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Conserved domains on  [gi|15231514|ref|NP_189245|]
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Cellulase (glycosyl hydrolase family 5) protein [Arabidopsis thaliana]

Protein Classification

Glyco_hydro_1 and RICIN domain-containing protein( domain architecture ID 11718376)

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];
45-348 8.28e-25

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


:

Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 104.36  E-value: 8.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514  45 DDLAKKIMAMGFNCVR--FTWpldlatnetlannvtvrQSFQslglnddisgfETKNPSMIDLPLIEAYKKVVAKLGNNN 122
Cdd:COG2730  29 EEDIDAIADWGFNTVRlpVSW-----------------ERLQ-----------DPDNPYTLDEAYLERVDEVVDWAKARG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514 123 VMVILDNHVTkPGWCCGYNDGNGffgdtffdpTTWIAGLTKIAMTFKGATNVVGMSLRNELRGPKQNvdDWFKYMQQGAE 202
Cdd:COG2730  81 LYVILDLHHA-PGYQGWYDAATQ---------ERFIAFWRQLAERYKDYPNVLGFELLNEPHGATWA--DWNALAQRAID 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514 203 AVHEANPNVLVILSGLSYDTDLSFVRSRHVNltfTRKLVFELHRY---SFTNTNTWSSKNPNEAcgEILKSIENGGGFNL 279
Cdd:COG2730 149 AIRATNPDRLIIVEGNNWGGAHNLRALDPLD---DDNLVYSVHFYgpfVFTHQGAWFAGPTYPA--NLEARLDNWGDWAA 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231514 280 R-DFPVFLSEFGIDLRGKNVNDNRYIGCILGWAAENDVDWSIWTLQGSyylregvvgmSEFYGILDS---DWV 348
Cdd:COG2730 224 DnGVPVFVGEFGAYNDDPDASRLAWLRDLLDYLEENGIGWTYWSFNPS----------GDTGGLLDRgtgDWG 286
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
380-484 1.03e-06

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


:

Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 47.51  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514    380 FHPLTGLCmLQSILDPTKVTLGLCN---ESQPWSYTPQNTLTLKDKSLCLeSTGPNAPVKLSETSCSSPNLSEWETISAS 456
Cdd:smart00458   2 ISGNTGKC-LDVNGNKNPVGLFDCHgtgGNQLWKLTSDGAIRIKDTDLCL-TANGNTGSTVTLYSCDGTNDNQYWEVNKD 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 15231514    457 NMLLAAKStnnSLCLDVDETN---NLMASNC 484
Cdd:smart00458  80 GTIRNPDS---GKCLDVKDGNtgtKVILWTC 107
 
Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
45-348 8.28e-25

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


Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 104.36  E-value: 8.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514  45 DDLAKKIMAMGFNCVR--FTWpldlatnetlannvtvrQSFQslglnddisgfETKNPSMIDLPLIEAYKKVVAKLGNNN 122
Cdd:COG2730  29 EEDIDAIADWGFNTVRlpVSW-----------------ERLQ-----------DPDNPYTLDEAYLERVDEVVDWAKARG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514 123 VMVILDNHVTkPGWCCGYNDGNGffgdtffdpTTWIAGLTKIAMTFKGATNVVGMSLRNELRGPKQNvdDWFKYMQQGAE 202
Cdd:COG2730  81 LYVILDLHHA-PGYQGWYDAATQ---------ERFIAFWRQLAERYKDYPNVLGFELLNEPHGATWA--DWNALAQRAID 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514 203 AVHEANPNVLVILSGLSYDTDLSFVRSRHVNltfTRKLVFELHRY---SFTNTNTWSSKNPNEAcgEILKSIENGGGFNL 279
Cdd:COG2730 149 AIRATNPDRLIIVEGNNWGGAHNLRALDPLD---DDNLVYSVHFYgpfVFTHQGAWFAGPTYPA--NLEARLDNWGDWAA 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231514 280 R-DFPVFLSEFGIDLRGKNVNDNRYIGCILGWAAENDVDWSIWTLQGSyylregvvgmSEFYGILDS---DWV 348
Cdd:COG2730 224 DnGVPVFVGEFGAYNDDPDASRLAWLRDLLDYLEENGIGWTYWSFNPS----------GDTGGLLDRgtgDWG 286
Cellulase pfam00150
Cellulase (glycosyl hydrolase family 5);
41-323 6.85e-14

Cellulase (glycosyl hydrolase family 5);


Pssm-ID: 395098 [Multi-domain]  Cd Length: 272  Bit Score: 72.02  E-value: 6.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514    41 KQSVDDLAKKIMAMGFNCVR--FTWpldlatnetlannvtvrqsFQSLGLNDDISgfetknpsmIDLPLIEAYKKVVAKL 118
Cdd:pfam00150  23 YVTTKAMIDLVKDWGFNVVRlpVSW-------------------GGYVPNNPDYL---------IDENWLNRVDEVVDYA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514   119 GNNNVMVILDNHVTkPGWccgYNDGNGFFGDT--FFDpTTWiaglTKIAMTFKGATNVvGMSLRNELRGPKQN--VDDWF 194
Cdd:pfam00150  75 IDNGMYVIIDWHHD-GGW---PGDPNGNIDTAkaFFK-KIW----TQIATRYGNNPNV-IFELMNEPHGNDQAtwADDVK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514   195 KYMQQGAEAVHEANPNVLVILSGLSYDTDLSFVRSRHVNLtfTRKLVFELHRYSFTN-TNTWSSKNPNEACGEILKSieN 273
Cdd:pfam00150 145 DYAQEAIDAIRAAGPNNLIIVGGNSWSQNPDGAALNDPND--DDNLIYSVHFYAPSDfSGTWFDCEDPTNLAQRLRA--A 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 15231514   274 GGGFNLRDFPVFLSEFGidLRGKNVNDNRYIGCILGWAAENDVDWSIWTL 323
Cdd:pfam00150 221 ANWALDNGIPVFIGEFG--GGNADGPCRDEAEKWLDYLKENGISWTGWSN 268
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
380-484 1.03e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 47.51  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514    380 FHPLTGLCmLQSILDPTKVTLGLCN---ESQPWSYTPQNTLTLKDKSLCLeSTGPNAPVKLSETSCSSPNLSEWETISAS 456
Cdd:smart00458   2 ISGNTGKC-LDVNGNKNPVGLFDCHgtgGNQLWKLTSDGAIRIKDTDLCL-TANGNTGSTVTLYSCDGTNDNQYWEVNKD 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 15231514    457 NMLLAAKStnnSLCLDVDETN---NLMASNC 484
Cdd:smart00458  80 GTIRNPDS---GKCLDVKDGNtgtKVILWTC 107
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
383-478 2.51e-06

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 46.76  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514   383 LTGLCM--LQSILDPTKVTLGLCNES---QPWSYTPQNTLTLKDKSLCLE--STGPNAPVKLSETSCSSPNlSEWETISA 455
Cdd:pfam00652   9 ASGKCLdvPGGSSAGGPVGLYPCHGSngnQLWTLTGDGTIRSVASDLCLDvgSTADGAKVVLWPCHPGNGN-QRWRYDED 87
                          90       100
                  ....*....|....*....|...
gi 15231514   456 SNMLLAAKStnnSLCLDVDETNN 478
Cdd:pfam00652  88 GTQIRNPQS---GKCLDVSGAGT 107
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
406-503 2.58e-04

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: 40.77  E-value: 2.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514 406 SQPWSYTPQNtlTLKDKSLCLE--STGPNAPVKLseTSCS-SPNLSEWETISASNMLlaaKSTNNSLCLDV--DETNNLM 480
Cdd:cd23434  34 NQEWSFTKDG--QIKHDDLCLTvvDRAPGSLVTL--QPCReDDSNQKWEQIENNSKL---RHVGSNLCLDSrnAKSGGLT 106
                        90       100
                ....*....|....*....|...
gi 15231514 481 ASNCKCVKGedsscdpiSQWFKI 503
Cdd:cd23434 107 VETCDPSSG--------SQQWKF 121
 
Name Accession Description Interval E-value
BglC COG2730
Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism];
45-348 8.28e-25

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


Pssm-ID: 442036 [Multi-domain]  Cd Length: 295  Bit Score: 104.36  E-value: 8.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514  45 DDLAKKIMAMGFNCVR--FTWpldlatnetlannvtvrQSFQslglnddisgfETKNPSMIDLPLIEAYKKVVAKLGNNN 122
Cdd:COG2730  29 EEDIDAIADWGFNTVRlpVSW-----------------ERLQ-----------DPDNPYTLDEAYLERVDEVVDWAKARG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514 123 VMVILDNHVTkPGWCCGYNDGNGffgdtffdpTTWIAGLTKIAMTFKGATNVVGMSLRNELRGPKQNvdDWFKYMQQGAE 202
Cdd:COG2730  81 LYVILDLHHA-PGYQGWYDAATQ---------ERFIAFWRQLAERYKDYPNVLGFELLNEPHGATWA--DWNALAQRAID 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514 203 AVHEANPNVLVILSGLSYDTDLSFVRSRHVNltfTRKLVFELHRY---SFTNTNTWSSKNPNEAcgEILKSIENGGGFNL 279
Cdd:COG2730 149 AIRATNPDRLIIVEGNNWGGAHNLRALDPLD---DDNLVYSVHFYgpfVFTHQGAWFAGPTYPA--NLEARLDNWGDWAA 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231514 280 R-DFPVFLSEFGIDLRGKNVNDNRYIGCILGWAAENDVDWSIWTLQGSyylregvvgmSEFYGILDS---DWV 348
Cdd:COG2730 224 DnGVPVFVGEFGAYNDDPDASRLAWLRDLLDYLEENGIGWTYWSFNPS----------GDTGGLLDRgtgDWG 286
Cellulase pfam00150
Cellulase (glycosyl hydrolase family 5);
41-323 6.85e-14

Cellulase (glycosyl hydrolase family 5);


Pssm-ID: 395098 [Multi-domain]  Cd Length: 272  Bit Score: 72.02  E-value: 6.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514    41 KQSVDDLAKKIMAMGFNCVR--FTWpldlatnetlannvtvrqsFQSLGLNDDISgfetknpsmIDLPLIEAYKKVVAKL 118
Cdd:pfam00150  23 YVTTKAMIDLVKDWGFNVVRlpVSW-------------------GGYVPNNPDYL---------IDENWLNRVDEVVDYA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514   119 GNNNVMVILDNHVTkPGWccgYNDGNGFFGDT--FFDpTTWiaglTKIAMTFKGATNVvGMSLRNELRGPKQN--VDDWF 194
Cdd:pfam00150  75 IDNGMYVIIDWHHD-GGW---PGDPNGNIDTAkaFFK-KIW----TQIATRYGNNPNV-IFELMNEPHGNDQAtwADDVK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514   195 KYMQQGAEAVHEANPNVLVILSGLSYDTDLSFVRSRHVNLtfTRKLVFELHRYSFTN-TNTWSSKNPNEACGEILKSieN 273
Cdd:pfam00150 145 DYAQEAIDAIRAAGPNNLIIVGGNSWSQNPDGAALNDPND--DDNLIYSVHFYAPSDfSGTWFDCEDPTNLAQRLRA--A 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 15231514   274 GGGFNLRDFPVFLSEFGidLRGKNVNDNRYIGCILGWAAENDVDWSIWTL 323
Cdd:pfam00150 221 ANWALDNGIPVFIGEFG--GGNADGPCRDEAEKWLDYLKENGISWTGWSN 268
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
380-484 1.03e-06

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


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 47.51  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514    380 FHPLTGLCmLQSILDPTKVTLGLCN---ESQPWSYTPQNTLTLKDKSLCLeSTGPNAPVKLSETSCSSPNLSEWETISAS 456
Cdd:smart00458   2 ISGNTGKC-LDVNGNKNPVGLFDCHgtgGNQLWKLTSDGAIRIKDTDLCL-TANGNTGSTVTLYSCDGTNDNQYWEVNKD 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 15231514    457 NMLLAAKStnnSLCLDVDETN---NLMASNC 484
Cdd:smart00458  80 GTIRNPDS---GKCLDVKDGNtgtKVILWTC 107
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
383-478 2.51e-06

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 46.76  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514   383 LTGLCM--LQSILDPTKVTLGLCNES---QPWSYTPQNTLTLKDKSLCLE--STGPNAPVKLSETSCSSPNlSEWETISA 455
Cdd:pfam00652   9 ASGKCLdvPGGSSAGGPVGLYPCHGSngnQLWTLTGDGTIRSVASDLCLDvgSTADGAKVVLWPCHPGNGN-QRWRYDED 87
                          90       100
                  ....*....|....*....|...
gi 15231514   456 SNMLLAAKStnnSLCLDVDETNN 478
Cdd:pfam00652  88 GTQIRNPQS---GKCLDVSGAGT 107
beta-trefoil_Ricin_GALNT2 cd23434
ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...
406-503 2.58e-04

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: 40.77  E-value: 2.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231514 406 SQPWSYTPQNtlTLKDKSLCLE--STGPNAPVKLseTSCS-SPNLSEWETISASNMLlaaKSTNNSLCLDV--DETNNLM 480
Cdd:cd23434  34 NQEWSFTKDG--QIKHDDLCLTvvDRAPGSLVTL--QPCReDDSNQKWEQIENNSKL---RHVGSNLCLDSrnAKSGGLT 106
                        90       100
                ....*....|....*....|...
gi 15231514 481 ASNCKCVKGedsscdpiSQWFKI 503
Cdd:cd23434 107 VETCDPSSG--------SQQWKF 121
 
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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