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Conserved domains on  [gi|51316021|sp|Q8MYY6|]
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RecName: Full=Putative polypeptide N-acetylgalactosaminyltransferase 13; Short=pp-GaNTase 13; AltName: Full=Protein-UDP acetylgalactosaminyltransferase 13; AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13

Protein Classification

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 ...
 113-422 1.11e-149

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: 431.63  E-value: 1.11e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 113 SVVISFHNEARSMLLRTIVSLLSRSPEDYLHELILVDDGSQRDVtLLDDLKrwmggVFGSRYRLGLTFLRNQERMGLIWS 192
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPE-LKLLLE-----EYYKKYLPKVKVLRLKKREGLIRA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 193 RNRGASLASGRYVLFLDSHCEVNEGWLEPLLERLALNTNLAVSPLLDPIDPTTLSYRKGNELLKGGFDWSLHFHW--LKR 270
Cdd:cd02510  75 RIAGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWlpLPE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 271 QLTNQESLEMPYQSPAFAGGVLMMSREWFLKLGSFNPYLKIWGGESIELAIKLWLCGGQIEIVPCSRIGHIFRR-RHAFD 349
Cdd:cd02510 155 EERRRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRkRKPYT 234

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51316021 350 FPPQSDrqlspaqeTYLHNSKIIAESWLDEYKNMFYALRPAARRIPLdHTYDELQRMRKERRCHPFEWYLRHV 422
Cdd:cd02510 235 FPGGSG--------TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDY-GDLSERKALRERLKCKSFKWYLENV 298
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 432-550 2.25e-33

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold 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 was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.


The actual alignment was detected with superfamily member cd23441:

Pssm-ID: 483949 [Multi-domain]  Cd Length: 122  Bit Score: 123.28  E-value: 2.25e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 432 ELSATGTLRNEDRCVHAR----QKDSQPILASCYLS-DITQWSMLRqSGQLSTHrELCLAVGF---GMRIALEPCGRNet 503
Cdd:cd23441   1 NELAYGQIKQGNLCLDSDeqlfQGPALLILAPCSNSsDSQEWSFTK-DGQLQTQ-GLCLTVDSsskDLPVVLETCSDD-- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 51316021 504 vrRSQRWVRLGTHLLHAESHLCLDNPLKDRLEMSTCRSHAVSQSFQF 550
Cdd:cd23441  77 --PKQKWTRTGRQLVHSESGLCLDSRKKKGLVVSPCRSGAPSQKWDF 121
 
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 ...
 113-422 1.11e-149

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: 431.63  E-value: 1.11e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 113 SVVISFHNEARSMLLRTIVSLLSRSPEDYLHELILVDDGSQRDVtLLDDLKrwmggVFGSRYRLGLTFLRNQERMGLIWS 192
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPE-LKLLLE-----EYYKKYLPKVKVLRLKKREGLIRA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 193 RNRGASLASGRYVLFLDSHCEVNEGWLEPLLERLALNTNLAVSPLLDPIDPTTLSYRKGNELLKGGFDWSLHFHW--LKR 270
Cdd:cd02510  75 RIAGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWlpLPE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 271 QLTNQESLEMPYQSPAFAGGVLMMSREWFLKLGSFNPYLKIWGGESIELAIKLWLCGGQIEIVPCSRIGHIFRR-RHAFD 349
Cdd:cd02510 155 EERRRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRkRKPYT 234

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51316021 350 FPPQSDrqlspaqeTYLHNSKIIAESWLDEYKNMFYALRPAARRIPLdHTYDELQRMRKERRCHPFEWYLRHV 422
Cdd:cd02510 235 FPGGSG--------TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDY-GDLSERKALRERLKCKSFKWYLENV 298
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 432-550 2.25e-33

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: 123.28  E-value: 2.25e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 432 ELSATGTLRNEDRCVHAR----QKDSQPILASCYLS-DITQWSMLRqSGQLSTHrELCLAVGF---GMRIALEPCGRNet 503
Cdd:cd23441   1 NELAYGQIKQGNLCLDSDeqlfQGPALLILAPCSNSsDSQEWSFTK-DGQLQTQ-GLCLTVDSsskDLPVVLETCSDD-- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 51316021 504 vrRSQRWVRLGTHLLHAESHLCLDNPLKDRLEMSTCRSHAVSQSFQF 550
Cdd:cd23441  77 --PKQKWTRTGRQLVHSESGLCLDSRKKKGLVVSPCRSGAPSQKWDF 121
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 113-299 7.17e-26

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: 104.01  E-value: 7.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021   113 SVVISFHNEArSMLLRTIVSLLSRSPEDYlhELILVDDGSQ-RDVTLLDDLKRWMGGVfgsryrlglTFLRNQERMGLIW 191
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGSTdGTVEIAEEYAKKDPRV---------RVIRLPENRGKAG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021   192 SRNRGASLASGRYVLFLDSHCEVNEGWLEPLLERLALNTNLAVSPLLDPIDPTTLSYRKGNELLKGGFDWSLHFHWLKrq 271
Cdd:pfam00535  69 ARNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLG-- 146

                         170       180
                  ....*....|....*....|....*...
gi 51316021   272 ltnqesLEMPYQSPAFAggvlMMSREWF 299
Cdd:pfam00535 147 ------LNLPFLIGGFA----LYRREAL 164
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
112-394 1.69e-19

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 86.97  E-value: 1.69e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 112 VSVVISFHNEArSMLLRTIVSLLSRSPEDYlhELILVDDGSQRDVtlLDDLKRWMGGvfgsryrlGLTFLRNQERMGLIW 191
Cdd:COG1216   5 VSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGT--AELLAALAFP--------RVRVIRNPENLGFAA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 192 SRNRGASLASGRYVLFLDSHCEVNEGWLEPLLERlalntnlavsplldpidpttlsyrkgnellkggfdwslhfhwlkrq 271
Cdd:COG1216  72 ARNLGLRAAGGDYLLFLDDDTVVEPDWLERLLAA---------------------------------------------- 105

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 272 ltnqeslempyqspafagGVLMMSREWFLKLGSFNPYLKIWGGEsIELAIKLWLCGGQIEIVPCSRIGHIFRRRHafdfp 351
Cdd:COG1216 106 ------------------ACLLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASS----- 161

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 51316021 352 pqsdrqlSPAQETYLH--NSKIIAESWLDEYKNMFYALRPAARRI 394
Cdd:COG1216 162 -------GPLLRAYYLgrNRLLFLRKHGPRPLLRLALLRGLRLRL 199
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
435-548 3.15e-14

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 69.48  E-value: 3.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021   435 ATGTLRNE--DRCVHARQKDS---QPILASCYLSDITQWSMLRQSGQLSTH-RELCLAVG---FGMRIALEPCGRNetvR 505
Cdd:pfam00652   1 ATGRIRNRasGKCLDVPGGSSaggPVGLYPCHGSNGNQLWTLTGDGTIRSVaSDLCLDVGstaDGAKVVLWPCHPG---N 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 51316021   506 RSQRWV--RLGTHLLHAESHLCLD----NPLKDRLEMSTCRSHAVSQSF 548
Cdd:pfam00652  78 GNQRWRydEDGTQIRNPQSGKCLDvsgaGTSNGKVILWTCDSGNPNQQW 126
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 112-234 6.19e-06

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 48.50  E-value: 6.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021  112 VSVVISFHNeARSMLLRTIVSLLSRSPEDYlhELILVDDGSQrDVTLlDDLKRWmggvfgsRYRLGLTFLRNQERMGLIW 191
Cdd:PRK10073   8 LSIIIPLYN-AGKDFRAFMESLIAQTWTAL--EIIIVNDGST-DNSV-EIAKHY-------AENYPHVRLLHQANAGVSV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 51316021  192 SRNRGASLASGRYVLFLDSHCEVNEGWLEPLLErLALNTNLAV 234
Cdd:PRK10073  76 ARNTGLAVATGKYVAFPDADDVVYPTMYETLMT-MALEDDLDV 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 ...
 113-422 1.11e-149

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: 431.63  E-value: 1.11e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 113 SVVISFHNEARSMLLRTIVSLLSRSPEDYLHELILVDDGSQRDVtLLDDLKrwmggVFGSRYRLGLTFLRNQERMGLIWS 192
Cdd:cd02510   1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPE-LKLLLE-----EYYKKYLPKVKVLRLKKREGLIRA 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 193 RNRGASLASGRYVLFLDSHCEVNEGWLEPLLERLALNTNLAVSPLLDPIDPTTLSYRKGNELLKGGFDWSLHFHW--LKR 270
Cdd:cd02510  75 RIAGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDARGGFDWSLHFKWlpLPE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 271 QLTNQESLEMPYQSPAFAGGVLMMSREWFLKLGSFNPYLKIWGGESIELAIKLWLCGGQIEIVPCSRIGHIFRR-RHAFD 349
Cdd:cd02510 155 EERRRESPTAPIRSPTMAGGLFAIDREWFLELGGYDEGMDIWGGENLELSFKVWQCGGSIEIVPCSRVGHIFRRkRKPYT 234

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51316021 350 FPPQSDrqlspaqeTYLHNSKIIAESWLDEYKNMFYALRPAARRIPLdHTYDELQRMRKERRCHPFEWYLRHV 422
Cdd:cd02510 235 FPGGSG--------TVLRNYKRVAEVWMDEYKEYFYKARPELRNIDY-GDLSERKALRERLKCKSFKWYLENV 298
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 432-550 2.25e-33

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: 123.28  E-value: 2.25e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 432 ELSATGTLRNEDRCVHAR----QKDSQPILASCYLS-DITQWSMLRqSGQLSTHrELCLAVGF---GMRIALEPCGRNet 503
Cdd:cd23441   1 NELAYGQIKQGNLCLDSDeqlfQGPALLILAPCSNSsDSQEWSFTK-DGQLQTQ-GLCLTVDSsskDLPVVLETCSDD-- 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 51316021 504 vrRSQRWVRLGTHLLHAESHLCLDNPLKDRLEMSTCRSHAVSQSFQF 550
Cdd:cd23441  77 --PKQKWTRTGRQLVHSESGLCLDSRKKKGLVVSPCRSGAPSQKWDF 121
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 113-299 7.17e-26

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: 104.01  E-value: 7.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021   113 SVVISFHNEArSMLLRTIVSLLSRSPEDYlhELILVDDGSQ-RDVTLLDDLKRWMGGVfgsryrlglTFLRNQERMGLIW 191
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQTYPNF--EIIVVDDGSTdGTVEIAEEYAKKDPRV---------RVIRLPENRGKAG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021   192 SRNRGASLASGRYVLFLDSHCEVNEGWLEPLLERLALNTNLAVSPLLDPIDPTTLSYRKGNELLKGGFDWSLHFHWLKrq 271
Cdd:pfam00535  69 ARNAGLRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLG-- 146

                         170       180
                  ....*....|....*....|....*...
gi 51316021   272 ltnqesLEMPYQSPAFAggvlMMSREWF 299
Cdd:pfam00535 147 ------LNLPFLIGGFA----LYRREAL 164
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
112-394 1.69e-19

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 86.97  E-value: 1.69e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 112 VSVVISFHNEArSMLLRTIVSLLSRSPEDYlhELILVDDGSQRDVtlLDDLKRWMGGvfgsryrlGLTFLRNQERMGLIW 191
Cdd:COG1216   5 VSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGT--AELLAALAFP--------RVRVIRNPENLGFAA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 192 SRNRGASLASGRYVLFLDSHCEVNEGWLEPLLERlalntnlavsplldpidpttlsyrkgnellkggfdwslhfhwlkrq 271
Cdd:COG1216  72 ARNLGLRAAGGDYLLFLDDDTVVEPDWLERLLAA---------------------------------------------- 105

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 272 ltnqeslempyqspafagGVLMMSREWFLKLGSFNPYLKIWGGEsIELAIKLWLCGGQIEIVPCSRIGHIFRRRHafdfp 351
Cdd:COG1216 106 ------------------ACLLIRREVFEEVGGFDERFFLYGED-VDLCLRLRKAGYRIVYVPDAVVYHLGGASS----- 161

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 51316021 352 pqsdrqlSPAQETYLH--NSKIIAESWLDEYKNMFYALRPAARRI 394
Cdd:COG1216 162 -------GPLLRAYYLgrNRLLFLRKHGPRPLLRLALLRGLRLRL 199
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 114-267 6.41e-19

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: 83.71  E-value: 6.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 114 VVISFHNEARsMLLRTIVSLLSRSPEDYlhELILVDDGSQRDVtlLDDLKRWmggvfgSRYRLGLTFLRNQERMGLIWSR 193
Cdd:cd00761   1 VIIPAYNEEP-YLERCLESLLAQTYPNF--EVIVVDDGSTDGT--LEILEEY------AKKDPRVIRVINEENQGLAAAR 69

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51316021 194 NRGASLASGRYVLFLDSHCEVNEGWLEPLLERLALNTNL-AVSPlldpidPTTLSYRKGNELLKGGFDWSLHFHW 267
Cdd:cd00761  70 NAGLKAARGEYILFLDADDLLLPDWLERLVAELLADPEAdAVGG------PGNLLFRRELLEEIGGFDEALLSGE 138
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 112-334 2.07e-16

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 78.21  E-value: 2.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 112 VSVVISFHNEARSmLLRTIVSLLSRSPEDYlhELILVDDGSqRD--VTLLDDLKRWMGGVfgsryrlglTFLRNQERMGL 189
Cdd:COG0463   4 VSVVIPTYNEEEY-LEEALESLLAQTYPDF--EIIVVDDGS-TDgtAEILRELAAKDPRI---------RVIRLERNRGK 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 190 IWSRNRGASLASGRYVLFLDSHCEVNEGWLEPLLERLALNTNLAVsplldpidpttLSYRKGNELLKGGFDWSLHFHWLK 269
Cdd:COG0463  71 GAARNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV-----------YGSRLIREGESDLRRLGSRLFNLV 139

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51316021 270 RQLTNqeslempyqSPAFAGGVLMMSREWFLKLGSFNPYLkiwggESIELaIKLWLCGGQIEIVP 334
Cdd:COG0463 140 RLLTN---------LPDSTSGFRLFRREVLEELGFDEGFL-----EDTEL-LRALRHGFRIAEVP 189
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 112-345 4.52e-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: 75.93  E-value: 4.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 112 VSVVISFHNEARsMLLRTIVSLLSRSPEDYLHELILVDDGSqRDVTLlDDLKRwmggvFGSRYRlGLTFLRNQERMGLIW 191
Cdd:COG1215  31 VSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGS-TDETA-EIARE-----LAAEYP-RVRVIERPENGGKAA 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 192 SRNRGASLASGRYVLFLDSHCEVNEGWLEPLLERLAlntnlavsplldpiDPTTlsyrkgnellkggfdwslhfhwlkrq 271
Cdd:COG1215 102 ALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFA--------------DPGV-------------------------- 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51316021 272 ltnqeslempyqspAFAGGVLMMSREWFLKLGSFNPYLkiwGGESIELAIKLWLCGGQIEIVPCSRIGHIFRRR 345
Cdd:COG1215 142 --------------GASGANLAFRREALEEVGGFDEDT---LGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPET 198
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
435-548 3.15e-14

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 69.48  E-value: 3.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021   435 ATGTLRNE--DRCVHARQKDS---QPILASCYLSDITQWSMLRQSGQLSTH-RELCLAVG---FGMRIALEPCGRNetvR 505
Cdd:pfam00652   1 ATGRIRNRasGKCLDVPGGSSaggPVGLYPCHGSNGNQLWTLTGDGTIRSVaSDLCLDVGstaDGAKVVLWPCHPG---N 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 51316021   506 RSQRWV--RLGTHLLHAESHLCLD----NPLKDRLEMSTCRSHAVSQSF 548
Cdd:pfam00652  78 GNQRWRydEDGTQIRNPQSGKCLDvsgaGTSNGKVILWTCDSGNPNQQW 126
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
 281-346 1.80e-13

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: 65.71  E-value: 1.80e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51316021   281 PYQSPAFAGGVLMMSREWFLKLGSFNPYLKIWGGESIELAIKLWLCGGQIEIVPCsRIGHIFRRRH 346
Cdd:pfam02709  13 KLPYKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERPPG-DIGRYYMLYH 77
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 114-340 2.47e-11

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: 62.19  E-value: 2.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 114 VVISFHNEARsMLLRTIVSLLSRSPEDYlhELILVDDGSQRDvtLLDDLKRwmggvfgsrYRLGLTFLRNQERMGLIWSR 193
Cdd:cd04186   1 IIIVNYNSLE-YLKACLDSLLAQTYPDF--EVIVVDNASTDG--SVELLRE---------LFPEVRLIRNGENLGFGAGN 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 194 NRGASLASGRYVLFLDSHCEVNEGWLEPLLERLALNTNLA-VSPLLdpidpttlsyrkgnellkggfdwslhfhwlkrql 272
Cdd:cd04186  67 NQGIREAKGDYVLLLNPDTVVEPGALLELLDAAEQDPDVGiVGPKV---------------------------------- 112

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51316021 273 tnqeslempyqspafAGGVLMMSREWFLKLGSFNPYLKIWgGESIELAIKLWLCGGQIEIVPCSRIGH 340
Cdd:cd04186 113 ---------------SGAFLLVRREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYH 164
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 112-330 6.14e-10

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


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 59.94  E-value: 6.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 112 VSVVISFHNEARSmLLRTIVSLLSRSPEDYLHELILVDDGSQrDVTLlDDLKRWMGGvfGSRYRLGLTFLRNQERmgliw 191
Cdd:cd02525   2 VSIIIPVRNEEKY-IEELLESLLNQSYPKDLIEIIVVDGGST-DGTR-EIVQEYAAK--DPRIRLIDNPKRIQSA----- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 192 SRNRGASLASGRYVLFLDSHCEVNEGWLEPLLERLALNTNLAVSPLLDPIDPT----TLSYRKGNELLKGGfdwSLHfhw 267
Cdd:cd02525  72 GLNIGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESkfqkAIAVAQSSPLGSGG---SAY--- 145

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51316021 268 lkrqltNQESLEMPYQSPAFAGgvlMMSREWFLKLGSFNPYLKIwgGESIELAIKLWLCGGQI 330
Cdd:cd02525 146 ------RGGAVKIGYVDTVHHG---AYRREVFEKVGGFDESLVR--NEDAELNYRLRKAGYKI 197
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 431-552 6.41e-08

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14) and similar proteins; GALNT14 (EC 2.4.1.41), also called polypeptide GalNAc transferase 14, GalNAc-T14, pp-GaNTase 14, protein-UDP acetylgalactosaminyltransferase 14, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14, 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. 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. GALNT14 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: 467356  Cd Length: 140  Bit Score: 51.79  E-value: 6.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 431 DELSATGTLRNEDRCVHARQKDSQ--PI--LASCYLSDIT-----QWsmLRQSGQLSTHRELCLAVGF---GMRIALEPC 498
Cdd:cd23478   4 ESDIQSGVIRQRQNCLESRRVEGQelPNlsLSPCIKSKGVpaksqEW--AYTYNQQIRQQQLCLSVHTlfpGSPVVLVPC 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51316021 499 grNETVRRsQRWVRLGTHLLHAESHLCLD-NPLKDRLE------MSTCRSHAVSQSFQFAL 552
Cdd:cd23478  82 --KEGDGK-QRWTKVGSHIEHMASRFCLDtEMFGDGTEsskeivINPCESSAMSQRWDMVL 139
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 114-308 4.71e-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: 50.30  E-value: 4.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 114 VVISFHNEARsMLLRTIVSLLSrspEDYLH-ELILVDDGSQRDVTLLddLKRwmggvFGSRYRLGLTFLRNQERMG---- 188
Cdd:cd06423   1 IIVPAYNEEA-VIERTIESLLA---LDYPKlEVIVVDDGSTDDTLEI--LEE-----LAALYIRRVLVVRDKENGGkaga 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 189 LiwsrNRGASLASGRYVLFLDSHCEVNEGWLEPLLERLALNTNL-AVSPLLDPIDPT--------TLSYRKGNELLKGGF 259
Cdd:cd06423  70 L----NAGLRHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVgAVQGRVRVRNGSenlltrlqAIEYLSIFRLGRRAQ 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 51316021 260 DWslhfhwlkrqltnqeslempYQSPAFAGGVLMM-SREWFLKLGSFNPY 308
Cdd:cd06423 146 SA--------------------LGGVLVLSGAFGAfRREALREVGGWDED 175
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 112-307 1.07e-06

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: 49.88  E-value: 1.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 112 VSVVISFHNEARSmLLRTIVSLLSRSPEDylHELILVDDGSQRDVTLLDdlkrwmggvfgsryRLGLTFLRNQERmgliw 191
Cdd:cd02522   1 LSIIIPTLNEAEN-LPRLLASLRRLNPLP--LEIIVVDGGSTDGTVAIA--------------RSAGVVVISSPK----- 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 192 SR----NRGASLASGRYVLFLDSHCEVNEGWLEPLLERLALNTNLAVS-PLLdpIDPTTLSYRkgnELLKGgfdWSLHFH 266
Cdd:cd02522  59 GRarqmNAGAAAARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAfRLR--FDDPGPRLR---LLELG---ANLRSR 130

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 51316021 267 WLKrqltnqesleMPY--QSpafaggvLMMSREWFLKLGSFNP 307
Cdd:cd02522 131 LFG----------LPYgdQG-------LFIRRELFEELGGFPE 156
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 437-550 1.79e-06

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: 46.93  E-value: 1.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 437 GTLRNEDRCVH--ARQKDSQPILASCYLSDITQ-WSMLrQSGQLsTHRELCLAVG---FGMRIALEPCGRNEtvrRSQRW 510
Cdd:cd23434   3 GSLKQGNLCLDtlGHKAGGTVGLYPCHGTGGNQeWSFT-KDGQI-KHDDLCLTVVdraPGSLVTLQPCREDD---SNQKW 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 51316021 511 VRL--GTHLLHAESHLCLD--NPLKDRLEMSTCRSHAVSQSFQF 550
Cdd:cd23434  78 EQIenNSKLRHVGSNLCLDsrNAKSGGLTVETCDPSSGSQQWKF 121
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 437-550 3.78e-06

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: 46.28  E-value: 3.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 437 GTLRNE--DRCV---HARQKDSQPILASCYLSDITQWSMLRQSGQLSTHReLCLAVGFGMRIALEPCgrnETVRRSQRWV 511
Cdd:cd23460   3 GQIKHTesGLCLdwaGESNGDKTVALKPCHGGGGNQFWMYTGDGQIRQDH-LCLTADEGNKVTLREC---ADQLPSQEWS 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 51316021 512 --RLGTHLLHAESHLCLD-NPLKDRLEMSTCRSHAVSQSFQF 550
Cdd:cd23460  79 ydEKTGTIRHRSTGLCLTlDANNDVVILKECDSNSLWQKWIF 120
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 112-234 6.19e-06

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 48.50  E-value: 6.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021  112 VSVVISFHNeARSMLLRTIVSLLSRSPEDYlhELILVDDGSQrDVTLlDDLKRWmggvfgsRYRLGLTFLRNQERMGLIW 191
Cdd:PRK10073   8 LSIIIPLYN-AGKDFRAFMESLIAQTWTAL--EIIIVNDGST-DNSV-EIAKHY-------AENYPHVRLLHQANAGVSV 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 51316021  192 SRNRGASLASGRYVLFLDSHCEVNEGWLEPLLErLALNTNLAV 234
Cdd:PRK10073  76 ARNTGLAVATGKYVAFPDADDVVYPTMYETLMT-MALEDDLDV 117
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 113-323 7.06e-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: 48.04  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021   113 SVVISFHN-EARSMLLRTIvsLLSRSPEDYLHELILVDDGSQRD-VTLLDDLKRWMGGVFGSRyrlgltflRNQERMGLI 190
Cdd:pfam10111   1 SVVIPVYNgEKTHWIQERI--LNQTFQYDPEFELIIINDGSTDKtLEEVSSIKDHNLQVYYPN--------APDTTYSLA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021   191 WSRNRGASLASGRYVLFLDSHCEVNEGWLEPLL---ERLALNTN---LAVSPLLDPIDPTTLSYRKGNELLkggfdWSLH 264
Cdd:pfam10111  71 ASRNRGTSHAIGEYISFIDGDCLWSPDKFEKQLkiaTSLALQENiqaAVVLPVTDLNDESSNFLRRGGDLT-----ASGD 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 51316021   265 FhwLKRQLTNQESLEMPYqspAFAGGVLMMSREWFLKLGSFNPYLKIWGGESIELAIKL 323
Cdd:pfam10111 146 V--LRDLLVFYSPLAIFF---APNSSNALINRQAFIEVGGFDESFRGHGAEDFDIFLRL 199
beta-trefoil_Ricin_GALNT3-like cd23435
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 478-550 9.56e-06

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: 45.02  E-value: 9.56e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51316021 478 STHRELCLAVGFGMRIALEPCGR-NETVRRSQRWV-RLGTHLLHAESHLCLDNpLKDRLEMSTCRSHAVSQSFQF 550
Cdd:cd23435  54 NIGKELCLHASGSDEVILQHCTSkGKDVPPEQKWLfTQDGTIRNPASGLCLHA-SGYKVLLRTCNPSDDSQKWTF 127
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 114-210 1.99e-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: 45.26  E-value: 1.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 114 VVISFHNEARSmLLRTIVSLLSRSPEDYLHELILVDDGSqRDVTL--LDDLkrwmggvfGSRYRlGLTFLRNQERMGLIW 191
Cdd:cd04179   1 VVIPAYNEEEN-IPELVERLLAVLEEGYDYEIIVVDDGS-TDGTAeiAREL--------AARVP-RVRVIRLSRNFGKGA 69

                        90
                ....*....|....*....
gi 51316021 192 SRNRGASLASGRYVLFLDS 210
Cdd:cd04179  70 AVRAGFKAARGDIVVTMDA 88
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 433-511 2.77e-05

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: 43.82  E-value: 2.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 433 LSATGTLRNEDRCVHARQKDSQPILASCYLSDITQWSMLRQSGQLS-THRELCLAVGFGMRIA-LEPCgrnETVRRSQRW 510
Cdd:cd23437  44 LNEAGQLAVGEQCLTASGSGGKVKLRKCNLGETGKWEYDEATGQIRhKGTGKCLDLNEGTNKLiLQPC---DSSSPSQKW 120


                .
gi 51316021 511 V 511
Cdd:cd23437 121 E 121
beta-trefoil_Ricin_GALNT16 cd23479
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 474-549 3.48e-05

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 16 (GALNT16) and similar proteins; GALNT16 (EC 2.4.1.41), also called polypeptide GalNAc transferase 16, GalNAc-T16, polypeptide GalNAc transferase-like protein 1, GalNAc-T-like protein 1, pp-GaNTase-like protein 1, polypeptide N-acetylgalactosaminyltransferase-like protein 1, protein-UDP acetylgalactosaminyltransferase-like protein 1, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 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. GALNT16 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: 467357  Cd Length: 129  Bit Score: 43.64  E-value: 3.48e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51316021 474 SGQLSTHRELCLAV---GFGMRIALEPCGRNETvrrSQRWVRLGTHLLHAESHLCLDNPlKDRLEMSTCRSHAVSQSFQ 549
Cdd:cd23479  51 SDPLIRQQDKCLAItsfSPGSKVILELCNQKDG---RQKWKLKGSFIQHQVSGLCLDSQ-SGRVVINQCQADLASQQWE 125
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 471-550 4.20e-05

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: 43.05  E-value: 4.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 471 LRQSGQLStHRELCL-AVGFGMRIALEPCGRNETvrrsQRWV--RLGTHLLHAESHLCLD-NPLKDRLEMSTCRSHAVSQ 546
Cdd:cd23437  44 LNEAGQLA-VGEQCLtASGSGGKVKLRKCNLGET----GKWEydEATGQIRHKGTGKCLDlNEGTNKLILQPCDSSSPSQ 118


                ....
gi 51316021 547 SFQF 550
Cdd:cd23437 119 KWEF 122
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 112-299 4.89e-05

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: 45.27  E-value: 4.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 112 VSVVISFHNEARsMLLRTIVSLLSRS-PEDYLhELILVDDGSQrDVTllDDLKRwmggvfgsRY-RLGLTFLRNQERMGL 189
Cdd:cd06439  31 VTIIIPAYNEEA-VIEAKLENLLALDyPRDRL-EIIVVSDGST-DGT--AEIAR--------EYaDKGVKLLRFPERRGK 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 190 IWSRNRGASLASGRYVLFLDSHCEVNEGWLEPLLERLALNTNLAVSPLLDPIDPTTLSyrkGNEllkgGFDWSLhFHWLK 269
Cdd:cd06439  98 AAALNRALALATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSGELVIVDGGGSG---SGE----GLYWKY-ENWLK 169

                       170       180       190
                ....*....|....*....|....*....|
gi 51316021 270 RQLTNQESLempyqsPAFAGGVLMMSREWF 299
Cdd:cd06439 170 RAESRLGST------VGANGAIYAIRRELF 193
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 114-210 8.02e-05

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 43.62  E-value: 8.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 114 VVISFHNEARSM--LLRTIVSLLSRSPEDYlhELILVDDGSqRDVTlLDDLKRWMggvfgsryrlgltflRNQERMGLIW 191
Cdd:cd04187   1 IVVPVYNEEENLpeLYERLKAVLESLGYDY--EIIFVDDGS-TDRT-LEILRELA---------------ARDPRVKVIR 61

                        90       100
                ....*....|....*....|....*...
gi 51316021 192 -SRNRG--ASL------ASGRYVLFLDS 210
Cdd:cd04187  62 lSRNFGqqAALlagldhARGDAVITMDA 89
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 114-209 1.11e-04

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


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 43.71  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 114 VVISFHNEAR---SMLLRTIVSLLSRSPEDYlhELILVDDGSqRDVTL--LDDLKRWMGGVFgsryRLgLTFLRNQERMG 188
Cdd:cd04188   1 VVIPAYNEEKrlpPTLEEAVEYLEERPSFSY--EIIVVDDGS-KDGTAevARKLARKNPALI----RV-LTLPKNRGKGG 72

                        90       100
                ....*....|....*....|.
gi 51316021 189 LIwsrNRGASLASGRYVLFLD 209
Cdd:cd04188  73 AV---RAGMLAARGDYILFAD 90
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 113-210 4.76e-04

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 42.45  E-value: 4.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021  113 SVVISFHNEAR---SMLLRTIVSLLSRSPED--YLHELILVDDGSqRDVTLLDDLKRWMGGVFGSryrLGLTFLRNQERM 187
Cdd:PTZ00260  73 SIVIPAYNEEDrlpKMLKETIKYLESRSRKDpkFKYEIIIVNDGS-KDKTLKVAKDFWRQNINPN---IDIRLLSLLRNK 148

                         90       100
                 ....*....|....*....|...
gi 51316021  188 GLIWSRNRGASLASGRYVLFLDS 210
Cdd:PTZ00260 149 GKGGAVRIGMLASRGKYILMVDA 171
beta-trefoil_Ricin_Pgant1-like cd23459
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 435-527 2.64e-03

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: 38.07  E-value: 2.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51316021 435 ATGTLRNE--DRCVHARQKD---SQPI-LASCYLSDIT-QWSMLRQSGQLstHREL-CLAV--GFGMRIALEPCGRNEtv 504
Cdd:cd23459   6 AYGQVRNPgtNLCLDTLQRDedkGYNLgLYPCQGGLSSnQLFSLSKKGEL--RREEsCADVqgTEESKVILITCHGLE-- 81

                        90       100
                ....*....|....*....|....
gi 51316021 505 RRSQRWV-RLGTHLLHAESHLCLD 527
Cdd:cd23459  82 KFNQKWKhTKGGQIVHLASGKCLD 105
 
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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