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Conserved domains on  [gi|1958683492|ref|XP_038950352|]
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N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase isoform X3 [Rattus norvegicus]

Protein Classification

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase( domain architecture ID 10139950)

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase catalyzes the hydrolysis of the glycosylamide bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 1-235 1.31e-112

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: 324.90  E-value: 1.31e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   1 MDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPS 80
Cdd:cd04513    69 MDVGAVAALRRIKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPS 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492  81 KYCgpykppDFLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGayaddmagaaaat 160
Cdd:cd04513   149 KSC------SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAG------------- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492 161 gdgdtL------------------LRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYPK-FFGAVICANVTGSYGAACN 221
Cdd:cd04513   210 -----LyadnevgaaaatgdgdimMRFLPSYQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAACN 284

                         250
                  ....*....|....
gi 1958683492 222 RlptfTQFSFMVYN 235
Cdd:cd04513   285 G----EGFSYAVRT 294
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 1-235 1.31e-112

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: 324.90  E-value: 1.31e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   1 MDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPS 80
Cdd:cd04513    69 MDVGAVAALRRIKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPS 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492  81 KYCgpykppDFLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGayaddmagaaaat 160
Cdd:cd04513   149 KSC------SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAG------------- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492 161 gdgdtL------------------LRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYPK-FFGAVICANVTGSYGAACN 221
Cdd:cd04513   210 -----LyadnevgaaaatgdgdimMRFLPSYQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAACN 284

                         250
                  ....*....|....
gi 1958683492 222 RlptfTQFSFMVYN 235
Cdd:cd04513   285 G----EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
1-221 1.65e-70

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 218.61  E-value: 1.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   1 MDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFT---SEDLSTNTSRALHSDWLSRNCQPNYWRNVIP 77
Cdd:pfam01112  85 LRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAP 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492  78 DPSKYCGPYKppdfleqnnrahkevdihsHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAA 157
Cdd:pfam01112 165 DPLKECGDSK-------------------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAV 225

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683492 158 AATGDGDTLLRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYPKfFGAVICANVTGSYGAACN 221
Cdd:pfam01112 226 SATGHGEDIIRETLAYDIVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFN 288
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 1-221 1.62e-47

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 159.50  E-value: 1.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   1 MD-----VGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRAlhsDWLSrncqpnywrnv 75
Cdd:COG1446    89 MDgatlrAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEK---RWKQ----------- 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492  76 ipdpskycgpykppdfLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGayaddmag 155
Cdd:COG1446   155 ----------------WKKALEYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAG-------- 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492 156 aaaatgdgdT-----------------LLRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYpKFFGAVICANVTGSYGA 218
Cdd:COG1446   211 ---------TyadnevgavsatghgeyFIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAA 280


                  ...
gi 1958683492 219 ACN 221
Cdd:COG1446   281 PFN 283
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 1-147 5.80e-20

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 86.68  E-value: 5.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   1 MDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHsDWLSRNCQPNywrNVIPDps 80
Cdd:PLN02689   91 RRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENV-ERLKQAKEAN---SVQFD-- 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683492  81 kycgpYKPPDFLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 147
Cdd:PLN02689  165 -----YRIPLDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAG 226
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 1-235 1.31e-112

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: 324.90  E-value: 1.31e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   1 MDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPS 80
Cdd:cd04513    69 MDVGAVAALRRIKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPS 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492  81 KYCgpykppDFLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGayaddmagaaaat 160
Cdd:cd04513   149 KSC------SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAG------------- 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492 161 gdgdtL------------------LRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYPK-FFGAVICANVTGSYGAACN 221
Cdd:cd04513   210 -----LyadnevgaaaatgdgdimMRFLPSYQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAACN 284

                         250
                  ....*....|....
gi 1958683492 222 RlptfTQFSFMVYN 235
Cdd:cd04513   285 G----EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
1-221 1.65e-70

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 218.61  E-value: 1.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   1 MDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFT---SEDLSTNTSRALHSDWLSRNCQPNYWRNVIP 77
Cdd:pfam01112  85 LRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAP 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492  78 DPSKYCGPYKppdfleqnnrahkevdihsHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAA 157
Cdd:pfam01112 165 DPLKECGDSK-------------------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAV 225

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683492 158 AATGDGDTLLRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYPKfFGAVICANVTGSYGAACN 221
Cdd:pfam01112 226 SATGHGEDIIRETLAYDIVARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFN 288
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 1-221 1.62e-47

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 159.50  E-value: 1.62e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   1 MD-----VGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRAlhsDWLSrncqpnywrnv 75
Cdd:COG1446    89 MDgatlrAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEK---RWKQ----------- 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492  76 ipdpskycgpykppdfLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGayaddmag 155
Cdd:COG1446   155 ----------------WKKALEYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAG-------- 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492 156 aaaatgdgdT-----------------LLRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYpKFFGAVICANVTGSYGA 218
Cdd:COG1446   211 ---------TyadnevgavsatghgeyFIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAA 280


                  ...
gi 1958683492 219 ACN 221
Cdd:COG1446   281 PFN 283
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 1-221 2.23e-32

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: 118.44  E-value: 2.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   1 MD-----VGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGftsedlstntsralhsdwlsrncqpnywrnv 75
Cdd:cd04512    78 MDgktlnAGAVAGVKGVKNPISLARAVMEKTPHVLLVGEGAERFAREHG------------------------------- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492  76 ipdpskycgpykppdfleqnnrahkevdihsHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAG 155
Cdd:cd04512   127 -------------------------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETG 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958683492 156 AAAATGDGDTLLRFLPSYQAVEYMRGGDDPARACQKVISRIqKYYPKFFGAVICANVTGSYGAACN 221
Cdd:cd04512   176 AVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAEAAIDYL-RRRVGGEGGLIVVDPDGRLGAAHN 240
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 1-221 2.28e-28

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: 108.05  E-value: 2.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   1 MDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFtsedlstntsralhsdwlsrncqpnywrnvipdps 80
Cdd:cd14950    83 LRVGAVAAVRAVKNPIRLARKVMEKTDHVLIVGEGADELAKRLGG----------------------------------- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492  81 kycgpykppdfleqnnrahkevdihshDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGaYADDMAGAAAAT 160
Cdd:cd14950   128 ---------------------------DTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAG-FYATNGVAVSAT 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958683492 161 GDGDTLLRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYPKFFGAVICANVTGSYGAACN 221
Cdd:cd14950   180 GIGEVIIRSLPALRADELVSMGGDIEEAVRAVVNKVTETFGKDTAGIIGIDARGNIAAAFN 240
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 4-147 9.96e-26

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: 101.88  E-value: 9.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   4 GAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFT---SEDLSTNTSRALHSDWLSRNCQPNywrnvipdps 80
Cdd:cd04702    88 GAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPqvpPESLVTERARERLEKFKKEKGANV---------- 157

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683492  81 KYCGpykppdfleqnnrahkevdiHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 147
Cdd:cd04702   158 EDTQ--------------------RGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSG 204
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 4-147 4.10e-22

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: 91.75  E-value: 4.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   4 GAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGftsedlstntsralhsdwlsrncqpnywrnvipdpskyc 83
Cdd:cd04701    91 GAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQG--------------------------------------- 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958683492  84 gpykppdfleqnnrahkeVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 147
Cdd:cd04701   132 ------------------LELVPQGTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAG 177
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 4-222 8.96e-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: 90.40  E-value: 8.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   4 GAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTsedlstntsralhsdwlsrncqpnywrnvipdpskyc 83
Cdd:cd04703    81 GAVAAIEGVKNPVLVARAVMETSPHVLLAGDGAVRFARRLGYP------------------------------------- 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492  84 gpykppdfleqnnrahkevdiHSHDTIGMVV-IHktGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGD 162
Cdd:cd04703   124 ---------------------DGCDTVGAVArDG--GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKGAVAATGIG 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492 163 GDTLLRFLpSYQAVEYMRGGDDPARACQKVISRIQKYYPkffGAVICANVTGSYGAACNR 222
Cdd:cd04703   181 EEIAKRLL-ARRVYRWIETGLSLQAAAQRAIDEFDDGVA---VGVIAVSRRGEAGIASNT 236
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 1-147 5.80e-20

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 86.68  E-value: 5.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   1 MDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHsDWLSRNCQPNywrNVIPDps 80
Cdd:PLN02689   91 RRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENV-ERLKQAKEAN---SVQFD-- 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958683492  81 kycgpYKPPDFLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 147
Cdd:PLN02689  165 -----YRIPLDKPAKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAG 226
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 1-193 4.26e-19

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 84.23  E-value: 4.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   1 MDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSedlstntsralhsdwlsrncqpnywrnviPDPS 80
Cdd:PRK10226   92 LKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMER-----------------------------VSPE 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492  81 KYCGPYKPPDFLEQNNRAHKEVDiHSH---------DTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYAD 151
Cdd:PRK10226  143 IFSTPLRYEQLLAARAEGATVLD-HSGapldekqkmGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYAN 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958683492 152 DMAGAAAATGDGDTLLRFLPSYQAVEYMR-GGDDPARACQKVI 193
Cdd:PRK10226  222 NASVAVSCTGTGEVFIRALAAYDIAALMDyGGLSLAEACERVV 264
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 10-147 3.44e-11

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: 61.86  E-value: 3.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492  10 RRIKNAIGVARKVLEHTtHTLLVGDSATKFAVSMGFtsedlstntsralhsdwlsrncqpnywrnvipdpskycGPYKPP 89
Cdd:cd14949    95 ENVKNPIEVAQKLQQED-DRVLSGEGATEFARENGF--------------------------------------PEYNPE 135

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958683492  90 DFLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPgAG 147
Cdd:cd14949   136 TPQRRQEYEEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AG 192
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 4-147 6.84e-11

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: 61.13  E-value: 6.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   4 GAVGGLRRIKNAIGVARKVLEHTTH---------TLLVGDSATKFAVSMGFTSedlstntsralhsdwlsrncqpnywrn 74
Cdd:cd04514    87 GAVGAVSGVKNPIQLARLLLKEQRKplslgrvppMFLVGEGAREWAKSKGIIT--------------------------- 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958683492  75 vipdpskycgpykppdfleqnnrahkevdihshDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 147
Cdd:cd04514   140 ---------------------------------DTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAG 179
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 4-147 4.13e-08

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 53.33  E-value: 4.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492   4 GAVGGLRRIKNAIGVARKVLEHTTH----------TLLVGDSATKFAVSMGFtseDLSTNTSRALHsdWLSRNCQPNYWR 73
Cdd:PLN02937   99 GAVGAVPGVRNAIQIAALLAKEQMMgssllgrippMFLVGEGARQWAKSKGI---DLPETVEEAEK--WLVTERAKEQWK 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958683492  74 -------NVIP-------DPSKYCGPYKPPDFLEQNNRAHKEVDIHSH------DTIGMVVIHKTGHTAAGTSTNGLKFK 133
Cdd:PLN02937  174 kyktmlaSAIAksscdsqSTSKLSELEAPRSNPSNGTGGGQSSMCTASdedcimDTVGVICVDSEGNIASGASSGGIAMK 253

                         170
                  ....*....|....
gi 1958683492 134 IPGRVGDSPIPGAG 147
Cdd:PLN02937  254 VSGRVGLAAMYGSG 267
 
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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