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Conserved domains on  [gi|285002253|ref|NP_001165459|]
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N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase isoform 2 precursor [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 ...
 29-322 8.05e-160

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: 448.16  E-value: 8.05e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  29 LVVNTWPFKNATEAAWRALASGGSALDAVESGCAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRI 108
Cdd:cd04513    1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 109 KNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTTASQALHSDWLARNCQPNYWRNVIPDPSKYCGPYKPPGIL 188
Cdd:cd04513   81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSCSSPKAPSRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 189 KQDIPIHketeddrGHDTIGMVVIHKTGHIAAGTSTNG----------DSPIPGAGAYADDTAGAAAATGNGDILMRFLP 258
Cdd:cd04513  161 ESAIPED-------NHDTIGMIALDANGNIAAGTSTSGaafkipgrvgDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285002253 259 SYQAVEYMRRGEDPTIACQKVISRIQKHFP-EFFGAVICANVTGSYGAACNKlstfTQFSFMVYN 322
Cdd:cd04513  234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 29-322 8.05e-160

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: 448.16  E-value: 8.05e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  29 LVVNTWPFKNATEAAWRALASGGSALDAVESGCAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRI 108
Cdd:cd04513    1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 109 KNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTTASQALHSDWLARNCQPNYWRNVIPDPSKYCGPYKPPGIL 188
Cdd:cd04513   81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSCSSPKAPSRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 189 KQDIPIHketeddrGHDTIGMVVIHKTGHIAAGTSTNG----------DSPIPGAGAYADDTAGAAAATGNGDILMRFLP 258
Cdd:cd04513  161 ESAIPED-------NHDTIGMIALDANGNIAAGTSTSGaafkipgrvgDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285002253 259 SYQAVEYMRRGEDPTIACQKVISRIQKHFP-EFFGAVICANVTGSYGAACNKlstfTQFSFMVYN 322
Cdd:cd04513  234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
35-316 1.39e-103

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 306.05  E-value: 1.39e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253   35 PFKNATEAAWRALASGGSALDAVESGCAMCErEQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGV 114
Cdd:pfam01112  24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  115 ARKVLEHTTHTLLVGESATTFAQSMGF---INEDLSTTASQALHSDWLARNCQPNYWRNVIPDPSKYCGpykppgilkqd 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLervPPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECG----------- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  192 ipihketedDRGHDTIGMVVIHKTGHIAAGTSTNG----------DSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQ 261
Cdd:pfam01112 172 ---------DSKRGTVGAVALDSEGNLAAGTSTGGmtnkrpgrvgDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYD 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 285002253  262 AVEYMRRGEDPTIACQKVISRIQKHFPEfFGAVICANVTGSYGAACNKLSTFTQF 316
Cdd:pfam01112 243 IVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFNTEGMYRAY 296
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 28-308 5.56e-62

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 199.56  E-value: 5.56e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  28 PLVVNTWPF--KNATEAAWRALASGGSALDAVESGCAMCEReqcDG--SVGFGGSPDELGETTLDAMIMDGTTMDVGAVG 103
Cdd:COG1446   24 PEVEAAYRAglRAALEAGYAVLEAGGSALDAVEAAVRVLED---DPlfNAGKGAVLTRDGTVELDASIMDGATLRAGAVA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 104 DLRRIKNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTTASQALHSDWLARncqpnywrnvipdpSKYcgpyk 183
Cdd:COG1446  101 GVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKA--------------LEY----- 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 184 ppgilkqdipihKETEDDRGHDTIGMVVIHKTGHIAAGTSTNG----------DSPIPGAGAYaddtagaaaaTGN---- 249
Cdd:COG1446  162 ------------KPIINERKHGTVGAVALDANGNLAAATSTGGmtnkrpgrvgDSPIIGAGTY----------ADNevga 219

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285002253 250 ------GDILMRFLPSYQAVEYMRRGEDPTIACQKVISRIQKHFpEFFGAVICANVTGSYGAACN 308
Cdd:COG1446  220 vsatghGEYFIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPFN 283
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 41-280 1.77e-20

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 90.01  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  41 EAAWRALASGGSALDAVESGCAMCEreQC---DGSVGFGGSPDELGEttLDAMIMDGTTMDVGAVGDLRRIKNAIGVARK 117
Cdd:PRK10226  37 ETGQKMLEAGESALDVVTEAVRLLE--ECplfNAGIGAVFTRDETHE--LDACVMDGNTLKAGAVAGVSHLRNPVLAARL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 118 VLEHTTHTLLVGESATTFA--QSMGFINEDLSTTasqalhsdwlarncqpnywrnvipdPSKYCG--PYKPPGILKQD-- 191
Cdd:PRK10226 113 VMEQSPHVMMIGEGAENFAfaHGMERVSPEIFST-------------------------PLRYEQllAARAEGATVLDhs 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 192 -IPIHKETEddrgHDTIGMVVIHKTGHIAAGTSTN----------GDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSY 260
Cdd:PRK10226 168 gAPLDEKQK----MGTVGAVALDLDGNLAAATSTGgmtnklpgrvGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAY 243

                        250       260
                 ....*....|....*....|.
gi 285002253 261 QAVEYMRRGE-DPTIACQKVI 280
Cdd:PRK10226 244 DIAALMDYGGlSLAEACERVV 264
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 29-322 8.05e-160

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: 448.16  E-value: 8.05e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  29 LVVNTWPFKNATEAAWRALASGGSALDAVESGCAMCEREQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRI 108
Cdd:cd04513    1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 109 KNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTTASQALHSDWLARNCQPNYWRNVIPDPSKYCGPYKPPGIL 188
Cdd:cd04513   81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSCSSPKAPSRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 189 KQDIPIHketeddrGHDTIGMVVIHKTGHIAAGTSTNG----------DSPIPGAGAYADDTAGAAAATGNGDILMRFLP 258
Cdd:cd04513  161 ESAIPED-------NHDTIGMIALDANGNIAAGTSTSGaafkipgrvgDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285002253 259 SYQAVEYMRRGEDPTIACQKVISRIQKHFP-EFFGAVICANVTGSYGAACNKlstfTQFSFMVYN 322
Cdd:cd04513  234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
35-316 1.39e-103

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 306.05  E-value: 1.39e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253   35 PFKNATEAAWRALASGGSALDAVESGCAMCErEQCDGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGV 114
Cdd:pfam01112  24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  115 ARKVLEHTTHTLLVGESATTFAQSMGF---INEDLSTTASQALHSDWLARNCQPNYWRNVIPDPSKYCGpykppgilkqd 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLervPPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECG----------- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  192 ipihketedDRGHDTIGMVVIHKTGHIAAGTSTNG----------DSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQ 261
Cdd:pfam01112 172 ---------DSKRGTVGAVALDSEGNLAAGTSTGGmtnkrpgrvgDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYD 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 285002253  262 AVEYMRRGEDPTIACQKVISRIQKHFPEfFGAVICANVTGSYGAACNKLSTFTQF 316
Cdd:pfam01112 243 IVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFNTEGMYRAY 296
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 28-308 5.56e-62

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 199.56  E-value: 5.56e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  28 PLVVNTWPF--KNATEAAWRALASGGSALDAVESGCAMCEReqcDG--SVGFGGSPDELGETTLDAMIMDGTTMDVGAVG 103
Cdd:COG1446   24 PEVEAAYRAglRAALEAGYAVLEAGGSALDAVEAAVRVLED---DPlfNAGKGAVLTRDGTVELDASIMDGATLRAGAVA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 104 DLRRIKNAIGVARKVLEHTTHTLLVGESATTFAQSMGFINEDLSTTASQALHSDWLARncqpnywrnvipdpSKYcgpyk 183
Cdd:COG1446  101 GVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKA--------------LEY----- 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 184 ppgilkqdipihKETEDDRGHDTIGMVVIHKTGHIAAGTSTNG----------DSPIPGAGAYaddtagaaaaTGN---- 249
Cdd:COG1446  162 ------------KPIINERKHGTVGAVALDANGNLAAATSTGGmtnkrpgrvgDSPIIGAGTY----------ADNevga 219

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 285002253 250 ------GDILMRFLPSYQAVEYMRRGEDPTIACQKVISRIQKHFpEFFGAVICANVTGSYGAACN 308
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 ...
 39-308 1.10e-43

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: 150.41  E-value: 1.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  39 ATEAAWRALASGGSALDAVESGCAMCEReqcDG--SVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVAR 116
Cdd:cd04512   26 ALEAGREVLEKGGSALDAVEAAVRLLED---DPlfNAGRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLAR 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 117 KVLEHTTHTLLVGESATTFAQsmgfinedlsttasqalhsdwlarncqpnywrnvipdpskycgpykppgilkqdipihk 196
Cdd:cd04512  103 AVMEKTPHVLLVGEGAERFAR----------------------------------------------------------- 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 197 etedDRGHDTIGMVVIHKTGHIAAGTSTNG----------DSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQAVEYM 266
Cdd:cd04512  124 ----EHGHGTVGAVARDAQGNLAAATSTGGmvnkrpgrvgDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLV 199

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 285002253 267 RRGEDPTIACQKVISRIQKHfPEFFGAVICANVTGSYGAACN 308
Cdd:cd04512  200 EFGGSAQEAAEAAIDYLRRR-VGGEGGLIVVDPDGRLGAAHN 240
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 37-308 2.40e-38

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: 136.56  E-value: 2.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  37 KNATEAAWRALASGgSALDAVESGCAMCEreqcDGSV---GFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIG 113
Cdd:cd14950   25 REALERGYEALRRG-SALEAVVEAVAYME----DSGVfnaGVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 114 VARKVLEHTTHTLLVGESATTFAQSMGFinedlsttasqalhsdwlarncqpnywrnvipdpskycgpykppgilkqdip 193
Cdd:cd14950  100 LARKVMEKTDHVLIVGEGADELAKRLGG---------------------------------------------------- 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 194 ihketeddrghDTIGMVVIHKTGHIAAGTSTN----------GDSPIPGAGAYaDDTAGAAAATGNGDILMRFLPSYQAV 263
Cdd:cd14950  128 -----------DTVGAVALDKDGNLAAATSTGgvwlklpgrvGDSPIPGAGFY-ATNGVAVSATGIGEVIIRSLPALRAD 195

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 285002253 264 EYMRRGEDPTIACQKVISRIQKHFPEFFGAVICANVTGSYGAACN 308
Cdd:cd14950  196 ELVSMGGDIEEAVRAVVNKVTETFGKDTAGIIGIDARGNIAAAFN 240
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 37-308 7.50e-35

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: 128.46  E-value: 7.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  37 KNATEAAWRALASGGSALDAVESG-CAMCEREQCDGsvGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVA 115
Cdd:cd04702   26 KRAARAGYSVLKAGGSALDAVEAAvRALEDDPVFNA--GYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 116 RKVLEHTTHTLLVGESATTFAQSMGF---INEDLSTTASQALHSDWLARNCQPNywrnvipdpskycgpykppgilkqdi 192
Cdd:cd04702  104 RLVMEKTPHCFLTGRGANKFAEEMGIpqvPPESLVTERARERLEKFKKEKGANV-------------------------- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 193 pihkeTEDDRGHDTIGMVVIHKTGHIAAGTSTNG----------DSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQA 262
Cdd:cd04702  158 -----EDTQRGHGTVGAVAIDCEGNVACATSTGGitnkmvgrvgDSPIIGSGGYADNLVGAVSTTGHGESIMKVNLARLI 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 285002253 263 VEYMRRGEDPTIACQKVI----SRIQKHfpeffGAVICANVTGSYGAACN 308
Cdd:cd04702  233 LFHMEQGKTAEEAAELALaymkSRVKGL-----GGLIVVSKTGDWGAKFT 277
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 39-280 5.72e-26

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: 104.08  E-value: 5.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  39 ATEAAWRALASGGSALDAVESgcAMCEREQC------DGSVgfggsPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAI 112
Cdd:cd04701   31 ALEAGYAVLASGGSALDAVTA--AVRLLEDCplfnagKGAV-----FTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 113 GVARKVLEHTTHTLLVGESATTFAQSMGfinedlsttasqalhsdwlarncqpnywrnvipdpskycGPYKPPGilkqdi 192
Cdd:cd04701  104 LLARAVLEKSPHVLLSGEGAEEFAREQG---------------------------------------LELVPQG------ 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 193 pihketeddrghdTIGMVVIHKTGHIAAGTST----N------GDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSYQA 262
Cdd:cd04701  139 -------------TVGAVALDSDGNLAAATSTggltNklpgriGDTPIIGAGFWAEEWAVAVSGTGNGDSFIRVAAARDV 205

                        250
                 ....*....|....*....
gi 285002253 263 VEYMR-RGEDPTIACQKVI 280
Cdd:cd04701  206 AARMRyKGLSLAEAAKEVV 224
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 37-309 1.40e-21

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: 91.55  E-value: 1.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  37 KNATEAAWRALASGGSALDAVESGCAMCEREQCDGSvGFGGSPDELGETTLDAMIMDGTTmDVGAVGDLRRIKNAIGVAR 116
Cdd:cd04703   20 ERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNA-GTGSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVAR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 117 KVLEHTTHTLLVGESATTFAQSMGFinedlsttasqalhsdwlarncqpnywrnvipdpskycgpykppgilkqdipihk 196
Cdd:cd04703   98 AVMETSPHVLLAGDGAVRFARRLGY------------------------------------------------------- 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 197 etedDRGHDTIGMVV-IHktGHIAAGTSTN----------GDSPIPGAGAYADDTAGAAAATGnGDILMRFLPSYQAVEY 265
Cdd:cd04703  123 ----PDGCDTVGAVArDG--GKFAAAVSTGgtspalrgrvGDVPIIGAGFYAGPKGAVAATGI-GEEIAKRLLARRVYRW 195

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 285002253 266 MRRGEDPTIACQKVISRiqkhFPEFFGA-VICANVTGSYGAACNK 309
Cdd:cd04703  196 IETGLSLQAAAQRAIDE----FDDGVAVgVIAVSRRGEAGIASNT 236
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 41-280 1.77e-20

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 90.01  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  41 EAAWRALASGGSALDAVESGCAMCEreQC---DGSVGFGGSPDELGEttLDAMIMDGTTMDVGAVGDLRRIKNAIGVARK 117
Cdd:PRK10226  37 ETGQKMLEAGESALDVVTEAVRLLE--ECplfNAGIGAVFTRDETHE--LDACVMDGNTLKAGAVAGVSHLRNPVLAARL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 118 VLEHTTHTLLVGESATTFA--QSMGFINEDLSTTasqalhsdwlarncqpnywrnvipdPSKYCG--PYKPPGILKQD-- 191
Cdd:PRK10226 113 VMEQSPHVMMIGEGAENFAfaHGMERVSPEIFST-------------------------PLRYEQllAARAEGATVLDhs 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 192 -IPIHKETEddrgHDTIGMVVIHKTGHIAAGTSTN----------GDSPIPGAGAYADDTAGAAAATGNGDILMRFLPSY 260
Cdd:PRK10226 168 gAPLDEKQK----MGTVGAVALDLDGNLAAATSTGgmtnklpgrvGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAY 243

                        250       260
                 ....*....|....*....|.
gi 285002253 261 QAVEYMRRGE-DPTIACQKVI 280
Cdd:PRK10226 244 DIAALMDYGGlSLAEACERVV 264
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 46-236 3.39e-18

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 83.60  E-value: 3.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  46 ALASGGSALDAVEsgCAMCEREQC-DGSVGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVARKVLEHTTH 124
Cdd:PLN02689  41 ALRSSLPALDVVE--LVVRELENDpLFNAGRGSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPH 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 125 TLLVGESATTFAQSMG--------FINEDLSTTASQALHsdwlARNCQPNYwRNVIPDPSKYCGPYKPpgilkqdipihk 196
Cdd:PLN02689 119 IYLAFDGAEAFARQQGvetvdnsyFITEENVERLKQAKE----ANSVQFDY-RIPLDKPAKAAALAAD------------ 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 285002253 197 eteDDRGHDTIGMVVIHKTGHIAAGTSTN----------GDSPIPGAGAY 236
Cdd:PLN02689 182 ---GDAQPETVGCVAVDSDGNCAAATSTGglvnkmvgriGDTPIIGAGTY 228
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 37-223 4.80e-16

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: 77.31  E-value: 4.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  37 KNATEAAWRALASGGSALDAVESGCAMCEREQCDGSvGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVAR 116
Cdd:cd04514   25 KRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNA-GYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLAR 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 117 KVLEHTTH---------TLLVGESATTFAQSMGFINedlsttasqalhsdwlarncqpnywrnvipdpskycgpykppgi 187
Cdd:cd04514  104 LLLKEQRKplslgrvppMFLVGEGAREWAKSKGIIT-------------------------------------------- 139

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 285002253 188 lkqdipihketeddrghDTIGMVVIHKTGHIAAGTS 223
Cdd:cd04514  140 -----------------DTVGAIAIDLYGNIAAGSS 158
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 41-236 2.48e-12

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: 66.09  E-value: 2.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  41 EAAWRALASGgSALDAVESGCAMCERE-----------QCDGSVgfggspdelgetTLDAMIMDGTTMDVGAVGDLRRIK 109
Cdd:cd14949   32 EEVYEYLKSH-SALEAVVYAVSLLEDDplfnagtgsqiQSDGQI------------RMSASLMDGQTQRFSGVINIENVK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 110 NAIGVARKVLEHtTHTLLVGESATTFAQSMGFINEDLSTTASQAlhsDWLArncqpnywrnvipdpskycgpykppGILK 189
Cdd:cd14949   99 NPIEVAQKLQQE-DDRVLSGEGATEFARENGFPEYNPETPQRRQ---EYEE-------------------------KKLK 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 285002253 190 QDipihketeddrGHDTIGMVVIHKTGHIAAGTSTNG----------DSPIPgAGAY 236
Cdd:cd14949  150 SG-----------GTGTVGCVALDSDGKLAAATSTGGkgfeipgrvsDSATV-AGNY 194
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 37-226 2.07e-11

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 64.50  E-value: 2.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253  37 KNATEAAWRALASG-GSALDAVESGCAMCEREQCDGSvGFGGSPDELGETTLDAMIMDGTTMDVGAVGDLRRIKNAIGVA 115
Cdd:PLN02937  36 RRACLAAAAILRQGsGGCIDAVSAAIQVLEDDPSTNA-GRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 116 RKVLEHTTH----------TLLVGESATTFAQSMGFINEDLSTTASQalhsdWLARNCQPNYWR-------NVIP----- 173
Cdd:PLN02937 115 ALLAKEQMMgssllgrippMFLVGEGARQWAKSKGIDLPETVEEAEK-----WLVTERAKEQWKkyktmlaSAIAksscd 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 285002253 174 --DPSKYCGPYKPPGILKQDIPIHKET-----EDDRGHDTIGMVVIHKTGHIAAGTSTNG 226
Cdd:PLN02937 190 sqSTSKLSELEAPRSNPSNGTGGGQSSmctasDEDCIMDTVGVICVDSEGNIASGASSGG 249
 
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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