|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
3-364 |
7.98e-120 |
|
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: 348.88 E-value: 7.98e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 3 GFVAVHTGAGNCID--ETKYQRVIKEACLRATEILRNGGSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAAIMD 80
Cdd:cd04514 1 FFVAVHAGAGYHSPsnEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 81 GSTLNFGACTNVSRVKNPIQLARRICDAQSSPQLLERIPPMILAGTGAEHYADEVGCSMvepgvlisskakfqfnhyksk 160
Cdd:cd04514 81 GSSGRFGAVGAVSGVKNPIQLARLLLKEQRKPLSLGRVPPMFLVGEGAREWAKSKGIIT--------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 161 ydlvvnsrlgkatseesvqvpepgnevelaaalDTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYGAGCWATDTD 240
Cdd:cd04514 140 ---------------------------------DTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRD 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 241 E---LAIATCTTGNGEYLMKTLLAREICHGAFSSDCAVTSLHKTFKQKFLDSPLL---PRQQDLYAGALTLLYYPGQSSG 314
Cdd:cd04514 187 PddkTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREESDEDEILRSFIESDFMghpGVKNSPSAGAIGVLAVKKTRSG 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 442632688 315 -EVMWSHTTQSFCVGYMATNQRVPKFVHSPLPtysvPGRSCVVNGHNFHLR 364
Cdd:cd04514 267 vELYFAHNTDSFALASMSSSDRKPKCVMSRLP----GNGSIAQGGRKIRLR 313
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
4-338 |
7.55e-75 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 237.46 E-value: 7.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 4 FVAVHTGAG--NCIDETKYQRVIKEACLRATEILRNG-GSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAAIMD 80
Cdd:PLN02937 13 FVAVHVGAGyhAPSNEKALRSAMRRACLAAAAILRQGsGGCIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASIMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 81 GSTLNFGACTNVSRVKNPIQLARRICDAQ-SSPQLLERIPPMILAGTGAEHYADEVGCSMVEP-----GVLISSKAKFQF 154
Cdd:PLN02937 93 GDSGAFGAVGAVPGVRNAIQIAALLAKEQmMGSSLLGRIPPMFLVGEGARQWAKSKGIDLPETveeaeKWLVTERAKEQW 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 155 NHYKSKYDLVVNSRLGKATSEESV-------QVPEPGNEVELAAA---------LDTVGAVCVDGAGNTAAGCSSGGILL 218
Cdd:PLN02937 173 KKYKTMLASAIAKSSCDSQSTSKLseleaprSNPSNGTGGGQSSMctasdedciMDTVGVICVDSEGNIASGASSGGIAM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 219 KVPGRVGQAATYGAGCWATDTD----ELAIATCTTGNGEYLMKTLLAREICHGAFSSDCA-VTSLHKTFKQKFLDSplLP 293
Cdd:PLN02937 253 KVSGRVGLAAMYGSGCWASSKGpfgaPFIVGCCVSGAGEYLMRGFAARECCVSSSLSQAGpASACMKVLRSVIQGS--SA 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 442632688 294 RQQDLYAGALTL-----LYYPGQSSG----EVMWSHTTQSFCVGYMATNQRVPK 338
Cdd:PLN02937 331 KTTDKDAGILLVqadasVMAPGNSPSlkavEIAAAYSSLSFGIGYFGSSMERPK 384
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
5-265 |
1.59e-64 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 207.27 E-value: 1.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 5 VAVHTGAGNC-------IDETKYQRVIKEACLRATEILRNGGSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAA 77
Cdd:COG1446 8 LIIHGGAGTIarsamtpEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 78 IMDGSTLNFGACTNVSRVKNPIQLARRicdaqsspqLLERIPPMILAGTGAEHYADEVGCSMVEPGVLISSKAKFQFnhy 157
Cdd:COG1446 88 IMDGATLRAGAVAGVTRIKNPISLARA---------VMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQW--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 158 kskydlvvnsrlgKATSEESVQVPEPGnevelaaaLDTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYGAGCWAt 237
Cdd:COG1446 156 -------------KKALEYKPIINERK--------HGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYA- 213
|
250 260
....*....|....*....|....*...
gi 442632688 238 dTDELAIATCtTGNGEYLMKTLLAREIC 265
Cdd:COG1446 214 -DNEVGAVSA-TGHGEYFIRTVVAHDIV 239
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
5-265 |
2.54e-59 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 193.95 E-value: 2.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 5 VAVHTGAGNCID----ETKYQRVIKEACLRATEILRNGGSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAAIMD 80
Cdd:pfam01112 2 LVIHGGAGSILRtkerEEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIMD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 81 GSTLNFGACTNVSRVKNPIQLARRicdaqsspqLLERIPPMILAGTGAEHYADEVGCSMVEPGVLISSKAKFQFNHYKSk 160
Cdd:pfam01112 82 GKTLRAGAVAGVSRIKNPISLARA---------VMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARK- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 161 ydlvvnsrlGKATSEESVQVPEPGNEVELAAALDTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYGAGCWAtDTD 240
Cdd:pfam01112 152 ---------ENFQPNMALNVAPDPLKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYA-DNA 221
|
250 260
....*....|....*....|....*
gi 442632688 241 ELAIAtcTTGNGEYLMKTLLAREIC 265
Cdd:pfam01112 222 TGAVS--ATGHGEDIIRETLAYDIV 244
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
3-364 |
7.98e-120 |
|
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: 348.88 E-value: 7.98e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 3 GFVAVHTGAGNCID--ETKYQRVIKEACLRATEILRNGGSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAAIMD 80
Cdd:cd04514 1 FFVAVHAGAGYHSPsnEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 81 GSTLNFGACTNVSRVKNPIQLARRICDAQSSPQLLERIPPMILAGTGAEHYADEVGCSMvepgvlisskakfqfnhyksk 160
Cdd:cd04514 81 GSSGRFGAVGAVSGVKNPIQLARLLLKEQRKPLSLGRVPPMFLVGEGAREWAKSKGIIT--------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 161 ydlvvnsrlgkatseesvqvpepgnevelaaalDTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYGAGCWATDTD 240
Cdd:cd04514 140 ---------------------------------DTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRD 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 241 E---LAIATCTTGNGEYLMKTLLAREICHGAFSSDCAVTSLHKTFKQKFLDSPLL---PRQQDLYAGALTLLYYPGQSSG 314
Cdd:cd04514 187 PddkTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREESDEDEILRSFIESDFMghpGVKNSPSAGAIGVLAVKKTRSG 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 442632688 315 -EVMWSHTTQSFCVGYMATNQRVPKFVHSPLPtysvPGRSCVVNGHNFHLR 364
Cdd:cd04514 267 vELYFAHNTDSFALASMSSSDRKPKCVMSRLP----GNGSIAQGGRKIRLR 313
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
4-338 |
7.55e-75 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 237.46 E-value: 7.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 4 FVAVHTGAG--NCIDETKYQRVIKEACLRATEILRNG-GSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAAIMD 80
Cdd:PLN02937 13 FVAVHVGAGyhAPSNEKALRSAMRRACLAAAAILRQGsGGCIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASIMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 81 GSTLNFGACTNVSRVKNPIQLARRICDAQ-SSPQLLERIPPMILAGTGAEHYADEVGCSMVEP-----GVLISSKAKFQF 154
Cdd:PLN02937 93 GDSGAFGAVGAVPGVRNAIQIAALLAKEQmMGSSLLGRIPPMFLVGEGARQWAKSKGIDLPETveeaeKWLVTERAKEQW 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 155 NHYKSKYDLVVNSRLGKATSEESV-------QVPEPGNEVELAAA---------LDTVGAVCVDGAGNTAAGCSSGGILL 218
Cdd:PLN02937 173 KKYKTMLASAIAKSSCDSQSTSKLseleaprSNPSNGTGGGQSSMctasdedciMDTVGVICVDSEGNIASGASSGGIAM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 219 KVPGRVGQAATYGAGCWATDTD----ELAIATCTTGNGEYLMKTLLAREICHGAFSSDCA-VTSLHKTFKQKFLDSplLP 293
Cdd:PLN02937 253 KVSGRVGLAAMYGSGCWASSKGpfgaPFIVGCCVSGAGEYLMRGFAARECCVSSSLSQAGpASACMKVLRSVIQGS--SA 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 442632688 294 RQQDLYAGALTL-----LYYPGQSSG----EVMWSHTTQSFCVGYMATNQRVPK 338
Cdd:PLN02937 331 KTTDKDAGILLVqadasVMAPGNSPSlkavEIAAAYSSLSFGIGYFGSSMERPK 384
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
5-265 |
1.59e-64 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 207.27 E-value: 1.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 5 VAVHTGAGNC-------IDETKYQRVIKEACLRATEILRNGGSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAA 77
Cdd:COG1446 8 LIIHGGAGTIarsamtpEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 78 IMDGSTLNFGACTNVSRVKNPIQLARRicdaqsspqLLERIPPMILAGTGAEHYADEVGCSMVEPGVLISSKAKFQFnhy 157
Cdd:COG1446 88 IMDGATLRAGAVAGVTRIKNPISLARA---------VMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQW--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 158 kskydlvvnsrlgKATSEESVQVPEPGnevelaaaLDTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYGAGCWAt 237
Cdd:COG1446 156 -------------KKALEYKPIINERK--------HGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYA- 213
|
250 260
....*....|....*....|....*...
gi 442632688 238 dTDELAIATCtTGNGEYLMKTLLAREIC 265
Cdd:COG1446 214 -DNEVGAVSA-TGHGEYFIRTVVAHDIV 239
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
5-330 |
3.08e-63 |
|
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: 202.03 E-value: 3.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 5 VAVHTGAGNCIDETK--YQRVIKEACLRATEILRNGGSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAAIMDGS 82
Cdd:cd04512 2 LIVHGGAGTIEDEDAeaYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIMDGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 83 TLNFGACTNVSRVKNPIQLARRIcdaqsspqlLERIPPMILAGTGAEHYADEVGcsmvepgvlisskakfqfnhykskyd 162
Cdd:cd04512 82 TLNAGAVAGVKGVKNPISLARAV---------MEKTPHVLLVGEGAERFAREHG-------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 163 lvvnsrlgkatseesvqvpepgnevelaaaLDTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYGAGCWAtdTDEL 242
Cdd:cd04512 127 ------------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYA--DNET 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 243 AIATCtTGNGEYLMKTLLAREICH---GAFSSDCAVtslhktfkQKFLDspLLPRQQDLYAGALTLlyypgQSSGEVMWS 319
Cdd:cd04512 175 GAVSA-TGHGESIIRTVLAKRIADlveFGGSAQEAA--------EAAID--YLRRRVGGEGGLIVV-----DPDGRLGAA 238
|
330
....*....|.
gi 442632688 320 HTTQSFCVGYM 330
Cdd:cd04512 239 HNTPGMAFAYI 249
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
5-265 |
2.54e-59 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 193.95 E-value: 2.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 5 VAVHTGAGNCID----ETKYQRVIKEACLRATEILRNGGSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAAIMD 80
Cdd:pfam01112 2 LVIHGGAGSILRtkerEEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIMD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 81 GSTLNFGACTNVSRVKNPIQLARRicdaqsspqLLERIPPMILAGTGAEHYADEVGCSMVEPGVLISSKAKFQFNHYKSk 160
Cdd:pfam01112 82 GKTLRAGAVAGVSRIKNPISLARA---------VMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARK- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 161 ydlvvnsrlGKATSEESVQVPEPGNEVELAAALDTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYGAGCWAtDTD 240
Cdd:pfam01112 152 ---------ENFQPNMALNVAPDPLKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYA-DNA 221
|
250 260
....*....|....*....|....*
gi 442632688 241 ELAIAtcTTGNGEYLMKTLLAREIC 265
Cdd:pfam01112 222 TGAVS--ATGHGEDIIRETLAYDIV 244
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
5-266 |
2.29e-58 |
|
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: 190.86 E-value: 2.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 5 VAVHTGAGNCIDETK--YQRVIKEACLRATEILRNGGSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAAIMDGS 82
Cdd:cd04702 4 IVVHGGAGSIPDDRIkgSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASIMDGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 83 TLNFGACTNVSRVKNPIQLARRIcdaqsspqlLERIPPMILAGTGAEHYADEVGCSMVEPGVLISSKAKFQFNHYKSkyd 162
Cdd:cd04702 84 TLRAGAVSAVRNIANPISLARLV---------MEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKK--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 163 lvvnsrlgkatseesvqvpEPGNEVELAA-ALDTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYGAGCWAtdtDE 241
Cdd:cd04702 152 -------------------EKGANVEDTQrGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYA---DN 209
|
250 260
....*....|....*....|....*
gi 442632688 242 LAIATCTTGNGEYLMKTLLAREICH 266
Cdd:cd04702 210 LVGAVSTTGHGESIMKVNLARLILF 234
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
5-266 |
1.15e-52 |
|
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: 175.34 E-value: 1.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 5 VAVHTGAGNCIDET-------KYQRVIKEACLRATEILRNGGSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAA 77
Cdd:cd04701 2 LAIHGGAGTISRANltperyaAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 78 IMDGSTLNFGACTNVSRVKNPIQLARRicdaqsspqLLERIPPMILAGTGAEHYADEVGCSMVEPGvlisskakfqfnhy 157
Cdd:cd04701 82 IMDGRTKRAGAVAGLRRVRNPILLARA---------VLEKSPHVLLSGEGAEEFAREQGLELVPQG-------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 158 kskydlvvnsrlgkatseesvqvpepgnevelaaaldTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYGAGCWAt 237
Cdd:cd04701 139 -------------------------------------TVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWA- 180
|
250 260
....*....|....*....|....*....
gi 442632688 238 dtDELAIATCTTGNGEYLMKTLLAREICH 266
Cdd:cd04701 181 --EEWAVAVSGTGNGDSFIRVAAARDVAA 207
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
5-265 |
1.76e-48 |
|
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: 163.90 E-value: 1.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 5 VAVHTGAGN---CIDETKYQRVIKEACLRATEILRNGgSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAAIMDG 81
Cdd:cd14950 2 LVVHGGAGSwknSDDEEKALRALREALERGYEALRRG-SALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDAGIMDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 82 STLNFGACTNVSRVKNPIQLARRIcdaqsspqlLERIPPMILAGTGAEHYADEVGcsmvepgvlisskakfqfnhyksky 161
Cdd:cd14950 81 RTLRVGAVAAVRAVKNPIRLARKV---------MEKTDHVLIVGEGADELAKRLG------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 162 dlvvnsrlgkatseesvqvpepgnevelaaaLDTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYGAGCWATDtde 241
Cdd:cd14950 127 -------------------------------GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN--- 172
|
250 260
....*....|....*....|....
gi 442632688 242 lAIATCTTGNGEYLMKTLLAREIC 265
Cdd:cd14950 173 -GVAVSATGIGEVIIRSLPALRAD 195
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
1-264 |
4.19e-43 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 152.17 E-value: 4.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 1 MAGF-VAVHTGAGNcIDET---KYQRVIKEACLRATEI----LRNGGSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSV 72
Cdd:PLN02689 1 MGGWaIALHGGAGD-IDPNlprERQEEAEAALRRCLDLgiaaLRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 73 QCDAAIMDGSTLNFGACTNVSRVKNPIQLARRIcdaqsspqlLERIPPMILAGTGAEHYADEVGCSMVEPGVLISSKakf 152
Cdd:PLN02689 80 EMEASIMDGRTRRCGAVSGLTTVVNPISLARLV---------MEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEE--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 153 qfNHYKSKYDLVVNSRLGKATSEESVQVPEPGNEVELAAALDTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYGA 232
Cdd:PLN02689 148 --NVERLKQAKEANSVQFDYRIPLDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGA 225
|
250 260 270
....*....|....*....|....*....|..
gi 442632688 233 GCWATDtdelAIATCTTGNGEYLMKTLLAREI 264
Cdd:PLN02689 226 GTYANH----LCAVSATGKGEAIIRGTVARDV 253
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
25-264 |
3.25e-37 |
|
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: 135.77 E-value: 3.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 25 KEACLRATEILRNGGSAVDACEAAI--VRLENCGYTnAGYGSNLCMDGSVQCDAAIMDGSTLNFGACTNVSRVKNPIQLA 102
Cdd:cd04513 9 TEAVEAAWEVLQKGGSALDAVEAGCsvCEDDQCDGS-VGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 103 RRicdaqsspqLLERIPPMILAGTGAEHYADEVGcsmVEPGVLISSKA-----KFQFNHYKSKYdlVVNSRLGKATSEES 177
Cdd:cd04513 88 RA---------VMEHTPHSLLVGEGATEFAVSMG---FKEENLLTEESrkmwkKWLKENCQPNF--WKNVVPDPSKSCSS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 178 VQVPEPGNEVELAAALDTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYGAGCWAtDtDELAIATCtTGNGEYLMK 257
Cdd:cd04513 154 PKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYA-D-NEVGAAAA-TGDGDIMMR 230
|
....*..
gi 442632688 258 TLLAREI 264
Cdd:cd04513 231 FLPSYQA 237
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
5-264 |
3.97e-37 |
|
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: 133.92 E-value: 3.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 5 VAVHTGAGnciDETKYQRVIKEACLRATEILRNGGSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAAIMDgSTL 84
Cdd:cd04703 3 VLVHGGAG---SDPERQDGLERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAVMT-SGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 85 NFGACTNVSRVKNPIQLARRIcdaqsspqlLERIPPMILAGTGAEHYADEVGcsmVEPGVlisskakfqfnhykskydlv 164
Cdd:cd04703 79 AFGAVAAIEGVKNPVLVARAV---------METSPHVLLAGDGAVRFARRLG---YPDGC-------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 165 vnsrlgkatseesvqvpepgnevelaaalDTVGAVCVDGaGNTAAGCSSGGILLKVPGRVGQAATYGAGCWATDTDelai 244
Cdd:cd04703 127 -----------------------------DTVGAVARDG-GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKG---- 172
|
250 260
....*....|....*....|
gi 442632688 245 ATCTTGNGEYLMKTLLAREI 264
Cdd:cd04703 173 AVAATGIGEEIAKRLLARRV 192
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
5-264 |
1.11e-36 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 135.08 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 5 VAVHTGAGNCI-------DETKYQRVIKEACLRATEILRNGGSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAA 77
Cdd:PRK10226 6 IAIHGGAGAISraqmslqQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDAC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 78 IMDGSTLNFGACTNVSRVKNPIQLARRIcdaqsspqlLERIPPMILAGTGAEHYADEVGCSMVEPGvLISSKAKFQfnhy 157
Cdd:PRK10226 86 VMDGNTLKAGAVAGVSHLRNPVLAARLV---------MEQSPHVMMIGEGAENFAFAHGMERVSPE-IFSTPLRYE---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 158 kskydlvvnsRLGKATSEESVQVPEPGNEVELAAALDTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYGAGCWAT 237
Cdd:PRK10226 152 ----------QLLAARAEGATVLDHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYAN 221
|
250 260
....*....|....*....|....*..
gi 442632688 238 DTdelAIATCTTGNGEYLMKTLLAREI 264
Cdd:PRK10226 222 NA---SVAVSCTGTGEVFIRALAAYDI 245
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
7-322 |
2.02e-27 |
|
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: 109.23 E-value: 2.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 7 VHTGAGNCIDETKYQRVIKEACL-----RATEILRNGgSAVDACEAAIVRLENCGYTNAGYGSNLCMDGSVQCDAAIMDG 81
Cdd:cd14949 5 IHGGFGSESSTNGETKAAKQEALaeiveEVYEYLKSH-SALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQIRMSASLMDG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 82 STLNFGACTNVSRVKNPIQLArricdaqsspQLLERIPPMILAGTGAEHYADEVGcsmvepgvlisskakFQFnhykskY 161
Cdd:cd14949 84 QTQRFSGVINIENVKNPIEVA----------QKLQQEDDRVLSGEGATEFARENG---------------FPE------Y 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 162 DLVVNSRLgkaTSEESVQVPEPGnevelaaaLDTVGAVCVDGAGNTAAGCSSGGILLKVPGRVGQAATYgAGCWATdtdE 241
Cdd:cd14949 133 NPETPQRR---QEYEEKKLKSGG--------TGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNYAN---A 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442632688 242 LAIATCtTGNGEYLMKTLLAREIChgafssdCAVT---SLHKTFKQKFLDSpllpRQQDLYAGALTLlyypgQSSGEVMW 318
Cdd:cd14949 198 FAGVSC-TGIGEDIVSEALAAKIV-------TRVTdgmSLQEAFEKSFAEA----KPRDGFAGAIGI-----DSKGNIYH 260
|
....
gi 442632688 319 SHTT 322
Cdd:cd14949 261 GDTH 264
|
|
| |
