|
Name |
Accession |
Description |
Interval |
E-value |
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
32-338 |
2.65e-138 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 394.47 E-value: 2.65e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 32 PIIVIHGGTSGL---GLTKEEFTKREKVMKESLKAGQSILEKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELD 108
Cdd:COG1446 6 RALIIHGGAGTIarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 109 ASLMDGKNLKAGAVAMARTIKNPIEAARLVMEKTPHTLIAGEGADKLAKKHGLEIVGQKYFFTEHRYKQLQEAKKSKEVL 188
Cdd:COG1446 86 ASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYKPII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 189 ldsdkakahlgvsTEPYLGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANNDSVAISCTGTGDIYIRV 268
Cdd:COG1446 166 -------------NERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRT 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1204953397 269 AAAHEVASLYKyKKLSVQKAAEETIKQ-VAKLGGTGGIISIDKNGKVGYAWTKDklGMYHGQAKIGEEPKV 338
Cdd:COG1446 233 VVAHDIVERMR-QGLSLQEAAEEVIERiLKKLGGDGGLIAVDKDGNIAAPFNTE--GMYRAYIDGDGELVV 300
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
34-328 |
3.83e-126 |
|
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: 362.16 E-value: 3.83e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 34 IVIHGGTSGL---GLTKEEFTKREKVMKESLKAGQSILEKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELDAS 110
Cdd:cd04701 2 LAIHGGAGTIsraNLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 111 LMDGKNLKAGAVAMARTIKNPIEAARLVMEKTPHTLIAGEGADKLAKKHGLEIVGQkyfftehrykqlqeakkskevlld 190
Cdd:cd04701 82 IMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELVPQ------------------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 191 sdkakahlgvstepylGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANNDSVAISCTGTGDIYIRVAA 270
Cdd:cd04701 138 ----------------GTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWAVAVSGTGNGDSFIRVAA 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1204953397 271 AHEVASLYKYKKLSVQKAAEETIKQVAKL-GGTGGIISIDKNGKVGYAWTKDklGMYHG 328
Cdd:cd04701 202 ARDVAARMRYKGLSLAEAAKEVVGPGGELgEGEGGIIAIDARGNVAMPFNCG--GMYRA 258
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
33-339 |
7.83e-122 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 353.04 E-value: 7.83e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 33 IIVIHGGTSGLGLTKEEFTKREKVMKESLKAGQSILEKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELDASLM 112
Cdd:pfam01112 1 VLVIHGGAGSILRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 113 DGKNLKAGAVAMARTIKNPIEAARLVMEKTPHTLIAGEGADKLAKKHGLEIVGQKYFFTEHRYKQLQEAKK-SKEVLLDS 191
Cdd:pfam01112 81 DGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKeNFQPNMAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 192 DKAKAHLGVSTEPYLGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANNDSVAISCTGTGDIYIRVAAA 271
Cdd:pfam01112 161 NVAPDPLKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1204953397 272 HEVASLYKYkKLSVQKAAEETI-KQVAKLGGTGGIISIDKNGKVgyAWTKDKLGMYHGQAKIGEEPKVF 339
Cdd:pfam01112 241 YDIVARMEY-GLSLEEAADKVItEMLKRVGGDGGVIAVDAKGNI--AAPFNTEGMYRAYHTGDGIGDVL 306
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
33-336 |
1.00e-96 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 289.16 E-value: 1.00e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 33 IIVIHGGTSGLG---LTKEEFTKREKVMKESLKAGQSILEKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELDA 109
Cdd:PRK10226 5 VIAIHGGAGAISraqMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 110 SLMDGKNLKAGAVAMARTIKNPIEAARLVMEKTPHTLIAGEGADKLAKKHGLEIVGQKYFFTEHRYKQLQEAKKSKEVLL 189
Cdd:PRK10226 85 CVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAARAEGATVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 190 DSDKAKahlgVSTEPYLGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANNDSVAISCTGTGDIYIRVA 269
Cdd:PRK10226 165 DHSGAP----LDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRAL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1204953397 270 AAHEVASLYKYKKLSVQKAAEETI-KQVAKLGGTGGIISIDKNGKVGYAWTKDklGMYHGQAKIGEEP 336
Cdd:PRK10226 241 AAYDIAALMDYGGLSLAEACERVVmEKLPALGGSGGLIAIDHEGNVALPFNTE--GMYRAWGYAGDTP 306
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
32-338 |
2.65e-138 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 394.47 E-value: 2.65e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 32 PIIVIHGGTSGL---GLTKEEFTKREKVMKESLKAGQSILEKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELD 108
Cdd:COG1446 6 RALIIHGGAGTIarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 109 ASLMDGKNLKAGAVAMARTIKNPIEAARLVMEKTPHTLIAGEGADKLAKKHGLEIVGQKYFFTEHRYKQLQEAKKSKEVL 188
Cdd:COG1446 86 ASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYKPII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 189 ldsdkakahlgvsTEPYLGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANNDSVAISCTGTGDIYIRV 268
Cdd:COG1446 166 -------------NERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRT 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1204953397 269 AAAHEVASLYKyKKLSVQKAAEETIKQ-VAKLGGTGGIISIDKNGKVGYAWTKDklGMYHGQAKIGEEPKV 338
Cdd:COG1446 233 VVAHDIVERMR-QGLSLQEAAEEVIERiLKKLGGDGGLIAVDKDGNIAAPFNTE--GMYRAYIDGDGELVV 300
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
34-328 |
3.83e-126 |
|
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: 362.16 E-value: 3.83e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 34 IVIHGGTSGL---GLTKEEFTKREKVMKESLKAGQSILEKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELDAS 110
Cdd:cd04701 2 LAIHGGAGTIsraNLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 111 LMDGKNLKAGAVAMARTIKNPIEAARLVMEKTPHTLIAGEGADKLAKKHGLEIVGQkyfftehrykqlqeakkskevlld 190
Cdd:cd04701 82 IMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELVPQ------------------------ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 191 sdkakahlgvstepylGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANNDSVAISCTGTGDIYIRVAA 270
Cdd:cd04701 138 ----------------GTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWAVAVSGTGNGDSFIRVAA 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1204953397 271 AHEVASLYKYKKLSVQKAAEETIKQVAKL-GGTGGIISIDKNGKVGYAWTKDklGMYHG 328
Cdd:cd04701 202 ARDVAARMRYKGLSLAEAAKEVVGPGGELgEGEGGIIAIDARGNVAMPFNCG--GMYRA 258
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
33-339 |
7.83e-122 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 353.04 E-value: 7.83e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 33 IIVIHGGTSGLGLTKEEFTKREKVMKESLKAGQSILEKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELDASLM 112
Cdd:pfam01112 1 VLVIHGGAGSILRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 113 DGKNLKAGAVAMARTIKNPIEAARLVMEKTPHTLIAGEGADKLAKKHGLEIVGQKYFFTEHRYKQLQEAKK-SKEVLLDS 191
Cdd:pfam01112 81 DGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKeNFQPNMAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 192 DKAKAHLGVSTEPYLGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANNDSVAISCTGTGDIYIRVAAA 271
Cdd:pfam01112 161 NVAPDPLKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1204953397 272 HEVASLYKYkKLSVQKAAEETI-KQVAKLGGTGGIISIDKNGKVgyAWTKDKLGMYHGQAKIGEEPKVF 339
Cdd:pfam01112 241 YDIVARMEY-GLSLEEAADKVItEMLKRVGGDGGVIAVDAKGNI--AAPFNTEGMYRAYHTGDGIGDVL 306
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
31-322 |
4.55e-103 |
|
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: 304.49 E-value: 4.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 31 EPIIVIHGGTSGLGLTKEEfTKREkVMKESLKAGQSILEKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELDAS 110
Cdd:cd04702 1 KPVIVVHGGAGSIPDDRIK-GSRE-GVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 111 LMDGKNLKAGAVAMARTIKNPIEAARLVMEKTPHTLIAGEGADKLAKKHGLEIVGQKYFFTEHRYKQLQEAKKSKevllD 190
Cdd:cd04702 79 IMDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEK----G 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 191 SDKAKAHLGvstepyLGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANNDSVAISCTGTGDIYIRVAA 270
Cdd:cd04702 155 ANVEDTQRG------HGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1204953397 271 AHEVASLYKYKKlSVQKAAEETIKQV-AKLGGTGGIISIDKNGKVGYAWTKDK 322
Cdd:cd04702 229 ARLILFHMEQGK-TAEEAAELALAYMkSRVKGLGGLIVVSKTGDWGAKFTSKR 280
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
33-336 |
1.00e-96 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 289.16 E-value: 1.00e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 33 IIVIHGGTSGLG---LTKEEFTKREKVMKESLKAGQSILEKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELDA 109
Cdd:PRK10226 5 VIAIHGGAGAISraqMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 110 SLMDGKNLKAGAVAMARTIKNPIEAARLVMEKTPHTLIAGEGADKLAKKHGLEIVGQKYFFTEHRYKQLQEAKKSKEVLL 189
Cdd:PRK10226 85 CVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAARAEGATVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 190 DSDKAKahlgVSTEPYLGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANNDSVAISCTGTGDIYIRVA 269
Cdd:PRK10226 165 DHSGAP----LDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRAL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1204953397 270 AAHEVASLYKYKKLSVQKAAEETI-KQVAKLGGTGGIISIDKNGKVGYAWTKDklGMYHGQAKIGEEP 336
Cdd:PRK10226 241 AAYDIAALMDYGGLSLAEACERVVmEKLPALGGSGGLIAIDHEGNVALPFNTE--GMYRAWGYAGDTP 306
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
33-328 |
1.07e-96 |
|
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: 286.77 E-value: 1.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 33 IIVIHGGTSGLGLTKEEftKREKVMKESLKAGQSILEKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELDASLM 112
Cdd:cd04512 1 SLIVHGGAGTIEDEDAE--AYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 113 DGKNLKAGAVAMARTIKNPIEAARLVMEKTPHTLIAGEGADKLAKKHGleivgqkyfftehrykqlqeakkskevlldsd 192
Cdd:cd04512 79 DGKTLNAGAVAGVKGVKNPISLARAVMEKTPHVLLVGEGAERFAREHG-------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 193 kakahlgvstepyLGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANNDSVAISCTGTGDIYIRVAAAH 272
Cdd:cd04512 127 -------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAK 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1204953397 273 EVASLYKYKKlSVQKAAEETI-KQVAKLGGTGGIISIDKNGKVGYAWTKDklGMYHG 328
Cdd:cd04512 194 RIADLVEFGG-SAQEAAEAAIdYLRRRVGGEGGLIVVDPDGRLGAAHNTP--GMAFA 247
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
34-341 |
1.40e-88 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 268.50 E-value: 1.40e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 34 IVIHGGTSG--LGLTKEEFTKREKVMKESLKAGQSILEKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELDASL 111
Cdd:PLN02689 6 IALHGGAGDidPNLPRERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEASI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 112 MDGKNLKAGAVAMARTIKNPIEAARLVMEKTPHTLIAGEGADKLAKKHGLEIVGQKYFFTEHRYKQLQEAKKSKEVLLD- 190
Cdd:PLN02689 86 MDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAKEANSVQFDy 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 191 -----SDKAKAHLGVSTEPYLGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYAnNDSVAISCTGTGDIY 265
Cdd:PLN02689 166 ripldKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYA-NHLCAVSATGKGEAI 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1204953397 266 IRVAAAHEVASLYKYKKLSVQKAAEETIKQVAKlGGTGGIISIDKNGKVGYAWtkDKLGMYHGQAKIGEEPKV-FWP 341
Cdd:PLN02689 245 IRGTVARDVAAVMEYKGLPLQEAVDYVIKERLP-EGPAGLIAVSATGEVAMAF--NTTGMFRACATEDGFMEVgIWP 318
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
33-317 |
3.41e-85 |
|
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: 257.51 E-value: 3.41e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 33 IIVIHGGTSGLGLTKEEfTKREKVMKESLKAGQSILeKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELDASLM 112
Cdd:cd14950 1 ALVVHGGAGSWKNSDDE-EKALRALREALERGYEAL-RRGSALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDAGIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 113 DGKNLKAGAVAMARTIKNPIEAARLVMEKTPHTLIAGEGADKLAKKHGleivgqkyfftehrykqlqeakkskevlldsd 192
Cdd:cd14950 79 DGRTLRVGAVAAVRAVKNPIRLARKVMEKTDHVLIVGEGADELAKRLG-------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 193 kakahlgvstepyLGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANNdSVAISCTGTGDIYIRVAAAH 272
Cdd:cd14950 127 -------------GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN-GVAVSATGIGEVIIRSLPAL 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1204953397 273 EVASLYKyKKLSVQKAAEETIKQVAKL--GGTGGIISIDKNGKVGYA 317
Cdd:cd14950 193 RADELVS-MGGDIEEAVRAVVNKVTETfgKDTAGIIGIDARGNIAAA 238
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
58-317 |
9.67e-64 |
|
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: 204.33 E-value: 9.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 58 KESLKAGQSILEKGGSSVDAVIAAIKVMEDSPE-FNAGKGAVFTSDGFNELDASLMDGKNLKAGAVAMARTIKNPIEAAR 136
Cdd:cd04513 9 TEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCdGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 137 LVMEKTPHTLIAGEGADKLAKKHGLEIvgqKYFFTEHRYKQLQEAKKS-------KEVLLDSDKA-----KAHLGVSTEP 204
Cdd:cd04513 89 AVMEHTPHSLLVGEGATEFAVSMGFKE---ENLLTEESRKMWKKWLKEncqpnfwKNVVPDPSKScsspkAPSRSESAIP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 205 YLG--TVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANNDSVAISCTGTGDIYIRVAAAHEVASLYKyKK 282
Cdd:cd04513 166 EDNhdTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLPSYQAVELMR-QG 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 1204953397 283 LSVQKAAEETIKQVAKLG---GTGGIISIDKNGKVGYA 317
Cdd:cd04513 245 MSPQEACEDAIRRIAKKYpkdFEGAVVAVNKAGEYGAA 282
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
32-333 |
9.54e-55 |
|
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: 180.50 E-value: 9.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 32 PIIVIHGGTSGLGLTKEEFtkrEKVMKESLKAgqsILEKG------GSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFN 105
Cdd:cd14949 1 PKLIIHGGFGSESSTNGET---KAAKQEALAE---IVEEVyeylksHSALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 106 ELDASLMDGKNLKAGAVAMARTIKNPIEAARLVMEKtPHTLIAGEGADKLAKKHGLEIvgqkyfftehrYKQLQEAKKSK 185
Cdd:cd14949 75 RMSASLMDGQTQRFSGVINIENVKNPIEVAQKLQQE-DDRVLSGEGATEFARENGFPE-----------YNPETPQRRQE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 186 EVLLDSDKAkahlgvstepYLGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIgAGNYAnNDSVAISCTGTGDIY 265
Cdd:cd14949 143 YEEKKLKSG----------GTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNYA-NAFAGVSCTGIGEDI 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1204953397 266 IRVAAAHEVASLYKyKKLSVQKAAEETIKQVAKLGGTGGIISIDKNGKVgyAWTKDKLGM---YHGQAKIG 333
Cdd:cd14949 211 VSEALAAKIVTRVT-DGMSLQEAFEKSFAEAKPRDGFAGAIGIDSKGNI--YHGDTHPVMvyaSYDGEKIG 278
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
32-317 |
3.40e-52 |
|
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: 172.83 E-value: 3.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 32 PIIVIHGGTsglGLTKEEFTKREKVMKESLKAgqsiLEKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELDASL 111
Cdd:cd04703 1 MAVLVHGGA---GSDPERQDGLERAAEAGLAE----LQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 112 MDGKNlKAGAVAMARTIKNPIEAARLVMEKTPHTLIAGEGADKLAKKHGLEivgqkyfftehrykqlqeakkskevlLDS 191
Cdd:cd04703 74 MTSGG-AFGAVAAIEGVKNPVLVARAVMETSPHVLLAGDGAVRFARRLGYP--------------------------DGC 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 192 DkakahlgvstepylgTVGAIALDkNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYAnNDSVAISCTGTGDIYIRVAAA 271
Cdd:cd04703 127 D---------------TVGAVARD-GGKFAAAVSTGGTSPALRGRVGDVPIIGAGFYA-GPKGAVAATGIGEEIAKRLLA 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1204953397 272 HEVASLYKyKKLSVQKAAEETIKQVaKLGGTGGIISIDKNGKVGYA 317
Cdd:cd04703 190 RRVYRWIE-TGLSLQAAAQRAIDEF-DDGVAVGVIAVSRRGEAGIA 233
|
|
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
32-279 |
4.93e-45 |
|
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: 156.28 E-value: 4.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 32 PIIVIHGGTSGLGLTKEEFTKRekVMKESLKAGQSILEKGGSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELDASL 111
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKR--ACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 112 MDGKNLKAGAVAMARTIKNPIEAARLVMEK---------TPHTLIAGEGADKLAKKHGLeivgqkyfftehrykqlqeak 182
Cdd:cd04514 79 MDGSSGRFGAVGAVSGVKNPIQLARLLLKEqrkplslgrVPPMFLVGEGAREWAKSKGI--------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 183 kskevLLDsdkakahlgvstepylgTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANN------DSVAI 256
Cdd:cd04514 138 -----ITD-----------------TVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPrdpddkTSVAV 195
|
250 260
....*....|....*....|....
gi 1204953397 257 SCTGTGDIYIRVAAAHEVA-SLYK 279
Cdd:cd04514 196 VTSGTGEHIATTMLARRCAeRLYH 219
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
56-273 |
2.80e-33 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 127.29 E-value: 2.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 56 VMKESLKAGQSILEKG-GSSVDAVIAAIKVMEDSPEFNAGKGAVFTSDGFNELDASLMDGKNLKAGAVAMARTIKNPIE- 133
Cdd:PLN02937 34 AMRRACLAAAAILRQGsGGCIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQi 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 134 AARLVME---------KTPHTLIAGEGADKLAKKHGL---EIVGQ--KYFFTEH------RYKQL--------------- 178
Cdd:PLN02937 114 AALLAKEqmmgssllgRIPPMFLVGEGARQWAKSKGIdlpETVEEaeKWLVTERakeqwkKYKTMlasaiaksscdsqst 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1204953397 179 -----QEAKKSKEVLLDSDKAKAHLGVSTEPY-LGTVGAIALDKNGNLAAGTSTGGTTNKMTGRIGDSPIIGAGNYANND 252
Cdd:PLN02937 194 sklseLEAPRSNPSNGTGGGQSSMCTASDEDCiMDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSK 273
|
250 260
....*....|....*....|....*...
gi 1204953397 253 -------SVAISCTGTGDIYIRVAAAHE 273
Cdd:PLN02937 274 gpfgapfIVGCCVSGAGEYLMRGFAARE 301
|
|
| |
