|
Name |
Accession |
Description |
Interval |
E-value |
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
2-291 |
0e+00 |
|
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: 530.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 2 NPIVVVHGGgAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASI 81
Cdd:cd04702 1 KPVIVVHGG-AGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 82 MDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTD 161
Cdd:cd04702 80 MDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEKGANVED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 162 CQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQG 241
Cdd:cd04702 160 TQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNLARLILFHMEQG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 145275200 242 KTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDG 291
Cdd:cd04702 240 KTAEEAAELALAYMKSRVKGLGGLIVVSKTGDWGAKFTSKRMAWAAVKDG 289
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
4-299 |
1.54e-128 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 368.45 E-value: 1.54e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 4 IVVVHGG-GAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIM 82
Cdd:pfam01112 1 VLVIHGGaGSILRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 83 DGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEK---------- 152
Cdd:pfam01112 81 DGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARkenfqpnmal 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 153 -HEKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLA 231
Cdd:pfam01112 161 nVAPDPLKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145275200 232 RLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDP 299
Cdd:pfam01112 241 YDIVARMEYGLSLEEAADKVITEMLKRVGGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGIGDVLIY 308
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
1-300 |
3.00e-117 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 339.78 E-value: 3.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 1 MNPIVVVHGGGAGPI-----SKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEV 75
Cdd:COG1446 3 MSRRALIIHGGAGTIarsamTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 76 EMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEK 155
Cdd:COG1446 83 ELDASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 156 GAQKtdcQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTL 235
Cdd:COG1446 163 PIIN---ERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRTVVAHDIV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145275200 236 FHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAK-DGKLHFGIDPD 300
Cdd:COG1446 240 ERMRQGLSLQEAAEEVIERILKKLGGDGGLIAVDKDGNIAAPFNTEGMYRAYIDgDGELVVAIYKD 305
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
5-299 |
5.98e-85 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 258.10 E-value: 5.98e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 5 VVVHGGgAGPISK----DRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDAS 80
Cdd:PLN02689 6 IALHGG-AGDIDPnlprERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 81 IMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKH------- 153
Cdd:PLN02689 85 IMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAKEansvqfd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 154 ---------EKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYAdNDIGAVSTTGHGES 224
Cdd:PLN02689 165 yripldkpaKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYA-NHLCAVSATGKGEA 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145275200 225 ILKVNLARLTLFHIE-QGKTVEEAADLSLgymKSRV-KGLGGLIVVSKTGDWVAKWTSTSMPWAAAK-DGKLHFGIDP 299
Cdd:PLN02689 244 IIRGTVARDVAAVMEyKGLPLQEAVDYVI---KERLpEGPAGLIAVSATGEVAMAFNTTGMFRACATeDGFMEVGIWP 318
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
2-291 |
0e+00 |
|
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: 530.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 2 NPIVVVHGGgAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASI 81
Cdd:cd04702 1 KPVIVVHGG-AGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 82 MDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTD 161
Cdd:cd04702 80 MDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEKGANVED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 162 CQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQG 241
Cdd:cd04702 160 TQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNLARLILFHMEQG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 145275200 242 KTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDG 291
Cdd:cd04702 240 KTAEEAAELALAYMKSRVKGLGGLIVVSKTGDWGAKFTSKRMAWAAVKDG 289
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
4-299 |
1.54e-128 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 368.45 E-value: 1.54e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 4 IVVVHGG-GAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIM 82
Cdd:pfam01112 1 VLVIHGGaGSILRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 83 DGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEK---------- 152
Cdd:pfam01112 81 DGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARkenfqpnmal 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 153 -HEKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLA 231
Cdd:pfam01112 161 nVAPDPLKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145275200 232 RLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDP 299
Cdd:pfam01112 241 YDIVARMEYGLSLEEAADKVITEMLKRVGGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGIGDVLIY 308
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
4-286 |
1.23e-121 |
|
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: 348.79 E-value: 1.23e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 4 IVVVHGGgAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMD 83
Cdd:cd04512 1 SLIVHGG-AGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIMD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 84 GKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGvpeipgeklvternkkrlekekhekgaqktdcq 163
Cdd:cd04512 80 GKTLNAGAVAGVKGVKNPISLARAVMEKTPHVLLVGEGAERFAREHG--------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 164 knLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQGKT 243
Cdd:cd04512 127 --HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLVEFGGS 204
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 145275200 244 VEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWA 286
Cdd:cd04512 205 AQEAAEAAIDYLRRRVGGEGGLIVVDPDGRLGAAHNTPGMAFA 247
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
1-300 |
3.00e-117 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 339.78 E-value: 3.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 1 MNPIVVVHGGGAGPI-----SKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEV 75
Cdd:COG1446 3 MSRRALIIHGGAGTIarsamTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 76 EMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEK 155
Cdd:COG1446 83 ELDASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 156 GAQKtdcQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTL 235
Cdd:COG1446 163 PIIN---ERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRTVVAHDIV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145275200 236 FHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAK-DGKLHFGIDPD 300
Cdd:COG1446 240 ERMRQGLSLQEAAEEVIERILKKLGGDGGLIAVDKDGNIAAPFNTEGMYRAYIDgDGELVVAIYKD 305
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
5-283 |
1.12e-87 |
|
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: 263.17 E-value: 1.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 5 VVVHGGgAGPISK-----DRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDA 79
Cdd:cd04701 2 LAIHGG-AGTISRanltpERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 80 SIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPgeklvternkkrlekekhekgaqk 159
Cdd:cd04701 81 SIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELVP------------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 160 tdcqknLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIE 239
Cdd:cd04701 137 ------QGTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWAVAVSGTGNGDSFIRVAAARDVAARMR 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 145275200 240 -QGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSM 283
Cdd:cd04701 211 yKGLSLAEAAKEVVGPGGELGEGEGGIIAIDARGNVAMPFNCGGM 255
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
5-299 |
5.98e-85 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 258.10 E-value: 5.98e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 5 VVVHGGgAGPISK----DRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDAS 80
Cdd:PLN02689 6 IALHGG-AGDIDPnlprERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 81 IMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKH------- 153
Cdd:PLN02689 85 IMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAKEansvqfd 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 154 ---------EKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYAdNDIGAVSTTGHGES 224
Cdd:PLN02689 165 yripldkpaKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYA-NHLCAVSATGKGEA 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145275200 225 ILKVNLARLTLFHIE-QGKTVEEAADLSLgymKSRV-KGLGGLIVVSKTGDWVAKWTSTSMPWAAAK-DGKLHFGIDP 299
Cdd:PLN02689 244 IIRGTVARDVAAVMEyKGLPLQEAVDYVI---KERLpEGPAGLIAVSATGEVAMAFNTTGMFRACATeDGFMEVGIWP 318
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
4-290 |
8.00e-73 |
|
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: 224.77 E-value: 8.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 4 IVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGgSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMD 83
Cdd:cd14950 1 ALVVHGGAGSWKNSDDEEKALRALREALERGYEALRRG-SALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDAGIMD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 84 GKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAamgvpeipgeklvternkkrlekekhekgaqktdcQ 163
Cdd:cd14950 80 GRTLRVGAVAAVRAVKNPIRLARKVMEKTDHVLIVGEGADELAK-----------------------------------R 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 164 KNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDiGAVSTTGHGESILKVNLARLTLFHIEQGKT 243
Cdd:cd14950 125 LGGDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATNG-VAVSATGIGEVIIRSLPALRADELVSMGGD 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 145275200 244 VEEAADLSLGYMKSRV-KGLGGLIVVSKTGDWVAKWTSTSMPWAAAKD 290
Cdd:cd14950 204 IEEAVRAVVNKVTETFgKDTAGIIGIDARGNIAAAFNTEAMPRGYIDD 251
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
34-274 |
4.00e-64 |
|
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: 203.95 E-value: 4.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 34 GYGILREGGSAVDAVEGAVVALEDDPE-FNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKT 112
Cdd:cd04513 15 AWEVLQKGGSALDAVEAGCSVCEDDQCdGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVARAVMEHT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 113 PHCFLTDQGAAQFAAAMGVPEipgEKLVTERNKKRLEKEKhekgaqKTDCQKNL-------------------------- 166
Cdd:cd04513 95 PHSLLVGEGATEFAVSMGFKE---ENLLTEESRKMWKKWL------KENCQPNFwknvvpdpskscsspkapsrsesaip 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 167 ----GTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQGK 242
Cdd:cd04513 166 ednhDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLPSYQAVELMRQGM 245
|
250 260 270
....*....|....*....|....*....|....
gi 145275200 243 TVEEAADLSLGYMKSRVKGL--GGLIVVSKTGDW 274
Cdd:cd04513 246 SPQEACEDAIRRIAKKYPKDfeGAVVAVNKAGEY 279
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
3-288 |
1.65e-60 |
|
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: 192.86 E-value: 1.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 3 PIVVVHGGGAGPISKDRkervhqGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIM 82
Cdd:cd04703 1 MAVLVHGGAGSDPERQD------GLERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAVM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 83 DGKDlSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPeipgeklvternkkrlekekhekgaqkTDC 162
Cdd:cd04703 75 TSGG-AFGAVAAIEGVKNPVLVARAVMETSPHVLLAGDGAVRFARRLGYP---------------------------DGC 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 163 qknlGTVGAVALDcKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDiGAVSTTGHGESILKVNLARLTLFHIEQGK 242
Cdd:cd04703 127 ----DTVGAVARD-GGKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPK-GAVAATGIGEEIAKRLLARRVYRWIETGL 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 145275200 243 TVEEAADLSLGYMKSRVkgLGGLIVVSKTGdWVAKWTSTSMPWAAA 288
Cdd:cd04703 201 SLQAAAQRAIDEFDDGV--AVGVIAVSRRG-EAGIASNTAMAWAIA 243
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
1-290 |
3.40e-55 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 181.69 E-value: 3.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 1 MNPIVVVHGGGAGPISK-----DRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEV 75
Cdd:PRK10226 1 MGKAVIAIHGGAGAISRaqmslQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 76 EMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVT-ERNKKRLEKEKH- 153
Cdd:PRK10226 81 ELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTpLRYEQLLAARAEg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 154 ----EKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVn 229
Cdd:PRK10226 161 atvlDHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRA- 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145275200 230 larLTLFHIeqgKTVEEAADLSLGYMKSRV--------KGLGGLIVVSKTGDWVAKWTSTSM--PWAAAKD 290
Cdd:PRK10226 240 ---LAAYDI---AALMDYGGLSLAEACERVvmeklpalGGSGGLIAIDHEGNVALPFNTEGMyrAWGYAGD 304
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
3-295 |
5.61e-55 |
|
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: 180.11 E-value: 5.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 3 PIVVVHGGgAGPISKDRKE--RVHQG-MVRAATVGYGILREGgSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDA 79
Cdd:cd14949 1 PKLIIHGG-FGSESSTNGEtkAAKQEaLAEIVEEVYEYLKSH-SALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQIRMSA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 80 SIMDGKDLSAGAVSAVQCIANPIKLARLVMEKtPHCFLTDQGAAQFAAAMGVPEIpgEKLVTERnkKRLEKEKHEKGAQK 159
Cdd:cd14949 79 SLMDGQTQRFSGVINIENVKNPIEVAQKLQQE-DDRVLSGEGATEFARENGFPEY--NPETPQR--RQEYEEKKLKSGGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 160 tdcqknlGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLgAGGYAdNDIGAVSTTGHGESILKVNLARLTLFHIE 239
Cdd:cd14949 154 -------GTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNYA-NAFAGVSCTGIGEDIVSEALAAKIVTRVT 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 145275200 240 QGKTVEEAADLSLGYMKSRvKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHF 295
Cdd:cd14949 225 DGMSLQEAFEKSFAEAKPR-DGFAGAIGIDSKGNIYHGDTHPVMVYASYDGEKIGV 279
|
|
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
3-232 |
5.95e-52 |
|
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: 173.23 E-value: 5.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 3 PIVVVHGGgAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIM 82
Cdd:cd04514 1 FFVAVHAG-AGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 83 DGKDLSAGAVSAVQCIANPIKLARLVMEK---------TPHCFLTDQGAAQFAAAMGVPeipgeklvternkkrlekekh 153
Cdd:cd04514 80 DGSSGRFGAVGAVSGVKNPIQLARLLLKEqrkplslgrVPPMFLVGEGAREWAKSKGII--------------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 154 ekgaqkTDcqknlgTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYA---DNDIG---AVSTTGHGESILK 227
Cdd:cd04514 139 ------TD------TVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAeprDPDDKtsvAVVTSGTGEHIAT 206
|
....*
gi 145275200 228 VNLAR 232
Cdd:cd04514 207 TMLAR 211
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
5-232 |
1.72e-32 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 124.21 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 5 VVVHGGgAGPISKDRKERVHQGMVRAATVGYGILREG-GSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMD 83
Cdd:PLN02937 14 VAVHVG-AGYHAPSNEKALRSAMRRACLAAAAILRQGsGGCIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASIMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 84 GKDLSAGAVSAVQCIANPIKLARLVME----------KTPHCFLTDQGAAQFAAAMGV--PEIPGEK---LVTERNKKR- 147
Cdd:PLN02937 93 GDSGAFGAVGAVPGVRNAIQIAALLAKeqmmgssllgRIPPMFLVGEGARQWAKSKGIdlPETVEEAekwLVTERAKEQw 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275200 148 --------------------------LEKEKHEK-----GAQKTDCQKN-----LGTVGAVALDCKGNVAYATSTGGIVN 191
Cdd:PLN02937 173 kkyktmlasaiaksscdsqstsklseLEAPRSNPsngtgGGQSSMCTASdedciMDTVGVICVDSEGNIASGASSGGIAM 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 145275200 192 KMVGRVGDSPCLGAGGYADND-------IGAVSTTGHGESILKVNLAR 232
Cdd:PLN02937 253 KVSGRVGLAAMYGSGCWASSKgpfgapfIVGCCVSGAGEYLMRGFAAR 300
|
|
|