|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
42-416 |
4.43e-130 |
|
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: 377.00 E-value: 4.43e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEDSPFTNAGIGSNLNLLGEIECDASIMD 121
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 122 GKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpscppstmttrfslaafkrnkr 201
Cdd:cd04514 81 GSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI---------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 202 klelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAQ 281
Cdd:cd04514 138 -----------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPD 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 282 NPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLACEDG---VLGGVIVLRSCRcssesds 357
Cdd:cd04514 189 DKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK------- 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 30424856 358 sqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 416
Cdd:cd04514 262 ---KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
37-395 |
7.21e-78 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 247.09 E-value: 7.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVE-LEDSPFTNAGIGSNLNLLGEIEC 115
Cdd:PLN02937 7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCIDAVSAAIQvLEDDPSTNAGRGSNLTEDGHVEC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 116 DASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPScpPSTMT------- 188
Cdd:PLN02937 87 DASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDL--PETVEeaekwlv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 189 TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT------------LDTVGAVVVDHEGNVAAA 249
Cdd:PLN02937 165 TERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIASG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 250 VSSGGLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGCGEHLVRTILARECSHAL---QAEDAHQA---LLET 322
Cdd:PLN02937 245 ASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSSslsQAGPASACmkvLRSV 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30424856 323 MQNkfiSSPFLACEDgvlGGVIVLRSCRCSSESDSSQDKQTllVEFLWSHTTESMCVGYMSAQDGKAKTHISR 395
Cdd:PLN02937 325 IQG---SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
44-393 |
8.33e-59 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 194.17 E-value: 8.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEDSPFTNAGIGSNLNLLGEIECDAS 118
Cdd:COG1446 8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 119 IMDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaaFKR 198
Cdd:COG1446 88 IMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDPLY---------FFT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 199 NKRKLelaervetdfiQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 278
Cdd:COG1446 149 EKRWK-----------QWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 279 GAqnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspfLAcEDGVLGGVIVLrscrcssesds 357
Cdd:COG1446 217 VG------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI------LK-KLGGDGGLIAV----------- 272
|
330 340 350
....*....|....*....|....*....|....*.
gi 30424856 358 sqDKQTllvEFLWSHTTESMCVGYMSAqDGKAKTHI 393
Cdd:COG1446 273 --DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
44-384 |
1.99e-54 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 182.78 E-value: 1.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEDSPFTNAGIGSNLNLLGEIECDASIMD 121
Cdd:pfam01112 2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIMD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 122 GKSLNFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKr 201
Cdd:pfam01112 82 GKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQKAR- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 202 klelaervETDFIQLKRRRQSSA--KENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 279
Cdd:pfam01112 151 --------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNAT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 280 AqnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflacedGVLGGVIVLrscrcsses 355
Cdd:pfam01112 223 G------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV----------GGDGGVIAV--------- 277
|
330 340
....*....|....*....|....*....
gi 30424856 356 dssqDKQTllvEFLWSHTTESMCVGYMSA 384
Cdd:pfam01112 278 ----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 ... |
42-416 |
4.43e-130 |
|
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: 377.00 E-value: 4.43e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEDSPFTNAGIGSNLNLLGEIECDASIMD 121
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 122 GKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIpscppstmttrfslaafkrnkr 201
Cdd:cd04514 81 GSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGI---------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 202 klelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAQ 281
Cdd:cd04514 138 -----------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPD 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 282 NPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLACEDG---VLGGVIVLRSCRcssesds 357
Cdd:cd04514 189 DKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsPSAGAIGVLAVK------- 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 30424856 358 sqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 416
Cdd:cd04514 262 ---KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
44-382 |
3.45e-86 |
|
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: 262.89 E-value: 3.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEDSPFTNAGIGSNLNLLGEIECDASIMDGK 123
Cdd:cd04512 2 LIVHGGAGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIMDGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 124 SLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscppstmttrfslaafkrnkrkl 203
Cdd:cd04512 82 TLNAGAVAGVKGVKNPISLARAVMEKT----------PHVLLVGEGAERFAREHG------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 204 elaervetdfiqlkrrrqssakendsgtLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTgaqnp 283
Cdd:cd04512 127 ----------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNE----- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 284 ySTAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFISSpflaceDGVLGGVIVLrscrcssesdssqDKQt 363
Cdd:cd04512 174 -TGAVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAEAAIDYLRRR------VGGEGGLIVV-------------DPD- 232
|
330
....*....|....*....
gi 30424856 364 llVEFLWSHTTESMCVGYM 382
Cdd:cd04512 233 --GRLGAAHNTPGMAFAYI 249
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
37-395 |
7.21e-78 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 247.09 E-value: 7.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVE-LEDSPFTNAGIGSNLNLLGEIEC 115
Cdd:PLN02937 7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCIDAVSAAIQvLEDDPSTNAGRGSNLTEDGHVEC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 116 DASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPScpPSTMT------- 188
Cdd:PLN02937 87 DASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSKGIDL--PETVEeaekwlv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 189 TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT------------LDTVGAVVVDHEGNVAAA 249
Cdd:PLN02937 165 TERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedciMDTVGVICVDSEGNIASG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 250 VSSGGLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGCGEHLVRTILARECSHAL---QAEDAHQA---LLET 322
Cdd:PLN02937 245 ASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSSslsQAGPASACmkvLRSV 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30424856 323 MQNkfiSSPFLACEDgvlGGVIVLRSCRCSSESDSSQDKQTllVEFLWSHTTESMCVGYMSAQDGKAKTHISR 395
Cdd:PLN02937 325 IQG---SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIGYFGSSMERPKVSILR 389
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
44-393 |
8.33e-59 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 194.17 E-value: 8.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEDSPFTNAGIGSNLNLLGEIECDAS 118
Cdd:COG1446 8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 119 IMDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTmttrfslaaFKR 198
Cdd:COG1446 88 IMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLELVDPLY---------FFT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 199 NKRKLelaervetdfiQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 278
Cdd:COG1446 149 EKRWK-----------QWKKALEYKPIINERKH-GTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 279 GAqnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspfLAcEDGVLGGVIVLrscrcssesds 357
Cdd:COG1446 217 VG------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI------LK-KLGGDGGLIAV----------- 272
|
330 340 350
....*....|....*....|....*....|....*.
gi 30424856 358 sqDKQTllvEFLWSHTTESMCVGYMSAqDGKAKTHI 393
Cdd:COG1446 273 --DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
44-346 |
2.63e-57 |
|
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: 189.70 E-value: 2.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEDSPFTNAGIGSNLNLLGEIECDASIMDGK 123
Cdd:cd04702 4 IVVHGGAGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASIMDGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 124 SLNFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKRKl 203
Cdd:cd04702 84 TLRAGAVSAVRNIANPISLA-RLVME---------KTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKE- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 204 elaervetdfiqlkrrrQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgaqnp 283
Cdd:cd04702 153 -----------------KGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADN------ 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30424856 284 YSTAVSTSGCGEHLVRTILARECSHALQ----AEDAHQALLETMQNKFisspflacedGVLGGVIVL 346
Cdd:cd04702 210 LVGAVSTTGHGESIMKVNLARLILFHMEqgktAEEAAELALAYMKSRV----------KGLGGLIVV 266
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
44-384 |
1.99e-54 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 182.78 E-value: 1.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEDSPFTNAGIGSNLNLLGEIECDASIMD 121
Cdd:pfam01112 2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIMD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 122 GKSLNFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKr 201
Cdd:pfam01112 82 GKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVPPEDFLTEERLQELQKAR- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 202 klelaervETDFIQLKRRRQSSA--KENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTG 279
Cdd:pfam01112 151 --------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNAT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 280 AqnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflacedGVLGGVIVLrscrcsses 355
Cdd:pfam01112 223 G------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV----------GGDGGVIAV--------- 277
|
330 340
....*....|....*....|....*....
gi 30424856 356 dssqDKQTllvEFLWSHTTESMCVGYMSA 384
Cdd:pfam01112 278 ----DAKG---NIAAPFNTEGMYRAYHTG 299
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
46-346 |
1.53e-42 |
|
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: 150.30 E-value: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 46 VHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEDSPFTNAGIGSNLNLLGEIECDASIM 120
Cdd:cd04701 4 IHGGAGtisraNLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEASIM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 121 DGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIPSCPPStmttrfslaafkrnk 200
Cdd:cd04701 84 DGRTKRAGAVAGLRRVRNPILLARAVLEKS----------PHVLLSGEGAEEFAREQGLELVPQG--------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 201 rklelaervetdfiqlkrrrqssakendsgtldTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtga 280
Cdd:cd04701 139 ---------------------------------TVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEE--- 182
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30424856 281 qnpYSTAVSTSGCGEHLVRTILARECSHalQAEDAHQALLETMqnKFISSPFLACEDGVlGGVIVL 346
Cdd:cd04701 183 ---WAVAVSGTGNGDSFIRVAAARDVAA--RMRYKGLSLAEAA--KEVVGPGGELGEGE-GGIIAI 240
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
46-305 |
7.90e-42 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 149.86 E-value: 7.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 46 VHAGAGYHSESKAKEYKHVCKRACQKA----IEKLQAGALATDAVAAALVELEDSPFTNAGIGSNLNLLGEIECDASIMD 121
Cdd:PLN02689 8 LHGGAGDIDPNLPRERQEEAEAALRRCldlgIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEASIMD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 122 GKSLNFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRfslaafkRNKR 201
Cdd:PLN02689 88 GRTRRCGAVSGLTTVVNPISLA-RLVME---------KTPHIYLAFDGAEAFARQQGVETVDNSYFITE-------ENVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 202 KLELAE---RVETDFIQ--LKRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAE 276
Cdd:PLN02689 151 RLKQAKeanSVQFDYRIplDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYAN 230
|
250 260
....*....|....*....|....*....
gi 30424856 277 NTGaqnpystAVSTSGCGEHLVRTILARE 305
Cdd:PLN02689 231 HLC-------AVSATGKGEAIIRGTVARD 252
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
44-383 |
7.29e-40 |
|
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: 142.72 E-value: 7.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 44 VLVHAGAGYHSESKAKE-YKHVCKRACQKAIEKLQAGALATDAVAAALVeLEDSPFTNAGIGSNLNLLGEIECDASIMDG 122
Cdd:cd14950 2 LVVHGGAGSWKNSDDEEkALRALREALERGYEALRRGSALEAVVEAVAY-MEDSGVFNAGVGSVLNLEGEVEMDAGIMDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 123 KSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscppstmttrfslaafkrnkrk 202
Cdd:cd14950 81 RTLRVGAVAAVRAVKNPIRLARKVMEKT----------DHVLIVGEGADELAKRLG------------------------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 203 lelaervetdfiqlkrrrqssakendsgtLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENtgaqn 282
Cdd:cd14950 127 -----------------------------GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN----- 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 283 pySTAVSTSGCGEHLVRTILARECSHA----LQAEDAHQALLETMQNKFISSpflacedgvLGGVIVLrscrcssesdss 358
Cdd:cd14950 173 --GVAVSATGIGEVIIRSLPALRADELvsmgGDIEEAVRAVVNKVTETFGKD---------TAGIIGI------------ 229
|
330 340
....*....|....*....|....*
gi 30424856 359 qDKQTllvEFLWSHTTESMCVGYMS 383
Cdd:cd14950 230 -DARG---NIAAAFNTEAMPRGYID 250
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
66-346 |
3.67e-37 |
|
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: 136.92 E-value: 3.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 66 KRACQKAIEKLQAGALATDAVAAALVELEDSPF-TNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAH 144
Cdd:cd04513 9 TEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCdGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 145 RLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKRKLELAERVETD---FIQLKRRRQ 221
Cdd:cd04513 89 AVM----------EHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDpskSCSSPKAPS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 222 SSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT-GAqnpystAVSTsGCGEhlvrt 300
Cdd:cd04513 159 RSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEvGA------AAAT-GDGD----- 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 30424856 301 ILARECShalqaedAHQAlLETMQNKFisSPFLACEDGVL-----------GGVIVL 346
Cdd:cd04513 227 IMMRFLP-------SYQA-VELMRQGM--SPQEACEDAIRriakkypkdfeGAVVAV 273
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
44-346 |
5.62e-35 |
|
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: 129.69 E-value: 5.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 44 VLVHAGAGyhsesKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEDSPFTNAGIGSNLNLLGEIECDASIMDGK 123
Cdd:cd04703 3 VLVHGGAG-----SDPERQDGLERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAVMTSG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 124 SlNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIPscppstmttrfslaafkrnkrkl 203
Cdd:cd04703 78 G-AFGAVAAIEGVKNPVLVARAVMETS----------PHVLLAGDGAVRFARRLGYP----------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 204 elaervetdfiqlkrrrqssakendsGTLDTVGAVVVDHeGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGaqnp 283
Cdd:cd04703 124 --------------------------DGCDTVGAVARDG-GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKG---- 172
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30424856 284 ystAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFisspflacEDGVLGGVIVL 346
Cdd:cd04703 173 ---AVAATGIGEEIAKRLLARRVYRWIETGLSLQAAAQRAIDEF--------DDGVAVGVIAV 224
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
44-303 |
1.37e-33 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 127.76 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 44 VLVHAGAGYHSESK-----AKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEDSPFTNAGIGSNLNLLGEIECDAS 118
Cdd:PRK10226 6 IAIHGGAGAISRAQmslqqELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDAC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 119 IMDGKSLNFGAVGALSGIKNPVsVAHRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTrfslaafkr 198
Cdd:PRK10226 86 VMDGNTLKAGAVAGVSHLRNPV-LAARLVME---------QSPHVMMIGEGAENFAFAHGMERVSPEIFST--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 199 NKRKLELAERVETDFIQLKrrrQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT 278
Cdd:PRK10226 147 PLRYEQLLAARAEGATVLD---HSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNA 223
|
250 260
....*....|....*....|....*
gi 30424856 279 gaqnpySTAVSTSGCGEHLVRTILA 303
Cdd:PRK10226 224 ------SVAVSCTGTGEVFIRALAA 242
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
44-303 |
3.70e-25 |
|
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: 103.84 E-value: 3.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 44 VLVHAGAGyhSESKAK-EYKHVCKRACQKAIEK----LQAGALATDAVAAALVeLEDSPFTNAGIGSNLNLLGEIECDAS 118
Cdd:cd14949 3 LIIHGGFG--SESSTNgETKAAKQEALAEIVEEvyeyLKSHSALEAVVYAVSL-LEDDPLFNAGTGSQIQSDGQIRMSAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 119 IMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKgklsagrippcFLVGEGAYRWAVDHGIPSCPPstmttrfslaafkr 198
Cdd:cd14949 80 LMDGQTQRFSGVINIENVKNPIEVAQKLQQEDDR-----------VLSGEGATEFARENGFPEYNP-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30424856 199 nkrklelaervETDFiqlkRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAAlygcgcwaenT 278
Cdd:cd14949 135 -----------ETPQ----RRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSA----------T 189
|
250 260
....*....|....*....|....*...
gi 30424856 279 GAQNpYST---AVSTSGCGEHLVRTILA 303
Cdd:cd14949 190 VAGN-YANafaGVSCTGIGEDIVSEALA 216
|
|
| |
