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Conserved domains on  [gi|759065118|ref|XP_011341982|]
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N-acetylgalactosaminyltransferase 7 isoform X2 [Ooceraea biroi]

Protein Classification

polypeptide N-acetylgalactosaminyltransferase( domain architecture ID 11551826)

polypeptide N-acetylgalactosaminyltransferase catalyzes 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
EC:  2.4.1.41
Gene Ontology:  GO:0004653|GO:0030246|GO:0046872
PubMed:  12634319|12691742|9445404|8844840
SCOP:  3000077|3000678

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 ...
 150-457 1.61e-172

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: 490.95  E-value: 1.61e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 150 SVIIVFHNEGWSVLLRTIHSVIDRTPSKFLEEILLVDDFSDKENLKGDLDSYIEQWGGKVRLLRNYERQGLIRTRSRGAR 229
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 230 DAKGEVIVFLDAHCEVNVNWLPPLLAPIAENRNVMTVPVIDGIDHKNFEYRPvyQEGHLyRGIFEWGMLYKENELPRREa 309
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRG--SSGDA-RGGFDWSLHFKWLPLPEEE- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 310 KTRTHDSMPYRSPTHAGGLFAINREYFLSLGGYDEGLLVWGGENFELSFKIWQCGGSILWVPCSHVGHVYRGFM-PYTFG 388
Cdd:cd02510  157 RRRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKRkPYTFP 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759065118 389 KLAQQkkgplITINYKRVIETWFDEkYKEFFYTREPLARLLDHGDITEQLLFKERKRCKSFQWYMDNVA 457
Cdd:cd02510  237 GGSGT-----VLRNYKRVAEVWMDE-YKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 469-589 2.31e-47

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


:

Pssm-ID: 467315 [Multi-domain]  Cd Length: 124  Bit Score: 161.69  E-value: 2.31e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 469 PNIHWGELRNVATGSCLDTMGHAPPSMMATSHCHGFGNNQLIRLNAKGQLGIGERCVEADGQG--IKYAFCRlGTVDGPW 546
Cdd:cd23437    1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGgkVKLRKCN-LGETGKW 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 759065118 547 QYDEKTKTLLHRVHKKCMALHPQIQQLSLMPCDMNNAYHQWSF 589
Cdd:cd23437   80 EYDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEF 122
 
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 ...
 150-457 1.61e-172

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: 490.95  E-value: 1.61e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 150 SVIIVFHNEGWSVLLRTIHSVIDRTPSKFLEEILLVDDFSDKENLKGDLDSYIEQWGGKVRLLRNYERQGLIRTRSRGAR 229
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 230 DAKGEVIVFLDAHCEVNVNWLPPLLAPIAENRNVMTVPVIDGIDHKNFEYRPvyQEGHLyRGIFEWGMLYKENELPRREa 309
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRG--SSGDA-RGGFDWSLHFKWLPLPEEE- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 310 KTRTHDSMPYRSPTHAGGLFAINREYFLSLGGYDEGLLVWGGENFELSFKIWQCGGSILWVPCSHVGHVYRGFM-PYTFG 388
Cdd:cd02510  157 RRRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKRkPYTFP 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759065118 389 KLAQQkkgplITINYKRVIETWFDEkYKEFFYTREPLARLLDHGDITEQLLFKERKRCKSFQWYMDNVA 457
Cdd:cd02510  237 GGSGT-----VLRNYKRVAEVWMDE-YKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 469-589 2.31e-47

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467315 [Multi-domain]  Cd Length: 124  Bit Score: 161.69  E-value: 2.31e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 469 PNIHWGELRNVATGSCLDTMGHAPPSMMATSHCHGFGNNQLIRLNAKGQLGIGERCVEADGQG--IKYAFCRlGTVDGPW 546
Cdd:cd23437    1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGgkVKLRKCN-LGETGKW 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 759065118 547 QYDEKTKTLLHRVHKKCMALHPQIQQLSLMPCDMNNAYHQWSF 589
Cdd:cd23437   80 EYDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEF 122
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 150-334 5.80e-31

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


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 118.65  E-value: 5.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118  150 SVIIVFHNEgWSVLLRTIHSVIDRTPSKFleEILLVDDFSdKENLKGDLDSYIEQwGGKVRLLRNYERQGLIRTRSRGAR 229
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKK-DPRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118  230 DAKGEVIVFLDAHCEVNVNWLPPLLAPIAENRNVMTVPVIDGIDHKNFEYRPVYQeghlyrgifewgmlYKENELPRREA 309
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASR--------------ITLSRLPFFLG 141

                         170       180
                  ....*....|....*....|....*
gi 759065118  310 KTRTHDSMPYRSPTHAGGLFAINRE 334
Cdd:pfam00535 142 LRLLGLNLPFLIGGFALYRREALEE 166
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
147-429 2.82e-21

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 91.98  E-value: 2.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 147 PRTSVIIVFHNeGWSVLLRTIHSVIDRTPSKFleEILLVDDFSDKenlkGDLDSYIEQWGGKVRLLRNYERQGLIRTRSR 226
Cdd:COG1216    3 PKVSVVIPTYN-RPELLRRCLESLLAQTYPPF--EVIVVDNGSTD----GTAELLAALAFPRVRVIRNPENLGFAAARNL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 227 GARDAKGEVIVFLDAHCEVNVNWLPPLLApiaenrnvmtvpvidgidhknfeyrpvyqeghlyrgifEWGMLYkenelpR 306
Cdd:COG1216   76 GLRAAGGDYLLFLDDDTVVEPDWLERLLA--------------------------------------AACLLI------R 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 307 REAktrthdsmpyrspthagglfainreyFLSLGGYDEGLLVWGGEnFELSFKIWQCGGSILWVPCSHVGHVYRGfmpyT 386
Cdd:COG1216  112 REV--------------------------FEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGA----S 160

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 759065118 387 FGKLAQQKkgpLITINYKRVIETWFDEKYKEFFYTREPLARLL 429
Cdd:COG1216  161 SGPLLRAY---YLGRNRLLFLRKHGPRPLLRLALLRGLRLRLR 200
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
473-587 7.83e-20

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 85.66  E-value: 7.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118  473 WGELRNVATGSCLDTMGHAPP-SMMATSHCHGFGNNQLIRLNAKGQL--GIGERCVE----ADGQGIKYAFCRLGTVDGP 545
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGGSSAgGPVGLYPCHGSNGNQLWTLTGDGTIrsVASDLCLDvgstADGAKVVLWPCHPGNGNQR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 759065118  546 WQYDEKTKTLLHRVHKKCMALHPQIQ---QLSLMPCDMNNAYHQW 587
Cdd:pfam00652  82 WRYDEDGTQIRNPQSGKCLDVSGAGTsngKVILWTCDSGNPNQQW 126
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 478-589 6.19e-07

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 48.28  E-value: 6.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118   478 NVATGSCLDTMGHapPSMMATSHCHGFGNNQLIRLNAKGQL--GIGERCVEADGQGIKYAF---CRLGTVDGPWQYdEKT 552
Cdd:smart00458   3 SGNTGKCLDVNGN--KNPVGLFDCHGTGGNQLWKLTSDGAIriKDTDLCLTANGNTGSTVTlysCDGTNDNQYWEV-NKD 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 759065118   553 KTLLHRVHKKCMALH--PQIQQLSLMPCDmNNAYHQWSF 589
Cdd:smart00458  80 GTIRNPDSGKCLDVKdgNTGTKVILWTCS-GNPNQKWIF 117
 
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 ...
 150-457 1.61e-172

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: 490.95  E-value: 1.61e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 150 SVIIVFHNEGWSVLLRTIHSVIDRTPSKFLEEILLVDDFSDKENLKGDLDSYIEQWGGKVRLLRNYERQGLIRTRSRGAR 229
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 230 DAKGEVIVFLDAHCEVNVNWLPPLLAPIAENRNVMTVPVIDGIDHKNFEYRPvyQEGHLyRGIFEWGMLYKENELPRREa 309
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRG--SSGDA-RGGFDWSLHFKWLPLPEEE- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 310 KTRTHDSMPYRSPTHAGGLFAINREYFLSLGGYDEGLLVWGGENFELSFKIWQCGGSILWVPCSHVGHVYRGFM-PYTFG 388
Cdd:cd02510  157 RRRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRKRkPYTFP 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 759065118 389 KLAQQkkgplITINYKRVIETWFDEkYKEFFYTREPLARLLDHGDITEQLLFKERKRCKSFQWYMDNVA 457
Cdd:cd02510  237 GGSGT-----VLRNYKRVAEVWMDE-YKEYFYKARPELRNIDYGDLSERKALRERLKCKSFKWYLENVY 299
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 469-589 2.31e-47

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 7 (GALNT7) and similar proteins; GALNT7 (EC 2.4.1.41), also called polypeptide GalNAc transferase 7, GalNAc-T7, pp-GaNTase 7, protein-UDP acetylgalactosaminyltransferase 7, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7, acts as glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Its appropriate peptide substrate remains unidentified. GALNT7 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467315 [Multi-domain]  Cd Length: 124  Bit Score: 161.69  E-value: 2.31e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 469 PNIHWGELRNVATGSCLDTMGHAPPSMMATSHCHGFGNNQLIRLNAKGQLGIGERCVEADGQG--IKYAFCRlGTVDGPW 546
Cdd:cd23437    1 KNLAWGEIRNLGTGLCLDTMGHQNGGPVGLYPCHGMGGNQLFRLNEAGQLAVGEQCLTASGSGgkVKLRKCN-LGETGKW 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 759065118 547 QYDEKTKTLLHRVHKKCMALHPQIQQLSLMPCDMNNAYHQWSF 589
Cdd:cd23437   80 EYDEATGQIRHKGTGKCLDLNEGTNKLILQPCDSSSPSQKWEF 122
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 150-334 5.80e-31

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


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 118.65  E-value: 5.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118  150 SVIIVFHNEgWSVLLRTIHSVIDRTPSKFleEILLVDDFSdKENLKGDLDSYIEQwGGKVRLLRNYERQGLIRTRSRGAR 229
Cdd:pfam00535   1 SVIIPTYNE-EKYLLETLESLLNQTYPNF--EIIVVDDGS-TDGTVEIAEEYAKK-DPRVRVIRLPENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118  230 DAKGEVIVFLDAHCEVNVNWLPPLLAPIAENRNVMTVPVIDGIDHKNFEYRPVYQeghlyrgifewgmlYKENELPRREA 309
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASR--------------ITLSRLPFFLG 141

                         170       180
                  ....*....|....*....|....*
gi 759065118  310 KTRTHDSMPYRSPTHAGGLFAINRE 334
Cdd:pfam00535 142 LRLLGLNLPFLIGGFALYRREALEE 166
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 469-589 4.53e-22

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 9 (Pgant9) and similar proteins; The subfamily includes Pgant9 (also called pp-GaNTase 9, protein-UDP acetylgalactosaminyltransferase 9, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9), Pgant4 (also called pp-GaNTase 4, N-acetylgalactosaminyltransferase 4, protein-UDP acetylgalactosaminyltransferase 4, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4) and Pgant6 (also called pp-GaNTase 6, N-acetylgalactosaminyltransferase 6, protein-UDP acetylgalactosaminyltransferase 6, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6). They function as GalNAc transferases (EC 2.4.1.41) that 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. Pgant9 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Pgant4 and Pgant6 do not act as a peptide transferase, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. They prefer the diglycosylated Muc5AC-3/13 as a substrate. Pgant6 may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467340 [Multi-domain]  Cd Length: 126  Bit Score: 92.04  E-value: 4.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 469 PNIHWGELRNVATGSCLDTMG--HAPPSMMATSHCHGFGNNQLIRLNAKGQLGIGERCVEADGQGIKYAF--CRLGTVDG 544
Cdd:cd23462    1 EALAYGEIRNLAGKLCLDAPGrkKELNKPVGLYPCHGQGGNQYWMLTKDGEIRRDDLCLDYAGGSGDVTLypCHGMKGNQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 759065118 545 PWQYDEKTKTLLHRVHKKCMALHPQIQQLSLMPCDMNNAYHQWSF 589
Cdd:cd23462   81 FWIYDEETKQIVHGTSKKCLELSDDSSKLVMEPCNGSSPRQQWEF 125
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
147-429 2.82e-21

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 91.98  E-value: 2.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 147 PRTSVIIVFHNeGWSVLLRTIHSVIDRTPSKFleEILLVDDFSDKenlkGDLDSYIEQWGGKVRLLRNYERQGLIRTRSR 226
Cdd:COG1216    3 PKVSVVIPTYN-RPELLRRCLESLLAQTYPPF--EVIVVDNGSTD----GTAELLAALAFPRVRVIRNPENLGFAAARNL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 227 GARDAKGEVIVFLDAHCEVNVNWLPPLLApiaenrnvmtvpvidgidhknfeyrpvyqeghlyrgifEWGMLYkenelpR 306
Cdd:COG1216   76 GLRAAGGDYLLFLDDDTVVEPDWLERLLA--------------------------------------AACLLI------R 111

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 307 REAktrthdsmpyrspthagglfainreyFLSLGGYDEGLLVWGGEnFELSFKIWQCGGSILWVPCSHVGHVYRGfmpyT 386
Cdd:COG1216  112 REV--------------------------FEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGA----S 160

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 759065118 387 FGKLAQQKkgpLITINYKRVIETWFDEKYKEFFYTREPLARLL 429
Cdd:COG1216  161 SGPLLRAY---YLGRNRLLFLRKHGPRPLLRLALLRGLRLRLR 200
beta-trefoil_Ricin_GALNT1-like cd23433
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 471-589 9.29e-21

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1)-like subfamily; The GALNT1-like subfamily includes GALNT1 and GALNT13. They 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. GALNT1 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT13 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467311 [Multi-domain]  Cd Length: 127  Bit Score: 88.14  E-value: 9.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 471 IHWGELRNVATGSCLDTMGHAPPSMMATSHCHGFGNNQLIRLNAKGQLGIGERCVEA--DGQGIKYAFCrlgTVDGP--- 545
Cdd:cd23433    4 YSLGEIRNVETNLCLDTMGRKAGEKVGLSSCHGQGGNQVFSYTAKGEIRSDDLCLDAsrKGGPVKLEKC---HGMGGnqe 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 759065118 546 WQYDEKTKTLLHRVHKKCMALHP--QIQQLSLMPCDmNNAYHQWSF 589
Cdd:cd23433   81 WEYDKETKQIRHVNSGLCLTAPNedDPNEPVLRPCD-GGPSQKWEL 125
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
473-587 7.83e-20

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 85.66  E-value: 7.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118  473 WGELRNVATGSCLDTMGHAPP-SMMATSHCHGFGNNQLIRLNAKGQL--GIGERCVE----ADGQGIKYAFCRLGTVDGP 545
Cdd:pfam00652   2 TGRIRNRASGKCLDVPGGSSAgGPVGLYPCHGSNGNQLWTLTGDGTIrsVASDLCLDvgstADGAKVVLWPCHPGNGNQR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 759065118  546 WQYDEKTKTLLHRVHKKCMALHPQIQ---QLSLMPCDMNNAYHQW 587
Cdd:pfam00652  82 WRYDEDGTQIRNPQSGKCLDVSGAGTsngKVILWTCDSGNPNQQW 126
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 138-395 1.55e-17

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 83.64  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 138 KNWDYPEELPRTSVIIVFHNEGwSVLLRTIHSVIDRTPSKFLEEILLVDDFSDkENLKGDLDSYIEQWGgKVRLLRNYER 217
Cdd:COG1215   20 RRRRAPADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYPKEKLEVIVVDDGST-DETAEIARELAAEYP-RVRVIERPEN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 218 QGLIRTRSRGARDAKGEVIVFLDAHCEVNVNWLPPLLAPIAENRNVMTvpvidgidhknfeyrpvyqeghlyrgifewgm 297
Cdd:COG1215   97 GGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS-------------------------------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 298 lykenelprreaktrthdsmpyrspthaGGLFAINREYFLSLGGYDEGLLvwgGENFELSFKIWQCGGSILWVPCSHVgh 377
Cdd:COG1215  145 ----------------------------GANLAFRREALEEVGGFDEDTL---GEDLDLSLRLLRAGYRIVYVPDAVV-- 191

                        250
                 ....*....|....*...
gi 759065118 378 vyRGFMPYTFGKLAQQKK 395
Cdd:COG1215  192 --YEEAPETLRALFRQRR 207
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 147-377 4.06e-17

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 80.13  E-value: 4.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 147 PRTSVIIVFHNEGwSVLLRTIHSVIDRTPSKFleEILLVDDFSDkenlkgdlDS---YIEQWGGK---VRLLRNYERQGL 220
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGST--------DGtaeILRELAAKdprIRVIRLERNRGK 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 221 IRTRSRGARDAKGEVIVFLDAHCEVNVNWLPPLLAPIAENRNVMTvpvidgidhknFEYRPVYQEGHLYRGIFEWGMLYk 300
Cdd:COG0463   71 GAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV-----------YGSRLIREGESDLRRLGSRLFNL- 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759065118 301 enelprreaktrthDSMPYRSPTHAGGLFAINREYFLSLgGYDEGLLvwggENFELsFKIWQCGGSILWVPCSHVGH 377
Cdd:COG0463  139 --------------VRLLTNLPDSTSGFRLFRREVLEEL-GFDEGFL----EDTEL-LRALRHGFRIAEVPVRYRAG 195
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 474-590 1.37e-16

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 3 (Pgant3) and similar proteins; Pgant3, also called pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes 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. Pgant3 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers EA2 as a substrate and has weak activity toward Muc5AC-3, -13 and -3/13 substrates. Pgant3 plays a critical role in the regulation of integrin-mediated cell adhesion during wing development by influencing, via glycosylation, the secretion and localization of the integrin ligand Tig to the basal cell layer interface. It may have a role in protein O-glycosylation in the Golgi and thereby in establishing and/or maintaining a proper secretory apparatus structure. Together with Pgant35A, Pgant3 regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467338 [Multi-domain]  Cd Length: 121  Bit Score: 75.94  E-value: 1.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 474 GELRNVATGSCLDtmGHAPPSMMAT---SHCHGFGNNQLIRLNAKGQLGIGERCVEADgQGIKY--AFCrlgTVDGP--- 545
Cdd:cd23460    3 GQIKHTESGLCLD--WAGESNGDKTvalKPCHGGGGNQFWMYTGDGQIRQDHLCLTAD-EGNKVtlREC---ADQLPsqe 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 759065118 546 WQYDEKTKTLLHRVHKKCMALHPQIQQLSLMPCDMNNAYHQWSFH 590
Cdd:cd23460   77 WSYDEKTGTIRHRSTGLCLTLDANNDVVILKECDSNSLWQKWIFQ 121
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 151-294 3.38e-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: 73.31  E-value: 3.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 151 VIIVFHNEGwSVLLRTIHSVIDRTPSKFleEILLVDDFSDKENLKgDLDSYIEQwGGKVRLLRNYERQGLIRTRSRGARD 230
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTLE-ILEEYAKK-DPRVIRVINEENQGLAAARNAGLKA 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 759065118 231 AKGEVIVFLDAHCEVNVNWLPPLLAPIAENRNV----------MTVPVIDGIDHKNFEYRPVYQEGHLYRGIFE 294
Cdd:cd00761   76 ARGEYILFLDADDLLLPDWLERLVAELLADPEAdavggpgnllFRRELLEEIGGFDEALLSGEEDDDFLLRLLR 149
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 151-377 1.07e-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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 66.43  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 151 VIIVFHNeGWSVLLRTIHSVIDRTPSKFleEILLVDDFSDKenlkGDLDsYIEQWGGKVRLLRNYERQGLIRTRSRGARD 230
Cdd:cd04186    1 IIIVNYN-SLEYLKACLDSLLAQTYPDF--EVIVVDNASTD----GSVE-LLRELFPEVRLIRNGENLGFGAGNNQGIRE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 231 AKGEVIVFLDAHCEVNVNWLPPLLAPIAENRNVmtvpvidgidhknfeyrpvyqeghlyrGIFewgmlykenelprreak 310
Cdd:cd04186   73 AKGDYVLLLNPDTVVEPGALLELLDAAEQDPDV---------------------------GIV----------------- 108

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 759065118 311 trthdsmpyrSPTHAGGLFAINREYFLSLGGYDEGLLVWgGENFELSFKIWQCGGSILWVPCSHVGH 377
Cdd:cd04186  109 ----------GPKVSGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYH 164
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 484-589 4.23e-11

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 2 (GALNT2) and similar proteins; GALNT2 (EC 2.4.1.41), also called polypeptide GalNAc transferase 2, GalNAc-T2, pp-GaNTase 2, protein-UDP acetylgalactosaminyltransferase 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2, catalyzes 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. GALNT2 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. It is probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. It is also involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism. GALNT2 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467312 [Multi-domain]  Cd Length: 121  Bit Score: 60.41  E-value: 4.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 484 CLDTMGHAPPSMMATSHCHGFGNNQLIRLNAKGQLGIGERCVEAD----GQGIKYAFCRLGTVDGPWQYDEKTKTLLHRV 559
Cdd:cd23434   11 CLDTLGHKAGGTVGLYPCHGTGGNQEWSFTKDGQIKHDDLCLTVVdrapGSLVTLQPCREDDSNQKWEQIENNSKLRHVG 90

                         90       100       110
                 ....*....|....*....|....*....|.
gi 759065118 560 HKKCMALHPQIQQ-LSLMPCDMNNAYHQWSF 589
Cdd:cd23434   91 SNLCLDSRNAKSGgLTVETCDPSSGSQQWKF 121
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 474-589 1.12e-10

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3)-like subfamily; The GALNT3-like subfamily includes GALNT3, GALNT4, GALNT6 and GALNT12. They act as GalNAc transferases (EC 2.4.1.41) that 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. GALNT3 has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. It probably glycosylates fibronectin in vivo as well as FGF23. It plays a central role in phosphate homeostasis. GALNT4 shows highest activity towards Muc7, EA2 and Muc2, with a lower activity compared to GALNT2. It glycosylates 'Thr-57' of SELPLG. GALNT6 may participate in the synthesis of oncofetal fibronectin. It has activity toward Muc1a, Muc2, EA2 and fibronectin peptides. GALNT12 has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with non-glycosylated Muc2 and Muc7. It displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. It may play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs. Members of this family comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467313 [Multi-domain]  Cd Length: 128  Bit Score: 59.27  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 474 GELRNVATGSCLDT-----MGHAPPSMmatSHCHGFGNNQLIRLNAKGQL---GIGERCVEADGQG-IKYAFCRLGTVDG 544
Cdd:cd23435    5 GALRNKGSELCLDVnnpngQGGKPVIM---YGCHGLGGNQYFEYTSKGEIrhnIGKELCLHASGSDeVILQHCTSKGKDV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 759065118 545 P----WQYDEKtKTLLHRVHKKCmaLHPQIQQLSLMPCDMNNAYHQWSF 589
Cdd:cd23435   82 PpeqkWLFTQD-GTIRNPASGLC--LHASGYKVLLRTCNPSDDSQKWTF 127
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 473-590 7.16e-10

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 1 (Pgant1) and similar proteins; Pgant1, also called pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, functions as a GalNAc transferase (EC 2.4.1.41) that catalyzes 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. Pgant1 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers the monoglycosylated Muc5AC-3 as a substrate. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467337 [Multi-domain]  Cd Length: 132  Bit Score: 57.33  E-value: 7.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 473 WGELRNVATGSCLDTMGHAP--PSMMATSHCHGFGN-NQLIRLNAKGQLGIGERCVEADGQGIKYAFCRLGTVDGP---- 545
Cdd:cd23459    7 YGQVRNPGTNLCLDTLQRDEdkGYNLGLYPCQGGLSsNQLFSLSKKGELRREESCADVQGTEESKVILITCHGLEKfnqk 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 759065118 546 WQYDeKTKTLLHRVHKKCMALHPQIQQ--LSLMPCDMNNayHQ-WSFH 590
Cdd:cd23459   87 WKHT-KGGQIVHLASGKCLDAEGLKSGddVTLAKCDGSL--SQkWTFE 131
beta-trefoil_Ricin_GALNT10-like cd23439
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 472-589 1.34e-09

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 10 (GALNT10)-like subfamily; The GALNT10-like subfamily includes GALNT10 and GALNTL6. They act as GalNAc transferases (EC 2.4.1.41) that 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. GALNT10 has activity toward Muc5Ac and EA2 peptide substrates. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467317 [Multi-domain]  Cd Length: 126  Bit Score: 56.20  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 472 HWGELRNVATGSCLDTMGHAPPSMMATSHC--HGFGNNQLIRLNAKGQLGIGER--CVEA----DGQGIKYAFCRLGTVD 543
Cdd:cd23439    1 ASGEIRNVGSGLCIDTKHGGENDEVRLSKCvkDGGGGEQQFELTWHEDIRPKKRkvCFDVsshtPGAPVILYACHGMKGN 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 759065118 544 GPWQYDEKTKTLLHRVHKKCMALHPQIQQLSLMPCDMNNAYHQWSF 589
Cdd:cd23439   81 QLWKYRPNTKQLYHPVSGLCLDADPGSGKVFMNHCDESSDTQKWTW 126
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 150-394 1.76e-09

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: 58.78  E-value: 1.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 150 SVIIVFHNEGwSVLLRTIHSVIDRTPSKFLEEILLVDDFSDKENLkgdldSYIEQWGGK---VRLLRNyERQGLIRTRSR 226
Cdd:cd02525    3 SIIIPVRNEE-KYIEELLESLLNQSYPKDLIEIIVVDGGSTDGTR-----EIVQEYAAKdprIRLIDN-PKRIQSAGLNI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 227 GARDAKGEVIVFLDAHCEVNVNWLPPLLAPIAENRNVMTVPVIDGIDHKNFEYRPVYQEGHLyrgifeWGMLYKENELPR 306
Cdd:cd02525   76 GIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIAVAQSSP------LGSGGSAYRGGA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 307 REAKtrthdsmpYRSPTHAGglfAINREYFLSLGGYDEGLLVwgGENFELSFKIWQCGGSILWVPCSHVGHVYRGfmpyT 386
Cdd:cd02525  150 VKIG--------YVDTVHHG---AYRREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPRS----T 212


                 ....*...
gi 759065118 387 FGKLAQQK 394
Cdd:cd02525  213 LKKLARQY 220
beta-trefoil_Ricin_GALNT1 cd23466
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 474-587 1.27e-08

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1) and similar proteins; GALNT1 (EC 2.4.1.41), also called polypeptide GalNAc transferase 1, GalNAc-T1, pp-GaNTase 1, protein-UDP acetylgalactosaminyltransferase 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1, catalyzes 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. It has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT1 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates.


Pssm-ID: 467344  Cd Length: 127  Bit Score: 53.51  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 474 GELRNVATGSCLDTMGHAPPSMMATSHCHGFGNNQLIRLNAKGQLGIGERCVEADGQGIKYAFCRLGTVDGP--WQYDEK 551
Cdd:cd23466    7 GEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDDLCLDVSKLNGPVMMLKCHHLKGNqlWEYDPV 86

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 759065118 552 TKTLLHRVHKKCM--ALHPQIQQLSLMPCDMNNAyHQW 587
Cdd:cd23466   87 KLTLLHVNSNQCLdkATEEDSQVPSIRDCNGSRS-QQW 123
beta-trefoil_Ricin_GALNT13 cd23467
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 474-564 1.91e-08

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 13 (GALNT13) and similar proteins; GALNT13 (EC 2.4.1.41), also called polypeptide GalNAc transferase 13, GalNAc-T13, pp-GaNTase 13, protein-UDP acetylgalactosaminyltransferase 13, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13, catalyzes 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. It has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. GALNT13 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). The model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467345  Cd Length: 127  Bit Score: 53.11  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 474 GELRNVATGSCLDTMGHAPPSMMATSHCHGFGNNQLIRLNAKGQLGIGERCVEADGQGIKYAFCRLGTVDGP--WQYDEK 551
Cdd:cd23467    7 GEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVVMLKCHHMRGNqlWEYDAE 86

                         90
                 ....*....|...
gi 759065118 552 TKTLLHRVHKKCM 564
Cdd:cd23467   87 RLTLRHVNSNQCL 99
beta-trefoil_Ricin_Pgant8-like cd23461
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 474-589 4.93e-08

ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide N-acetylgalactosaminyltransferase 8 (Pgant8) and similar proteins; This subfamily includes Pgant8 (also called pp-GaNTase 8, protein-UDP acetylgalactosaminyltransferase 8, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8), Pgant10 (also called polypeptide N-acetylgalactosaminyltransferase 10, pp-GaNTase 10, protein-UDP acetylgalactosaminyltransferase 10, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10), Pgant11 (also called polypeptide N-acetylgalactosaminyltransferase 11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11) and Pgant12 (also called polypeptide N-acetylgalactosaminyltransferase 12, pp-GaNTase 12, protein-UDP acetylgalactosaminyltransferase 12, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12). They function as GalNAc transferases (EC 2.4.1.41) that 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. Pgant8 can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. It prefers both EA2 and the diglycosylated Muc5AC-3/13 as substrates, albeit at very low levels for Muc5AC-3/13. Members of this subfamily contain a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467339  Cd Length: 128  Bit Score: 52.02  E-value: 4.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 474 GELRNVA-TGSCLDTMGHAPPSMMATSHCHG----FGNNQLIRLNAKGQLGIGER--CVEADGQGIKYAFCRLGTVDGPW 546
Cdd:cd23461    4 GVIQSVAfPNLCLDILGRSHGGPPVLAKCSSnksmPGTFQNFSLTFHRQIKHGTSddCLEVRGNNVRLSRCHYQGGNQYW 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 759065118 547 QYDEKTKTLLH-RVHKKCMALHPQIQQLSLMPCDMNNAYHQWSF 589
Cdd:cd23461   84 KYDYETHQLINgGQNNKCLEADVESLKITLSICDSDNVEQKWKW 127
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 151-344 5.08e-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: 5.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 151 VIIVFHNEGwsvllRTIHSVIDRTPSKFLE----EILLVDDFS-DkenlkgdlDSY--IEQWG---GKVRLLRNYERQGL 220
Cdd:cd04179    1 VVIPAYNEE-----ENIPELVERLLAVLEEgydyEIIVVDDGStD--------GTAeiARELAarvPRVRVIRLSRNFGK 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 221 IRTRSRGARDAKGEVIVFLDAHCEVNVNWLPPLLAPIAENRN--VMTVPVIDGIDHKnfeyrpvyqeGHLYRGIFEWGMl 298
Cdd:cd04179   68 GAAVRAGFKAARGDIVVTMDADLQHPPEDIPKLLEKLLEGGAdvVIGSRFVRGGGAG----------MPLLRRLGSRLF- 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 759065118 299 ykeNELPRREAKTRTHDSMpyrspthaGGLFAINREYFLSLGGYDE 344
Cdd:cd04179  137 ---NFLIRLLLGVRISDTQ--------SGFRLFRREVLEALLSLLE 171
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 318-379 9.14e-08

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: 49.53  E-value: 9.14e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 759065118  318 PYRSPTHAGGLFAINREYFLSLGGYDEGLLVWGGENFELSFKIWQCGGSILWVPCShVGHVY 379
Cdd:pfam02709  13 KLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPGD-IGRYY 73
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 151-348 2.92e-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: 50.69  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 151 VIIVFHNEGwSVLLRTIHSVIDRTPSKFleEILLVDDFS-DKENLKgdldsyIEQWGGKVRLLRNYERQGLIRTRSR--- 226
Cdd:cd06423    1 IIVPAYNEE-AVIERTIESLLALDYPKL--EVIVVDDGStDDTLEI------LEELAALYIRRVLVVRDKENGGKAGaln 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 227 -GARDAKGEVIVFLDAHCEVNVNWLPPLLAPIAENRNVmtVPVIDGIDHKNFEYRPVYQEGHL-YRGIFEWGmlykenel 304
Cdd:cd06423   72 aGLRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKV--GAVQGRVRVRNGSENLLTRLQAIeYLSIFRLG-------- 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 759065118 305 prREAKTRTHDSMPYrspthAGGLFAINREYFLSLGGYDEGLLV 348
Cdd:cd06423  142 --RRAQSALGGVLVL-----SGAFGAFRREALREVGGWDEDTLT 178
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 478-589 6.19e-07

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 48.28  E-value: 6.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118   478 NVATGSCLDTMGHapPSMMATSHCHGFGNNQLIRLNAKGQL--GIGERCVEADGQGIKYAF---CRLGTVDGPWQYdEKT 552
Cdd:smart00458   3 SGNTGKCLDVNGN--KNPVGLFDCHGTGGNQLWKLTSDGAIriKDTDLCLTANGNTGSTVTlysCDGTNDNQYWEV-NKD 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 759065118   553 KTLLHRVHKKCMALH--PQIQQLSLMPCDmNNAYHQWSF 589
Cdd:smart00458  80 GTIRNPDSGKCLDVKdgNTGTKVILWTCS-GNPNQKWIF 117
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 151-352 1.27e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 49.59  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 151 VIIVFHNEGWSvLLRTIHSV--IDRTPSKFleEILLVDDFS-DKENlkgDLDSYIEQWGGK-VRLLRNYERQG-----LI 221
Cdd:cd04192    1 VVIAARNEAEN-LPRLLQSLsaLDYPKEKF--EVILVDDHStDGTV---QILEFAAAKPNFqLKILNNSRVSIsgkknAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 222 RTrsrGARDAKGEVIVFLDAHCEVNVNWLPPLLAPIAENRNVMTV-PVIdgidhknfeyrpVYQEGHL--YRGIFEWGML 298
Cdd:cd04192   75 TT---AIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAgPVI------------YFKGKSLlaKFQRLDWLSL 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 759065118 299 YkenelprreakTRTHDSMPYRSPTHAGGL-FAINREYFLSLGGYDEGLLVWGGE 352
Cdd:cd04192  140 L-----------GLIAGSFGLGKPFMCNGAnMAYRKEAFFEVGGFEGNDHIASGD 183
beta-trefoil_Ricin_GALNTL6 cd23477
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 468-593 1.31e-06

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase-like 6 (GALNTL6) and similar proteins; GALNTL6 (EC 2.4.1.41), also called polypeptide GalNAc transferase 17, GalNAc-T17, pp-GaNTase 17, protein-UDP acetylgalactosaminyltransferase 17, putative polypeptide N-acetylgalactosaminyltransferase 17, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17, catalyzes 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. GALNTL6 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467355  Cd Length: 148  Bit Score: 48.39  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 468 PPNIHWGELRNVATGSCLDTMGHAPPSMMATSHC------HGFGNNQLIRLNAKGQLGIGER------CVEADGQG--IK 533
Cdd:cd23477    2 PPPAAWGEIRNVAANLCVDSKHGATGTELRLDICvkdgseRTWSHEQLFTFGWREDIRPGEPlhtrkfCFDAISHNspVT 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 534 YAFCRLGTVDGPWQYdEKTKTLLHRVHKKCMALHPQIQQLSLMPCDMNNAYHQWSFHQIH 593
Cdd:cd23477   82 LYDCHGMKGNQLWSY-RKDKTLFHPVSNSCMDCNPADKKIFMNRCDPLSETQQWIFEHTN 140
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 143-339 2.68e-06

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


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 49.12  E-value: 2.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 143 PEELPRTSVIIVFHNEGwSVLLRTIHSVIDRTPSKFLEEILLVDDFS-DKENLKgdLDSYIEQwggKVRLLRNYERQGLI 221
Cdd:cd06439   25 PAYLPTVTIIIPAYNEE-AVIEAKLENLLALDYPRDRLEIIVVSDGStDGTAEI--AREYADK---GVKLLRFPERRGKA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 222 RTRSRGARDAKGEVIVFLDAhcevNVNWLPPLLAPIAENRNVMTVPVIDGidhknfEYRPVYQEGH-----LYRGIFEWg 296
Cdd:cd06439   99 AALNRALALATGEIVVFTDA----NALLDPDALRLLVRHFADPSVGAVSG------ELVIVDGGGSgsgegLYWKYENW- 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 759065118 297 mlykenelpRREAKTRTHdSMpyrsPTHAGGLFAINREYFLSL 339
Cdd:cd06439  168 ---------LKRAESRLG-ST----VGANGAIYAIRRELFRPL 196
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 181-360 5.68e-06

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: 48.43  E-value: 5.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118  181 EILLVDDFSDKENLKgDLDSYIEQWGGKVRLLRNYERQGLIRTRSRGARDAKGEVIVFLDAHCEVNVNWLPPLLAP---- 256
Cdd:pfam10111  31 ELIIINDGSTDKTLE-EVSSIKDHNLQVYYPNAPDTTYSLAASRNRGTSHAIGEYISFIDGDCLWSPDKFEKQLKIatsl 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118  257 -IAENRNVMTV-PVIDGIDHKNFEYRPVyqEGHLYRGIFEWGMLYKENELPRreaktrthDSMPYrspthaGGLFAINRE 334
Cdd:pfam10111 110 aLQENIQAAVVlPVTDLNDESSNFLRRG--GDLTASGDVLRDLLVFYSPLAI--------FFAPN------SSNALINRQ 173

                         170       180
                  ....*....|....*....|....*.
gi 759065118  335 YFLSLGGYDEGLLVWGGENFELSFKI 360
Cdd:pfam10111 174 AFIEVGGFDESFRGHGAEDFDIFLRL 199
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 147-240 1.53e-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: 43.35  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 147 PRTSVIIVFHNEGWSVLLRTIHSVIDRTPSKFleEILLVDDFSDKENLKGDLDSYIEQwGGKVRLLRNYERQGLIRTRSR 226
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYAAQ-DPRIKVVFREENGGISAATNS 77

                         90
                 ....*....|....
gi 759065118 227 GARDAKGEVIVFLD 240
Cdd:cd04184   78 ALELATGEFVALLD 91
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 470-590 2.21e-04

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. They act as GalNAc transferases (EC 2.4.1.41) that 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. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467319 [Multi-domain]  Cd Length: 122  Bit Score: 41.23  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 470 NIHWGELRNvatGS-CLDTMGH--APPSMMATSHCHGFGNNQLIRLNAKGQLGIGERCVEAD----GQGIKYAFCRLGTV 542
Cdd:cd23441    2 ELAYGQIKQ---GNlCLDSDEQlfQGPALLILAPCSNSSDSQEWSFTKDGQLQTQGLCLTVDssskDLPVVLETCSDDPK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 759065118 543 DgPWQYdeKTKTLLHRVHKKCMALHpQIQQLSLMPCDMNNAYHQWSFH 590
Cdd:cd23441   79 Q-KWTR--TGRQLVHSESGLCLDSR-KKKGLVVSPCRSGAPSQKWDFT 122
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 181-394 4.92e-04

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 42.00  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 181 EILLVDDFSDKENLKGDLDSYIEQWGGKVRL-----LRNYERQGLIRTRSRGARDAkgEVIVFLDAHCEVNVNWLPPlLA 255
Cdd:cd06435   30 EVIVIDNNTKDEALWKPVEAHCAQLGERFRFfhvepLPGAKAGALNYALERTAPDA--EIIAVIDADYQVEPDWLKR-LV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 256 PIAENRNVMTVPVIDgiDHKNFE----YRPVYQEghlYRGIFEWGMLYKeNElprreaktrthdsmpYRSPTHAGGLFAI 331
Cdd:cd06435  107 PIFDDPRVGFVQAPQ--DYRDGEeslfKRMCYAE---YKGFFDIGMVSR-NE---------------RNAIIQHGTMCLI 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 759065118 332 NREYFLSLGGYDEGLLVwggENFELSFKIWQCGGSILWVPCShVGHvyrGFMPYTFGKLAQQK 394
Cdd:cd06435  166 RRSALDDVGGWDEWCIT---EDSELGLRMHEAGYIGVYVAQS-YGH---GLIPDTFEAFKKQR 221
beta-trefoil_Ricin_GALNT15 cd23442
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 473-587 1.50e-03

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 15 (GALNT15) and similar proteins; GALNT15 (EC 2.4.1.41), also called polypeptide GalNAc transferase 15, GalNAc-T15, polypeptide GalNAc transferase-like protein 2, GalNAc-T-like protein 2, pp-GaNTase-like protein 2, polypeptide N-acetylgalactosaminyltransferase-like protein 2, protein-UDP acetylgalactosaminyltransferase-like protein 2, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2, catalyzes 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. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, GALNT15 can transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. It prefers Muc1a as its substrate. GALNT15 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467320 [Multi-domain]  Cd Length: 124  Bit Score: 38.96  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 473 WGELRNVATGSCLDT-----MGHAPPSMmatSHCHGFGNNQLIRLNAKGQL--GIGERCVEADGQGIKYAFCRLGTVDGP 545
Cdd:cd23442    5 SGQLYNTGTGYCADYihgwrLAGGPVEL---SPCSGQNGNQLFEYTSDKEIrfGSLQLCLDVRQEQVVLQNCTKEKTSQK 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 759065118 546 WQYDEkTKTLLHRVHKKCMALHPQ--IQQLSLMPCDmNNAYHQW 587
Cdd:cd23442   82 WDFQE-TGRIVHILSGKCIEAVESenSKLLFLSPCN-GQRNQMW 123
beta-trefoil_Ricin_GALNT3 cd23468
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 469-589 4.43e-03

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) and similar proteins; GALNT3 (EC 2.4.1.41), also called polypeptide GalNAc transferase 3, GalNAc-T3, pp-GaNTase 3, protein-UDP acetylgalactosaminyltransferase 3, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, catalyzes 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. GALNT3 has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. It probably glycosylates fibronectin in vivo as well as FGF23. It plays a central role in phosphate homeostasis. GALNT3 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.


Pssm-ID: 467346  Cd Length: 129  Bit Score: 37.48  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 469 PNIHwGELRNVATGSCLDTMGH---APPSMMATshCHGFGNNQL--------IRLNAKGQLgigerCVEADGQGIKYAFC 537
Cdd:cd23468    2 PLIF-GAIKNVGKELCLDVGENnhgGKPLIMYN--CHGLGGNQYfeysthheIRHNIQKEL-----CLHGSQGSVQLKEC 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 759065118 538 RL---GTVDGP---WQYdEKTKTLLHRVHKKCMALHPQiqQLSLMPCDMNNAYHQWSF 589
Cdd:cd23468   74 TYkgrNTAVLPeekWEL-QKDQLLYNPALNMCLSANGE--NPSLVPCNPSDPFQQWIF 128
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 151-241 8.73e-03

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: 37.93  E-value: 8.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759065118 151 VIIVFHNEGwSVLLRTIHSVID----RTPSKFleEILLVDDFSDKENLKgDLDSYIEQWGGKVRLLRNYERQGLIRTRSR 226
Cdd:cd04188    1 VVIPAYNEE-KRLPPTLEEAVEyleeRPSFSY--EIIVVDDGSKDGTAE-VARKLARKNPALIRVLTLPKNRGKGGAVRA 76

                         90
                 ....*....|....*
gi 759065118 227 GARDAKGEVIVFLDA 241
Cdd:cd04188   77 GMLAARGDYILFADA 91
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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