|
Name |
Accession |
Description |
Interval |
E-value |
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
19-308 |
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: 532.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 19 SLVVVVHGGgASNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASI 98
Cdd:cd04702 1 KPVIVVHGG-AGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 99 MDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIPQVPVEKLITERTKKHLEKEKLEKGAQNAD 178
Cdd:cd04702 80 MDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEKGANVED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 179 CPKNSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLALFHVEQG 258
Cdd:cd04702 160 TQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNLARLILFHMEQG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 31560239 259 KTVEEAAQLALDYMKSKLKGLGGLILVNKTGDWVAKWTSASMPWAAVKNG 308
Cdd:cd04702 240 KTAEEAAELALAYMKSRVKGLGGLIVVSKTGDWGAKFTSKRMAWAAVKDG 289
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
21-310 |
1.23e-130 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 374.61 E-value: 1.23e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 21 VVVVHGG-GASNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASIM 99
Cdd:pfam01112 1 VLVIHGGaGSILRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 100 DGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIPQVPVEKLITERTKKHLEKEKLEKGAQN--- 176
Cdd:pfam01112 81 DGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKENFQPNmal 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 177 --ADCPKNS------GTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLA 248
Cdd:pfam01112 161 nvAPDPLKEcgdskrGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31560239 249 RLALFHVEQGKTVEEAAQLALDYMKSKLKGLGGLILVNKTGDWVAKWTSASMPWAAVKNGKL 310
Cdd:pfam01112 241 YDIVARMEYGLSLEEAADKVITEMLKRVGGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGI 302
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
21-309 |
6.92e-122 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 352.10 E-value: 6.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 21 VVVVHGG----GASNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDA 96
Cdd:COG1446 7 ALIIHGGagtiARSAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 97 SIMDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIPQVPVEKLITERTKKHLEKEKLEKGAQN 176
Cdd:COG1446 87 SIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYKPIIN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 177 adcPKNSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLALFHVE 256
Cdd:COG1446 167 ---ERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRTVVAHDIVERMR 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 31560239 257 QGKTVEEAAQLALDYMKSKLKGLGGLILVNKTGDWVAKWTSASMPWAAVKNGK 309
Cdd:COG1446 244 QGLSLQEAAEEVIERILKKLGGDGGLIAVDKDGNIAAPFNTEGMYRAYIDGDG 296
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
22-314 |
4.49e-78 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 241.15 E-value: 4.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 22 VVVHGGG---ASNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASI 98
Cdd:PLN02689 6 IALHGGAgdiDPNLPRERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEASI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 99 MDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIPQVPVEKLITERTKKHLEKEK--------- 169
Cdd:PLN02689 86 MDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAKeansvqfdy 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 170 -------LEKGAQNADCPKNSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYAdNNLGAVSTTGHGESI 242
Cdd:PLN02689 166 ripldkpAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYA-NHLCAVSATGKGEAI 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31560239 243 LKVNLAR-LALFHVEQGKTVEEAAQLALDymKSKLKGLGGLILVNKTGDWVAKWTSASMPWA-AVKNGKLQAGI 314
Cdd:PLN02689 245 IRGTVARdVAAVMEYKGLPLQEAVDYVIK--ERLPEGPAGLIAVSATGEVAMAFNTTGMFRAcATEDGFMEVGI 316
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
19-308 |
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: 532.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 19 SLVVVVHGGgASNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASI 98
Cdd:cd04702 1 KPVIVVHGG-AGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 99 MDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIPQVPVEKLITERTKKHLEKEKLEKGAQNAD 178
Cdd:cd04702 80 MDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEKGANVED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 179 CPKNSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLALFHVEQG 258
Cdd:cd04702 160 TQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNLARLILFHMEQG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 31560239 259 KTVEEAAQLALDYMKSKLKGLGGLILVNKTGDWVAKWTSASMPWAAVKNG 308
Cdd:cd04702 240 KTAEEAAELALAYMKSRVKGLGGLIVVSKTGDWGAKFTSKRMAWAAVKDG 289
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
21-310 |
1.23e-130 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 374.61 E-value: 1.23e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 21 VVVVHGG-GASNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASIM 99
Cdd:pfam01112 1 VLVIHGGaGSILRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 100 DGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIPQVPVEKLITERTKKHLEKEKLEKGAQN--- 176
Cdd:pfam01112 81 DGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKENFQPNmal 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 177 --ADCPKNS------GTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLA 248
Cdd:pfam01112 161 nvAPDPLKEcgdskrGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31560239 249 RLALFHVEQGKTVEEAAQLALDYMKSKLKGLGGLILVNKTGDWVAKWTSASMPWAAVKNGKL 310
Cdd:pfam01112 241 YDIVARMEYGLSLEEAADKVITEMLKRVGGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGI 302
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
21-309 |
6.92e-122 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 352.10 E-value: 6.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 21 VVVVHGG----GASNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDA 96
Cdd:COG1446 7 ALIIHGGagtiARSAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 97 SIMDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIPQVPVEKLITERTKKHLEKEKLEKGAQN 176
Cdd:COG1446 87 SIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYKPIIN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 177 adcPKNSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLALFHVE 256
Cdd:COG1446 167 ---ERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRTVVAHDIVERMR 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 31560239 257 QGKTVEEAAQLALDYMKSKLKGLGGLILVNKTGDWVAKWTSASMPWAAVKNGK 309
Cdd:COG1446 244 QGLSLQEAAEEVIERILKKLGGDGGLIAVDKDGNIAAPFNTEGMYRAYIDGDG 296
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
21-303 |
2.92e-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: 348.40 E-value: 2.92e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 21 VVVVHGGgASNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASIMD 100
Cdd:cd04512 1 SLIVHGG-AGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIMD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 101 GKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGipqvpveklitertkkhlekeklekgaqnadcp 180
Cdd:cd04512 80 GKTLNAGAVAGVKGVKNPISLARAVMEKTPHVLLVGEGAERFAREHG--------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 181 knSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLALFHVEQGKT 260
Cdd:cd04512 127 --HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLVEFGGS 204
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 31560239 261 VEEAAQLALDYMKSKLKGLGGLILVNKTGDWVAKWTSASMPWA 303
Cdd:cd04512 205 AQEAAEAAIDYLRRRVGGEGGLIVVDPDGRLGAAHNTPGMAFA 247
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
21-300 |
5.51e-93 |
|
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: 277.03 E-value: 5.51e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 21 VVVVHGGgASNIS-----ANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMD 95
Cdd:cd04701 1 ALAIHGG-AGTISranltPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 96 ASIMDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIPQVPVeklitertkkhlekeklekgaq 175
Cdd:cd04701 80 ASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELVPQ---------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 176 nadcpknsGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLALFHV 255
Cdd:cd04701 138 --------GTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWAVAVSGTGNGDSFIRVAAARDVAARM 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 31560239 256 E-QGKTVEEAAQLALDYMKSKLKGLGGLILVNKTGDWVAKWTSASM 300
Cdd:cd04701 210 RyKGLSLAEAAKEVVGPGGELGEGEGGIIAIDARGNVAMPFNCGGM 255
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
22-314 |
4.49e-78 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 241.15 E-value: 4.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 22 VVVHGGG---ASNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASI 98
Cdd:PLN02689 6 IALHGGAgdiDPNLPRERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEASI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 99 MDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIPQVPVEKLITERTKKHLEKEK--------- 169
Cdd:PLN02689 86 MDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAKeansvqfdy 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 170 -------LEKGAQNADCPKNSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYAdNNLGAVSTTGHGESI 242
Cdd:PLN02689 166 ripldkpAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYA-NHLCAVSATGKGEAI 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31560239 243 LKVNLAR-LALFHVEQGKTVEEAAQLALDymKSKLKGLGGLILVNKTGDWVAKWTSASMPWA-AVKNGKLQAGI 314
Cdd:PLN02689 245 IRGTVARdVAAVMEYKGLPLQEAVDYVIK--ERLPEGPAGLIAVSATGEVAMAFNTTGMFRAcATEDGFMEVGI 316
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
21-307 |
8.88e-77 |
|
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: 235.55 E-value: 8.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 21 VVVVHGGGASNISANRKELVREGIARAATEGYKILKaGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASIMD 100
Cdd:cd14950 1 ALVVHGGAGSWKNSDDEEKALRALREALERGYEALR-RGSALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDAGIMD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 101 GKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGipqvpveklitertkkhlekeklekgaqnadcp 180
Cdd:cd14950 80 GRTLRVGAVAAVRAVKNPIRLARKVMEKTDHVLIVGEGADELAKRLG--------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 181 knSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNlGAVSTTGHGESILKVNLARLALFHVEQGKT 260
Cdd:cd14950 127 --GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATNG-VAVSATGIGEVIIRSLPALRADELVSMGGD 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 31560239 261 VEEAAQLALDYMKSKL-KGLGGLILVNKTGDWVAKWTSASMPWAAVKN 307
Cdd:cd14950 204 IEEAVRAVVNKVTETFgKDTAGIIGIDARGNIAAAFNTEAMPRGYIDD 251
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
45-291 |
7.04e-68 |
|
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: 214.35 E-value: 7.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 45 ARAATE-GYKILKAGGSAVDAVEGAVTVLENDPE-FNAGYGSVLNVNGDIEMDASIMDGKDLSAGAVSAVRCIANPVKLA 122
Cdd:cd04513 8 FTEAVEaAWEVLQKGGSALDAVEAGCSVCEDDQCdGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 123 RLVMEKTPHCFLTGHGAEKFAEDMGipqVPVEKLITERTKKHLEKEKLEKGAQN------------------------AD 178
Cdd:cd04513 88 RAVMEHTPHSLLVGEGATEFAVSMG---FKEENLLTEESRKMWKKWLKENCQPNfwknvvpdpskscsspkapsrsesAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 179 CPKNSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLARLAlfhVE-- 256
Cdd:cd04513 165 PEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLPSYQA---VElm 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 31560239 257 -QGKTVEEAAQLALDYMKSKLKGL--GGLILVNKTGDW 291
Cdd:cd04513 242 rQGMSPQEACEDAIRRIAKKYPKDfeGAVVAVNKAGEY 279
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
21-304 |
2.92e-64 |
|
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: 203.26 E-value: 2.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 21 VVVVHGGGASNISAnrkelvREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASIMD 100
Cdd:cd04703 2 AVLVHGGAGSDPER------QDGLERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAVMT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 101 GKDlSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIpqvpveklitertkkhlekeklekgaqnadcP 180
Cdd:cd04703 76 SGG-AFGAVAAIEGVKNPVLVARAVMETSPHVLLAGDGAVRFARRLGY-------------------------------P 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 181 KNSGTVGAVALDcRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNlGAVSTTGHGESILKVNLARLALFHVEQGKT 260
Cdd:cd04703 124 DGCDTVGAVARD-GGKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPK-GAVAATGIGEEIAKRLLARRVYRWIETGLS 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 31560239 261 VEEAAQLALDYMksKLKGLGGLILVNKTGdWVAKWTSASMPWAA 304
Cdd:cd04703 202 LQAAAQRAIDEF--DDGVAVGVIAVSRRG-EAGIASNTAMAWAI 242
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
21-300 |
4.35e-58 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 189.77 E-value: 4.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 21 VVVVHGGGA----SNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDA 96
Cdd:PRK10226 5 VIAIHGGAGaisrAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 97 SIMDGKDLSAGAVSAVRCIANPVKLARLVMEKTPHCFLTGHGAEKFAEDMGIPQVPVEKLIT-ERTKKHLEKEK-----L 170
Cdd:PRK10226 85 CVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTpLRYEQLLAARAegatvL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 171 EKGAQNADCPKNSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLGAVSTTGHGESILKVNLA-R 249
Cdd:PRK10226 165 DHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAyD 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 31560239 250 LALFHVEQGKTVEEAAQLALDYMKSKLKGLGGLILVNKTGDWVAKWTSASM 300
Cdd:PRK10226 245 IAALMDYGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGM 295
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
22-303 |
4.00e-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: 180.88 E-value: 4.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 22 VVVHGGGASNISANR--KELVREGIARAATEGYKILKAGgSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASIM 99
Cdd:cd14949 3 LIIHGGFGSESSTNGetKAAKQEALAEIVEEVYEYLKSH-SALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQIRMSASLM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 100 DGKDLSAGAVSAVRCIANPVKLARLVMEKtPHCFLTGHGAEKFAEDMGIPqvPVEKLITERtkKHLEKEKLEKGAQnadc 179
Cdd:cd14949 82 DGQTQRFSGVINIENVKNPIEVAQKLQQE-DDRVLSGEGATEFARENGFP--EYNPETPQR--RQEYEEKKLKSGG---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 180 pknSGTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIgAGGYAdNNLGAVSTTGHGESILKVNLARLALFHVEQGK 259
Cdd:cd14949 153 ---TGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNYA-NAFAGVSCTGIGEDIVSEALAAKIVTRVTDGM 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 31560239 260 TVEEAAQLALDYMKSKlKGLGGLILVNKTGDWVAKWTSASMPWA 303
Cdd:cd14949 228 SLQEAFEKSFAEAKPR-DGFAGAIGIDSKGNIYHGDTHPVMVYA 270
|
|
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
22-249 |
1.67e-54 |
|
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: 180.16 E-value: 1.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 22 VVVHGGgASNISANRKELVREGIARAATEGYKILKAGGSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASIMDG 101
Cdd:cd04514 3 VAVHAG-AGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 102 KDLSAGAVSAVRCIANPVKLARLVMEK---------TPHCFLTGHGAEKFAEDMGIPQvpveklitertkkhlekeklek 172
Cdd:cd04514 82 SSGRFGAVGAVSGVKNPIQLARLLLKEqrkplslgrVPPMFLVGEGAREWAKSKGIIT---------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 173 gaqnaDcpknsgTVGAVALDCRGNLAYATSTGGIVNKMVGRVGDSPCIGAGGYADNNLG------AVSTTGHGESILKVN 246
Cdd:cd04514 140 -----D------TVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPddktsvAVVTSGTGEHIATTM 208
|
...
gi 31560239 247 LAR 249
Cdd:cd04514 209 LAR 211
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
22-249 |
1.77e-29 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 116.50 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 22 VVVHGGGASNISANRKELvREGIARAATEGYKILKAG-GSAVDAVEGAVTVLENDPEFNAGYGSVLNVNGDIEMDASIMD 100
Cdd:PLN02937 14 VAVHVGAGYHAPSNEKAL-RSAMRRACLAAAAILRQGsGGCIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASIMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 101 GKDLSAGAVSAVRCIANPVKLARLVME----------KTPHCFLTGHGAEKFAEDMGI--PQVPVEK---LITERTK--- 162
Cdd:PLN02937 93 GDSGAFGAVGAVPGVRNAIQIAALLAKeqmmgssllgRIPPMFLVGEGARQWAKSKGIdlPETVEEAekwLVTERAKeqw 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560239 163 ----------------------KHLEKEKLEKGAQNADCPKNSG------------TVGAVALDCRGNLAYATSTGGIVN 208
Cdd:PLN02937 173 kkyktmlasaiaksscdsqstsKLSELEAPRSNPSNGTGGGQSSmctasdedcimdTVGVICVDSEGNIASGASSGGIAM 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 31560239 209 KMVGRVGDSPCIGAGGYADNN--LGA-----VSTTGHGESILKVNLAR 249
Cdd:PLN02937 253 KVSGRVGLAAMYGSGCWASSKgpFGApfivgCCVSGAGEYLMRGFAAR 300
|
|
| |
