA 159
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 237-336 6.28e-10

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: 59.94  E-value: 6.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 237 SIIIPFHNEGwTSLLRTIHSIINRTPESLIAEIILVDDFS-DREhlKDKLEDYMARFSKVRIVRTKKR---EGlirtRLL 312
Cdd:cd02525     3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGStDGT--REIVQEYAAKDPRIRLIDNPKRiqsAG----LNI 75

                          90       100
                  ....*....|....*....|....
gi 1907189560 313 GASVARGEVLTFLDSHCEVNVNWL 336
Cdd:cd02525    76 GIRNSRGDIIIRVDAHAVYPKDYI 99
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 234-327 4.84e-09

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: 56.44  E-value: 4.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 234 PNTSIIIPFHNEGWTSLLRTIHSIINRTPESLiaEIILVDDFSDREHLKDKLEDYMARFSKVRIVRTKKREGLIRTRLLG 313
Cdd:cd04184     1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSA 78

                          90
                  ....*....|....
gi 1907189560 314 ASVARGEVLTFLDS 327
Cdd:cd04184    79 LELATGEFVALLDH 92
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 238-427 1.14e-08

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: 54.93  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 238 IIIPFHNEGwTSLLRTIHSIINRTPESLiaEIILVDDFSDREHLkDKLEDYMARFSKVRIVRTKKREG-----LIRtrll 312
Cdd:cd06423     1 IIVPAYNEE-AVIERTIESLLALDYPKL--EVIVVDDGSTDDTL-EILEELAALYIRRVLVVRDKENGgkagaLNA---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 313 GASVARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTI-VCPMIDVIDHN-HFGYEAQAGDAMRgafdWEMYYKRIpipp 390
Cdd:cd06423    73 GLRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGaVQGRVRVRNGSeNLLTRLQAIEYLS----IFRLGRRA---- 144

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907189560 391 elQRADpsdpFESPVMAGGLFAVDRKWFWELGGYDPG 427
Cdd:cd06423   145 --QSAL----GGVLVLSGAFGAFRREALREVGGWDED 175
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 238-352 3.55e-08

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: 53.35  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 238 IIIPFHNEGwtsllRTIHSIINRTPESLIA----EIILVDDFS-DREhlKDKLEDYMARFSKVRIVRTKKREGL---IRT 309
Cdd:cd04179     1 VVIPAYNEE-----ENIPELVERLLAVLEEgydyEIIVVDDGStDGT--AEIARELAARVPRVRVIRLSRNFGKgaaVRA 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907189560 310 rllGASVARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVC 352
Cdd:cd04179    74 ---GFKAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVI 113
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 238-434 6.97e-08

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: 53.45  E-value: 6.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 238 IIIPFHNEGwTSLLRTIHSIINRT-PESLIaEIILVDDFS-DR-------EHLKDKLEDYMARFSKVRIVRTKKregLIR 308
Cdd:cd04192     1 VVIAARNEA-ENLPRLLQSLSALDyPKEKF-EVILVDDHStDGtvqilefAAAKPNFQLKILNNSRVSISGKKN---ALT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 309 TrllGASVARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVCPMIDVIDHNHFGYEAQAGDAM------RGAFDWEMy 382
Cdd:cd04192    76 T---AIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFKGKSLLAKFQRLDWLsllgliAGSFGLGK- 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907189560 383 ykripippelqradpsdpfesPVMAGGL-FAVDRKWFWELGGYDPGLEIWGGE 434
Cdd:cd04192   152 ---------------------PFMCNGAnMAYRKEAFFEVGGFEGNDHIASGD 183
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 234-326 9.89e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 50.81  E-value: 9.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 234 PNTSIIIPFHNEGwTSLLRTIHSIINRTPESLiaEIILVDDFSDrEHLKDKLEDYMARFSKVRIVrTKKREGLIRTRLLG 313
Cdd:PRK10073    6 PKLSIIIPLYNAG-KDFRAFMESLIAQTWTAL--EIIIVNDGST-DNSVEIAKHYAENYPHVRLL-HQANAGVSVARNTG 80

                          90
                  ....*....|...
gi 1907189560 314 ASVARGEVLTFLD 326
Cdd:PRK10073   81 LAVATGKYVAFPD 93
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 238-327 1.78e-05

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: 45.55  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 238 IIIPFHNEGWT--SLLRTIHSIINRTPESLiaEIILVDDFS-DREHlkDKLEDYMARFSKVRIVRTKKREGLIRTRLLGA 314
Cdd:cd04187     1 IVVPVYNEEENlpELYERLKAVLESLGYDY--EIIFVDDGStDRTL--EILRELAARDPRVKVIRLSRNFGQQAALLAGL 76

                          90
                  ....*....|...
gi 1907189560 315 SVARGEVLTFLDS 327
Cdd:cd04187    77 DHARGDAVITMDA 89
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 400-461 2.63e-05

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


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 42.60  E-value: 2.63e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907189560 400 PFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGEMFDVPCsRVGHIY 461
Cdd:pfam02709  13 KLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG-DIGRYY 73
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 237-428 7.43e-05

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 44.10  E-value: 7.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 237 SIIIPFHNEGwTSLLRTIHSIinRTPESLIAEIILVDDFSDrehlkDKLEDyMARFSKVRIVRTKK-REGLIRTrllGAS 315
Cdd:cd02522     2 SIIIPTLNEA-ENLPRLLASL--RRLNPLPLEIIVVDGGST-----DGTVA-IARSAGVVVISSPKgRARQMNA---GAA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 316 VARGEVLTFL--DShcevnvnWLPPllnqialnhktivcPMIDVIDHNHFGYEAQAGdAMRGAFD---WemYYKRIPIPP 390
Cdd:cd02522    70 AARGDWLLFLhaDT-------RLPP--------------DWDAAIIETLRADGAVAG-AFRLRFDdpgP--RLRLLELGA 125

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1907189560 391 ELQRADPSDPFespvmaG--GLFaVDRKWFWELGGYDPGL 428
Cdd:cd02522   126 NLRSRLFGLPY------GdqGLF-IRRELFEELGGFPELP 158
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 238-345 9.23e-05

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: 44.06  E-value: 9.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 238 IIIPFHNEgwtSL-LRTIHSIINRTPESLIAEIILVDDFSdrehlKDK----LEDYMARFSKVRIVRTKKREGLIRTRLL 312
Cdd:cd06442     1 IIIPTYNE---REnIPELIERLDAALKGIDYEIIVVDDNS-----PDGtaeiVRELAKEYPRVRLIVRPGKRGLGSAYIE 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1907189560 313 GASVARGEVLTFLD---SHcevNVNWLPPLLNQIAL 345
Cdd:cd06442    73 GFKAARGDVIVVMDadlSH---PPEYIPELLEAQLE 105
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 238-459 9.50e-05

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: 42.93  E-value: 9.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 238 IIIPFHNeGWTSLLRTIHSIINRTPESLiaEIILVDDFS---DREHLKDkledymaRFSKVRIVRTKKREGLIRTRLLGA 314
Cdd:cd04186     1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVDNAStdgSVELLRE-------LFPEVRLIRNGENLGFGAGNNQGI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 315 SVARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKT-IVCPMIdvidhnhfgyeaqagdamrgafdwemyykripippelq 393
Cdd:cd04186    71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDPDVgIVGPKV-------------------------------------- 112

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907189560 394 radpsdpfespvmAGGLFAVDRKWFWELGGYDPGLEIWgGEQYEISFKVWMCGGEMFDVPCSRVGH 459
Cdd:cd04186   113 -------------SGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYH 164
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 238-352 9.72e-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: 9.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 238 IIIPFHNEGwTSLLRTIHSII---NRTPESlIAEIILVDDFSDREHLkDKLEDYMARF-SKVRIVRTKKREG---LIRTr 310
Cdd:cd04188     1 VVIPAYNEE-KRLPPTLEEAVeylEERPSF-SYEIIVVDDGSKDGTA-EVARKLARKNpALIRVLTLPKNRGkggAVRA- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907189560 311 llGASVARGEVLTFLDSHCEVNVNWLPPLLNQIALNHKTIVC 352
Cdd:cd04188    77 --GMLAARGDYILFADADLATPFEELEKLEEALKTSGYDIAI 116
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 236-343 4.76e-03

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: 38.77  E-value: 4.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907189560 236 TSIIIPFHNEGWTSLLRTIHSIINRTPesliAEIILVDDfSDREHLKDKLEDyMARFSKVRIVRTK---KREGLIRtrll 312
Cdd:cd06434     2 VTVIIPVYDEDPDVFRECLRSILRQKP----LEIIVVTD-GDDEPYLSILSQ-TVKYGGIFVITVPhpgKRRALAE---- 71

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907189560 313 GASVARGEVLTFLDSHcevnVNWLPPLLNQI 343
Cdd:cd06434    72 GIRHVTTDIVVLLDSD----TVWPPNALPEM 98
 
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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