|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
2-347 |
2.21e-117 |
|
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: 341.94 E-value: 2.21e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 2 QAIEKLQAGALATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEg 81
Cdd:cd04514 30 AAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKE- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 82 QKGKLSAGRIPPCFLVGEGAYRWAVDHGIPscppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsg 161
Cdd:cd04514 109 QRKPLSLGRVPPMFLVGEGAREWAKSKGII-------------------------------------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 162 aLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHNPYSTAVSTSGCGEHLVRTILARECSHAL 241
Cdd:cd04514 139 -TDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 242 QAEDAHQ-ALLETMQNKFISSPFLASEDG---VLGGVIVLRSCRcpsesdpsqdKQTLLVEFLWSHSTESMCVGYMSAQD 317
Cdd:cd04514 218 YHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSD 287
|
330 340 350
....*....|....*....|....*....|
gi 1958761949 318 GKAKTHISRLPPGAvagqSVAIEGGVCRLE 347
Cdd:cd04514 288 RKPKCVMSRLPGNG----SIAQGGRKIRLR 313
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
15-326 |
1.09e-70 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 226.28 E-value: 1.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 15 DAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPC 94
Cdd:PLN02937 55 DAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPM 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 95 FLVGEGAYRWAVDHGIPScpPSTMT-------TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDS 160
Cdd:PLN02937 135 FLVGEGARQWAKSKGIDL--PETVEeaekwlvTERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 161 GA------------LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEH 227
Cdd:PLN02937 213 GQssmctasdedciMDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 228 LVRTILARECSHAL---QAEDAHQA---LLETMQNkfiSSPFLASEDgvlGGVIVLRSCRcpSESDPSQDKQTLLVEFLW 301
Cdd:PLN02937 293 LMRGFAARECCVSSslsQAGPASACmkvLRSVIQG---SSAKTTDKD---AGILLVQADA--SVMAPGNSPSLKAVEIAA 364
|
330 340
....*....|....*....|....*
gi 1958761949 302 SHSTESMCVGYMSAQDGKAKTHISR 326
Cdd:PLN02937 365 AYSSLSFGIGYFGSSMERPKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
5-324 |
3.05e-61 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 198.41 E-value: 3.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 5 EKLQAGALATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLcegqkg 84
Cdd:COG1446 43 AVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISLARAVM------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 85 klsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaaFKRNKRKLelaervetdfiQLKRRRQSSAKENDSGaLD 164
Cdd:COG1446 117 ----EKTPHVLLVGEGAERFAREQGLELVDPLY---------FFTEKRWK-----------QWKKALEYKPIINERK-HG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 165 TVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECSHALQA- 243
Cdd:COG1446 172 TVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVG------AVSATGHGEYFIRTVVAHDIVERMRQg 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 244 EDAHQALLETMQNKfisspflASEDGVLGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSAqDGKAKTH 323
Cdd:COG1446 246 LSLQEAAEEVIERI-------LKKLGGDGGLIAV-------------DKDG---NIAAPFNTEGMYRAYIDG-DGELVVA 301
|
.
gi 1958761949 324 I 324
Cdd:COG1446 302 I 302
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
3-315 |
8.27e-56 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 184.32 E-value: 8.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 3 AIEKLQAGALATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAhRLLCEGQ 82
Cdd:pfam01112 32 GYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLA-RAVMEKT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 83 KGKLsagrippcfLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKrklelaervETDFIQLKRRRQSSA--KENDS 160
Cdd:pfam01112 111 PHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQKAR---------KENFQPNMALNVAPDplKECGD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 161 GALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECS-- 238
Cdd:pfam01112 173 SKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVar 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958761949 239 --HALQAEDAHQALLETMQNKFisspflasedGVLGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSA 315
Cdd:pfam01112 247 meYGLSLEEAADKVITEMLKRV----------GGDGGVIAV-------------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 ... |
2-347 |
2.21e-117 |
|
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: 341.94 E-value: 2.21e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 2 QAIEKLQAGALATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEg 81
Cdd:cd04514 30 AAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKE- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 82 QKGKLSAGRIPPCFLVGEGAYRWAVDHGIPscppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsg 161
Cdd:cd04514 109 QRKPLSLGRVPPMFLVGEGAREWAKSKGII-------------------------------------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 162 aLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHNPYSTAVSTSGCGEHLVRTILARECSHAL 241
Cdd:cd04514 139 -TDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 242 QAEDAHQ-ALLETMQNKFISSPFLASEDG---VLGGVIVLRSCRcpsesdpsqdKQTLLVEFLWSHSTESMCVGYMSAQD 317
Cdd:cd04514 218 YHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSD 287
|
330 340 350
....*....|....*....|....*....|
gi 1958761949 318 GKAKTHISRLPPGAvagqSVAIEGGVCRLE 347
Cdd:cd04514 288 RKPKCVMSRLPGNG----SIAQGGRKIRLR 313
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
2-313 |
1.80e-80 |
|
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: 245.55 E-value: 1.80e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 2 QAIEKLQAGALATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEG 81
Cdd:cd04512 29 AGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLARAVMEKT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 82 qkgklsagriPPCFLVGEGAYRWAVDHGipscppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsg 161
Cdd:cd04512 109 ----------PHVLLVGEGAERFAREHG---------------------------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 162 aLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTgahnpySTAVSTSGCGEHLVRTILARECSHAL 241
Cdd:cd04512 127 -HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNE------TGAVSATGHGESIIRTVLAKRIADLV 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958761949 242 QAEDAHQALLETMQNKfisspfLASEDGVLGGVIVLrscrcpsesdpsqDKQtllVEFLWSHSTESMCVGYM 313
Cdd:cd04512 200 EFGGSAQEAAEAAIDY------LRRRVGGEGGLIVV-------------DPD---GRLGAAHNTPGMAFAYI 249
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
15-326 |
1.09e-70 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 226.28 E-value: 1.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 15 DAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPC 94
Cdd:PLN02937 55 DAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPM 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 95 FLVGEGAYRWAVDHGIPScpPSTMT-------TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDS 160
Cdd:PLN02937 135 FLVGEGARQWAKSKGIDL--PETVEeaekwlvTERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 161 GA------------LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEH 227
Cdd:PLN02937 213 GQssmctasdedciMDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEY 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 228 LVRTILARECSHAL---QAEDAHQA---LLETMQNkfiSSPFLASEDgvlGGVIVLRSCRcpSESDPSQDKQTLLVEFLW 301
Cdd:PLN02937 293 LMRGFAARECCVSSslsQAGPASACmkvLRSVIQG---SSAKTTDKD---AGILLVQADA--SVMAPGNSPSLKAVEIAA 364
|
330 340
....*....|....*....|....*
gi 1958761949 302 SHSTESMCVGYMSAQDGKAKTHISR 326
Cdd:PLN02937 365 AYSSLSFGIGYFGSSMERPKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
5-324 |
3.05e-61 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 198.41 E-value: 3.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 5 EKLQAGALATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLcegqkg 84
Cdd:COG1446 43 AVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISLARAVM------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 85 klsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaaFKRNKRKLelaervetdfiQLKRRRQSSAKENDSGaLD 164
Cdd:COG1446 117 ----EKTPHVLLVGEGAERFAREQGLELVDPLY---------FFTEKRWK-----------QWKKALEYKPIINERK-HG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 165 TVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECSHALQA- 243
Cdd:COG1446 172 TVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVG------AVSATGHGEYFIRTVVAHDIVERMRQg 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 244 EDAHQALLETMQNKfisspflASEDGVLGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSAqDGKAKTH 323
Cdd:COG1446 246 LSLQEAAEEVIERI-------LKKLGGDGGLIAV-------------DKDG---NIAAPFNTEGMYRAYIDG-DGELVVA 301
|
.
gi 1958761949 324 I 324
Cdd:COG1446 302 I 302
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
5-277 |
2.96e-56 |
|
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: 185.08 E-value: 2.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 5 EKLQAGALATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAhRLLCEgqkg 84
Cdd:cd04702 34 SVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLA-RLVME---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 85 klsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKRKlelaervetdfiqlkrrrQSSAKENDSGALD 164
Cdd:cd04702 109 -----KTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKE------------------KGANVEDTQRGHG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 165 TVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgahnpYSTAVSTSGCGEHLVRTILARECSHALQ-- 242
Cdd:cd04702 166 TVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADN------LVGAVSTTGHGESIMKVNLARLILFHMEqg 239
|
250 260 270
....*....|....*....|....*....|....*..
gi 1958761949 243 --AEDAHQALLETMQNKFisspflasedGVLGGVIVL 277
Cdd:cd04702 240 ktAEEAAELALAYMKSRV----------KGLGGLIVV 266
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
3-315 |
8.27e-56 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 184.32 E-value: 8.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 3 AIEKLQAGALATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAhRLLCEGQ 82
Cdd:pfam01112 32 GYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLA-RAVMEKT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 83 KGKLsagrippcfLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKrklelaervETDFIQLKRRRQSSA--KENDS 160
Cdd:pfam01112 111 PHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQKAR---------KENFQPNMALNVAPDplKECGD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 161 GALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECS-- 238
Cdd:pfam01112 173 SKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVar 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958761949 239 --HALQAEDAHQALLETMQNKFisspflasedGVLGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSA 315
Cdd:pfam01112 247 meYGLSLEEAADKVITEMLKRV----------GGDGGVIAV-------------DAKG---NIAAPFNTEGMYRAYHTG 299
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
5-277 |
1.35e-43 |
|
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: 151.07 E-value: 1.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 5 EKLQAGALATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGqkg 84
Cdd:cd04701 37 AVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKS--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 85 klsagriPPCFLVGEGAYRWAVDHGIPSCPPStmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgald 164
Cdd:cd04701 114 -------PHVLLSGEGAEEFAREQGLELVPQG------------------------------------------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 165 TVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgahnpYSTAVSTSGCGEHLVRTILARECSHalQAE 244
Cdd:cd04701 139 TVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEE------WAVAVSGTGNGDSFIRVAAARDVAA--RMR 210
|
250 260 270
....*....|....*....|....*....|...
gi 1958761949 245 DAHQALLETMqnKFISSPFLASEDGVlGGVIVL 277
Cdd:cd04701 211 YKGLSLAEAA--KEVVGPGGELGEGE-GGIIAI 240
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
3-314 |
1.99e-42 |
|
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: 147.73 E-value: 1.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 3 AIEKLQAGAlATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGq 82
Cdd:cd14950 31 GYEALRRGS-ALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIRLARKVMEKT- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 83 kgklsagriPPCFLVGEGAYRWAVDHGipscppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsga 162
Cdd:cd14950 109 ---------DHVLIVGEGADELAKRLG----------------------------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 163 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgahnpySTAVSTSGCGEHLVRTILARECSHA-- 240
Cdd:cd14950 127 GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN-------GVAVSATGIGEVIIRSLPALRADELvs 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958761949 241 --LQAEDAHQALLETMQNKFISSpflasedgvLGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMS 314
Cdd:cd14950 200 mgGDIEEAVRAVVNKVTETFGKD---------TAGIIGI-------------DARG---NIAAAFNTEAMPRGYID 250
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
3-236 |
4.38e-42 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 149.09 E-value: 4.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 3 AIEKLQAGALATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAhRLLCEgq 82
Cdd:PLN02689 38 GIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLA-RLVME-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 83 kgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRfslaafkRNKRKLELAE---RVETDFIQ--LKRRRQSSAKE 157
Cdd:PLN02689 115 -------KTPHIYLAFDGAEAFARQQGVETVDNSYFITE-------ENVERLKQAKeanSVQFDYRIplDKPAKAAALAA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958761949 158 NDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGahnpystAVSTSGCGEHLVRTILARE 236
Cdd:PLN02689 181 DGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYANHLC-------AVSATGKGEAIIRGTVARD 252
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
2-236 |
6.91e-40 |
|
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: 142.32 E-value: 6.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 2 QAIEKLQAGALATDAVMAALVELEDSPF-TNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLce 80
Cdd:cd04513 14 AAWEVLQKGGSALDAVEAGCSVCEDDQCdGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVARAVM-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 81 gqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKRKLELAERVETD-----FIQLKRRRQSSA 155
Cdd:cd04513 92 --------EHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDpskscSSPKAPSRSESA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 156 KENDSGalDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT-GAhnpystAVSTsGCGEHLVRTILA 234
Cdd:cd04513 164 IPEDNH--DTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEvGA------AAAT-GDGDIMMRFLPS 234
|
..
gi 1958761949 235 RE 236
Cdd:cd04513 235 YQ 236
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
7-234 |
4.85e-35 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 130.07 E-value: 4.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 7 LQAGALATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVsVAHRLLCEgqkgkl 86
Cdd:PRK10226 43 LEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPV-LAARLVME------ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 87 sagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTrfslaafkrNKRKLELAERVETDFIQLKrrrQSSAKENDSGALDTV 166
Cdd:PRK10226 116 ---QSPHVMMIGEGAENFAFAHGMERVSPEIFST---------PLRYEQLLAARAEGATVLD---HSGAPLDEKQKMGTV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958761949 167 GAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTgahnpySTAVSTSGCGEHLVRTILA 234
Cdd:PRK10226 181 GAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNA------SVAVSCTGTGEVFIRALAA 242
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
3-277 |
1.90e-34 |
|
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: 126.60 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 3 AIEKLQAGALATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSlSFGAVGALSGIKNPVSVAHRLLCEGq 82
Cdd:cd04703 26 GLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVARAVMETS- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 83 kgklsagriPPCFLVGEGAYRWAVDHGIP-SCppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsg 161
Cdd:cd04703 104 ---------PHVLLAGDGAVRFARRLGYPdGC------------------------------------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 162 alDTVGAVVVDHeGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGahnpystAVSTSGCGEHLVRTILARECSHAL 241
Cdd:cd04703 127 --DTVGAVARDG-GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKG-------AVAATGIGEEIAKRLLARRVYRWI 196
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958761949 242 QAEDAHQALLETMQNKFisspflasEDGVLGGVIVL 277
Cdd:cd04703 197 ETGLSLQAAAQRAIDEF--------DDGVAVGVIAV 224
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
2-234 |
3.95e-25 |
|
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: 102.69 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 2 QAIEKLQAGAlATDAVMAALVELEDSPFTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEG 81
Cdd:cd14949 33 EVYEYLKSHS-ALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQIRMSASLMDGQTQRFSGVINIENVKNPIEVAQKLQQED 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761949 82 QKgklsagrippcFLVGEGAYRWAVDHGIPSCPPstmttrfslaafkrnkrklelaervETDFiqlkRRRQSSAKENDSG 161
Cdd:cd14949 112 DR-----------VLSGEGATEFARENGFPEYNP-------------------------ETPQ----RRQEYEEKKLKSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958761949 162 ALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAAlygcgcwaenTGAHNpYST---AVSTSGCGEHLVRTILA 234
Cdd:cd14949 152 GTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSA----------TVAGN-YANafaGVSCTGIGEDIVSEALA 216
|
|
| |
