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Conserved domains on  [gi|755525329|ref|XP_006509312|]
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N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase isoform X1 [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

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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 ...
 29-313 3.62e-152

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


:

Pssm-ID: 271335  Cd Length: 294  Bit Score: 428.13  E-value: 3.62e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  29 LVVNTWPFKNATEAAWWTLLSGGSALDAVENGCAVCEKEQCDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRI 108
Cdd:cd04513    1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 109 KNAIGVARRVLEHTTHTLLVGDSATKFAESMGFTNEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCgpykpsgFL 188
Cdd:cd04513   81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC-------SS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 189 KQSISPHKEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLP 268
Cdd:cd04513  154 PKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 755525329 269 SYQAVEYMRGGDDPAIACQKVILRIQKYYP-NFFGAVICASVNGSY 313
Cdd:cd04513  234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEY 279
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 29-313 3.62e-152

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


Pssm-ID: 271335  Cd Length: 294  Bit Score: 428.13  E-value: 3.62e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  29 LVVNTWPFKNATEAAWWTLLSGGSALDAVENGCAVCEKEQCDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRI 108
Cdd:cd04513    1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 109 KNAIGVARRVLEHTTHTLLVGDSATKFAESMGFTNEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCgpykpsgFL 188
Cdd:cd04513   81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC-------SS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 189 KQSISPHKEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLP 268
Cdd:cd04513  154 PKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 755525329 269 SYQAVEYMRGGDDPAIACQKVILRIQKYYP-NFFGAVICASVNGSY 313
Cdd:cd04513  234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEY 279
Asparaginase_2 pfam01112
Asparaginase;
35-315 2.92e-98

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 291.80  E-value: 2.92e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329   35 PFKNATEAAWWTLLSGGSALDAVENGCAVCEkEQCDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGV 114
Cdd:pfam01112  24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  115 ARRVLEHTTHTLLVGDSATKFAESMGFT---NEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCGPYKpsgflkqs 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK-------- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  192 isphkeevdihsHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLPSYQ 271
Cdd:pfam01112 175 ------------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYD 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 755525329  272 AVEYMRGGDDPAIACQKVILRIQKYYPNfFGAVICASVNGSYVF 315
Cdd:pfam01112 243 IVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAA 285
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 21-315 1.08e-62

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 200.72  E-value: 1.08e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  21 VRGSSPLPLVVNTWPF--KNATEAAWWTLLSGGSALDAVENGCAVCEKeqcDG--TVGFGGSPDEGGETTLDAMIMDGTA 96
Cdd:COG1446   17 IARSAMTPEVEAAYRAglRAALEAGYAVLEAGGSALDAVEAAVRVLED---DPlfNAGKGAVLTRDGTVELDASIMDGAT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  97 MDVGAVGGLRRIKNAIGVARRVLEHTTHTLLVGDSATKFAESMGFTNEDLSTKTSRDLHSDWlsrncqpnywrnvipdps 176
Cdd:COG1446   94 LRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQW------------------ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 177 kycgpykpsgflkQSISPHKEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYaddtagaaaa 256
Cdd:COG1446  156 -------------KKALEYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTY---------- 212

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755525329 257 tgdgdtL----------------LRFLPSYQAVEYMRGGDDPAIACQKVILRIQKYYpNFFGAVICASVNGSYVF 315
Cdd:COG1446  213 ------AdnevgavsatghgeyfIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAA 280
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 47-291 4.50e-28

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 110.81  E-value: 4.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  47 LLSGGSALDAVENgcAVCEKEQCD-GTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARRVLEHTTHT 125
Cdd:PRK10226  43 LEAGESALDVVTE--AVRLLEECPlFNAGIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 126 LLVGDSATKFAESMGFTnedlstKTSRDLHSDwlsrncqpnywrnvipdPSKYCG--PYKPSG--FLKQSISPHKEEVDI 201
Cdd:PRK10226 121 MMIGEGAENFAFAHGME------RVSPEIFST-----------------PLRYEQllAARAEGatVLDHSGAPLDEKQKM 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 202 hshDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLPSYQAVEYMR-GGD 280
Cdd:PRK10226 178 ---GTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAALMDyGGL 254

                        250
                 ....*....|.
gi 755525329 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 ...
 29-313 3.62e-152

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


Pssm-ID: 271335  Cd Length: 294  Bit Score: 428.13  E-value: 3.62e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  29 LVVNTWPFKNATEAAWWTLLSGGSALDAVENGCAVCEKEQCDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRI 108
Cdd:cd04513    1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 109 KNAIGVARRVLEHTTHTLLVGDSATKFAESMGFTNEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCgpykpsgFL 188
Cdd:cd04513   81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC-------SS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 189 KQSISPHKEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLP 268
Cdd:cd04513  154 PKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 755525329 269 SYQAVEYMRGGDDPAIACQKVILRIQKYYP-NFFGAVICASVNGSY 313
Cdd:cd04513  234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEY 279
Asparaginase_2 pfam01112
Asparaginase;
35-315 2.92e-98

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 291.80  E-value: 2.92e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329   35 PFKNATEAAWWTLLSGGSALDAVENGCAVCEkEQCDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGV 114
Cdd:pfam01112  24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  115 ARRVLEHTTHTLLVGDSATKFAESMGFT---NEDLSTKTSRDLHSDWLSRNCQPNYWRNVIPDPSKYCGPYKpsgflkqs 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK-------- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  192 isphkeevdihsHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLPSYQ 271
Cdd:pfam01112 175 ------------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYD 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 755525329  272 AVEYMRGGDDPAIACQKVILRIQKYYPNfFGAVICASVNGSYVF 315
Cdd:pfam01112 243 IVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAA 285
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 21-315 1.08e-62

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 200.72  E-value: 1.08e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  21 VRGSSPLPLVVNTWPF--KNATEAAWWTLLSGGSALDAVENGCAVCEKeqcDG--TVGFGGSPDEGGETTLDAMIMDGTA 96
Cdd:COG1446   17 IARSAMTPEVEAAYRAglRAALEAGYAVLEAGGSALDAVEAAVRVLED---DPlfNAGKGAVLTRDGTVELDASIMDGAT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  97 MDVGAVGGLRRIKNAIGVARRVLEHTTHTLLVGDSATKFAESMGFTNEDLSTKTSRDLHSDWlsrncqpnywrnvipdps 176
Cdd:COG1446   94 LRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQW------------------ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 177 kycgpykpsgflkQSISPHKEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYaddtagaaaa 256
Cdd:COG1446  156 -------------KKALEYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTY---------- 212

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755525329 257 tgdgdtL----------------LRFLPSYQAVEYMRGGDDPAIACQKVILRIQKYYpNFFGAVICASVNGSYVF 315
Cdd:COG1446  213 ------AdnevgavsatghgeyfIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAA 280
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 39-315 1.92e-48

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: 162.35  E-value: 1.92e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  39 ATEAAWWTLLSGGSALDAVENGCAVCEKeqcDGT--VGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVAR 116
Cdd:cd04512   26 ALEAGREVLEKGGSALDAVEAAVRLLED---DPLfnAGRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLAR 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 117 RVLEHTTHTLLVGDSATKFAESMGftnedlstktsrdlhsdwlsrncqpnywrnvipdpskycgpykpsgflkqsisphk 196
Cdd:cd04512  103 AVMEKTPHVLLVGEGAERFAREHG-------------------------------------------------------- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 197 eevdihsHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLPSYQAVEYM 276
Cdd:cd04512  127 -------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLV 199

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 755525329 277 RGGDDPAIACQKVIlRIQKYYPNFFGAVICASVNGSYVF 315
Cdd:cd04512  200 EFGGSAQEAAEAAI-DYLRRRVGGEGGLIVVDPDGRLGA 237
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 37-246 3.21e-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: 142.33  E-value: 3.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  37 KNATEAAWWTLLSGGSALDAVEngCAVCEKEqCDGTV--GFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGV 114
Cdd:cd04702   26 KRAARAGYSVLKAGGSALDAVE--AAVRALE-DDPVFnaGYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 115 ARRVLEHTTHTLLVGDSATKFAESMGFT---NEDLSTKTSRDLHSDwlsrncqpnywrnvipdpskycgpykpsgFLKQS 191
Cdd:cd04702  103 ARLVMEKTPHCFLTGRGANKFAEEMGIPqvpPESLVTERARERLEK-----------------------------FKKEK 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755525329 192 ISPhkEEVDIHSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAY 246
Cdd:cd04702  154 GAN--VEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGY 206
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 37-315 1.90e-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: 1.90e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  37 KNATEAAWwTLLSGGSALDAVENGCAVCEkeqcDGTV---GFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIG 113
Cdd:cd14950   25 REALERGY-EALRRGSALEAVVEAVAYME----DSGVfnaGVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 114 VARRVLEHTTHTLLVGDSATKFAESMGFtnedlstktsrdlhsdwlsrncqpnywrnvipdpskycgpykpsgflkqsis 193
Cdd:cd14950  100 LARKVMEKTDHVLIVGEGADELAKRLGG---------------------------------------------------- 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 194 phkeevdihshDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYaDDTAGAAAATGDGDTLLRFLPSYQAV 273
Cdd:cd14950  128 -----------DTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFY-ATNGVAVSATGIGEVIIRSLPALRAD 195

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 755525329 274 EYMRGGDDPAIACQKVILRIQKYYPNFFGAVICASVNGSYVF 315
Cdd:cd14950  196 ELVSMGGDIEEAVRAVVNKVTETFGKDTAGIIGIDARGNIAA 237
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 47-246 6.95e-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: 119.49  E-value: 6.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  47 LLSGGSALDAVENgcAVCEKEQCdgtV----GFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARRVLEHT 122
Cdd:cd04701   39 LASGGSALDAVTA--AVRLLEDC---PlfnaGKGAVFTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 123 THTLLVGDSATKFAESMGftnedlstktsrdlhsdwlsrncqpnywrnvipdpskycgpykpsgflkqsisphkeeVDIH 202
Cdd:cd04701  114 PHVLLSGEGAEEFAREQG----------------------------------------------------------LELV 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 755525329 203 SHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAY 246
Cdd:cd04701  136 PQGTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFW 179
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 47-291 4.50e-28

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 110.81  E-value: 4.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  47 LLSGGSALDAVENgcAVCEKEQCD-GTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARRVLEHTTHT 125
Cdd:PRK10226  43 LEAGESALDVVTE--AVRLLEECPlFNAGIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHV 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 126 LLVGDSATKFAESMGFTnedlstKTSRDLHSDwlsrncqpnywrnvipdPSKYCG--PYKPSG--FLKQSISPHKEEVDI 201
Cdd:PRK10226 121 MMIGEGAENFAFAHGME------RVSPEIFST-----------------PLRYEQllAARAEGatVLDHSGAPLDEKQKM 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 202 hshDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAYADDTAGAAAATGDGDTLLRFLPSYQAVEYMR-GGD 280
Cdd:PRK10226 178 ---GTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAALMDyGGL 254

                        250
                 ....*....|.
gi 755525329 281 DPAIACQKVIL 291
Cdd:PRK10226 255 SLAEACERVVM 265
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 37-246 3.94e-26

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: 103.88  E-value: 3.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  37 KNATEAAWWTLLSGGSALDAVENGCAVCEKeqcDGT--VGFGGSPDEGGETTLDAMIMDGTAmDVGAVGGLRRIKNAIGV 114
Cdd:cd04703   20 ERAAEAGLAELQNGGDALDAVVAAVRVLED---DPRfnAGTGSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 115 ARRVLEHTTHTLLVGDSATKFAESMGFTnedlstktsrdlhsdwlsrncqpnywrnvipdpskycgpykpsgflkqsisp 194
Cdd:cd04703   96 ARAVMETSPHVLLAGDGAVRFARRLGYP---------------------------------------------------- 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755525329 195 hkeevdiHSHDTIGMVV-IHktGHTAAGTSTNGIKFKIPGRVGDSPIPGAGAY 246
Cdd:cd04703  124 -------DGCDTVGAVArDG--GKFAAAVSTGGTSPALRGRVGDVPIIGAGFY 167
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 47-246 6.92e-25

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 102.09  E-value: 6.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  47 LLSGGSALDAVEngCAVCEKEQC-DGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARRVLEHTTHT 125
Cdd:PLN02689  42 LRSSLPALDVVE--LVVRELENDpLFNAGRGSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 126 LLVGDSATKFAESMGFTNEDLSTKTSRDLHSDW-LSRNCQPNYWRNVIPdpskyCGPYKPSGFLKQSISPHKEevdihsh 204
Cdd:PLN02689 120 YLAFDGAEAFARQQGVETVDNSYFITEENVERLkQAKEANSVQFDYRIP-----LDKPAKAAALAADGDAQPE------- 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755525329 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 1.68e-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: 1.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  37 KNATEAAWWTLLSGGSALDAVENGCAVCEKEQCDGTvGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVAR 116
Cdd:cd04514   25 KRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNA-GYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLAR 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 117 RVLEHTTH---------TLLVGDSATKFAESMGFTNedlstktsrdlhsdwlsrncqpnywrnvipdpskycgpykpsgf 187
Cdd:cd04514  104 LLLKEQRKplslgrvppMFLVGEGAREWAKSKGIIT-------------------------------------------- 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755525329 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 2.56e-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: 77.65  E-value: 2.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  45 WTLLSGGSALDAVENGCAVCEKEQcDGTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARRVLEHTtH 124
Cdd:cd14949   35 YEYLKSHSALEAVVYAVSLLEDDP-LFNAGTGSQIQSDGQIRMSASLMDGQTQRFSGVINIENVKNPIEVAQKLQQED-D 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 125 TLLVGDSATKFAESMGFTNEDLSTKTSRdlhsdwlsrncqpnywrnvipdpSKYCGPYKPSGflkqsisphkeevdihSH 204
Cdd:cd14949  113 RVLSGEGATEFARENGFPEYNPETPQRR-----------------------QEYEEKKLKSG----------------GT 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755525329 205 DTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPgAGAY 246
Cdd:cd14949  154 GTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNY 194
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 37-246 2.77e-14

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 72.97  E-value: 2.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329  37 KNATEAAWwTLLSGGS--ALDAVENGCAVCEKEQCDgTVGFGGSPDEGGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGV 114
Cdd:PLN02937  36 RRACLAAA-AILRQGSggCIDAVSAAIQVLEDDPST-NAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQI 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 115 ARRVLEHTTH----------TLLVGDSATKFAESMGFTNEDLSTKTSRdlhsdWLSRNCQPNYWR-------NVIP---- 173
Cdd:PLN02937 114 AALLAKEQMMgssllgrippMFLVGEGARQWAKSKGIDLPETVEEAEK-----WLVTERAKEQWKkyktmlaSAIAkssc 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755525329 174 ---DPSKYCGPYKPSGFL------KQSISPHKEEVDIhSHDTIGMVVIHKTGHTAAGTSTNGIKFKIPGRVGDSPIPGAG 244
Cdd:PLN02937 189 dsqSTSKLSELEAPRSNPsngtggGQSSMCTASDEDC-IMDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSG 267


                 ..
gi 755525329 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.
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