|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
1-313 |
0e+00 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 620.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 1 MGKAVIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETH 80
Cdd:PRK10226 1 MGKAVIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 81 ELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAAREEG 160
Cdd:PRK10226 81 ELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAARAEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 161 ATVLDHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRAL 240
Cdd:PRK10226 161 ATVLDHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRAL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446435906 241 AAYDIAALMDYGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAWGYAGDTPTTGIYRE 313
Cdd:PRK10226 241 AAYDIAALMDYGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAWGYAGDTPTTGIYRE 313
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
1-313 |
2.29e-166 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 464.58 E-value: 2.29e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 1 MGKAVIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETH 80
Cdd:COG1446 3 MSRRALIIHGGAGTIARSAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 81 ELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAAREEG 160
Cdd:COG1446 83 ELDASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 161 atvldhsgaPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRAL 240
Cdd:COG1446 163 ---------PIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRTV 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446435906 241 AAYDIAALMDyGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAWGYAGDTPTTGIYRE 313
Cdd:COG1446 234 VAHDIVERMR-QGLSLQEAAEEVIERILKKLGGDGGLIAVDKDGNIAAPFNTEGMYRAYIDGDGELVVAIYKD 305
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
5-299 |
8.22e-152 |
|
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: 426.11 E-value: 8.22e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 5 VIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDA 84
Cdd:cd04701 1 ALAIHGGAGTISRANLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 85 CVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVspeifstplryeqllaareegatvl 164
Cdd:cd04701 81 SIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELV------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 165 dhsgapldekqKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYD 244
Cdd:cd04701 136 -----------PQGTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWAVAVSGTGNGDSFIRVAAARD 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446435906 245 IAALMDYGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAW 299
Cdd:cd04701 205 VAARMRYKGLSLAEAAKEVVGPGGELGEGEGGIIAIDARGNVAMPFNCGGMYRAW 259
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
5-311 |
7.70e-150 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 423.15 E-value: 7.70e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 5 VIAIHGGAGAISRaqmSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDA 84
Cdd:pfam01112 1 VLVIHGGAGSILR---TKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 85 CVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAAREEGATV- 163
Cdd:pfam01112 78 SIMDGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKENFQPn 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 164 --LDHSGAPLDEKQ--KMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRA 239
Cdd:pfam01112 158 maLNVAPDPLKECGdsKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRE 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446435906 240 LAAYDIAALMDYgGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAWGYAGDTPTTGIY 311
Cdd:pfam01112 238 TLAYDIVARMEY-GLSLEEAADKVITEMLKRVGGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGIGDVLIY 308
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
1-313 |
0e+00 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 620.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 1 MGKAVIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETH 80
Cdd:PRK10226 1 MGKAVIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 81 ELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAAREEG 160
Cdd:PRK10226 81 ELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAARAEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 161 ATVLDHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRAL 240
Cdd:PRK10226 161 ATVLDHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRAL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446435906 241 AAYDIAALMDYGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAWGYAGDTPTTGIYRE 313
Cdd:PRK10226 241 AAYDIAALMDYGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAWGYAGDTPTTGIYRE 313
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
1-313 |
2.29e-166 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 464.58 E-value: 2.29e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 1 MGKAVIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETH 80
Cdd:COG1446 3 MSRRALIIHGGAGTIARSAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 81 ELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAAREEG 160
Cdd:COG1446 83 ELDASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 161 atvldhsgaPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRAL 240
Cdd:COG1446 163 ---------PIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRTV 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446435906 241 AAYDIAALMDyGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAWGYAGDTPTTGIYRE 313
Cdd:COG1446 234 VAHDIVERMR-QGLSLQEAAEEVIERILKKLGGDGGLIAVDKDGNIAAPFNTEGMYRAYIDGDGELVVAIYKD 305
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
5-299 |
8.22e-152 |
|
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: 426.11 E-value: 8.22e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 5 VIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDA 84
Cdd:cd04701 1 ALAIHGGAGTISRANLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 85 CVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVspeifstplryeqllaareegatvl 164
Cdd:cd04701 81 SIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELV------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 165 dhsgapldekqKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYD 244
Cdd:cd04701 136 -----------PQGTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWAVAVSGTGNGDSFIRVAAARD 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446435906 245 IAALMDYGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAW 299
Cdd:cd04701 205 VAARMRYKGLSLAEAAKEVVGPGGELGEGEGGIIAIDARGNVAMPFNCGGMYRAW 259
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
5-311 |
7.70e-150 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 423.15 E-value: 7.70e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 5 VIAIHGGAGAISRaqmSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDA 84
Cdd:pfam01112 1 VLVIHGGAGSILR---TKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 85 CVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAAREEGATV- 163
Cdd:pfam01112 78 SIMDGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKENFQPn 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 164 --LDHSGAPLDEKQ--KMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRA 239
Cdd:pfam01112 158 maLNVAPDPLKECGdsKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRE 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446435906 240 LAAYDIAALMDYgGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAWGYAGDTPTTGIY 311
Cdd:pfam01112 238 TLAYDIVARMEY-GLSLEEAADKVITEMLKRVGGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGIGDVLIY 308
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
5-299 |
3.26e-111 |
|
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: 322.98 E-value: 3.26e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 5 VIAIHGGAGAISRAQmslqqELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDA 84
Cdd:cd04512 1 SLIVHGGAGTIEDED-----AEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 85 CVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGmervspeifstplryeqllaareegatvl 164
Cdd:cd04512 76 AIMDGKTLNAGAVAGVKGVKNPISLARAVMEKTPHVLLVGEGAERFAREHG----------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 165 dhsgapldekqkMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYD 244
Cdd:cd04512 127 ------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKR 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446435906 245 IAALMDYGGlsLAEACERVVMEKLPAL-GGSGGLIAIDHEGNVALPFNTEGMYRAW 299
Cdd:cd04512 195 IADLVEFGG--SAQEAAEAAIDYLRRRvGGEGGLIVVDPDGRLGAAHNTPGMAFAY 248
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
1-298 |
1.27e-97 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 290.84 E-value: 1.27e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 1 MGKAVIAIHGGAGAISRaQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETH 80
Cdd:PLN02689 1 MGGWAIALHGGAGDIDP-NLPRERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 81 ELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAAREEG 160
Cdd:PLN02689 80 EMEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAKEAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 161 ATVLDH----------SGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASvAVSCT 230
Cdd:PLN02689 160 SVQFDYripldkpakaAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYANHLC-AVSAT 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446435906 231 GTGEVFIRALAAYDIAALMDYGGLSLAEACERVVMEKLPAlgGSGGLIAIDHEGNVALPFNTEGMYRA 298
Cdd:PLN02689 239 GKGEAIIRGTVARDVAAVMEYKGLPLQEAVDYVIKERLPE--GPAGLIAVSATGEVAMAFNTTGMFRA 304
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
3-304 |
5.67e-93 |
|
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: 277.92 E-value: 5.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 3 KAVIAIHGGAGAISRAQmslqqELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHEL 82
Cdd:cd04702 1 KPVIVVHGGAGSIPDDR-----IKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 83 DACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPlryeqllAAREEGAT 162
Cdd:cd04702 76 DASIMDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTE-------RARERLEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 163 VLDHSGAPLDEKQK-MGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALA 241
Cdd:cd04702 149 FKKEKGANVEDTQRgHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 242 AYDIAALMDYGG-------LSLAEACERVvmeklpalGGSGGLIAIDHEGNVALPFNTEGMyrAWGYAGD 304
Cdd:cd04702 229 ARLILFHMEQGKtaeeaaeLALAYMKSRV--------KGLGGLIVVSKTGDWGAKFTSKRM--AWAAVKD 288
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
5-301 |
7.51e-84 |
|
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: 253.27 E-value: 7.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 5 VIAIHGGAGAISRAQmslqQELRYIEALSAIVETGQKMLEAGeSALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDA 84
Cdd:cd14950 1 ALVVHGGAGSWKNSD----DEEKALRALREALERGYEALRRG-SALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 85 CVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGmervspeifstplryeqllaareegatvl 164
Cdd:cd14950 76 GIMDGRTLRVGAVAAVRAVKNPIRLARKVMEKTDHVLIVGEGADELAKRLG----------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 165 dhsgapldekqkMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNaSVAVSCTGTGEVFIRALAAYD 244
Cdd:cd14950 127 ------------GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN-GVAVSATGIGEVIIRSLPALR 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446435906 245 IAALMDyGGLSLAEACERVVmEKLPALGGSG--GLIAIDHEGNVALPFNTEGMYRAWGY 301
Cdd:cd14950 194 ADELVS-MGGDIEEAVRAVV-NKVTETFGKDtaGIIGIDARGNIAAAFNTEAMPRGYID 250
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
6-287 |
1.63e-61 |
|
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: 197.06 E-value: 1.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 6 IAIHGGAGaiSRAQMSLQQELRYIEALSAIVETGQKMLEAGeSALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDAC 85
Cdd:cd14949 3 LIIHGGFG--SESSTNGETKAAKQEALAEIVEEVYEYLKSH-SALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQIRMSAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 86 VMDGNTLKAGAVAGVSHLRNPVLAARLVMEQsPHVMMIGEGAENFAFAHGMERVSPEifsTPLRyeqllaaREEGATVLD 165
Cdd:cd14949 80 LMDGQTQRFSGVINIENVKNPIEVAQKLQQE-DDRVLSGEGATEFARENGFPEYNPE---TPQR-------RQEYEEKKL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 166 HSGapldekqKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVgAGCYAnNASVAVSCTGTGEVFI-RALAAYD 244
Cdd:cd14949 149 KSG-------GTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNYA-NAFAGVSCTGIGEDIVsEALAAKI 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446435906 245 IAALMDygGLSLAEACERvVMEKLPALGGSGGLIAIDHEGNVA 287
Cdd:cd14949 220 VTRVTD--GMSLQEAFEK-SFAEAKPRDGFAGAIGIDSKGNIY 259
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
36-287 |
5.72e-56 |
|
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: 183.53 E-value: 5.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 36 VETGQKMLEAGESALDVVTEAVRLLEECPlfnagigAVFT------RDETHE--LDACVMDGNTLKAGAVAGVSHLRNPV 107
Cdd:cd04513 12 VEAAWEVLQKGGSALDAVEAGCSVCEDDQ-------CDGSvgyggsPDENGEttLDAAIMDGDTMDVGAVAALRRIKNAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 108 LAARLVMEQSPHVMMIGEGAENFAFAHGMERvspEIFSTPLRYEQLLAAREEG-------ATVLDHSGAPLDEKQKM--- 177
Cdd:cd04513 85 SVARAVMEHTPHSLLVGEGATEFAVSMGFKE---ENLLTEESRKMWKKWLKENcqpnfwkNVVPDPSKSCSSPKAPSrse 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 178 --------GTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAALM 249
Cdd:cd04513 162 saipednhDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLPSYQAVELM 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446435906 250 DYgGLSLAEACERVV---MEKLPALgGSGGLIAIDHEGNVA 287
Cdd:cd04513 242 RQ-GMSPQEACEDAIrriAKKYPKD-FEGAVVAVNKAGEYG 280
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
4-299 |
2.43e-54 |
|
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: 177.45 E-value: 2.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 4 AVIAIHGGAGAISRAQMSLQQelryiealsaIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELD 83
Cdd:cd04703 1 MAVLVHGGAGSDPERQDGLER----------AAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 84 ACVMDGnTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSpeifstplryeqllaareegatv 163
Cdd:cd04703 71 AAVMTS-GGAFGAVAAIEGVKNPVLVARAVMETSPHVLLAGDGAVRFARRLGYPDGC----------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 164 ldhsgapldekqkmGTVGAVALDlDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYAnNASVAVSCTGTGEVFIRALAAY 243
Cdd:cd04703 127 --------------DTVGAVARD-GGKFAAAVSTGGTSPALRGRVGDVPIIGAGFYA-GPKGAVAATGIGEEIAKRLLAR 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446435906 244 DIAALMDyGGLSLAEACERVVmeKLPALGGSGGLIAIDHEGNVALPFNTeGMYRAW 299
Cdd:cd04703 191 RVYRWIE-TGLSLQAAAQRAI--DEFDDGVAVGVIAVSRRGEAGIASNT-AMAWAI 242
|
|
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
6-246 |
2.72e-47 |
|
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: 161.29 E-value: 2.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 6 IAIHGGAGAisraqMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDAC 85
Cdd:cd04514 3 VAVHAGAGY-----HSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 86 VMDGNTLKAGAVAGVSHLRNPVLAARLVMEQS---------PHVMMIGEGAENFAFAHGMervspeifstplryeqllaa 156
Cdd:cd04514 78 IMDGSSGRFGAVGAVSGVKNPIQLARLLLKEQrkplslgrvPPMFLVGEGAREWAKSKGI-------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 157 reegatVLDhsgapldekqkmgTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNA------SVAVSCT 230
Cdd:cd04514 138 ------ITD-------------TVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRdpddktSVAVVTS 198
|
250
....*....|....*.
gi 446435906 231 GTGEVFIRALAAYDIA 246
Cdd:cd04514 199 GTGEHIATTMLARRCA 214
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
6-291 |
6.47e-31 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 120.35 E-value: 6.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 6 IAIHGGAG--AISRAQMSLQQELRYIEALSAIVETGqkmleAGESaLDVVTEAVRLLEECPLFNAGIGAVFTRDETHELD 83
Cdd:PLN02937 14 VAVHVGAGyhAPSNEKALRSAMRRACLAAAAILRQG-----SGGC-IDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 84 ACVMDGNTLKAGAVAGVSHLRNPV-LAARLVMEQS---------PHVMMIGEGAENFAFAHGMErvSPEIFSTP------ 147
Cdd:PLN02937 88 ASIMDGDSGAFGAVGAVPGVRNAIqIAALLAKEQMmgssllgriPPMFLVGEGARQWAKSKGID--LPETVEEAekwlvt 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 148 -------LRYEQLLAAREEGATVLDHSGAPL-------------------------DEKQKMGTVGAVALDLDGNLAAAT 195
Cdd:PLN02937 166 erakeqwKKYKTMLASAIAKSSCDSQSTSKLseleaprsnpsngtgggqssmctasDEDCIMDTVGVICVDSEGNIASGA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446435906 196 STGGMTNKLPGRVGDSPLVGAGCYANN-----ASVAVSC--TGTGEVFIRALAAYDI---AALMDYGGLSLAEACERVVM 265
Cdd:PLN02937 246 SSGGIAMKVSGRVGLAAMYGSGCWASSkgpfgAPFIVGCcvSGAGEYLMRGFAARECcvsSSLSQAGPASACMKVLRSVI 325
|
330 340
....*....|....*....|....*...
gi 446435906 266 EKLPALGG--SGGLIAIDHEGNVALPFN 291
Cdd:PLN02937 326 QGSSAKTTdkDAGILLVQADASVMAPGN 353
|
|
| |
