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Conserved domains on  [gi|1021312309|ref|NP_001310531|]
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threonine aspartase 1 isoform 2 [Homo sapiens]

Protein Classification

threonine aspartase 1( domain architecture ID 10139957)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 42-285 1.92e-79

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: 242.95  E-value: 1.92e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEEND------------SGT--------- 100
Cdd:cd04514     1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPltnagygsnlteDGTvecdasimd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 101 ----------------------------------------------------------LDTVGAVVVDHEGNVAAAVSSG 122
Cdd:cd04514    81 gssgrfgavgavsgvknpiqlarlllkeqrkplslgrvppmflvgegarewakskgiiTDTVGAIAIDLYGNIAAGSSSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 123 GLALKHPGRVGQAALYGCGCWAENTGAHNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPF 201
Cdd:cd04514   161 GIGLKHPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 202 LASEDG---VLGGVIVLRscrcsaepdsSQNKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIE 278
Cdd:cd04514   241 MGHPGVknsPSAGAIGVL----------AVKKTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQG 306


                  ....*..
gi 1021312309 279 GGVCRLE 285
Cdd:cd04514   307 GRKIRLR 313
 
Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 42-285 1.92e-79

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: 242.95  E-value: 1.92e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEEND------------SGT--------- 100
Cdd:cd04514     1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPltnagygsnlteDGTvecdasimd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 101 ----------------------------------------------------------LDTVGAVVVDHEGNVAAAVSSG 122
Cdd:cd04514    81 gssgrfgavgavsgvknpiqlarlllkeqrkplslgrvppmflvgegarewakskgiiTDTVGAIAIDLYGNIAAGSSSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 123 GLALKHPGRVGQAALYGCGCWAENTGAHNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPF 201
Cdd:cd04514   161 GIGLKHPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 202 LASEDG---VLGGVIVLRscrcsaepdsSQNKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIE 278
Cdd:cd04514   241 MGHPGVknsPSAGAIGVL----------AVKKTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQG 306


                  ....*..
gi 1021312309 279 GGVCRLE 285
Cdd:cd04514   307 GRKIRLR 313
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 101-264 8.06e-28

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 111.11  E-value: 8.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 101 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEHLVRTILARECSHAL 179
Cdd:PLN02937  227 MDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSS 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 180 ---QAEDAHQA---LLETMQNkfiSSPFLASEDgvlGGVIVLRSCRCSAEPDSSQNKQTllVEFLWSHTTESMCVGYMSA 253
Cdd:PLN02937  307 slsQAGPASACmkvLRSVIQG---SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIGYFGS 378

                         170
                  ....*....|.
gi 1021312309 254 QDGKAKTHISR 264
Cdd:PLN02937  379 SMERPKVSILR 389
Asparaginase_2 pfam01112
Asparaginase;
70-253 1.33e-19

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 86.48  E-value: 1.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309  70 QKAIEKLQAGALATDAVTAALVELEENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGA 149
Cdd:pfam01112 144 QELQKARKENFQPNMALNVAPDPLKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATG 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 150 hnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflasedGVLGGVIVLrscrcsaepd 225
Cdd:pfam01112 224 ------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV----------GGDGGVIAV---------- 277

                         170       180
                  ....*....|....*....|....*...
gi 1021312309 226 ssqNKQTllvEFLWSHTTESMCVGYMSA 253
Cdd:pfam01112 278 ---DAKG---NIAAPFNTEGMYRAYHTG 299
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 102-262 7.51e-19

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 84.39  E-value: 7.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 102 DTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECSHALQA 181
Cdd:COG1446   171 GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVG------AVSATGHGEYFIRTVVAHDIVERMRQ 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 182 -EDAHQALLETMQNKfisspflASEDGVLGGVIVLrscrcsaepdssqNKQTllvEFLWSHTTESMCVGYMSAqDGKAKT 260
Cdd:COG1446   245 gLSLQEAAEEVIERI-------LKKLGGDGGLIAV-------------DKDG---NIAAPFNTEGMYRAYIDG-DGELVV 300


                  ..
gi 1021312309 261 HI 262
Cdd:COG1446   301 AI 302
 
Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 42-285 1.92e-79

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: 242.95  E-value: 1.92e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEEND------------SGT--------- 100
Cdd:cd04514     1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPltnagygsnlteDGTvecdasimd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 101 ----------------------------------------------------------LDTVGAVVVDHEGNVAAAVSSG 122
Cdd:cd04514    81 gssgrfgavgavsgvknpiqlarlllkeqrkplslgrvppmflvgegarewakskgiiTDTVGAIAIDLYGNIAAGSSSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 123 GLALKHPGRVGQAALYGCGCWAENTGAHNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPF 201
Cdd:cd04514   161 GIGLKHPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 202 LASEDG---VLGGVIVLRscrcsaepdsSQNKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIE 278
Cdd:cd04514   241 MGHPGVknsPSAGAIGVL----------AVKKTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQG 306


                  ....*..
gi 1021312309 279 GGVCRLE 285
Cdd:cd04514   307 GRKIRLR 313
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 44-251 1.03e-47

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: 159.65  E-value: 1.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309  44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEEN---DSGT-------------------- 100
Cdd:cd04512     2 LIVHGGAGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDplfNAGRgsvlnedgevemdaaimdgk 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 101 ---------------------------------------------LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQA 135
Cdd:cd04512    82 tlnagavagvkgvknpislaravmektphvllvgegaerfarehgHGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 136 ALYGCGCWAENTgahnpySTAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKfisspfLASEDGVLGGVIVL 215
Cdd:cd04512   162 PIIGAGTYADNE------TGAVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAEAAIDY------LRRRVGGEGGLIVV 229

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1021312309 216 RScrcsaepdssqnkqtlLVEFLWSHTTESMCVGYM 251
Cdd:cd04512   230 DP----------------DGRLGAAHNTPGMAFAYI 249
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 101-264 8.06e-28

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 111.11  E-value: 8.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 101 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEHLVRTILARECSHAL 179
Cdd:PLN02937  227 MDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSS 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 180 ---QAEDAHQA---LLETMQNkfiSSPFLASEDgvlGGVIVLRSCRCSAEPDSSQNKQTllVEFLWSHTTESMCVGYMSA 253
Cdd:PLN02937  307 slsQAGPASACmkvLRSVIQG---SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIGYFGS 378

                         170
                  ....*....|.
gi 1021312309 254 QDGKAKTHISR 264
Cdd:PLN02937  379 SMERPKVSILR 389
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 66-215 1.42e-21

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: 91.86  E-value: 1.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309  66 KRACQKAIEKLQAGALATDAVTAAL-------VELEENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALY 138
Cdd:cd04702   122 KFAEEMGIPQVPPESLVTERARERLekfkkekGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPII 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 139 GCGCWAENtgahnpYSTAVSTSGCGEHLVRTILARECSHALQ----AEDAHQALLETMQNKFisspflasedGVLGGVIV 214
Cdd:cd04702   202 GSGGYADN------LVGAVSTTGHGESIMKVNLARLILFHMEqgktAEEAAELALAYMKSRV----------KGLGGLIV 265


                  .
gi 1021312309 215 L 215
Cdd:cd04702   266 V 266
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 75-252 5.12e-21

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: 89.56  E-value: 5.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309  75 KLQAGALAT-----DAVTAALVELEEND--------------SGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQA 135
Cdd:cd14950    82 TLRVGAVAAvravkNPIRLARKVMEKTDhvlivgegadelakRLGGDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDS 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 136 ALYGCGCWAENtgahnpySTAVSTSGCGEHLVRTILARECSHA----LQAEDAHQALLETMQNKFISSpflasedgvLGG 211
Cdd:cd14950   162 PIPGAGFYATN-------GVAVSATGIGEVIIRSLPALRADELvsmgGDIEEAVRAVVNKVTETFGKD---------TAG 225

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1021312309 212 VIVLrscrcsaepDSSQNkqtllveFLWSHTTESMCVGYMS 252
Cdd:cd14950   226 IIGI---------DARGN-------IAAAFNTEAMPRGYID 250
Asparaginase_2 pfam01112
Asparaginase;
70-253 1.33e-19

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 86.48  E-value: 1.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309  70 QKAIEKLQAGALATDAVTAALVELEENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGA 149
Cdd:pfam01112 144 QELQKARKENFQPNMALNVAPDPLKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATG 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 150 hnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflasedGVLGGVIVLrscrcsaepd 225
Cdd:pfam01112 224 ------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV----------GGDGGVIAV---------- 277

                         170       180
                  ....*....|....*....|....*...
gi 1021312309 226 ssqNKQTllvEFLWSHTTESMCVGYMSA 253
Cdd:pfam01112 278 ---DAKG---NIAAPFNTEGMYRAYHTG 299
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 102-262 7.51e-19

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 84.39  E-value: 7.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 102 DTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECSHALQA 181
Cdd:COG1446   171 GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVG------AVSATGHGEYFIRTVVAHDIVERMRQ 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 182 -EDAHQALLETMQNKfisspflASEDGVLGGVIVLrscrcsaepdssqNKQTllvEFLWSHTTESMCVGYMSAqDGKAKT 260
Cdd:COG1446   245 gLSLQEAAEEVIERI-------LKKLGGDGGLIAV-------------DKDG---NIAAPFNTEGMYRAYIDG-DGELVV 300


                  ..
gi 1021312309 261 HI 262
Cdd:COG1446   301 AI 302
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 46-177 1.66e-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: 82.89  E-value: 1.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309  46 VHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEEN------------------------ 96
Cdd:cd04701     4 IHGGAGtisraNLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCplfnagkgavftrdgtneleasim 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309  97 DSGTLD-------------------------------------------------TVGAVVVDHEGNVAAAVSSGGLALK 127
Cdd:cd04701    84 DGRTKRagavaglrrvrnpillaravleksphvllsgegaeefareqglelvpqgTVGAVALDSDGNLAAATSTGGLTNK 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1021312309 128 HPGRVGQAALYGCGCWAENtgahnpYSTAVSTSGCGEHLVRTILARECSH 177
Cdd:cd04701   164 LPGRIGDTPIIGAGFWAEE------WAVAVSGTGNGDSFIRVAAARDVAA 207
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 44-215 1.48e-15

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: 74.22  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309  44 VLVHAGAGyhsesKAKEYKHVCKRACQKAIEKLQAGALATDAVTAALVELEE------------NDSGTL---------- 101
Cdd:cd04703     3 VLVHGGAG-----SDPERQDGLERAAEAGLAELQNGGDALDAVVAAVRVLEDdprfnagtgsvlRDDGSIqmdaavmtsg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 102 -------------------------------------------------DTVGAVVVDHeGNVAAAVSSGGLALKHPGRV 132
Cdd:cd04703    78 gafgavaaiegvknpvlvaravmetsphvllagdgavrfarrlgypdgcDTVGAVARDG-GKFAAAVSTGGTSPALRGRV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309 133 GQAALYGCGCWAENTGahnpystAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFisspflasEDGVLGGV 212
Cdd:cd04703   157 GDVPIIGAGFYAGPKG-------AVAATGIGEEIAKRLLARRVYRWIETGLSLQAAAQRAIDEF--------DDGVAVGV 221


                  ...
gi 1021312309 213 IVL 215
Cdd:cd04703   222 IAV 224
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 70-172 4.35e-14

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 71.13  E-value: 4.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309  70 QKAIEKLQAGALATDAVTAALveleeNDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTga 149
Cdd:PRK10226  151 EQLLAARAEGATVLDHSGAPL-----DEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNA-- 223

                          90       100
                  ....*....|....*....|...
gi 1021312309 150 hnpySTAVSTSGCGEHLVRTILA 172
Cdd:PRK10226  224 ----SVAVSCTGTGEVFIRALAA 242
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 102-174 5.79e-12

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 65.11  E-value: 5.79e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021312309 102 DTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGahnpystAVSTSGCGEHLVRTILARE 174
Cdd:PLN02689  187 ETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYANHLC-------AVSATGKGEAIIRGTVARD 252
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 102-174 1.37e-11

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: 63.73  E-value: 1.37e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021312309 102 DTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT-GAhnpystAVSTsGCGEHLVRTILARE 174
Cdd:cd04513   170 DTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEvGA------AAAT-GDGDIMMRFLPSYQ 236
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 92-172 1.69e-08

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: 54.54  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021312309  92 ELEENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAAlygcgcwaenTGAHNpYST---AVSTSGCGEHLVR 168
Cdd:cd14949   144 EEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSA----------TVAGN-YANafaGVSCTGIGEDIVS 212


                  ....
gi 1021312309 169 TILA 172
Cdd:cd14949   213 EALA 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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