NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|676248249|gb|KFO12121|]
View 

Threonine aspartase 1, partial [Balearica regulorum gibbericeps]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 42-292 2.60e-107

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: 314.59  E-value: 2.60e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDASIMD 121
Cdd:cd04514    1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 122 GKSLNFGAVGALSGIKNPVSVANRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpacppgimatrfslaafkrnkr 201
Cdd:cd04514   81 GSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI---------------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 202 klelaekvetdliqlkkrrqsnekendsgTLDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAH 281
Cdd:cd04514  138 -----------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPD 188

                        250
                 ....*....|.
gi 676248249 282 TPYSTAVSTSG 292
Cdd:cd04514  189 DKTSVAVVTSG 199
 
Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 42-292 2.60e-107

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: 314.59  E-value: 2.60e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDASIMD 121
Cdd:cd04514    1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 122 GKSLNFGAVGALSGIKNPVSVANRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpacppgimatrfslaafkrnkr 201
Cdd:cd04514   81 GSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI---------------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 202 klelaekvetdliqlkkrrqsnekendsgTLDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAH 281
Cdd:cd04514  138 -----------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPD 188

                        250
                 ....*....|.
gi 676248249 282 TPYSTAVSTSG 292
Cdd:cd04514  189 DKTSVAVVTSG 199
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 34-292 1.52e-75

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 237.07  E-value: 1.52e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  34 QTQRGKRVGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALAT-DAVTAALIELEDSPFTNAGLGSNLNLLGE 112
Cdd:PLN02937   4 DGADQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCiDAVSAAIQVLEDDPSTNAGRGSNLTEDGH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 113 IECDASIMDGKSLNFGAVGALSGIKNPVSVANRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPAcpPGIMA---- 188
Cdd:PLN02937  84 VECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDL--PETVEeaek 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 189 ---TRFSLAAFKRNKRKLELA-EKVETD------LIQLKKRRQSNEKENDSGT------------LDTVGAVVVDQEGNV 246
Cdd:PLN02937 162 wlvTERAKEQWKKYKTMLASAiAKSSCDsqstskLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNI 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 676248249 247 AAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAH-TPYSTAVSTSG 292
Cdd:PLN02937 242 ASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFgAPFIVGCCVSG 288
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 44-293 1.38e-64

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 205.34  E-value: 1.38e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDAS 118
Cdd:COG1446    8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDAS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 119 IMDGKSLNFGAVGALSGIKNPVSVANRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPACPPgimatrfslaafkr 198
Cdd:COG1446   88 IMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDP-------------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 199 nkrkleLAEKVETDLIQLKKRRQSNEKENDSGTlDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 278
Cdd:COG1446  144 ------LYFFTEKRWKQWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNE 216

                        250
                 ....*....|....*
gi 676248249 279 GAhtpystAVSTSGI 293
Cdd:COG1446  217 VG------AVSATGH 225
Asparaginase_2 pfam01112
Asparaginase;
44-293 2.91e-55

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 181.24  E-value: 2.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249   44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDASIMD 121
Cdd:pfam01112   2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIMD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  122 GKSLNFGAVGALSGIKNPVSVAnRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPACPPGIMATRFSLAAFKRnkr 201
Cdd:pfam01112  82 GKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQK--- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  202 klELAEKVETDLIQLKKRRQSNEKENDSgtLDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAh 281
Cdd:pfam01112 149 --ARKENFQPNMALNVAPDPLKECGDSK--RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATG- 223

                         250
                  ....*....|..
gi 676248249  282 tpystAVSTSGI 293
Cdd:pfam01112 224 -----AVSATGH 230
 
Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 42-292 2.60e-107

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: 314.59  E-value: 2.60e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDASIMD 121
Cdd:cd04514    1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 122 GKSLNFGAVGALSGIKNPVSVANRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpacppgimatrfslaafkrnkr 201
Cdd:cd04514   81 GSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI---------------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 202 klelaekvetdliqlkkrrqsnekendsgTLDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAH 281
Cdd:cd04514  138 -----------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPD 188

                        250
                 ....*....|.
gi 676248249 282 TPYSTAVSTSG 292
Cdd:cd04514  189 DKTSVAVVTSG 199
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 44-293 3.92e-77

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: 235.54  E-value: 3.92e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDASIMDGK 123
Cdd:cd04512    2 LIVHGGAGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIMDGK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 124 SLNFGAVGALSGIKNPVSVANRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipacppgimatrfslaafkrnkrkl 203
Cdd:cd04512   82 TLNAGAVAGVKGVKNPISLARAVMEKT----------PHVLLVGEGAERFAREHG------------------------- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 204 elaekvetdliqlkkrrqsnekendsgtLDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTgahtp 283
Cdd:cd04512  127 ----------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNE----- 173

                        250
                 ....*....|
gi 676248249 284 ySTAVSTSGI 293
Cdd:cd04512  174 -TGAVSATGH 182
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 34-292 1.52e-75

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 237.07  E-value: 1.52e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  34 QTQRGKRVGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALAT-DAVTAALIELEDSPFTNAGLGSNLNLLGE 112
Cdd:PLN02937   4 DGADQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCiDAVSAAIQVLEDDPSTNAGRGSNLTEDGH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 113 IECDASIMDGKSLNFGAVGALSGIKNPVSVANRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPAcpPGIMA---- 188
Cdd:PLN02937  84 VECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDL--PETVEeaek 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 189 ---TRFSLAAFKRNKRKLELA-EKVETD------LIQLKKRRQSNEKENDSGT------------LDTVGAVVVDQEGNV 246
Cdd:PLN02937 162 wlvTERAKEQWKKYKTMLASAiAKSSCDsqstskLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNI 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 676248249 247 AAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAH-TPYSTAVSTSG 292
Cdd:PLN02937 242 ASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFgAPFIVGCCVSG 288
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 44-293 1.38e-64

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 205.34  E-value: 1.38e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDAS 118
Cdd:COG1446    8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDAS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 119 IMDGKSLNFGAVGALSGIKNPVSVANRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPACPPgimatrfslaafkr 198
Cdd:COG1446   88 IMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDP-------------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 199 nkrkleLAEKVETDLIQLKKRRQSNEKENDSGTlDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 278
Cdd:COG1446  144 ------LYFFTEKRWKQWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNE 216

                        250
                 ....*....|....*
gi 676248249 279 GAhtpystAVSTSGI 293
Cdd:COG1446  217 VG------AVSATGH 225
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 44-292 2.25e-59

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: 191.25  E-value: 2.25e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDASIMDGK 123
Cdd:cd04702    4 IVVHGGAGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASIMDGK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 124 SLNFGAVGALSGIKNPVSVAnRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPACPPGIMATRFSLAAFKRNKRKl 203
Cdd:cd04702   84 TLRAGAVSAVRNIANPISLA-RLVME---------KTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKE- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 204 elaekvetdliqlkkrrQSNEKENDSGTLDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgahtp 283
Cdd:cd04702  153 -----------------KGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADN------ 209


                 ....*....
gi 676248249 284 YSTAVSTSG 292
Cdd:cd04702  210 LVGAVSTTG 218
Asparaginase_2 pfam01112
Asparaginase;
44-293 2.91e-55

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 181.24  E-value: 2.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249   44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDASIMD 121
Cdd:pfam01112   2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIMD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  122 GKSLNFGAVGALSGIKNPVSVAnRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPACPPGIMATRFSLAAFKRnkr 201
Cdd:pfam01112  82 GKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQK--- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  202 klELAEKVETDLIQLKKRRQSNEKENDSgtLDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAh 281
Cdd:pfam01112 149 --ARKENFQPNMALNVAPDPLKECGDSK--RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATG- 223

                         250
                  ....*....|..
gi 676248249  282 tpystAVSTSGI 293
Cdd:pfam01112 224 -----AVSATGH 230
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 46-292 1.75e-48

Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzyme undergoes an autoproteolytic cleavage into alpha and beta subunits to expose a threonine residue which becomes the N-terminal residue of the beta subunit. The threonine residue plays a central role in hydrolase activity. Some asparaginases can also hydrolyze L-glutamine and are termed glutaminase-asparaginase. This is a member of the Ntn-hydrolase superfamily, and this subfamily covers mostly bacterial and fungal enzymes.


Pssm-ID: 271337  Cd Length: 264  Bit Score: 162.63  E-value: 1.75e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  46 VHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDASIM 120
Cdd:cd04701    4 IHGGAGtisraNLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEASIM 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 121 DGKSLNFGAVGALSGIKNPVSVAnRLLCEGQkgklsagriPPCFLVGEGAYRWAVDHGIPACPPGimatrfslaafkrnk 200
Cdd:cd04701   84 DGRTKRAGAVAGLRRVRNPILLA-RAVLEKS---------PHVLLSGEGAEEFAREQGLELVPQG--------------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 201 rklelaekvetdliqlkkrrqsnekendsgtldTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtga 280
Cdd:cd04701  139 ---------------------------------TVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEE--- 182

                        250
                 ....*....|..
gi 676248249 281 htpYSTAVSTSG 292
Cdd:cd04701  183 ---WAVAVSGTG 191
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 66-290 1.05e-42

Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoproteins. This enzyme is an amidase located inside lysosomes. Mutation of this gene in humans causes a genetic disorder known as aspartylglycosaminuria (AGU). The glycosylasparaginase precursor undergoes autoproteolysis through an N-O or N-S acyl rearrangement of the peptide bond, which leads to the cleavage of a peptide bond between an Asp and a Thr. This proteolysis step generates an exposed N-terminal catalytic threonine and activates the enzyme.


Pssm-ID: 271335  Cd Length: 294  Bit Score: 148.48  E-value: 1.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  66 KRACQKAIEKLQAGALATDAVTAALIELEDSPF-TNAGLGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAN 144
Cdd:cd04513    9 TEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCdGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVAR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 145 RLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPACPpgiMATRFSLAA---FKRNKRKLELAEKVETD---LIQLKK 218
Cdd:cd04513   89 AVM----------EHTPHSLLVGEGATEFAVSMGFKEEN---LLTEESRKMwkkWLKENCQPNFWKNVVPDpskSCSSPK 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 676248249 219 RRQSNEKENDSGTLDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT-GAhtpystAVST 290
Cdd:cd04513  156 APSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEvGA------AAAT 222
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 46-293 2.72e-42

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 147.93  E-value: 2.72e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  46 VHAGAGYHSESKAKEYKHVCKRACQKA----IEKLQAGALATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDASIMD 121
Cdd:PLN02689   8 LHGGAGDIDPNLPRERQEEAEAALRRCldlgIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEASIMD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 122 GKSLNFGAVGALSGIKNPVSVAnRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPACPPGIMATRfslaafkRNKR 201
Cdd:PLN02689  88 GRTRRCGAVSGLTTVVNPISLA-RLVME---------KTPHIYLAFDGAEAFARQQGVETVDNSYFITE-------ENVE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 202 KLELAEkvETDLIQL-------KKRRQSNEKENDSGTLDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCW 274
Cdd:PLN02689 151 RLKQAK--EANSVQFdyripldKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTY 228

                        250
                 ....*....|....*....
gi 676248249 275 AENTGahtpystAVSTSGI 293
Cdd:PLN02689 229 ANHLC-------AVSATGK 240
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 44-293 7.51e-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: 145.03  E-value: 7.51e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  44 VLVHAGAGYHSESKAKE-YKHVCKRACQKAIEKLQAGAlATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDASIMDG 122
Cdd:cd14950    2 LVVHGGAGSWKNSDDEEkALRALREALERGYEALRRGS-ALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDAGIMDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 123 KSLNFGAVGALSGIKNPVSVANRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipacppgimatrfslaafkrnkrk 202
Cdd:cd14950   81 RTLRVGAVAAVRAVKNPIRLARKVMEKT----------DHVLIVGEGADELAKRLG------------------------ 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 203 lelaekvetdliqlkkrrqsnekendsgtLDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgaht 282
Cdd:cd14950  127 -----------------------------GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN----- 172

                        250
                 ....*....|.
gi 676248249 283 pySTAVSTSGI 293
Cdd:cd14950  173 --GVAVSATGI 181
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 44-292 8.66e-36

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 130.84  E-value: 8.66e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  44 VLVHAGAGYHSESK-----AKEYKHVCKRACQKAIEKLQAGALATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDAS 118
Cdd:PRK10226   6 IAIHGGAGAISRAQmslqqELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDAC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 119 IMDGKSLNFGAVGALSGIKNPVsVANRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPACPPGIMATrfslaafkr 198
Cdd:PRK10226  86 VMDGNTLKAGAVAGVSHLRNPV-LAARLVME---------QSPHVMMIGEGAENFAFAHGMERVSPEIFST--------- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 199 NKRKLELAEKVETDLIQLKkrrQSNEKENDSGTLDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 278
Cdd:PRK10226 147 PLRYEQLLAARAEGATVLD---HSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNA 223

                        250
                 ....*....|....
gi 676248249 279 gahtpySTAVSTSG 292
Cdd:PRK10226 224 ------SVAVSCTG 231
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 44-293 2.06e-33

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: 122.75  E-value: 2.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  44 VLVHAGAGyhsesKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDASIMDGK 123
Cdd:cd04703    3 VLVHGGAG-----SDPERQDGLERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAVMTSG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 124 SlNFGAVGALSGIKNPVSVANRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIPacppgimatrfslaafkrnkrkl 203
Cdd:cd04703   78 G-AFGAVAAIEGVKNPVLVARAVMETS----------PHVLLAGDGAVRFARRLGYP----------------------- 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 204 elaekvetdliqlkkrrqsnekendsGTLDTVGAVVVDqEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGahtp 283
Cdd:cd04703  124 --------------------------DGCDTVGAVARD-GGKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKG---- 172

                        250
                 ....*....|
gi 676248249 284 ystAVSTSGI 293
Cdd:cd04703  173 ---AVAATGI 179
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 44-267 1.39e-26

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: 105.38  E-value: 1.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249  44 VLVHAGAGyhSESKAK-EYKHVCKRACQKAIEK----LQAGAlATDAVTAALIELEDSPFTNAGLGSNLNLLGEIECDAS 118
Cdd:cd14949    3 LIIHGGFG--SESSTNgETKAAKQEALAEIVEEvyeyLKSHS-ALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQIRMSAS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676248249 119 IMDGKSLNFGAVGALSGIKNPVSVANRLLCEGQKgklsagrippcFLVGEGAYRWAVDHGIPACPPgimatrfslaafkr 198
Cdd:cd14949   80 LMDGQTQRFSGVINIENVKNPIEVAQKLQQEDDR-----------VLSGEGATEFARENGFPEYNP-------------- 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 676248249 199 nkrklelaekvETDliqlKKRRQSNEKENDSGTLDTVGAVVVDQEGNVAAAVSSGGLALKHPGRVGQAA 267
Cdd:cd14949  135 -----------ETP----QRRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSA 188
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH