|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
4-339 |
4.22e-98 |
|
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: 292.64 E-value: 4.22e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 4 GLVILHAGAGLYSGQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAGVMD 83
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 84 SESGLTASVACCNCCRHPSEACLYILNKRKVMSQHGLVPPAMLVGNGIEKLLLHSNIklvpeshlitersmktqikwkei 163
Cdd:cd04514 81 GSSGRFGAVGAVSGVKNPIQLARLLLKEQRKPLSLGRVPPMFLVGEGAREWAKSKGI----------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 164 lyqnpinlsSQDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIESFDNkSHSSTCAVATSGTGEHISNT 243
Cdd:cd04514 138 ---------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDP-DDKTSVAVVTSGTGEHIATT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 244 CFACRSSQ-LLVSEDNVVSSLNKLINDFHEHP---SATLYSDLQVGIIFAKVEtsNSHNKRIIFGLAHSSPDMVFGFMKG 319
Cdd:cd04514 208 MLARRCAErLYHSTRREESDEDEILRSFIESDfmgHPGVKNSPSAGAIGVLAV--KKTRSGVELYFAHNTDSFALASMSS 285
|
330 340
....*....|....*....|
gi 429242553 320 DHSKPTTEISRKGSKRSSVQ 339
Cdd:cd04514 286 SDRKPKCVMSRLPGNGSIAQ 305
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
6-246 |
9.82e-49 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 165.67 E-value: 9.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 6 VILHAGAG-----LYSGQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAG 80
Cdd:COG1446 8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 81 VMDSESGLTASVACCNCCRHPSEAClyilnkRKVM--SQHglvppAMLVGNGIEKLLLHSNIKLVPESHLITERSMKtqi 158
Cdd:COG1446 88 IMDGATLRAGAVAGVTRIKNPISLA------RAVMekTPH-----VLLVGEGAERFAREQGLELVDPLYFFTEKRWK--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 159 KWKEIL-YQNPINLSSQDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIesfDNKshssTCAVATSGTG 237
Cdd:COG1446 154 QWKKALeYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYA---DNE----VGAVSATGHG 226
|
....*....
gi 429242553 238 EHISNTCFA 246
Cdd:COG1446 227 EYFIRTVVA 235
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
6-246 |
2.14e-44 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 154.66 E-value: 2.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 6 VILHAGAG--LYSGQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAGVMD 83
Cdd:pfam01112 2 LVIHGGAGsiLRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIMD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 84 SESGLTASVACCNCCRHPseaclyILNKRKVMSQHglvPPAMLVGNGIEKLLLHSNIKLVPESHLITERSMKTQIKWKE- 162
Cdd:pfam01112 82 GKTLRAGAVAGVSRIKNP------ISLARAVMEKT---PHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKe 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 163 ----ILYQNPINLSSQ-------DTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIesfDNKshssTCAV 231
Cdd:pfam01112 153 nfqpNMALNVAPDPLKecgdskrGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYA---DNA----TGAV 225
|
250
....*....|....*
gi 429242553 232 ATSGTGEHISNTCFA 246
Cdd:pfam01112 226 SATGHGEDIIRETLA 240
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
6-345 |
2.87e-34 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 129.98 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 6 VILHAGAGLYSGQREIQAKKTCSDACKAAIQALKVGQ----SALSAAIQaakIMEDSPVTNAGVGSNLNIDGKVECEAGV 81
Cdd:PLN02937 14 VAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSggciDAVSAAIQ---VLEDDPSTNAGRGSNLTEDGHVECDASI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 82 MDSESGLTASVACCNCCRHPSE-ACLYILNKRKVMSQHGLVPPAMLVGNG-----IEKLLLHSNIKLVPESHLITERSMK 155
Cdd:PLN02937 91 MDGDSGAFGAVGAVPGVRNAIQiAALLAKEQMMGSSLLGRIPPMFLVGEGarqwaKSKGIDLPETVEEAEKWLVTERAKE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 156 TQIKWKEILY--------------------QNPINLSS------------------QDTIGVICVDKNGRIAVVSSSGGL 197
Cdd:PLN02937 171 QWKKYKTMLAsaiaksscdsqstsklseleAPRSNPSNgtgggqssmctasdedciMDTVGVICVDSEGNIASGASSGGI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 198 LLKPAGRIGSSPIPGHGFWIESFDNKSHSSTCAVATSGTGEHISNTCFA---CRSSQLLVSEDNVVSS--LNKLINDFHE 272
Cdd:PLN02937 251 AMKVSGRVGLAAMYGSGCWASSKGPFGAPFIVGCCVSGAGEYLMRGFAArecCVSSSLSQAGPASACMkvLRSVIQGSSA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 273 HPSAT------LYSDLQVGIIFAKVETsnshnKRIIFGLAHSSPDMVFGFMKGDHSKPTTEI--SRKGSKRSSVQLYAER 344
Cdd:PLN02937 331 KTTDKdagillVQADASVMAPGNSPSL-----KAVEIAAAYSSLSFGIGYFGSSMERPKVSIlrSTKQQSKTGIDHFEAR 405
|
.
gi 429242553 345 L 345
Cdd:PLN02937 406 I 406
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
4-339 |
4.22e-98 |
|
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: 292.64 E-value: 4.22e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 4 GLVILHAGAGLYSGQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAGVMD 83
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 84 SESGLTASVACCNCCRHPSEACLYILNKRKVMSQHGLVPPAMLVGNGIEKLLLHSNIklvpeshlitersmktqikwkei 163
Cdd:cd04514 81 GSSGRFGAVGAVSGVKNPIQLARLLLKEQRKPLSLGRVPPMFLVGEGAREWAKSKGI----------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 164 lyqnpinlsSQDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIESFDNkSHSSTCAVATSGTGEHISNT 243
Cdd:cd04514 138 ---------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDP-DDKTSVAVVTSGTGEHIATT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 244 CFACRSSQ-LLVSEDNVVSSLNKLINDFHEHP---SATLYSDLQVGIIFAKVEtsNSHNKRIIFGLAHSSPDMVFGFMKG 319
Cdd:cd04514 208 MLARRCAErLYHSTRREESDEDEILRSFIESDfmgHPGVKNSPSAGAIGVLAV--KKTRSGVELYFAHNTDSFALASMSS 285
|
330 340
....*....|....*....|
gi 429242553 320 DHSKPTTEISRKGSKRSSVQ 339
Cdd:cd04514 286 SDRKPKCVMSRLPGNGSIAQ 305
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
6-246 |
9.82e-49 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 165.67 E-value: 9.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 6 VILHAGAG-----LYSGQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAG 80
Cdd:COG1446 8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTVELDAS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 81 VMDSESGLTASVACCNCCRHPSEAClyilnkRKVM--SQHglvppAMLVGNGIEKLLLHSNIKLVPESHLITERSMKtqi 158
Cdd:COG1446 88 IMDGATLRAGAVAGVTRIKNPISLA------RAVMekTPH-----VLLVGEGAERFAREQGLELVDPLYFFTEKRWK--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 159 KWKEIL-YQNPINLSSQDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIesfDNKshssTCAVATSGTG 237
Cdd:COG1446 154 QWKKALeYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYA---DNE----VGAVSATGHG 226
|
....*....
gi 429242553 238 EHISNTCFA 246
Cdd:COG1446 227 EYFIRTVVA 235
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
5-317 |
1.36e-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: 163.51 E-value: 1.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 5 LVILHAGAGLYSGQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAGVMDS 84
Cdd:cd04512 1 SLIVHGGAGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIMDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 85 ESGLTASVACCNCCRHPseaclyILNKRKVMSQhglVPPAMLVGNGIEKlllhsniklvpeshLITERSMktqikwkeil 164
Cdd:cd04512 81 KTLNAGAVAGVKGVKNP------ISLARAVMEK---TPHVLLVGEGAER--------------FAREHGH---------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 165 yqnpinlssqDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIesfDNkshsSTCAVATSGTGEHISNTC 244
Cdd:cd04512 128 ----------GTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYA---DN----ETGAVSATGHGESIIRTV 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429242553 245 FACRSSQLLVSEDNVVSSLNKLINDFHEHPSAtlysdlQVGIIFAkvetsnSHNKRIifGLAHSSPDMVFGFM 317
Cdd:cd04512 191 LAKRIADLVEFGGSAQEAAEAAIDYLRRRVGG------EGGLIVV------DPDGRL--GAAHNTPGMAFAYI 249
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
6-246 |
2.14e-44 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 154.66 E-value: 2.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 6 VILHAGAG--LYSGQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAGVMD 83
Cdd:pfam01112 2 LVIHGGAGsiLRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIMD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 84 SESGLTASVACCNCCRHPseaclyILNKRKVMSQHglvPPAMLVGNGIEKLLLHSNIKLVPESHLITERSMKTQIKWKE- 162
Cdd:pfam01112 82 GKTLRAGAVAGVSRIKNP------ISLARAVMEKT---PHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARKe 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 163 ----ILYQNPINLSSQ-------DTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIesfDNKshssTCAV 231
Cdd:pfam01112 153 nfqpNMALNVAPDPLKecgdskrGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYA---DNA----TGAV 225
|
250
....*....|....*
gi 429242553 232 ATSGTGEHISNTCFA 246
Cdd:pfam01112 226 SATGHGEDIIRETLA 240
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
6-287 |
1.14e-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: 137.71 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 6 VILHAGAGLYSGQREIQ-AKKTCSDACKAAIQALKVGqSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAGVMDS 84
Cdd:cd14950 2 LVVHGGAGSWKNSDDEEkALRALREALERGYEALRRG-SALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDAGIMDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 85 ESGLTASVACCNCCRHPseaclyILNKRKVMSQHGLVppaMLVGNGIEKLLLhsniklvpeshlitersmktqikwkeil 164
Cdd:cd14950 81 RTLRVGAVAAVRAVKNP------IRLARKVMEKTDHV---LIVGEGADELAK---------------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 165 yqnpinLSSQDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIEsfdnkshsSTCAVATSGTGEHISNTC 244
Cdd:cd14950 124 ------RLGGDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYAT--------NGVAVSATGIGEVIIRSL 189
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 429242553 245 FACRSSQLLVSEDNVVSSLNKLINDFHEhpsatLYSDLQVGII 287
Cdd:cd14950 190 PALRADELVSMGGDIEEAVRAVVNKVTE-----TFGKDTAGII 227
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
6-238 |
1.22e-38 |
|
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: 137.98 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 6 VILHAGAGLYS-----GQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAG 80
Cdd:cd04701 2 LAIHGGAGTISranltPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 81 VMDSESGLTASVACCNCCRHPSEAClyilnkRKVMSQHglvPPAMLVGNGIEKLLLHSNIKLVPeshlitersmktqikw 160
Cdd:cd04701 82 IMDGRTKRAGAVAGLRRVRNPILLA------RAVLEKS---PHVLLSGEGAEEFAREQGLELVP---------------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429242553 161 keilyqnpinlssQDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIEsfdnkshSSTCAVATSGTGE 238
Cdd:cd04701 137 -------------QGTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAE-------EWAVAVSGTGNGD 194
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
6-246 |
1.92e-37 |
|
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: 135.78 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 6 VILHAGAGLYSGQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAGVMDSE 85
Cdd:cd04702 4 IVVHGGAGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASIMDGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 86 SGLTASVACCNCCRHPseaclyILNKRKVMSQHglvPPAMLVGNGIEKLLLHSNIKLVPESHLITERSMKT-QIKWKEIL 164
Cdd:cd04702 84 TLRAGAVSAVRNIANP------ISLARLVMEKT---PHCFLTGRGANKFAEEMGIPQVPPESLVTERARERlEKFKKEKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 165 YQNPINLSSQDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIesfDNKSHsstcAVATSGTGEHISNTC 244
Cdd:cd04702 155 ANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYA---DNLVG----AVSTTGHGESIMKVN 227
|
..
gi 429242553 245 FA 246
Cdd:cd04702 228 LA 229
|
|
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
6-345 |
2.87e-34 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 129.98 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 6 VILHAGAGLYSGQREIQAKKTCSDACKAAIQALKVGQ----SALSAAIQaakIMEDSPVTNAGVGSNLNIDGKVECEAGV 81
Cdd:PLN02937 14 VAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSggciDAVSAAIQ---VLEDDPSTNAGRGSNLTEDGHVECDASI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 82 MDSESGLTASVACCNCCRHPSE-ACLYILNKRKVMSQHGLVPPAMLVGNG-----IEKLLLHSNIKLVPESHLITERSMK 155
Cdd:PLN02937 91 MDGDSGAFGAVGAVPGVRNAIQiAALLAKEQMMGSSLLGRIPPMFLVGEGarqwaKSKGIDLPETVEEAEKWLVTERAKE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 156 TQIKWKEILY--------------------QNPINLSS------------------QDTIGVICVDKNGRIAVVSSSGGL 197
Cdd:PLN02937 171 QWKKYKTMLAsaiaksscdsqstsklseleAPRSNPSNgtgggqssmctasdedciMDTVGVICVDSEGNIASGASSGGI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 198 LLKPAGRIGSSPIPGHGFWIESFDNKSHSSTCAVATSGTGEHISNTCFA---CRSSQLLVSEDNVVSS--LNKLINDFHE 272
Cdd:PLN02937 251 AMKVSGRVGLAAMYGSGCWASSKGPFGAPFIVGCCVSGAGEYLMRGFAArecCVSSSLSQAGPASACMkvLRSVIQGSSA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 273 HPSAT------LYSDLQVGIIFAKVETsnshnKRIIFGLAHSSPDMVFGFMKGDHSKPTTEI--SRKGSKRSSVQLYAER 344
Cdd:PLN02937 331 KTTDKdagillVQADASVMAPGNSPSL-----KAVEIAAAYSSLSFGIGYFGSSMERPKVSIlrSTKQQSKTGIDHFEAR 405
|
.
gi 429242553 345 L 345
Cdd:PLN02937 406 I 406
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
4-287 |
7.06e-32 |
|
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: 119.67 E-value: 7.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 4 GLVILHAGAGlysGQREIQAKktCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAGVMD 83
Cdd:cd04703 1 MAVLVHGGAG---SDPERQDG--LERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAVMT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 84 SeSGLTASVACCNCCRHPseaclyILNKRKVMSQhglVPPAMLVGNGIEKLLLHSNIklvPESHlitersmktqikwkei 163
Cdd:cd04703 76 S-GGAFGAVAAIEGVKNP------VLVARAVMET---SPHVLLAGDGAVRFARRLGY---PDGC---------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 164 lyqnpinlssqDTIGVICVDkNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIesfdnkshSSTCAVATSGTGEHISNT 243
Cdd:cd04703 127 -----------DTVGAVARD-GGKFAAAVSTGGTSPALRGRVGDVPIIGAGFYA--------GPKGAVAATGIGEEIAKR 186
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 429242553 244 CFACRSSQLLVSEDNVVSSLNKLINDFHEhpsatlysDLQVGII 287
Cdd:cd04703 187 LLARRVYRWIETGLSLQAAAQRAIDEFDD--------GVAVGVI 222
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
6-240 |
4.66e-31 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 119.43 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 6 VILHAGAGLYS----GQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAGV 81
Cdd:PLN02689 6 IALHGGAGDIDpnlpRERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEASI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 82 MDSESGLTASVACCNCCRHPseaclyILNKRKVMSQhglVPPAMLVGNGIEKLLLHSNIKLVPESHLITERSMKTQIKWK 161
Cdd:PLN02689 86 MDGRTRRCGAVSGLTTVVNP------ISLARLVMEK---TPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 162 E-----ILYQNPINL------------SSQDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIESFdnks 224
Cdd:PLN02689 157 EansvqFDYRIPLDKpakaaalaadgdAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYANHL---- 232
|
250
....*....|....*.
gi 429242553 225 hsstCAVATSGTGEHI 240
Cdd:PLN02689 233 ----CAVSATGKGEAI 244
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
1-238 |
4.61e-26 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 105.80 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 1 MSNGLVILHAGAGL-----YSGQREIQAKKTCSDACKAAIQALKVGQSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKV 75
Cdd:PRK10226 1 MGKAVIAIHGGAGAisraqMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 76 ECEAGVMDSESGLTASVACCNCCRHPseaclyILNKRKVMSQHglvPPAMLVGNGIEKLLL-HSNIKLVPESHLITERSM 154
Cdd:PRK10226 81 ELDACVMDGNTLKAGAVAGVSHLRNP------VLAARLVMEQS---PHVMMIGEGAENFAFaHGMERVSPEIFSTPLRYE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 155 KTQIKWKEILYQ-----NPINLSSQ-DTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWiesfdnkSHSST 228
Cdd:PRK10226 152 QLLAARAEGATVldhsgAPLDEKQKmGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCY-------ANNAS 224
|
250
....*....|
gi 429242553 229 CAVATSGTGE 238
Cdd:PRK10226 225 VAVSCTGTGE 234
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
29-238 |
4.15e-24 |
|
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: 99.94 E-value: 4.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 29 DACKAAIQALKVGQSALSAAIQAAKIMEDSP-VTNAGVGSNLNIDGKVECEAGVMDSESGLTASVACCNCCRHPSEACly 107
Cdd:cd04513 10 EAVEAAWEVLQKGGSALDAVEAGCSVCEDDQcDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVA-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 108 ilnkRKVM--SQHglvppAMLVGNGIEKLLLHSNiklVPESHLITERSMKTQIKWKEILYQNP----------------- 168
Cdd:cd04513 88 ----RAVMehTPH-----SLLVGEGATEFAVSMG---FKEENLLTEESRKMWKKWLKENCQPNfwknvvpdpskscsspk 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429242553 169 --------INLSSQDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFWIesfDNKshsSTCAVATsGTGE 238
Cdd:cd04513 156 apsrsesaIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYA---DNE---VGAAAAT-GDGD 226
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
6-248 |
7.90e-19 |
|
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: 84.97 E-value: 7.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 6 VILHAGAGLYSGQREiQAKKTCSDACKAAI----QALKVGqSALSAAIQAAKIMEDSPVTNAGVGSNLNIDGKVECEAGV 81
Cdd:cd14949 3 LIIHGGFGSESSTNG-ETKAAKQEALAEIVeevyEYLKSH-SALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQIRMSASL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 82 MDSESGLTASVACCNCCRHPSEAClYILNKR--KVMSQHGlvppamlvgngiEKLLLHSNiKLVPESHLITERsmktQIK 159
Cdd:cd14949 81 MDGQTQRFSGVINIENVKNPIEVA-QKLQQEddRVLSGEG------------ATEFAREN-GFPEYNPETPQR----RQE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429242553 160 WKEILYQNPInlssQDTIGVICVDKNGRIAVVSSSGGLLLKPAGRIGSSPIPGHGFwiesfdnksHSSTCAVATSGTGEH 239
Cdd:cd14949 143 YEEKKLKSGG----TGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATVAGNY---------ANAFAGVSCTGIGED 209
|
....*....
gi 429242553 240 ISNTCFACR 248
Cdd:cd14949 210 IVSEALAAK 218
|
|
| |
