|
Name |
Accession |
Description |
Interval |
E-value |
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
29-350 |
4.32e-154 |
|
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: 435.07 E-value: 4.32e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 29 LVVNTWPFKNATEAvsvislrgdifatqrktvtAWWTLVSGGSALDAVEKGCAMCEKEQCGGTVGFGGSPDEVGETTLDA 108
Cdd:cd04513 1 LVINTWNFTEAVEA-------------------AWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 109 MIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHSDWLSRNCQPNYWR 188
Cdd:cd04513 62 AIMDGDTMDVGAVAALRRIKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 189 NVIPDPSKYCgpykppDFLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDM 268
Cdd:cd04513 142 NVVPDPSKSC------SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 269 AGAAAATGDGDTLLRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYPK-FFGAVICANVTGSYGAACNRlptfTQFSFM 347
Cdd:cd04513 216 VGAAAATGDGDIMMRFLPSYQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAACNG----EGFSYA 291
|
...
gi 564389084 348 VYN 350
Cdd:cd04513 292 VRT 294
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
61-336 |
3.46e-93 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 280.62 E-value: 3.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 61 TAWWTLVSGGSALDAVEKGCAMCEkEQCGGTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEH 140
Cdd:pfam01112 31 AGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLARAVMEK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 141 TTHTLLVGDSATKFAVSMGFT---SEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPSKYCGPYKppdfleqnnrahkev 217
Cdd:pfam01112 110 TPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK--------------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 218 dihsHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEYMRGG 297
Cdd:pfam01112 175 ----RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYDIVARMEYG 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 564389084 298 DDPARACQKVISRIQKYYPKfFGAVICANVTGSYGAACN 336
Cdd:pfam01112 251 LSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFN 288
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
61-339 |
5.85e-54 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 224363 Cd Length: 307 Bit Score: 179.86 E-value: 5.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 61 TAWWTLVSGGSALDAVEKGCAMCEKeqCGGT-VGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLE 139
Cdd:COG1446 33 AGYQLLSAGGSALDAVVEAVRVLED--SPLFnAGTGSVLNIDGKVEMDASIMDGATLRAGAVAAVEGVKNPILAARAVME 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 140 HTTHTLLVGDSATKFAVSMGF-TSEDLSTNTSRALHSDWLSRNcqpnywRNVIPDPSKycgpykppdfleqnNRAHKEVD 218
Cdd:COG1446 111 KTPHVLLVGEGAVAFAREMGLpREYDPFTEERRAEWLQAERDA------KKQVLDHSK--------------TYEEPEDP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 219 IHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEYMRGGD 298
Cdd:COG1446 171 DSKHGTVGAVALDADGNLAAATSTGGVFLKRPGRVGDSPIPGAGFYAENGAGAVSCTGVGEVIIRNALAFDIAARVRYGL 250
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 564389084 299 DPARACQKVISRIQKYYPKFFGAvICANVTGSYGAACNRLP 339
Cdd:COG1446 251 SLDAACERVVEEALKALGGDGGL-IAVDAKGNVAAAFNTKG 290
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
66-262 |
3.28e-25 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 104.02 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 66 LVSGGSALDAVE---------------KGCAMCEKeqcgGTVgfggspdevgetTLDAMIMDGTAMDVGAVGGLRRIKNA 130
Cdd:PLN02689 42 LRSSLPALDVVElvvrelendplfnagRGSVLTED----GTV------------EMEASIMDGRTRRCGAVSGLTTVVNP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 131 IGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHsDWLSRNCQPNywrNVIPDpskycgpYKPPDFLEQN 210
Cdd:PLN02689 106 ISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENV-ERLKQAKEAN---SVQFD-------YRIPLDKPAK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564389084 211 NRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 262
Cdd:PLN02689 175 AAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAG 226
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
29-350 |
4.32e-154 |
|
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: 435.07 E-value: 4.32e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 29 LVVNTWPFKNATEAvsvislrgdifatqrktvtAWWTLVSGGSALDAVEKGCAMCEKEQCGGTVGFGGSPDEVGETTLDA 108
Cdd:cd04513 1 LVINTWNFTEAVEA-------------------AWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 109 MIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHSDWLSRNCQPNYWR 188
Cdd:cd04513 62 AIMDGDTMDVGAVAALRRIKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 189 NVIPDPSKYCgpykppDFLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDM 268
Cdd:cd04513 142 NVVPDPSKSC------SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 269 AGAAAATGDGDTLLRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYPK-FFGAVICANVTGSYGAACNRlptfTQFSFM 347
Cdd:cd04513 216 VGAAAATGDGDIMMRFLPSYQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAACNG----EGFSYA 291
|
...
gi 564389084 348 VYN 350
Cdd:cd04513 292 VRT 294
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
61-336 |
3.46e-93 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 280.62 E-value: 3.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 61 TAWWTLVSGGSALDAVEKGCAMCEkEQCGGTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEH 140
Cdd:pfam01112 31 AGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLARAVMEK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 141 TTHTLLVGDSATKFAVSMGFT---SEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPSKYCGPYKppdfleqnnrahkev 217
Cdd:pfam01112 110 TPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK--------------- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 218 dihsHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEYMRGG 297
Cdd:pfam01112 175 ----RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYDIVARMEYG 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 564389084 298 DDPARACQKVISRIQKYYPKfFGAVICANVTGSYGAACN 336
Cdd:pfam01112 251 LSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFN 288
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
61-339 |
5.85e-54 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 224363 Cd Length: 307 Bit Score: 179.86 E-value: 5.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 61 TAWWTLVSGGSALDAVEKGCAMCEKeqCGGT-VGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLE 139
Cdd:COG1446 33 AGYQLLSAGGSALDAVVEAVRVLED--SPLFnAGTGSVLNIDGKVEMDASIMDGATLRAGAVAAVEGVKNPILAARAVME 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 140 HTTHTLLVGDSATKFAVSMGF-TSEDLSTNTSRALHSDWLSRNcqpnywRNVIPDPSKycgpykppdfleqnNRAHKEVD 218
Cdd:COG1446 111 KTPHVLLVGEGAVAFAREMGLpREYDPFTEERRAEWLQAERDA------KKQVLDHSK--------------TYEEPEDP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 219 IHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEYMRGGD 298
Cdd:COG1446 171 DSKHGTVGAVALDADGNLAAATSTGGVFLKRPGRVGDSPIPGAGFYAENGAGAVSCTGVGEVIIRNALAFDIAARVRYGL 250
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 564389084 299 DPARACQKVISRIQKYYPKFFGAvICANVTGSYGAACNRLP 339
Cdd:COG1446 251 SLDAACERVVEEALKALGGDGGL-IAVDAKGNVAAAFNTKG 290
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
61-336 |
5.98e-46 |
|
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: 157.34 E-value: 5.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 61 TAWWTLVSGGSALDAVEKGCAMCEKEqcgGT--VGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVL 138
Cdd:cd04512 29 AGREVLEKGGSALDAVEAAVRLLEDD---PLfnAGRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLARAVM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 139 EHTTHTLLVGDSATKFAVSMGftsedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnrahkevd 218
Cdd:cd04512 106 EKTPHVLLVGEGAERFAREHG----------------------------------------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 219 ihsHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEYMRGGD 298
Cdd:cd04512 127 ---HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLVEFGG 203
|
250 260 270
....*....|....*....|....*....|....*...
gi 564389084 299 DPARACQKVISRIqKYYPKFFGAVICANVTGSYGAACN 336
Cdd:cd04512 204 SAQEAAEAAIDYL-RRRVGGEGGLIVVDPDGRLGAAHN 240
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
57-336 |
4.14e-38 |
|
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: 136.94 E-value: 4.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 57 RKTVTAWWTLVSGGSALDAVEKGCAMCEKEqcgG--TVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVA 134
Cdd:cd14950 25 REALERGYEALRRGSALEAVVEAVAYMEDS---GvfNAGVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIRLA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 135 RKVLEHTTHTLLVGDSATKFAVSMGFtsedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnrah 214
Cdd:cd14950 102 RKVMEKTDHVLIVGEGADELAKRLGG------------------------------------------------------ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 215 kevdihshDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGaYADDMAGAAAATGDGDTLLRFLPSYQAVEYM 294
Cdd:cd14950 128 --------DTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAG-FYATNGVAVSATGIGEVIIRSLPALRADELV 198
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 564389084 295 RGGDDPARACQKVISRIQKYYPKFFGAVICANVTGSYGAACN 336
Cdd:cd14950 199 SMGGDIEEAVRAVVNKVTETFGKDTAGIIGIDARGNIAAAFN 240
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
66-262 |
2.00e-35 |
|
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: 130.77 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 66 LVSGGSALDAVEKGCAMCEKEQCGGTvGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTHTL 145
Cdd:cd04702 36 LKAGGSALDAVEAAVRALEDDPVFNA-GYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 146 LVGDSATKFAVSMGFT---SEDLSTNTSRALHSDWLSRNCQPNywrnvipdpsKYCGpykppdfleqnnrahkevdiHSH 222
Cdd:cd04702 115 LTGRGANKFAEEMGIPqvpPESLVTERARERLEKFKKEKGANV----------EDTQ--------------------RGH 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564389084 223 DTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 262
Cdd:cd04702 165 GTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSG 204
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
66-262 |
9.36e-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: 114.87 E-value: 9.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 66 LVSGGSALDAVEKgcAMCEKEQCG-GTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTHT 144
Cdd:cd04701 39 LASGGSALDAVTA--AVRLLEDCPlFNAGKGAVFTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 145 LLVGDSATKFAVSMGftsedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnrahkeVDIHSHDT 224
Cdd:cd04701 117 LLSGEGAEEFAREQG---------------------------------------------------------LELVPQGT 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 564389084 225 IGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 262
Cdd:cd04701 140 VGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAG 177
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
66-337 |
2.66e-25 |
|
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: 102.34 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 66 LVSGGSALDAVEKGCAMCEKEQC--GGTvgfGGSPDEVGETTLDAMIMDGTAmDVGAVGGLRRIKNAIGVARKVLEHTTH 143
Cdd:cd04703 30 LQNGGDALDAVVAAVRVLEDDPRfnAGT---GSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVARAVMETSPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 144 TLLVGDSATKFAVSMGFTsedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnrahkevdiHSHD 223
Cdd:cd04703 106 VLLAGDGAVRFARRLGYP----------------------------------------------------------DGCD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 224 TIGMVV-IHktGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLpSYQAVEYMRGGDDPAR 302
Cdd:cd04703 128 TVGAVArDG--GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKGAVAATGIGEEIAKRLL-ARRVYRWIETGLSLQA 204
|
250 260 270
....*....|....*....|....*....|....*
gi 564389084 303 ACQKVISRIQKYYPkffGAVICANVTGSYGAACNR 337
Cdd:cd04703 205 AAQRAIDEFDDGVA---VGVIAVSRRGEAGIASNT 236
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
66-262 |
3.28e-25 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 104.02 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 66 LVSGGSALDAVE---------------KGCAMCEKeqcgGTVgfggspdevgetTLDAMIMDGTAMDVGAVGGLRRIKNA 130
Cdd:PLN02689 42 LRSSLPALDVVElvvrelendplfnagRGSVLTED----GTV------------EMEASIMDGRTRRCGAVSGLTTVVNP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 131 IGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHsDWLSRNCQPNywrNVIPDpskycgpYKPPDFLEQN 210
Cdd:PLN02689 106 ISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENV-ERLKQAKEAN---SVQFD-------YRIPLDKPAK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564389084 211 NRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 262
Cdd:PLN02689 175 AAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAG 226
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
66-308 |
3.45e-25 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 103.88 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 66 LVSGGSALDAVEKGCAMCEkeQC---GGTVGFGGSPDEVGEttLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTT 142
Cdd:PRK10226 43 LEAGESALDVVTEAVRLLE--ECplfNAGIGAVFTRDETHE--LDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 143 HTLLVGDSATKFAVSMGFTSedlstntsralhsdwlsrncqpnywrnviPDPSKYCGPYKPPDFLEQNNRAHKEVDiHSH 222
Cdd:PRK10226 119 HVMMIGEGAENFAFAHGMER-----------------------------VSPEIFSTPLRYEQLLAARAEGATVLD-HSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 223 ---------DTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEY 293
Cdd:PRK10226 169 apldekqkmGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAAL 248
|
250
....*....|....*.
gi 564389084 294 MR-GGDDPARACQKVI 308
Cdd:PRK10226 249 MDyGGLSLAEACERVV 264
|
|
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
66-262 |
2.19e-19 |
|
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: 87.33 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 66 LVSGGSALDAVEKGCAMCEKEQCGGTvGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTH-- 143
Cdd:cd04514 35 LKAGGSALDAVEAAIKVLEDSPLTNA-GYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKEQRKpl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 144 -------TLLVGDSATKFAVSMGFTSedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnrahke 216
Cdd:cd04514 114 slgrvppMFLVGEGAREWAKSKGIIT------------------------------------------------------ 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564389084 217 vdihshDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 262
Cdd:cd04514 140 ------DTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAG 179
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
60-262 |
3.27e-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: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 60 VTAWWTLVSGGSALDAVEKGCAMCEKEQC--GGTvgfgGS---PDevGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVA 134
Cdd:cd14949 31 VEEVYEYLKSHSALEAVVYAVSLLEDDPLfnAGT----GSqiqSD--GQIRMSASLMDGQTQRFSGVINIENVKNPIEVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 135 RKVLEHTtHTLLVGDSATKFAVSMGFtsedlstntsralhsdwlsrncqpnywrnvipdpskycGPYKPPDFLEQNNRAH 214
Cdd:cd14949 105 QKLQQED-DRVLSGEGATEFARENGF--------------------------------------PEYNPETPQRRQEYEE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564389084 215 KEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPgAG 262
Cdd:cd14949 146 KKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AG 192
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
70-262 |
3.23e-12 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 67.20 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 70 GSALDAVEKGCAMCEKEQCGgTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTH------ 143
Cdd:PLN02937 51 GGCIDAVSAAIQVLEDDPST-NAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMgssllg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 144 ----TLLVGDSATKFAVSMGFtseDLSTNTSRALHsdWLSRNCQPNYWR-------NVIP-------DPSKYCGPYKPPD 205
Cdd:PLN02937 130 rippMFLVGEGARQWAKSKGI---DLPETVEEAEK--WLVTERAKEQWKkyktmlaSAIAksscdsqSTSKLSELEAPRS 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564389084 206 FLEQNNRAHKEVDIHSH------DTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 262
Cdd:PLN02937 205 NPSNGTGGGQSSMCTASdedcimDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSG 267
|
|
|