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Conserved domains on  [gi|755500764|ref|XP_011238131|]
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threonine aspartase 1 isoform X1 [Mus musculus]

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 ...
 42-439 2.28e-125

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: 365.83  E-value: 2.28e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPF 121
Cdd:cd04514    1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLE-----------------------DSPL 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 122 TNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHG 201
Cdd:cd04514   58 TNAGYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKG 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 202 IpscppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALK 281
Cdd:cd04514  137 I---------------------------------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLK 165

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 282 HPGRVGQAALYGCGCWAENTGAQNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLACED 360
Cdd:cd04514  166 HPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPG 245

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 361 G---VLGGVIVLRSCRcssesdssqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCR 437
Cdd:cd04514  246 VknsPSAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIR 311


                 ..
gi 755500764 438 LE 439
Cdd:cd04514  312 LR 313
 
Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 42-439 2.28e-125

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: 365.83  E-value: 2.28e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPF 121
Cdd:cd04514    1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLE-----------------------DSPL 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 122 TNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHG 201
Cdd:cd04514   58 TNAGYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKG 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 202 IpscppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALK 281
Cdd:cd04514  137 I---------------------------------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLK 165

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 282 HPGRVGQAALYGCGCWAENTGAQNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLACED 360
Cdd:cd04514  166 HPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPG 245

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 361 G---VLGGVIVLRSCRcssesdssqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCR 437
Cdd:cd04514  246 VknsPSAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIR 311


                 ..
gi 755500764 438 LE 439
Cdd:cd04514  312 LR 313
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 37-418 6.96e-74

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 237.46  E-value: 6.96e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGAlatdavaaalveleGLSLwltdnkdfSLSVPGLQAS 116
Cdd:PLN02937   7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGS--------------GGCI--------DAVSAAIQVL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 117 VDSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRW 196
Cdd:PLN02937  65 EDDPSTNAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQW 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 197 AVDHGIPScpPSTMT-------TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT-------- 254
Cdd:PLN02937 145 AKSKGIDL--PETVEeaekwlvTERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasd 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 255 ----LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGCGEHLVRTILAREC 329
Cdd:PLN02937 223 edciMDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAAREC 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 330 SHAL---QAEDAHQA---LLETMQNkfiSSPFLACEDgvlGGVIVLRSCRCSSESDSSQDKQTllVEFLWSHTTESMCVG 403
Cdd:PLN02937 303 CVSSslsQAGPASACmkvLRSVIQG---SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIG 374

                        410
                 ....*....|....*
gi 755500764 404 YMSAQDGKAKTHISR 418
Cdd:PLN02937 375 YFGSSMERPKVSILR 389
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 44-416 1.27e-54

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 183.77  E-value: 1.27e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGalatdavaaalveleGLSLwltdnkDfslsvpGLQASV- 117
Cdd:COG1446    8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAG---------------GSAL------D------AVEAAVr 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 118 ---DSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAY 194
Cdd:COG1446   61 vleDDPLFNAGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAE 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 195 RWAVDHGIPSCPPSTmttrfslaaFKRNKRKLelaervetdfiQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVS 274
Cdd:COG1446  131 RFAREQGLELVDPLY---------FFTEKRWK-----------QWKKALEYKPIINERKH-GTVGAVALDANGNLAAATS 189

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 275 SGGLALKHPGRVGQAALYGCGCWAENTGAqnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfiss 353
Cdd:COG1446  190 TGGMTNKRPGRVGDSPIIGAGTYADNEVG------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI---- 259

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755500764 354 pfLAcEDGVLGGVIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMSAqDGKAKTHI 416
Cdd:COG1446  260 --LK-KLGGDGGLIAV-------------DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
Asparaginase_2 pfam01112
Asparaginase;
44-407 1.53e-49

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 170.84  E-value: 1.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764   44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPF 121
Cdd:pfam01112   2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLE-----------------------DDPL 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  122 TNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHG 201
Cdd:pfam01112  59 FNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMG 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  202 IPSCPPSTMTTRFSLAAFKRNKrklelaervETDFIQLKRRRQSSA--KENDSGTLDTVGAVVVDHEGNVAAAVSSGGLA 279
Cdd:pfam01112 129 LERVPPEDFLTEERLQELQKAR---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMT 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  280 LKHPGRVGQAALYGCGCWAENTGAqnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspf 355
Cdd:pfam01112 200 NKRPGRVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV----- 268

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755500764  356 lacedGVLGGVIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMSA 407
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 ...
 42-439 2.28e-125

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: 365.83  E-value: 2.28e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  42 GFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPF 121
Cdd:cd04514    1 FFVAVHAGAGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLE-----------------------DSPL 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 122 TNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEgQKGKLSAGRIPPCFLVGEGAYRWAVDHG 201
Cdd:cd04514   58 TNAGYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKE-QRKPLSLGRVPPMFLVGEGAREWAKSKG 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 202 IpscppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgTLDTVGAVVVDHEGNVAAAVSSGGLALK 281
Cdd:cd04514  137 I---------------------------------------------------ITDTVGAIAIDLYGNIAAGSSSGGIGLK 165

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 282 HPGRVGQAALYGCGCWAENTGAQNPYSTAVSTSGCGEHLVRTILARECSHALQAEDAHQ-ALLETMQNKFISSPFLACED 360
Cdd:cd04514  166 HPGRVGPAALYGAGCWAEPRDPDDKTSVAVVTSGTGEHIATTMLARRCAERLYHSTRREeSDEDEILRSFIESDFMGHPG 245

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 361 G---VLGGVIVLRSCRcssesdssqdKQTLLVEFLWSHTTESMCVGYMSAQDGKAKTHISRLPPGAvagqSVAIEGGVCR 437
Cdd:cd04514  246 VknsPSAGAIGVLAVK----------KTRSGVELYFAHNTDSFALASMSSSDRKPKCVMSRLPGNG----SIAQGGRKIR 311


                 ..
gi 755500764 438 LE 439
Cdd:cd04514  312 LR 313
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 44-405 2.06e-81

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: 251.33  E-value: 2.06e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPFTN 123
Cdd:cd04512    2 LIVHGGAGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLE-----------------------DDPLFN 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 124 AGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGip 203
Cdd:cd04512   59 AGRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLARAVMEKT----------PHVLLVGEGAERFAREHG-- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 204 scppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgtLDTVGAVVVDHEGNVAAAVSSGGLALKHP 283
Cdd:cd04512  127 ---------------------------------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRP 155

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 284 GRVGQAALYGCGCWAENTgaqnpySTAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFISSpflaceDGVL 363
Cdd:cd04512  156 GRVGDSPIIGAGTYADNE------TGAVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAEAAIDYLRRR------VGGE 223

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 755500764 364 GGVIVLrscrcssesdssqDKQtllVEFLWSHTTESMCVGYM 405
Cdd:cd04512  224 GGLIVV-------------DPD---GRLGAAHNTPGMAFAYI 249
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 37-418 6.96e-74

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 237.46  E-value: 6.96e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  37 KEKRGGFVLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGAlatdavaaalveleGLSLwltdnkdfSLSVPGLQAS 116
Cdd:PLN02937   7 DQNRRFFVAVHVGAGYHAPSNEKALRSAMRRACLAAAAILRQGS--------------GGCI--------DAVSAAIQVL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 117 VDSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKGKLSAGRIPPCFLVGEGAYRW 196
Cdd:PLN02937  65 EDDPSTNAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMGSSLLGRIPPMFLVGEGARQW 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 197 AVDHGIPScpPSTMT-------TRFSLAAFKRNKRKLELAE-------RVETDFIQLKRRRQSSAKENDSGT-------- 254
Cdd:PLN02937 145 AKSKGIDL--PETVEeaekwlvTERAKEQWKKYKTMLASAIaksscdsQSTSKLSELEAPRSNPSNGTGGGQssmctasd 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 255 ----LDTVGAVVVDHEGNVAAAVSSGGLALKHPGRVGQAALYGCGCWAENTGAQN-PYSTAVSTSGCGEHLVRTILAREC 329
Cdd:PLN02937 223 edciMDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGPFGaPFIVGCCVSGAGEYLMRGFAAREC 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 330 SHAL---QAEDAHQA---LLETMQNkfiSSPFLACEDgvlGGVIVLRSCRCSSESDSSQDKQTllVEFLWSHTTESMCVG 403
Cdd:PLN02937 303 CVSSslsQAGPASACmkvLRSVIQG---SSAKTTDKD---AGILLVQADASVMAPGNSPSLKA--VEIAAAYSSLSFGIG 374

                        410
                 ....*....|....*
gi 755500764 404 YMSAQDGKAKTHISR 418
Cdd:PLN02937 375 YFGSSMERPKVSILR 389
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 44-416 1.27e-54

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 183.77  E-value: 1.27e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  44 VLVHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGalatdavaaalveleGLSLwltdnkDfslsvpGLQASV- 117
Cdd:COG1446    8 LIIHGGAGtiarsAMTPEVEAAYRAGLRAALEAGYAVLEAG---------------GSAL------D------AVEAAVr 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 118 ---DSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAY 194
Cdd:COG1446   61 vleDDPLFNAGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISLARAVM----------EKTPHVLLVGEGAE 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 195 RWAVDHGIPSCPPSTmttrfslaaFKRNKRKLelaervetdfiQLKRRRQSSAKENDSGTlDTVGAVVVDHEGNVAAAVS 274
Cdd:COG1446  131 RFAREQGLELVDPLY---------FFTEKRWK-----------QWKKALEYKPIINERKH-GTVGAVALDANGNLAAATS 189

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 275 SGGLALKHPGRVGQAALYGCGCWAENTGAqnpystAVSTSGCGEHLVRTILARECSHALQA-EDAHQALLETMQNKfiss 353
Cdd:COG1446  190 TGGMTNKRPGRVGDSPIIGAGTYADNEVG------AVSATGHGEYFIRTVVAHDIVERMRQgLSLQEAAEEVIERI---- 259

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755500764 354 pfLAcEDGVLGGVIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMSAqDGKAKTHI 416
Cdd:COG1446  260 --LK-KLGGDGGLIAV-------------DKDG---NIAAPFNTEGMYRAYIDG-DGELVVAI 302
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 44-369 2.29e-52

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: 177.38  E-value: 2.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  44 VLVHAGAGYHSESKAKEYKHVCKRACQKAIEKLQAGalatdavaaalveleGLSLwltdnkDfslSVP-GLQASVDSPFT 122
Cdd:cd04702    4 IVVHGGAGSIPDDRIKGSREGVKRAARAGYSVLKAG---------------GSAL------D---AVEaAVRALEDDPVF 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 123 NAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHGI 202
Cdd:cd04702   60 NAGYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLA-RLVME---------KTPHCFLTGRGANKFAEEMGI 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 203 PSCPPSTMTTRFSLAAFKRNKRKlelaervetdfiqlkrrrQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALKH 282
Cdd:cd04702  130 PQVPPESLVTERARERLEKFKKE------------------KGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKM 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 283 PGRVGQAALYGCGCWAENtgaqnpYSTAVSTSGCGEHLVRTILARECSHALQ----AEDAHQALLETMQNKFisspflac 358
Cdd:cd04702  192 VGRVGDSPIIGSGGYADN------LVGAVSTTGHGESIMKVNLARLILFHMEqgktAEEAAELALAYMKSRV-------- 257

                        330
                 ....*....|.
gi 755500764 359 edGVLGGVIVL 369
Cdd:cd04702  258 --KGLGGLIVV 266
Asparaginase_2 pfam01112
Asparaginase;
44-407 1.53e-49

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 170.84  E-value: 1.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764   44 VLVHAGAGY--HSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPF 121
Cdd:pfam01112   2 LVIHGGAGSilRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLE-----------------------DDPL 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  122 TNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAhRLLCEGQKGKLsagrippcfLVGEGAYRWAVDHG 201
Cdd:pfam01112  59 FNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLA-RAVMEKTPHVM---------LSGEGAEQFAREMG 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  202 IPSCPPSTMTTRFSLAAFKRNKrklelaervETDFIQLKRRRQSSA--KENDSGTLDTVGAVVVDHEGNVAAAVSSGGLA 279
Cdd:pfam01112 129 LERVPPEDFLTEERLQELQKAR---------KENFQPNMALNVAPDplKECGDSKRGTVGAVALDSEGNLAAGTSTGGMT 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  280 LKHPGRVGQAALYGCGCWAENTGAqnpystAVSTSGCGEHLVRTILARECS----HALQAEDAHQALLETMQNKFisspf 355
Cdd:pfam01112 200 NKRPGRVGDSPIIGAGTYADNATG------AVSATGHGEDIIRETLAYDIVarmeYGLSLEEAADKVITEMLKRV----- 268

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755500764  356 lacedGVLGGVIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMSA 407
Cdd:pfam01112 269 -----GGDGGVIAV-------------DAKG---NIAAPFNTEGMYRAYHTG 299
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 46-369 9.47e-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: 9.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  46 VHAGAG-----YHSESKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSP 120
Cdd:cd04701    4 IHGGAGtisraNLTPERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLE-----------------------DCP 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 121 FTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDH 200
Cdd:cd04701   61 LFNAGKGAVFTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKS----------PHVLLSGEGAEEFAREQ 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 201 GIPSCPPStmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgtldTVGAVVVDHEGNVAAAVSSGGLAL 280
Cdd:cd04701  131 GLELVPQG------------------------------------------------TVGAVALDSDGNLAAATSTGGLTN 162

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 281 KHPGRVGQAALYGCGCWAENtgaqnpYSTAVSTSGCGEHLVRTILARECSHalQAEDAHQALLETMqnKFISSPFLACED 360
Cdd:cd04701  163 KLPGRIGDTPIIGAGFWAEE------WAVAVSGTGNGDSFIRVAAARDVAA--RMRYKGLSLAEAA--KEVVGPGGELGE 232


                 ....*....
gi 755500764 361 GVlGGVIVL 369
Cdd:cd04701  233 GE-GGIIAI 240
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 46-328 3.96e-37

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 137.92  E-value: 3.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  46 VHAGAGYHSESKAKEYKHVCKRACQKA----IEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPF 121
Cdd:PLN02689   8 LHGGAGDIDPNLPRERQEEAEAALRRCldlgIAALRSSLPALDVVELVVRELE-----------------------NDPL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 122 TNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAhRLLCEgqkgklsagRIPPCFLVGEGAYRWAVDHG 201
Cdd:PLN02689  65 FNAGRGSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLA-RLVME---------KTPHIYLAFDGAEAFARQQG 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 202 IPSCPPSTMTTRfslaafkRNKRKLELAE---RVETDFIQ--LKRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSG 276
Cdd:PLN02689 135 VETVDNSYFITE-------ENVERLKQAKeanSVQFDYRIplDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTG 207

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755500764 277 GLALKHPGRVGQAALYGCGCWAENTGaqnpystAVSTSGCGEHLVRTILARE 328
Cdd:PLN02689 208 GLVNKMVGRIGDTPIIGAGTYANHLC-------AVSATGKGEAIIRGTVARD 252
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 125-369 4.72e-37

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: 136.92  E-value: 4.72e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 125 GIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLcegqkgklsaGRIPPCFLVGEGAYRWAVDHGIPS 204
Cdd:cd04513   46 GYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVARAVM----------EHTPHSLLVGEGATEFAVSMGFKE 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 205 CPPSTMTTRFSLAAFKRNKRKLELAERVETD---FIQLKRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLALK 281
Cdd:cd04513  116 ENLLTEESRKMWKKWLKENCQPNFWKNVVPDpskSCSSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFK 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 282 HPGRVGQAALYGCGCWAENT-GAqnpystAVSTsGCGEhlvrtILARECShalqaedAHQAlLETMQNKFisSPFLACED 360
Cdd:cd04513  196 IPGRVGDSPIPGAGLYADNEvGA------AAAT-GDGD-----IMMRFLP-------SYQA-VELMRQGM--SPQEACED 253

                        250       260
                 ....*....|....*....|
gi 755500764 361 GVL-----------GGVIVL 369
Cdd:cd04513  254 AIRriakkypkdfeGAVVAV 273
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 118-406 5.38e-37

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: 135.78  E-value: 5.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 118 DSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWA 197
Cdd:cd14950   53 DSGVFNAGVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIRLARKVMEKT----------DHVLIVGEGADELA 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 198 VDHGipscppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsgtLDTVGAVVVDHEGNVAAAVSSGG 277
Cdd:cd14950  123 KRLG-----------------------------------------------------GDTVGAVALDKDGNLAAATSTGG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 278 LALKHPGRVGQAALYGCGCWAENtgaqnpySTAVSTSGCGEHLVRTILARECSHA----LQAEDAHQALLETMQNKFISS 353
Cdd:cd14950  150 VWLKLPGRVGDSPIPGAGFYATN-------GVAVSATGIGEVIIRSLPALRADELvsmgGDIEEAVRAVVNKVTETFGKD 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755500764 354 pflacedgvLGGVIVLrscrcssesdssqDKQTllvEFLWSHTTESMCVGYMS 406
Cdd:cd14950  223 ---------TAGIIGI-------------DARG---NIAAAFNTEAMPRGYID 250
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 120-326 1.48e-30

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 120.05  E-value: 1.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 120 PFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVsVAHRLLCEgqkgklsagRIPPCFLVGEGAYRWAVD 199
Cdd:PRK10226  64 PLFNAGIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPV-LAARLVME---------QSPHVMMIGEGAENFAFA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 200 HGIPSCPPSTMTTrfslaafkrNKRKLELAERVETDFIQLKrrrQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGGLA 279
Cdd:PRK10226 134 HGMERVSPEIFST---------PLRYEQLLAARAEGATVLD---HSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMT 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 755500764 280 LKHPGRVGQAALYGCGCWAENTgaqnpySTAVSTSGCGEHLVRTILA 326
Cdd:PRK10226 202 NKLPGRVGDSPLVGAGCYANNA------SVAVSCTGTGEVFIRALAA 242
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 44-369 2.94e-30

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: 117.36  E-value: 2.94e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764  44 VLVHAGAGyhsesKAKEYKHVCKRACQKAIEKLQAGALATDAVAAALVELEglslwltdnkdfslsvpglqasvDSPFTN 123
Cdd:cd04703    3 VLVHGGAG-----SDPERQDGLERAAEAGLAELQNGGDALDAVVAAVRVLE-----------------------DDPRFN 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 124 AGIGSNLNLLGEIECDASIMDGKSlNFGAVGALSGIKNPVSVAHRLLCEGqkgklsagriPPCFLVGEGAYRWAVDHGIP 203
Cdd:cd04703   55 AGTGSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVARAVMETS----------PHVLLAGDGAVRFARRLGYP 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 204 scppstmttrfslaafkrnkrklelaervetdfiqlkrrrqssakendsGTLDTVGAVVVDHeGNVAAAVSSGGLALKHP 283
Cdd:cd04703  124 -------------------------------------------------DGCDTVGAVARDG-GKFAAAVSTGGTSPALR 153

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 284 GRVGQAALYGCGCWAENTGaqnpystAVSTSGCGEHLVRTILARECSHALQAEDAHQALLETMQNKFisspflacEDGVL 363
Cdd:cd04703  154 GRVGDVPIIGAGFYAGPKG-------AVAATGIGEEIAKRLLARRVYRWIETGLSLQAAAQRAIDEF--------DDGVA 218


                 ....*.
gi 755500764 364 GGVIVL 369
Cdd:cd04703  219 VGVIAV 224
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 118-326 7.85e-23

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: 97.68  E-value: 7.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 118 DSPFTNAGIGSNLNLLGEIECDASIMDGKSLNFGAVGALSGIKNPVSVAHRLLCEGQKgklsagrippcFLVGEGAYRWA 197
Cdd:cd14949   56 DDPLFNAGTGSQIQSDGQIRMSASLMDGQTQRFSGVINIENVKNPIEVAQKLQQEDDR-----------VLSGEGATEFA 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755500764 198 VDHGIPSCPPstmttrfslaafkrnkrklelaervETDFiqlkRRRQSSAKENDSGTLDTVGAVVVDHEGNVAAAVSSGG 277
Cdd:cd14949  125 RENGFPEYNP-------------------------ETPQ----RRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGG 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755500764 278 LALKHPGRVGQAAlygcgcwaenTGAQNpYST---AVSTSGCGEHLVRTILA 326
Cdd:cd14949  176 KGFEIPGRVSDSA----------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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