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Conserved domains on  [gi|254553456|ref|NP_080725|]
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inactive polypeptide N-acetylgalactosaminyltransferase-like protein 5 [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
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 ...
118-414 3.79e-155

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: 440.49  E-value: 3.79e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 118 SIIICFYNEEFNTLLRAVSSVVNLSPQHLLEEIILVDDMSEFDDLKDKLDYYLEIFRGKVKLIRNKKREGLIRSKMIGAS 197
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 198 RASGDILVFLDSHCEVNRVWLEPLLHAIAKDHKMVVCPIIDVINELTLDYMAAP-IVRGAFDWNLNLRWDNVFAYELDgP 276
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEERR-R 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 277 EGPSTPIRSPAMTGGIFAINRHYFNELGQYDNGMDICGGENVELSLRIWMCGGQLFILPCSRVG---------YNSKALS 347
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGhifrrkrkpYTFPGGS 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254553456 348 qhrranqSALSRNLLRVVHVWLDEYKGNFFLQRPSLTYVSCGNISERVELRKRLGCKSFQWYLDNIF 414
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 ...
118-414 3.79e-155

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: 440.49  E-value: 3.79e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 118 SIIICFYNEEFNTLLRAVSSVVNLSPQHLLEEIILVDDMSEFDDLKDKLDYYLEIFRGKVKLIRNKKREGLIRSKMIGAS 197
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 198 RASGDILVFLDSHCEVNRVWLEPLLHAIAKDHKMVVCPIIDVINELTLDYMAAP-IVRGAFDWNLNLRWDNVFAYELDgP 276
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEERR-R 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 277 EGPSTPIRSPAMTGGIFAINRHYFNELGQYDNGMDICGGENVELSLRIWMCGGQLFILPCSRVG---------YNSKALS 347
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGhifrrkrkpYTFPGGS 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254553456 348 qhrranqSALSRNLLRVVHVWLDEYKGNFFLQRPSLTYVSCGNISERVELRKRLGCKSFQWYLDNIF 414
Cdd:cd02510  240 -------GTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
118-298 6.40e-30

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 113.64  E-value: 6.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456  118 SIIICFYNEEfNTLLRAVSSVVNLSPQHLleEIILVDDMSEfDDLKDKLDYYLEIFrGKVKLIRNKKREGLIRSKMIGAS 197
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGST-DGTVEIAEEYAKKD-PRVRVIRLPENRGKAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456  198 RASGDILVFLDSHCEVNRVWLEPLLHAIAKDHKMVVCPIIDVINELTLDYMaapivrgafdWNLNLRWDNVFAYELDGPE 277
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR----------RASRITLSRLPFFLGLRLL 145
                         170       180
                  ....*....|....*....|.
gi 254553456  278 GPSTPIRSPAMTGGIFAINRH 298
Cdd:pfam00535 146 GLNLPFLIGGFALYRREALEE 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
104-386 2.10e-15

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: 76.32  E-value: 2.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 104 ICQQKHYPFNLPTASIIICFYNEEfNTLLRAVSSVVNLSPQHLLEEIILVDDMSEfDDLKDKLDYYLEIFRgKVKLIRNK 183
Cdd:COG1215   18 LARRRRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIARELAAEYP-RVRVIERP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 184 KREGLIRSKMIGASRASGDILVFLDSHCEVNRVWLepllhaiakdhkmvvcpiidvinELTLDYMAAPIVrgafdwnlnl 263
Cdd:COG1215   95 ENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWL-----------------------RRLVAAFADPGV---------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 264 rwdnvfayeldgpegpstpirspAMTGGIFAINRHYFNELGQYDngmDICGGENVELSLRIWMCGGqlfilpcsRVGYNS 343
Cdd:COG1215  142 -----------------------GASGANLAFRREALEEVGGFD---EDTLGEDLDLSLRLLRAGY--------RIVYVP 187
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 254553456 344 KALSQHR-RANQSALSRNLLRVVHVWLDEYKGNFFLQRPSLTYV 386
Cdd:COG1215  188 DAVVYEEaPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLL 231
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
118-336 4.48e-04

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 41.34  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456  118 SIIICFYNEEFN--TLLRAvssvvnLSPQHLLEEIILVDDMSEfddlkdklDYYLEIFR-GKVKLIRNKKreGliRSK-M 193
Cdd:TIGR04283   2 SIIIPVLNEAATlpELLAD------LQALRGDAEVIVVDGGST--------DGTVEIARsLGAKVIHSPK--G--RARqM 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456  194 I-GASRASGDILVFLDSHCEVNRVWLEPLLHAIAKDHkmvvcpiidvineltldymaapIVRGAFDwnlnlrwdnvfaYE 272
Cdd:TIGR04283  64 NaGAALAKGDILLFLHADTRLPKDFLEAIRRALAKPG----------------------YVAGAFD------------LR 109
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254553456  273 LDGPeGPSTPIRSPAM----------TG--GIFaINRHYFNELGQYDngmDICGGENVELSLRIwMCGGQLFILPC 336
Cdd:TIGR04283 110 FDGP-GLLLRLIEWGVnlrsrltgipYGdqGLF-VRRSLFEQIGGFP---DIPLMEDIELSRRL-RRLGRLAILPA 179
 
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 ...
118-414 3.79e-155

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: 440.49  E-value: 3.79e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 118 SIIICFYNEEFNTLLRAVSSVVNLSPQHLLEEIILVDDMSEFDDLKDKLDYYLEIFRGKVKLIRNKKREGLIRSKMIGAS 197
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 198 RASGDILVFLDSHCEVNRVWLEPLLHAIAKDHKMVVCPIIDVINELTLDYMAAP-IVRGAFDWNLNLRWDNVFAYELDgP 276
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSgDARGGFDWSLHFKWLPLPEEERR-R 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 277 EGPSTPIRSPAMTGGIFAINRHYFNELGQYDNGMDICGGENVELSLRIWMCGGQLFILPCSRVG---------YNSKALS 347
Cdd:cd02510  160 ESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGhifrrkrkpYTFPGGS 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254553456 348 qhrranqSALSRNLLRVVHVWLDEYKGNFFLQRPSLTYVSCGNISERVELRKRLGCKSFQWYLDNIF 414
Cdd:cd02510  240 -------GTVLRNYKRVAEVWMDEYKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
118-298 6.40e-30

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 113.64  E-value: 6.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456  118 SIIICFYNEEfNTLLRAVSSVVNLSPQHLleEIILVDDMSEfDDLKDKLDYYLEIFrGKVKLIRNKKREGLIRSKMIGAS 197
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGST-DGTVEIAEEYAKKD-PRVRVIRLPENRGKAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456  198 RASGDILVFLDSHCEVNRVWLEPLLHAIAKDHKMVVCPIIDVINELTLDYMaapivrgafdWNLNLRWDNVFAYELDGPE 277
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYR----------RASRITLSRLPFFLGLRLL 145
                         170       180
                  ....*....|....*....|.
gi 254553456  278 GPSTPIRSPAMTGGIFAINRH 298
Cdd:pfam00535 146 GLNLPFLIGGFALYRREALEE 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
104-386 2.10e-15

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: 76.32  E-value: 2.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 104 ICQQKHYPFNLPTASIIICFYNEEfNTLLRAVSSVVNLSPQHLLEEIILVDDMSEfDDLKDKLDYYLEIFRgKVKLIRNK 183
Cdd:COG1215   18 LARRRRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIARELAAEYP-RVRVIERP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 184 KREGLIRSKMIGASRASGDILVFLDSHCEVNRVWLepllhaiakdhkmvvcpiidvinELTLDYMAAPIVrgafdwnlnl 263
Cdd:COG1215   95 ENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWL-----------------------RRLVAAFADPGV---------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 264 rwdnvfayeldgpegpstpirspAMTGGIFAINRHYFNELGQYDngmDICGGENVELSLRIWMCGGqlfilpcsRVGYNS 343
Cdd:COG1215  142 -----------------------GASGANLAFRREALEEVGGFD---EDTLGEDLDLSLRLLRAGY--------RIVYVP 187
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 254553456 344 KALSQHR-RANQSALSRNLLRVVHVWLDEYKGNFFLQRPSLTYV 386
Cdd:COG1215  188 DAVVYEEaPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLL 231
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
115-365 4.65e-15

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 73.58  E-value: 4.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 115 PTASIIICFYNEEfNTLLRAVSSVVNLSPQHLleEIILVDDMSEfDDLKDKLDYYLEIFrGKVKLIRNKKREGLIRSKMI 194
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGST-DGTAEILRELAAKD-PRIRVIRLERNRGKGAARNA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 195 GASRASGDILVFLDSHCEVNRVWLEPLLHAIAKDHKMVVCpiidvineltldymaapivrGAFDWNLNLRWDNVFAYELD 274
Cdd:COG0463   77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY--------------------GSRLIREGESDLRRLGSRLF 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 275 GPEGPSTPIrsPAMTGGIFAINRHYFNELGqYDNGMdicgGENVELsLRIWmcggqlfilpcsRVGYNSKALSQHRRANQ 354
Cdd:COG0463  137 NLVRLLTNL--PDSTSGFRLFRREVLEELG-FDEGF----LEDTEL-LRAL------------RHGFRIAEVPVRYRAGE 196
                        250
                 ....*....|..
gi 254553456 355 SALS-RNLLRVV 365
Cdd:COG0463  197 SKLNlRDLLRLL 208
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
119-271 5.37e-15

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: 72.15  E-value: 5.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 119 IIICFYNEEfNTLLRAVSSVVNLSPQHLleEIILVDDMSEfDDLKDKLDYYLEIFRgKVKLIRNKKREGLIRSKMIGASR 198
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGST-DGTLEILEEYAKKDP-RVIRVINEENQGLAAARNAGLKA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 199 ASGDILVFLDSHCEVNRVWLEPLLHAIAKDHK--MVVCPII-----DVINELTLDYMAAPIVRGAFDWNLNLRWDNVFAY 271
Cdd:cd00761   76 ARGEYILFLDADDLLLPDWLERLVAELLADPEadAVGGPGNllfrrELLEEIGGFDEALLSGEEDDDFLLRLLRGGKVAF 155
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
115-370 1.40e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 71.95  E-value: 1.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 115 PTASIIICFYNEEfNTLLRAVSSVVNLSPQHLleEIILVDDMSEfDDLKDKLDyylEIFRGKVKLIRNKKREGLIRSKMI 194
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGST-DGTAELLA---ALAFPRVRVIRNPENLGFAAARNL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 195 GASRASGDILVFLDSHCEVNRVWLEPLLHAiakdhkmvvcpiidvineltldymaapivrgafdwnlnlrwdnvfayeld 274
Cdd:COG1216   76 GLRAAGGDYLLFLDDDTVVEPDWLERLLAA-------------------------------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 275 gpegpstpirspamtgGIFAINRHYFNELGQYDNGMDIcGGENVELSLRIWMCGGQLFILPCSRVgYNSKALSQHRRANQ 354
Cdd:COG1216  106 ----------------ACLLIRREVFEEVGGFDERFFL-YGEDVDLCLRLRKAGYRIVYVPDAVV-YHLGGASSGPLLRA 167
                        250
                 ....*....|....*.
gi 254553456 355 SALSRNLLRVVHVWLD 370
Cdd:COG1216  168 YYLGRNRLLFLRKHGP 183
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
116-360 2.61e-13

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: 69.18  E-value: 2.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 116 TASIIICFYNEEfNTLLRAVSSVVNLSPQHLLEEIILVDDMSEfDDLKDKLDYYLEIFrGKVKLIRNKKReglIRSKM-- 193
Cdd:cd02525    1 FVSIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGST-DGTREIVQEYAAKD-PRIRLIDNPKR---IQSAGln 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 194 IGASRASGDILVFLDSHCEVNRVWLEPLLHAIAK-DHKMVVCPIIdvineltldymaaPIVRGAFDWNLNLRWDNVF--- 269
Cdd:cd02525   75 IGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRtGADNVGGPME-------------TIGESKFQKAIAVAQSSPLgsg 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 270 --AYE-LDGPEGPSTPIRSPAMtggifaiNRHYFNELGQYDNGMDICggENVELSLRIWMCGGQLFILPCSRVGYnskal 346
Cdd:cd02525  142 gsAYRgGAVKIGYVDTVHHGAY-------RREVFEKVGGFDESLVRN--EDAELNYRLRKAGYKIWLSPDIRVYY----- 207
                        250
                 ....*....|....
gi 254553456 347 sqHRRANQSALSRN 360
Cdd:cd02525  208 --YPRSTLKKLARQ 219
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
119-237 2.20e-12

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: 66.16  E-value: 2.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 119 IIICFYNEEFNtLLRAVSSVVNLS-PQHLLEeIILVDDMSEfDDLKDKLDYYLEIFRGKVKLIRNKKREGLIRSKMI--G 195
Cdd:cd04192    1 VVIAARNEAEN-LPRLLQSLSALDyPKEKFE-VILVDDHST-DGTVQILEFAAAKPNFQLKILNNSRVSISGKKNALttA 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 254553456 196 ASRASGDILVFLDSHCEVNRVWLEPLLHAIAKDH-KMVVCPII 237
Cdd:cd04192   78 IKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQiGLVAGPVI 120
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
119-310 8.10e-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: 51.84  E-value: 8.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 119 IIICFYNEEfNTLLRAVSSVVNLspQHLLEEIILVDDMSEfDDLKDKLDYYLEIFRGKVKLIRNK----KREGLIRskmi 194
Cdd:cd06423    1 IIVPAYNEE-AVIERTIESLLAL--DYPKLEVIVVDDGST-DDTLEILEELAALYIRRVLVVRDKenggKAGALNA---- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 195 GASRASGDILVFLDSHCEVNRVWLEPLLHAIAKDHKMV-VCPIIDVINE--------LTLDYMaapivrGAFDWNLNLRW 265
Cdd:cd06423   73 GLRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGaVQGRVRVRNGsenlltrlQAIEYL------SIFRLGRRAQS 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 254553456 266 dnvfayELDGPegpstpirsPAMTGGIFAINRHYFNELGQYDNGM 310
Cdd:cd06423  147 ------ALGGV---------LVLSGAFGAFRREALREVGGWDEDT 176
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
114-208 1.28e-07

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 52.58  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 114 LPTASIIICFYNEEfNTLLRAVSSVVNLS-PQHLLeEIILVDDMSEfDDLKDKLDYYLEifrGKVKLIRNKKREGLIRSK 192
Cdd:cd06439   28 LPTVTIIIPAYNEE-AVIEAKLENLLALDyPRDRL-EIIVVSDGST-DGTAEIAREYAD---KGVKLLRFPERRGKAAAL 101
                         90
                 ....*....|....*.
gi 254553456 193 MIGASRASGDILVFLD 208
Cdd:cd06439  102 NRALALATGEIVVFTD 117
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
119-339 1.57e-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: 44.86  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 119 IIICFYNEEfNTLLRAVSSVVNLSPQHLleEIILVDDMSEfddlkdklDYYLEIFR---GKVKLIRNKKREGLIRSKMIG 195
Cdd:cd04186    1 IIIVNYNSL-EYLKACLDSLLAQTYPDF--EVIVVDNAST--------DGSVELLRelfPEVRLIRNGENLGFGAGNNQG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 196 ASRASGDILVFLDSHCEVNRVWLEPLLHAIAKDhkmvvcpiidvineltLDY-MAAPIVRGAFdwnlnlrwdnvfayeld 274
Cdd:cd04186   70 IREAKGDYVLLLNPDTVVEPGALLELLDAAEQD----------------PDVgIVGPKVSGAF----------------- 116
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254553456 275 gpegpstpirspamtggiFAINRHYFNELGqydnGMD---ICGGENVELSLRIWMCGGQLFILPCSRV 339
Cdd:cd04186  117 ------------------LLVRREVFEEVG----GFDedfFLYYEDVDLCLRARLAGYRVLYVPQAVI 162
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
118-324 1.68e-05

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: 46.12  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456  118 SIIICFYNEEFNTLLRavSSVVNLSPQHLLE-EIILVDDMSEFD---DLKDKLDYYLEIFRGKVklirNKKREGLIRSKM 193
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQ--ERILNQTFQYDPEfELIIINDGSTDKtleEVSSIKDHNLQVYYPNA----PDTTYSLAASRN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456  194 IGASRASGDILVFLDSHCEVNRVWLEPLLhAIAKDHKM-------VVCPIIDVINEltldymAAPIVRGAFDwnlnLRWD 266
Cdd:pfam10111  75 RGTSHAIGEYISFIDGDCLWSPDKFEKQL-KIATSLALqeniqaaVVLPVTDLNDE------SSNFLRRGGD----LTAS 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 254553456  267 NVFAYELDGPEGPSTPIRSPamTGGIFAINRHYFNELGQYDNGMDICGGENVELSLRI 324
Cdd:pfam10111 144 GDVLRDLLVFYSPLAIFFAP--NSSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRL 199
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
119-209 2.47e-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: 44.87  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 119 IIICFYNEEfNTLLRAVSSVVNLSPQHLLEEIILVDDMSEfDDLKDKLDYYLEIFrGKVKLIRNKKREGLIRSKMIGASR 198
Cdd:cd04179    1 VVIPAYNEE-ENIPELVERLLAVLEEGYDYEIIVVDDGST-DGTAEIARELAARV-PRVRVIRLSRNFGKGAAVRAGFKA 77
                         90
                 ....*....|.
gi 254553456 199 ASGDILVFLDS 209
Cdd:cd04179   78 ARGDIVVTMDA 88
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
119-234 8.94e-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: 43.32  E-value: 8.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 119 IIICFYNEEfNTLLRAVSSVVNLSPQHLLE--EIILVDDMSEfDDLKDKLDYYLEIFRGKVKLIRNKKREGLIRSKMIGA 196
Cdd:cd04188    1 VVIPAYNEE-KRLPPTLEEAVEYLEERPSFsyEIIVVDDGSK-DGTAEVARKLARKNPALIRVLTLPKNRGKGGAVRAGM 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 254553456 197 SRASGDILVFLD-------SHcevnrvwLEPLLHAIAKDHKMVVC 234
Cdd:cd04188   79 LAARGDYILFADadlatpfEE-------LEKLEEALKTSGYDIAI 116
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
115-209 1.85e-04

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


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 42.19  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 115 PTASIIICFYNEEFNTLLRAVSSVVNLSPQHLleEIILVDDMSEFDDLKDKLDYYLEIFRgKVKLIRNKKREGLIRSKMI 194
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYAAQDP-RIKVVFREENGGISAATNS 77
                         90
                 ....*....|....*
gi 254553456 195 GASRASGDILVFLDS 209
Cdd:cd04184   78 ALELATGEFVALLDH 92
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
118-336 4.48e-04

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 41.34  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456  118 SIIICFYNEEFN--TLLRAvssvvnLSPQHLLEEIILVDDMSEfddlkdklDYYLEIFR-GKVKLIRNKKreGliRSK-M 193
Cdd:TIGR04283   2 SIIIPVLNEAATlpELLAD------LQALRGDAEVIVVDGGST--------DGTVEIARsLGAKVIHSPK--G--RARqM 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456  194 I-GASRASGDILVFLDSHCEVNRVWLEPLLHAIAKDHkmvvcpiidvineltldymaapIVRGAFDwnlnlrwdnvfaYE 272
Cdd:TIGR04283  64 NaGAALAKGDILLFLHADTRLPKDFLEAIRRALAKPG----------------------YVAGAFD------------LR 109
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254553456  273 LDGPeGPSTPIRSPAM----------TG--GIFaINRHYFNELGQYDngmDICGGENVELSLRIwMCGGQLFILPC 336
Cdd:TIGR04283 110 FDGP-GLLLRLIEWGVnlrsrltgipYGdqGLF-VRRSLFEQIGGFP---DIPLMEDIELSRRL-RRLGRLAILPA 179
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
119-209 7.13e-04

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: 40.15  E-value: 7.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 119 IIICFYNEEFN--TLLRAVSSVvnLSPQHLLEEIILVDDMSEfDDLKDKLDYYLEIFrGKVKLIRNKKREGLIRSKMIGA 196
Cdd:cd04187    1 IVVPVYNEEENlpELYERLKAV--LESLGYDYEIIFVDDGST-DRTLEILRELAARD-PRVKVIRLSRNFGQQAALLAGL 76
                         90
                 ....*....|...
gi 254553456 197 SRASGDILVFLDS 209
Cdd:cd04187   77 DHARGDAVITMDA 89
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
118-324 8.61e-04

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: 40.63  E-value: 8.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 118 SIIICFYNEEfNTLLRAVSSVVNLSPQHLleEIILVDDMSEfDDLkdkldyyLEIFRGK-VKLIRNKKreGliRSK-M-I 194
Cdd:cd02522    2 SIIIPTLNEA-ENLPRLLASLRRLNPLPL--EIIVVDGGST-DGT-------VAIARSAgVVVISSPK--G--RARqMnA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553456 195 GASRASGDILVFL--DShcevnrvWLEPllhaiakdhkmvvcPIIDVINELTLDYmaaPIVRGAFD-------------- 258
Cdd:cd02522   67 GAAAARGDWLLFLhaDT-------RLPP--------------DWDAAIIETLRAD---GAVAGAFRlrfddpgprlrlle 122
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254553456 259 --WNLNLRWdnvfayeldgpegPSTPirspamTG--GIFaINRHYFNELGQYDNG--MdicggENVELSLRI 324
Cdd:cd02522  123 lgANLRSRL-------------FGLP------YGdqGLF-IRRELFEELGGFPELplM-----EDVELVRRL 169
 
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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