NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1972265862|ref|NP_001379234|]
View 

TASPase homolog [Caenorhabditis elegans]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
5-304 4.10e-72

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: 226.00  E-value: 4.10e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862   5 EIIAVHGGA--CAKFDASLA-EDCRFAC------------GTGTVENALTDLERIEKFNCGFGSHLTIDQEVECEASYMS 69
Cdd:cd04514     1 FFVAVHAGAgyHSPSNEKAYkRACKRACkaaaavlkaggsALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  70 SKNLSFGAVGAISNVFHPSRVARHLAHSNWWKQ-RRLLHPLILVGRGAEKYAVKNDFPTctpeelvskaakesfekylhr 148
Cdd:cd04514    81 GSSGRFGAVGAVSGVKNPIQLARLLLKEQRKPLsLGRVPPMFLVGEGAREWAKSKGIIT--------------------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 149 mlhpydthDTVGAISINTNtMNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSERRQYEEPfdqvseRTISICSTGHGESL 228
Cdd:cd04514   140 --------DTVGAIAIDLY-GNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPDDK------TSVAVVTSGTGEHI 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 229 VKADFCRGIATRVL--DDEEGIMYSEIIREFIHEKMEHGS------RYGGIALIADKfKDRMSLEFLIFHNCRYLPAAVR 300
Cdd:cd04514   205 ATTMLARRCAERLYhsTRREESDEDEILRSFIESDFMGHPgvknspSAGAIGVLAVK-KTRSGVELYFAHNTDSFALASM 283

                  ....
gi 1972265862 301 CRDN 304
Cdd:cd04514   284 SSSD 287
 
Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
5-304 4.10e-72

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: 226.00  E-value: 4.10e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862   5 EIIAVHGGA--CAKFDASLA-EDCRFAC------------GTGTVENALTDLERIEKFNCGFGSHLTIDQEVECEASYMS 69
Cdd:cd04514     1 FFVAVHAGAgyHSPSNEKAYkRACKRACkaaaavlkaggsALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  70 SKNLSFGAVGAISNVFHPSRVARHLAHSNWWKQ-RRLLHPLILVGRGAEKYAVKNDFPTctpeelvskaakesfekylhr 148
Cdd:cd04514    81 GSSGRFGAVGAVSGVKNPIQLARLLLKEQRKPLsLGRVPPMFLVGEGAREWAKSKGIIT--------------------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 149 mlhpydthDTVGAISINTNtMNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSERRQYEEPfdqvseRTISICSTGHGESL 228
Cdd:cd04514   140 --------DTVGAIAIDLY-GNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPDDK------TSVAVVTSGTGEHI 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 229 VKADFCRGIATRVL--DDEEGIMYSEIIREFIHEKMEHGS------RYGGIALIADKfKDRMSLEFLIFHNCRYLPAAVR 300
Cdd:cd04514   205 ATTMLARRCAERLYhsTRREESDEDEILRSFIESDFMGHPgvknspSAGAIGVLAVK-KTRSGVELYFAHNTDSFALASM 283

                  ....
gi 1972265862 301 CRDN 304
Cdd:cd04514   284 SSSD 287
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
7-240 1.72e-27

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 111.11  E-value: 1.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862   7 IAVHGGA---CAKFDASLAEDCRFAC---------GTGT----VENALTDLERIEKFNCGFGSHLTIDQEVECEASYMSS 70
Cdd:PLN02937   14 VAVHVGAgyhAPSNEKALRSAMRRAClaaaailrqGSGGcidaVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASIMDG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  71 KNLSFGAVGAISNVFHPSRVARHLAhsnwwKQRRL-------LHPLILVGRGAEKYAVKN--DFPTCTPEE---LVSKAA 138
Cdd:PLN02937   94 DSGAFGAVGAVPGVRNAIQIAALLA-----KEQMMgssllgrIPPMFLVGEGARQWAKSKgiDLPETVEEAekwLVTERA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 139 KESFEKYlHRML---------------------HPYDTH---------------------DTVGAISINTNTmNSESGTS 176
Cdd:PLN02937  169 KEQWKKY-KTMLasaiaksscdsqstsklseleAPRSNPsngtgggqssmctasdedcimDTVGVICVDSEG-NIASGAS 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972265862 177 SGGIVLKHSGRLGHSCVYGSGTW-SERRQYEEPFdqvserTISICSTGHGESLVkadfcRGIATR 240
Cdd:PLN02937  247 SGGIAMKVSGRVGLAAMYGSGCWaSSKGPFGAPF------IVGCCVSGAGEYLM-----RGFAAR 300
Asparaginase_2 pfam01112
Asparaginase;
6-241 2.25e-24

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 100.74  E-value: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862   6 IIAVHGGACAKFD-ASLAEDCRFA------CG----------TGTVENALTDLERIEKFNCGFGSHLTIDQEVECEASYM 68
Cdd:pfam01112   1 VLVIHGGAGSILRtKEREEAYRAGlkealeAGyavlaaggsaLDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  69 SSKNLSFGAVGAISNVFHPSRVARHLA----HSnwwkqrrllhplILVGRGAEKYAVKNDFPTCTPEELVSKAAKESFEK 144
Cdd:pfam01112  81 DGKTLRAGAVAGVSRIKNPISLARAVMektpHV------------MLSGEGAEQFAREMGLERVPPEDFLTEERLQELQK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 145 YLHRM---------------LHPYDTHDTVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSERRqyeepF 209
Cdd:pfam01112 149 ARKENfqpnmalnvapdplkECGDSKRGTVGAVALDSEG-NLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNA-----T 222
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1972265862 210 DQVSertisicSTGHGESLVKADFCRGIATRV 241
Cdd:pfam01112 223 GAVS-------ATGHGEDIIRETLAYDIVARM 247
 
Name Accession Description Interval E-value
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
5-304 4.10e-72

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: 226.00  E-value: 4.10e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862   5 EIIAVHGGA--CAKFDASLA-EDCRFAC------------GTGTVENALTDLERIEKFNCGFGSHLTIDQEVECEASYMS 69
Cdd:cd04514     1 FFVAVHAGAgyHSPSNEKAYkRACKRACkaaaavlkaggsALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIMD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  70 SKNLSFGAVGAISNVFHPSRVARHLAHSNWWKQ-RRLLHPLILVGRGAEKYAVKNDFPTctpeelvskaakesfekylhr 148
Cdd:cd04514    81 GSSGRFGAVGAVSGVKNPIQLARLLLKEQRKPLsLGRVPPMFLVGEGAREWAKSKGIIT--------------------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 149 mlhpydthDTVGAISINTNtMNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSERRQYEEPfdqvseRTISICSTGHGESL 228
Cdd:cd04514   140 --------DTVGAIAIDLY-GNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAEPRDPDDK------TSVAVVTSGTGEHI 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 229 VKADFCRGIATRVL--DDEEGIMYSEIIREFIHEKMEHGS------RYGGIALIADKfKDRMSLEFLIFHNCRYLPAAVR 300
Cdd:cd04514   205 ATTMLARRCAERLYhsTRREESDEDEILRSFIESDFMGHPgvknspSAGAIGVLAVK-KTRSGVELYFAHNTDSFALASM 283

                  ....
gi 1972265862 301 CRDN 304
Cdd:cd04514   284 SSSD 287
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
6-237 1.10e-33

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: 125.38  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862   6 IIAVHGGACAKFDA---------SLAEDCRFAC--GTGT----VENALTDLERIEKFNCGFGSHLTIDQEVECEASYMSS 70
Cdd:cd04702     3 VIVVHGGAGSIPDDrikgsregvKRAARAGYSVlkAGGSaldaVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASIMDG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  71 KNLSFGAVGAISNVFHPSRVARHLAHsnwwKQRRLLhpliLVGRGAEKYAVKNDFPTCTPEELVSKAAKESFEKYLHRML 150
Cdd:cd04702    83 KTLRAGAVSAVRNIANPISLARLVME----KTPHCF----LTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEKG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 151 HPYD----THDTVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSERRqyeepfdqvsertISICS-TGHG 225
Cdd:cd04702   155 ANVEdtqrGHGTVGAVAIDCEG-NVACATSTGGITNKMVGRVGDSPIIGSGGYADNL-------------VGAVStTGHG 220
                         250
                  ....*....|..
gi 1972265862 226 ESLVKADFCRGI 237
Cdd:cd04702   221 ESIMKVNLARLI 232
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
6-241 1.07e-29

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: 113.82  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862   6 IIAVHGGACA---KFDASLAEDCRFACGTG------------TVENALTDLERIEKFNCGFGSHLTIDQEVECEASYMSS 70
Cdd:cd04512     1 SLIVHGGAGTiedEDAEAYREGLLRALEAGrevlekggsaldAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIMDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  71 KNLSFGAVGAISNVFHPSRVARhlahsnwwkqrRLL---HPLILVGRGAEKYAVKNDfptctpeelvskaakesfekylh 147
Cdd:cd04512    81 KTLNAGAVAGVKGVKNPISLAR-----------AVMektPHVLLVGEGAERFAREHG----------------------- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 148 rmlhpydtHDTVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSErrqyeepfdqvsERTISICSTGHGES 227
Cdd:cd04512   127 --------HGTVGAVARDAQG-NLAAATSTGGMVNKRPGRVGDSPIIGAGTYAD------------NETGAVSATGHGES 185
                         250
                  ....*....|....
gi 1972265862 228 LVKADFCRGIATRV 241
Cdd:cd04512   186 IIRTVLAKRIADLV 199
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
7-240 1.72e-27

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 111.11  E-value: 1.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862   7 IAVHGGA---CAKFDASLAEDCRFAC---------GTGT----VENALTDLERIEKFNCGFGSHLTIDQEVECEASYMSS 70
Cdd:PLN02937   14 VAVHVGAgyhAPSNEKALRSAMRRAClaaaailrqGSGGcidaVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASIMDG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  71 KNLSFGAVGAISNVFHPSRVARHLAhsnwwKQRRL-------LHPLILVGRGAEKYAVKN--DFPTCTPEE---LVSKAA 138
Cdd:PLN02937   94 DSGAFGAVGAVPGVRNAIQIAALLA-----KEQMMgssllgrIPPMFLVGEGARQWAKSKgiDLPETVEEAekwLVTERA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 139 KESFEKYlHRML---------------------HPYDTH---------------------DTVGAISINTNTmNSESGTS 176
Cdd:PLN02937  169 KEQWKKY-KTMLasaiaksscdsqstsklseleAPRSNPsngtgggqssmctasdedcimDTVGVICVDSEG-NIASGAS 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972265862 177 SGGIVLKHSGRLGHSCVYGSGTW-SERRQYEEPFdqvserTISICSTGHGESLVkadfcRGIATR 240
Cdd:PLN02937  247 SGGIAMKVSGRVGLAAMYGSGCWaSSKGPFGAPF------IVGCCVSGAGEYLM-----RGFAAR 300
Asparaginase_2 pfam01112
Asparaginase;
6-241 2.25e-24

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 100.74  E-value: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862   6 IIAVHGGACAKFD-ASLAEDCRFA------CG----------TGTVENALTDLERIEKFNCGFGSHLTIDQEVECEASYM 68
Cdd:pfam01112   1 VLVIHGGAGSILRtKEREEAYRAGlkealeAGyavlaaggsaLDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  69 SSKNLSFGAVGAISNVFHPSRVARHLA----HSnwwkqrrllhplILVGRGAEKYAVKNDFPTCTPEELVSKAAKESFEK 144
Cdd:pfam01112  81 DGKTLRAGAVAGVSRIKNPISLARAVMektpHV------------MLSGEGAEQFAREMGLERVPPEDFLTEERLQELQK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 145 YLHRM---------------LHPYDTHDTVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSERRqyeepF 209
Cdd:pfam01112 149 ARKENfqpnmalnvapdplkECGDSKRGTVGAVALDSEG-NLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNA-----T 222
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1972265862 210 DQVSertisicSTGHGESLVKADFCRGIATRV 241
Cdd:pfam01112 223 GAVS-------ATGHGEDIIRETLAYDIVARM 247
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
7-241 3.42e-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: 99.07  E-value: 3.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862   7 IAVHGGA----CAKFDASLAEDCRFA--------------CGTG--TVENALTDLERIEKFNCGFGSHLTIDQEVECEAS 66
Cdd:cd04701     2 LAIHGGAgtisRANLTPERYAAYRAAlrraleagyavlasGGSAldAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEAS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  67 YMSSKNLSFGAVGAISNVFHPSRVARHLAHSNWwkqrrllHPLiLVGRGAEKYAVKNDfptctpEELVSkaakesfekyl 146
Cdd:cd04701    82 IMDGRTKRAGAVAGLRRVRNPILLARAVLEKSP-------HVL-LSGEGAEEFAREQG------LELVP----------- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 147 hrmlhpydtHDTVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSErrqyeepfdqvsERTISICSTGHGE 226
Cdd:cd04701   137 ---------QGTVGAVALDSDG-NLAAATSTGGLTNKLPGRIGDTPIIGAGFWAE------------EWAVAVSGTGNGD 194
                         250
                  ....*....|....*
gi 1972265862 227 SLVKADFCRGIATRV 241
Cdd:cd04701   195 SFIRVAAARDVAARM 209
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
6-273 1.49e-22

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: 94.25  E-value: 1.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862   6 IIAVHGGACAkfDASLAEDCRFACGTGT------------VENALTDLERIEKFNCGFGSHLTIDQEVECEASYMSSKNl 73
Cdd:cd04703     2 AVLVHGGAGS--DPERQDGLERAAEAGLaelqnggdaldaVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAVMTSGG- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  74 SFGAVGAISNVFHPSRVARHLAhsnwwkqRRLLHpLILVGRGAEKYAVKNDFPtctpeelvskaakesfekylhrmlhpy 153
Cdd:cd04703    79 AFGAVAAIEGVKNPVLVARAVM-------ETSPH-VLLAGDGAVRFARRLGYP--------------------------- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 154 DTHDTVGAISINTNTMnsESGTSSGGIVLKHSGRLGHSCVYGSGTwserrqYEEPFDQVSertisicSTGHGESLVKADF 233
Cdd:cd04703   124 DGCDTVGAVARDGGKF--AAAVSTGGTSPALRGRVGDVPIIGAGF------YAGPKGAVA-------ATGIGEEIAKRLL 188
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1972265862 234 CRGIATRVlddEEGIMYSEIIREFIhEKMEHGSRYGGIAL 273
Cdd:cd04703   189 ARRVYRWI---ETGLSLQAAAQRAI-DEFDDGVAVGVIAV 224
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
7-275 3.81e-19

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 86.30  E-value: 3.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862   7 IAVHGGAcAKFDASLAEDCRFAC----------GTGTVENALTDLERIE----------KFNCGFGSHLTIDQEVECEAS 66
Cdd:PLN02689    6 IALHGGA-GDIDPNLPRERQEEAeaalrrcldlGIAALRSSLPALDVVElvvrelendpLFNAGRGSVLTEDGTVEMEAS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  67 YMSSKNLSFGAVGAISNVFHPSRVARHLA----HSnwwkqrrllhplILVGRGAEKYAVKNDFPTCTPEELVSKAAKESF 142
Cdd:PLN02689   85 IMDGRTRRCGAVSGLTTVVNPISLARLVMektpHI------------YLAFDGAEAFARQQGVETVDNSYFITEENVERL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 143 --EKYLHRMLHPY------------------DTHDTVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTwser 202
Cdd:PLN02689  153 kqAKEANSVQFDYripldkpakaaalaadgdAQPETVGCVAVDSDG-NCAAATSTGGLVNKMVGRIGDTPIIGAGT---- 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972265862 203 rqYEEPFDQVSertisicSTGHGESLVKADFCRGIATRVldDEEGIMYSEIIREFIHEKMEHGsrYGGiaLIA 275
Cdd:PLN02689  228 --YANHLCAVS-------ATGKGEAIIRGTVARDVAAVM--EYKGLPLQEAVDYVIKERLPEG--PAG--LIA 285
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
34-197 7.79e-18

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: 82.22  E-value: 7.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  34 VENALTdleRIEKFNC----GFGSHLTIDQEVECEASYMSSKNLSFGAVGAISNVFHPSRVAR----HLAHSnwwkqrrl 105
Cdd:cd04513    29 VEAGCS---VCEDDQCdgsvGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVARavmeHTPHS-------- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 106 lhplILVGRGAEKYAVKNDFPtctPEELVSKAAKESFEKYL----------------------------HRMLHPYDTHD 157
Cdd:cd04513    98 ----LLVGEGATEFAVSMGFK---EENLLTEESRKMWKKWLkencqpnfwknvvpdpskscsspkapsrSESAIPEDNHD 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1972265862 158 TVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSG 197
Cdd:cd04513   171 TIGMIALDANG-NIAAGTSTSGAAFKIPGRVGDSPIPGAG 209
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
6-286 2.86e-15

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 75.37  E-value: 2.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862   6 IIAVHGGACA--KFDASLAEDCRFA------CGTG------------TVENALTDLERIEKFNCGFGSHLTIDQEVECEA 65
Cdd:PRK10226    5 VIAIHGGAGAisRAQMSLQQELRYIealsaiVETGqkmleagesaldVVTEAVRLLEECPLFNAGIGAVFTRDETHELDA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  66 SYMSSKNLSFGAVGAISNVFHPSRVARHLahsnwwkQRRLLHpLILVGRGAEKYA-------VKNDFPTcTPEELVS-KA 137
Cdd:PRK10226   85 CVMDGNTLKAGAVAGVSHLRNPVLAARLV-------MEQSPH-VMMIGEGAENFAfahgmerVSPEIFS-TPLRYEQlLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 138 AKESFEKYLHRMLHPYDTHD---TVGAISINTNTmNSESGTSSGGIVLKHSGRLGHSCVYGSGTWSerrqyeepfdqvSE 214
Cdd:PRK10226  156 ARAEGATVLDHSGAPLDEKQkmgTVGAVALDLDG-NLAAATSTGGMTNKLPGRVGDSPLVGAGCYA------------NN 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972265862 215 RTISICSTGHGESLVKADFCRGIATrvLDDEEGIMYSEIIREFIHEKMEHGSRYGGiaLIADKFKDRMSLEF 286
Cdd:PRK10226  223 ASVAVSCTGTGEVFIRALAAYDIAA--LMDYGGLSLAEACERVVMEKLPALGGSGG--LIAIDHEGNVALPF 290
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
33-273 2.13e-13

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: 69.17  E-value: 2.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862  33 TVENALTDLERIEKFNCGFGSHLTIDQEVECEASYMSSKNLSFGAVGAISNVFHPSRVARHLAHSnwwKQRrllhplILV 112
Cdd:cd14949    46 AVVYAVSLLEDDPLFNAGTGSQIQSDGQIRMSASLMDGQTQRFSGVINIENVKNPIEVAQKLQQE---DDR------VLS 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 113 GRGAEKYAVKNDFP---TCTPEELVSKAAKESFEkylhrmlhpyDTHDTVGAISINTNTmNSESGTSSGGIVLKHSGRLG 189
Cdd:cd14949   117 GEGATEFARENGFPeynPETPQRRQEYEEKKLKS----------GGTGTVGCVALDSDG-KLAAATSTGGKGFEIPGRVS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972265862 190 HSC-VYGSgtwserrqYEEPFDQVSertisiCsTGHGESLVKADFCRGIATRVLDdeeGIMYSEIIREFIHEKMEHGSRY 268
Cdd:cd14949   186 DSAtVAGN--------YANAFAGVS------C-TGIGEDIVSEALAAKIVTRVTD---GMSLQEAFEKSFAEAKPRDGFA 247

                  ....*
gi 1972265862 269 GGIAL 273
Cdd:cd14949   248 GAIGI 252
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH