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Conserved domains on  [gi|1039762216|ref|XP_017174802|]
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threonine aspartase 1 isoform X7 [Mus musculus]

Protein Classification

threonine aspartase 1( domain architecture ID 10139957)

threonine aspartase 1 (also known as taspase-1) is protease which cleaves the mixed-lineage leukemia (MLL) and transcription factor (TF) IIA families of nuclear proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 1-297 4.07e-89

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: 268.37  E-value: 4.07e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpscppstmttrfslaafkrn 80
Cdd:cd04514    79 MDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI-------------------- 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 krklelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:cd04514   138 -------------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRD 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216 161 AQNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLACEDG---VLGGVIVLRSCRcsses 236
Cdd:cd04514   187 PDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK----- 261

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039762216 237 dssqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 297
Cdd:cd04514   262 -----KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
 
Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 1-297 4.07e-89

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: 268.37  E-value: 4.07e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpscppstmttrfslaafkrn 80
Cdd:cd04514    79 MDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI-------------------- 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 krklelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:cd04514   138 -------------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRD 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216 161 AQNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLACEDG---VLGGVIVLRSCRcsses 236
Cdd:cd04514   187 PDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK----- 261

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039762216 237 dssqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 297
Cdd:cd04514   262 -----KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 1-276 7.16e-51

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 172.74  E-value: 7.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPScpPSTMT-------TRFS 73
Cdd:PLN02937   91 MDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDL--PETVEeaekwlvTERA 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  74 LAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT------------LDTVGAVVVDHEGNVAAAVSSG 134
Cdd:PLN02937  169 KEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIASGASSG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216 135 GLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGCGEHLVRTILARECSHAL---QAEDAHQA---LLETMQNk 207
Cdd:PLN02937  249 GIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSSslsQAGPASACmkvLRSVIQG- 327

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039762216 208 fiSSPFLACEDgvlGGVIVLRSCRCSSESDSSQDKQTllVEFLWSHTTESMCVGYMSAQDGKAKTHISR 276
Cdd:PLN02937  328 --SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 1-274 6.63e-42

Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];


Pssm-ID: 441055  Cd Length: 305  Bit Score: 146.41  E-value: 6.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaaFKRN 80
Cdd:COG1446    89 MDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDPLY---------FFTE 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 KRKLelaervetdfiQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:COG1446   150 KRWK-----------QWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEV 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216 161 AqnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspfLAcEDGVLGGVIVLrscrcssesdss 239
Cdd:COG1446   218 G------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI------LK-KLGGDGGLIAV------------ 272

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039762216 240 qDKQTllvEFLWSHTTESMCVGYMSAqDGKAKTHI 274
Cdd:COG1446   273 -DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
Asparaginase_2 pfam01112
Asparaginase;
1-265 4.62e-38

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 136.56  E-value: 4.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRN 80
Cdd:pfam01112  80 MDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQKA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 KrklelaervETDFIQLKRRRQSSA--KENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAEN 158
Cdd:pfam01112 150 R---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADN 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216 159 TGAqnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflacedGVLGGVIVLrscrcss 234
Cdd:pfam01112 221 ATG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV----------GGDGGVIAV------- 277

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1039762216 235 esdssqDKQTllvEFLWSHTTESMCVGYMSA 265
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 ...
 1-297 4.07e-89

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: 268.37  E-value: 4.07e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpscppstmttrfslaafkrn 80
Cdd:cd04514    79 MDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI-------------------- 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 krklelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:cd04514   138 -------------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRD 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216 161 AQNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLACEDG---VLGGVIVLRSCRcsses 236
Cdd:cd04514   187 PDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK----- 261

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039762216 237 dssqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 297
Cdd:cd04514   262 -----KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 1-263 1.23e-55

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: 180.46  E-value: 1.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscppstmttrfslaafkrn 80
Cdd:cd04512    78 MDGKTLNAGAVAGVKGVKNPISLARAVMEKT----------PHVLLVGEGAERFAREHG--------------------- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 krklelaervetdfiqlkrrrqssakendsgtLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTg 160
Cdd:cd04512   127 --------------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNE- 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216 161 aqnpySTAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFISSpflaceDGVLGGVIVLrscrcssesdssq 240
Cdd:cd04512   174 -----TGAVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAEAAIDYLRRR------VGGEGGLIVV------------- 229

                         250       260
                  ....*....|....*....|...
gi 1039762216 241 DKQtllVEFLWSHTTESMCVGYM 263
Cdd:cd04512   230 DPD---GRLGAAHNTPGMAFAYI 249
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 1-276 7.16e-51

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 172.74  E-value: 7.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPScpPSTMT-------TRFS 73
Cdd:PLN02937   91 MDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDL--PETVEeaekwlvTERA 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  74 LAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT------------LDTVGAVVVDHEGNVAAAVSSG 134
Cdd:PLN02937  169 KEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIASGASSG 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216 135 GLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGCGEHLVRTILARECSHAL---QAEDAHQA---LLETMQNk 207
Cdd:PLN02937  249 GIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSSslsQAGPASACmkvLRSVIQG- 327

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039762216 208 fiSSPFLACEDgvlGGVIVLRSCRCSSESDSSQDKQTllVEFLWSHTTESMCVGYMSAQDGKAKTHISR 276
Cdd:PLN02937  328 --SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 1-274 6.63e-42

Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];


Pssm-ID: 441055  Cd Length: 305  Bit Score: 146.41  E-value: 6.63e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaaFKRN 80
Cdd:COG1446    89 MDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDPLY---------FFTE 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 KRKLelaervetdfiQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:COG1446   150 KRWK-----------QWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEV 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216 161 AqnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspfLAcEDGVLGGVIVLrscrcssesdss 239
Cdd:COG1446   218 G------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI------LK-KLGGDGGLIAV------------ 272

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1039762216 240 qDKQTllvEFLWSHTTESMCVGYMSAqDGKAKTHI 274
Cdd:COG1446   273 -DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 1-227 2.04e-38

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: 136.93  E-value: 2.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRN 80
Cdd:cd04702    80 MDGKTLRAGAVSAVRNIANPISLA-RLVME---------KTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKF 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 KRKlelaervetdfiqlkrrrQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtg 160
Cdd:cd04702   150 KKE------------------KGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADN-- 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039762216 161 aqnpYSTAVSTSGCGEHLVRTILARECSHALQ----AEDAHQALLETMQNKFisspflacedGVLGGVIVL 227
Cdd:cd04702   210 ----LVGAVSTTGHGESIMKVNLARLILFHMEqgktAEEAAELALAYMKSRV----------KGLGGLIVV 266
Asparaginase_2 pfam01112
Asparaginase;
1-265 4.62e-38

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 136.56  E-value: 4.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRN 80
Cdd:pfam01112  80 MDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQKA 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 KrklelaervETDFIQLKRRRQSSA--KENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAEN 158
Cdd:pfam01112 150 R---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADN 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216 159 TGAqnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflacedGVLGGVIVLrscrcss 234
Cdd:pfam01112 221 ATG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV----------GGDGGVIAV------- 277

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1039762216 235 esdssqDKQTllvEFLWSHTTESMCVGYMSA 265
Cdd:pfam01112 278 ------DAKG---NIAAPFNTEGMYRAYHTG 299
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 1-220 4.72e-31

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: 117.66  E-value: 4.72e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRN 80
Cdd:cd04513    64 MDGDTMDVGAVAALRRIKNAISVARAVM----------EHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKE 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 KRKLELAERVETD---FIQLKRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAE 157
Cdd:cd04513   134 NCQPNFWKNVVPDpskSCSSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYAD 213

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039762216 158 NT-GAqnpystAVSTsGCGEhlvrtILARECShalqaedAHQAlLETMQNKFisSPFLACEDGV 220
Cdd:cd04513   214 NEvGA------AAAT-GDGD-----IMMRFLP-------SYQA-VELMRQGM--SPQEACEDAI 255
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 1-186 4.23e-27

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 107.49  E-value: 4.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRfslaafkRN 80
Cdd:PLN02689   86 MDGRTRRCGAVSGLTTVVNPISLA-RLVME---------KTPHIYLAFDGAEAFARQQGVETVDNSYFITE-------EN 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 KRKLELAE---RVETDFIQ--LKRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCW 155
Cdd:PLN02689  149 VERLKQAKeanSVQFDYRIplDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTY 228

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1039762216 156 AENTGaqnpystAVSTSGCGEHLVRTILARE 186
Cdd:PLN02689  229 ANHLC-------AVSATGKGEAIIRGTVARD 252
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 1-184 5.43e-26

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 104.65  E-value: 5.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVsVAHRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTrfslaafkrN 80
Cdd:PRK10226   87 MDGNTLKAGAVAGVSHLRNPV-LAARLVME---------QSPHVMMIGEGAENFAFAHGMERVSPEIFST---------P 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 KRKLELAERVETDFIQLKrrrQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTg 160
Cdd:PRK10226  148 LRYEQLLAARAEGATVLD---HSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNA- 223

                         170       180
                  ....*....|....*....|....
gi 1039762216 161 aqnpySTAVSTSGCGEHLVRTILA 184
Cdd:PRK10226  224 -----SVAVSCTGTGEVFIRALAA 242
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 1-227 6.19e-26

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: 103.31  E-value: 6.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaafkrn 80
Cdd:cd04701    83 MDGRTKRAGAVAGLRRVRNPILLARAVLEKS----------PHVLLSGEGAEEFAREQGLELVPQGT------------- 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 krklelaervetdfiqlkrrrqssakendsgtldtVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtg 160
Cdd:cd04701   140 -----------------------------------VGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEE-- 182

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039762216 161 aqnpYSTAVSTSGCGEHLVRTILARECSHalQAEDAHQALLETMqnKFISSPFLACEDGVlGGVIVL 227
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 ...
 1-264 9.98e-26

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: 102.27  E-value: 9.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscppstmttrfslaafkrn 80
Cdd:cd14950    78 MDGRTLRVGAVAAVRAVKNPIRLARKVMEKT----------DHVLIVGEGADELAKRLG--------------------- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 krklelaervetdfiqlkrrrqssakendsgtLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtg 160
Cdd:cd14950   127 --------------------------------GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN-- 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216 161 aqnpySTAVSTSGCGEHLVRTILARECSHA----LQAEDAHQALLETMQNKFISSpflacedgvLGGVIVLrscrcsses 236
Cdd:cd14950   173 -----GVAVSATGIGEVIIRSLPALRADELvsmgGDIEEAVRAVVNKVTETFGKD---------TAGIIGI--------- 229

                         250       260
                  ....*....|....*....|....*...
gi 1039762216 237 dssqDKQTllvEFLWSHTTESMCVGYMS 264
Cdd:cd14950   230 ----DARG---NIAAAFNTEAMPRGYID 250
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 1-227 1.78e-19

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: 85.39  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSlNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIPScppstmttrfslaafkrn 80
Cdd:cd04703    74 MTSGG-AFGAVAAIEGVKNPVLVARAVMETS----------PHVLLAGDGAVRFARRLGYPD------------------ 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 krklelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHeGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 160
Cdd:cd04703   125 -------------------------------GCDTVGAVARDG-GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKG 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039762216 161 aqnpystAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFisspflacEDGVLGGVIVL 227
Cdd:cd04703   173 -------AVAATGIGEEIAKRLLARRVYRWIETGLSLQAAAQRAIDEF--------DDGVAVGVIAV 224
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 1-184 2.44e-16

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: 77.26  E-value: 2.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216   1 MDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKgklsagrippcFLVGEGAYRWAVDHGIPSCPPstmttrfslaafkrn 80
Cdd:cd14949    81 MDGQTQRFSGVINIENVKNPIEVAQKLQQEDDR-----------VLSGEGATEFARENGFPEYNP--------------- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762216  81 krklelaervETDFiqlkRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAAlygcgcwaenTG 160
Cdd:cd14949   135 ----------ETPQ----RRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSA----------TV 190

                         170       180
                  ....*....|....*....|....*..
gi 1039762216 161 AQNpYST---AVSTSGCGEHLVRTILA 184
Cdd:cd14949   191 AGN-YANafaGVSCTGIGEDIVSEALA 216
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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