NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|54292135|ref|NP_001005847|]
View 

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase isoform 1 preproprotein [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 29-332 1.57e-159

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: 1.57e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  29 LVVNTWPFKNATEAAWWTLLSGGSALDAVENGCAVCEKEQCDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRI 108
Cdd:cd04513   1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 109 KNAIGVARRVLEHTTHTLLVGDSATKFAESMGFTNEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCgpykpsgFL 188
Cdd:cd04513  81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC-------SS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 189 KQSISPHKEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLP 268
Cdd:cd04513 154 PKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 54292135 269 SYQAVEYMRGGDDPAIACQKVILRIQKYYP-NFFGAVICASVNGSYGAACNKlptfTQFSFMVSN 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 1.57e-159

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: 1.57e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  29 LVVNTWPFKNATEAAWWTLLSGGSALDAVENGCAVCEKEQCDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRI 108
Cdd:cd04513   1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 109 KNAIGVARRVLEHTTHTLLVGDSATKFAESMGFTNEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCgpykpsgFL 188
Cdd:cd04513  81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC-------SS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 189 KQSISPHKEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLP 268
Cdd:cd04513 154 PKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 54292135 269 SYQAVEYMRGGDDPAIACQKVILRIQKYYP-NFFGAVICASVNGSYGAACNKlptfTQFSFMVSN 332
Cdd:cd04513 234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
35-318 1.82e-101

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 301.04  E-value: 1.82e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135    35 PFKNATEAAWWTLLSGGSALDAVENGCAVCEkEQCDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGV 114
Cdd:pfam01112  24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135   115 ARRVLEHTTHTLLVGDSATKFAESMGFT---NEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCGPYKpsgflkqs 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK-------- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135   192 isphkeevdihsHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLPSYQ 271
Cdd:pfam01112 175 ------------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYD 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 54292135   272 AVEYMRGGDDPAIACQKVILRIQKYYPNfFGAVICASVNGSYGAACN 318
Cdd:pfam01112 243 IVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFN 288
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 21-318 1.38e-65

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 209.19  E-value: 1.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  21 VRGSSPLPLVVNTWPF--KNATEAAWWTLLSGGSALDAVENGCAVCEKeqcDG--TVGFGGSPDEGGETTLDAMIMDGTA 96
Cdd:COG1446  17 IARSAMTPEVEAAYRAglRAALEAGYAVLEAGGSALDAVEAAVRVLED---DPlfNAGKGAVLTRDGTVELDASIMDGAT 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  97 MDVGAVGGLRRIKNAIGVARRVLEHTTHTLLVGDSATKFAESMGFTNEDLSTKTSRDLHSDWlsrncqpnywrnvipdps 176
Cdd:COG1446  94 LRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQW------------------ 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 177 kycgpykpsgflkQSISPHKEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYaddtagaaaa 256
Cdd:COG1446 156 -------------KKALEYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTY---------- 212

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54292135 257 tgdgdtL----------------LRFLPSYQAVEYMRGGDDPAIACQKVILRIQKYYpNFFGAVICASVNGSYGAACN 318
Cdd:COG1446 213 ------AdnevgavsatghgeyfIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPFN 283
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 47-291 3.73e-28

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 111.58  E-value: 3.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135   47 LLSGGSALDAVENgcAVCEKEQCD-GTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARRVLEHTTHT 125
Cdd:PRK10226  43 LEAGESALDVVTE--AVRLLEECPlFNAGIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  126 LLVGDSATKFAESMGFTnedlstKTSRDLHSDwlsrncqpnywrnvipdPSKYCG--PYKPSG--FLKQSISPHKEEVDI 201
Cdd:PRK10226 121 MMIGEGAENFAFAHGME------RVSPEIFST-----------------PLRYEQllAARAEGatVLDHSGAPLDEKQKM 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  202 hshDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLPSYQAVEYMR-GGD 280
Cdd:PRK10226 178 ---GTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAALMDyGGL 254

                        250
                 ....*....|.
gi 54292135  281 DPAIACQKVIL 291
Cdd:PRK10226 255 SLAEACERVVM 265
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 29-332 1.57e-159

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: 1.57e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  29 LVVNTWPFKNATEAAWWTLLSGGSALDAVENGCAVCEKEQCDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRI 108
Cdd:cd04513   1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 109 KNAIGVARRVLEHTTHTLLVGDSATKFAESMGFTNEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCgpykpsgFL 188
Cdd:cd04513  81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC-------SS 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 189 KQSISPHKEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLP 268
Cdd:cd04513 154 PKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 54292135 269 SYQAVEYMRGGDDPAIACQKVILRIQKYYP-NFFGAVICASVNGSYGAACNKlptfTQFSFMVSN 332
Cdd:cd04513 234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
35-318 1.82e-101

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 301.04  E-value: 1.82e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135    35 PFKNATEAAWWTLLSGGSALDAVENGCAVCEkEQCDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGV 114
Cdd:pfam01112  24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135   115 ARRVLEHTTHTLLVGDSATKFAESMGFT---NEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCGPYKpsgflkqs 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK-------- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135   192 isphkeevdihsHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLPSYQ 271
Cdd:pfam01112 175 ------------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYD 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 54292135   272 AVEYMRGGDDPAIACQKVILRIQKYYPNfFGAVICASVNGSYGAACN 318
Cdd:pfam01112 243 IVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFN 288
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 21-318 1.38e-65

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 209.19  E-value: 1.38e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  21 VRGSSPLPLVVNTWPF--KNATEAAWWTLLSGGSALDAVENGCAVCEKeqcDG--TVGFGGSPDEGGETTLDAMIMDGTA 96
Cdd:COG1446  17 IARSAMTPEVEAAYRAglRAALEAGYAVLEAGGSALDAVEAAVRVLED---DPlfNAGKGAVLTRDGTVELDASIMDGAT 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  97 MDVGAVGGLRRIKNAIGVARRVLEHTTHTLLVGDSATKFAESMGFTNEDLSTKTSRDLHSDWlsrncqpnywrnvipdps 176
Cdd:COG1446  94 LRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQW------------------ 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 177 kycgpykpsgflkQSISPHKEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYaddtagaaaa 256
Cdd:COG1446 156 -------------KKALEYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTY---------- 212

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54292135 257 tgdgdtL----------------LRFLPSYQAVEYMRGGDDPAIACQKVILRIQKYYpNFFGAVICASVNGSYGAACN 318
Cdd:COG1446 213 ------AdnevgavsatghgeyfIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPFN 283
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 39-318 2.43e-51

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: 170.83  E-value: 2.43e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  39 ATEAAWWTLLSGGSALDAVENGCAVCEKeqcDGT--VGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVAR 116
Cdd:cd04512  26 ALEAGREVLEKGGSALDAVEAAVRLLED---DPLfnAGRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLAR 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 117 RVLEHTTHTLLVGDSATKFAESMGftnedlstktsrdlhsdwlsrncqpnywrnvipdpskycgpykpsgflkqsisphk 196
Cdd:cd04512 103 AVMEKTPHVLLVGEGAERFAREHG-------------------------------------------------------- 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 197 eevdihsHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLPSYQAVEYM 276
Cdd:cd04512 127 -------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLV 199

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 54292135 277 RGGDDPAIACQKVIlRIQKYYPNFFGAVICASVNGSYGAACN 318
Cdd:cd04512 200 EFGGSAQEAAEAAI-DYLRRRVGGEGGLIVVDPDGRLGAAHN 240
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 37-318 6.40e-41

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: 143.87  E-value: 6.40e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  37 KNATEAAWwTLLSGGSALDAVENGCAVCEkeqcDGTV---GFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIG 113
Cdd:cd14950  25 REALERGY-EALRRGSALEAVVEAVAYME----DSGVfnaGVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIR 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 114 VARRVLEHTTHTLLVGDSATKFAESMGFtnedlstktsrdlhsdwlsrncqpnywrnvipdpskycgpykpsgflkqsis 193
Cdd:cd14950 100 LARKVMEKTDHVLIVGEGADELAKRLGG---------------------------------------------------- 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 194 phkeevdihshDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYaDDTAGAAAATGDGDTLLRFLPSYQAV 273
Cdd:cd14950 128 -----------DTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFY-ATNGVAVSATGIGEVIIRSLPALRAD 195

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 54292135 274 EYMRGGDDPAIACQKVILRIQKYYPNFFGAVICASVNGSYGAACN 318
Cdd:cd14950 196 ELVSMGGDIEEAVRAVVNKVTETFGKDTAGIIGIDARGNIAAAFN 240
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 37-246 2.57e-40

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: 143.10  E-value: 2.57e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  37 KNATEAAWWTLLSGGSALDAVEngCAVCEKEqCDGTV--GFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGV 114
Cdd:cd04702  26 KRAARAGYSVLKAGGSALDAVE--AAVRALE-DDPVFnaGYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISL 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 115 ARRVLEHTTHTLLVGDSATKFAESMGFT---NEDLSTKTSRDLHSDwlsrncqpnywrnvipdpskycgpykpsgFLKQS 191
Cdd:cd04702 103 ARLVMEKTPHCFLTGRGANKFAEEMGIPqvpPESLVTERARERLEK-----------------------------FKKEK 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 54292135 192 ISPhkEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAY 246
Cdd:cd04702 154 GAN--VEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGY 206
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 47-246 4.23e-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: 120.64  E-value: 4.23e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  47 LLSGGSALDAVENgcAVCEKEQCdgtV----GFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARRVLEHT 122
Cdd:cd04701  39 LASGGSALDAVTA--AVRLLEDC---PlfnaGKGAVFTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKS 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 123 THTLLVGDSATKFAESMGftnedlstktsrdlhsdwlsrncqpnywrnvipdpskycgpykpsgflkqsisphkeeVDIH 202
Cdd:cd04701 114 PHVLLSGEGAEEFAREQG----------------------------------------------------------LELV 135

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 54292135 203 SHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAY 246
Cdd:cd04701 136 PQGTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFW 179
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 37-319 2.53e-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: 110.04  E-value: 2.53e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  37 KNATEAAWWTLLSGGSALDAVENGCAVCEKeqcDGT--VGFGGSPDEGGETTLDAMIMDGTAmDVGAVGGLRRIKNAIGV 114
Cdd:cd04703  20 ERAAEAGLAELQNGGDALDAVVAAVRVLED---DPRfnAGTGSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLV 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 115 ARRVLEHTTHTLLVGDSATKFAESMGFTnedlstktsrdlhsdwlsrncqpnywrnvipdpskycgpykpsgflkqsisp 194
Cdd:cd04703  96 ARAVMETSPHVLLAGDGAVRFARRLGYP---------------------------------------------------- 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 195 hkeevdiHSHDTIGMVV-IHktGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLpSYQAV 273
Cdd:cd04703 124 -------DGCDTVGAVArDG--GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKGAVAATGIGEEIAKRLL-ARRVY 193

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 54292135 274 EYMRGGDDPAIACQKVILRIQKYYPnffGAVICASVNGSYGAACNK 319
Cdd:cd04703 194 RWIETGLSLQAAAQRAIDEFDDGVA---VGVIAVSRRGEAGIASNT 236
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 47-291 3.73e-28

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 111.58  E-value: 3.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135   47 LLSGGSALDAVENgcAVCEKEQCD-GTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARRVLEHTTHT 125
Cdd:PRK10226  43 LEAGESALDVVTE--AVRLLEECPlFNAGIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  126 LLVGDSATKFAESMGFTnedlstKTSRDLHSDwlsrncqpnywrnvipdPSKYCG--PYKPSG--FLKQSISPHKEEVDI 201
Cdd:PRK10226 121 MMIGEGAENFAFAHGME------RVSPEIFST-----------------PLRYEQllAARAEGatVLDHSGAPLDEKQKM 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  202 hshDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLPSYQAVEYMR-GGD 280
Cdd:PRK10226 178 ---GTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAALMDyGGL 254

                        250
                 ....*....|.
gi 54292135  281 DPAIACQKVIL 291
Cdd:PRK10226 255 SLAEACERVVM 265
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 47-246 7.59e-25

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 102.48  E-value: 7.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135   47 LLSGGSALDAVEngCAVCEKEQC-DGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARRVLEHTTHT 125
Cdd:PLN02689  42 LRSSLPALDVVE--LVVRELENDpLFNAGRGSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  126 LLVGDSATKFAESMGFTNEDLSTKTSRDLHSDW-LSRNCQPNYWRNVIPdpskyCGPYKPSGFLKQSISPHKEevdihsh 204
Cdd:PLN02689 120 YLAFDGAEAFARQQGVETVDNSYFITEENVERLkQAKEANSVQFDYRIP-----LDKPAKAAALAADGDAQPE------- 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 54292135  205 dTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAY 246
Cdd:PLN02689 188 -TVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTY 228
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 37-246 2.04e-21

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: 92.72  E-value: 2.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  37 KNATEAAWWTLLSGGSALDAVENGCAVCEKEQCDGTvGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVAR 116
Cdd:cd04514  25 KRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNA-GYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLAR 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 117 RVLEHTTH---------TLLVGDSATKFAESMGFTNedlstktsrdlhsdwlsrncqpnywrnvipdpskycgpykpsgf 187
Cdd:cd04514 104 LLLKEQRKplslgrvppMFLVGEGAREWAKSKGIIT-------------------------------------------- 139

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 54292135 188 lkqsisphkeevdihshDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAY 246
Cdd:cd04514 140 -----------------DTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCW 181
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 45-246 2.57e-16

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: 78.03  E-value: 2.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  45 WTLLSGGSALDAVENGCAVCEKEQcDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARRVLEHTtH 124
Cdd:cd14949  35 YEYLKSHSALEAVVYAVSLLEDDP-LFNAGTGSQIQSDGQIRMSASLMDGQTQRFSGVINIENVKNPIEVAQKLQQED-D 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135 125 TLLVGDSATKFAESMGFTNEDLSTKTSRdlhsdwlsrncqpnywrnvipdpSKYCGPYKPSGflkqsisphkeevdihSH 204
Cdd:cd14949 113 RVLSGEGATEFARENGFPEYNPETPQRR-----------------------QEYEEKKLKSG----------------GT 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 54292135 205 DTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPgAGAY 246
Cdd:cd14949 154 GTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNY 194
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 37-246 3.78e-14

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 72.97  E-value: 3.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135   37 KNATEAAWwTLLSGGS--ALDAVENGCAVCEKEQCDgTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGV 114
Cdd:PLN02937  36 RRACLAAA-AILRQGSggCIDAVSAAIQVLEDDPST-NAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQI 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  115 ARRVLEHTTH----------TLLVGDSATKFAESMGFTNEDLSTKTSRdlhsdWLSRNCQPNYWR-------NVIP---- 173
Cdd:PLN02937 114 AALLAKEQMMgssllgrippMFLVGEGARQWAKSKGIDLPETVEEAEK-----WLVTERAKEQWKkyktmlaSAIAkssc 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54292135  174 ---DPSKYCGPYKPSGFL------KQSISPHKEEVDIhSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAG 244
Cdd:PLN02937 189 dsqSTSKLSELEAPRSNPsngtggGQSSMCTASDEDC-IMDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSG 267


                 ..
gi 54292135  245 AY 246
Cdd:PLN02937 268 CW 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH