|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
42-416 |
1.67e-138 |
|
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: 398.57 E-value: 1.67e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDASIMD 121
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 122 GKSLNFGAVGALSGIKNPVSVANRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpscppnimttrfslaafkrnkr 201
Cdd:cd04514 81 GSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI---------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 202 klelaervdtdfmqlkkrrqssekendsgTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAH 281
Cdd:cd04514 138 -----------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPD 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 282 NPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLASEDG---VLGGVIVLRscrcsaepds 357
Cdd:cd04514 189 DKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVL---------- 258
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
2A8J_A 358 SQNKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 416
Cdd:cd04514 259 AVKKTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
34-395 |
2.64e-85 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 266.35 E-value: 2.64e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 34 QSYKEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALAT-DAVTAALVELEDSPFTNAGMGSNLNLLGE 112
Cdd:PLN02937 4 DGADQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCiDAVSAAIQVLEDDPSTNAGRGSNLTEDGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 113 IECDASIMDGKSLNFGAVGALSGIKNPVSVANRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIP-----SCPPNIM 187
Cdd:PLN02937 84 VECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDlpetvEEAEKWL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 188 TTRFSLAAFKRNKRKLELAE-------RVDTDFMQLKKRRQSSEKENDSGT------------LDTVGAVVVDHEGNVAA 248
Cdd:PLN02937 164 VTERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 249 AVSSGGLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEHLVRTILARECSHAL---QAEDAHQA---LLE 321
Cdd:PLN02937 244 GASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSSslsQAGPASACmkvLRS 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2A8J_A 322 TMQNkfiSSPFLASEDgvlGGVIVLRSCRCSAEPDSSQNKQTllVEFLWSHTTESMCVGYMSAQDGKAKTHISR 395
Cdd:PLN02937 324 VIQG---SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
44-393 |
1.84e-66 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 214.20 E-value: 1.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDAS 118
Cdd:COG1446 8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 119 IMDGKSLNFGAVGALSGIKNPVSVANRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPnimttrfslAAFKR 198
Cdd:COG1446 88 IMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDP---------LYFFT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 199 NKRklelaervdtdFMQLKKRRQSSEKENDSGTlDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 278
Cdd:COG1446 149 EKR-----------WKQWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 279 GAhnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspflASEDGVLGGVIVLrscrcsaepds 357
Cdd:COG1446 217 VG------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI-------LKKLGGDGGLIAV----------- 272
|
330 340 350
....*....|....*....|....*....|....*.
2A8J_A 358 sqNKQTllvEFLWSHTTESMCVGYMSAqDGKAKTHI 393
Cdd:COG1446 273 --DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
44-384 |
8.50e-59 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 194.34 E-value: 8.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDASIMD 121
Cdd:pfam01112 2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIMD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 122 GKSLNFGAVGALSGIKNPVSVAnRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCPPNIMTTRFSLAAFKRNKr 201
Cdd:pfam01112 82 GKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQKAR- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 202 klelaervDTDFmQLKKRRQSSEKENDSGTLD---TVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 278
Cdd:pfam01112 151 --------KENF-QPNMALNVAPDPLKECGDSkrgTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 279 GAhnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflasedGVLGGVIVLrscrcsae 354
Cdd:pfam01112 222 TG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV----------GGDGGVIAV-------- 277
|
330 340 350
....*....|....*....|....*....|
2A8J_A 355 pdssqNKQTllvEFLWSHTTESMCVGYMSA 384
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 ... |
42-416 |
1.67e-138 |
|
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: 398.57 E-value: 1.67e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDASIMD 121
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 122 GKSLNFGAVGALSGIKNPVSVANRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpscppnimttrfslaafkrnkr 201
Cdd:cd04514 81 GSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI---------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 202 klelaervdtdfmqlkkrrqssekendsgTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAH 281
Cdd:cd04514 138 -----------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPD 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 282 NPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLASEDG---VLGGVIVLRscrcsaepds 357
Cdd:cd04514 189 DKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVL---------- 258
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
2A8J_A 358 SQNKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 416
Cdd:cd04514 259 AVKKTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
44-382 |
8.95e-95 |
|
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: 284.84 E-value: 8.95e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDASIMDGK 123
Cdd:cd04512 2 LIVHGGAGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIMDGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 124 SLNFGAVGALSGIKNPVSVANRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscppnimttrfslaafkrnkrkl 203
Cdd:cd04512 82 TLNAGAVAGVKGVKNPISLARAVMEKT----------PHVLLVGEGAERFAREHG------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 204 elaervdtdfmqlkkrrqssekendsgtLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTgahnp 283
Cdd:cd04512 127 ----------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNE----- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 284 ySTAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKfisspfLASEDGVLGGVIVLRScrcsaepdssqnkqt 363
Cdd:cd04512 174 -TGAVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAEAAIDY------LRRRVGGEGGLIVVDP--------------- 231
|
330
....*....|....*....
2A8J_A 364 lLVEFLWSHTTESMCVGYM 382
Cdd:cd04512 232 -DGRLGAAHNTPGMAFAYI 249
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
34-395 |
2.64e-85 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 266.35 E-value: 2.64e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 34 QSYKEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALAT-DAVTAALVELEDSPFTNAGMGSNLNLLGE 112
Cdd:PLN02937 4 DGADQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCiDAVSAAIQVLEDDPSTNAGRGSNLTEDGH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 113 IECDASIMDGKSLNFGAVGALSGIKNPVSVANRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIP-----SCPPNIM 187
Cdd:PLN02937 84 VECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDlpetvEEAEKWL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 188 TTRFSLAAFKRNKRKLELAE-------RVDTDFMQLKKRRQSSEKENDSGT------------LDTVGAVVVDHEGNVAA 248
Cdd:PLN02937 164 VTERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 249 AVSSGGLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEHLVRTILARECSHAL---QAEDAHQA---LLE 321
Cdd:PLN02937 244 GASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSSslsQAGPASACmkvLRS 323
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2A8J_A 322 TMQNkfiSSPFLASEDgvlGGVIVLRSCRCSAEPDSSQNKQTllVEFLWSHTTESMCVGYMSAQDGKAKTHISR 395
Cdd:PLN02937 324 VIQG---SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
44-393 |
1.84e-66 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 214.20 E-value: 1.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDAS 118
Cdd:COG1446 8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 119 IMDGKSLNFGAVGALSGIKNPVSVANRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPnimttrfslAAFKR 198
Cdd:COG1446 88 IMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDP---------LYFFT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 199 NKRklelaervdtdFMQLKKRRQSSEKENDSGTlDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 278
Cdd:COG1446 149 EKR-----------WKQWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 279 GAhnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspflASEDGVLGGVIVLrscrcsaepds 357
Cdd:COG1446 217 VG------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI-------LKKLGGDGGLIAV----------- 272
|
330 340 350
....*....|....*....|....*....|....*.
2A8J_A 358 sqNKQTllvEFLWSHTTESMCVGYMSAqDGKAKTHI 393
Cdd:COG1446 273 --DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
44-346 |
3.92e-63 |
|
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: 204.73 E-value: 3.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDASIMDGK 123
Cdd:cd04702 4 IVVHGGAGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASIMDGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 124 SLNFGAVGALSGIKNPVSVAnRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPNIMTTRFSLAAFKRNKRKl 203
Cdd:cd04702 84 TLRAGAVSAVRNIANPISLA-RLVME---------KTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKE- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 204 elaervdtdfmqlkkrrQSSEKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgahnp 283
Cdd:cd04702 153 -----------------KGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADN------ 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2A8J_A 284 YSTAVSTSGCGEHLVRTILARECSHALQ----AEDAHQALLETMQNKFisspflasedGVLGGVIVL 346
Cdd:cd04702 210 LVGAVSTTGHGESIMKVNLARLILFHMEqgktAEEAAELALAYMKSRV----------KGLGGLIVV 266
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
44-384 |
8.50e-59 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 194.34 E-value: 8.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDASIMD 121
Cdd:pfam01112 2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIMD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 122 GKSLNFGAVGALSGIKNPVSVAnRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCPPNIMTTRFSLAAFKRNKr 201
Cdd:pfam01112 82 GKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQKAR- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 202 klelaervDTDFmQLKKRRQSSEKENDSGTLD---TVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 278
Cdd:pfam01112 151 --------KENF-QPNMALNVAPDPLKECGDSkrgTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 279 GAhnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflasedGVLGGVIVLrscrcsae 354
Cdd:pfam01112 222 TG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV----------GGDGGVIAV-------- 277
|
330 340 350
....*....|....*....|....*....|
2A8J_A 355 pdssqNKQTllvEFLWSHTTESMCVGYMSA 384
Cdd:pfam01112 278 -----DAKG---NIAAPFNTEGMYRAYHTG 299
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
46-346 |
1.39e-48 |
|
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: 166.10 E-value: 1.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 46 VHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDASIM 120
Cdd:cd04701 4 IHGGAGtisraNLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEASIM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 121 DGKSLNFGAVGALSGIKNPVSVAnRLLCEGQkgklsagriPPCFLVGEGAYRWAVDHGIPSCPPNimttrfslaafkrnk 200
Cdd:cd04701 84 DGRTKRAGAVAGLRRVRNPILLA-RAVLEKS---------PHVLLSGEGAEEFAREQGLELVPQG--------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 201 rklelaervdtdfmqlkkrrqssekendsgtldTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtga 280
Cdd:cd04701 139 ---------------------------------TVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEE--- 182
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
2A8J_A 281 hnpYSTAVSTSGCGEHLVRTILARECSHalQAEDAHQALLETMqnKFISSPFLASEDGVlGGVIVL 346
Cdd:cd04701 183 ---WAVAVSGTGNGDSFIRVAAARDVAA--RMRYKGLSLAEAA--KEVVGPGGELGEGE-GGIIAI 240
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
44-383 |
1.16e-45 |
|
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: 158.13 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 44 VLVHAGAGYHSESKAKE-YKHVCKRACQKAIEKLQAGAlATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDASIMDG 122
Cdd:cd14950 2 LVVHGGAGSWKNSDDEEkALRALREALERGYEALRRGS-ALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDAGIMDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 123 KSLNFGAVGALSGIKNPVSVANRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscppnimttrfslaafkrnkrk 202
Cdd:cd14950 81 RTLRVGAVAAVRAVKNPIRLARKVMEKT----------DHVLIVGEGADELAKRLG------------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 203 lelaervdtdfmqlkkrrqssekendsgtLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgahn 282
Cdd:cd14950 127 -----------------------------GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN----- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 283 pySTAVSTSGCGEHLVRTILARECSHA----LQAEDAHQALLETMQNKFISSpflasedgvLGGVIVLrscrcsaepDSS 358
Cdd:cd14950 173 --GVAVSATGIGEVIIRSLPALRADELvsmgGDIEEAVRAVVNKVTETFGKD---------TAGIIGI---------DAR 232
|
330 340
....*....|....*....|....*
2A8J_A 359 QNkqtllveFLWSHTTESMCVGYMS 383
Cdd:cd14950 233 GN-------IAAAFNTEAMPRGYID 250
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
46-305 |
3.22e-45 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 159.10 E-value: 3.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 46 VHAGAGYHSESKAKEYKHVCKRACQKA----IEKLQAGALATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDASIMD 121
Cdd:PLN02689 8 LHGGAGDIDPNLPRERQEEAEAALRRCldlgIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEASIMD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 122 GKSLNFGAVGALSGIKNPVSVAnRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPNIMTTRfslaafkRNKR 201
Cdd:PLN02689 88 GRTRRCGAVSGLTTVVNPISLA-RLVME---------KTPHIYLAFDGAEAFARQQGVETVDNSYFITE-------ENVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 202 KLELAE---RVDTDFMQ--LKKRRQSSEKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAE 276
Cdd:PLN02689 151 RLKQAKeanSVQFDYRIplDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYAN 230
|
250 260
....*....|....*....|....*....
2A8J_A 277 NTGahnpystAVSTSGCGEHLVRTILARE 305
Cdd:PLN02689 231 HLC-------AVSATGKGEAIIRGTVARD 252
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
66-305 |
1.97e-41 |
|
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: 148.09 E-value: 1.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 66 KRACQKAIEKLQAGALATDAVTAALVELEDSPF-TNAGMGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAN 144
Cdd:cd04513 9 TEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCdGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 145 RLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPpniMTTRFSLAAFKRNKRK------LELAERVDTDFMQLKK 218
Cdd:cd04513 89 AVM----------EHTPHSLLVGEGATEFAVSMGFKEEN---LLTEESRKMWKKWLKEncqpnfWKNVVPDPSKSCSSPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 219 RRQSSEKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT-GAhnpystAVSTsGCGEHL 297
Cdd:cd04513 156 APSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEvGA------AAAT-GDGDIM 228
|
....*...
2A8J_A 298 VRTILARE 305
Cdd:cd04513 229 MRFLPSYQ 236
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
44-346 |
1.33e-39 |
|
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: 142.01 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 44 VLVHAGAGyhsesKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDASIMDGK 123
Cdd:cd04703 3 VLVHGGAG-----SDPERQDGLERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAVMTSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 124 SlNFGAVGALSGIKNPVSVANRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIPScppnimttrfslaafkrnkrkl 203
Cdd:cd04703 78 G-AFGAVAAIEGVKNPVLVARAVMETS----------PHVLLAGDGAVRFARRLGYPD---------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 204 elaervdtdfmqlkkrrqssekendsgTLDTVGAVVVDHeGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGahnp 283
Cdd:cd04703 125 ---------------------------GCDTVGAVARDG-GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKG---- 172
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
2A8J_A 284 ystAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFisspflasEDGVLGGVIVL 346
Cdd:cd04703 173 ---AVAATGIGEEIAKRLLARRVYRWIETGLSLQAAAQRAIDEF--------DDGVAVGVIAV 224
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
44-303 |
6.69e-38 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 139.31 E-value: 6.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 44 VLVHAGAGYHSESK-----AKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDAS 118
Cdd:PRK10226 6 IAIHGGAGAISRAQmslqqELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDAC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 119 IMDGKSLNFGAVGALSGIKNPVsVANRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPNIMTTrfslaafkr 198
Cdd:PRK10226 86 VMDGNTLKAGAVAGVSHLRNPV-LAARLVME---------QSPHVMMIGEGAENFAFAHGMERVSPEIFST--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 199 NKRKLELAERVDTDFMQLKkrrQSSEKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 278
Cdd:PRK10226 147 PLRYEQLLAARAEGATVLD---HSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNA 223
|
250 260
....*....|....*....|....*
2A8J_A 279 gahnpySTAVSTSGCGEHLVRTILA 303
Cdd:PRK10226 224 ------SVAVSCTGTGEVFIRALAA 242
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
44-303 |
2.66e-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: 109.62 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 44 VLVHAGAGyhSESKAK-EYKHVCKRACQKAIEK----LQAGAlATDAVTAALVELEDSPFTNAGMGSNLNLLGEIECDAS 118
Cdd:cd14949 3 LIIHGGFG--SESSTNgETKAAKQEALAEIVEEvyeyLKSHS-ALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQIRMSAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 119 IMDGKSLNFGAVGALSGIKNPVSVANRLLCEGQKgklsagrippcFLVGEGAYRWAVDHGIPSCPPnIMTTRfslaafkr 198
Cdd:cd14949 80 LMDGQTQRFSGVINIENVKNPIEVAQKLQQEDDR-----------VLSGEGATEFARENGFPEYNP-ETPQR-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2A8J_A 199 nkrklelaervdtdfmqlkkRRQSSEKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAAlygcgcwaenT 278
Cdd:cd14949 140 --------------------RQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSA----------T 189
|
250 260
....*....|....*....|....*...
2A8J_A 279 GAHNpYST---AVSTSGCGEHLVRTILA 303
Cdd:cd14949 190 VAGN-YANafaGVSCTGIGEDIVSEALA 216
|
|
| |
