|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
42-349 |
1.17e-76 |
|
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: 238.33 E-value: 1.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEESRI----------------------- 98
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLtnagygsnltedgtvecdasimd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 99 QSQLLTGSC--VKGRR-ASSLQAEFLpgfslaafkRNKRKLELAERVETDFIQLKRRRQSsAKENDsGTLDTVGAVVVDH 175
Cdd:cd04514 81 GSSGRFGAVgaVSGVKnPIQLARLLL---------KEQRKPLSLGRVPPMFLVGEGAREW-AKSKG-IITDTVGAIAIDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 176 EGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAQNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLE 254
Cdd:cd04514 150 YGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDED 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 255 TMQNKFISSPFLACEDG---VLGGVIVLRSCRcssesdssqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPP 331
Cdd:cd04514 230 EILRSFIESDFMGHPGVknsPSAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPG 299
|
330
....*....|....*...
gi 1720401051 332 GAvagqSVAIEGGVCRLE 349
Cdd:cd04514 300 NG----SIAQGGRKIRLR 313
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
37-328 |
7.36e-27 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 109.95 E-value: 7.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVE-LEESRI----------------- 98
Cdd:PLN02937 7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCIDAVSAAIQvLEDDPStnagrgsnltedghvec 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 99 QSQLLTGS--------CVKGRR-----ASSLQAEFLPGFSL--------------------------------------- 126
Cdd:PLN02937 87 DASIMDGDsgafgavgAVPGVRnaiqiAALLAKEQMMGSSLlgrippmflvgegarqwakskgidlpetveeaekwlvte 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 127 ---AAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT------------LDTVGAVVVDHEGNVAAAVS 184
Cdd:PLN02937 167 rakEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIASGAS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 185 SGGLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGCGEHLVRTILARECSHAL---QAEDAHQA---LLETMQ 257
Cdd:PLN02937 247 SGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSSslsQAGPASACmkvLRSVIQ 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401051 258 NkfiSSPFLACEDgvlGGVIVLRSCRCSSESDSSQDKQTllVEFLWSHTTESMCVGYMSAQDGKAKTHISR 328
Cdd:PLN02937 327 G---SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
138-326 |
5.46e-21 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 91.71 E-value: 5.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 138 LAERVETDFIQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAqnpy 217
Cdd:COG1446 144 LYFFTEKRWKQWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVG---- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 218 stAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspfLAcEDGVLGGVIVLrscrcssesdssqDKQT 296
Cdd:COG1446 219 --AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI------LK-KLGGDGGLIAV-------------DKDG 276
|
170 180 190
....*....|....*....|....*....|
gi 1720401051 297 llvEFLWSHTTESMCVGYMSAqDGKAKTHI 326
Cdd:COG1446 277 ---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
166-317 |
3.11e-20 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 89.57 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 166 DTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAqnpystAVSTSGCGEHLVRTILARECS----H 241
Cdd:pfam01112 176 GTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVarmeY 249
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401051 242 ALQAEDAHQALLETMQNKFisspflacedGVLGGVIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMSA 317
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 ... |
42-349 |
1.17e-76 |
|
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: 238.33 E-value: 1.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEESRI----------------------- 98
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLtnagygsnltedgtvecdasimd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 99 QSQLLTGSC--VKGRR-ASSLQAEFLpgfslaafkRNKRKLELAERVETDFIQLKRRRQSsAKENDsGTLDTVGAVVVDH 175
Cdd:cd04514 81 GSSGRFGAVgaVSGVKnPIQLARLLL---------KEQRKPLSLGRVPPMFLVGEGAREW-AKSKG-IITDTVGAIAIDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 176 EGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAQNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLE 254
Cdd:cd04514 150 YGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDED 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 255 TMQNKFISSPFLACEDG---VLGGVIVLRSCRcssesdssqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPP 331
Cdd:cd04514 230 EILRSFIESDFMGHPGVknsPSAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPG 299
|
330
....*....|....*...
gi 1720401051 332 GAvagqSVAIEGGVCRLE 349
Cdd:cd04514 300 NG----SIAQGGRKIRLR 313
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
44-315 |
3.94e-42 |
|
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: 146.94 E-value: 3.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEESRiqsqLL---TGScVKGRR------AS 114
Cdd:cd04512 2 LIVHGGAGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDP----LFnagRGS-VLNEDgevemdAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 115 SLQAEFLPGFSLAAFKRNKRKLELAERV--ETDFIQL-KRRRQSSAKENDsgtLDTVGAVVVDHEGNVAAAVSSGGLALK 191
Cdd:cd04512 77 IMDGKTLNAGAVAGVKGVKNPISLARAVmeKTPHVLLvGEGAERFAREHG---HGTVGAVARDAQGNLAAATSTGGMVNK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 192 HPGRVGQAALYGCGCWAENTgaqnpySTAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFISSpflaceDG 271
Cdd:cd04512 154 RPGRVGDSPIIGAGTYADNE------TGAVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAEAAIDYLRRR------VG 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1720401051 272 VLGGVIVLrscrcssesdssqDKQtllVEFLWSHTTESMCVGYM 315
Cdd:cd04512 222 GEGGLIVV-------------DPD---GRLGAAHNTPGMAFAYI 249
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
37-328 |
7.36e-27 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 109.95 E-value: 7.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVE-LEESRI----------------- 98
Cdd:PLN02937 7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCIDAVSAAIQvLEDDPStnagrgsnltedghvec 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 99 QSQLLTGS--------CVKGRR-----ASSLQAEFLPGFSL--------------------------------------- 126
Cdd:PLN02937 87 DASIMDGDsgafgavgAVPGVRnaiqiAALLAKEQMMGSSLlgrippmflvgegarqwakskgidlpetveeaekwlvte 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 127 ---AAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT------------LDTVGAVVVDHEGNVAAAVS 184
Cdd:PLN02937 167 rakEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIASGAS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 185 SGGLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGCGEHLVRTILARECSHAL---QAEDAHQA---LLETMQ 257
Cdd:PLN02937 247 SGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSSslsQAGPASACmkvLRSVIQ 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720401051 258 NkfiSSPFLACEDgvlGGVIVLRSCRCSSESDSSQDKQTllVEFLWSHTTESMCVGYMSAQDGKAKTHISR 328
Cdd:PLN02937 327 G---SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
158-279 |
1.68e-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: 92.63 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 158 KENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgaqnpYSTAVSTSGCGEHLVRTILAR 237
Cdd:cd04702 157 VEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADN------LVGAVSTTGHGESIMKVNLAR 230
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720401051 238 ECSHALQ----AEDAHQALLETMQNKFisspflacedGVLGGVIVL 279
Cdd:cd04702 231 LILFHMEqgktAEEAAELALAYMKSRV----------KGLGGLIVV 266
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
165-316 |
2.03e-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: 91.87 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 165 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgaqnpySTAVSTSGCGEHLVRTILARECSHA-- 242
Cdd:cd14950 127 GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN-------GVAVSATGIGEVIIRSLPALRADELvs 199
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401051 243 --LQAEDAHQALLETMQNKFISSpflacedgvLGGVIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMS 316
Cdd:cd14950 200 mgGDIEEAVRAVVNKVTETFGKD---------TAGIIGI-------------DARG---NIAAAFNTEAMPRGYID 250
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
138-326 |
5.46e-21 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 91.71 E-value: 5.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 138 LAERVETDFIQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAqnpy 217
Cdd:COG1446 144 LYFFTEKRWKQWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVG---- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 218 stAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspfLAcEDGVLGGVIVLrscrcssesdssqDKQT 296
Cdd:COG1446 219 --AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI------LK-KLGGDGGLIAV-------------DKDG 276
|
170 180 190
....*....|....*....|....*....|
gi 1720401051 297 llvEFLWSHTTESMCVGYMSAqDGKAKTHI 326
Cdd:COG1446 277 ---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
166-317 |
3.11e-20 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 89.57 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 166 DTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAqnpystAVSTSGCGEHLVRTILARECS----H 241
Cdd:pfam01112 176 GTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVarmeY 249
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720401051 242 ALQAEDAHQALLETMQNKFisspflacedGVLGGVIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMSA 317
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 ... |
167-279 |
7.02e-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: 82.12 E-value: 7.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 167 TVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgaqnpYSTAVSTSGCGEHLVRTILARECSHalQAE 246
Cdd:cd04701 139 TVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEE------WAVAVSGTGNGDSFIRVAAARDVAA--RMR 210
|
90 100 110
....*....|....*....|....*....|...
gi 1720401051 247 DAHQALLETMqnKFISSPFLACEDGVlGGVIVL 279
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; ... |
166-279 |
3.71e-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: 76.91 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 166 DTVGAVVVDHeGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGaqnpystAVSTSGCGEHLVRTILARECSHALQA 245
Cdd:cd04703 127 DTVGAVARDG-GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKG-------AVAATGIGEEIAKRLLARRVYRWIET 198
|
90 100 110
....*....|....*....|....*....|....
gi 1720401051 246 EDAHQALLETMQNKFisspflacEDGVLGGVIVL 279
Cdd:cd04703 199 GLSLQAAAQRAIDEF--------DDGVAVGVIAV 224
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
154-236 |
1.64e-14 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 73.44 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 154 QSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTgaqnpySTAVSTSGCGEHLVRT 233
Cdd:PRK10226 166 HSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNA------SVAVSCTGTGEVFIRA 239
|
...
gi 1720401051 234 ILA 236
Cdd:PRK10226 240 LAA 242
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
130-238 |
5.55e-14 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 71.66 E-value: 5.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 130 KRNKRKLELAE---RVETDFIQ--LKRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGC 204
Cdd:PLN02689 146 EENVERLKQAKeanSVQFDYRIplDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGA 225
|
90 100 110
....*....|....*....|....*....|....
gi 1720401051 205 GCWAENTGaqnpystAVSTSGCGEHLVRTILARE 238
Cdd:PLN02689 226 GTYANHLC-------AVSATGKGEAIIRGTVARD 252
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
166-279 |
3.35e-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: 66.05 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 166 DTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT-GAqnpystAVSTsGCGEhlvrtILARECShalq 244
Cdd:cd04513 170 DTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEvGA------AAAT-GDGD-----IMMRFLP---- 233
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720401051 245 aedAHQAlLETMQNKFisSPFLACEDGVL-----------GGVIVL 279
Cdd:cd04513 234 ---SYQA-VELMRQGM--SPQEACEDAIRriakkypkdfeGAVVAV 273
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
151-236 |
4.39e-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: 59.54 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720401051 151 RRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAAlygcgcwaenTGAQNpYST---AVSTSGCG 227
Cdd:cd14949 139 RRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSA----------TVAGN-YANafaGVSCTGIG 207
|
....*....
gi 1720401051 228 EHLVRTILA 236
Cdd:cd14949 208 EDIVSEALA 216
|
|
| |
