|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
2-393 |
0e+00 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 663.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 2 MAGDGADQSRRFFVAVHVGAGYHAAANEKALRSVMRRACLAASTILRQDSGECIDAVSAAIQVLEDDPSTNAGRGSNLTE 81
Cdd:PLN02937 1 MAGDGADQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCIDAVSAAIQVLEDDPSTNAGRGSNLTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 82 DGHVECDASLMDGDSGMFGGVGAVPD-----QVSEMLSKLLLCWLL----------VGEGARRWGKSKSVLIPGTVTEAD 146
Cdd:PLN02937 81 DGHVECDASIMDGDSGAFGAVGAVPGvrnaiQIAALLAKEQMMGSSllgrippmflVGEGARQWAKSKGIDLPETVEEAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 147 QWLVTERARNQWRRFKAMLSEVGAK--------SILSAEEHPRGTENNETCEENVSSCAAADEDKIMDTVGVICVDNEGH 218
Cdd:PLN02937 161 KWLVTERAKEQWKKYKTMLASAIAKsscdsqstSKLSELEAPRSNPSNGTGGGQSSMCTASDEDCIMDTVGVICVDSEGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 219 IACGSSSGGIAMKISGRVGLAATYGSGCWASSKGPFGAPFLVGCCVSGAGEYLMRGFAARECCTSLALSQAGPASAAMKV 298
Cdd:PLN02937 241 IASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGAPFIVGCCVSGAGEYLMRGFAARECCVSSSLSQAGPASACMKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 299 LRSVMHQESSKigTADKTAGILVVQADASVVVPGSKPELNAVEIAAAYSSLSFGVGYYGNSIEKPKISILRTRRQMSEAG 378
Cdd:PLN02937 321 LRSVIQGSSAK--TTDKDAGILLVQADASVMAPGNSPSLKAVEIAAAYSSLSFGIGYFGSSMERPKVSILRSTKQQSKTG 398
|
410
....*....|....*
gi 334186248 379 VDHFEARIDLRPTCC 393
Cdd:PLN02937 399 IDHFEARIDLSAKCS 413
|
|
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
13-389 |
1.44e-99 |
|
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: 298.42 E-value: 1.44e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 13 FFVAVHVGAGYHAAANEKALRSVMRRACLAASTILRqDSGECIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASLM 92
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLK-AGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 93 DGDSGMFGGVGAVPD-----QVSEMLSKLLLCWLL---------VGEGARRWGKSKSVlipgtvteadqwlvterarnqw 158
Cdd:cd04514 80 DGSSGRFGAVGAVSGvknpiQLARLLLKEQRKPLSlgrvppmflVGEGAREWAKSKGI---------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 159 rrfkamlsevgaksilsaeehprgtennetceenvsscaaadedkIMDTVGVICVDNEGHIACGSSSGGIAMKISGRVGL 238
Cdd:cd04514 138 ---------------------------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGP 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 239 AATYGSGCWASSKGPFgAPFLVGCCVSGAGEYLMRGFAARECCTSLALSQAGPASAAMKVLRSVMHQESSKIGTadktaG 318
Cdd:cd04514 173 AALYGAGCWAEPRDPD-DKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREESDEDEILRSFIESDFMGHPG-----V 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334186248 319 ILVVQADASVVVPgSKPELNAVEIAAAYSSLSFGVGYYGNSIEKPKISILRTRRqmsEAGVDHFEARIDLR 389
Cdd:cd04514 247 KNSPSAGAIGVLA-VKKTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPG---NGSIAQGGRKIRLR 313
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
10-300 |
2.02e-38 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 139.86 E-value: 2.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 10 SRRFFVAVHVGAGYHAAAN-----EKALRSVMRRACLAASTILrQDSGECIDAVSAAIQVLEDDPSTNAGRGSNLTEDGH 84
Cdd:COG1446 3 MSRRALIIHGGAGTIARSAmtpevEAAYRAGLRAALEAGYAVL-EAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 85 VECDASLMDGDSGMFGGVGAV-----PDQVSEMLSKLLLCWLLVGEGARRWGKSKsvlipGTVTEADQWLVTERARNQWR 159
Cdd:COG1446 82 VELDASIMDGATLRAGAVAGVtriknPISLARAVMEKTPHVLLVGEGAERFAREQ-----GLELVDPLYFFTEKRWKQWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 160 RFKAMlsevgaksilsaeehprgtennetceenvsscAAADEDKIMDTVGVICVDNEGHIACGSSSGGIAMKISGRVGLA 239
Cdd:COG1446 157 KALEY--------------------------------KPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDS 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186248 240 ATYGSGCWASSKgpFGApflVGCcvSGAGEYLMRGFAARECCtslALSQAG--PASAAMKVLR 300
Cdd:COG1446 205 PIIGAGTYADNE--VGA---VSA--TGHGEYFIRTVVAHDIV---ERMRQGlsLQEAAEEVIE 257
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
15-299 |
3.80e-36 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 133.86 E-value: 3.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 15 VAVHVGAGY--HAAANEKALRSVMRRACLAASTILRqDSGECIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASLM 92
Cdd:pfam01112 2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLA-AGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 93 DGDSGMFGGVGAV-----PDQVSEMLSKLLLCWLLVGEGARRWGKSKSVlipGTVTEADqwLVTERARNQWRRFKAmlse 167
Cdd:pfam01112 81 DGKTLRAGAVAGVsriknPISLARAVMEKTPHVMLSGEGAEQFAREMGL---ERVPPED--FLTEERLQELQKARK---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 168 vgaksilsaeehprgTENNETCEENVS-SCAAADEDKIMDTVGVICVDNEGHIACGSSSGGIAMKISGRVGLAATYGSGC 246
Cdd:pfam01112 152 ---------------ENFQPNMALNVApDPLKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGT 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 334186248 247 WASSKgpFGApflVGCcvSGAGEYLMRGFAARECCTSLALSQAgPASAAMKVL 299
Cdd:pfam01112 217 YADNA--TGA---VSA--TGHGEDIIRETLAYDIVARMEYGLS-LEEAADKVI 261
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02937 |
PLN02937 |
Putative isoaspartyl peptidase/L-asparaginase |
2-393 |
0e+00 |
|
Putative isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215506 [Multi-domain] Cd Length: 414 Bit Score: 663.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 2 MAGDGADQSRRFFVAVHVGAGYHAAANEKALRSVMRRACLAASTILRQDSGECIDAVSAAIQVLEDDPSTNAGRGSNLTE 81
Cdd:PLN02937 1 MAGDGADQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCIDAVSAAIQVLEDDPSTNAGRGSNLTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 82 DGHVECDASLMDGDSGMFGGVGAVPD-----QVSEMLSKLLLCWLL----------VGEGARRWGKSKSVLIPGTVTEAD 146
Cdd:PLN02937 81 DGHVECDASIMDGDSGAFGAVGAVPGvrnaiQIAALLAKEQMMGSSllgrippmflVGEGARQWAKSKGIDLPETVEEAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 147 QWLVTERARNQWRRFKAMLSEVGAK--------SILSAEEHPRGTENNETCEENVSSCAAADEDKIMDTVGVICVDNEGH 218
Cdd:PLN02937 161 KWLVTERAKEQWKKYKTMLASAIAKsscdsqstSKLSELEAPRSNPSNGTGGGQSSMCTASDEDCIMDTVGVICVDSEGN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 219 IACGSSSGGIAMKISGRVGLAATYGSGCWASSKGPFGAPFLVGCCVSGAGEYLMRGFAARECCTSLALSQAGPASAAMKV 298
Cdd:PLN02937 241 IASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGAPFIVGCCVSGAGEYLMRGFAARECCVSSSLSQAGPASACMKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 299 LRSVMHQESSKigTADKTAGILVVQADASVVVPGSKPELNAVEIAAAYSSLSFGVGYYGNSIEKPKISILRTRRQMSEAG 378
Cdd:PLN02937 321 LRSVIQGSSAK--TTDKDAGILLVQADASVMAPGNSPSLKAVEIAAAYSSLSFGIGYFGSSMERPKVSILRSTKQQSKTG 398
|
410
....*....|....*
gi 334186248 379 VDHFEARIDLRPTCC 393
Cdd:PLN02937 399 IDHFEARIDLSAKCS 413
|
|
| Taspase1_like |
cd04514 |
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ... |
13-389 |
1.44e-99 |
|
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: 298.42 E-value: 1.44e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 13 FFVAVHVGAGYHAAANEKALRSVMRRACLAASTILRqDSGECIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASLM 92
Cdd:cd04514 1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLK-AGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 93 DGDSGMFGGVGAVPD-----QVSEMLSKLLLCWLL---------VGEGARRWGKSKSVlipgtvteadqwlvterarnqw 158
Cdd:cd04514 80 DGSSGRFGAVGAVSGvknpiQLARLLLKEQRKPLSlgrvppmflVGEGAREWAKSKGI---------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 159 rrfkamlsevgaksilsaeehprgtennetceenvsscaaadedkIMDTVGVICVDNEGHIACGSSSGGIAMKISGRVGL 238
Cdd:cd04514 138 ---------------------------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGP 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 239 AATYGSGCWASSKGPFgAPFLVGCCVSGAGEYLMRGFAARECCTSLALSQAGPASAAMKVLRSVMHQESSKIGTadktaG 318
Cdd:cd04514 173 AALYGAGCWAEPRDPD-DKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREESDEDEILRSFIESDFMGHPG-----V 246
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334186248 319 ILVVQADASVVVPgSKPELNAVEIAAAYSSLSFGVGYYGNSIEKPKISILRTRRqmsEAGVDHFEARIDLR 389
Cdd:cd04514 247 KNSPSAGAIGVLA-VKKTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPG---NGSIAQGGRKIRLR 313
|
|
| IaaA |
COG1446 |
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ... |
10-300 |
2.02e-38 |
|
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];
Pssm-ID: 441055 Cd Length: 305 Bit Score: 139.86 E-value: 2.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 10 SRRFFVAVHVGAGYHAAAN-----EKALRSVMRRACLAASTILrQDSGECIDAVSAAIQVLEDDPSTNAGRGSNLTEDGH 84
Cdd:COG1446 3 MSRRALIIHGGAGTIARSAmtpevEAAYRAGLRAALEAGYAVL-EAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 85 VECDASLMDGDSGMFGGVGAV-----PDQVSEMLSKLLLCWLLVGEGARRWGKSKsvlipGTVTEADQWLVTERARNQWR 159
Cdd:COG1446 82 VELDASIMDGATLRAGAVAGVtriknPISLARAVMEKTPHVLLVGEGAERFAREQ-----GLELVDPLYFFTEKRWKQWK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 160 RFKAMlsevgaksilsaeehprgtennetceenvsscAAADEDKIMDTVGVICVDNEGHIACGSSSGGIAMKISGRVGLA 239
Cdd:COG1446 157 KALEY--------------------------------KPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDS 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186248 240 ATYGSGCWASSKgpFGApflVGCcvSGAGEYLMRGFAARECCtslALSQAG--PASAAMKVLR 300
Cdd:COG1446 205 PIIGAGTYADNE--VGA---VSA--TGHGEYFIRTVVAHDIV---ERMRQGlsLQEAAEEVIE 257
|
|
| Asparaginase_2 |
pfam01112 |
Asparaginase; |
15-299 |
3.80e-36 |
|
Asparaginase;
Pssm-ID: 426055 Cd Length: 308 Bit Score: 133.86 E-value: 3.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 15 VAVHVGAGY--HAAANEKALRSVMRRACLAASTILRqDSGECIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASLM 92
Cdd:pfam01112 2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLA-AGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 93 DGDSGMFGGVGAV-----PDQVSEMLSKLLLCWLLVGEGARRWGKSKSVlipGTVTEADqwLVTERARNQWRRFKAmlse 167
Cdd:pfam01112 81 DGKTLRAGAVAGVsriknPISLARAVMEKTPHVMLSGEGAEQFAREMGL---ERVPPED--FLTEERLQELQKARK---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 168 vgaksilsaeehprgTENNETCEENVS-SCAAADEDKIMDTVGVICVDNEGHIACGSSSGGIAMKISGRVGLAATYGSGC 246
Cdd:pfam01112 152 ---------------ENFQPNMALNVApDPLKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGT 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 334186248 247 WASSKgpFGApflVGCcvSGAGEYLMRGFAARECCTSLALSQAgPASAAMKVL 299
Cdd:pfam01112 217 YADNA--TGA---VSA--TGHGEDIIRETLAYDIVARMEYGLS-LEEAADKVI 261
|
|
| Ntn_Asparaginase_2_like |
cd04512 |
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ... |
15-356 |
8.27e-35 |
|
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: 128.84 E-value: 8.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 15 VAVHVGAGYHAAANEKALRSVMRRACLAASTILRQdSGECIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASLMDG 94
Cdd:cd04512 2 LIVHGGAGTIEDEDAEAYREGLLRALEAGREVLEK-GGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIMDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 95 DSGMFGGVGAV-----PDQVSEMLSKLLLCWLLVGEGARRWgksksvlipgtvteadqwlvterarnqwrrfkamlsevg 169
Cdd:cd04512 81 KTLNAGAVAGVkgvknPISLARAVMEKTPHVLLVGEGAERF--------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 170 aksilsAEEHprgtennetceenvsscaaadedkIMDTVGVICVDNEGHIACGSSSGGIAMKISGRVGLAATYGSGCWAS 249
Cdd:cd04512 122 ------AREH------------------------GHGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYAD 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 250 SKgpfgapfLVGCCVSGAGEYLMRGFAARECCTslALSQAGPA-SAAMKVLRSVmhqESSKIGtadkTAGILVVQADAsv 328
Cdd:cd04512 172 NE-------TGAVSATGHGESIIRTVLAKRIAD--LVEFGGSAqEAAEAAIDYL---RRRVGG----EGGLIVVDPDG-- 233
|
330 340
....*....|....*....|....*...
gi 334186248 329 vvpgskpelnavEIAAAYSSLSFGVGYY 356
Cdd:cd04512 234 ------------RLGAAHNTPGMAFAYI 249
|
|
| ASRGL1_like |
cd04702 |
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ... |
15-295 |
4.77e-30 |
|
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: 116.90 E-value: 4.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 15 VAVHVGAGYHAAANEKALRSVMRRACLAASTILRQdSGECIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASLMDG 94
Cdd:cd04702 4 IVVHGGAGSIPDDRIKGSREGVKRAARAGYSVLKA-GGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASIMDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 95 DSGMFGGVGAVPD-----QVSEMLSKLLLCWLLVGEGARRWGKSKsvlipGTVTEADQWLVTERARNQWRRFKAmlsEVG 169
Cdd:cd04702 83 KTLRAGAVSAVRNianpiSLARLVMEKTPHCFLTGRGANKFAEEM-----GIPQVPPESLVTERARERLEKFKK---EKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 170 AKSILSAEEHprgtennetceenvsscaaadedkimDTVGVICVDNEGHIACGSSSGGIAMKISGRVGLAATYGSGCWAS 249
Cdd:cd04702 155 ANVEDTQRGH--------------------------GTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYAD 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 334186248 250 SkgpfgapfLVGCC-VSGAGEYLMRGFAARecctsLALS---QAGPASAA 295
Cdd:cd04702 209 N--------LVGAVsTTGHGESIMKVNLAR-----LILFhmeQGKTAEEA 245
|
|
| Glycosylasparaginase |
cd04513 |
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ... |
37-303 |
5.16e-29 |
|
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: 114.20 E-value: 5.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 37 RRACLAASTILRQdSGECIDAVSAAIQVLEDDPS-TNAGRGSNLTEDGHVECDASLMDGDSGMFGGVGAVPD-----QVS 110
Cdd:cd04513 9 TEAVEAAWEVLQK-GGSALDAVEAGCSVCEDDQCdGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRiknaiSVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 111 EMLSKLLLCWLLVGEGARRWGKSKsvlipGTVTEAdqwLVTERARNQWRRFKamlsEVGAKSILSAEEHPRGTENNETCE 190
Cdd:cd04513 88 RAVMEHTPHSLLVGEGATEFAVSM-----GFKEEN---LLTEESRKMWKKWL----KENCQPNFWKNVVPDPSKSCSSPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 191 ENVSSCAAADEDkIMDTVGVICVDNEGHIACGSSSGGIAMKISGRVGLAATYGSGCWASSKgpFGApflvgCCVSGAGEY 270
Cdd:cd04513 156 APSRSESAIPED-NHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNE--VGA-----AAATGDGDI 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 334186248 271 LMRGfaareCCTSLALSQ----AGPASAAMKVLRSVM 303
Cdd:cd04513 228 MMRF-----LPSYQAVELmrqgMSPQEACEDAIRRIA 259
|
|
| Asparaginase_2 |
cd04701 |
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ... |
15-331 |
1.06e-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: 101.77 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 15 VAVHVGAGYHAAAN-----EKALRSVMRRACLAASTILRQdSGECIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDA 89
Cdd:cd04701 2 LAIHGGAGTISRANltperYAAYRAALRRALEAGYAVLAS-GGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 90 SLMDGDSGMFGGVGAVpdqvsemlsklllcwllvgegarrwgksKSVLIPGTVTEAdqwlVTERARNqwrrfkAMLSEVG 169
Cdd:cd04701 81 SIMDGRTKRAGAVAGL----------------------------RRVRNPILLARA----VLEKSPH------VLLSGEG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 170 AKSIlsAEEHprGtennetcEENVSscaaadedkiMDTVGVICVDNEGHIACGSSSGGIAMKISGRVGLAATYGSGCWAS 249
Cdd:cd04701 123 AEEF--AREQ--G-------LELVP----------QGTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAE 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 250 SKgpfgapflvGCCVS--GAGEYLMRGFAARECCtslALSQAGPASAAmKVLRSVMHQessKIGTADKTAGILVVQADAS 327
Cdd:cd04701 182 EW---------AVAVSgtGNGDSFIRVAAARDVA---ARMRYKGLSLA-EAAKEVVGP---GGELGEGEGGIIAIDARGN 245
|
....
gi 334186248 328 VVVP 331
Cdd:cd04701 246 VAMP 249
|
|
| Asparaginase_2_like_2 |
cd14950 |
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
15-324 |
1.44e-23 |
|
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: 98.42 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 15 VAVHVGAG-YHAAANEKALRSVMRRACLAASTILRqdSGECIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASLMD 93
Cdd:cd14950 2 LVVHGGAGsWKNSDDEEKALRALREALERGYEALR--RGSALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDAGIMD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 94 GDSGMFGGVGAVpdqvsemlsklllcwllvgegarrwgksksvlipgtvteadqwlvtERARNQWRRFKAMLSEvGAKSI 173
Cdd:cd14950 80 GRTLRVGAVAAV----------------------------------------------RAVKNPIRLARKVMEK-TDHVL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 174 LSAEEhprgtennetceenvsscaaADED---KIMDTVGVICVDNEGHIACGSSSGGIAMKISGRVGLAATYGSGCWASS 250
Cdd:cd14950 113 IVGEG--------------------ADELakrLGGDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATN 172
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334186248 251 KgpfgapflVGCCVSGAGEYLMRGFAARECCTslALSQAGPASAAmkvLRSVMHQESSKIGtaDKTAGILVVQA 324
Cdd:cd14950 173 G--------VAVSATGIGEVIIRSLPALRADE--LVSMGGDIEEA---VRAVVNKVTETFG--KDTAGIIGIDA 231
|
|
| PLN02689 |
PLN02689 |
Bifunctional isoaspartyl peptidase/L-asparaginase |
15-279 |
5.24e-23 |
|
Bifunctional isoaspartyl peptidase/L-asparaginase
Pssm-ID: 215372 Cd Length: 318 Bit Score: 98.24 E-value: 5.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 15 VAVHVGAGYHA----AANEKALRSVMRRaCLAASTILRQDSGECIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDAS 90
Cdd:PLN02689 6 IALHGGAGDIDpnlpRERQEEAEAALRR-CLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 91 LMDGDSGMFGGVGAV-----PDQVSEMLSKLLLCWLLVGEGARRWGKSKsvlipGTVTEADQWLVTERARNQWRRFKAml 165
Cdd:PLN02689 85 IMDGRTRRCGAVSGLttvvnPISLARLVMEKTPHIYLAFDGAEAFARQQ-----GVETVDNSYFITEENVERLKQAKE-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 166 sevgAKSILSAEEHPrgTENNETCeenvsSCAAADEDKIMDTVGVICVDNEGHIACGSSSGGIAMKISGRVGLAATYGSG 245
Cdd:PLN02689 158 ----ANSVQFDYRIP--LDKPAKA-----AALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAG 226
|
250 260 270
....*....|....*....|....*....|....
gi 334186248 246 CWAsskGPFGApflVGCcvSGAGEYLMRGFAARE 279
Cdd:PLN02689 227 TYA---NHLCA---VSA--TGKGEAIIRGTVARD 252
|
|
| PRK10226 |
PRK10226 |
isoaspartyl peptidase; Provisional |
15-331 |
2.65e-18 |
|
isoaspartyl peptidase; Provisional
Pssm-ID: 182319 Cd Length: 313 Bit Score: 84.62 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 15 VAVHVGAGYHAAAN---EKALRSVMRRACLAASTILRQDSGE-CIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDAS 90
Cdd:PRK10226 6 IAIHGGAGAISRAQmslQQELRYIEALSAIVETGQKMLEAGEsALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDAC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 91 LMDGDSGMFGGVGAV-----PDQVSEMLSKLLLCWLLVGEGARRWGKSKSVlipgtvteadqwlvtERARNQwrrfkaml 165
Cdd:PRK10226 86 VMDGNTLKAGAVAGVshlrnPVLAARLVMEQSPHVMMIGEGAENFAFAHGM---------------ERVSPE-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 166 sevgaksILSAEEHPRGTENNETCEENV--SSCAAADEDKIMDTVGVICVDNEGHIACGSSSGGIAMKISGRVGLAATYG 243
Cdd:PRK10226 143 -------IFSTPLRYEQLLAARAEGATVldHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 244 SGCWASSkgpfgAPFLVGCcvSGAGEYLMRGFAARECCtslALSQAGPASAAMKVLRSVMHqessKIGTADKTAGILVVQ 323
Cdd:PRK10226 216 AGCYANN-----ASVAVSC--TGTGEVFIRALAAYDIA---ALMDYGGLSLAEACERVVME----KLPALGGSGGLIAID 281
|
....*...
gi 334186248 324 ADASVVVP 331
Cdd:PRK10226 282 HEGNVALP 289
|
|
| Asparaginase_2_like_3 |
cd14949 |
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ... |
17-241 |
2.36e-14 |
|
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: 72.64 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 17 VHVGAGYHAAANEKALRsvMRRACLAAstILRQ-----DSGECIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASL 91
Cdd:cd14949 5 IHGGFGSESSTNGETKA--AKQEALAE--IVEEvyeylKSHSALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQIRMSASL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 92 MDGDSGMFGGVGAVPDqvsemlsklllcwllvgegarrwgksksVLIPgtvTEADQWLVTERARnqwrrfkaMLSEVGAK 171
Cdd:cd14949 81 MDGQTQRFSGVINIEN----------------------------VKNP---IEVAQKLQQEDDR--------VLSGEGAT 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 172 SILSAEEHPrgTENNETCEENVSSCAAADEDKIMDTVGVICVDNEGHIACGSSSGGIAMKISGRVGLAAT 241
Cdd:cd14949 122 EFARENGFP--EYNPETPQRRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSAT 189
|
|
| Asparaginase_2_like_1 |
cd04703 |
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ... |
15-299 |
2.64e-12 |
|
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: 66.13 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 15 VAVHVGAGYHAAANEKAlrsvmrRACLAASTILRQDSGECIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASLMDG 94
Cdd:cd04703 3 VLVHGGAGSDPERQDGL------ERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAVMTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 95 DsGMFGGVGAVPDqvsemlsklllcwllvgegarrwgksksVLIPGTVTEAdqwlVTERARNQwrrfkaMLSEVGAKSIL 174
Cdd:cd04703 77 G-GAFGAVAAIEG----------------------------VKNPVLVARA----VMETSPHV------LLAGDGAVRFA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186248 175 SAEEHPRGTennetceenvsscaaadedkimDTVGVICVDNeGHIACGSSSGGIAMKISGRVGLAATYGSGCWAsskGPF 254
Cdd:cd04703 118 RRLGYPDGC----------------------DTVGAVARDG-GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYA---GPK 171
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 334186248 255 GApflvgCCVSGAGEYLMRGFAARECCTSLAlSQAGPASAAMKVL 299
Cdd:cd04703 172 GA-----VAATGIGEEIAKRLLARRVYRWIE-TGLSLQAAAQRAI 210
|
|
| |
