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Conserved domains on  [gi|1958761953|ref|XP_038960956|]
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threonine aspartase 1 isoform X10 [Rattus norvegicus]

Protein Classification

threonine aspartase 1( domain architecture ID 10139957)

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

EC:  3.4.25.-
Gene Ontology:  GO:0004298|GO:0005515|GO:0006508
MEROPS:  T02
PubMed:  27308523

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 ...
 46-230 1.73e-64

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: 202.50  E-value: 1.73e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  46 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHNPYSTAVSTSGCGEHLVRTILARECSHALQ 125
Cdd:cd04514   139 TDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLY 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953 126 AEDAHQ-ALLETMQNKFISSPFLASEDG---VLGGVIVLRSCRcpsesdpsqdKQTLLVEFLWSHSTESMCVGYMSAQDG 201
Cdd:cd04514   219 HSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDR 288

                         170       180
                  ....*....|....*....|....*....
gi 1958761953 202 KAKTHISRLPPGAvagqSVAIEGGVCRLE 230
Cdd:cd04514   289 KPKCVMSRLPGNG----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 ...
 46-230 1.73e-64

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: 202.50  E-value: 1.73e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  46 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHNPYSTAVSTSGCGEHLVRTILARECSHALQ 125
Cdd:cd04514   139 TDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLY 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953 126 AEDAHQ-ALLETMQNKFISSPFLASEDG---VLGGVIVLRSCRcpsesdpsqdKQTLLVEFLWSHSTESMCVGYMSAQDG 201
Cdd:cd04514   219 HSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDR 288

                         170       180
                  ....*....|....*....|....*....
gi 1958761953 202 KAKTHISRLPPGAvagqSVAIEGGVCRLE 230
Cdd:cd04514   289 KPKCVMSRLPGNG----SIAQGGRKIRLR 313
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 46-209 4.10e-29

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 112.65  E-value: 4.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  46 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEHLVRTILARECSHAL 124
Cdd:PLN02937  227 MDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSS 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953 125 ---QAEDAHQA---LLETMQNkfiSSPFLASEDgvlGGVIVLRSCRcpSESDPSQDKQTLLVEFLWSHSTESMCVGYMSA 198
Cdd:PLN02937  307 slsQAGPASACmkvLRSVIQG---SSAKTTDKD---AGILLVQADA--SVMAPGNSPSLKAVEIAAAYSSLSFGIGYFGS 378

                         170
                  ....*....|.
gi 1958761953 199 QDGKAKTHISR 209
Cdd:PLN02937  379 SMERPKVSILR 389
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 19-207 9.00e-22

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 90.94  E-value: 9.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  19 LAERVETDFIQLKRRRQSSAKENDSGaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAhnpy 98
Cdd:COG1446   144 LYFFTEKRWKQWKKALEYKPIINERK-HGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVG---- 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  99 stAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspflASEDGVLGGVIVLrscrcpsesdpsqDKQT 177
Cdd:COG1446   219 --AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI-------LKKLGGDGGLIAV-------------DKDG 276

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958761953 178 llvEFLWSHSTESMCVGYMSAqDGKAKTHI 207
Cdd:COG1446   277 ---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
Asparaginase_2 pfam01112
Asparaginase;
47-198 1.52e-20

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 88.02  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  47 DTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECS----H 122
Cdd:pfam01112 176 GTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVarmeY 249

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958761953 123 ALQAEDAHQALLETMQNKFisspflasedGVLGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSA 198
Cdd:pfam01112 250 GLSLEEAADKVITEMLKRV----------GGDGGVIAV-------------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 ...
 46-230 1.73e-64

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: 202.50  E-value: 1.73e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  46 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHNPYSTAVSTSGCGEHLVRTILARECSHALQ 125
Cdd:cd04514   139 TDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLY 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953 126 AEDAHQ-ALLETMQNKFISSPFLASEDG---VLGGVIVLRSCRcpsesdpsqdKQTLLVEFLWSHSTESMCVGYMSAQDG 201
Cdd:cd04514   219 HSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDR 288

                         170       180
                  ....*....|....*....|....*....
gi 1958761953 202 KAKTHISRLPPGAvagqSVAIEGGVCRLE 230
Cdd:cd04514   289 KPKCVMSRLPGNG----SIAQGGRKIRLR 313
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 46-196 2.24e-38

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: 133.46  E-value: 2.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  46 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTgahnpySTAVSTSGCGEHLVRTILARECSHALQ 125
Cdd:cd04512   127 HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNE------TGAVSATGHGESIIRTVLAKRIADLVE 200

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958761953 126 AEDAHQALLETMQNKfisspfLASEDGVLGGVIVLrscrcpsesdpsqDKQtllVEFLWSHSTESMCVGYM 196
Cdd:cd04512   201 FGGSAQEAAEAAIDY------LRRRVGGEGGLIVV-------------DPD---GRLGAAHNTPGMAFAYI 249
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 46-209 4.10e-29

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 112.65  E-value: 4.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  46 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEHLVRTILARECSHAL 124
Cdd:PLN02937  227 MDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSS 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953 125 ---QAEDAHQA---LLETMQNkfiSSPFLASEDgvlGGVIVLRSCRcpSESDPSQDKQTLLVEFLWSHSTESMCVGYMSA 198
Cdd:PLN02937  307 slsQAGPASACmkvLRSVIQG---SSAKTTDKD---AGILLVQADA--SVMAPGNSPSLKAVEIAAAYSSLSFGIGYFGS 378

                         170
                  ....*....|.
gi 1958761953 199 QDGKAKTHISR 209
Cdd:PLN02937  379 SMERPKVSILR 389
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 39-160 1.20e-22

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: 93.02  E-value: 1.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  39 KENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgahnpYSTAVSTSGCGEHLVRTILAR 118
Cdd:cd04702   157 VEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADN------LVGAVSTTGHGESIMKVNLAR 230

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958761953 119 ECSHALQ----AEDAHQALLETMQNKFisspflasedGVLGGVIVL 160
Cdd:cd04702   231 LILFHMEqgktAEEAAELALAYMKSRV----------KGLGGLIVV 266
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 46-197 4.62e-22

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: 90.72  E-value: 4.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  46 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgahnpySTAVSTSGCGEHLVRTILARECSHA-- 123
Cdd:cd14950   127 GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN-------GVAVSATGIGEVIIRSLPALRADELvs 199

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958761953 124 --LQAEDAHQALLETMQNKFISSpflasedgvLGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMS 197
Cdd:cd14950   200 mgGDIEEAVRAVVNKVTETFGKD---------TAGIIGI-------------DARG---NIAAAFNTEAMPRGYID 250
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 19-207 9.00e-22

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 90.94  E-value: 9.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  19 LAERVETDFIQLKRRRQSSAKENDSGaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAhnpy 98
Cdd:COG1446   144 LYFFTEKRWKQWKKALEYKPIINERK-HGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVG---- 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  99 stAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspflASEDGVLGGVIVLrscrcpsesdpsqDKQT 177
Cdd:COG1446   219 --AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI-------LKKLGGDGGLIAV-------------DKDG 276

                         170       180       190
                  ....*....|....*....|....*....|
gi 1958761953 178 llvEFLWSHSTESMCVGYMSAqDGKAKTHI 207
Cdd:COG1446   277 ---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
Asparaginase_2 pfam01112
Asparaginase;
47-198 1.52e-20

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 88.02  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  47 DTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECS----H 122
Cdd:pfam01112 176 GTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVarmeY 249

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958761953 123 ALQAEDAHQALLETMQNKFisspflasedGVLGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSA 198
Cdd:pfam01112 250 GLSLEEAADKVITEMLKRV----------GGDGGVIAV-------------DAKG---NIAAPFNTEGMYRAYHTG 299
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 48-160 1.99e-18

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: 81.35  E-value: 1.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  48 TVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgahnpYSTAVSTSGCGEHLVRTILARECSHalQAE 127
Cdd:cd04701   139 TVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEE------WAVAVSGTGNGDSFIRVAAARDVAA--RMR 210

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958761953 128 DAHQALLETMqnKFISSPFLASEDGVlGGVIVL 160
Cdd:cd04701   211 YKGLSLAEAA--KEVVGPGGELGEGE-GGIIAI 240
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 47-160 3.16e-16

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: 74.99  E-value: 3.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  47 DTVGAVVVDHeGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGahnpystAVSTSGCGEHLVRTILARECSHALQA 126
Cdd:cd04703   127 DTVGAVARDG-GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKG-------AVAATGIGEEIAKRLLARRVYRWIET 198

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958761953 127 EDAHQALLETMQNKFisspflasEDGVLGGVIVL 160
Cdd:cd04703   199 GLSLQAAAQRAIDEF--------DDGVAVGVIAV 224
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 35-117 3.18e-15

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 73.06  E-value: 3.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  35 QSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTgahnpySTAVSTSGCGEHLVRT 114
Cdd:PRK10226  166 HSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNA------SVAVSCTGTGEVFIRA 239


                  ...
gi 1958761953 115 ILA 117
Cdd:PRK10226  240 LAA 242
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 11-119 1.08e-14

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 71.66  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  11 KRNKRKLELAE---RVETDFIQ--LKRRRQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGC 85
Cdd:PLN02689  146 EENVERLKQAKeanSVQFDYRIplDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGA 225

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958761953  86 GCWAENTGahnpystAVSTSGCGEHLVRTILARE 119
Cdd:PLN02689  226 GTYANHLC-------AVSATGKGEAIIRGTVARD 252
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 47-119 3.06e-12

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: 64.50  E-value: 3.06e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958761953  47 DTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT-GAhnpystAVSTsGCGEHLVRTILARE 119
Cdd:cd04513   170 DTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEvGA------AAAT-GDGDIMMRFLPSYQ 236
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 32-117 2.69e-10

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: 58.77  E-value: 2.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958761953  32 RRRQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAAlygcgcwaenTGAHNpYST---AVSTSGCG 108
Cdd:cd14949   139 RRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSA----------TVAGN-YANafaGVSCTGIG 207


                  ....*....
gi 1958761953 109 EHLVRTILA 117
Cdd:cd14949   208 EDIVSEALA 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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