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Conserved domains on  [gi|15214539|gb|AAH12392|]
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Aspartylglucosaminidase [Homo sapiens]

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 ...
 29-332 1.01e-170

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: 476.28  E-value: 1.01e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  29 LVVNTWPFKNATEAAWRALASGGSALDAVESGCAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRI 108
Cdd:cd04513   1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 109 KNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTSASQALHSDWLARNCQPNYWRNVIPDPSKYCGPYKPPGIL 188
Cdd:cd04513  81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSCSSPKAPSRS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 189 KQDIPIHketeddrGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLP 268
Cdd:cd04513 161 ESAIPED-------NHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15214539 269 SYQAVEYMRRGEDPTIACQKVISRIQKHFP-EFFGAVICANVTGSYGAACNKlstfTQFSFMVYN 332
Cdd:cd04513 234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 29-332 1.01e-170

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: 476.28  E-value: 1.01e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  29 LVVNTWPFKNATEAAWRALASGGSALDAVESGCAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRI 108
Cdd:cd04513   1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 109 KNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTSASQALHSDWLARNCQPNYWRNVIPDPSKYCGPYKPPGIL 188
Cdd:cd04513  81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSCSSPKAPSRS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 189 KQDIPIHketeddrGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLP 268
Cdd:cd04513 161 ESAIPED-------NHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15214539 269 SYQAVEYMRRGEDPTIACQKVISRIQKHFP-EFFGAVICANVTGSYGAACNKlstfTQFSFMVYN 332
Cdd:cd04513 234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
35-326 1.14e-113

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 332.24  E-value: 1.14e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539    35 PFKNATEAAWRALASGGSALDAVESGCAMCErEQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGV 114
Cdd:pfam01112  24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539   115 ARKVLEHTTHTLLVGESATTFAQSMGF---INEDLSTSASQALHSDWLARNCQPNYWRNVIPDPSKYCGpykppgilkqd 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLervPPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECG----------- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539   192 ipihketedDRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQ 271
Cdd:pfam01112 172 ---------DSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYD 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15214539   272 AVEYMRRGEDPTIACQKVISRIQKHFPEfFGAVICANVTGSYGAACNKLSTFTQF 326
Cdd:pfam01112 243 IVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFNTEGMYRAY 296
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 28-318 2.23e-71

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 224.22  E-value: 2.23e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  28 PLVVNTWPF--KNATEAAWRALASGGSALDAVESGCAMCEReqcDG--SVGFGGSPDELGETTLDAMIMDGTTMDVGAVG 103
Cdd:COG1446  24 PEVEAAYRAglRAALEAGYAVLEAGGSALDAVEAAVRVLED---DPlfNAGKGAVLTRDGTVELDASIMDGATLRAGAVA 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 104 DLRRIKNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTSASQALHSDWLARNcqpnywrnvipdpsKYcgpyk 183
Cdd:COG1446 101 GVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKAL--------------EY----- 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 184 ppgilkqdipihKETEDDRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYaddtagaaaaTGN---- 259
Cdd:COG1446 162 ------------KPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTY----------ADNevga 219

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15214539 260 ------GDILMRFLPSYQAVEYMRRGEDPTIACQKVISRIQKHFpEFFGAVICANVTGSYGAACN 318
Cdd:COG1446 220 vsatghGEYFIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPFN 283
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 41-290 1.74e-26

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 106.96  E-value: 1.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539   41 EAAWRALASGGSALDAVESGCAMCEreQC---DGSVGFGGSPDELGEttLDAMIMDGTTMDVGAVGDLRRIKNAIGVARK 117
Cdd:PRK10226  37 ETGQKMLEAGESALDVVTEAVRLLE--ECplfNAGIGAVFTRDETHE--LDACVMDGNTLKAGAVAGVSHLRNPVLAARL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  118 VLEHTTHTLLVGESATTFAQSMGFINEDLSTSASQALHSDWLARncqpnywrnvipdpskycgpyKPPGILKQD---IPI 194
Cdd:PRK10226 113 VMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAA---------------------RAEGATVLDhsgAPL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  195 HKETEddrgHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQAVE 274
Cdd:PRK10226 172 DEKQK----MGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAA 247

                        250
                 ....*....|....*..
gi 15214539  275 YMRRGE-DPTIACQKVI 290
Cdd:PRK10226 248 LMDYGGlSLAEACERVV 264
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 29-332 1.01e-170

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: 476.28  E-value: 1.01e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  29 LVVNTWPFKNATEAAWRALASGGSALDAVESGCAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRI 108
Cdd:cd04513   1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 109 KNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTSASQALHSDWLARNCQPNYWRNVIPDPSKYCGPYKPPGIL 188
Cdd:cd04513  81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSCSSPKAPSRS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 189 KQDIPIHketeddrGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLP 268
Cdd:cd04513 161 ESAIPED-------NHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15214539 269 SYQAVEYMRRGEDPTIACQKVISRIQKHFP-EFFGAVICANVTGSYGAACNKlstfTQFSFMVYN 332
Cdd:cd04513 234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
35-326 1.14e-113

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 332.24  E-value: 1.14e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539    35 PFKNATEAAWRALASGGSALDAVESGCAMCErEQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGV 114
Cdd:pfam01112  24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539   115 ARKVLEHTTHTLLVGESATTFAQSMGF---INEDLSTSASQALHSDWLARNCQPNYWRNVIPDPSKYCGpykppgilkqd 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLervPPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECG----------- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539   192 ipihketedDRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQ 271
Cdd:pfam01112 172 ---------DSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYD 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15214539   272 AVEYMRRGEDPTIACQKVISRIQKHFPEfFGAVICANVTGSYGAACNKLSTFTQF 326
Cdd:pfam01112 243 IVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFNTEGMYRAY 296
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 28-318 2.23e-71

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 224.22  E-value: 2.23e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  28 PLVVNTWPF--KNATEAAWRALASGGSALDAVESGCAMCEReqcDG--SVGFGGSPDELGETTLDAMIMDGTTMDVGAVG 103
Cdd:COG1446  24 PEVEAAYRAglRAALEAGYAVLEAGGSALDAVEAAVRVLED---DPlfNAGKGAVLTRDGTVELDASIMDGATLRAGAVA 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 104 DLRRIKNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTSASQALHSDWLARNcqpnywrnvipdpsKYcgpyk 183
Cdd:COG1446 101 GVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKAL--------------EY----- 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 184 ppgilkqdipihKETEDDRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYaddtagaaaaTGN---- 259
Cdd:COG1446 162 ------------KPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTY----------ADNevga 219

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15214539 260 ------GDILMRFLPSYQAVEYMRRGEDPTIACQKVISRIQKHFpEFFGAVICANVTGSYGAACN 318
Cdd:COG1446 220 vsatghGEYFIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPFN 283
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 39-318 4.82e-52

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: 172.75  E-value: 4.82e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  39 ATEAAWRALASGGSALDAVESGCAMCEReqcDG--SVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVAR 116
Cdd:cd04512  26 ALEAGREVLEKGGSALDAVEAAVRLLED---DPlfNAGRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLAR 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 117 KVLEHTTHTLLVGESATTFAQsmgfinedlstsasqalhsdwlarncqpnywrnvipdpskycgpykppgilkqdipihk 196
Cdd:cd04512 103 AVMEKTPHVLLVGEGAERFAR----------------------------------------------------------- 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 197 etedDRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQAVEYM 276
Cdd:cd04512 124 ----EHGHGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLV 199

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15214539 277 RRGEDPTIACQKVISRIQKHfPEFFGAVICANVTGSYGAACN 318
Cdd:cd04512 200 EFGGSAQEAAEAAIDYLRRR-VGGEGGLIVVDPDGRLGAAHN 240
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 37-318 1.06e-45

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: 156.20  E-value: 1.06e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  37 KNATEAAWRALASGgSALDAVESGCAMCEreqcDGSV---GFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIG 113
Cdd:cd14950  25 REALERGYEALRRG-SALEAVVEAVAYME----DSGVfnaGVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIR 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 114 VARKVLEHTTHTLLVGESATTFAQSMGFinedlstsasqalhsdwlarncqpnywrnvipdpskycgpykppgilkqdip 193
Cdd:cd14950 100 LARKVMEKTDHVLIVGEGADELAKRLGG---------------------------------------------------- 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 194 ihketeddrghDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYaDDTAGAAAATGNGDILMRFLPSYQAV 273
Cdd:cd14950 128 -----------DTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFY-ATNGVAVSATGIGEVIIRSLPALRAD 195

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15214539 274 EYMRRGEDPTIACQKVISRIQKHFPEFFGAVICANVTGSYGAACN 318
Cdd:cd14950 196 ELVSMGGDIEEAVRAVVNKVTETFGKDTAGIIGIDARGNIAAAFN 240
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 37-318 2.07e-41

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: 146.18  E-value: 2.07e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  37 KNATEAAWRALASGGSALDAVESG-CAMCEREQCDGsvGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVA 115
Cdd:cd04702  26 KRAARAGYSVLKAGGSALDAVEAAvRALEDDPVFNA--GYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLA 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 116 RKVLEHTTHTLLVGESATTFAQSMGF---INEDLSTSASQALHSDWLARncqpnywrnvipdpskycgpykppgilkqdi 192
Cdd:cd04702 104 RLVMEKTPHCFLTGRGANKFAEEMGIpqvPPESLVTERARERLEKFKKE------------------------------- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 193 PIHKETEDDRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQA 272
Cdd:cd04702 153 KGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNLARLI 232

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15214539 273 VEYMRRGEDPTIACQKVI----SRIQKHfpeffGAVICANVTGSYGAACN 318
Cdd:cd04702 233 LFHMEQGKTAEEAAELALaymkSRVKGL-----GGLIVVSKTGDWGAKFT 277
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 39-290 1.23e-32

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: 122.18  E-value: 1.23e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  39 ATEAAWRALASGGSALDAVESgcAMCEREQC------DGSVgfggsPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAI 112
Cdd:cd04701  31 ALEAGYAVLASGGSALDAVTA--AVRLLEDCplfnagKGAV-----FTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPI 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 113 GVARKVLEHTTHTLLVGESATTFAQSMGfinedlstsasqalhsdwlarncqpnywrnvipdpskycGPYKPPGilkqdi 192
Cdd:cd04701 104 LLARAVLEKSPHVLLSGEGAEEFAREQG---------------------------------------LELVPQG------ 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 193 pihketeddrghdTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQA 272
Cdd:cd04701 139 -------------TVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWAVAVSGTGNGDSFIRVAAARDV 205

                       250
                ....*....|....*....
gi 15214539 273 VEYMR-RGEDPTIACQKVI 290
Cdd:cd04701 206 AARMRyKGLSLAEAAKEVV 224
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 37-319 1.03e-27

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: 108.50  E-value: 1.03e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  37 KNATEAAWRALASGGSALDAVESGCAMCEREQCDGSvGFGGSPDELGETTLDAMIMDGTTmDVGAVGDLRRIKNAIGVAR 116
Cdd:cd04703  20 ERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNA-GTGSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVAR 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 117 KVLEHTTHTLLVGESATTFAQSMGFinedlstsasqalhsdwlarncqpnywrnvipdpskycgpykppgilkqdipihk 196
Cdd:cd04703  98 AVMETSPHVLLAGDGAVRFARRLGY------------------------------------------------------- 122

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 197 etedDRGHDTIGMVV-IHktGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGnGDILMRFLPSYQAVEY 275
Cdd:cd04703 123 ----PDGCDTVGAVArDG--GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKGAVAATGI-GEEIAKRLLARRVYRW 195

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15214539 276 MRRGEDPTIACQKVISRiqkhFPEFFGA-VICANVTGSYGAACNK 319
Cdd:cd04703 196 IETGLSLQAAAQRAIDE----FDDGVAVgVIAVSRRGEAGIASNT 236
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 41-290 1.74e-26

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 106.96  E-value: 1.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539   41 EAAWRALASGGSALDAVESGCAMCEreQC---DGSVGFGGSPDELGEttLDAMIMDGTTMDVGAVGDLRRIKNAIGVARK 117
Cdd:PRK10226  37 ETGQKMLEAGESALDVVTEAVRLLE--ECplfNAGIGAVFTRDETHE--LDACVMDGNTLKAGAVAGVSHLRNPVLAARL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  118 VLEHTTHTLLVGESATTFAQSMGFINEDLSTSASQALHSDWLARncqpnywrnvipdpskycgpyKPPGILKQD---IPI 194
Cdd:PRK10226 113 VMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAA---------------------RAEGATVLDhsgAPL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  195 HKETEddrgHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQAVE 274
Cdd:PRK10226 172 DEKQK----MGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAA 247

                        250
                 ....*....|....*..
gi 15214539  275 YMRRGE-DPTIACQKVI 290
Cdd:PRK10226 248 LMDYGGlSLAEACERVV 264
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 46-246 9.90e-24

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 99.40  E-value: 9.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539   46 ALASGGSALDAVEsgCAMCEREQC-DGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVARKVLEHTTH 124
Cdd:PLN02689  41 ALRSSLPALDVVE--LVVRELENDpLFNAGRGSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPH 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  125 TLLVGESATTFAQSMG--------FINEDLSTSASQALHsdwlARNCQPNYwRNVIPDPSKYCGPYKPpgilkqdipihk 196
Cdd:PLN02689 119 IYLAFDGAEAFARQQGvetvdnsyFITEENVERLKQAKE----ANSVQFDY-RIPLDKPAKAAALAAD------------ 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15214539  197 eteDDRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAY 246
Cdd:PLN02689 182 ---GDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTY 228
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 37-246 1.11e-22

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: 96.57  E-value: 1.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  37 KNATEAAWRALASGGSALDAVESGCAMCEREQCDGSvGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVAR 116
Cdd:cd04514  25 KRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNA-GYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLAR 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 117 KVLEHTTH---------TLLVGESATTFAQSMGFINedlstsasqalhsdwlarncqpnywrnvipdpskycgpykppgi 187
Cdd:cd04514 104 LLLKEQRKplslgrvppMFLVGEGAREWAKSKGIIT-------------------------------------------- 139

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15214539 188 lkqdipihketeddrghDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAY 246
Cdd:cd04514 140 -----------------DTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCW 181
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 41-246 4.60e-18

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: 83.04  E-value: 4.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  41 EAAWRALASGgSALDAVESGCAMCERE-----------QCDGSVgfggspdelgetTLDAMIMDGTTMDVGAVGDLRRIK 109
Cdd:cd14949  32 EEVYEYLKSH-SALEAVVYAVSLLEDDplfnagtgsqiQSDGQI------------RMSASLMDGQTQRFSGVINIENVK 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 110 NAIGVARKVLEHTtHTLLVGESATTFAQSMGFinedlstsasqalhsdwlarncqpnywrnvipdpskycGPYKPPgilk 189
Cdd:cd14949  99 NPIEVAQKLQQED-DRVLSGEGATEFARENGF--------------------------------------PEYNPE---- 135

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539 190 QDIPIHKETEDDR---GHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPgAGAY 246
Cdd:cd14949 136 TPQRRQEYEEKKLksgGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNY 194
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 37-246 3.59e-17

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 81.83  E-value: 3.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539   37 KNATEAAWRALASG-GSALDAVESGCAMCEREQCDGSvGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVA 115
Cdd:PLN02937  36 RRACLAAAAILRQGsGGCIDAVSAAIQVLEDDPSTNA-GRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  116 RKVLEHTTH----------TLLVGESATTFAQSMGFINEDLSTSASQalhsdWLARNCQPNYWR-------NVIP----- 173
Cdd:PLN02937 115 ALLAKEQMMgssllgrippMFLVGEGARQWAKSKGIDLPETVEEAEK-----WLVTERAKEQWKkyktmlaSAIAksscd 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15214539  174 --DPSKYCGPYKPPGILKQDIPIHKET-----EDDRGHDTIGMVVIHKTGHIAAGTSTNGIKFKIHGRVGDSPIPGAGAY 246
Cdd:PLN02937 190 sqSTSKLSELEAPRSNPSNGTGGGQSSmctasDEDCIMDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCW 269
 
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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