|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
42-402 |
7.99e-105 |
|
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: 312.28 E-value: 7.99e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPF 121
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLE-----------------------DSPL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 122 TNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHG 201
Cdd:cd04514 58 TNAGYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 202 IpscppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALK 281
Cdd:cd04514 137 I---------------------------------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLK 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 282 HPGRVGQAALYGCGCWAENTGAQNPYSTAVSTSG--------------------------------------SPFLACED 323
Cdd:cd04514 166 HPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGtgehiattmlarrcaerlyhstrreesdedeilrsfieSDFMGHPG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 324 G---VLGGVIVLRSCRcssesdssqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCR 400
Cdd:cd04514 246 VknsPSAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIR 311
|
..
gi 1039762207 401 LE 402
Cdd:cd04514 312 LR 313
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
37-381 |
5.91e-63 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 207.79 E-value: 5.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGAlatdavaaalveleGLSLwltdnkdfSLSVPGLQAS 116
Cdd:PLN02937 7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGS--------------GGCI--------DAVSAAIQVL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 117 VDSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRW 196
Cdd:PLN02937 65 EDDPSTNAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 197 AVDHGIPScpPSTMT-------TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT-------- 254
Cdd:PLN02937 145 AKSKGIDL--PETVEeaekwlvTERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasd 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 255 ----LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGS------PFLACED 323
Cdd:PLN02937 223 edciMDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAgeylmrGFAAREC 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 324 GVLGGVI----------VLRSCRCSSESDSSQDKQTLL-------------------VEFLWSHTTESMCVGYMSAQDGK 374
Cdd:PLN02937 303 CVSSSLSqagpasacmkVLRSVIQGSSAKTTDKDAGILlvqadasvmapgnspslkaVEIAAAYSSLSFGIGYFGSSMER 382
|
....*..
gi 1039762207 375 AKTHISR 381
Cdd:PLN02937 383 PKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
44-379 |
8.81e-50 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 170.29 E-value: 8.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGalatdavaaalveleGLSLwltdnkDfslsvpGLQASV- 117
Cdd:COG1446 8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAG---------------GSAL------D------AVEAAVr 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 118 ---DSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAY 194
Cdd:COG1446 61 vleDDPLFNAGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 195 RWAVDHGIPSCPPSTmttrfslaaFKRNKRKLelaervetdfiQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVS 274
Cdd:COG1446 131 RFAREQGLELVDPLY---------FFTEKRWK-----------QWKKALEYKPIINERKH-GTVGAVALDANGNLAAATS 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 275 SGGLALKHPGRVGQAALYGCGCWAENTGAqnpystAVSTSG----------------------SPFLACEDGVL------ 326
Cdd:COG1446 190 TGGMTNKRPGRVGDSPIIGAGTYADNEVG------AVSATGhgeyfirtvvahdivermrqglSLQEAAEEVIErilkkl 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039762207 327 ---GGVIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMSAqDGKAKTHI 379
Cdd:COG1446 264 ggdGGLIAV-------------DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
44-370 |
7.78e-43 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 151.97 E-value: 7.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPF 121
Cdd:pfam01112 2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLE-----------------------DDPL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 122 TNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHG 201
Cdd:pfam01112 59 FNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 202 IPSCPPSTMTTRFSLAAFKRNKrklelaervETDFIQLKRRRQSSA--KENDSGTLDTVGAVVVDHEGNVAAAVSSGGLA 279
Cdd:pfam01112 129 LERVPPEDFLTEERLQELQKAR---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMT 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 280 LKHPGRVGQAALYGCGCWAENTGAqnpystAVSTSG----------------------SPFLACEDGV---------LGG 328
Cdd:pfam01112 200 NKRPGRVGDSPIIGAGTYADNATG------AVSATGhgediiretlaydivarmeyglSLEEAADKVItemlkrvggDGG 273
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1039762207 329 VIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMSA 370
Cdd:pfam01112 274 VIAV-------------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 ... |
42-402 |
7.99e-105 |
|
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: 312.28 E-value: 7.99e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPF 121
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLE-----------------------DSPL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 122 TNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHG 201
Cdd:cd04514 58 TNAGYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 202 IpscppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALK 281
Cdd:cd04514 137 I---------------------------------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLK 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 282 HPGRVGQAALYGCGCWAENTGAQNPYSTAVSTSG--------------------------------------SPFLACED 323
Cdd:cd04514 166 HPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGtgehiattmlarrcaerlyhstrreesdedeilrsfieSDFMGHPG 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 324 G---VLGGVIVLRSCRcssesdssqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCR 400
Cdd:cd04514 246 VknsPSAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIR 311
|
..
gi 1039762207 401 LE 402
Cdd:cd04514 312 LR 313
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
44-368 |
1.57e-65 |
|
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: 209.35 E-value: 1.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPFTN 123
Cdd:cd04512 2 LIVHGGAGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLE-----------------------DDPLFN 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 124 AGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGip 203
Cdd:cd04512 59 AGRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLARAVMEKT----------PHVLLVGEGAERFAREHG-- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 204 scppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgtLDTVGAVVVDHEGNVAAAVSSGGLALKHP 283
Cdd:cd04512 127 ---------------------------------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRP 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 284 GRVGQAALYGCGCWAENTgaqnpySTAVSTSG----------------------SPFLACE---------DGVLGGVIVL 332
Cdd:cd04512 156 GRVGDSPIIGAGTYADNE------TGAVSATGhgesiirtvlakriadlvefggSAQEAAEaaidylrrrVGGEGGLIVV 229
|
330 340 350
....*....|....*....|....*....|....*.
gi 1039762207 333 rscrcssesdssqDKQtllVEFLWSHTTESMCVGYM 368
Cdd:cd04512 230 -------------DPD---GRLGAAHNTPGMAFAYI 249
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
37-381 |
5.91e-63 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 207.79 E-value: 5.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGAlatdavaaalveleGLSLwltdnkdfSLSVPGLQAS 116
Cdd:PLN02937 7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGS--------------GGCI--------DAVSAAIQVL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 117 VDSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRW 196
Cdd:PLN02937 65 EDDPSTNAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 197 AVDHGIPScpPSTMT-------TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT-------- 254
Cdd:PLN02937 145 AKSKGIDL--PETVEeaekwlvTERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasd 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 255 ----LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGS------PFLACED 323
Cdd:PLN02937 223 edciMDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAgeylmrGFAAREC 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 324 GVLGGVI----------VLRSCRCSSESDSSQDKQTLL-------------------VEFLWSHTTESMCVGYMSAQDGK 374
Cdd:PLN02937 303 CVSSSLSqagpasacmkVLRSVIQGSSAKTTDKDAGILlvqadasvmapgnspslkaVEIAAAYSSLSFGIGYFGSSMER 382
|
....*..
gi 1039762207 375 AKTHISR 381
Cdd:PLN02937 383 PKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
44-379 |
8.81e-50 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 170.29 E-value: 8.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGalatdavaaalveleGLSLwltdnkDfslsvpGLQASV- 117
Cdd:COG1446 8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAG---------------GSAL------D------AVEAAVr 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 118 ---DSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAY 194
Cdd:COG1446 61 vleDDPLFNAGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 195 RWAVDHGIPSCPPSTmttrfslaaFKRNKRKLelaervetdfiQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVS 274
Cdd:COG1446 131 RFAREQGLELVDPLY---------FFTEKRWK-----------QWKKALEYKPIINERKH-GTVGAVALDANGNLAAATS 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 275 SGGLALKHPGRVGQAALYGCGCWAENTGAqnpystAVSTSG----------------------SPFLACEDGVL------ 326
Cdd:COG1446 190 TGGMTNKRPGRVGDSPIIGAGTYADNEVG------AVSATGhgeyfirtvvahdivermrqglSLQEAAEEVIErilkkl 263
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1039762207 327 ---GGVIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMSAqDGKAKTHI 379
Cdd:COG1446 264 ggdGGLIAV-------------DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
44-315 |
7.20e-45 |
|
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: 156.96 E-value: 7.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGalatdavaaalveleGLSLwltdnkDfslSVP-GLQASVDSPFT 122
Cdd:cd04702 4 IVVHGGAGSIPDDRIKGSREGVKRAARAGYSVLKAG---------------GSAL------D---AVEaAVRALEDDPVF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 123 NAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGI 202
Cdd:cd04702 60 NAGYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLA-RLVME---------KTPHCFLTGRGANKFAEEMGI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 203 PSCPPSTMTTRFSLAAFKRNKRKlelaervetdfiqlkrrrQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKH 282
Cdd:cd04702 130 PQVPPESLVTERARERLEKFKKE------------------KGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKM 191
|
250 260 270
....*....|....*....|....*....|...
gi 1039762207 283 PGRVGQAALYGCGCWAENtgaqnpYSTAVSTSG 315
Cdd:cd04702 192 VGRVGDSPIIGSGGYADN------LVGAVSTTG 218
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
44-370 |
7.78e-43 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 151.97 E-value: 7.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPF 121
Cdd:pfam01112 2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLE-----------------------DDPL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 122 TNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHG 201
Cdd:pfam01112 59 FNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 202 IPSCPPSTMTTRFSLAAFKRNKrklelaervETDFIQLKRRRQSSA--KENDSGTLDTVGAVVVDHEGNVAAAVSSGGLA 279
Cdd:pfam01112 129 LERVPPEDFLTEERLQELQKAR---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMT 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 280 LKHPGRVGQAALYGCGCWAENTGAqnpystAVSTSG----------------------SPFLACEDGV---------LGG 328
Cdd:pfam01112 200 NKRPGRVGDSPIIGAGTYADNATG------AVSATGhgediiretlaydivarmeyglSLEEAADKVItemlkrvggDGG 273
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1039762207 329 VIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMSA 370
Cdd:pfam01112 274 VIAV-------------DAKG---NIAAPFNTEGMYRAYHTG 299
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
125-313 |
1.94e-36 |
|
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: 134.61 E-value: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 125 GIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPS 204
Cdd:cd04513 46 GYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVARAVM----------EHTPHSLLVGEGATEFAVSMGFKE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 205 CPPSTMTTRFSLAAFKRNKRKLELAERVETD---FIQLKRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALK 281
Cdd:cd04513 116 ENLLTEESRKMWKKWLKENCQPNFWKNVVPDpskSCSSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFK 195
|
170 180 190
....*....|....*....|....*....|...
gi 1039762207 282 HPGRVGQAALYGCGCWAENT-GAqnpystAVST 313
Cdd:cd04513 196 IPGRVGDSPIPGAGLYADNEvGA------AAAT 222
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
46-315 |
1.77e-34 |
|
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: 128.35 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 46 VHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSP 120
Cdd:cd04701 4 IHGGAGtisraNLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLE-----------------------DCP 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 121 FTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDH 200
Cdd:cd04701 61 LFNAGKGAVFTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKS----------PHVLLSGEGAEEFAREQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 201 GIPSCPPStmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgtldTVGAVVVDHEGNVAAAVSSGGLAL 280
Cdd:cd04701 131 GLELVPQG------------------------------------------------TVGAVALDSDGNLAAATSTGGLTN 162
|
250 260 270
....*....|....*....|....*....|....*
gi 1039762207 281 KHPGRVGQAALYGCGCWAENtgaqnpYSTAVSTSG 315
Cdd:cd04701 163 KLPGRIGDTPIIGAGFWAEE------WAVAVSGTG 191
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
46-315 |
1.44e-32 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 124.82 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 46 VHAGAGYHSESKAKEYKHVCKRACQKA----IEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPF 121
Cdd:PLN02689 8 LHGGAGDIDPNLPRERQEEAEAALRRCldlgIAALRSSLPALDVVELVVRELE-----------------------NDPL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 122 TNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHG 201
Cdd:PLN02689 65 FNAGRGSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLA-RLVME---------KTPHIYLAFDGAEAFARQQG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 202 IPSCPPSTMTTRfslaafkRNKRKLELAE---RVETDFIQ--LKRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSG 276
Cdd:PLN02689 135 VETVDNSYFITE-------ENVERLKQAKeanSVQFDYRIplDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTG 207
|
250 260 270
....*....|....*....|....*....|....*....
gi 1039762207 277 GLALKHPGRVGQAALYGCGCWAENTGaqnpystAVSTSG 315
Cdd:PLN02689 208 GLVNKMVGRIGDTPIIGAGTYANHLC-------AVSATG 239
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
118-303 |
1.73e-31 |
|
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: 119.99 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 118 DSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWA 197
Cdd:cd14950 53 DSGVFNAGVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIRLARKVMEKT----------DHVLIVGEGADELA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 198 VDHGipscppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgtLDTVGAVVVDHEGNVAAAVSSGG 277
Cdd:cd14950 123 KRLG-----------------------------------------------------GDTVGAVALDKDGNLAAATSTGG 149
|
170 180
....*....|....*....|....*.
gi 1039762207 278 LALKHPGRVGQAALYGCGCWAENTGA 303
Cdd:cd14950 150 VWLKLPGRVGDSPIPGAGFYATNGVA 175
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
120-316 |
1.51e-27 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 111.19 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 120 PFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVsVAHRLLCEgqkgklsagRIPPCFLVGEGAYRWAVD 199
Cdd:PRK10226 64 PLFNAGIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPV-LAARLVME---------QSPHVMMIGEGAENFAFA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 200 HGIPSCPPSTMTTrfslaafkrNKRKLELAERVETDFIQLKrrrQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLA 279
Cdd:PRK10226 134 HGMERVSPEIFST---------PLRYEQLLAARAEGATVLD---HSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMT 201
|
170 180 190
....*....|....*....|....*....|....*..
gi 1039762207 280 LKHPGRVGQAALYGCGCWAENTgaqnpySTAVSTSGS 316
Cdd:PRK10226 202 NKLPGRVGDSPLVGAGCYANNA------SVAVSCTGT 232
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
44-303 |
6.05e-23 |
|
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: 96.56 E-value: 6.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 44 VLVHAGAGyhsesKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPFTN 123
Cdd:cd04703 3 VLVHGGAG-----SDPERQDGLERAAEAGLAELQNGGDALDAVVAAVRVLE-----------------------DDPRFN 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 124 AGIGSNLNLLGEIECDASIMDGKSlNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIP 203
Cdd:cd04703 55 AGTGSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVARAVMETS----------PHVLLAGDGAVRFARRLGYP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 204 scppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsGTLDTVGAVVVDHeGNVAAAVSSGGLALKHP 283
Cdd:cd04703 124 -------------------------------------------------DGCDTVGAVARDG-GKFAAAVSTGGTSPALR 153
|
250 260
....*....|....*....|
gi 1039762207 284 GRVGQAALYGCGCWAENTGA 303
Cdd:cd04703 154 GRVGDVPIIGAGFYAGPKGA 173
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
118-290 |
1.34e-20 |
|
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: 90.75 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 118 DSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKgklsagrippcFLVGEGAYRWA 197
Cdd:cd14949 56 DDPLFNAGTGSQIQSDGQIRMSASLMDGQTQRFSGVINIENVKNPIEVAQKLQQEDDR-----------VLSGEGATEFA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039762207 198 VDHGIPSCPPstmttrfslaafkrnkrklelaervETDFiqlkRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGG 277
Cdd:cd14949 125 RENGFPEYNP-------------------------ETPQ----RRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGG 175
|
170
....*....|...
gi 1039762207 278 LALKHPGRVGQAA 290
Cdd:cd14949 176 KGFEIPGRVSDSA 188
|
|
| |
