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Conserved domains on  [gi|1972235894|ref|NP_001379302|]
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Non-lysosomal glucosylceramidase [Caenorhabditis elegans]

Protein Classification

non-lysosomal glucosylceramidase( domain architecture ID 12114824)

non-lysosomal glucosylceramidase catalyzes the hydrolysis of glucosylceramide (GlcCer) to free glucose and ceramide

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF608 pfam04685
Glycosyl-hydrolase family 116, catalytic region; This represents a family of archaeal, ...
522-888 0e+00

Glycosyl-hydrolase family 116, catalytic region; This represents a family of archaeal, bacterial and eukaryotic glycosyl hydrolases, that belong to superfamily GH116. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335, with the likely acid/base at Asp-442 and the aspartates at Asp-406 and Asp-458 residues also playing a role in the catalysis of glucosides and xylosides that are beta-bound to hydrophobic groups. The family is defined as GH116, which presently includes enzymes with beta-glucosidase, EC:3.2.1.21, beta-xylosidase, EC:3.2.1.37, and glucocerebrosidase EC:3.2.1.45 activity.


:

Pssm-ID: 461391  Cd Length: 362  Bit Score: 589.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 522 GRFGYLESWEYRMVNTYDVHFYASFALAELWPELEITIQSEFTDQVYHSIEKPTRFHMEGDWANVKTASRVPHDLGNPAD 601
Cdd:pfam04685   1 GRFAYLEGQEYRMYNTYDVHFYASFALLMLWPKLELSLQRDFADAVLREDPTKRKILMDGKTAPRKVKGAVPHDLGDPLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 602 EPWIATNAYVMHDTGKWKDLNMKYVLTSWRDYVVLSNEheDFLFHTWPAVRMIMLEALEnWDQDGDGMIENFGKADQTYD 681
Cdd:pfam04685  81 DPWIRVNAYNIHDTSRWKDLNPKFVLQVYRDYVFTGDK--EFLKAMWPSVKAVMDYLLQ-FDKDGDGLIENEGFPDQTYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 682 AWQMEGVSAYCGSLWLASLRVAIEMAGLMKDDETQQLFRNTLEKAKKVFIDTLWTGTYFRFCERSRS-RETVMADQLCGY 760
Cdd:pfam04685 158 AWSMTGPSAYCGGLWLAALQAAIEMAELLGDKADVAKYKEKLEKAKKVFEKKLWNGKYFNYDSSSSSySNSIMADQLAGQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 761 WFLQSVSPEladELLPNHMVRSALDTIYRLNVCKFGNGRMGAVNGMKPSGVVDREYIQADEMWTGVTYAVASLLIQQGEV 840
Cdd:pfam04685 238 WYLRACGLE---PIVPEDKVRSALETIYELNVMKFKGGKMGAVNGMRPDGGVDTSSVQSEEVWTGVTYALAATMIQEGMV 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1972235894 841 EKAFHTASGSYLTCFEETGLQYQTPEALYESKFYRAIGYMRPLSIWAM 888
Cdd:pfam04685 315 EEGFKTAEGIYDTVWERLGMQFQTPEAWTANGEYRALGYMRPLSIWAM 362
Glyco_hydr_116N pfam12215
beta-glucosidase 2, glycosyl-hydrolase family 116 N-term; This domain is found in bacteria, ...
149-457 1.30e-86

beta-glucosidase 2, glycosyl-hydrolase family 116 N-term; This domain is found in bacteria, archaea and eukaryotes. This domain is typically between 320 to 354 amino acids in length. This domain is found associated with pfam04685. It is found just after the extreme N terminus. The N-terminal is thought to be the luminal domain while the C terminal is the cytosolic domain. The catalytic domain of GBA-2 is unknown. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335 in the downstream family pfam04685.


:

Pssm-ID: 463496  Cd Length: 309  Bit Score: 279.93  E-value: 1.30e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 149 RDFRGGFCKFSLRPGlvEHKVDVVAADQFILSV-RENDRCIYQKVLSAadvQRPSGQ-LSTWDFKFPKKNVHYRGLFPRS 226
Cdd:pfam12215  14 RGGRGDFRRWQIFPG--PHEFKSVPANQFAVFVsKGGGLKVQARVLST---EPPDGSlLSSWDWNYPGSKGTYHALYPRA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 227 WTTFRVPELELTVVIRQVSPVLPHNYEDTTYPVCLFLIDVENggSASREYEISVAFTFRNGTGNRRWEREAECSGVKFET 306
Cdd:pfam12215  89 WTVYEDPDFPVKVTCEQFSPIIPHNYKESSLPVAVFEWTVEN--PTDEPVDVSIMFTWQNGVGWFEVSDRDGGHPNEPFK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 307 EEEGlkptttaqekISGVSLYHTISS----MPCTYGLATTHREHTTTTVCERFDPSRNGAALWNHLKQTGDVPSCEEE-C 381
Cdd:pfam12215 167 ERDG----------VVGVLLHHVTLDeegeGPGTFAIATEKNPGVEVTYCTRFDPSGDGRELWDDFAKDGSLPNSGDStP 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972235894 382 LINAREMAVAVCNRFTLPPNSTKTHDYALSWDMPKVHFGSVARSYHRRYTRFFeasEAGSAADSLCVRALRLKDKW 457
Cdd:pfam12215 237 SSPGEQIAAAVAVRFTLAPGESKTIPFLLAWDFPVREFAWGRKYYGRRYTKFF---GNGDNAWAVAHYALKNYKRW 309
 
Name Accession Description Interval E-value
DUF608 pfam04685
Glycosyl-hydrolase family 116, catalytic region; This represents a family of archaeal, ...
522-888 0e+00

Glycosyl-hydrolase family 116, catalytic region; This represents a family of archaeal, bacterial and eukaryotic glycosyl hydrolases, that belong to superfamily GH116. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335, with the likely acid/base at Asp-442 and the aspartates at Asp-406 and Asp-458 residues also playing a role in the catalysis of glucosides and xylosides that are beta-bound to hydrophobic groups. The family is defined as GH116, which presently includes enzymes with beta-glucosidase, EC:3.2.1.21, beta-xylosidase, EC:3.2.1.37, and glucocerebrosidase EC:3.2.1.45 activity.


Pssm-ID: 461391  Cd Length: 362  Bit Score: 589.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 522 GRFGYLESWEYRMVNTYDVHFYASFALAELWPELEITIQSEFTDQVYHSIEKPTRFHMEGDWANVKTASRVPHDLGNPAD 601
Cdd:pfam04685   1 GRFAYLEGQEYRMYNTYDVHFYASFALLMLWPKLELSLQRDFADAVLREDPTKRKILMDGKTAPRKVKGAVPHDLGDPLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 602 EPWIATNAYVMHDTGKWKDLNMKYVLTSWRDYVVLSNEheDFLFHTWPAVRMIMLEALEnWDQDGDGMIENFGKADQTYD 681
Cdd:pfam04685  81 DPWIRVNAYNIHDTSRWKDLNPKFVLQVYRDYVFTGDK--EFLKAMWPSVKAVMDYLLQ-FDKDGDGLIENEGFPDQTYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 682 AWQMEGVSAYCGSLWLASLRVAIEMAGLMKDDETQQLFRNTLEKAKKVFIDTLWTGTYFRFCERSRS-RETVMADQLCGY 760
Cdd:pfam04685 158 AWSMTGPSAYCGGLWLAALQAAIEMAELLGDKADVAKYKEKLEKAKKVFEKKLWNGKYFNYDSSSSSySNSIMADQLAGQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 761 WFLQSVSPEladELLPNHMVRSALDTIYRLNVCKFGNGRMGAVNGMKPSGVVDREYIQADEMWTGVTYAVASLLIQQGEV 840
Cdd:pfam04685 238 WYLRACGLE---PIVPEDKVRSALETIYELNVMKFKGGKMGAVNGMRPDGGVDTSSVQSEEVWTGVTYALAATMIQEGMV 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1972235894 841 EKAFHTASGSYLTCFEETGLQYQTPEALYESKFYRAIGYMRPLSIWAM 888
Cdd:pfam04685 315 EEGFKTAEGIYDTVWERLGMQFQTPEAWTANGEYRALGYMRPLSIWAM 362
COG4354 COG4354
Uncharacterized conserved protein, contains GBA2_N and DUF608 domains [Function unknown];
166-888 1.30e-101

Uncharacterized conserved protein, contains GBA2_N and DUF608 domains [Function unknown];


Pssm-ID: 443491 [Multi-domain]  Cd Length: 744  Bit Score: 334.57  E-value: 1.30e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 166 EHKVDVVAADQFILSVRENDRCIYQKVLSA----ADVQRPSGQLSTWDfKFPK-KNVHYRGLFPRSWTTFRVPELELTVV 240
Cdd:COG4354    56 PHKFGFLPACQFAIFEEDEGGKAQARALEGplppYDGSGTEGSPAPNH-GLPRfEKGTFKALYPRSWVEYEDPVFPVQVT 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 241 IRQVSPVLPHNYEDTTYPVCLFLIDVENggSASREYEISVAFTFRN---GTGNRR--WEREAECSGVKFETEEeglkptt 315
Cdd:COG4354   135 CEAFSPIIPGNYQESSYPVAVFEWTVHN--PTDKPITLSIALSWQNfvgWFTNAIksPKVKVRWGGSDGNFNE------- 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 316 tAQEKISGVSLYHTISSMPCT---YG-LATTHREHTTTTVCERFDPSR---NGAALWNHLKQTGDVPSCEEECLINARE- 387
Cdd:COG4354   206 -WREDNGLVGILMTSEGVDPDsegEGqMALATITNPGVSYRTRWNPGAwggDGLDFWDDFSADGSLPDREDETPAEAGEq 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 388 MAVAVCNRFTLPPNSTKTHDYALSWDMPkVHFGSVARSYHRRYTRFFEASEAGSAAdslCVR-ALRLKDKWESEIEAWQS 466
Cdd:COG4354   285 PAGALAVRFTLAPGETREIPFVLAWDFP-NREFWWGVNYYRRYTNFYATQGKDAWA---VARtALKHLDELEEQTLAFQE 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 467 PILNHKkLPDWYKSAIFNELYFITDGGTVWfefdenwaehethlshyTKDkmkeiGRFGYLE---SWEYRMVNTYDVHFY 543
Cdd:COG4354   361 PLLRSD-LPDWVKEALLNNLYTLRSGTCLR-----------------TED-----GQFAVWEgldDDEGSCYGSCTHVWN 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 544 ASFALAELWPELEITIqseftdqvyhsiekptrfhMEGDWA-NVKTASRVPHDLGNPADEPWIATNAyvmhdtgkWKDLN 622
Cdd:COG4354   418 YSFALAFLFPELEKSM-------------------REVEFArAIDDEGAMPFRLGLPLEHPWEDCNL--------AADGQ 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 623 MKYVLTSWRDYVvLSNEHEdFLFHTWPAVRmimlEALE----NWDQDGDGMIEnfGKADQTYDaWQMEGVSAYCGSLWLA 698
Cdd:COG4354   471 MGFVLQVYRDWL-LSGDDE-FLRECWPAVK----KALEyawiGWDADQDGVPE--GAQHNTFD-WELYGPNPYCGGLYLA 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 699 SLRVAIEMAGLMKDDETQQLFRNTLEKAKKVFIDTLWTGTYFR------FCERSRSRETVMADQLCGYWFLQsvspeLAD 772
Cdd:COG4354   542 ALEAAAEMAEYLGDEEFAKTYRQWLEQGSKWYDENLWNGEYYIqdidsgASEEYQLGEGCLADQLCGQFYAH-----LLG 616
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 773 --ELLPNHMVRSALDTIYRLNVCKF-----GNGRM-------GAVNGMKPSGVVDREYIQADEMWTGVTYAVASLLIQQG 838
Cdd:COG4354   617 lgDLVPPENIRSALKSIYKYNFRKFfrehfNNGRSyalgdefGLANGTWPDGRPENPFPYPLEVWTGIEYGAAAFMIQEG 696
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972235894 839 EVEKAfhtasgsyLTCFE--------ETGLQYQTPEAlyeskfyrAIGYMRPLSIWAM 888
Cdd:COG4354   697 MKEEG--------LKLIEavrdrydgNKRNPFNEPEC--------GSHYARAMASWAL 738
Glyco_hydr_116N pfam12215
beta-glucosidase 2, glycosyl-hydrolase family 116 N-term; This domain is found in bacteria, ...
149-457 1.30e-86

beta-glucosidase 2, glycosyl-hydrolase family 116 N-term; This domain is found in bacteria, archaea and eukaryotes. This domain is typically between 320 to 354 amino acids in length. This domain is found associated with pfam04685. It is found just after the extreme N terminus. The N-terminal is thought to be the luminal domain while the C terminal is the cytosolic domain. The catalytic domain of GBA-2 is unknown. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335 in the downstream family pfam04685.


Pssm-ID: 463496  Cd Length: 309  Bit Score: 279.93  E-value: 1.30e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 149 RDFRGGFCKFSLRPGlvEHKVDVVAADQFILSV-RENDRCIYQKVLSAadvQRPSGQ-LSTWDFKFPKKNVHYRGLFPRS 226
Cdd:pfam12215  14 RGGRGDFRRWQIFPG--PHEFKSVPANQFAVFVsKGGGLKVQARVLST---EPPDGSlLSSWDWNYPGSKGTYHALYPRA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 227 WTTFRVPELELTVVIRQVSPVLPHNYEDTTYPVCLFLIDVENggSASREYEISVAFTFRNGTGNRRWEREAECSGVKFET 306
Cdd:pfam12215  89 WTVYEDPDFPVKVTCEQFSPIIPHNYKESSLPVAVFEWTVEN--PTDEPVDVSIMFTWQNGVGWFEVSDRDGGHPNEPFK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 307 EEEGlkptttaqekISGVSLYHTISS----MPCTYGLATTHREHTTTTVCERFDPSRNGAALWNHLKQTGDVPSCEEE-C 381
Cdd:pfam12215 167 ERDG----------VVGVLLHHVTLDeegeGPGTFAIATEKNPGVEVTYCTRFDPSGDGRELWDDFAKDGSLPNSGDStP 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972235894 382 LINAREMAVAVCNRFTLPPNSTKTHDYALSWDMPKVHFGSVARSYHRRYTRFFeasEAGSAADSLCVRALRLKDKW 457
Cdd:pfam12215 237 SSPGEQIAAAVAVRFTLAPGESKTIPFLLAWDFPVREFAWGRKYYGRRYTKFF---GNGDNAWAVAHYALKNYKRW 309
 
Name Accession Description Interval E-value
DUF608 pfam04685
Glycosyl-hydrolase family 116, catalytic region; This represents a family of archaeal, ...
522-888 0e+00

Glycosyl-hydrolase family 116, catalytic region; This represents a family of archaeal, bacterial and eukaryotic glycosyl hydrolases, that belong to superfamily GH116. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335, with the likely acid/base at Asp-442 and the aspartates at Asp-406 and Asp-458 residues also playing a role in the catalysis of glucosides and xylosides that are beta-bound to hydrophobic groups. The family is defined as GH116, which presently includes enzymes with beta-glucosidase, EC:3.2.1.21, beta-xylosidase, EC:3.2.1.37, and glucocerebrosidase EC:3.2.1.45 activity.


Pssm-ID: 461391  Cd Length: 362  Bit Score: 589.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 522 GRFGYLESWEYRMVNTYDVHFYASFALAELWPELEITIQSEFTDQVYHSIEKPTRFHMEGDWANVKTASRVPHDLGNPAD 601
Cdd:pfam04685   1 GRFAYLEGQEYRMYNTYDVHFYASFALLMLWPKLELSLQRDFADAVLREDPTKRKILMDGKTAPRKVKGAVPHDLGDPLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 602 EPWIATNAYVMHDTGKWKDLNMKYVLTSWRDYVVLSNEheDFLFHTWPAVRMIMLEALEnWDQDGDGMIENFGKADQTYD 681
Cdd:pfam04685  81 DPWIRVNAYNIHDTSRWKDLNPKFVLQVYRDYVFTGDK--EFLKAMWPSVKAVMDYLLQ-FDKDGDGLIENEGFPDQTYD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 682 AWQMEGVSAYCGSLWLASLRVAIEMAGLMKDDETQQLFRNTLEKAKKVFIDTLWTGTYFRFCERSRS-RETVMADQLCGY 760
Cdd:pfam04685 158 AWSMTGPSAYCGGLWLAALQAAIEMAELLGDKADVAKYKEKLEKAKKVFEKKLWNGKYFNYDSSSSSySNSIMADQLAGQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 761 WFLQSVSPEladELLPNHMVRSALDTIYRLNVCKFGNGRMGAVNGMKPSGVVDREYIQADEMWTGVTYAVASLLIQQGEV 840
Cdd:pfam04685 238 WYLRACGLE---PIVPEDKVRSALETIYELNVMKFKGGKMGAVNGMRPDGGVDTSSVQSEEVWTGVTYALAATMIQEGMV 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1972235894 841 EKAFHTASGSYLTCFEETGLQYQTPEALYESKFYRAIGYMRPLSIWAM 888
Cdd:pfam04685 315 EEGFKTAEGIYDTVWERLGMQFQTPEAWTANGEYRALGYMRPLSIWAM 362
COG4354 COG4354
Uncharacterized conserved protein, contains GBA2_N and DUF608 domains [Function unknown];
166-888 1.30e-101

Uncharacterized conserved protein, contains GBA2_N and DUF608 domains [Function unknown];


Pssm-ID: 443491 [Multi-domain]  Cd Length: 744  Bit Score: 334.57  E-value: 1.30e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 166 EHKVDVVAADQFILSVRENDRCIYQKVLSA----ADVQRPSGQLSTWDfKFPK-KNVHYRGLFPRSWTTFRVPELELTVV 240
Cdd:COG4354    56 PHKFGFLPACQFAIFEEDEGGKAQARALEGplppYDGSGTEGSPAPNH-GLPRfEKGTFKALYPRSWVEYEDPVFPVQVT 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 241 IRQVSPVLPHNYEDTTYPVCLFLIDVENggSASREYEISVAFTFRN---GTGNRR--WEREAECSGVKFETEEeglkptt 315
Cdd:COG4354   135 CEAFSPIIPGNYQESSYPVAVFEWTVHN--PTDKPITLSIALSWQNfvgWFTNAIksPKVKVRWGGSDGNFNE------- 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 316 tAQEKISGVSLYHTISSMPCT---YG-LATTHREHTTTTVCERFDPSR---NGAALWNHLKQTGDVPSCEEECLINARE- 387
Cdd:COG4354   206 -WREDNGLVGILMTSEGVDPDsegEGqMALATITNPGVSYRTRWNPGAwggDGLDFWDDFSADGSLPDREDETPAEAGEq 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 388 MAVAVCNRFTLPPNSTKTHDYALSWDMPkVHFGSVARSYHRRYTRFFEASEAGSAAdslCVR-ALRLKDKWESEIEAWQS 466
Cdd:COG4354   285 PAGALAVRFTLAPGETREIPFVLAWDFP-NREFWWGVNYYRRYTNFYATQGKDAWA---VARtALKHLDELEEQTLAFQE 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 467 PILNHKkLPDWYKSAIFNELYFITDGGTVWfefdenwaehethlshyTKDkmkeiGRFGYLE---SWEYRMVNTYDVHFY 543
Cdd:COG4354   361 PLLRSD-LPDWVKEALLNNLYTLRSGTCLR-----------------TED-----GQFAVWEgldDDEGSCYGSCTHVWN 417
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 544 ASFALAELWPELEITIqseftdqvyhsiekptrfhMEGDWA-NVKTASRVPHDLGNPADEPWIATNAyvmhdtgkWKDLN 622
Cdd:COG4354   418 YSFALAFLFPELEKSM-------------------REVEFArAIDDEGAMPFRLGLPLEHPWEDCNL--------AADGQ 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 623 MKYVLTSWRDYVvLSNEHEdFLFHTWPAVRmimlEALE----NWDQDGDGMIEnfGKADQTYDaWQMEGVSAYCGSLWLA 698
Cdd:COG4354   471 MGFVLQVYRDWL-LSGDDE-FLRECWPAVK----KALEyawiGWDADQDGVPE--GAQHNTFD-WELYGPNPYCGGLYLA 541
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 699 SLRVAIEMAGLMKDDETQQLFRNTLEKAKKVFIDTLWTGTYFR------FCERSRSRETVMADQLCGYWFLQsvspeLAD 772
Cdd:COG4354   542 ALEAAAEMAEYLGDEEFAKTYRQWLEQGSKWYDENLWNGEYYIqdidsgASEEYQLGEGCLADQLCGQFYAH-----LLG 616
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 773 --ELLPNHMVRSALDTIYRLNVCKF-----GNGRM-------GAVNGMKPSGVVDREYIQADEMWTGVTYAVASLLIQQG 838
Cdd:COG4354   617 lgDLVPPENIRSALKSIYKYNFRKFfrehfNNGRSyalgdefGLANGTWPDGRPENPFPYPLEVWTGIEYGAAAFMIQEG 696
                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972235894 839 EVEKAfhtasgsyLTCFE--------ETGLQYQTPEAlyeskfyrAIGYMRPLSIWAM 888
Cdd:COG4354   697 MKEEG--------LKLIEavrdrydgNKRNPFNEPEC--------GSHYARAMASWAL 738
Glyco_hydr_116N pfam12215
beta-glucosidase 2, glycosyl-hydrolase family 116 N-term; This domain is found in bacteria, ...
149-457 1.30e-86

beta-glucosidase 2, glycosyl-hydrolase family 116 N-term; This domain is found in bacteria, archaea and eukaryotes. This domain is typically between 320 to 354 amino acids in length. This domain is found associated with pfam04685. It is found just after the extreme N terminus. The N-terminal is thought to be the luminal domain while the C terminal is the cytosolic domain. The catalytic domain of GBA-2 is unknown. The primary catabolic pathway for glucosylceramide is catalysis by the lysosomal enzyme glucocerebrosidase. In higher eukaryotes, glucosylceramide is the precursor of glycosphingolipids, a complex group of ubiquitous membrane lipids. Mutations in the human protein cause motor-neurone defects in hereditary spastic paraplegia. The catalytic nucleophile, identified in UniProtKB:Q97YG8_SULSO, is a glutamine-335 in the downstream family pfam04685.


Pssm-ID: 463496  Cd Length: 309  Bit Score: 279.93  E-value: 1.30e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 149 RDFRGGFCKFSLRPGlvEHKVDVVAADQFILSV-RENDRCIYQKVLSAadvQRPSGQ-LSTWDFKFPKKNVHYRGLFPRS 226
Cdd:pfam12215  14 RGGRGDFRRWQIFPG--PHEFKSVPANQFAVFVsKGGGLKVQARVLST---EPPDGSlLSSWDWNYPGSKGTYHALYPRA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 227 WTTFRVPELELTVVIRQVSPVLPHNYEDTTYPVCLFLIDVENggSASREYEISVAFTFRNGTGNRRWEREAECSGVKFET 306
Cdd:pfam12215  89 WTVYEDPDFPVKVTCEQFSPIIPHNYKESSLPVAVFEWTVEN--PTDEPVDVSIMFTWQNGVGWFEVSDRDGGHPNEPFK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 307 EEEGlkptttaqekISGVSLYHTISS----MPCTYGLATTHREHTTTTVCERFDPSRNGAALWNHLKQTGDVPSCEEE-C 381
Cdd:pfam12215 167 ERDG----------VVGVLLHHVTLDeegeGPGTFAIATEKNPGVEVTYCTRFDPSGDGRELWDDFAKDGSLPNSGDStP 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972235894 382 LINAREMAVAVCNRFTLPPNSTKTHDYALSWDMPKVHFGSVARSYHRRYTRFFeasEAGSAADSLCVRALRLKDKW 457
Cdd:pfam12215 237 SSPGEQIAAAVAVRFTLAPGESKTIPFLLAWDFPVREFAWGRKYYGRRYTKFF---GNGDNAWAVAHYALKNYKRW 309
GDB1 COG3408
Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];
641-740 1.48e-04

Glycogen debranching enzyme (alpha-1,6-glucosidase) [Carbohydrate transport and metabolism];


Pssm-ID: 442634 [Multi-domain]  Cd Length: 353  Bit Score: 45.25  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972235894 641 EDFLFHTWPAVRMIMlEALENWDQDGDGMIENF--GKADQTY-DAwQMEGVSAYCG------SLWLASLRVAIEMAGLMK 711
Cdd:COG3408   104 LAFLRELLPALEAAL-DWILRGDRDGDGLLEYGrsGLDNQTWmDS-KVDSVTPRSGalvevqALWYNALRALAELARALG 181
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1972235894 712 DDETQQLFRNTLEKAKKVFIDTLW---TGTYF 740
Cdd:COG3408   182 DPELAARWRELAERLKESFNERFWneeLGYLA 213
 
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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