|
Name |
Accession |
Description |
Interval |
E-value |
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
7-321 |
1.88e-150 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 424.52 E-value: 1.88e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 7 PVIAIHGGAGTISAATTSAEQAQAYHDALKSIVAAAQAMLLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELD 86
Cdd:COG1446 6 RALIIHGGAGTIARSAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 87 AAVMDGATLAAGAIAGVCHIRRPVRAARAVLEDGAHVLLAGAGAEAFARERGLEMVEPSFFSTEARRQQLYRVRgtgrvv 166
Cdd:COG1446 86 ASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKAL------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 167 tdhegasmtAASPLDEDKKFGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDRTAAVSCTGSGEMFI 246
Cdd:COG1446 160 ---------EYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFI 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1543420836 247 RVAAAYDVCARMAyGGATLEAATHAVVQQSLPAIGGSGGLIAVDRHGNLSLAFNSEGMYRGHARGNEAPKTAIFA 321
Cdd:COG1446 231 RTVVAHDIVERMR-QGLSLQEAAEEVIERILKKLGGDGGLIAVDKDGNIAAPFNTEGMYRAYIDGDGELVVAIYK 304
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
8-307 |
2.10e-134 |
|
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: 382.19 E-value: 2.10e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 8 VIAIHGGAGTISAATTSAEQAQAYHDALKSIVAAAQAMLLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELDA 87
Cdd:cd04701 1 ALAIHGGAGTISRANLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 88 AVMDGATLAAGAIAGVCHIRRPVRAARAVLEDGAHVLLAGAGAEAFARERGLEMVepsffstearrqqlyrvrgtgrvvt 167
Cdd:cd04701 81 SIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELV------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 168 dhegasmtaaspldedkKFGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDRTAAVSCTGSGEMFIR 247
Cdd:cd04701 136 -----------------PQGTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWAVAVSGTGNGDSFIR 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 248 VAAAYDVCARMAYGGATLEAATHAVVQQSLPAIGGSGGLIAVDRHGNLSLAFNSEGMYRG 307
Cdd:cd04701 199 VAAARDVAARMRYKGLSLAEAAKEVVGPGGELGEGEGGIIAIDARGNVAMPFNCGGMYRA 258
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
8-320 |
2.33e-128 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 368.45 E-value: 2.33e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 8 VIAIHGGAGTISAattSAEQAQAYHDALKSIVAAAQAMLLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELDA 87
Cdd:pfam01112 1 VLVIHGGAGSILR---TKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 88 AVMDGATLAAGAIAGVCHIRRPVRAARAVLEDGAHVLLAGAGAEAFARERGLEMVEPSFFSTEARRQQLYRVRGTGRVVT 167
Cdd:pfam01112 78 SIMDGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKENFQPN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 168 DhegASMTAASPLDE--DKKFGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDRTAAVSCTGSGEMF 245
Cdd:pfam01112 158 M---ALNVAPDPLKEcgDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDI 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1543420836 246 IRVAAAYDVCARMAYgGATLEAATHAVVQQSLPAIGGSGGLIAVDRHGNLSLAFNSEGMYRGHARGNEAPKTAIF 320
Cdd:pfam01112 235 IRETLAYDIVARMEY-GLSLEEAADKVITEMLKRVGGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGIGDVLIY 308
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
8-320 |
4.64e-127 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 365.43 E-value: 4.64e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 8 VIAIHGGAGTISAATTSAEQAQAYHDALKSIVAAAQAMLLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELDA 87
Cdd:PRK10226 5 VIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 88 AVMDGATLAAGAIAGVCHIRRPVRAARAVLEDGAHVLLAGAGAEAFARERGLEMVEPSFFSTEARRQQLYRVRGTGRVVT 167
Cdd:PRK10226 85 CVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAARAEGATVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 168 DHEGAsmtaasPLDEDKKFGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDRTAAVSCTGSGEMFIR 247
Cdd:PRK10226 165 DHSGA------PLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1543420836 248 VAAAYDVCARMAYGGATLEAATHAVVQQSLPAIGGSGGLIAVDRHGNLSLAFNSEGMYRGHARGNEAPKTAIF 320
Cdd:PRK10226 239 ALAAYDIAALMDYGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAWGYAGDTPTTGIY 311
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
7-321 |
1.88e-150 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 424.52 E-value: 1.88e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 7 PVIAIHGGAGTISAATTSAEQAQAYHDALKSIVAAAQAMLLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELD 86
Cdd:COG1446 6 RALIIHGGAGTIARSAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 87 AAVMDGATLAAGAIAGVCHIRRPVRAARAVLEDGAHVLLAGAGAEAFARERGLEMVEPSFFSTEARRQQLYRVRgtgrvv 166
Cdd:COG1446 86 ASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKAL------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 167 tdhegasmtAASPLDEDKKFGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDRTAAVSCTGSGEMFI 246
Cdd:COG1446 160 ---------EYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFI 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1543420836 247 RVAAAYDVCARMAyGGATLEAATHAVVQQSLPAIGGSGGLIAVDRHGNLSLAFNSEGMYRGHARGNEAPKTAIFA 321
Cdd:COG1446 231 RTVVAHDIVERMR-QGLSLQEAAEEVIERILKKLGGDGGLIAVDKDGNIAAPFNTEGMYRAYIDGDGELVVAIYK 304
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
8-307 |
2.10e-134 |
|
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: 382.19 E-value: 2.10e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 8 VIAIHGGAGTISAATTSAEQAQAYHDALKSIVAAAQAMLLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELDA 87
Cdd:cd04701 1 ALAIHGGAGTISRANLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 88 AVMDGATLAAGAIAGVCHIRRPVRAARAVLEDGAHVLLAGAGAEAFARERGLEMVepsffstearrqqlyrvrgtgrvvt 167
Cdd:cd04701 81 SIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELV------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 168 dhegasmtaaspldedkKFGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDRTAAVSCTGSGEMFIR 247
Cdd:cd04701 136 -----------------PQGTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWAVAVSGTGNGDSFIR 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 248 VAAAYDVCARMAYGGATLEAATHAVVQQSLPAIGGSGGLIAVDRHGNLSLAFNSEGMYRG 307
Cdd:cd04701 199 VAAARDVAARMRYKGLSLAEAAKEVVGPGGELGEGEGGIIAIDARGNVAMPFNCGGMYRA 258
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
8-320 |
2.33e-128 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 368.45 E-value: 2.33e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 8 VIAIHGGAGTISAattSAEQAQAYHDALKSIVAAAQAMLLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELDA 87
Cdd:pfam01112 1 VLVIHGGAGSILR---TKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 88 AVMDGATLAAGAIAGVCHIRRPVRAARAVLEDGAHVLLAGAGAEAFARERGLEMVEPSFFSTEARRQQLYRVRGTGRVVT 167
Cdd:pfam01112 78 SIMDGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKENFQPN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 168 DhegASMTAASPLDE--DKKFGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDRTAAVSCTGSGEMF 245
Cdd:pfam01112 158 M---ALNVAPDPLKEcgDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDI 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1543420836 246 IRVAAAYDVCARMAYgGATLEAATHAVVQQSLPAIGGSGGLIAVDRHGNLSLAFNSEGMYRGHARGNEAPKTAIF 320
Cdd:pfam01112 235 IRETLAYDIVARMEY-GLSLEEAADKVITEMLKRVGGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGIGDVLIY 308
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
8-320 |
4.64e-127 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 365.43 E-value: 4.64e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 8 VIAIHGGAGTISAATTSAEQAQAYHDALKSIVAAAQAMLLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELDA 87
Cdd:PRK10226 5 VIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 88 AVMDGATLAAGAIAGVCHIRRPVRAARAVLEDGAHVLLAGAGAEAFARERGLEMVEPSFFSTEARRQQLYRVRGTGRVVT 167
Cdd:PRK10226 85 CVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTPLRYEQLLAARAEGATVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 168 DHEGAsmtaasPLDEDKKFGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDRTAAVSCTGSGEMFIR 247
Cdd:PRK10226 165 DHSGA------PLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1543420836 248 VAAAYDVCARMAYGGATLEAATHAVVQQSLPAIGGSGGLIAVDRHGNLSLAFNSEGMYRGHARGNEAPKTAIF 320
Cdd:PRK10226 239 ALAAYDIAALMDYGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAWGYAGDTPTTGIY 311
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
8-307 |
6.33e-91 |
|
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: 271.36 E-value: 6.33e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 8 VIAIHGGAGTISAattsaEQAQAYHDALKSIVAAAQAMLLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELDA 87
Cdd:cd04512 1 SLIVHGGAGTIED-----EDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 88 AVMDGATLAAGAIAGVCHIRRPVRAARAVLEDGAHVLLAGAGAEAFARERGLemvepsffstearrqqlyrvrgtgrvvt 167
Cdd:cd04512 76 AIMDGKTLNAGAVAGVKGVKNPISLARAVMEKTPHVLLVGEGAERFAREHGH---------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 168 dhegasmtaaspldedkkfGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDRTAAVSCTGSGEMFIR 247
Cdd:cd04512 128 -------------------GTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIR 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 248 VAAAYDVCARMAYGGaTLEAATHAVVQQSLPAIGGSGGLIAVDRHGNLSLAFNSEGMYRG 307
Cdd:cd04512 189 TVLAKRIADLVEFGG-SAQEAAEAAIDYLRRRVGGEGGLIVVDPDGRLGAAHNTPGMAFA 247
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
7-312 |
1.49e-86 |
|
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: 261.74 E-value: 1.49e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 7 PVIAIHGGAGTISAattsaEQAQAYHDALKSIVAAAQAMLLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELD 86
Cdd:cd04702 2 PVIVVHGGAGSIPD-----DRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 87 AAVMDGATLAAGAIAGVCHIRRPVRAARAVLEDGAHVLLAGAGAEAFARERGLEMVEPSFFSTEARRQQLYRVRGTGrvv 166
Cdd:cd04702 77 ASIMDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEK--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 167 tdhegasmtAASPLDEDKKFGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDRTAAVSCTGSGEMFI 246
Cdd:cd04702 154 ---------GANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIM 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1543420836 247 RVAAAYDVCARMAYGGATLEAATHAvVQQSLPAIGGSGGLIAVDRHGNLSLAFNSEGMYRGHARGN 312
Cdd:cd04702 225 KVNLARLILFHMEQGKTAEEAAELA-LAYMKSRVKGLGGLIVVSKTGDWGAKFTSKRMAWAAVKDG 289
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
9-309 |
4.39e-86 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 261.56 E-value: 4.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 9 IAIHGGAGTISAATTSAEQAQAyHDALKSIVAAAQAMLLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELDAA 88
Cdd:PLN02689 6 IALHGGAGDIDPNLPRERQEEA-EAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 89 VMDGATLAAGAIAGVCHIRRPVRAARAVLEDGAHVLLAGAGAEAFARERGLEMVEPSFFSTEARRQQLYRVRGTGRVVTD 168
Cdd:PLN02689 85 IMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAKEANSVQFD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 169 H----EGASMTAASPLDEDKKFGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDrTAAVSCTGSGEM 244
Cdd:PLN02689 165 YriplDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYANH-LCAVSATGKGEA 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1543420836 245 FIRVAAAYDVCARMAYGGATLEAATHAVVQQSLPAigGSGGLIAVDRHGNLSLAFNSEGMYRGHA 309
Cdd:PLN02689 244 IIRGTVARDVAAVMEYKGLPLQEAVDYVIKERLPE--GPAGLIAVSATGEVAMAFNTTGMFRACA 306
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
8-311 |
1.12e-63 |
|
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: 201.65 E-value: 1.12e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 8 VIAIHGGAGTISAATTSAEQAQAYHDALKSIVAAaqamlLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELDA 87
Cdd:cd14950 1 ALVVHGGAGSWKNSDDEEKALRALREALERGYEA-----LRRGSALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 88 AVMDGATLAAGAIAGVCHIRRPVRAARAVLEDGAHVLLAGAGAEAFARERGlemvepsffstearrqqlyrvrgtgrvvt 167
Cdd:cd14950 76 GIMDGRTLRVGAVAAVRAVKNPIRLARKVMEKTDHVLIVGEGADELAKRLG----------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 168 dhegasmtaaspldedkkFGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDRTaAVSCTGSGEMFIR 247
Cdd:cd14950 127 ------------------GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATNGV-AVSATGIGEVIIR 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1543420836 248 VAAAYDVCARMAYGGATLEAATHAVVQQSLPAIGGSGGLIAVDRHGNLSLAFNSEGMYRGHARG 311
Cdd:cd14950 188 SLPALRADELVSMGGDIEEAVRAVVNKVTETFGKDTAGIIGIDARGNIAAAFNTEAMPRGYIDD 251
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
7-294 |
3.45e-56 |
|
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: 183.58 E-value: 3.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 7 PVIAIHGGAGtiSAATTSAEQAQAYHDALKSIVAAAQAMLLKGaSALDATCLAVEMLEECPLFNAGHGAVFTHDETHELD 86
Cdd:cd14949 1 PKLIIHGGFG--SESSTNGETKAAKQEALAEIVEEVYEYLKSH-SALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQIRMS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 87 AAVMDGATLAAGAIAGVCHIRRPVRAARAvLEDGAHVLLAGAGAEAFARERGLEMVEPSffsTEARRQQLYRVRgtgrvv 166
Cdd:cd14949 78 ASLMDGQTQRFSGVINIENVKNPIEVAQK-LQQEDDRVLSGEGATEFARENGFPEYNPE---TPQRRQEYEEKK------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 167 tdhegasmtaaspLDEDKKfGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIgAGTYADDRtAAVSCTGSGEMFI 246
Cdd:cd14949 148 -------------LKSGGT-GTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNYANAF-AGVSCTGIGEDIV 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1543420836 247 RVAAAYDVCARMAyGGATLEAATHAVVQQSLPaIGGSGGLIAVDRHGN 294
Cdd:cd14949 212 SEALAAKIVTRVT-DGMSLQEAFEKSFAEAKP-RDGFAGAIGIDSKGN 257
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
33-294 |
1.64e-49 |
|
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: 166.58 E-value: 1.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 33 DALKSIVAAAQAmLLKGASALDA---TCLAVEmLEECPLFNAGHGAVFTHDEThELDAAVMDGATLAAGAIAGVCHIRRP 109
Cdd:cd04513 7 NFTEAVEAAWEV-LQKGGSALDAveaGCSVCE-DDQCDGSVGYGGSPDENGET-TLDAAIMDGDTMDVGAVAALRRIKNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 110 VRAARAVLEDGAHVLLAGAGAEAFARERGLEmvEPSFFSTEARRQQL----------YR--VRGTGRVVTDHEGASMTAA 177
Cdd:cd04513 84 ISVARAVMEHTPHSLLVGEGATEFAVSMGFK--EENLLTEESRKMWKkwlkencqpnFWknVVPDPSKSCSSPKAPSRSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 178 SPLDEDKkFGTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDRTAAVSCTGSGEMFIRVAAAYDVCAR 257
Cdd:cd04513 162 SAIPEDN-HDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLPSYQAVEL 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 1543420836 258 MAYgGATLEAATHAVVQ--QSLPAIGGSGGLIAVDRHGN 294
Cdd:cd04513 241 MRQ-GMSPQEACEDAIRriAKKYPKDFEGAVVAVNKAGE 278
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
7-301 |
1.24e-44 |
|
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: 152.41 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 7 PVIAIHGGAGTISAATTSAEQAqayhdalksiVAAAQAMLLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELD 86
Cdd:cd04703 1 MAVLVHGGAGSDPERQDGLERA----------AEAGLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 87 AAVMDGATlAAGAIAGVCHIRRPVRAARAVLEDGAHVLLAGAGAEAFARERGLEMVEpsffstearrqqlyrvrgtgrvv 166
Cdd:cd04703 71 AAVMTSGG-AFGAVAAIEGVKNPVLVARAVMETSPHVLLAGDGAVRFARRLGYPDGC----------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 167 tdhegasmtaaspldedkkfGTVGAVALDmHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYADDRtAAVSCTGSGEMFI 246
Cdd:cd04703 127 --------------------DTVGAVARD-GGKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPK-GAVAATGIGEEIA 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1543420836 247 RVAAAYDVCARMAYGGATLEAATHAVvqqSLPAIGGSGGLIAVDRHGNLSLAFNS 301
Cdd:cd04703 185 KRLLARRVYRWIETGLSLQAAAQRAI---DEFDDGVAVGVIAVSRRGEAGIASNT 236
|
|
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
9-314 |
4.37e-37 |
|
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: 134.71 E-value: 4.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 9 IAIHGGAGTISAATTSAeqaqaYHDALKSIVAAAQAMLLKGASALDATCLAVEMLEECPLFNAGHGAVFTHDETHELDAA 88
Cdd:cd04514 3 VAVHAGAGYHSPSNEKA-----YKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 89 VMDGATLAAGAIAGVCHIRRPVRAARAVLE-----DGAH----VLLAGAGAEAFARERGLemvepsffstearrqqlyrv 159
Cdd:cd04514 78 IMDGSSGRFGAVGAVSGVKNPIQLARLLLKeqrkpLSLGrvppMFLVGEGAREWAKSKGI-------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 160 rgtgrvVTDhegasmtaaspldedkkfgTVGAVALDMHGHLAAATSTGGMTNKRVGRIGDSPLIGAGTYA------DDRT 233
Cdd:cd04514 138 ------ITD-------------------TVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAeprdpdDKTS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 234 AAVSCTGSGEMFIRVAAAYDVCARMAYGGATLEAATHAVVQQ------------SLPAIGGSGGLIAVDRHGN---LSLA 298
Cdd:cd04514 193 VAVVTSGTGEHIATTMLARRCAERLYHSTRREESDEDEILRSfiesdfmghpgvKNSPSAGAIGVLAVKKTRSgveLYFA 272
|
330
....*....|....*.
gi 1543420836 299 FNSEGMYRGHARGNEA 314
Cdd:cd04514 273 HNTDSFALASMSSSDR 288
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
9-256 |
2.55e-24 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 101.86 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 9 IAIHGGAGTISAAttsaeQAQAYHDALKSIVAAAQAMLLKGA-SALDATCLAVEMLEECPLFNAGHGAVFTHDETHELDA 87
Cdd:PLN02937 14 VAVHVGAGYHAPS-----NEKALRSAMRRACLAAAAILRQGSgGCIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 88 AVMDGATLAAGAIAGVCHIRRPVRAARAVLEDGAH----------VLLAGAGAEAFARERGLEMVEP-----SFFSTEAR 152
Cdd:PLN02937 89 SIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMgssllgrippMFLVGEGARQWAKSKGIDLPETveeaeKWLVTERA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543420836 153 RQQLYRVRG-------------------------TGRVVTDHEGASMTAASPLDEDKKFGTVGAVALDMHGHLAAATSTG 207
Cdd:PLN02937 169 KEQWKKYKTmlasaiaksscdsqstsklseleapRSNPSNGTGGGQSSMCTASDEDCIMDTVGVICVDSEGNIASGASSG 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1543420836 208 GMTNKRVGRIGDSPLIGAGTYADDR-----TAAVSC--TGSGEMFIRVAAAYDVCA 256
Cdd:PLN02937 249 GIAMKVSGRVGLAAMYGSGCWASSKgpfgaPFIVGCcvSGAGEYLMRGFAARECCV 304
|
|
| |
