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Conserved domains on  [gi|72255513|ref|NP_001026811|]
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N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase precursor [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 ...
 29-331 1.13e-158

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: 445.85  E-value: 1.13e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  29 LVVNTWPFKNATEAAWWTLVSGGSALDAVEKGCAMCEKEQCGGTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRI 108
Cdd:cd04513   1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 109 KNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPSKYCgpykppDFL 188
Cdd:cd04513  81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC------SSP 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 189 EQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPS 268
Cdd:cd04513 155 KAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLPS 234

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72255513 269 YQAVEYMRGGDDPARACQKVISRIQKYYPK-FFGAVICANVTGSYGAACNRlptfTQFSFMVYN 331
Cdd:cd04513 235 YQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 29-331 1.13e-158

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: 445.85  E-value: 1.13e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  29 LVVNTWPFKNATEAAWWTLVSGGSALDAVEKGCAMCEKEQCGGTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRI 108
Cdd:cd04513   1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 109 KNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPSKYCgpykppDFL 188
Cdd:cd04513  81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC------SSP 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 189 EQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPS 268
Cdd:cd04513 155 KAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLPS 234

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72255513 269 YQAVEYMRGGDDPARACQKVISRIQKYYPK-FFGAVICANVTGSYGAACNRlptfTQFSFMVYN 331
Cdd:cd04513 235 YQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
35-317 9.04e-97

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 289.10  E-value: 9.04e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513    35 PFKNATEAAWWTLVSGGSALDAVEKGCAMCEkEQCGGTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGV 114
Cdd:pfam01112  24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513   115 ARKVLEHTTHTLLVGDSATKFAVSMGFT---SEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPSKYCGPYKppdfleqn 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK-------- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513   192 nrahkevdihsHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQA 271
Cdd:pfam01112 175 -----------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYDI 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 72255513   272 VEYMRGGDDPARACQKVISRIQKYYPKfFGAVICANVTGSYGAACN 317
Cdd:pfam01112 244 VARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFN 288
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 21-317 2.21e-66

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 211.50  E-value: 2.21e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  21 VRGSNPLPLVVNTWPF--KNATEAAWWTLVSGGSALDAVEKGCAMCEKeqCGG-TVGFGGSPDEVGETTLDAMIMDGTAM 97
Cdd:COG1446  17 IARSAMTPEVEAAYRAglRAALEAGYAVLEAGGSALDAVEAAVRVLED--DPLfNAGKGAVLTRDGTVELDASIMDGATL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  98 DVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRAlhsDWLSrncqpnywrnvipdpsk 177
Cdd:COG1446  95 RAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEK---RWKQ----------------- 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 178 ycgpykppdfLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGayaddmagaaaatg 257
Cdd:COG1446 155 ----------WKKALEYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAG-------------- 210

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 72255513 258 dgdT-----------------LLRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYpKFFGAVICANVTGSYGAACN 317
Cdd:COG1446 211 ---TyadnevgavsatghgeyFIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPFN 283
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 47-243 2.54e-25

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 103.63  E-value: 2.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513   47 LVSGGSALDAVE---------------KGCAMCEKeqcgGTVgfggspdevgetTLDAMIMDGTAMDVGAVGGLRRIKNA 111
Cdd:PLN02689  42 LRSSLPALDVVElvvrelendplfnagRGSVLTED----GTV------------EMEASIMDGRTRRCGAVSGLTTVVNP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  112 IGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHsDWLSRNCQPNywrNVIPDpskycgpYKPPDFLEQN 191
Cdd:PLN02689 106 ISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENV-ERLKQAKEAN---SVQFD-------YRIPLDKPAK 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 72255513  192 NRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 243
Cdd:PLN02689 175 AAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAG 226
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 29-331 1.13e-158

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: 445.85  E-value: 1.13e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  29 LVVNTWPFKNATEAAWWTLVSGGSALDAVEKGCAMCEKEQCGGTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRI 108
Cdd:cd04513   1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 109 KNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPSKYCgpykppDFL 188
Cdd:cd04513  81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC------SSP 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 189 EQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPS 268
Cdd:cd04513 155 KAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLPS 234

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 72255513 269 YQAVEYMRGGDDPARACQKVISRIQKYYPK-FFGAVICANVTGSYGAACNRlptfTQFSFMVYN 331
Cdd:cd04513 235 YQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
35-317 9.04e-97

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 289.10  E-value: 9.04e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513    35 PFKNATEAAWWTLVSGGSALDAVEKGCAMCEkEQCGGTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGV 114
Cdd:pfam01112  24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513   115 ARKVLEHTTHTLLVGDSATKFAVSMGFT---SEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPSKYCGPYKppdfleqn 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK-------- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513   192 nrahkevdihsHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQA 271
Cdd:pfam01112 175 -----------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYDI 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 72255513   272 VEYMRGGDDPARACQKVISRIQKYYPKfFGAVICANVTGSYGAACN 317
Cdd:pfam01112 244 VARMEYGLSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFN 288
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 21-317 2.21e-66

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 211.50  E-value: 2.21e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  21 VRGSNPLPLVVNTWPF--KNATEAAWWTLVSGGSALDAVEKGCAMCEKeqCGG-TVGFGGSPDEVGETTLDAMIMDGTAM 97
Cdd:COG1446  17 IARSAMTPEVEAAYRAglRAALEAGYAVLEAGGSALDAVEAAVRVLED--DPLfNAGKGAVLTRDGTVELDASIMDGATL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  98 DVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRAlhsDWLSrncqpnywrnvipdpsk 177
Cdd:COG1446  95 RAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEK---RWKQ----------------- 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 178 ycgpykppdfLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGayaddmagaaaatg 257
Cdd:COG1446 155 ----------WKKALEYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAG-------------- 210

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 72255513 258 dgdT-----------------LLRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYpKFFGAVICANVTGSYGAACN 317
Cdd:COG1446 211 ---TyadnevgavsatghgeyFIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPFN 283
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 39-317 1.56e-47

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: 160.81  E-value: 1.56e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  39 ATEAAWWTLVSGGSALDAVEKGCAMCEKEqcgGT--VGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVAR 116
Cdd:cd04512  26 ALEAGREVLEKGGSALDAVEAAVRLLEDD---PLfnAGRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLAR 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 117 KVLEHTTHTLLVGDSATKFAVSMGftsedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnrahk 196
Cdd:cd04512 103 AVMEKTPHVLLVGEGAERFAREHG-------------------------------------------------------- 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 197 evdihsHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEYMR 276
Cdd:cd04512 127 ------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLVE 200

                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 72255513 277 GGDDPARACQKVISRIqKYYPKFFGAVICANVTGSYGAACN 317
Cdd:cd04512 201 FGGSAQEAAEAAIDYL-RRRVGGEGGLIVVDPDGRLGAAHN 240
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 37-317 2.85e-39

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: 139.25  E-value: 2.85e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  37 KNATEAAWwTLVSGGSALDAVEKGCAMCEKEqcgG--TVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGV 114
Cdd:cd14950  25 REALERGY-EALRRGSALEAVVEAVAYMEDS---GvfNAGVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIRL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 115 ARKVLEHTTHTLLVGDSATKFAVSMGFtsedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnra 194
Cdd:cd14950 101 ARKVMEKTDHVLIVGEGADELAKRLGG----------------------------------------------------- 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 195 hkevdihshDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGaYADDMAGAAAATGDGDTLLRFLPSYQAVEY 274
Cdd:cd14950 128 ---------DTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAG-FYATNGVAVSATGIGEVIIRSLPALRADEL 197

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 72255513 275 MRGGDDPARACQKVISRIQKYYPKFFGAVICANVTGSYGAACN 317
Cdd:cd14950 198 VSMGGDIEEAVRAVVNKVTETFGKDTAGIIGIDARGNIAAAFN 240
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 37-243 1.90e-36

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: 133.08  E-value: 1.90e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  37 KNATEAAWWTLVSGGSALDAVEKGCAMCEKEQCGGTvGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVAR 116
Cdd:cd04702  26 KRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNA-GYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLAR 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 117 KVLEHTTHTLLVGDSATKFAVSMGFT---SEDLSTNTSRALHSDWLSRNCQPNywrnvipdpsKYCGpykppdfleqnnr 193
Cdd:cd04702 105 LVMEKTPHCFLTGRGANKFAEEMGIPqvpPESLVTERARERLEKFKKEKGANV----------EDTQ------------- 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 72255513 194 ahkevdiHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 243
Cdd:cd04702 162 -------RGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSG 204
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 47-243 6.86e-30

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: 114.87  E-value: 6.86e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  47 LVSGGSALDAVEKgcAMCEKEQCG-GTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTHT 125
Cdd:cd04701  39 LASGGSALDAVTA--AVRLLEDCPlFNAGKGAVFTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHV 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 126 LLVGDSATKFAVSMGftsedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnrahkeVDIHSHDT 205
Cdd:cd04701 117 LLSGEGAEEFAREQG---------------------------------------------------------LELVPQGT 139

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 72255513 206 IGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 243
Cdd:cd04701 140 VGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAG 177
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 37-318 5.06e-26

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: 103.88  E-value: 5.06e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  37 KNATEAAWWTLVSGGSALDAVEKGCAMCEKEQC--GGTvgfGGSPDEVGETTLDAMIMDGTAmDVGAVGGLRRIKNAIGV 114
Cdd:cd04703  20 ERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRfnAGT---GSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLV 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 115 ARKVLEHTTHTLLVGDSATKFAVSMGFTsedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnra 194
Cdd:cd04703  96 ARAVMETSPHVLLAGDGAVRFARRLGYP---------------------------------------------------- 123

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 195 hkevdiHSHDTIGMVV-IHktGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLpSYQAVE 273
Cdd:cd04703 124 ------DGCDTVGAVArDG--GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKGAVAATGIGEEIAKRLL-ARRVYR 194

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 72255513 274 YMRGGDDPARACQKVISRIQKYYPkffGAVICANVTGSYGAACNR 318
Cdd:cd04703 195 WIETGLSLQAAAQRAIDEFDDGVA---VGVIAVSRRGEAGIASNT 236
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 47-243 2.54e-25

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 103.63  E-value: 2.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513   47 LVSGGSALDAVE---------------KGCAMCEKeqcgGTVgfggspdevgetTLDAMIMDGTAMDVGAVGGLRRIKNA 111
Cdd:PLN02689  42 LRSSLPALDVVElvvrelendplfnagRGSVLTED----GTV------------EMEASIMDGRTRRCGAVSGLTTVVNP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  112 IGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHsDWLSRNCQPNywrNVIPDpskycgpYKPPDFLEQN 191
Cdd:PLN02689 106 ISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENV-ERLKQAKEAN---SVQFD-------YRIPLDKPAK 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 72255513  192 NRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 243
Cdd:PLN02689 175 AAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAG 226
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 47-289 3.14e-25

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 103.49  E-value: 3.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513   47 LVSGGSALDAVEKGCAMCEkeQC---GGTVGFGGSPDEVGEttLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTT 123
Cdd:PRK10226  43 LEAGESALDVVTEAVRLLE--ECplfNAGIGAVFTRDETHE--LDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSP 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  124 HTLLVGDSATKFAVSMGFTSedlstntsralhsdwlsrncqpnywrnviPDPSKYCGPYKPPDFLEQNNRAHKEVDiHSH 203
Cdd:PRK10226 119 HVMMIGEGAENFAFAHGMER-----------------------------VSPEIFSTPLRYEQLLAARAEGATVLD-HSG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  204 ---------DTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEY 274
Cdd:PRK10226 169 apldekqkmGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAAL 248

                        250
                 ....*....|....*.
gi 72255513  275 MR-GGDDPARACQKVI 289
Cdd:PRK10226 249 MDyGGLSLAEACERVV 264
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 37-243 1.09e-19

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: 88.10  E-value: 1.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  37 KNATEAAWWTLVSGGSALDAVEKGCAMCEKEQCGGTvGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVAR 116
Cdd:cd04514  25 KRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNA-GYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLAR 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 117 KVLEHTTH---------TLLVGDSATKFAVSMGFTSedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdf 187
Cdd:cd04514 104 LLLKEQRKplslgrvppMFLVGEGAREWAKSKGIIT-------------------------------------------- 139

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 72255513 188 leqnnrahkevdihshDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 243
Cdd:cd04514 140 ----------------DTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAG 179
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 51-243 3.12e-16

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: 77.65  E-value: 3.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  51 GSALDAVEKGCAMCEKEQC--GGTvgfgGS---PDevGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTtHT 125
Cdd:cd14949  41 HSALEAVVYAVSLLEDDPLfnAGT----GSqiqSD--GQIRMSASLMDGQTQRFSGVINIENVKNPIEVAQKLQQED-DR 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513 126 LLVGDSATKFAVSMGFtsedlstntsralhsdwlsrncqpnywrnvipdpskycGPYKPPDFLEQNNRAHKEVDIHSHDT 205
Cdd:cd14949 114 VLSGEGATEFARENGF--------------------------------------PEYNPETPQRRQEYEEKKLKSGGTGT 155

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 72255513 206 IGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPgAG 243
Cdd:cd14949 156 VGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AG 192
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 37-243 2.01e-12

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 67.58  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513   37 KNATEAAWWTLVSG-GSALDAVEKGCAMCEKEQCGgTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVA 115
Cdd:PLN02937  36 RRACLAAAAILRQGsGGCIDAVSAAIQVLEDDPST-NAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72255513  116 RKVLEHTTH----------TLLVGDSATKFAVSMGFtseDLSTNTSRALHsdWLSRNCQPNYWR-------NVIP----- 173
Cdd:PLN02937 115 ALLAKEQMMgssllgrippMFLVGEGARQWAKSKGI---DLPETVEEAEK--WLVTERAKEQWKkyktmlaSAIAksscd 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 72255513  174 --DPSKYCGPYKPPDFLEQNNRAHKEVDIHSH------DTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 243
Cdd:PLN02937 190 sqSTSKLSELEAPRSNPSNGTGGGQSSMCTASdedcimDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSG 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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