|
Name |
Accession |
Description |
Interval |
E-value |
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
29-332 |
2.26e-160 |
|
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: 450.09 E-value: 2.26e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 29 LVLNTWPFKNATEAAWRALASGGSALDAVESGCAMCETEQCDGSVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRI 108
Cdd:cd04513 1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 109 KNAIGVARKVLEHTTHTLLVGESATKFAESMGFVNEDLSTRASQALHSDWLARNCQPNYWRNVVPDPSKYCGPYKPLGIL 188
Cdd:cd04513 81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSCSSPKAPSRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 189 KQDIPIHketednrGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLP 268
Cdd:cd04513 161 ESAIPED-------NHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622937078 269 SYQAVEYMRGGEDPTIACQKVISRIQKYFP-EFFGAVICANVTGSYGAACNKlstfTQFSFMVFN 332
Cdd:cd04513 234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
35-326 |
4.58e-105 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 310.28 E-value: 4.58e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 35 PFKNATEAAWRALASGGSALDAVESGCAMCEtEQCDGSVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGV 114
Cdd:pfam01112 24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 115 ARKVLEHTTHTLLVGESATKFAESMGFV---NEDLSTRASQALHSDWLARNCQPNYWRNVVPDPSKYCGPYKplgilkqd 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK-------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 192 ipihketednrgHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLPSYQ 271
Cdd:pfam01112 175 ------------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYD 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622937078 272 AVEYMRGGEDPTIACQKVISRIQKYFPEfFGAVICANVTGSYGAACNKLSTFTQF 326
Cdd:pfam01112 243 IVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFNTEGMYRAY 296
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
37-318 |
8.09e-67 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 212.66 E-value: 8.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 37 KNATEAAWRALASGGSALDAVESGCAMCETeqcDG--SVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGV 114
Cdd:COG1446 35 RAALEAGYAVLEAGGSALDAVEAAVRVLED---DPlfNAGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 115 ARKVLEHTTHTLLVGESATKFAESMGFVNEDLSTRASQALHSDWLARNcqpnywrnvvpdpskycgPYKPLgilkqdipi 194
Cdd:COG1446 112 ARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKAL------------------EYKPI--------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 195 hketEDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYaddtagaaaatgdgdiL----------- 263
Cdd:COG1446 165 ----INERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTY----------------Adnevgavsatg 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 264 -----MRFLPSYQAVEYMRGGEDPTIACQKVISRIQKYFpEFFGAVICANVTGSYGAACN 318
Cdd:COG1446 225 hgeyfIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPFN 283
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
41-290 |
3.20e-25 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 103.49 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 41 EAAWRALASGGSALDAVESGCAMceTEQC---DGSVGFGGSPDELGEttLDAMIMEGTTMDVGAVGDLRRIKNAIGVARK 117
Cdd:PRK10226 37 ETGQKMLEAGESALDVVTEAVRL--LEECplfNAGIGAVFTRDETHE--LDACVMDGNTLKAGAVAGVSHLRNPVLAARL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 118 VLEHTTHTLLVGESATKFAESMGF--VNEDL-ST--RASQALHsdwlARNCQpnywrNVVPDPSKycgpyKPLgilkqdi 192
Cdd:PRK10226 113 VMEQSPHVMMIGEGAENFAFAHGMerVSPEIfSTplRYEQLLA----ARAEG-----ATVLDHSG-----APL------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 193 pihketEDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLPSYQA 272
Cdd:PRK10226 172 ------DEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDI 245
|
250
....*....|....*....
gi 1622937078 273 VEYMR-GGEDPTIACQKVI 290
Cdd:PRK10226 246 AALMDyGGLSLAEACERVV 264
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
29-332 |
2.26e-160 |
|
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: 450.09 E-value: 2.26e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 29 LVLNTWPFKNATEAAWRALASGGSALDAVESGCAMCETEQCDGSVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRI 108
Cdd:cd04513 1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 109 KNAIGVARKVLEHTTHTLLVGESATKFAESMGFVNEDLSTRASQALHSDWLARNCQPNYWRNVVPDPSKYCGPYKPLGIL 188
Cdd:cd04513 81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSCSSPKAPSRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 189 KQDIPIHketednrGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLP 268
Cdd:cd04513 161 ESAIPED-------NHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622937078 269 SYQAVEYMRGGEDPTIACQKVISRIQKYFP-EFFGAVICANVTGSYGAACNKlstfTQFSFMVFN 332
Cdd:cd04513 234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
35-326 |
4.58e-105 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 310.28 E-value: 4.58e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 35 PFKNATEAAWRALASGGSALDAVESGCAMCEtEQCDGSVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGV 114
Cdd:pfam01112 24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 115 ARKVLEHTTHTLLVGESATKFAESMGFV---NEDLSTRASQALHSDWLARNCQPNYWRNVVPDPSKYCGPYKplgilkqd 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK-------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 192 ipihketednrgHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLPSYQ 271
Cdd:pfam01112 175 ------------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYD 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622937078 272 AVEYMRGGEDPTIACQKVISRIQKYFPEfFGAVICANVTGSYGAACNKLSTFTQF 326
Cdd:pfam01112 243 IVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFNTEGMYRAY 296
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
37-318 |
8.09e-67 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 212.66 E-value: 8.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 37 KNATEAAWRALASGGSALDAVESGCAMCETeqcDG--SVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGV 114
Cdd:COG1446 35 RAALEAGYAVLEAGGSALDAVEAAVRVLED---DPlfNAGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 115 ARKVLEHTTHTLLVGESATKFAESMGFVNEDLSTRASQALHSDWLARNcqpnywrnvvpdpskycgPYKPLgilkqdipi 194
Cdd:COG1446 112 ARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKAL------------------EYKPI--------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 195 hketEDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYaddtagaaaatgdgdiL----------- 263
Cdd:COG1446 165 ----INERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTY----------------Adnevgavsatg 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 264 -----MRFLPSYQAVEYMRGGEDPTIACQKVISRIQKYFpEFFGAVICANVTGSYGAACN 318
Cdd:COG1446 225 hgeyfIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPFN 283
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
39-318 |
1.89e-48 |
|
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: 163.12 E-value: 1.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 39 ATEAAWRALASGGSALDAVESGCAMCETeqcDG--SVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGVAR 116
Cdd:cd04512 26 ALEAGREVLEKGGSALDAVEAAVRLLED---DPlfNAGRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 117 KVLEHTTHTLLVGESATKFAESMGfvnedlstrasqalhsdwlarncqpnywrnvvpdpskycgpykplgilkqdipihk 196
Cdd:cd04512 103 AVMEKTPHVLLVGEGAERFAREHG-------------------------------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 197 etednrgHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLPSYQAVEYM 276
Cdd:cd04512 127 -------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLV 199
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622937078 277 RGGEDPTIACQKVISRIqKYFPEFFGAVICANVTGSYGAACN 318
Cdd:cd04512 200 EFGGSAQEAAEAAIDYL-RRRVGGEGGLIVVDPDGRLGAAHN 240
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
37-318 |
1.19e-42 |
|
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: 148.11 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 37 KNATEAAWRALASGgSALDAVESGCAMCEteqcDGSV---GFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIG 113
Cdd:cd14950 25 REALERGYEALRRG-SALEAVVEAVAYME----DSGVfnaGVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 114 VARKVLEHTTHTLLVGESATKFAESMGFvnedlstrasqalhsdwlarncqpnywrnvvpdpskycgpykplgilkqdip 193
Cdd:cd14950 100 LARKVMEKTDHVLIVGEGADELAKRLGG---------------------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 194 ihketednrghDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDIlMRFLPSYQAV 273
Cdd:cd14950 128 -----------DTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATNGVAVSATGIGEVI-IRSLPALRAD 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1622937078 274 EYMRGGEDPTIACQKVISRIQKYFPEFFGAVICANVTGSYGAACN 318
Cdd:cd14950 196 ELVSMGGDIEEAVRAVVNKVTETFGKDTAGIIGIDARGNIAAAFN 240
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
37-246 |
2.93e-39 |
|
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: 140.40 E-value: 2.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 37 KNATEAAWRALASGGSALDAVESG-CAMCETEQCDGsvGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGVA 115
Cdd:cd04702 26 KRAARAGYSVLKAGGSALDAVEAAvRALEDDPVFNA--GYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 116 RKVLEHTTHTLLVGESATKFAESMGFV---NEDLSTRASQALHSDWLARncqpnywrnvvpdpskycgpykplgilkqdi 192
Cdd:cd04702 104 RLVMEKTPHCFLTGRGANKFAEEMGIPqvpPESLVTERARERLEKFKKE------------------------------- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622937078 193 PIHKETEDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAY 246
Cdd:cd04702 153 KGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGY 206
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
39-246 |
2.38e-30 |
|
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: 116.02 E-value: 2.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 39 ATEAAWRALASGGSALDAVESgcAMCETEQC------DGSVgfggsPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAI 112
Cdd:cd04701 31 ALEAGYAVLASGGSALDAVTA--AVRLLEDCplfnagKGAV-----FTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 113 GVARKVLEHTTHTLLVGESATKFAESMGfvnedlstrasqalhsdwlarncqpnywrnvvpdpskycGPYKPLGilkqdi 192
Cdd:cd04701 104 LLARAVLEKSPHVLLSGEGAEEFAREQG---------------------------------------LELVPQG------ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622937078 193 pihketednrghdTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAY 246
Cdd:cd04701 139 -------------TVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFW 179
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
37-319 |
4.74e-26 |
|
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: 104.26 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 37 KNATEAAWRALASGGSALDAVESGCAMCETEQCDGSvGFGGSPDELGETTLDAMIMEGTTmDVGAVGDLRRIKNAIGVAR 116
Cdd:cd04703 20 ERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNA-GTGSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVAR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 117 KVLEHTTHTLLVGESATKFAESMGFVnedlstrasqalhsdwlarncqpnywrnvvpdpskycgpykplgilkqdipihk 196
Cdd:cd04703 98 AVMETSPHVLLAGDGAVRFARRLGYP------------------------------------------------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 197 etednRGHDTIGMVV-IHktGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLpSYQAVEY 275
Cdd:cd04703 124 -----DGCDTVGAVArDG--GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKGAVAATGIGEEIAKRLL-ARRVYRW 195
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1622937078 276 MRGGEDPTIACQKVISRiqkyFPEFFGA-VICANVTGSYGAACNK 319
Cdd:cd04703 196 IETGLSLQAAAQRAIDE----FDDGVAVgVIAVSRRGEAGIASNT 236
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
41-290 |
3.20e-25 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 103.49 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 41 EAAWRALASGGSALDAVESGCAMceTEQC---DGSVGFGGSPDELGEttLDAMIMEGTTMDVGAVGDLRRIKNAIGVARK 117
Cdd:PRK10226 37 ETGQKMLEAGESALDVVTEAVRL--LEECplfNAGIGAVFTRDETHE--LDACVMDGNTLKAGAVAGVSHLRNPVLAARL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 118 VLEHTTHTLLVGESATKFAESMGF--VNEDL-ST--RASQALHsdwlARNCQpnywrNVVPDPSKycgpyKPLgilkqdi 192
Cdd:PRK10226 113 VMEQSPHVMMIGEGAENFAFAHGMerVSPEIfSTplRYEQLLA----ARAEG-----ATVLDHSG-----APL------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 193 pihketEDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLPSYQA 272
Cdd:PRK10226 172 ------DEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDI 245
|
250
....*....|....*....
gi 1622937078 273 VEYMR-GGEDPTIACQKVI 290
Cdd:PRK10226 246 AALMDyGGLSLAEACERVV 264
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
46-246 |
4.92e-22 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 94.77 E-value: 4.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 46 ALASGGSALDAVEsgCAMCETEQC-DGSVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGVARKVLEHTTH 124
Cdd:PLN02689 41 ALRSSLPALDVVE--LVVRELENDpLFNAGRGSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 125 TLLVGESATKFAESMG--------FVNEDLSTRASQALHsdwlARNCQPNYwRNVVPDPSKYCGPYKPlgilkqdipihk 196
Cdd:PLN02689 119 IYLAFDGAEAFARQQGvetvdnsyFITEENVERLKQAKE----ANSVQFDY-RIPLDKPAKAAALAAD------------ 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622937078 197 eteDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAY 246
Cdd:PLN02689 182 ---GDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTY 228
|
|
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
37-246 |
4.74e-21 |
|
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: 91.95 E-value: 4.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 37 KNATEAAWRALASGGSALDAVESgcAMCETEqcDGSV---GFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIG 113
Cdd:cd04514 25 KRACKAAAAVLKAGGSALDAVEA--AIKVLE--DSPLtnaGYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 114 VARKVLEHTTH---------TLLVGESATKFAESMGFVNedlstrasqalhsdwlarncqpnywrnvvpdpskycgpykp 184
Cdd:cd04514 101 LARLLLKEQRKplslgrvppMFLVGEGAREWAKSKGIIT----------------------------------------- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622937078 185 lgilkqdipihketednrghDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAY 246
Cdd:cd04514 140 --------------------DTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCW 181
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
41-246 |
3.18e-16 |
|
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: 77.65 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 41 EAAWRALASGgSALDAVESGCAMCETE-----------QCDGSVgfggspdelgetTLDAMIMEGTTMDVGAVGDLRRIK 109
Cdd:cd14949 32 EEVYEYLKSH-SALEAVVYAVSLLEDDplfnagtgsqiQSDGQI------------RMSASLMDGQTQRFSGVINIENVK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 110 NAIGVARKVLEHTtHTLLVGESATKFAESMGFvnedlstrasqalhsdwlarncqpnywrnvvpdpskycGPYKPLGILK 189
Cdd:cd14949 99 NPIEVAQKLQQED-DRVLSGEGATEFARENGF--------------------------------------PEYNPETPQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622937078 190 QDIPIHKEtEDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPgAGAY 246
Cdd:cd14949 140 RQEYEEKK-LKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNY 194
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
37-246 |
1.73e-15 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 76.83 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 37 KNATEAAWRALASG-GSALDAVESGCAMCETEQCDGSvGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGVA 115
Cdd:PLN02937 36 RRACLAAAAILRQGsGGCIDAVSAAIQVLEDDPSTNA-GRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 116 RKVLEHTTH----------TLLVGESATKFAESMGFVNEDLSTRASQalhsdWLARNCQPNYWRN-----VVPDPSKYCG 180
Cdd:PLN02937 115 ALLAKEQMMgssllgrippMFLVGEGARQWAKSKGIDLPETVEEAEK-----WLVTERAKEQWKKyktmlASAIAKSSCD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622937078 181 PYKPLGILKQDIPIHKETEDNRGH--------------DTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAY 246
Cdd:PLN02937 190 SQSTSKLSELEAPRSNPSNGTGGGqssmctasdedcimDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCW 269
|
|
| |
