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Conserved domains on  [gi|17569239|ref|NP_508448|]
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Glycosylasparaginase beta chain [Caenorhabditis elegans]

Protein Classification

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase( domain architecture ID 10139950)

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase catalyzes the hydrolysis of the glycosylamide bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 25-333 7.43e-152

Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoproteins. This enzyme is an amidase located inside lysosomes. Mutation of this gene in humans causes a genetic disorder known as aspartylglycosaminuria (AGU). The glycosylasparaginase precursor undergoes autoproteolysis through an N-O or N-S acyl rearrangement of the peptide bond, which leads to the cleavage of a peptide bond between an Asp and a Thr. This proteolysis step generates an exposed N-terminal catalytic threonine and activates the enzyme.


:

Pssm-ID: 271335  Cd Length: 294  Bit Score: 429.29  E-value: 7.43e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  25 MVITTWGsdgFKKATKNAVDATLLGGR-MFGLVEGLSTCEALQCDTTVGYGGSPDENGETCLDSLVIDADGMRVGAVANL 103
Cdd:cd04513   1 LVINTWN---FTEAVEAAWEVLQKGGSaLDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAAL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 104 HRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGFKEEDLSTEETKSWISKWKTEKCQPNFWKNVSPDPSSSCgpyktn 183
Cdd:cd04513  78 RRIKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC------ 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 184 pltksmryySLVNQSDEAGYLVEKTNHDTIGMVVRDTENIFSAGTSSNGARFKIPGRVGDSPIPGAGAYA-NKFGGAAAT 262
Cdd:cd04513 152 ---------SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYAdNEVGAAAAT 222

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17569239 263 GDGDVMMRFLPSFFAVTQMELGTKPSKAAYKAITRILKVFPK-FSGAVVAMNVKGRIGASCaNINKFGYNVA 333
Cdd:cd04513 223 GDGDIMMRFLPSYQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAAC-NGEGFSYAVR 293
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 25-333 7.43e-152

Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoproteins. This enzyme is an amidase located inside lysosomes. Mutation of this gene in humans causes a genetic disorder known as aspartylglycosaminuria (AGU). The glycosylasparaginase precursor undergoes autoproteolysis through an N-O or N-S acyl rearrangement of the peptide bond, which leads to the cleavage of a peptide bond between an Asp and a Thr. This proteolysis step generates an exposed N-terminal catalytic threonine and activates the enzyme.


Pssm-ID: 271335  Cd Length: 294  Bit Score: 429.29  E-value: 7.43e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  25 MVITTWGsdgFKKATKNAVDATLLGGR-MFGLVEGLSTCEALQCDTTVGYGGSPDENGETCLDSLVIDADGMRVGAVANL 103
Cdd:cd04513   1 LVINTWN---FTEAVEAAWEVLQKGGSaLDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAAL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 104 HRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGFKEEDLSTEETKSWISKWKTEKCQPNFWKNVSPDPSSSCgpyktn 183
Cdd:cd04513  78 RRIKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC------ 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 184 pltksmryySLVNQSDEAGYLVEKTNHDTIGMVVRDTENIFSAGTSSNGARFKIPGRVGDSPIPGAGAYA-NKFGGAAAT 262
Cdd:cd04513 152 ---------SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYAdNEVGAAAAT 222

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17569239 263 GDGDVMMRFLPSFFAVTQMELGTKPSKAAYKAITRILKVFPK-FSGAVVAMNVKGRIGASCaNINKFGYNVA 333
Cdd:cd04513 223 GDGDIMMRFLPSYQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAAC-NGEGFSYAVR 293
Asparaginase_2 pfam01112
Asparaginase;
25-342 7.20e-111

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 325.69  E-value: 7.20e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239    25 MVITTWGS--------------DGFKKATKNAVDATLLGGRMFGLVE-GLSTCEaLQCDTTVGYGGSPDENGETCLDSLV 89
Cdd:pfam01112   1 VLVIHGGAgsilrtkereeayrAGLKEALEAGYAVLAAGGSALDAVEaAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239    90 IDADGMRVGAVANLHRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGF---KEEDLSTEETKSWISKWKTEKCQPNFW 166
Cdd:pfam01112  80 MDGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLervPPEDFLTEERLQELQKARKENFQPNMA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239   167 KNVSPDPSSSCGPYKtnpltksmryyslvnqsdeagylvektnHDTIGMVVRDTENIFSAGTSSNGARFKIPGRVGDSPI 246
Cdd:pfam01112 160 LNVAPDPLKECGDSK----------------------------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPI 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239   247 PGAGAYA-NKFGGAAATGDGDVMMRFLPSFFAVTQMELGTKPSKAAYKAITRILKVFPKfSGAVVAMNVKGRIGASCANI 325
Cdd:pfam01112 212 IGAGTYAdNATGAVSATGHGEDIIRETLAYDIVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFNTE 290

                         330
                  ....*....|....*...
gi 17569239   326 NKF-GYNVAFQNGTVVTY 342
Cdd:pfam01112 291 GMYrAYHTGDGIGDVLIY 308
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 16-322 8.30e-57

Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];


Pssm-ID: 441055  Cd Length: 305  Bit Score: 187.24  E-value: 8.30e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  16 GTINDDSL-PMVITTWgsdgfKKATKNAVDAtllGGRMfgLVEGLSTCEALQC---------DTTVGYGGSPDENGETCL 85
Cdd:COG1446  15 GTIARSAMtPEVEAAY-----RAGLRAALEA---GYAV--LEAGGSALDAVEAavrvleddpLFNAGKGAVLTRDGTVEL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  86 DSLVIDADGMRVGAVANLHRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGFKEEDLSTEETKSwisKWKTekcqpnf 165
Cdd:COG1446  85 DASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEK---RWKQ------- 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 166 WKNVSpdpssscgpyktnpltksmryyslvnqsdEAGYLVEKTNHDTIGMVVRDTENIFSAGTSSNGARFKIPGRVGDSP 245
Cdd:COG1446 155 WKKAL-----------------------------EYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSP 205

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17569239 246 IPGAGAYA-NKFGGAAATGDGDVMMRFLPSFFAVTQMELGTKPSKAAYKAITRILKVFpKFSGAVVAMNVKGRIGASC 322
Cdd:COG1446 206 IIGAGTYAdNEVGAVSATGHGEYFIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPF 282
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 78-318 1.65e-22

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 96.17  E-value: 1.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239   78 DENGEtcLDSLVIDADGMRVGAVANLHRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGFKEedlsteetkswiskwk 157
Cdd:PRK10226  77 DETHE--LDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMER---------------- 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  158 tekcqpnfwknVSPDPSSScgPYKTNPLTKSmRYYSLVNQSDEAGYLVEKTNHDTIGMVVRDTENIFSAGTSSNGARFKI 237
Cdd:PRK10226 139 -----------VSPEIFST--PLRYEQLLAA-RAEGATVLDHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  238 PGRVGDSPIPGAGAYANKFGGAAA-TGDGDVMMRFLPSFFAVTQMELGtkpSKAAYKAITR-ILKVFPKF--SGAVVAMN 313
Cdd:PRK10226 205 PGRVGDSPLVGAGCYANNASVAVScTGTGEVFIRALAAYDIAALMDYG---GLSLAEACERvVMEKLPALggSGGLIAID 281


                 ....*
gi 17569239  314 VKGRI 318
Cdd:PRK10226 282 HEGNV 286
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 25-333 7.43e-152

Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoproteins. This enzyme is an amidase located inside lysosomes. Mutation of this gene in humans causes a genetic disorder known as aspartylglycosaminuria (AGU). The glycosylasparaginase precursor undergoes autoproteolysis through an N-O or N-S acyl rearrangement of the peptide bond, which leads to the cleavage of a peptide bond between an Asp and a Thr. This proteolysis step generates an exposed N-terminal catalytic threonine and activates the enzyme.


Pssm-ID: 271335  Cd Length: 294  Bit Score: 429.29  E-value: 7.43e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  25 MVITTWGsdgFKKATKNAVDATLLGGR-MFGLVEGLSTCEALQCDTTVGYGGSPDENGETCLDSLVIDADGMRVGAVANL 103
Cdd:cd04513   1 LVINTWN---FTEAVEAAWEVLQKGGSaLDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAAL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 104 HRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGFKEEDLSTEETKSWISKWKTEKCQPNFWKNVSPDPSSSCgpyktn 183
Cdd:cd04513  78 RRIKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC------ 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 184 pltksmryySLVNQSDEAGYLVEKTNHDTIGMVVRDTENIFSAGTSSNGARFKIPGRVGDSPIPGAGAYA-NKFGGAAAT 262
Cdd:cd04513 152 ---------SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYAdNEVGAAAAT 222

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17569239 263 GDGDVMMRFLPSFFAVTQMELGTKPSKAAYKAITRILKVFPK-FSGAVVAMNVKGRIGASCaNINKFGYNVA 333
Cdd:cd04513 223 GDGDIMMRFLPSYQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAAC-NGEGFSYAVR 293
Asparaginase_2 pfam01112
Asparaginase;
25-342 7.20e-111

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 325.69  E-value: 7.20e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239    25 MVITTWGS--------------DGFKKATKNAVDATLLGGRMFGLVE-GLSTCEaLQCDTTVGYGGSPDENGETCLDSLV 89
Cdd:pfam01112   1 VLVIHGGAgsilrtkereeayrAGLKEALEAGYAVLAAGGSALDAVEaAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239    90 IDADGMRVGAVANLHRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGF---KEEDLSTEETKSWISKWKTEKCQPNFW 166
Cdd:pfam01112  80 MDGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLervPPEDFLTEERLQELQKARKENFQPNMA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239   167 KNVSPDPSSSCGPYKtnpltksmryyslvnqsdeagylvektnHDTIGMVVRDTENIFSAGTSSNGARFKIPGRVGDSPI 246
Cdd:pfam01112 160 LNVAPDPLKECGDSK----------------------------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPI 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239   247 PGAGAYA-NKFGGAAATGDGDVMMRFLPSFFAVTQMELGTKPSKAAYKAITRILKVFPKfSGAVVAMNVKGRIGASCANI 325
Cdd:pfam01112 212 IGAGTYAdNATGAVSATGHGEDIIRETLAYDIVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFNTE 290

                         330
                  ....*....|....*...
gi 17569239   326 NKF-GYNVAFQNGTVVTY 342
Cdd:pfam01112 291 GMYrAYHTGDGIGDVLIY 308
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 16-322 8.30e-57

Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];


Pssm-ID: 441055  Cd Length: 305  Bit Score: 187.24  E-value: 8.30e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  16 GTINDDSL-PMVITTWgsdgfKKATKNAVDAtllGGRMfgLVEGLSTCEALQC---------DTTVGYGGSPDENGETCL 85
Cdd:COG1446  15 GTIARSAMtPEVEAAY-----RAGLRAALEA---GYAV--LEAGGSALDAVEAavrvleddpLFNAGKGAVLTRDGTVEL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  86 DSLVIDADGMRVGAVANLHRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGFKEEDLSTEETKSwisKWKTekcqpnf 165
Cdd:COG1446  85 DASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEK---RWKQ------- 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 166 WKNVSpdpssscgpyktnpltksmryyslvnqsdEAGYLVEKTNHDTIGMVVRDTENIFSAGTSSNGARFKIPGRVGDSP 245
Cdd:COG1446 155 WKKAL-----------------------------EYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSP 205

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17569239 246 IPGAGAYA-NKFGGAAATGDGDVMMRFLPSFFAVTQMELGTKPSKAAYKAITRILKVFpKFSGAVVAMNVKGRIGASC 322
Cdd:COG1446 206 IIGAGTYAdNEVGAVSATGHGEYFIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPF 282
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 72-322 1.08e-36

L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2 enzymes. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue. The family is circularly permuted relative to other NTN-hydrolase families.


Pssm-ID: 271334  Cd Length: 249  Bit Score: 133.08  E-value: 1.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  72 GYGGSPDENGETCLDSLVIDADGMRVGAVANLHRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGfkeedlsteetks 151
Cdd:cd04512  60 GRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLARAVMEKTPHVLLVGEGAERFAREHG------------- 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 152 wiskwktekcqpnfwknvspdpssscgpyktnpltksmryyslvnqsdeagylvektnHDTIGMVVRDTENIFSAGTSSN 231
Cdd:cd04512 127 ----------------------------------------------------------HGTVGAVARDAQGNLAAATSTG 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 232 GARFKIPGRVGDSPIPGAGAYA-NKFGGAAATGDGDVMMRFLPSFFAVTQMELGTKPSKAAYKAItRILKVFPKFSGAVV 310
Cdd:cd04512 149 GMVNKRPGRVGDSPIIGAGTYAdNETGAVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAEAAI-DYLRRRVGGEGGLI 227

                       250
                ....*....|..
gi 17569239 311 AMNVKGRIGASC 322
Cdd:cd04512 228 VVDPDGRLGAAH 239
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 72-321 3.19e-34

Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; The wider family of Asparaginase 2-like enzymes includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue.


Pssm-ID: 271341  Cd Length: 251  Bit Score: 126.54  E-value: 3.19e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  72 GYGGSPDENGETCLDSLVIDADGMRVGAVANLHRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGFkeedlsteetks 151
Cdd:cd14950  60 GVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIRLARKVMEKTDHVLIVGEGADELAKRLGG------------ 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 152 wiskwktekcqpnfwknvspdpssscgpyktnpltksmryyslvnqsdeagylvektnhDTIGMVVRDTENIFSAGTSSN 231
Cdd:cd14950 128 -----------------------------------------------------------DTVGAVALDKDGNLAAATSTG 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 232 GARFKIPGRVGDSPIPGAGAYANKFGGAAATGDGDVMMRFLPSFFAVTQMELGTKPSKAAYKAITRILKVFPKFSGAVVA 311
Cdd:cd14950 149 GVWLKLPGRVGDSPIPGAGFYATNGVAVSATGIGEVIIRSLPALRADELVSMGGDIEEAVRAVVNKVTETFGKDTAGIIG 228

                       250
                ....*....|
gi 17569239 312 MNVKGRIGAS 321
Cdd:cd14950 229 IDARGNIAAA 238
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 72-322 1.02e-30

Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the L-Asparaginase type 2-like enzymes. The wider family includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2 enzymes. The proenzymes undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue. ASRGL1, or asparaginase-like 1, has been cloned from mammalian testis cDNA libraries. It has been identified as a sperm antigen that may induce the production of autoantibodies following obstruction of the male reproductive tract, e.g. vasectomy.


Pssm-ID: 271338  Cd Length: 289  Bit Score: 118.06  E-value: 1.02e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  72 GYGGSPDENGETCLDSLVIDADGMRVGAVANLHRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGFKEEDLSTEETKS 151
Cdd:cd04702  62 GYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTER 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 152 WISKWKTEKCQPNfwknvspdpssscgpyktNPLTKSMRyyslvnqsdeagylvektNHDTIGMVVRDTE-NIfSAGTSS 230
Cdd:cd04702 142 ARERLEKFKKEKG------------------ANVEDTQR------------------GHGTVGAVAIDCEgNV-ACATST 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 231 NGARFKIPGRVGDSPIPGAGAYA-NKFGGAAATGDGDVMMRFLPSFFAVTQMELGTKPSKAAYKAITRILKVFpKFSGAV 309
Cdd:cd04702 185 GGITNKMVGRVGDSPIIGSGGYAdNLVGAVSTTGHGESIMKVNLARLILFHMEQGKTAEEAAELALAYMKSRV-KGLGGL 263

                       250
                ....*....|...
gi 17569239 310 VAMNVKGRIGASC 322
Cdd:cd04702 264 IVVSKTGDWGAKF 276
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 72-298 1.13e-28

Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; The wider family of Asparaginase 2-like enzymes includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue.


Pssm-ID: 271339  Cd Length: 243  Bit Score: 111.58  E-value: 1.13e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  72 GYGGSPDENGETCLDSLVIDADGmRVGAVANLHRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGFkeedlsteetks 151
Cdd:cd04703  56 GTGSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVARAVMETSPHVLLAGDGAVRFARRLGY------------ 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 152 wiskwktekcqpnfwknvsPDPssscgpyktnpltksmryyslvnqsdeagylvektnHDTIGMVVRDTEnIFSAGTSSN 231
Cdd:cd04703 123 -------------------PDG------------------------------------CDTVGAVARDGG-KFAAAVSTG 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17569239 232 GARFKIPGRVGDSPIPGAGAYANKFGGAAATGDGDVMMRFLPSFFAVTQMELGTKPSKAAYKAITRI 298
Cdd:cd04703 147 GTSPALRGRVGDVPIIGAGFYAGPKGAVAATGIGEEIAKRLLARRVYRWIETGLSLQAAAQRAIDEF 213
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 78-318 1.65e-22

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 96.17  E-value: 1.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239   78 DENGEtcLDSLVIDADGMRVGAVANLHRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGFKEedlsteetkswiskwk 157
Cdd:PRK10226  77 DETHE--LDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMER---------------- 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  158 tekcqpnfwknVSPDPSSScgPYKTNPLTKSmRYYSLVNQSDEAGYLVEKTNHDTIGMVVRDTENIFSAGTSSNGARFKI 237
Cdd:PRK10226 139 -----------VSPEIFST--PLRYEQLLAA-RAEGATVLDHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKL 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  238 PGRVGDSPIPGAGAYANKFGGAAA-TGDGDVMMRFLPSFFAVTQMELGtkpSKAAYKAITR-ILKVFPKF--SGAVVAMN 313
Cdd:PRK10226 205 PGRVGDSPLVGAGCYANNASVAVScTGTGEVFIRALAAYDIAALMDYG---GLSLAEACERvVMEKLPALggSGGLIAID 281


                 ....*
gi 17569239  314 VKGRI 318
Cdd:PRK10226 282 HEGNV 286
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 72-318 3.92e-22

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 95.16  E-value: 3.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239   72 GYGGSPDENGETCLDSLVIDADGMRVGAVANLHRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGFKEEDLSTEETKS 151
Cdd:PLN02689  68 GRGSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEE 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  152 WISKWKTEKcqpnfwknvspdpssscgpyKTNPLTKSMRYYSLVNQSDEAGYLVEKTNHDTIGMVVRDTENIFSAGTSSN 231
Cdd:PLN02689 148 NVERLKQAK--------------------EANSVQFDYRIPLDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTG 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  232 GARFKIPGRVGDSPIPGAGAYANKFGGAAATGDGDVMMRFLPSFFAVTQMEL-GTKPSKAAYKAITRILkvfPKFSGAVV 310
Cdd:PLN02689 208 GLVNKMVGRIGDTPIIGAGTYANHLCAVSATGKGEAIIRGTVARDVAAVMEYkGLPLQEAVDYVIKERL---PEGPAGLI 284


                 ....*...
gi 17569239  311 AMNVKGRI 318
Cdd:PLN02689 285 AVSATGEV 292
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 72-318 1.65e-21

Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzyme undergoes an autoproteolytic cleavage into alpha and beta subunits to expose a threonine residue which becomes the N-terminal residue of the beta subunit. The threonine residue plays a central role in hydrolase activity. Some asparaginases can also hydrolyze L-glutamine and are termed glutaminase-asparaginase. This is a member of the Ntn-hydrolase superfamily, and this subfamily covers mostly bacterial and fungal enzymes.


Pssm-ID: 271337  Cd Length: 264  Bit Score: 92.52  E-value: 1.65e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  72 GYGGSPDENGETCLDSLVIDADGMRVGAVANLHRIRDAARVAWGVMNFTKHTLLVGESATQFAKTLGfkeedlsteetks 151
Cdd:cd04701  65 GKGAVFTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQG------------- 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 152 wiskwktekcqpnfwknvspdpssscgpyktnpltksmryyslvnqsdeagylVEKTNHDTIGMVVRDTENIFSAGTSSN 231
Cdd:cd04701 132 -----------------------------------------------------LELVPQGTVGAVALDSDGNLAAATSTG 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 232 GARFKIPGRVGDSPIPGAGAYANKFG-GAAATGDGDVMMRFLPSFFAVTQMELGTKP-SKAAYKAITRILKVfPKFSGAV 309
Cdd:cd04701 159 GLTNKLPGRIGDTPIIGAGFWAEEWAvAVSGTGNGDSFIRVAAARDVAARMRYKGLSlAEAAKEVVGPGGEL-GEGEGGI 237


                ....*....
gi 17569239 310 VAMNVKGRI 318
Cdd:cd04701 238 IAIDARGNV 246
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 89-265 3.07e-15

Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; The wider family of Asparaginase 2-like enzymes includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue.


Pssm-ID: 271340  Cd Length: 280  Bit Score: 74.95  E-value: 3.07e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  89 VIDADGMRVGAVANLHRIRDAARVAWGVMNFtKHTLLVGESATQFAKTLGFkeedlsteetkswiskwktekcqPNFwkn 168
Cdd:cd14949  80 LMDGQTQRFSGVINIENVKNPIEVAQKLQQE-DDRVLSGEGATEFARENGF-----------------------PEY--- 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 169 vspdpssscgpyktNPLTKSMR--YYSLVNQSDEAGylvektnhdTIGMVVRDTENIFSAGTSSNGARFKIPGRVGDSPI 246
Cdd:cd14949 133 --------------NPETPQRRqeYEEKKLKSGGTG---------TVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSAT 189

                       170
                ....*....|....*....
gi 17569239 247 PgAGAYANKFGGAAATGDG 265
Cdd:cd14949 190 V-AGNYANAFAGVSCTGIG 207
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 69-270 1.56e-10

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 62.19  E-value: 1.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239   69 TTVGYGGSPDENGETCLDSLVIDADGMRVGAVANLHRIRDAARVAwgvMNFTKHT-------------LLVGESATQFAK 135
Cdd:PLN02937  70 TNAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIA---ALLAKEQmmgssllgrippmFLVGEGARQWAK 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  136 TLGfkeedLSTEETKSWISKWKTEKCQPNFWKN-----VSPDPSSSCGPYKTNPLTK------SMRYYSLVNQSDEAGYL 204
Cdd:PLN02937 147 SKG-----IDLPETVEEAEKWLVTERAKEQWKKyktmlASAIAKSSCDSQSTSKLSEleaprsNPSNGTGGGQSSMCTAS 221

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17569239  205 VEKTNHDTIGMVVRDTENIFSAGTSSNGARFKIPGRVGDSPIPGAGAYANK---FG-----GAAATGDGDVMMR 270
Cdd:PLN02937 222 DEDCIMDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSkgpFGapfivGCCVSGAGEYLMR 295
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 72-270 1.90e-06

Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the mix lineage leukemia (MLL) nuclear protein and transcription factor TFIIA. Taspase1 is a threonine aspartase, a member of the Ntn hydrolase superfamily and the type 2 asparaginase family. A threonine residue acts as the active site nucleophile in both endopeptidease and protease activities to cleave polypeptide substrates after an aspartate residue. The Taspase1 proenzyme undergoes autoproteolysis into alpha and beta subunits. The N-terminal residue of the beta subunit is a threonine which is the active catalytic residue. The active enzyme is a heterotetramer.


Pssm-ID: 271336  Cd Length: 313  Bit Score: 48.81  E-value: 1.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239  72 GYGGSPDENGE-TClDSLVIDADGMRVGAVANLHRIRDAARVAWGVMN--FTKHTL-------LVGESATQFAKTLGFke 141
Cdd:cd04514  61 GYGSNLTEDGTvEC-DASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKeqRKPLSLgrvppmfLVGEGAREWAKSKGI-- 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17569239 142 edlsteetkswiskwktekcqpnfwknvspdpssscgpyktnpltksmryyslvnqsdeagylvektNHDTIGMVVRDTE 221
Cdd:cd04514 138 -------------------------------------------------------------------ITDTVGAIAIDLY 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17569239 222 NIFSAGTSSNGARFKIPGRVGDSPIPGAGAYANKFG-------GAAATGDGDVMMR 270
Cdd:cd04514 151 GNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDpddktsvAVVTSGTGEHIAT 206
 
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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