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Conserved domains on  [gi|1046879704|ref|XP_017447248|]
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threonine aspartase 1 isoform X1 [Rattus norvegicus]

Protein Classification

threonine aspartase 1( domain architecture ID 10139957)

threonine aspartase 1 (also known as taspase-1) is protease which cleaves the mixed-lineage leukemia (MLL) and transcription factor (TF) IIA families of nuclear proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
42-434 5.35e-132

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: 382.78  E-value: 5.35e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGV 121
Cdd:cd04514     1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLE------------------DSPLTNAGY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 122 GSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPscp 201
Cdd:cd04514    63 GSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGII--- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 202 pstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRV 281
Cdd:cd04514   139 ------------------------------------------------TDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRV 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 282 GQAALYGCGCWAENTGAHNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLASEDG---V 357
Cdd:cd04514   171 GPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsP 250
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046879704 358 LGGVIVLRSCRcpsesdpsqdKQTLLVEFLWSHSTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 434
Cdd:cd04514   251 SAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
 
Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
42-434 5.35e-132

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: 382.78  E-value: 5.35e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGV 121
Cdd:cd04514     1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLE------------------DSPLTNAGY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 122 GSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPscp 201
Cdd:cd04514    63 GSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGII--- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 202 pstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRV 281
Cdd:cd04514   139 ------------------------------------------------TDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRV 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 282 GQAALYGCGCWAENTGAHNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLASEDG---V 357
Cdd:cd04514   171 GPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsP 250
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046879704 358 LGGVIVLRSCRcpsesdpsqdKQTLLVEFLWSHSTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 434
Cdd:cd04514   251 SAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
37-413 2.60e-80

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 254.02  E-value: 2.60e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALAT-DAVMAALVELEhlsalyplleaylvsivlDSP 115
Cdd:PLN02937    7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCiDAVSAAIQVLE------------------DDP 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 116 FTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDH 195
Cdd:PLN02937   69 STNAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 196 GIPScpPSTMT-------TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGA------------ 249
Cdd:PLN02937  149 GIDL--PETVEeaekwlvTERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedci 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 250 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEHLVRTILARECSHAL 328
Cdd:PLN02937  227 MDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSS 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 329 ---QAEDAHQA---LLETMQNkfiSSPFLASEDgvlGGVIVLRSCRcpSESDPSQDKQTLLVEFLWSHSTESMCVGYMSA 402
Cdd:PLN02937  307 slsQAGPASACmkvLRSVIQG---SSAKTTDKD---AGILLVQADA--SVMAPGNSPSLKAVEIAAAYSSLSFGIGYFGS 378
                         410
                  ....*....|.
gi 1046879704 403 QDGKAKTHISR 413
Cdd:PLN02937  379 SMERPKVSILR 389
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
44-411 2.69e-62

Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];


Pssm-ID: 441055  Cd Length: 305  Bit Score: 203.80  E-value: 2.69e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTN 118
Cdd:COG1446     8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLE------------------DDPLFN 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 119 AGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIP 198
Cdd:COG1446    70 AGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 199 SCPPSTmttrfslaaFKRNKRKLelaervetdfiQLKRRRQSSAKENDSGaLDTVGAVVVDHEGNVAAAVSSGGLALKHP 278
Cdd:COG1446   140 LVDPLY---------FFTEKRWK-----------QWKKALEYKPIINERK-HGTVGAVALDANGNLAAATSTGGMTNKRP 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 279 GRVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspflASEDGV 357
Cdd:COG1446   199 GRVGDSPIIGAGTYADNEVG------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI-------LKKLGG 265
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046879704 358 LGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSAqDGKAKTHI 411
Cdd:COG1446   266 DGGLIAV-------------DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
Asparaginase_2 pfam01112
Asparaginase;
44-402 2.13e-55

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 185.87  E-value: 2.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGV 121
Cdd:pfam01112   2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLE------------------DDPLFNAGK 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 122 GSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCP 201
Cdd:pfam01112  64 GSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVP 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 202 PSTMTTRFSLAAFKRNKrklelaervETDFIQLKRRRQSSA--KENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPG 279
Cdd:pfam01112 134 PEDFLTEERLQELQKAR---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPG 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 280 RVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflased 355
Cdd:pfam01112 205 RVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV---------- 268
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1046879704 356 GVLGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSA 402
Cdd:pfam01112 269 GGDGGVIAV-------------DAKG---NIAAPFNTEGMYRAYHTG 299
 
Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
42-434 5.35e-132

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: 382.78  E-value: 5.35e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGV 121
Cdd:cd04514     1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLE------------------DSPLTNAGY 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 122 GSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHGIPscp 201
Cdd:cd04514    63 GSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKGII--- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 202 pstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRV 281
Cdd:cd04514   139 ------------------------------------------------TDTVGAIAIDLYGNIAAGSSSGGIGLKHPGRV 170
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 282 GQAALYGCGCWAENTGAHNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLASEDG---V 357
Cdd:cd04514   171 GPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPGVknsP 250
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046879704 358 LGGVIVLRSCRcpsesdpsqdKQTLLVEFLWSHSTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCRLE 434
Cdd:cd04514   251 SAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIRLR 313
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
44-400 3.02e-88

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: 268.67  E-value: 3.02e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGVGS 123
Cdd:cd04512     2 LIVHGGAGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLE------------------DDPLFNAGRGS 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 124 NLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscpps 203
Cdd:cd04512    64 VLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLARAVMEKT----------PHVLLVGEGAERFAREHG------- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 204 tmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQ 283
Cdd:cd04512   127 ----------------------------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGD 160
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 284 AALYGCGCWAENTgahnpySTAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKfisspfLASEDGVLGGVIV 363
Cdd:cd04512   161 SPIIGAGTYADNE------TGAVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAEAAIDY------LRRRVGGEGGLIV 228
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1046879704 364 LrscrcpsesdpsqDKQtllVEFLWSHSTESMCVGYM 400
Cdd:cd04512   229 V-------------DPD---GRLGAAHNTPGMAFAYI 249
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
37-413 2.60e-80

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 254.02  E-value: 2.60e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALAT-DAVMAALVELEhlsalyplleaylvsivlDSP 115
Cdd:PLN02937    7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGSGGCiDAVSAAIQVLE------------------DDP 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 116 FTNAGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRWAVDH 195
Cdd:PLN02937   69 STNAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQWAKSK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 196 GIPScpPSTMT-------TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGA------------ 249
Cdd:PLN02937  149 GIDL--PETVEeaekwlvTERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasdedci 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 250 LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAHN-PYSTAVSTSGCGEHLVRTILARECSHAL 328
Cdd:PLN02937  227 MDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAARECCVSS 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 329 ---QAEDAHQA---LLETMQNkfiSSPFLASEDgvlGGVIVLRSCRcpSESDPSQDKQTLLVEFLWSHSTESMCVGYMSA 402
Cdd:PLN02937  307 slsQAGPASACmkvLRSVIQG---SSAKTTDKD---AGILLVQADA--SVMAPGNSPSLKAVEIAAAYSSLSFGIGYFGS 378
                         410
                  ....*....|.
gi 1046879704 403 QDGKAKTHISR 413
Cdd:PLN02937  379 SMERPKVSILR 389
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
44-411 2.69e-62

Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and metabolism];


Pssm-ID: 441055  Cd Length: 305  Bit Score: 203.80  E-value: 2.69e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTN 118
Cdd:COG1446     8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLE------------------DDPLFN 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 119 AGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIP 198
Cdd:COG1446    70 AGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAERFAREQGLE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 199 SCPPSTmttrfslaaFKRNKRKLelaervetdfiQLKRRRQSSAKENDSGaLDTVGAVVVDHEGNVAAAVSSGGLALKHP 278
Cdd:COG1446   140 LVDPLY---------FFTEKRWK-----------QWKKALEYKPIINERK-HGTVGAVALDANGNLAAATSTGGMTNKRP 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 279 GRVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfisspflASEDGV 357
Cdd:COG1446   199 GRVGDSPIIGAGTYADNEVG------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI-------LKKLGG 265
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1046879704 358 LGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSAqDGKAKTHI 411
Cdd:COG1446   266 DGGLIAV-------------DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
44-364 9.62e-60

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: 196.64  E-value: 9.62e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGVGS 123
Cdd:cd04702     4 IVVHGGAGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALE------------------DDPVFNAGYGS 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 124 NLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCPPS 203
Cdd:cd04702    66 VLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLA-RLVME---------KTPHCFLTGRGANKFAEEMGIPQVPPE 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 204 TMTTRFSLAAFKRNKRKlelaervetdfiqlkrrrQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQ 283
Cdd:cd04702   136 SLVTERARERLEKFKKE------------------KGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGD 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 284 AALYGCGCWAENtgahnpYSTAVSTSGCGEHLVRTILARECSHALQ----AEDAHQALLETMQNKFisspflasedGVLG 359
Cdd:cd04702   198 SPIIGSGGYADN------LVGAVSTTGHGESIMKVNLARLILFHMEqgktAEEAAELALAYMKSRV----------KGLG 261

                  ....*
gi 1046879704 360 GVIVL 364
Cdd:cd04702   262 GLIVV 266
Asparaginase_2 pfam01112
Asparaginase;
44-402 2.13e-55

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 185.87  E-value: 2.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGV 121
Cdd:pfam01112   2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLE------------------DDPLFNAGK 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 122 GSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHGIPSCP 201
Cdd:pfam01112  64 GSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMGLERVP 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 202 PSTMTTRFSLAAFKRNKrklelaervETDFIQLKRRRQSSA--KENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHPG 279
Cdd:pfam01112 134 PEDFLTEERLQELQKAR---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPG 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 280 RVGQAALYGCGCWAENTGAhnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspflased 355
Cdd:pfam01112 205 RVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV---------- 268
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1046879704 356 GVLGGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMSA 402
Cdd:pfam01112 269 GGDGGVIAV-------------DAKG---NIAAPFNTEGMYRAYHTG 299
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
46-364 1.08e-43

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: 153.77  E-value: 1.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  46 VHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAG 120
Cdd:cd04701     4 IHGGAGtisraNLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLE------------------DCPLFNAG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 121 VGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIPSC 200
Cdd:cd04701    66 KGAVFTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKS----------PHVLLSGEGAEEFAREQGLELV 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 201 PPStmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgaldTVGAVVVDHEGNVAAAVSSGGLALKHPGR 280
Cdd:cd04701   136 PQG------------------------------------------------TVGAVALDSDGNLAAATSTGGLTNKLPGR 167
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 281 VGQAALYGCGCWAENtgahnpYSTAVSTSGCGEHLVRTILARECSHalQAEDAHQALLETMqnKFISSPFLASEDGVlGG 360
Cdd:cd04701   168 IGDTPIIGAGFWAEE------WAVAVSGTGNGDSFIRVAAARDVAA--RMRYKGLSLAEAA--KEVVGPGGELGEGE-GG 236

                  ....
gi 1046879704 361 VIVL 364
Cdd:cd04701   237 IIAI 240
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
44-401 2.71e-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: 149.65  E-value: 2.71e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  44 VLVHAGAGYHSESKAKE-YKHVCKRACQKAIEKLQAGAlATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGVG 122
Cdd:cd14950     2 LVVHGGAGSWKNSDDEEkALRALREALERGYEALRRGS-ALEAVVEAVAYME------------------DSGVFNAGVG 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 123 SNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGipscpp 202
Cdd:cd14950    63 SVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIRLARKVMEKT----------DHVLIVGEGADELAKRLG------ 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 203 stmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgaLDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVG 282
Cdd:cd14950   127 -----------------------------------------------GDTVGAVALDKDGNLAAATSTGGVWLKLPGRVG 159
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 283 QAALYGCGCWAENtgahnpySTAVSTSGCGEHLVRTILARECSHA----LQAEDAHQALLETMQNKFISSpflasedgvL 358
Cdd:cd14950   160 DSPIPGAGFYATN-------GVAVSATGIGEVIIRSLPALRADELvsmgGDIEEAVRAVVNKVTETFGKD---------T 223
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1046879704 359 GGVIVLrscrcpsesdpsqDKQTllvEFLWSHSTESMCVGYMS 401
Cdd:cd14950   224 AGIIGI-------------DARG---NIAAAFNTEAMPRGYID 250
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
46-323 3.18e-42

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 151.40  E-value: 3.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  46 VHAGAGYHSESKAKEYKHVCKRACQKA----IEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGV 121
Cdd:PLN02689    8 LHGGAGDIDPNLPRERQEEAEAALRRCldlgIAALRSSLPALDVVELVVRELE------------------NDPLFNAGR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 122 GSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIPSCP 201
Cdd:PLN02689   70 GSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLA-RLVME---------KTPHIYLAFDGAEAFARQQGVETVD 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 202 PSTMTTRfslaafkRNKRKLELAE---RVETDFIQ--LKRRRQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALK 276
Cdd:PLN02689  140 NSYFITE-------ENVERLKQAKeanSVQFDYRIplDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNK 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1046879704 277 HPGRVGQAALYGCGCWAENTGahnpystAVSTSGCGEHLVRTILARE 323
Cdd:PLN02689  213 MVGRIGDTPIIGAGTYANHLC-------AVSATGKGEAIIRGTVARD 252
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
66-323 1.62e-38

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: 140.77  E-value: 1.62e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  66 KRACQKAIEKLQAGALATDAVMAAL--VELEhlsalyplLEAYLVsivldspftnaGVGSNLNLLGEIECDASIMDGKSL 143
Cdd:cd04513     9 TEAVEAAWEVLQKGGSALDAVEAGCsvCEDD--------QCDGSV-----------GYGGSPDENGETTLDAAIMDGDTM 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 144 SFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPSCPPSTMTTRFSLAAFKRNKRKLEL 223
Cdd:cd04513    70 DVGAVAALRRIKNAISVARAVM----------EHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNF 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 224 AERVETD-----FIQLKRRRQSSAKENDSGalDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENT-G 297
Cdd:cd04513   140 WKNVVPDpskscSSPKAPSRSESAIPEDNH--DTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEvG 217
                         250       260
                  ....*....|....*....|....*.
gi 1046879704 298 AhnpystAVSTsGCGEHLVRTILARE 323
Cdd:cd04513   218 A------AAAT-GDGDIMMRFLPSYQ 236
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
44-364 8.12e-36

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: 132.38  E-value: 8.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  44 VLVHAGAGyhsesKAKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTNAGVGS 123
Cdd:cd04703     3 VLVHGGAG-----SDPERQDGLERAAEAGLAELQNGGDALDAVVAAVRVLE------------------DDPRFNAGTGS 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 124 NLNLLGEIECDASIMDGKSlSFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIP-SCpp 202
Cdd:cd04703    60 VLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVARAVMETS----------PHVLLAGDGAVRFARRLGYPdGC-- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 203 stmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgalDTVGAVVVDHeGNVAAAVSSGGLALKHPGRVG 282
Cdd:cd04703   127 ------------------------------------------------DTVGAVARDG-GKFAAAVSTGGTSPALRGRVG 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 283 QAALYGCGCWAENTGahnpystAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFisspflasEDGVLGGVI 362
Cdd:cd04703   158 DVPIIGAGFYAGPKG-------AVAATGIGEEIAKRLLARRVYRWIETGLSLQAAAQRAIDEF--------DDGVAVGVI 222

                  ..
gi 1046879704 363 VL 364
Cdd:cd04703   223 AV 224
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
44-321 5.72e-32

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 123.91  E-value: 5.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  44 VLVHAGAGYHSESK-----AKEYKHVCKRACQKAIEKLQAGALATDAVMAALVELEhlsalyplleaylvsivlDSPFTN 118
Cdd:PRK10226    6 IAIHGGAGAISRAQmslqqELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLE------------------ECPLFN 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 119 AGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVsVAHRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGIP 198
Cdd:PRK10226   68 AGIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPV-LAARLVME---------QSPHVMMIGEGAENFAFAHGME 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 199 SCPPSTMTTrfslaafkrNKRKLELAERVETDFIQLKrrrQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHP 278
Cdd:PRK10226  138 RVSPEIFST---------PLRYEQLLAARAEGATVLD---HSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLP 205
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1046879704 279 GRVGQAALYGCGCWAENTgahnpySTAVSTSGCGEHLVRTILA 321
Cdd:PRK10226  206 GRVGDSPLVGAGCYANNA------SVAVSCTGTGEVFIRALAA 242
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
44-321 4.55e-24

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: 101.15  E-value: 4.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704  44 VLVHAGAGyhSESKAK-EYKHVCKRACQKAIEK----LQAGAlATDAVmaalvelehlsalyplleAYLVSIVLDSPFTN 118
Cdd:cd14949     3 LIIHGGFG--SESSTNgETKAAKQEALAEIVEEvyeyLKSHS-ALEAV------------------VYAVSLLEDDPLFN 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 119 AGVGSNLNLLGEIECDASIMDGKSLSFGAVGALSGIKNPVSVAHRLLCEGQKgklsagrippcFLVGEGAYRWAVDHGIP 198
Cdd:cd14949    62 AGTGSQIQSDGQIRMSASLMDGQTQRFSGVINIENVKNPIEVAQKLQQEDDR-----------VLSGEGATEFARENGFP 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046879704 199 SCPPstmttrfslaafkrnkrklelaervETDFiqlkRRRQSSAKENDSGALDTVGAVVVDHEGNVAAAVSSGGLALKHP 278
Cdd:cd14949   131 EYNP-------------------------ETPQ----RRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIP 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1046879704 279 GRVGQAAlygcgcwaenTGAHNpYST---AVSTSGCGEHLVRTILA 321
Cdd:cd14949   182 GRVSDSA----------TVAGN-YANafaGVSCTGIGEDIVSEALA 216
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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