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Conserved domains on  [gi|257341250|emb|CBC16816|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

Glyco_hydro_1 and RICIN domain-containing protein( domain architecture ID 11042414)

Glyco_hydro_1 and RICIN domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
66-357 3.21e-28

Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 114.37  E-value: 3.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250  66 AEGLSKQPVDAVAKKIVEMGFNCVRLtwpldLMTNETLANNvtvrqsfqslglnddivgfqtNNPSIIDLPLIEAYKTVV 145
Cdd:COG2730   20 FETLWGNITEEDIDAIADWGFNTVRL-----PVSWERLQDP---------------------DNPYTLDEAYLERVDEVV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250 146 TTLGNNDVMVILDNHltkpgwccaNDDGNGFFGDQFFDpTVWVAALKKMAATFNGVSNVVGMSLRNELRGPkqNVNDWFK 225
Cdd:COG2730   74 DWAKARGLYVILDLH---------HAPGYQGWYDAATQ-ERFIAFWRQLAERYKDYPNVLGFELLNEPHGA--TWADWNA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250 226 YMQQGAEAVHSANNKVLVILSGLSFDADLSFVRSRPVKLSftgKLVFELHWY---SFSDGNSWAANNpnDICGRVLNRIG 302
Cdd:COG2730  142 LAQRAIDAIRATNPDRLIIVEGNNWGGAHNLRALDPLDDD---NLVYSVHFYgpfVFTHQGAWFAGP--TYPANLEARLD 216

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 257341250 303 NGGGYLLNQGFPLFLSEFGIDERGVNTNDNRYFGCLTGWAAENDVDWSLWALTGS 357
Cdd:COG2730  217 NWGDWAADNGVPVFVGEFGAYNDDPDASRLAWLRDLLDYLEENGIGWTYWSFNPS 271
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 411-514 4.33e-09

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


:

Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 54.44  E-value: 4.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250   411 FHPLTGLCIVRSLDDpKMLTLGPCNSSEP---WSYT-KKALRIKDQQLCLQSNGPkNPVTMTRTSCSTSGS--KWQTISA 484
Cdd:smart00458   2 ISGNTGKCLDVNGNK-NPVGLFDCHGTGGnqlWKLTsDGAIRIKDTDLCLTANGN-TGSTVTLYSCDGTNDnqYWEVNKD 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 257341250   485 SRMHLAsttsnKTSLCLDV---DTANNVVANAC 514
Cdd:smart00458  80 GTIRNP-----DSGKCLDVkdgNTGTKVILWTC 107
 
Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
66-357 3.21e-28

Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];


Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 114.37  E-value: 3.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250  66 AEGLSKQPVDAVAKKIVEMGFNCVRLtwpldLMTNETLANNvtvrqsfqslglnddivgfqtNNPSIIDLPLIEAYKTVV 145
Cdd:COG2730   20 FETLWGNITEEDIDAIADWGFNTVRL-----PVSWERLQDP---------------------DNPYTLDEAYLERVDEVV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250 146 TTLGNNDVMVILDNHltkpgwccaNDDGNGFFGDQFFDpTVWVAALKKMAATFNGVSNVVGMSLRNELRGPkqNVNDWFK 225
Cdd:COG2730   74 DWAKARGLYVILDLH---------HAPGYQGWYDAATQ-ERFIAFWRQLAERYKDYPNVLGFELLNEPHGA--TWADWNA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250 226 YMQQGAEAVHSANNKVLVILSGLSFDADLSFVRSRPVKLSftgKLVFELHWY---SFSDGNSWAANNpnDICGRVLNRIG 302
Cdd:COG2730  142 LAQRAIDAIRATNPDRLIIVEGNNWGGAHNLRALDPLDDD---NLVYSVHFYgpfVFTHQGAWFAGP--TYPANLEARLD 216

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 257341250 303 NGGGYLLNQGFPLFLSEFGIDERGVNTNDNRYFGCLTGWAAENDVDWSLWALTGS 357
Cdd:COG2730  217 NWGDWAADNGVPVFVGEFGAYNDDPDASRLAWLRDLLDYLEENGIGWTYWSFNPS 271
Cellulase pfam00150
Cellulase (glycosyl hydrolase family 5);
71-356 9.60e-17

Cellulase (glycosyl hydrolase family 5);


Pssm-ID: 395098 [Multi-domain]  Cd Length: 272  Bit Score: 80.50  E-value: 9.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250   71 KQPVDAVAKKIVEMGFNCVRL--TWPldlmtnetlannvtvrqsfqslglnddivGFQTNNPSI-IDLPLIEAYKTVVTT 147
Cdd:pfam00150  23 YVTTKAMIDLVKDWGFNVVRLpvSWG-----------------------------GYVPNNPDYlIDENWLNRVDEVVDY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250  148 LGNNDVMVILDNHlTKPGWccaNDDGNGFFG--DQFFDpTVWvaalKKMAATFNgVSNVVGMSLRNELRGPKQN--VNDW 223
Cdd:pfam00150  74 AIDNGMYVIIDWH-HDGGW---PGDPNGNIDtaKAFFK-KIW----TQIATRYG-NNPNVIFELMNEPHGNDQAtwADDV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250  224 FKYMQQGAEAVHSANNKVLVILSGLSFDADLSF-VRSRPVKLSftgKLVFELHWYSFSD--GNSWAANNPNDICGRVLNR 300
Cdd:pfam00150 144 KDYAQEAIDAIRAAGPNNLIIVGGNSWSQNPDGaALNDPNDDD---NLIYSVHFYAPSDfsGTWFDCEDPTNLAQRLRAA 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257341250  301 IgnggGYLLNQGFPLFLSEFGiderGVNTNDnryfGCLTG------WAAENDVDWSLWALTG 356
Cdd:pfam00150 221 A----NWALDNGIPVFIGEFG----GGNADG----PCRDEaekwldYLKENGISWTGWSNGN 270
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 411-514 4.33e-09

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 54.44  E-value: 4.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250   411 FHPLTGLCIVRSLDDpKMLTLGPCNSSEP---WSYT-KKALRIKDQQLCLQSNGPkNPVTMTRTSCSTSGS--KWQTISA 484
Cdd:smart00458   2 ISGNTGKCLDVNGNK-NPVGLFDCHGTGGnqlWKLTsDGAIRIKDTDLCLTANGN-TGSTVTLYSCDGTNDnqYWEVNKD 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 257341250   485 SRMHLAsttsnKTSLCLDV---DTANNVVANAC 514
Cdd:smart00458  80 GTIRNP-----DSGKCLDVkdgNTGTKVILWTC 107
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 425-515 4.48e-06

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: 46.40  E-value: 4.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250 425 DPKMLTLGPCNS-------SEPWSYTKKAlRIKDQQLCLQSNG--PKNPVTMTRTSCSTSGSKWQTISASRMHLASttsn 495
Cdd:cd23478   28 ELPNLSLSPCIKskgvpakSQEWAYTYNQ-QIRQQQLCLSVHTlfPGSPVVLVPCKEGDGKQRWTKVGSHIEHMAS---- 102

                         90       100
                 ....*....|....*....|....*..
gi 257341250 496 ktSLCLDVDTANN-------VVANACK 515
Cdd:cd23478  103 --RFCLDTEMFGDgtesskeIVINPCE 127
 
Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
66-357 3.21e-28

Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];


Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 114.37  E-value: 3.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250  66 AEGLSKQPVDAVAKKIVEMGFNCVRLtwpldLMTNETLANNvtvrqsfqslglnddivgfqtNNPSIIDLPLIEAYKTVV 145
Cdd:COG2730   20 FETLWGNITEEDIDAIADWGFNTVRL-----PVSWERLQDP---------------------DNPYTLDEAYLERVDEVV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250 146 TTLGNNDVMVILDNHltkpgwccaNDDGNGFFGDQFFDpTVWVAALKKMAATFNGVSNVVGMSLRNELRGPkqNVNDWFK 225
Cdd:COG2730   74 DWAKARGLYVILDLH---------HAPGYQGWYDAATQ-ERFIAFWRQLAERYKDYPNVLGFELLNEPHGA--TWADWNA 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250 226 YMQQGAEAVHSANNKVLVILSGLSFDADLSFVRSRPVKLSftgKLVFELHWY---SFSDGNSWAANNpnDICGRVLNRIG 302
Cdd:COG2730  142 LAQRAIDAIRATNPDRLIIVEGNNWGGAHNLRALDPLDDD---NLVYSVHFYgpfVFTHQGAWFAGP--TYPANLEARLD 216

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 257341250 303 NGGGYLLNQGFPLFLSEFGIDERGVNTNDNRYFGCLTGWAAENDVDWSLWALTGS 357
Cdd:COG2730  217 NWGDWAADNGVPVFVGEFGAYNDDPDASRLAWLRDLLDYLEENGIGWTYWSFNPS 271
Cellulase pfam00150
Cellulase (glycosyl hydrolase family 5);
71-356 9.60e-17

Cellulase (glycosyl hydrolase family 5);


Pssm-ID: 395098 [Multi-domain]  Cd Length: 272  Bit Score: 80.50  E-value: 9.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250   71 KQPVDAVAKKIVEMGFNCVRL--TWPldlmtnetlannvtvrqsfqslglnddivGFQTNNPSI-IDLPLIEAYKTVVTT 147
Cdd:pfam00150  23 YVTTKAMIDLVKDWGFNVVRLpvSWG-----------------------------GYVPNNPDYlIDENWLNRVDEVVDY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250  148 LGNNDVMVILDNHlTKPGWccaNDDGNGFFG--DQFFDpTVWvaalKKMAATFNgVSNVVGMSLRNELRGPKQN--VNDW 223
Cdd:pfam00150  74 AIDNGMYVIIDWH-HDGGW---PGDPNGNIDtaKAFFK-KIW----TQIATRYG-NNPNVIFELMNEPHGNDQAtwADDV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250  224 FKYMQQGAEAVHSANNKVLVILSGLSFDADLSF-VRSRPVKLSftgKLVFELHWYSFSD--GNSWAANNPNDICGRVLNR 300
Cdd:pfam00150 144 KDYAQEAIDAIRAAGPNNLIIVGGNSWSQNPDGaALNDPNDDD---NLIYSVHFYAPSDfsGTWFDCEDPTNLAQRLRAA 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257341250  301 IgnggGYLLNQGFPLFLSEFGiderGVNTNDnryfGCLTG------WAAENDVDWSLWALTG 356
Cdd:pfam00150 221 A----NWALDNGIPVFIGEFG----GGNADG----PCRDEaekwldYLKENGISWTGWSNGN 270
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 411-514 4.33e-09

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 54.44  E-value: 4.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250   411 FHPLTGLCIVRSLDDpKMLTLGPCNSSEP---WSYT-KKALRIKDQQLCLQSNGPkNPVTMTRTSCSTSGS--KWQTISA 484
Cdd:smart00458   2 ISGNTGKCLDVNGNK-NPVGLFDCHGTGGnqlWKLTsDGAIRIKDTDLCLTANGN-TGSTVTLYSCDGTNDnqYWEVNKD 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 257341250   485 SRMHLAsttsnKTSLCLDV---DTANNVVANAC 514
Cdd:smart00458  80 GTIRNP-----DSGKCLDVkdgNTGTKVILWTC 107
beta-trefoil_Ricin_GALNT14 cd23478
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 425-515 4.48e-06

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: 46.40  E-value: 4.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250 425 DPKMLTLGPCNS-------SEPWSYTKKAlRIKDQQLCLQSNG--PKNPVTMTRTSCSTSGSKWQTISASRMHLASttsn 495
Cdd:cd23478   28 ELPNLSLSPCIKskgvpakSQEWAYTYNQ-QIRQQQLCLSVHTlfPGSPVVLVPCKEGDGKQRWTKVGSHIEHMAS---- 102

                         90       100
                 ....*....|....*....|....*..
gi 257341250 496 ktSLCLDVDTANN-------VVANACK 515
Cdd:cd23478  103 --RFCLDTEMFGDgtesskeIVINPCE 127
beta-trefoil_Ricin_GALNT14-like cd23441
ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...
 426-514 9.35e-05

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: 42.00  E-value: 9.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250 426 PKMLTLGPCNSSEP---WSYTKKALrIKDQQLCL--QSNGPKNPVTMTrtSCSTSGS-KWQTISASRMHLasttsnKTSL 499
Cdd:cd23441   25 PALLILAPCSNSSDsqeWSFTKDGQ-LQTQGLCLtvDSSSKDLPVVLE--TCSDDPKqKWTRTGRQLVHS------ESGL 95

                         90
                 ....*....|....*
gi 257341250 500 CLDVDTANNVVANAC 514
Cdd:cd23441   96 CLDSRKKKGLVVSPC 110
beta-trefoil_Ricin_GALNT7 cd23437
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
 417-480 2.69e-04

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: 40.74  E-value: 2.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250 417 LCIVRSLDDPKMlTLGPCNSSE--PWSYTK--KALRIKDQQLCLQSNGPKNPVTMTRtsCSTSGS--KWQ 480
Cdd:cd23437   55 QCLTASGSGGKV-KLRKCNLGEtgKWEYDEatGQIRHKGTGKCLDLNEGTNKLILQP--CDSSSPsqKWE 121
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 412-529 1.28e-03

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: 38.96  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250 412 HPLTGLCiVRSLDDPKM---LTLGPCNS---SEPWSYTKKAlRIKDQQLCLQSNGPKNPVTmtrTSCSTSGSK--WQtIS 483
Cdd:cd23460    7 HTESGLC-LDWAGESNGdktVALKPCHGgggNQFWMYTGDG-QIRQDHLCLTADEGNKVTL---RECADQLPSqeWS-YD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 257341250 484 ASRMHLastTSNKTSLCLDVDTANNVVanackCLskdKSCEPMSQW 529
Cdd:cd23460   81 EKTGTI---RHRSTGLCLTLDANNDVV-----IL---KECDSNSLW 115
beta-trefoil_Ricin_Pgant3-like cd23460
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 417-480 6.33e-03

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: 37.04  E-value: 6.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257341250 417 LCIvrSLDDPKMLTLGPC---NSSEPWSYTKKALRIKDQ--QLCLQSNGPKNPVTMtrTSCStSGSKWQ 480
Cdd:cd23460   53 LCL--TADEGNKVTLRECadqLPSQEWSYDEKTGTIRHRstGLCLTLDANNDVVIL--KECD-SNSLWQ 116
beta-trefoil_Ricin_Pgant9-like cd23462
ricin B-type lectin domain, beta-trefoil fold, found in Drosophila melanogaster polypeptide ...
 415-515 9.81e-03

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: 36.57  E-value: 9.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257341250 415 TGLCI---VRSLDDPKMLTLGPCNSSEP---WSYTKKA-LRIKDqqLCLQSNGPKNPVTMtrTSCSTSGS--KWqTISAS 485
Cdd:cd23462   13 GKLCLdapGRKKELNKPVGLYPCHGQGGnqyWMLTKDGeIRRDD--LCLDYAGGSGDVTL--YPCHGMKGnqFW-IYDEE 87

                         90       100       110
                 ....*....|....*....|....*....|.
gi 257341250 486 RMHLASTTSNKtslCLDVDTAN-NVVANACK 515
Cdd:cd23462   88 TKQIVHGTSKK---CLELSDDSsKLVMEPCN 115
 
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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