|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
1-325 |
0e+00 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 586.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 1 MGGWAIAVHGGAG-IDPNLPAERQEEAKQLLTRCLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTVE 79
Cdd:PLN02689 1 MGGWAIALHGGAGdIDPNLPRERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 80 MEASIMDGTKRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGVEIVDNEYFVTDDNVGMLKLAKEANS 159
Cdd:PLN02689 81 MEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAKEANS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 160 ILFDYRIPPMGCAGAAATDSPIQMNglpisiyaPETVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYASEF 239
Cdd:PLN02689 161 VQFDYRIPLDKPAKAAALAADGDAQ--------PETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYANHL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 240 CGVSCTGEGEAIIRATLARDVSAVMEYKGLNLQEAVDYVIKHRLDEGFAGLIAVSNKGEVVCGFNSNGMFRGCATEDGFM 319
Cdd:PLN02689 233 CAVSATGKGEAIIRGTVARDVAAVMEYKGLPLQEAVDYVIKERLPEGPAGLIAVSATGEVAMAFNTTGMFRACATEDGFM 312
|
....*.
gi 18401029 320 EVAIWE 325
Cdd:PLN02689 313 EVGIWP 318
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
5-317 |
2.66e-126 |
|
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: 361.78 E-value: 2.66e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 5 AIAVHGGAGIDP--NLPAERQEEAKQLLTRCLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTVEMEA 82
Cdd:cd04701 1 ALAIHGGAGTISraNLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 83 SIMDGTKRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGVEIVdneyfvtddnvgmlklakeansilf 162
Cdd:cd04701 81 SIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELV------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 163 dyripPMGcagaaatdspiqmnglpisiyapeTVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYASEF-CG 241
Cdd:cd04701 136 -----PQG------------------------TVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWaVA 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18401029 242 VSCTGEGEAIIRATLARDVSAVMEYKGLNLQEAVDYVIKHRLD--EGFAGLIAVSNKGEVVCGFNSNGMFRGCATEDG 317
Cdd:cd04701 187 VSGTGNGDSFIRVAAARDVAARMRYKGLSLAEAAKEVVGPGGElgEGEGGIIAIDARGNVAMPFNCGGMYRAWIDEDG 264
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
5-324 |
5.92e-119 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 344.95 E-value: 5.92e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 5 AIAVHGGAGIDPNlPAERQEEAKQLLTRCLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTVEMEASI 84
Cdd:pfam01112 1 VLVIHGGAGSILR-TKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 85 MDGTKRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGVEIVDNEYFVTDDNVGMLKLAKEAN---SIL 161
Cdd:pfam01112 80 MDGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKENfqpNMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 162 FDYRIPPMGCAGAAATDspiqmnglpisiyapeTVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYA-SEFC 240
Cdd:pfam01112 160 LNVAPDPLKECGDSKRG----------------TVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYAdNATG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 241 GVSCTGEGEAIIRATLARDVSAVMEYkGLNLQEAVDYVIKHRLDE--GFAGLIAVSNKGEVVCGFNSNGMFRGCATEDGF 318
Cdd:pfam01112 224 AVSATGHGEDIIRETLAYDIVARMEY-GLSLEEAADKVITEMLKRvgGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGI 302
|
....*.
gi 18401029 319 MEVAIW 324
Cdd:pfam01112 303 GDVLIY 308
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
1-325 |
9.11e-116 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 336.69 E-value: 9.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 1 MGGWAIAVHGGAG--IDPNLPAERQEEAKQLLTRCLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTV 78
Cdd:COG1446 3 MSRRALIIHGGAGtiARSAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 79 EMEASIMDGTKRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGVEIVDNEYFVTDDNVGMLKLAKEAN 158
Cdd:COG1446 83 ELDASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 159 SILFDYRippMGcagaaatdspiqmnglpisiyapeTVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYAS- 237
Cdd:COG1446 163 PIINERK---HG------------------------TVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADn 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 238 EFCGVSCTGEGEAIIRATLARDVSAVMEyKGLNLQEAVDYVIKHRLDE--GFAGLIAVSNKGEVVCGFNSNGMFRGCATE 315
Cdd:COG1446 216 EVGAVSATGHGEYFIRTVVAHDIVERMR-QGLSLQEAAEEVIERILKKlgGDGGLIAVDKDGNIAAPFNTEGMYRAYIDG 294
|
330
....*....|
gi 18401029 316 DGFMEVAIWE 325
Cdd:COG1446 295 DGELVVAIYK 304
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
1-325 |
0e+00 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 586.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 1 MGGWAIAVHGGAG-IDPNLPAERQEEAKQLLTRCLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTVE 79
Cdd:PLN02689 1 MGGWAIALHGGAGdIDPNLPRERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 80 MEASIMDGTKRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGVEIVDNEYFVTDDNVGMLKLAKEANS 159
Cdd:PLN02689 81 MEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAKEANS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 160 ILFDYRIPPMGCAGAAATDSPIQMNglpisiyaPETVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYASEF 239
Cdd:PLN02689 161 VQFDYRIPLDKPAKAAALAADGDAQ--------PETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYANHL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 240 CGVSCTGEGEAIIRATLARDVSAVMEYKGLNLQEAVDYVIKHRLDEGFAGLIAVSNKGEVVCGFNSNGMFRGCATEDGFM 319
Cdd:PLN02689 233 CAVSATGKGEAIIRGTVARDVAAVMEYKGLPLQEAVDYVIKERLPEGPAGLIAVSATGEVAMAFNTTGMFRACATEDGFM 312
|
....*.
gi 18401029 320 EVAIWE 325
Cdd:PLN02689 313 EVGIWP 318
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
5-317 |
2.66e-126 |
|
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: 361.78 E-value: 2.66e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 5 AIAVHGGAGIDP--NLPAERQEEAKQLLTRCLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTVEMEA 82
Cdd:cd04701 1 ALAIHGGAGTISraNLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 83 SIMDGTKRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGVEIVdneyfvtddnvgmlklakeansilf 162
Cdd:cd04701 81 SIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELV------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 163 dyripPMGcagaaatdspiqmnglpisiyapeTVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYASEF-CG 241
Cdd:cd04701 136 -----PQG------------------------TVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWaVA 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18401029 242 VSCTGEGEAIIRATLARDVSAVMEYKGLNLQEAVDYVIKHRLD--EGFAGLIAVSNKGEVVCGFNSNGMFRGCATEDG 317
Cdd:cd04701 187 VSGTGNGDSFIRVAAARDVAARMRYKGLSLAEAAKEVVGPGGElgEGEGGIIAIDARGNVAMPFNCGGMYRAWIDEDG 264
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
5-324 |
5.92e-119 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 344.95 E-value: 5.92e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 5 AIAVHGGAGIDPNlPAERQEEAKQLLTRCLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTVEMEASI 84
Cdd:pfam01112 1 VLVIHGGAGSILR-TKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 85 MDGTKRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGVEIVDNEYFVTDDNVGMLKLAKEAN---SIL 161
Cdd:pfam01112 80 MDGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKENfqpNMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 162 FDYRIPPMGCAGAAATDspiqmnglpisiyapeTVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYA-SEFC 240
Cdd:pfam01112 160 LNVAPDPLKECGDSKRG----------------TVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYAdNATG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 241 GVSCTGEGEAIIRATLARDVSAVMEYkGLNLQEAVDYVIKHRLDE--GFAGLIAVSNKGEVVCGFNSNGMFRGCATEDGF 318
Cdd:pfam01112 224 AVSATGHGEDIIRETLAYDIVARMEY-GLSLEEAADKVITEMLKRvgGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGI 302
|
....*.
gi 18401029 319 MEVAIW 324
Cdd:pfam01112 303 GDVLIY 308
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
1-325 |
9.11e-116 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 336.69 E-value: 9.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 1 MGGWAIAVHGGAG--IDPNLPAERQEEAKQLLTRCLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTV 78
Cdd:COG1446 3 MSRRALIIHGGAGtiARSAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 79 EMEASIMDGTKRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGVEIVDNEYFVTDDNVGMLKLAKEAN 158
Cdd:COG1446 83 ELDASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 159 SILFDYRippMGcagaaatdspiqmnglpisiyapeTVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYAS- 237
Cdd:COG1446 163 PIINERK---HG------------------------TVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADn 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 238 EFCGVSCTGEGEAIIRATLARDVSAVMEyKGLNLQEAVDYVIKHRLDE--GFAGLIAVSNKGEVVCGFNSNGMFRGCATE 315
Cdd:COG1446 216 EVGAVSATGHGEYFIRTVVAHDIVERMR-QGLSLQEAAEEVIERILKKlgGDGGLIAVDKDGNIAAPFNTEGMYRAYIDG 294
|
330
....*....|
gi 18401029 316 DGFMEVAIWE 325
Cdd:COG1446 295 DGELVVAIYK 304
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
5-311 |
3.38e-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: 259.42 E-value: 3.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 5 AIAVHGGAGIDPNLPAERQEEAkqlLTRCLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTVEMEASI 84
Cdd:cd04512 1 SLIVHGGAGTIEDEDAEAYREG---LLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 85 MDGTKRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGveivdneyfvtddnvgmlklakeansilfdy 164
Cdd:cd04512 78 MDGKTLNAGAVAGVKGVKNPISLARAVMEKTPHVLLVGEGAERFAREHG------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 165 rippmgcagaaatdspiqmnglpisiyaPETVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYA-SEFCGVS 243
Cdd:cd04512 127 ----------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYAdNETGAVS 178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 244 CTGEGEAIIRATLARDVSAVMEYkGLNLQEAVDYVIKH--RLDEGFAGLIAVSNKGEVVCGFNSNGMFRG 311
Cdd:cd04512 179 ATGHGESIIRTVLAKRIADLVEF-GGSAQEAAEAAIDYlrRRVGGEGGLIVVDPDGRLGAAHNTPGMAFA 247
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
4-308 |
2.83e-85 |
|
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: 258.27 E-value: 2.83e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 4 WAIAVHGGAGidpNLPAERQEEAKQLLTRCLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTVEMEAS 83
Cdd:cd04702 2 PVIVVHGGAG---SIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 84 IMDGTKRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGVEIVDNEYFVTDDNVGMLKLAKEANSILFD 163
Cdd:cd04702 79 IMDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEKGANVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 164 YRIPPMGcagaaatdspiqmnglpisiyapeTVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYA-SEFCGV 242
Cdd:cd04702 159 DTQRGHG------------------------TVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYAdNLVGAV 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18401029 243 SCTGEGEAIIRATLARDVSAVMEYkGLNLQEAVDYVIKH---RLDeGFAGLIAVSNKGEVVCGFNSNGM 308
Cdd:cd04702 215 STTGHGESIMKVNLARLILFHMEQ-GKTAEEAAELALAYmksRVK-GLGGLIVVSKTGDWGAKFTSKRM 281
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
1-310 |
6.46e-74 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 230.22 E-value: 6.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 1 MGGWAIAVHGGAG--IDPNLPAERQEEAKQLLTRCLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTV 78
Cdd:PRK10226 1 MGKAVIAIHGGAGaiSRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 79 EMEASIMDGTKRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGVEIVDNEYFVTDDNVGMLKLAKEAN 158
Cdd:PRK10226 81 ELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAARAEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 159 SILFDYRIPPMgcagaaatDSPIQMNglpisiyapeTVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYASE 238
Cdd:PRK10226 161 ATVLDHSGAPL--------DEKQKMG----------TVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANN 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18401029 239 F-CGVSCTGEGEAIIRATLARDVSAVMEYKGLNLQEAVDYVIKHRLDE--GFAGLIAVSNKGEVVCGFNSNGMFR 310
Cdd:PRK10226 223 AsVAVSCTGTGEVFIRALAAYDIAALMDYGGLSLAEACERVVMEKLPAlgGSGGLIAIDHEGNVALPFNTEGMYR 297
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
5-315 |
2.10e-68 |
|
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: 213.98 E-value: 2.10e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 5 AIAVHGGAGIDPNlpAERQEEAKQLLTRCLNLGIIALRSNvSAIDVVELVIRELETDPLFNSGRGSALTEKGTVEMEASI 84
Cdd:cd14950 1 ALVVHGGAGSWKN--SDDEEKALRALREALERGYEALRRG-SALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 85 MDGTKRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGveivdneyfvtddnvgmlklakeansilFDy 164
Cdd:cd14950 78 MDGRTLRVGAVAAVRAVKNPIRLARKVMEKTDHVLIVGEGADELAKRLG----------------------------GD- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 165 rippmgcagaaatdspiqmnglpisiyapeTVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYASEFCGVSC 244
Cdd:cd14950 129 ------------------------------TVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATNGVAVSA 178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18401029 245 TGEGEAIIRATLARDVSAVMEyKGLNLQEAVDYVIKH---RLDEGFAGLIAVSNKGEVVCGFNSNGMFRGCATE 315
Cdd:cd14950 179 TGIGEVIIRSLPALRADELVS-MGGDIEEAVRAVVNKvteTFGKDTAGIIGIDARGNIAAAFNTEAMPRGYIDD 251
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
5-307 |
4.16e-53 |
|
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: 174.37 E-value: 4.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 5 AIAVHGGAGIDPnlpaERQEEAKQLLTRCLNlgiiALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTVEMEASI 84
Cdd:cd04703 2 AVLVHGGAGSDP----ERQDGLERAAEAGLA----ELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 85 MDGTkRRCGAVSGITTVKNPISLARLVMDKSPHSYLAFSGAEDFARKQGVeivdneyfvtddnvgmlklakeansilfdy 164
Cdd:cd04703 74 MTSG-GAFGAVAAIEGVKNPVLVARAVMETSPHVLLAGDGAVRFARRLGY------------------------------ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 165 ripPMGCagaaatdspiqmnglpisiyapETVGCVVVDGkGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYASEFCGVSC 244
Cdd:cd04703 123 ---PDGC----------------------DTVGAVARDG-GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKGAVAA 176
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18401029 245 TGEGEAIIRATLARDVSAVMEyKGLNLQEAVDYVIKHRLDEGFAGLIAVSNKGEvvCGFNSNG 307
Cdd:cd04703 177 TGIGEEIAKRLLARRVYRWIE-TGLSLQAAAQRAIDEFDDGVAVGVIAVSRRGE--AGIASNT 236
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
6-318 |
5.23e-53 |
|
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: 175.49 E-value: 5.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 6 IAVHGGAGidpnlpAERQEEAKQLLTRCLNLGIIALRS-----NVSAIDVVELVIRELETDPLFNSGRGSALTEKGTVEM 80
Cdd:cd14949 3 LIIHGGFG------SESSTNGETKAAKQEALAEIVEEVyeylkSHSALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQIRM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 81 EASIMDGTKRRCGAVSGITTVKNPISLARLVMDkSPHSYLAFSGAEDFARKQGVEIVDN-------EYfvtddnvgMLKL 153
Cdd:cd14949 77 SASLMDGQTQRFSGVINIENVKNPIEVAQKLQQ-EDDRVLSGEGATEFARENGFPEYNPetpqrrqEY--------EEKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 154 AKEANsilfdyrippMGcagaaatdspiqmnglpisiyapeTVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIgAG 233
Cdd:cd14949 148 LKSGG----------TG------------------------TVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 234 TYASEFCGVSCTGEGEAII-RATLARDVSAVMEykGLNLQEAVDYVIKHRLD-EGFAGLIAVSNKGEVVCGFNSNGMFRG 311
Cdd:cd14949 193 NYANAFAGVSCTGIGEDIVsEALAAKIVTRVTD--GMSLQEAFEKSFAEAKPrDGFAGAIGIDSKGNIYHGDTHPVMVYA 270
|
....*..
gi 18401029 312 CATEDGF 318
Cdd:cd14949 271 SYDGEKI 277
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
40-299 |
3.06e-50 |
|
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: 168.51 E-value: 3.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 40 ALRSNVSAIDVVELVIRELETDPLFNS-GRGSALTEKGTVEMEASIMDGTKRRCGAVSGITTVKNPISLARLVMDKSPHS 118
Cdd:cd04513 18 VLQKGGSALDAVEAGCSVCEDDQCDGSvGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVARAVMEHTPHS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 119 YLAFSGAEDFARKQGVEIvdnEYFVTDDNVGMLKLAKEANSILFDYRIPPMGCAGAAATDSPIQMNGLPISIYAPETVGC 198
Cdd:cd04513 98 LLVGEGATEFAVSMGFKE---ENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSCSSPKAPSRSESAIPEDNHDTIGM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 199 VVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGTYA-SEFCGVSCTGEGEAIIRATLARdvSAVMEYK-GLNLQEAVD 276
Cdd:cd04513 175 IALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYAdNEVGAAAATGDGDIMMRFLPSY--QAVELMRqGMSPQEACE 252
|
250 260
....*....|....*....|....*..
gi 18401029 277 YVI----KHRLDEGFAGLIAVSNKGEV 299
Cdd:cd04513 253 DAIrriaKKYPKDFEGAVVAVNKAGEY 279
|
|
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
4-258 |
1.05e-49 |
|
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: 167.83 E-value: 1.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 4 WAIAVHGGAGidpNLPAERQEEAKQLLTRCLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTVEMEAS 83
Cdd:cd04514 1 FFVAVHAGAG---YHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 84 IMDGTKRRCGAVSGITTVKNPISLARLVMDKS---------PHSYLAFSGAEDFARKQGveivdneyFVTDdnvgmlkla 154
Cdd:cd04514 78 IMDGSSGRFGAVGAVSGVKNPIQLARLLLKEQrkplslgrvPPMFLVGEGAREWAKSKG--------IITD--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 155 keansilfdyrippmgcagaaatdspiqmnglpisiyapeTVGCVVVDGKGHCAAGTSTGGLMNKMMGRIGDSPLIGAGT 234
Cdd:cd04514 141 ----------------------------------------TVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGC 180
|
250 260 270
....*....|....*....|....*....|.
gi 18401029 235 YASEF-------CGVSCTGEGEAIIRATLAR 258
Cdd:cd04514 181 WAEPRdpddktsVAVVTSGTGEHIATTMLAR 211
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
6-262 |
2.12e-31 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 121.90 E-value: 2.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 6 IAVHGGAGIDpnlpAERQEEAKQLLTR--CLNLGIIALRSNVSAIDVVELVIRELETDPLFNSGRGSALTEKGTVEMEAS 83
Cdd:PLN02937 14 VAVHVGAGYH----APSNEKALRSAMRraCLAAAAILRQGSGGCIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDAS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 84 IMDGTKRRCGAVSGITTVKNPISLARLVMDKS----------PHSYLAFSGAEDFARKQGVEIVD-----NEYFVTDDN- 147
Cdd:PLN02937 90 IMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQmmgssllgriPPMFLVGEGARQWAKSKGIDLPEtveeaEKWLVTERAk 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18401029 148 ------VGMLKLAKEANSILFDYRIPPMGCAGAAATDSPIQMNGLPISIYAPE------TVGCVVVDGKGHCAAGTSTGG 215
Cdd:PLN02937 170 eqwkkyKTMLASAIAKSSCDSQSTSKLSELEAPRSNPSNGTGGGQSSMCTASDedcimdTVGVICVDSEGNIASGASSGG 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 18401029 216 LMNKMMGRIGDSPLIGAGTYASE--------FCGVSCTGEGEAIIRATLARDVSA 262
Cdd:PLN02937 250 IAMKVSGRVGLAAMYGSGCWASSkgpfgapfIVGCCVSGAGEYLMRGFAARECCV 304
|
|
| |
