|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
1-260 |
1.22e-68 |
|
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: 214.44 E-value: 1.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpscppstmttrfslaafkrn 80
Cdd:cd04514 79 MDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI-------------------- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 krklelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:cd04514 138 -------------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 161 AQNPYSTAVSTSG--------------------------------------SPFLACEDG---VLGGVIVLRSCRcsses 199
Cdd:cd04514 187 PDDKTSVAVVTSGtgehiattmlarrcaerlyhstrreesdedeilrsfieSDFMGHPGVknsPSAGAIGVLAVK----- 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401057 200 dssqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 260
Cdd:cd04514 262 -----KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
1-239 |
3.66e-40 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 143.47 E-value: 3.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPScpPSTMT-------TRFS 73
Cdd:PLN02937 91 MDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDL--PETVEeaekwlvTERA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 74 LAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT------------LDTVGAVVVDHEGNVAAAVSSG 134
Cdd:PLN02937 169 KEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIASGASSG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 135 GLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGS------PFLACEDGVLGGVI----------VLRSCRCSS 197
Cdd:PLN02937 249 GIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAgeylmrGFAARECCVSSSLSqagpasacmkVLRSVIQGS 328
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401057 198 ESDSSQDKQTLL-------------------VEFLWSHTTESMCVGYMSAQDGKAKTHISR 239
Cdd:PLN02937 329 SAKTTDKDAGILlvqadasvmapgnspslkaVEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
1-237 |
4.63e-37 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 132.54 E-value: 4.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaaFKRN 80
Cdd:COG1446 89 MDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDPLY---------FFTE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 KRKLelaervetdfiQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:COG1446 150 KRWK-----------QWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 161 AqnpystAVSTSG----------------------SPFLACEDGVL---------GGVIVLrscrcssesdssqDKQTll 209
Cdd:COG1446 218 G------AVSATGhgeyfirtvvahdivermrqglSLQEAAEEVIErilkklggdGGLIAV-------------DKDG-- 276
|
250 260
....*....|....*....|....*...
gi 1720401057 210 vEFLWSHTTESMCVGYMSAqDGKAKTHI 237
Cdd:COG1446 277 -NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
1-228 |
2.35e-31 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 117.69 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRN 80
Cdd:pfam01112 80 MDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 KrklelaervETDFIQLKRRRQSSA--KENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAEN 158
Cdd:pfam01112 150 R---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 159 TGAqnpystAVSTSG----------------------SPFLACEDGV---------LGGVIVLrscrcssesdssqDKQT 207
Cdd:pfam01112 221 ATG------AVSATGhgediiretlaydivarmeyglSLEEAADKVItemlkrvggDGGVIAV-------------DAKG 281
|
250 260
....*....|....*....|.
gi 1720401057 208 llvEFLWSHTTESMCVGYMSA 228
Cdd:pfam01112 282 ---NIAAPFNTEGMYRAYHTG 299
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
1-260 |
1.22e-68 |
|
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: 214.44 E-value: 1.22e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpscppstmttrfslaafkrn 80
Cdd:cd04514 79 MDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI-------------------- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 krklelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:cd04514 138 -------------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 161 AQNPYSTAVSTSG--------------------------------------SPFLACEDG---VLGGVIVLRSCRcsses 199
Cdd:cd04514 187 PDDKTSVAVVTSGtgehiattmlarrcaerlyhstrreesdedeilrsfieSDFMGHPGVknsPSAGAIGVLAVK----- 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401057 200 dssqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 260
Cdd:cd04514 262 -----KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
1-239 |
3.66e-40 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 143.47 E-value: 3.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPScpPSTMT-------TRFS 73
Cdd:PLN02937 91 MDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDL--PETVEeaekwlvTERA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 74 LAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT------------LDTVGAVVVDHEGNVAAAVSSG 134
Cdd:PLN02937 169 KEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIASGASSG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 135 GLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGS------PFLACEDGVLGGVI----------VLRSCRCSS 197
Cdd:PLN02937 249 GIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAgeylmrGFAARECCVSSSLSqagpasacmkVLRSVIQGS 328
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401057 198 ESDSSQDKQTLL-------------------VEFLWSHTTESMCVGYMSAQDGKAKTHISR 239
Cdd:PLN02937 329 SAKTTDKDAGILlvqadasvmapgnspslkaVEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
1-226 |
8.26e-40 |
|
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: 138.47 E-value: 8.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscppstmttrfslaafkrn 80
Cdd:cd04512 78 MDGKTLNAGAVAGVKGVKNPISLARAVMEKT----------PHVLLVGEGAERFAREHG--------------------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 krklelaervetdfiqlkrrrqssakendsgtLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTg 160
Cdd:cd04512 127 --------------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNE- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 161 aqnpySTAVSTSG----------------------SPFLACE---------DGVLGGVIVLrscrcssesdssqDKQtll 209
Cdd:cd04512 174 -----TGAVSATGhgesiirtvlakriadlvefggSAQEAAEaaidylrrrVGGEGGLIVV-------------DPD--- 232
|
250
....*....|....*..
gi 1720401057 210 VEFLWSHTTESMCVGYM 226
Cdd:cd04512 233 GRLGAAHNTPGMAFAYI 249
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
1-237 |
4.63e-37 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 132.54 E-value: 4.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaaFKRN 80
Cdd:COG1446 89 MDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDPLY---------FFTE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 KRKLelaervetdfiQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:COG1446 150 KRWK-----------QWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 161 AqnpystAVSTSG----------------------SPFLACEDGVL---------GGVIVLrscrcssesdssqDKQTll 209
Cdd:COG1446 218 G------AVSATGhgeyfirtvvahdivermrqglSLQEAAEEVIErilkklggdGGLIAV-------------DKDG-- 276
|
250 260
....*....|....*....|....*...
gi 1720401057 210 vEFLWSHTTESMCVGYMSAqDGKAKTHI 237
Cdd:COG1446 277 -NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
1-228 |
2.35e-31 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 117.69 E-value: 2.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRN 80
Cdd:pfam01112 80 MDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 KrklelaervETDFIQLKRRRQSSA--KENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAEN 158
Cdd:pfam01112 150 R---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 159 TGAqnpystAVSTSG----------------------SPFLACEDGV---------LGGVIVLrscrcssesdssqDKQT 207
Cdd:pfam01112 221 ATG------AVSATGhgediiretlaydivarmeyglSLEEAADKVItemlkrvggDGGVIAV-------------DAKG 281
|
250 260
....*....|....*....|.
gi 1720401057 208 llvEFLWSHTTESMCVGYMSA 228
Cdd:pfam01112 282 ---NIAAPFNTEGMYRAYHTG 299
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
1-173 |
4.83e-31 |
|
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: 116.52 E-value: 4.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRN 80
Cdd:cd04702 80 MDGKTLRAGAVSAVRNIANPISLA-RLVME---------KTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 KRKlelaervetdfiqlkrrrQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtg 160
Cdd:cd04702 150 KKE------------------KGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADN-- 209
|
170
....*....|...
gi 1720401057 161 aqnpYSTAVSTSG 173
Cdd:cd04702 210 ----LVGAVSTTG 218
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
1-171 |
1.59e-30 |
|
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoproteins. This enzyme is an amidase located inside lysosomes. Mutation of this gene in humans causes a genetic disorder known as aspartylglycosaminuria (AGU). The glycosylasparaginase precursor undergoes autoproteolysis through an N-O or N-S acyl rearrangement of the peptide bond, which leads to the cleavage of a peptide bond between an Asp and a Thr. This proteolysis step generates an exposed N-terminal catalytic threonine and activates the enzyme.
Pssm-ID: 271335 Cd Length: 294 Bit Score: 115.35 E-value: 1.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRN 80
Cdd:cd04513 64 MDGDTMDVGAVAALRRIKNAISVARAVM----------EHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 KRKLELAERVETD---FIQLKRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAE 157
Cdd:cd04513 134 NCQPNFWKNVVPDpskSCSSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYAD 213
|
170
....*....|....*
gi 1720401057 158 NT-GAqnpystAVST 171
Cdd:cd04513 214 NEvGA------AAAT 222
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
1-174 |
5.45e-23 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 95.40 E-value: 5.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVsVAHRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTrfslaafkrN 80
Cdd:PRK10226 87 MDGNTLKAGAVAGVSHLRNPV-LAARLVME---------QSPHVMMIGEGAENFAFAHGMERVSPEIFST---------P 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 KRKLELAERVETDFIQLKrrrQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTg 160
Cdd:PRK10226 148 LRYEQLLAARAEGATVLD---HSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNA- 223
|
170
....*....|....
gi 1720401057 161 aqnpySTAVSTSGS 174
Cdd:PRK10226 224 -----SVAVSCTGT 232
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
1-173 |
8.35e-23 |
|
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: 94.07 E-value: 8.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaafkrn 80
Cdd:cd04701 83 MDGRTKRAGAVAGLRRVRNPILLARAVLEKS----------PHVLLSGEGAEEFAREQGLELVPQGT------------- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 krklelaervetdfiqlkrrrqssakendsgtldtVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtg 160
Cdd:cd04701 140 -----------------------------------VGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEE-- 182
|
170
....*....|...
gi 1720401057 161 aqnpYSTAVSTSG 173
Cdd:cd04701 183 ----WAVAVSGTG 191
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
1-173 |
1.05e-22 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 94.77 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRfslaafkRN 80
Cdd:PLN02689 86 MDGRTRRCGAVSGLTTVVNPISLA-RLVME---------KTPHIYLAFDGAEAFARQQGVETVDNSYFITE-------EN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 KRKLELAE---RVETDFIQ--LKRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCW 155
Cdd:PLN02689 149 VERLKQAKeanSVQFDYRIplDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTY 228
|
170
....*....|....*...
gi 1720401057 156 AENTGaqnpystAVSTSG 173
Cdd:PLN02689 229 ANHLC-------AVSATG 239
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
1-161 |
3.63e-20 |
|
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: 86.48 E-value: 3.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscppstmttrfslaafkrn 80
Cdd:cd14950 78 MDGRTLRVGAVAAVRAVKNPIRLARKVMEKT----------DHVLIVGEGADELAKRLG--------------------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 krklelaervetdfiqlkrrrqssakendsgtLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:cd14950 127 --------------------------------GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATNGV 174
|
.
gi 1720401057 161 A 161
Cdd:cd14950 175 A 175
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
1-148 |
3.43e-14 |
|
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: 70.71 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKgklsagrippcFLVGEGAYRWAVDHGIPSCPPstmttrfslaafkrn 80
Cdd:cd14949 81 MDGQTQRFSGVINIENVKNPIEVAQKLQQEDDR-----------VLSGEGATEFARENGFPEYNP--------------- 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720401057 81 krklelaervETDFiqlkRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAA 148
Cdd:cd14949 135 ----------ETPQ----RRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSA 188
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
1-161 |
2.28e-12 |
|
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: 64.97 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 1 MDGKSlNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIPScppstmttrfslaafkrn 80
Cdd:cd04703 74 MTSGG-AFGAVAAIEGVKNPVLVARAVMETS----------PHVLLAGDGAVRFARRLGYPD------------------ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401057 81 krklelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHeGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:cd04703 125 -------------------------------GCDTVGAVARDG-GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKG 172
|
.
gi 1720401057 161 A 161
Cdd:cd04703 173 A 173
|
|
|