|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
5-304 |
4.10e-72 |
|
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: 226.00 E-value: 4.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 5 EIIAVHGGA--CAKFDASLA-EDCRFAC------------GTGTVENALTDLERIEKFNCGFGSHLTIDQEVECEASYMS 69
Cdd:cd04514 1 FFVAVHAGAgyHSPSNEKAYkRACKRACkaaaavlkaggsALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 70 SKNLSFGAVGAISNVFHPSRVARHLAHSNWWKQ-RRLLHPLILVGRGAEKYAVKNDFPTctpeelvskaakesfekylhr 148
Cdd:cd04514 81 GSSGRFGAVGAVSGVKNPIQLARLLLKEQRKPLsLGRVPPMFLVGEGAREWAKSKGIIT--------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 149 mlhpydthDTVGAISINTNtMNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSERRQYEEPfdqvseRTISICSTGHGESL 228
Cdd:cd04514 140 --------DTVGAIAIDLY-GNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPDDK------TSVAVVTSGTGEHI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 229 VKADFCRGIATRVL--DDEEGIMYSEIIREFIHEKMEHGS------RYGGIALIADKfKDRMSLEFLIFHNCRYLPAAVR 300
Cdd:cd04514 205 ATTMLARRCAERLYhsTRREESDEDEILRSFIESDFMGHPgvknspSAGAIGVLAVK-KTRSGVELYFAHNTDSFALASM 283
|
....
gi 26985839 301 CRDN 304
Cdd:cd04514 284 SSSD 287
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
7-240 |
1.72e-27 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 111.11 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 7 IAVHGGA---CAKFDASLAEDCRFAC---------GTGT----VENALTDLERIEKFNCGFGSHLTIDQEVECEASYMSS 70
Cdd:PLN02937 14 VAVHVGAgyhAPSNEKALRSAMRRAClaaaailrqGSGGcidaVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASIMDG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 71 KNLSFGAVGAISNVFHPSRVARHLAhsnwwKQRRL-------LHPLILVGRGAEKYAVKN--DFPTCTPEE---LVSKAA 138
Cdd:PLN02937 94 DSGAFGAVGAVPGVRNAIQIAALLA-----KEQMMgssllgrIPPMFLVGEGARQWAKSKgiDLPETVEEAekwLVTERA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 139 KESFEKYlHRML---------------------HPYDTH---------------------DTVGAISINTNTmNSESGTS 176
Cdd:PLN02937 169 KEQWKKY-KTMLasaiaksscdsqstsklseleAPRSNPsngtgggqssmctasdedcimDTVGVICVDSEG-NIASGAS 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26985839 177 SGGIVLKHSGRLGHSCVYGSGTW-SERRQYEEPFdqvserTISICSTGHGESLVkadfcRGIATR 240
Cdd:PLN02937 247 SGGIAMKVSGRVGLAAMYGSGCWaSSKGPFGAPF------IVGCCVSGAGEYLM-----RGFAAR 300
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
6-241 |
2.25e-24 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 100.74 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 6 IIAVHGGACAKFD-ASLAEDCRFA------CG----------TGTVENALTDLERIEKFNCGFGSHLTIDQEVECEASYM 68
Cdd:pfam01112 1 VLVIHGGAGSILRtKEREEAYRAGlkealeAGyavlaaggsaLDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 69 SSKNLSFGAVGAISNVFHPSRVARHLA----HSnwwkqrrllhplILVGRGAEKYAVKNDFPTCTPEELVSKAAKESFEK 144
Cdd:pfam01112 81 DGKTLRAGAVAGVSRIKNPISLARAVMektpHV------------MLSGEGAEQFAREMGLERVPPEDFLTEERLQELQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 145 YLHRM---------------LHPYDTHDTVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSERRqyeepF 209
Cdd:pfam01112 149 ARKENfqpnmalnvapdplkECGDSKRGTVGAVALDSEG-NLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNA-----T 222
|
250 260 270
....*....|....*....|....*....|..
gi 26985839 210 DQVSertisicSTGHGESLVKADFCRGIATRV 241
Cdd:pfam01112 223 GAVS-------ATGHGEDIIRETLAYDIVARM 247
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
5-304 |
4.10e-72 |
|
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: 226.00 E-value: 4.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 5 EIIAVHGGA--CAKFDASLA-EDCRFAC------------GTGTVENALTDLERIEKFNCGFGSHLTIDQEVECEASYMS 69
Cdd:cd04514 1 FFVAVHAGAgyHSPSNEKAYkRACKRACkaaaavlkaggsALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 70 SKNLSFGAVGAISNVFHPSRVARHLAHSNWWKQ-RRLLHPLILVGRGAEKYAVKNDFPTctpeelvskaakesfekylhr 148
Cdd:cd04514 81 GSSGRFGAVGAVSGVKNPIQLARLLLKEQRKPLsLGRVPPMFLVGEGAREWAKSKGIIT--------------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 149 mlhpydthDTVGAISINTNtMNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSERRQYEEPfdqvseRTISICSTGHGESL 228
Cdd:cd04514 140 --------DTVGAIAIDLY-GNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPDDK------TSVAVVTSGTGEHI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 229 VKADFCRGIATRVL--DDEEGIMYSEIIREFIHEKMEHGS------RYGGIALIADKfKDRMSLEFLIFHNCRYLPAAVR 300
Cdd:cd04514 205 ATTMLARRCAERLYhsTRREESDEDEILRSFIESDFMGHPgvknspSAGAIGVLAVK-KTRSGVELYFAHNTDSFALASM 283
|
....
gi 26985839 301 CRDN 304
Cdd:cd04514 284 SSSD 287
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
6-237 |
1.10e-33 |
|
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: 125.38 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 6 IIAVHGGACAKFDA---------SLAEDCRFAC--GTGT----VENALTDLERIEKFNCGFGSHLTIDQEVECEASYMSS 70
Cdd:cd04702 3 VIVVHGGAGSIPDDrikgsregvKRAARAGYSVlkAGGSaldaVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASIMDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 71 KNLSFGAVGAISNVFHPSRVARHLAHsnwwKQRRLLhpliLVGRGAEKYAVKNDFPTCTPEELVSKAAKESFEKYLHRML 150
Cdd:cd04702 83 KTLRAGAVSAVRNIANPISLARLVME----KTPHCF----LTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 151 HPYD----THDTVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSERRqyeepfdqvsertISICS-TGHG 225
Cdd:cd04702 155 ANVEdtqrGHGTVGAVAIDCEG-NVACATSTGGITNKMVGRVGDSPIIGSGGYADNL-------------VGAVStTGHG 220
|
250
....*....|..
gi 26985839 226 ESLVKADFCRGI 237
Cdd:cd04702 221 ESIMKVNLARLI 232
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
6-241 |
1.07e-29 |
|
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: 113.82 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 6 IIAVHGGACA---KFDASLAEDCRFACGTG------------TVENALTDLERIEKFNCGFGSHLTIDQEVECEASYMSS 70
Cdd:cd04512 1 SLIVHGGAGTiedEDAEAYREGLLRALEAGrevlekggsaldAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIMDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 71 KNLSFGAVGAISNVFHPSRVARhlahsnwwkqrRLL---HPLILVGRGAEKYAVKNDfptctpeelvskaakesfekylh 147
Cdd:cd04512 81 KTLNAGAVAGVKGVKNPISLAR-----------AVMektPHVLLVGEGAERFAREHG----------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 148 rmlhpydtHDTVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSErrqyeepfdqvsERTISICSTGHGES 227
Cdd:cd04512 127 --------HGTVGAVARDAQG-NLAAATSTGGMVNKRPGRVGDSPIIGAGTYAD------------NETGAVSATGHGES 185
|
250
....*....|....
gi 26985839 228 LVKADFCRGIATRV 241
Cdd:cd04512 186 IIRTVLAKRIADLV 199
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
7-240 |
1.72e-27 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 111.11 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 7 IAVHGGA---CAKFDASLAEDCRFAC---------GTGT----VENALTDLERIEKFNCGFGSHLTIDQEVECEASYMSS 70
Cdd:PLN02937 14 VAVHVGAgyhAPSNEKALRSAMRRAClaaaailrqGSGGcidaVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASIMDG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 71 KNLSFGAVGAISNVFHPSRVARHLAhsnwwKQRRL-------LHPLILVGRGAEKYAVKN--DFPTCTPEE---LVSKAA 138
Cdd:PLN02937 94 DSGAFGAVGAVPGVRNAIQIAALLA-----KEQMMgssllgrIPPMFLVGEGARQWAKSKgiDLPETVEEAekwLVTERA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 139 KESFEKYlHRML---------------------HPYDTH---------------------DTVGAISINTNTmNSESGTS 176
Cdd:PLN02937 169 KEQWKKY-KTMLasaiaksscdsqstsklseleAPRSNPsngtgggqssmctasdedcimDTVGVICVDSEG-NIASGAS 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26985839 177 SGGIVLKHSGRLGHSCVYGSGTW-SERRQYEEPFdqvserTISICSTGHGESLVkadfcRGIATR 240
Cdd:PLN02937 247 SGGIAMKVSGRVGLAAMYGSGCWaSSKGPFGAPF------IVGCCVSGAGEYLM-----RGFAAR 300
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
6-241 |
2.25e-24 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 100.74 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 6 IIAVHGGACAKFD-ASLAEDCRFA------CG----------TGTVENALTDLERIEKFNCGFGSHLTIDQEVECEASYM 68
Cdd:pfam01112 1 VLVIHGGAGSILRtKEREEAYRAGlkealeAGyavlaaggsaLDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 69 SSKNLSFGAVGAISNVFHPSRVARHLA----HSnwwkqrrllhplILVGRGAEKYAVKNDFPTCTPEELVSKAAKESFEK 144
Cdd:pfam01112 81 DGKTLRAGAVAGVSRIKNPISLARAVMektpHV------------MLSGEGAEQFAREMGLERVPPEDFLTEERLQELQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 145 YLHRM---------------LHPYDTHDTVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSERRqyeepF 209
Cdd:pfam01112 149 ARKENfqpnmalnvapdplkECGDSKRGTVGAVALDSEG-NLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNA-----T 222
|
250 260 270
....*....|....*....|....*....|..
gi 26985839 210 DQVSertisicSTGHGESLVKADFCRGIATRV 241
Cdd:pfam01112 223 GAVS-------ATGHGEDIIRETLAYDIVARM 247
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
7-241 |
3.42e-24 |
|
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: 99.07 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 7 IAVHGGA----CAKFDASLAEDCRFA--------------CGTG--TVENALTDLERIEKFNCGFGSHLTIDQEVECEAS 66
Cdd:cd04701 2 LAIHGGAgtisRANLTPERYAAYRAAlrraleagyavlasGGSAldAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 67 YMSSKNLSFGAVGAISNVFHPSRVARHLAHSNWwkqrrllHPLiLVGRGAEKYAVKNDfptctpEELVSkaakesfekyl 146
Cdd:cd04701 82 IMDGRTKRAGAVAGLRRVRNPILLARAVLEKSP-------HVL-LSGEGAEEFAREQG------LELVP----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 147 hrmlhpydtHDTVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSErrqyeepfdqvsERTISICSTGHGE 226
Cdd:cd04701 137 ---------QGTVGAVALDSDG-NLAAATSTGGLTNKLPGRIGDTPIIGAGFWAE------------EWAVAVSGTGNGD 194
|
250
....*....|....*
gi 26985839 227 SLVKADFCRGIATRV 241
Cdd:cd04701 195 SFIRVAAARDVAARM 209
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
6-273 |
1.49e-22 |
|
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: 94.25 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 6 IIAVHGGACAkfDASLAEDCRFACGTGT------------VENALTDLERIEKFNCGFGSHLTIDQEVECEASYMSSKNl 73
Cdd:cd04703 2 AVLVHGGAGS--DPERQDGLERAAEAGLaelqnggdaldaVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAVMTSGG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 74 SFGAVGAISNVFHPSRVARHLAhsnwwkqRRLLHpLILVGRGAEKYAVKNDFPtctpeelvskaakesfekylhrmlhpy 153
Cdd:cd04703 79 AFGAVAAIEGVKNPVLVARAVM-------ETSPH-VLLAGDGAVRFARRLGYP--------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 154 DTHDTVGAISINTNTMnsESGTSSGGIVLKHSGRLGHSCVYGSGTwserrqYEEPFDQVSertisicSTGHGESLVKADF 233
Cdd:cd04703 124 DGCDTVGAVARDGGKF--AAAVSTGGTSPALRGRVGDVPIIGAGF------YAGPKGAVA-------ATGIGEEIAKRLL 188
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 26985839 234 CRGIATRVlddEEGIMYSEIIREFIhEKMEHGSRYGGIAL 273
Cdd:cd04703 189 ARRVYRWI---ETGLSLQAAAQRAI-DEFDDGVAVGVIAV 224
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
7-275 |
3.81e-19 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 86.30 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 7 IAVHGGAcAKFDASLAEDCRFAC----------GTGTVENALTDLERIE----------KFNCGFGSHLTIDQEVECEAS 66
Cdd:PLN02689 6 IALHGGA-GDIDPNLPRERQEEAeaalrrcldlGIAALRSSLPALDVVElvvrelendpLFNAGRGSVLTEDGTVEMEAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 67 YMSSKNLSFGAVGAISNVFHPSRVARHLA----HSnwwkqrrllhplILVGRGAEKYAVKNDFPTCTPEELVSKAAKESF 142
Cdd:PLN02689 85 IMDGRTRRCGAVSGLTTVVNPISLARLVMektpHI------------YLAFDGAEAFARQQGVETVDNSYFITEENVERL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 143 --EKYLHRMLHPY------------------DTHDTVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTwser 202
Cdd:PLN02689 153 kqAKEANSVQFDYripldkpakaaalaadgdAQPETVGCVAVDSDG-NCAAATSTGGLVNKMVGRIGDTPIIGAGT---- 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26985839 203 rqYEEPFDQVSertisicSTGHGESLVKADFCRGIATRVldDEEGIMYSEIIREFIHEKMEHGsrYGGiaLIA 275
Cdd:PLN02689 228 --YANHLCAVS-------ATGKGEAIIRGTVARDVAAVM--EYKGLPLQEAVDYVIKERLPEG--PAG--LIA 285
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
34-197 |
7.79e-18 |
|
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: 82.22 E-value: 7.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 34 VENALTdleRIEKFNC----GFGSHLTIDQEVECEASYMSSKNLSFGAVGAISNVFHPSRVAR----HLAHSnwwkqrrl 105
Cdd:cd04513 29 VEAGCS---VCEDDQCdgsvGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVARavmeHTPHS-------- 97
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 106 lhplILVGRGAEKYAVKNDFPtctPEELVSKAAKESFEKYL----------------------------HRMLHPYDTHD 157
Cdd:cd04513 98 ----LLVGEGATEFAVSMGFK---EENLLTEESRKMWKKWLkencqpnfwknvvpdpskscsspkapsrSESAIPEDNHD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 26985839 158 TVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSG 197
Cdd:cd04513 171 TIGMIALDANG-NIAAGTSTSGAAFKIPGRVGDSPIPGAG 209
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| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
6-286 |
2.86e-15 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 75.37 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 6 IIAVHGGACA--KFDASLAEDCRFA------CGTG------------TVENALTDLERIEKFNCGFGSHLTIDQEVECEA 65
Cdd:PRK10226 5 VIAIHGGAGAisRAQMSLQQELRYIealsaiVETGqkmleagesaldVVTEAVRLLEECPLFNAGIGAVFTRDETHELDA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 66 SYMSSKNLSFGAVGAISNVFHPSRVARHLahsnwwkQRRLLHpLILVGRGAEKYA-------VKNDFPTcTPEELVS-KA 137
Cdd:PRK10226 85 CVMDGNTLKAGAVAGVSHLRNPVLAARLV-------MEQSPH-VMMIGEGAENFAfahgmerVSPEIFS-TPLRYEQlLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 138 AKESFEKYLHRMLHPYDTHD---TVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSerrqyeepfdqvSE 214
Cdd:PRK10226 156 ARAEGATVLDHSGAPLDEKQkmgTVGAVALDLDG-NLAAATSTGGMTNKLPGRVGDSPLVGAGCYA------------NN 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26985839 215 RTISICSTGHGESLVKADFCRGIATrvLDDEEGIMYSEIIREFIHEKMEHGSRYGGiaLIADKFKDRMSLEF 286
Cdd:PRK10226 223 ASVAVSCTGTGEVFIRALAAYDIAA--LMDYGGLSLAEACERVVMEKLPALGGSGG--LIAIDHEGNVALPF 290
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|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
33-273 |
2.13e-13 |
|
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: 69.17 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 33 TVENALTDLERIEKFNCGFGSHLTIDQEVECEASYMSSKNLSFGAVGAISNVFHPSRVARHLAHSnwwKQRrllhplILV 112
Cdd:cd14949 46 AVVYAVSLLEDDPLFNAGTGSQIQSDGQIRMSASLMDGQTQRFSGVINIENVKNPIEVAQKLQQE---DDR------VLS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 113 GRGAEKYAVKNDFP---TCTPEELVSKAAKESFEkylhrmlhpyDTHDTVGAISINTNTmNSESGTSSGGIVLKHSGRLG 189
Cdd:cd14949 117 GEGATEFARENGFPeynPETPQRRQEYEEKKLKS----------GGTGTVGCVALDSDG-KLAAATSTGGKGFEIPGRVS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26985839 190 HSC-VYGSgtwserrqYEEPFDQVSertisiCsTGHGESLVKADFCRGIATRVLDdeeGIMYSEIIREFIHEKMEHGSRY 268
Cdd:cd14949 186 DSAtVAGN--------YANAFAGVS------C-TGIGEDIVSEALAAKIVTRVTD---GMSLQEAFEKSFAEAKPRDGFA 247
|
....*
gi 26985839 269 GGIAL 273
Cdd:cd14949 248 GAIGI 252
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