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Conserved domains on  [gi|513178396|ref|XP_004940500|]
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isoaspartyl peptidase/L-asparaginase [Gallus gallus]

Protein Classification

isoaspartyl peptidase/L-asparaginase( domain architecture ID 10140429)

isoaspartyl peptidase/L-asparaginase degrades proteins which are compromised via the formation of L-isoaspartyl residues by removing beta-linked aspartyl residues from the N-terminus; the enzyme also shows activity as an L-asparaginase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 2-289 1.38e-175

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: 487.08  E-value: 1.38e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   2 RPVIVVHGGAGRIFKEREEGCRTGVVRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEMDAIIM 81
Cdd:cd04702    1 KPVIVVHGGAGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASIM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  82 DGKNLASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGVPEIPGEKLITERSRERWKKNLEPDSNPVE-F 160
Cdd:cd04702   81 DGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEKGANVEdT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 161 QKDLGTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYADNSSGATSTTGHGESIMKVVLARLILYHMEQGM 240
Cdd:cd04702  161 QRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNLARLILFHMEQGK 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 513178396 241 SPEMAADTALEYMKTRVGGLGGVIVVSSSGEWAARFSTKQMSWATVKDD 289
Cdd:cd04702  241 TAEEAAELALAYMKSRVKGLGGLIVVSKTGDWGAKFTSKRMAWAAVKDG 289
 
Name Accession Description Interval E-value
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 2-289 1.38e-175

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: 487.08  E-value: 1.38e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   2 RPVIVVHGGAGRIFKEREEGCRTGVVRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEMDAIIM 81
Cdd:cd04702    1 KPVIVVHGGAGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASIM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  82 DGKNLASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGVPEIPGEKLITERSRERWKKNLEPDSNPVE-F 160
Cdd:cd04702   81 DGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEKGANVEdT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 161 QKDLGTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYADNSSGATSTTGHGESIMKVVLARLILYHMEQGM 240
Cdd:cd04702  161 QRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNLARLILFHMEQGK 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 513178396 241 SPEMAADTALEYMKTRVGGLGGVIVVSSSGEWAARFSTKQMSWATVKDD 289
Cdd:cd04702  241 TAEEAAELALAYMKSRVKGLGGLIVVSKTGDWGAKFTSKRMAWAAVKDG 289
Asparaginase_2 pfam01112
Asparaginase;
4-296 2.09e-142

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 403.89  E-value: 2.09e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396    4 VIVVHGGAGRIFK--EREEGCRTGVVRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEMDAIIM 81
Cdd:pfam01112   1 VLVIHGGAGSILRtkEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   82 DGKNLASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGVPEIPGEKLITERSRERWKKNLEPDSNPVEFQ 161
Cdd:pfam01112  81 DGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKENFQPNMAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  162 ------------KDLGTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYADNSSGATSTTGHGESIMKVVLA 229
Cdd:pfam01112 161 nvapdplkecgdSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLA 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 513178396  230 RLILYHMEQGMSPEMAADTALEYMKTRVGGLGGVIVVSSSGEWAARFSTKQMSWATVKDDELHYGIY 296
Cdd:pfam01112 241 YDIVARMEYGLSLEEAADKVITEMLKRVGGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGIGDVLI 307
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 1-296 5.86e-117

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 339.39  E-value: 5.86e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   1 MRPVIVVHGGAGRIFK-----EREEGCRTGVVRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVE 75
Cdd:COG1446    4 SRRALIIHGGAGTIARsamtpEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  76 MDAIIMDGKNLASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGVPEIPGEKLITERSRERWKKNLEPDs 155
Cdd:COG1446   84 LDASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYK- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 156 nPVEFQKDLGTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYADNSSGATSTTGHGESIMKVVLARLILYH 235
Cdd:COG1446  163 -PIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRTVVAHDIVER 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 513178396 236 MEQGMSPEMAADTALEYMKTRVGGLGGVIVVSSSGEWAARFSTKQMSWATVKDD-ELHYGIY 296
Cdd:COG1446  242 MRQGLSLQEAAEEVIERILKKLGGDGGLIAVDKDGNIAAPFNTEGMYRAYIDGDgELVVAIY 303
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 5-247 1.66e-76

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 236.91  E-value: 1.66e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   5 IVVHGGAGRIFK----EREEGCRTGVVRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEMDAII 80
Cdd:PLN02689   6 IALHGGAGDIDPnlprERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEASI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  81 MDGKNLASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGVPEIPGEKLITERSRERWKKNLEPDSNPVEF 160
Cdd:PLN02689  86 MDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAKEANSVQFDY 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 161 QKDL-----------------GTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYAdNSSGATSTTGHGESI 223
Cdd:PLN02689 166 RIPLdkpakaaalaadgdaqpETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYA-NHLCAVSATGKGEAI 244

                        250       260
                 ....*....|....*....|....*
gi 513178396 224 MKVVLARLILYHME-QGMSPEMAAD 247
Cdd:PLN02689 245 IRGTVARDVAAVMEyKGLPLQEAVD 269
 
Name Accession Description Interval E-value
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 2-289 1.38e-175

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: 487.08  E-value: 1.38e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   2 RPVIVVHGGAGRIFKEREEGCRTGVVRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEMDAIIM 81
Cdd:cd04702    1 KPVIVVHGGAGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASIM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  82 DGKNLASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGVPEIPGEKLITERSRERWKKNLEPDSNPVE-F 160
Cdd:cd04702   81 DGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEKGANVEdT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 161 QKDLGTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYADNSSGATSTTGHGESIMKVVLARLILYHMEQGM 240
Cdd:cd04702  161 QRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNLARLILFHMEQGK 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 513178396 241 SPEMAADTALEYMKTRVGGLGGVIVVSSSGEWAARFSTKQMSWATVKDD 289
Cdd:cd04702  241 TAEEAAELALAYMKSRVKGLGGLIVVSKTGDWGAKFTSKRMAWAAVKDG 289
Asparaginase_2 pfam01112
Asparaginase;
4-296 2.09e-142

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 403.89  E-value: 2.09e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396    4 VIVVHGGAGRIFK--EREEGCRTGVVRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEMDAIIM 81
Cdd:pfam01112   1 VLVIHGGAGSILRtkEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   82 DGKNLASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGVPEIPGEKLITERSRERWKKNLEPDSNPVEFQ 161
Cdd:pfam01112  81 DGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKENFQPNMAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  162 ------------KDLGTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYADNSSGATSTTGHGESIMKVVLA 229
Cdd:pfam01112 161 nvapdplkecgdSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLA 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 513178396  230 RLILYHMEQGMSPEMAADTALEYMKTRVGGLGGVIVVSSSGEWAARFSTKQMSWATVKDDELHYGIY 296
Cdd:pfam01112 241 YDIVARMEYGLSLEEAADKVITEMLKRVGGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGIGDVLI 307
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 1-296 5.86e-117

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 339.39  E-value: 5.86e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   1 MRPVIVVHGGAGRIFK-----EREEGCRTGVVRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVE 75
Cdd:COG1446    4 SRRALIIHGGAGTIARsamtpEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  76 MDAIIMDGKNLASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGVPEIPGEKLITERSRERWKKNLEPDs 155
Cdd:COG1446   84 LDASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYK- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 156 nPVEFQKDLGTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYADNSSGATSTTGHGESIMKVVLARLILYH 235
Cdd:COG1446  163 -PIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRTVVAHDIVER 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 513178396 236 MEQGMSPEMAADTALEYMKTRVGGLGGVIVVSSSGEWAARFSTKQMSWATVKDD-ELHYGIY 296
Cdd:COG1446  242 MRQGLSLQEAAEEVIERILKKLGGDGGLIAVDKDGNIAAPFNTEGMYRAYIDGDgELVVAIY 303
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 4-284 3.36e-108

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: 314.89  E-value: 3.36e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   4 VIVVHGGAGRIFKEREEGCRTGVVRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEMDAIIMDG 83
Cdd:cd04512    1 SLIVHGGAGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIMDG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  84 KNLASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGvpeipgeklitersrerwkknlepdsnpvefqkd 163
Cdd:cd04512   81 KTLNAGAVAGVKGVKNPISLARAVMEKTPHVLLVGEGAERFAREHG---------------------------------- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 164 LGTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYADNSSGATSTTGHGESIMKVVLARLILYHMEQGMSPE 243
Cdd:cd04512  127 HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLVEFGGSAQ 206

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 513178396 244 MAADTALEYMKTRVGGLGGVIVVSSSGEWAARFSTKQMSWA 284
Cdd:cd04512  207 EAAEAAIDYLRRRVGGEGGLIVVDPDGRLGAAHNTPGMAFA 247
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 4-249 1.51e-85

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: 257.77  E-value: 1.51e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   4 VIVVHGGAGRIFK-----EREEGCRTGVVRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEMDA 78
Cdd:cd04701    1 ALAIHGGAGTISRanltpERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  79 IIMDGKNLASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGVPEIPgeklitersrerwkknlepdsnpv 158
Cdd:cd04701   81 SIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELVP------------------------ 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 159 efqkdLGTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYADNSSGATSTTGHGESIMKVVLARLILYHME- 237
Cdd:cd04701  137 -----QGTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWAVAVSGTGNGDSFIRVAAARDVAARMRy 211

                        250
                 ....*....|..
gi 513178396 238 QGMSPEMAADTA 249
Cdd:cd04701  212 KGLSLAEAAKEV 223
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 5-247 1.66e-76

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 236.91  E-value: 1.66e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   5 IVVHGGAGRIFK----EREEGCRTGVVRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEMDAII 80
Cdd:PLN02689   6 IALHGGAGDIDPnlprERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEASI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  81 MDGKNLASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGVPEIPGEKLITERSRERWKKNLEPDSNPVEF 160
Cdd:PLN02689  86 MDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAKEANSVQFDY 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 161 QKDL-----------------GTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYAdNSSGATSTTGHGESI 223
Cdd:PLN02689 166 RIPLdkpakaaalaadgdaqpETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYA-NHLCAVSATGKGEAI 244

                        250       260
                 ....*....|....*....|....*
gi 513178396 224 MKVVLARLILYHME-QGMSPEMAAD 247
Cdd:PLN02689 245 IRGTVARDVAAVMEyKGLPLQEAVD 269
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 4-288 3.69e-74

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: 228.23  E-value: 3.69e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   4 VIVVHGGAGRI-FKEREEGCRTGVVRAALRGYGVLKqGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEMDAIIMD 82
Cdd:cd14950    1 ALVVHGGAGSWkNSDDEEKALRALREALERGYEALR-RGSALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDAGIMD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  83 GKNLASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGvpeipgeklitersrerwkknlepdsnpvefqk 162
Cdd:cd14950   80 GRTLRVGAVAAVRAVKNPIRLARKVMEKTDHVLIVGEGADELAKRLG--------------------------------- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 163 dLGTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYADNsSGATSTTGHGESIMKVVLARLILYHMEQGMSP 242
Cdd:cd14950  127 -GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN-GVAVSATGIGEVIIRSLPALRADELVSMGGDI 204

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 513178396 243 EMAADTALEYM-KTRVGGLGGVIVVSSSGEWAARFSTKQMSWATVKD 288
Cdd:cd14950  205 EEAVRAVVNKVtETFGKDTAGIIGIDARGNIAAAFNTEAMPRGYIDD 251
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 29-251 9.11e-71

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: 221.28  E-value: 9.11e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  29 AALRGYGVLKQGGSALDAVEEAVRSMEDDPH-FNAGCGSVLNEKGEVEMDAIIMDGKNLASGAVSAVKCIANPIKLARLV 107
Cdd:cd04513   11 AVEAAWEVLQKGGSALDAVEAGCSVCEDDQCdGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVARAV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 108 MEKTKHMLLTDHGAQLFAQAMGVPEipgEKLITERSRERWKKNLE------------PDSNPVEFQKDL----------- 164
Cdd:cd04513   91 MEHTPHSLLVGEGATEFAVSMGFKE---ENLLTEESRKMWKKWLKencqpnfwknvvPDPSKSCSSPKApsrsesaiped 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 165 --GTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYADNSSGATSTTGHGESIMKVVLARLILYHMEQGMSP 242
Cdd:cd04513  168 nhDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLPSYQAVELMRQGMSP 247


                 ....*....
gi 513178396 243 EMAADTALE 251
Cdd:cd04513  248 QEACEDAIR 256
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 3-284 1.65e-61

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: 195.94  E-value: 1.65e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   3 PVIVVHGGAGRIfKEREEGCRtgvvRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEMDAIIMD 82
Cdd:cd04703    1 MAVLVHGGAGSD-PERQDGLE----RAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAVMT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  83 GKNlASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGVPeipgeklitersrerwkknlepdsnpvefqK 162
Cdd:cd04703   76 SGG-AFGAVAAIEGVKNPVLVARAVMETSPHVLLAGDGAVRFARRLGYP------------------------------D 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 163 DLGTVGAVAVDSeGNVACATSTGGLSNKLVGRVGDTACIGSGGYADnSSGATSTTGHGESIMKVVLARLILYHMEQGMSP 242
Cdd:cd04703  125 GCDTVGAVARDG-GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAG-PKGAVAATGIGEEIAKRLLARRVYRWIETGLSL 202

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 513178396 243 EMAADTALEYMKTRVGGLGGVIvvsSSGEWAARFSTKQMSWA 284
Cdd:cd04703  203 QAAAQRAIDEFDDGVAVGVIAV---SRRGEAGIASNTAMAWA 241
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 2-239 2.31e-55

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 182.46  E-value: 2.31e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   2 RPVIVVHGGAGRIFK-----EREEGCRTGVVRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEM 76
Cdd:PRK10226   3 KAVIAIHGGAGAISRaqmslQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  77 DAIIMDGKNLASGAVSAVKCIANPIKLARLVMEKTKHMLLTDHGAQLFAQAMGVPEIPGEKLIT-ER------SRERWKK 149
Cdd:PRK10226  83 DACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTpLRyeqllaARAEGAT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 150 NLEPDSNPVEFQKDLGTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYADNSSGATSTTGHGESIMKVVLA 229
Cdd:PRK10226 163 VLDHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAA 242

                        250
                 ....*....|
gi 513178396 230 RLILYHMEQG 239
Cdd:PRK10226 243 YDIAALMDYG 252
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 5-230 4.48e-54

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: 179.00  E-value: 4.48e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   5 IVVHGGAGRIFKEREEGCRTGVVRAALRGYGVLKQGGSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEMDAIIMDGK 84
Cdd:cd04514    3 VAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMDGS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  85 NLASGAVSAVKCIANPIKLARLVMEKTKH---------MLLTDHGAQLFAQAMGvpeipgekLITErsrerwkknlepds 155
Cdd:cd04514   83 SGRFGAVGAVSGVKNPIQLARLLLKEQRKplslgrvppMFLVGEGAREWAKSKG--------IITD-------------- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 156 npvefqkdlgTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIGSGGYADNSSG------ATSTTGHGESIMKVVLA 229
Cdd:cd04514  141 ----------TVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPddktsvAVVTSGTGEHIATTMLA 210


                 .
gi 513178396 230 R 230
Cdd:cd04514  211 R 211
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 3-256 1.27e-48

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: 163.93  E-value: 1.27e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   3 PVIVVHGGAGRIFKEREEgcrTGVVR-AAL-----RGYGVLKQGgSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEM 76
Cdd:cd14949    1 PKLIIHGGFGSESSTNGE---TKAAKqEALaeiveEVYEYLKSH-SALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQIRM 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  77 DAIIMDGKNLASGAVSAVKCIANPIKLARLVMEKtKHMLLTDHGAQLFAQAMGVPEIpgEKLITERsRERWKKNLEPDSN 156
Cdd:cd14949   77 SASLMDGQTQRFSGVINIENVKNPIEVAQKLQQE-DDRVLSGEGATEFARENGFPEY--NPETPQR-RQEYEEKKLKSGG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 157 pvefqkdLGTVGAVAVDSEGNVACATSTGGLSNKLVGRVGDTACIgSGGYAdNSSGATSTTGHGESIMKVVLARLILYHM 236
Cdd:cd14949  153 -------TGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNYA-NAFAGVSCTGIGEDIVSEALAAKIVTRV 223

                        250       260
                 ....*....|....*....|
gi 513178396 237 EQGMSPEMAADTALEYMKTR 256
Cdd:cd14949  224 TDGMSLQEAFEKSFAEAKPR 243
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 2-230 1.00e-40

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 146.55  E-value: 1.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396   2 RPVIVVHGGAGRIFKEREEGCRTGVVRAALRGYGVLKQG-GSALDAVEEAVRSMEDDPHFNAGCGSVLNEKGEVEMDAII 80
Cdd:PLN02937  11 RFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGsGGCIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396  81 MDGKNLASGAVSAVKCIANPIKLARLVMEKTKH----------MLLTDHGAQLFAQAMGV--PEIPGEK---LITERSRE 145
Cdd:PLN02937  91 MDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMgssllgrippMFLVGEGARQWAKSKGIdlPETVEEAekwLVTERAKE 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513178396 146 RWKK------NLEPDSNP----------VEFQKD----------------------LGTVGAVAVDSEGNVACATSTGGL 187
Cdd:PLN02937 171 QWKKyktmlaSAIAKSSCdsqstsklseLEAPRSnpsngtgggqssmctasdedciMDTVGVICVDSEGNIASGASSGGI 250

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 513178396 188 SNKLVGRVGDTACIGSGGYADN-------SSGATSTTGHGESIMKVVLAR 230
Cdd:PLN02937 251 AMKVSGRVGLAAMYGSGCWASSkgpfgapFIVGCCVSGAGEYLMRGFAAR 300
 
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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