|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
1-297 |
6.49e-89 |
|
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: 267.60 E-value: 6.49e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPscppstmttrfslaafkrn 80
Cdd:cd04514 79 MDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGII------------------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 krklelaervetdfiqlkrrrqssakendsgaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:cd04514 139 --------------------------------TDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 161 AHNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLASEDG---VLGGVIVLRSCRcpses 236
Cdd:cd04514 187 PDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK----- 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958761951 237 dpsqdKQTLLVEFLWSHSTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 297
Cdd:cd04514 262 -----KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
1-276 |
7.68e-53 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 178.13 E-value: 7.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPScpPSTMT-------TRFS 73
Cdd:PLN02937 91 MDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDL--PETVEeaekwlvTERA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 74 LAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGA------------LDTVGAVVVDHEGNVAAAVSSG 134
Cdd:PLN02937 169 KEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIASGASSG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 135 GLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEHLVRTILARECSHAL---QAEDAHQA---LLETMQNk 207
Cdd:PLN02937 249 GIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSSslsQAGPASACmkvLRSVIQG- 327
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958761951 208 fiSSPFLASEDgvlGGVIVLRSCRcpSESDPSQDKQTLLVEFLWSHSTESMCVGYMSAQDGKAKTHISR 276
Cdd:PLN02937 328 --SSAKTTDKD---AGILLVQADA--SVMAPGNSPSLKAVEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
1-274 |
2.58e-41 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 144.87 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaaFKRN 80
Cdd:COG1446 89 MDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDPLY---------FFTE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 KRKLelaervetdfiQLKRRRQSSAKENDSGaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:COG1446 150 KRWK-----------QWKKALEYKPIINERK-HGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 161 AhnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspflASEDGVLGGVIVLrscrcpsesdps 239
Cdd:COG1446 218 G------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI-------LKKLGGDGGLIAV------------ 272
|
250 260 270
....*....|....*....|....*....|....*
gi 1958761951 240 qDKQTllvEFLWSHSTESMCVGYMSAqDGKAKTHI 274
Cdd:COG1446 273 -DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
1-265 |
6.63e-37 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 133.48 E-value: 6.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRN 80
Cdd:pfam01112 80 MDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 KrklelaervETDFIQLKRRRQSSA--KENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAEN 158
Cdd:pfam01112 150 R---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 159 TGAhnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflasedGVLGGVIVLrscrcps 234
Cdd:pfam01112 221 ATG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV----------GGDGGVIAV------- 277
|
250 260 270
....*....|....*....|....*....|.
gi 1958761951 235 esdpsqDKQTllvEFLWSHSTESMCVGYMSA 265
Cdd:pfam01112 278 ------DAKG---NIAAPFNTEGMYRAYHTG 299
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
1-297 |
6.49e-89 |
|
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: 267.60 E-value: 6.49e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPscppstmttrfslaafkrn 80
Cdd:cd04514 79 MDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGII------------------- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 krklelaervetdfiqlkrrrqssakendsgaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:cd04514 139 --------------------------------TDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 161 AHNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLASEDG---VLGGVIVLRSCRcpses 236
Cdd:cd04514 187 PDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK----- 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958761951 237 dpsqdKQTLLVEFLWSHSTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 297
Cdd:cd04514 262 -----KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
1-263 |
3.51e-55 |
|
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: 179.30 E-value: 3.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscppstmttrfslaafkrn 80
Cdd:cd04512 78 MDGKTLNAGAVAGVKGVKNPISLARAVMEKT----------PHVLLVGEGAERFAREHG--------------------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 krklelaervetdfiqlkrrrqssakendsgaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTg 160
Cdd:cd04512 127 --------------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNE- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 161 ahnpySTAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKfisspfLASEDGVLGGVIVLrscrcpsesdpsq 240
Cdd:cd04512 174 -----TGAVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAEAAIDY------LRRRVGGEGGLIVV------------- 229
|
250 260
....*....|....*....|...
gi 1958761951 241 DKQtllVEFLWSHSTESMCVGYM 263
Cdd:cd04512 230 DPD---GRLGAAHNTPGMAFAYI 249
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
1-276 |
7.68e-53 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 178.13 E-value: 7.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPScpPSTMT-------TRFS 73
Cdd:PLN02937 91 MDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDL--PETVEeaekwlvTERA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 74 LAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGA------------LDTVGAVVVDHEGNVAAAVSSG 134
Cdd:PLN02937 169 KEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIASGASSG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 135 GLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEHLVRTILARECSHAL---QAEDAHQA---LLETMQNk 207
Cdd:PLN02937 249 GIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSSslsQAGPASACmkvLRSVIQG- 327
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958761951 208 fiSSPFLASEDgvlGGVIVLRSCRcpSESDPSQDKQTLLVEFLWSHSTESMCVGYMSAQDGKAKTHISR 276
Cdd:PLN02937 328 --SSAKTTDKD---AGILLVQADA--SVMAPGNSPSLKAVEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
1-274 |
2.58e-41 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 144.87 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaaFKRN 80
Cdd:COG1446 89 MDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDPLY---------FFTE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 KRKLelaervetdfiQLKRRRQSSAKENDSGaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:COG1446 150 KRWK-----------QWKKALEYKPIINERK-HGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 161 AhnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspflASEDGVLGGVIVLrscrcpsesdps 239
Cdd:COG1446 218 G------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI-------LKKLGGDGGLIAV------------ 272
|
250 260 270
....*....|....*....|....*....|....*
gi 1958761951 240 qDKQTllvEFLWSHSTESMCVGYMSAqDGKAKTHI 274
Cdd:COG1446 273 -DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
1-227 |
7.72e-39 |
|
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: 138.09 E-value: 7.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRN 80
Cdd:cd04702 80 MDGKTLRAGAVSAVRNIANPISLA-RLVME---------KTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 KRKlelaervetdfiqlkrrrQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtg 160
Cdd:cd04702 150 KKE------------------KGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADN-- 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958761951 161 ahnpYSTAVSTSGCGEHLVRTILARECSHALQ----AEDAHQALLETMQNKFisspflasedGVLGGVIVL 227
Cdd:cd04702 210 ----LVGAVSTTGHGESIMKVNLARLILFHMEqgktAEEAAELALAYMKSRV----------KGLGGLIVV 266
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
1-265 |
6.63e-37 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 133.48 E-value: 6.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRN 80
Cdd:pfam01112 80 MDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 KrklelaervETDFIQLKRRRQSSA--KENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAEN 158
Cdd:pfam01112 150 R---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 159 TGAhnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflasedGVLGGVIVLrscrcps 234
Cdd:pfam01112 221 ATG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV----------GGDGGVIAV------- 277
|
250 260 270
....*....|....*....|....*....|.
gi 1958761951 235 esdpsqDKQTllvEFLWSHSTESMCVGYMSA 265
Cdd:pfam01112 278 ------DAKG---NIAAPFNTEGMYRAYHTG 299
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
1-186 |
5.56e-30 |
|
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: 114.97 E-value: 5.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRN 80
Cdd:cd04513 64 MDGDTMDVGAVAALRRIKNAISVARAVM----------EHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 KRKLELAERVETD-----FIQLKRRRQSSAKENDSGalDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCW 155
Cdd:cd04513 134 NCQPNFWKNVVPDpskscSSPKAPSRSESAIPEDNH--DTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLY 211
|
170 180 190
....*....|....*....|....*....|..
gi 1958761951 156 AENT-GAhnpystAVSTsGCGEHLVRTILARE 186
Cdd:cd04513 212 ADNEvGA------AAAT-GDGDIMMRFLPSYQ 236
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
1-186 |
1.55e-26 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 105.94 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRfslaafkRN 80
Cdd:PLN02689 86 MDGRTRRCGAVSGLTTVVNPISLA-RLVME---------KTPHIYLAFDGAEAFARQQGVETVDNSYFITE-------EN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 KRKLELAE---RVETDFIQ--LKRRRQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCW 155
Cdd:PLN02689 149 VERLKQAKeanSVQFDYRIplDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTY 228
|
170 180 190
....*....|....*....|....*....|.
gi 1958761951 156 AENTGahnpystAVSTSGCGEHLVRTILARE 186
Cdd:PLN02689 229 ANHLC-------AVSATGKGEAIIRGTVARD 252
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
1-264 |
1.92e-26 |
|
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: 104.20 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscppstmttrfslaafkrn 80
Cdd:cd14950 78 MDGRTLRVGAVAAVRAVKNPIRLARKVMEKT----------DHVLIVGEGADELAKRLG--------------------- 126
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 krklelaervetdfiqlkrrrqssakendsgaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtg 160
Cdd:cd14950 127 --------------------------------GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN-- 172
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 161 ahnpySTAVSTSGCGEHLVRTILARECSHA----LQAEDAHQALLETMQNKFISSpflasedgvLGGVIVLrscrcpses 236
Cdd:cd14950 173 -----GVAVSATGIGEVIIRSLPALRADELvsmgGDIEEAVRAVVNKVTETFGKD---------TAGIIGI--------- 229
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250 260
....*....|....*....|....*...
gi 1958761951 237 dpsqDKQTllvEFLWSHSTESMCVGYMS 264
Cdd:cd14950 230 ----DARG---NIAAAFNTEAMPRGYID 250
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| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
1-227 |
1.41e-25 |
|
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: 102.15 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaafkrn 80
Cdd:cd04701 83 MDGRTKRAGAVAGLRRVRNPILLARAVLEKS----------PHVLLSGEGAEEFAREQGLELVPQGT------------- 139
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 krklelaervetdfiqlkrrrqssakendsgaldtVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtg 160
Cdd:cd04701 140 -----------------------------------VGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEE-- 182
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170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958761951 161 ahnpYSTAVSTSGCGEHLVRTILARECSHalQAEDAHQALLETMqnKFISSPFLASEDGVlGGVIVL 227
Cdd:cd04701 183 ----WAVAVSGTGNGDSFIRVAAARDVAA--RMRYKGLSLAEAA--KEVVGPGGELGEGE-GGIIAI 240
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| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
1-184 |
1.52e-25 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 103.49 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVsVAHRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTrfslaafkrN 80
Cdd:PRK10226 87 MDGNTLKAGAVAGVSHLRNPV-LAARLVME---------QSPHVMMIGEGAENFAFAHGMERVSPEIFST---------P 147
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 KRKLELAERVETDFIQLKrrrQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTg 160
Cdd:PRK10226 148 LRYEQLLAARAEGATVLD---HSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNA- 223
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170 180
....*....|....*....|....
gi 1958761951 161 ahnpySTAVSTSGCGEHLVRTILA 184
Cdd:PRK10226 224 -----SVAVSCTGTGEVFIRALAA 242
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| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
1-227 |
3.39e-19 |
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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: 84.62 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSlSFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIP-SCppstmttrfslaafkr 79
Cdd:cd04703 74 MTSGG-AFGAVAAIEGVKNPVLVARAVMETS----------PHVLLAGDGAVRFARRLGYPdGC---------------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 80 nkrklelaervetdfiqlkrrrqssakendsgalDTVGAVVVDHeGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 159
Cdd:cd04703 127 ----------------------------------DTVGAVARDG-GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958761951 160 GahnpystAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFisspflasEDGVLGGVIVL 227
Cdd:cd04703 172 G-------AVAATGIGEEIAKRLLARRVYRWIETGLSLQAAAQRAIDEF--------DDGVAVGVIAV 224
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| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
1-184 |
1.25e-15 |
|
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; The wider family of Asparaginase 2-like enzymes includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue.
Pssm-ID: 271340 Cd Length: 280 Bit Score: 75.34 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 1 MDGKSLSFGAVGALSGIKNPVSVAHRLLCEGQKgklsagrippcFLVGEGAYRWAVDHGIPSCPPstmttrfslaafkrn 80
Cdd:cd14949 81 MDGQTQRFSGVINIENVKNPIEVAQKLQQEDDR-----------VLSGEGATEFARENGFPEYNP--------------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761951 81 krklelaervETDFiqlkRRRQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAAlygcgcwaenTG 160
Cdd:cd14949 135 ----------ETPQ----RRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSA----------TV 190
|
170 180
....*....|....*....|....*..
gi 1958761951 161 AHNpYST---AVSTSGCGEHLVRTILA 184
Cdd:cd14949 191 AGN-YANafaGVSCTGIGEDIVSEALA 216
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