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Conserved domains on  [gi|24657358|ref|NP_611615|]
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uncharacterized protein Dmel_CG4372 [Drosophila melanogaster]

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 ...
54-356 3.30e-143

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: 408.87  E-value: 3.30e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  54 LLISTWNYTDANLQAWSVLQQGpRRTRQAVIQGCMACQNQRCGRLLTGRSSPDTEGALTLEAAIMDGESLEYGAVAGMNG 133
Cdd:cd04513   1 LVINTWNFTEAVEAAWEVLQKG-GSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 134 VRNAILVADAVLKYTKHSVLVGKSATKFARSLGYKEEYLTDARTRNVLKKWRSNGCQPNFWRDVHPSPAENCgpysplpe 213
Cdd:cd04513  80 IKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC-------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 214 HMHQHPMHQEYAIIQGQHDQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVPGAGIYADNEVGGAVASGDGDVLMRH 293
Cdd:cd04513 152 SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRF 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24657358 294 LPAFLAVEAMRAGKEPDKAAELVVQRLLRHNT-EFNGAVVVVNRRGIYAAACAGlDEFHFVVSG 356
Cdd:cd04513 232 LPSYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG-EGFSYAVRT 294
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
54-356 3.30e-143

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: 408.87  E-value: 3.30e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  54 LLISTWNYTDANLQAWSVLQQGpRRTRQAVIQGCMACQNQRCGRLLTGRSSPDTEGALTLEAAIMDGESLEYGAVAGMNG 133
Cdd:cd04513   1 LVINTWNFTEAVEAAWEVLQKG-GSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 134 VRNAILVADAVLKYTKHSVLVGKSATKFARSLGYKEEYLTDARTRNVLKKWRSNGCQPNFWRDVHPSPAENCgpysplpe 213
Cdd:cd04513  80 IKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC-------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 214 HMHQHPMHQEYAIIQGQHDQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVPGAGIYADNEVGGAVASGDGDVLMRH 293
Cdd:cd04513 152 SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRF 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24657358 294 LPAFLAVEAMRAGKEPDKAAELVVQRLLRHNT-EFNGAVVVVNRRGIYAAACAGlDEFHFVVSG 356
Cdd:cd04513 232 LPSYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG-EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
68-344 1.04e-59

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 195.88  E-value: 1.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358    68 AWSVLQQGpRRTRQAVIQGCMACQNQRCGRLLTGrSSPDTEGALTLEAAIMDGESLEYGAVAGMNGVRNAILVADAVLKY 147
Cdd:pfam01112  32 GYAVLAAG-GSALDAVEAAVRLLEDDPLFNAGKG-SVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLARAVMEK 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358   148 TKHSVLVGKSATKFARSLG---YKEEYL-TDARtRNVLKKWRSNGCQPNFWRDVHPSPAENCGPYsplpehmhqhpmhqe 223
Cdd:pfam01112 110 TPHVMLSGEGAEQFAREMGlerVPPEDFlTEER-LQELQKARKENFQPNMALNVAPDPLKECGDS--------------- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358   224 yaiiqgQHDQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVPGAGIYADNEVGGAVASGDGDVLMRHLPAFLAVEAM 303
Cdd:pfam01112 174 ------KRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYDIVARM 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 24657358   304 RAGKEPDKAAELVVQRLLRHNTEFnGAVVVVNRRGIYAAAC 344
Cdd:pfam01112 248 EYGLSLEEAADKVITEMLKRVGGD-GGVIAVDAKGNIAAPF 287
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
45-344 4.67e-56

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 186.47  E-value: 4.67e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  45 GTKKTEIQS-LLISTWN--YTDANLQAWSVLQQGpRRTRQAVIQGCM---ACQNQRCGRlltGrSSPDTEGALTLEAAIM 118
Cdd:COG1446  15 GTIARSAMTpEVEAAYRagLRAALEAGYAVLEAG-GSALDAVEAAVRvleDDPLFNAGK---G-AVLTRDGTVELDASIM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 119 DGESLEYGAVAGMNGVRNAILVADAVLKYTKHSVLVGKSATKFARSLGYKEEYLTDARTRNVLKKWRSNgcqpnfwrdvh 198
Cdd:COG1446  90 DGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKA----------- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 199 pspaencgpysplpehmhqhpMHQEYAIIQGQHDQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVPGAGIYADNEV 278
Cdd:COG1446 159 ---------------------LEYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEV 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24657358 279 GGAVASGDGDVLMRHLPAFLAVEAMRAGKEPDKAAELVVQRLLRHNtEFNGAVVVVNRRGIYAAAC 344
Cdd:COG1446 218 GAVSATGHGEYFIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPF 282
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
113-306 2.78e-20

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 90.39  E-value: 2.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  113 LEAAIMDGESLEYGAVAGMNGVRNAILVADAVLKYTKHSVLVGKSATKFARSLGYK----EEYLTDARTRNVLKKwrsng 188
Cdd:PRK10226  82 LDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMErvspEIFSTPLRYEQLLAA----- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  189 cqpnfwRDVHPSPAENCGpySPLPEhmhqhpmhqeyaiiQGQHDQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVP 268
Cdd:PRK10226 157 ------RAEGATVLDHSG--APLDE--------------KQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLV 214
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 24657358  269 GAGIYADNEVGGAVASGDGDVLMRHLPAFLAVEAMRAG 306
Cdd:PRK10226 215 GAGCYANNASVAVSCTGTGEVFIRALAAYDIAALMDYG 252
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
54-356 3.30e-143

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: 408.87  E-value: 3.30e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  54 LLISTWNYTDANLQAWSVLQQGpRRTRQAVIQGCMACQNQRCGRLLTGRSSPDTEGALTLEAAIMDGESLEYGAVAGMNG 133
Cdd:cd04513   1 LVINTWNFTEAVEAAWEVLQKG-GSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 134 VRNAILVADAVLKYTKHSVLVGKSATKFARSLGYKEEYLTDARTRNVLKKWRSNGCQPNFWRDVHPSPAENCgpysplpe 213
Cdd:cd04513  80 IKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSC-------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 214 HMHQHPMHQEYAIIQGQHDQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVPGAGIYADNEVGGAVASGDGDVLMRH 293
Cdd:cd04513 152 SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRF 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24657358 294 LPAFLAVEAMRAGKEPDKAAELVVQRLLRHNT-EFNGAVVVVNRRGIYAAACAGlDEFHFVVSG 356
Cdd:cd04513 232 LPSYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG-EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
68-344 1.04e-59

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 195.88  E-value: 1.04e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358    68 AWSVLQQGpRRTRQAVIQGCMACQNQRCGRLLTGrSSPDTEGALTLEAAIMDGESLEYGAVAGMNGVRNAILVADAVLKY 147
Cdd:pfam01112  32 GYAVLAAG-GSALDAVEAAVRLLEDDPLFNAGKG-SVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLARAVMEK 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358   148 TKHSVLVGKSATKFARSLG---YKEEYL-TDARtRNVLKKWRSNGCQPNFWRDVHPSPAENCGPYsplpehmhqhpmhqe 223
Cdd:pfam01112 110 TPHVMLSGEGAEQFAREMGlerVPPEDFlTEER-LQELQKARKENFQPNMALNVAPDPLKECGDS--------------- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358   224 yaiiqgQHDQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVPGAGIYADNEVGGAVASGDGDVLMRHLPAFLAVEAM 303
Cdd:pfam01112 174 ------KRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYDIVARM 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 24657358   304 RAGKEPDKAAELVVQRLLRHNTEFnGAVVVVNRRGIYAAAC 344
Cdd:pfam01112 248 EYGLSLEEAADKVITEMLKRVGGD-GGVIAVDAKGNIAAPF 287
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
45-344 4.67e-56

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 186.47  E-value: 4.67e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  45 GTKKTEIQS-LLISTWN--YTDANLQAWSVLQQGpRRTRQAVIQGCM---ACQNQRCGRlltGrSSPDTEGALTLEAAIM 118
Cdd:COG1446  15 GTIARSAMTpEVEAAYRagLRAALEAGYAVLEAG-GSALDAVEAAVRvleDDPLFNAGK---G-AVLTRDGTVELDASIM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 119 DGESLEYGAVAGMNGVRNAILVADAVLKYTKHSVLVGKSATKFARSLGYKEEYLTDARTRNVLKKWRSNgcqpnfwrdvh 198
Cdd:COG1446  90 DGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKA----------- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 199 pspaencgpysplpehmhqhpMHQEYAIIQGQHDQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVPGAGIYADNEV 278
Cdd:COG1446 159 ---------------------LEYKPIINERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEV 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24657358 279 GGAVASGDGDVLMRHLPAFLAVEAMRAGKEPDKAAELVVQRLLRHNtEFNGAVVVVNRRGIYAAAC 344
Cdd:COG1446 218 GAVSATGHGEYFIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPF 282
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
64-344 8.25e-42

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: 147.33  E-value: 8.25e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  64 ANLQAWSVLQQGpRRTRQAViqgcmacqnQRCGRLL---------TGrSSPDTEGALTLEAAIMDGESLEYGAVAGMNGV 134
Cdd:cd04512  26 ALEAGREVLEKG-GSALDAV---------EAAVRLLeddplfnagRG-SVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 135 RNAILVADAVLKYTKHSVLVGKSATKFARSLGykeeyltdartrnvlkkwrsngcqpnfwrdvhpspaencgpysplpeh 214
Cdd:cd04512  95 KNPISLARAVMEKTPHVLLVGEGAERFAREHG------------------------------------------------ 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 215 mhqhpmhqeyaiiqgqHDQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVPGAGIYADNEVGGAVASGDGDVLMRHL 294
Cdd:cd04512 127 ----------------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTV 190
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 24657358 295 PAFLAVEAMRAGKEPDKAAELVVQRLLRHnTEFNGAVVVVNRRGIYAAAC 344
Cdd:cd04512 191 LAKRIADLVEFGGSAQEAAEAAIDYLRRR-VGGEGGLIVVDPDGRLGAAH 239
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
103-343 7.87e-31

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: 118.07  E-value: 7.87e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 103 SSPDTEGALTLEAAIMDGESLEYGAVAGMNGVRNAILVADAVLKYTKHSVLVGKSATKFARSLGYkeeyltdartrnvlk 182
Cdd:cd14950  63 SVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIRLARKVMEKTDHVLIVGEGADELAKRLGG--------------- 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 183 kwrsngcqpnfwrdvhpspaencgpysplpehmhqhpmhqeyaiiqgqhDQLAFLALDAEGKFHVASQSSGAQFRIPGRV 262
Cdd:cd14950 128 -------------------------------------------------DTVGAVALDKDGNLAAATSTGGVWLKLPGRV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 263 GDSAVPGAGIYADNEVgGAVASGDGDVLMRHLPAFLAVEAMRAGKEPDKAAELVVQRLLRHNTEFNGAVVVVNRRGIYAA 342
Cdd:cd14950 159 GDSPIPGAGFYATNGV-AVSATGIGEVIIRSLPALRADELVSMGGDIEEAVRAVVNKVTETFGKDTAGIIGIDARGNIAA 237

                .
gi 24657358 343 A 343
Cdd:cd14950 238 A 238
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
68-344 6.06e-30

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: 116.90  E-value: 6.06e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  68 AWSVLQQGpRRTRQAVIQG--CM---ACQNQRCGRLLTgrsspdTEGALTLEAAIMDGESLEYGAVAGMNGVRNAILVAD 142
Cdd:cd04702  32 GYSVLKAG-GSALDAVEAAvrALeddPVFNAGYGSVLN------ADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLAR 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 143 AVLKYTKHSVLVGKSATKFARSLGYKE---EYLTDARTRNVLKKWRSNGCQPNFWRdvhpspaencgpysplpehmhqhp 219
Cdd:cd04702 105 LVMEKTPHCFLTGRGANKFAEEMGIPQvppESLVTERARERLEKFKKEKGANVEDT------------------------ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 220 mhqeyaiiQGQHDQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVPGAGIYADNEVGGAVASGDGDVLMRHLPAFLA 299
Cdd:cd04702 161 --------QRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNLARLI 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 24657358 300 VEAMRAGKEPDKAAELVVQrLLRHNTEFNGAVVVVNRRGIYAAAC 344
Cdd:cd04702 233 LFHMEQGKTAEEAAELALA-YMKSRVKGLGGLIVVSKTGDWGAKF 276
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
100-343 8.83e-25

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: 101.57  E-value: 8.83e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 100 TGrSSPDTEGALTLEAAIMDGESlEYGAVAGMNGVRNAILVADAVLKYTKHSVLVGKSATKFARSLGYKEEyltdartrn 179
Cdd:cd04703  57 TG-SVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVARAVMETSPHVLLAGDGAVRFARRLGYPDG--------- 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 180 vlkkwrsngcqpnfwrdvhpspaencgpysplpehmhqhpmhqeyaiiqgqHDQLAFLALDAeGKFHVASQSSGAQFRIP 259
Cdd:cd04703 126 ---------------------------------------------------CDTVGAVARDG-GKFAAAVSTGGTSPALR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 260 GRVGDSAVPGAGIYADnEVGGAVASGDGDVLMRHLPAFLAVEAMRAGKEPDKAAELVVqrllrhnTEFNGA----VVVVN 335
Cdd:cd04703 154 GRVGDVPIIGAGFYAG-PKGAVAATGIGEEIAKRLLARRVYRWIETGLSLQAAAQRAI-------DEFDDGvavgVIAVS 225

                ....*...
gi 24657358 336 RRGIYAAA 343
Cdd:cd04703 226 RRGEAGIA 233
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
113-338 4.76e-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: 99.84  E-value: 4.76e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 113 LEAAIMDGESLEYGAVAGMNGVRNAILVADAVLKYTKHSVLVGKSATKFARSLGYKEEyltdartrnvlkkwrsngcqpn 192
Cdd:cd04701  78 LEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELV---------------------- 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 193 fwrdvhpsPAENCGpysplpehmhqhpmhqeyAIiqgqhdqlaflALDAEGkfHVASQSS--GAQFRIPGRVGDSAVPGA 270
Cdd:cd04701 136 --------PQGTVG------------------AV-----------ALDSDG--NLAAATStgGLTNKLPGRIGDTPIIGA 176
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24657358 271 GIYADNEVGGAVASGDGDVLMRHLPAFLAVEAMR-AGKEPDKAAELVVQRLLRHnTEFNGAVVVVNRRG 338
Cdd:cd04701 177 GFWAEEWAVAVSGTGNGDSFIRVAAARDVAARMRyKGLSLAEAAKEVVGPGGEL-GEGEGGIIAIDARG 244
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
113-306 2.78e-20

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 90.39  E-value: 2.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  113 LEAAIMDGESLEYGAVAGMNGVRNAILVADAVLKYTKHSVLVGKSATKFARSLGYK----EEYLTDARTRNVLKKwrsng 188
Cdd:PRK10226  82 LDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMErvspEIFSTPLRYEQLLAA----- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  189 cqpnfwRDVHPSPAENCGpySPLPEhmhqhpmhqeyaiiQGQHDQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVP 268
Cdd:PRK10226 157 ------RAEGATVLDHSG--APLDE--------------KQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLV 214
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 24657358  269 GAGIYADNEVGGAVASGDGDVLMRHLPAFLAVEAMRAG 306
Cdd:PRK10226 215 GAGCYANNASVAVSCTGTGEVFIRALAAYDIAALMDYG 252
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
95-345 8.23e-20

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 89.38  E-value: 8.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358   95 CGRLLTGRSSPDTE-GALTLEAAIMDGESLEYGAVAGMNGVRNAILVADAVLKYTKHSVLVGKSATKFARSLGYK----E 169
Cdd:PLN02689  62 DPLFNAGRGSVLTEdGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVEtvdnS 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  170 EYLTDartRNVLKKWRSNGCQPNFWrDVHPsPAENCGPYSPLPehmhqhpmhqeyAIIQGQHDQLAFLALDAEGKFHVAS 249
Cdd:PLN02689 142 YFITE---ENVERLKQAKEANSVQF-DYRI-PLDKPAKAAALA------------ADGDAQPETVGCVAVDSDGNCAAAT 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  250 QSSGAQFRIPGRVGDSAVPGAGIYAdNEVGGAVASGDGDVLMRHLPAFLAVEAMRAGKEP-DKAAELVVQRLLRHNTefn 328
Cdd:PLN02689 205 STGGLVNKMVGRIGDTPIIGAGTYA-NHLCAVSATGKGEAIIRGTVARDVAAVMEYKGLPlQEAVDYVIKERLPEGP--- 280
                        250
                 ....*....|....*..
gi 24657358  329 GAVVVVNRRGiyAAACA 345
Cdd:PLN02689 281 AGLIAVSATG--EVAMA 295
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
67-287 3.90e-15

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: 74.95  E-value: 3.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  67 QAWSVLQQGprRTRQAVIQGCmacqnqrcgRLL---------TGrSSPDTEGALTLEAAIMDGESLEYGAVAGMNGVRNA 137
Cdd:cd14949  33 EVYEYLKSH--SALEAVVYAV---------SLLeddplfnagTG-SQIQSDGQIRMSASLMDGQTQRFSGVINIENVKNP 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 138 ILVADAVLKYtKHSVLVGKSATKFARSLGYkeeyltdartrnvlkkwrsngcqpnfwrdvhpspaencGPYSPL-PEHMh 216
Cdd:cd14949 101 IEVAQKLQQE-DDRVLSGEGATEFARENGF--------------------------------------PEYNPEtPQRR- 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24657358 217 qhpmhQEYAIIQ---GQHDQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVPgAGIYAdNEVGGAVASGDG 287
Cdd:cd14949 141 -----QEYEEKKlksGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNYA-NAFAGVSCTGIG 207
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
64-296 2.60e-13

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 71.05  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358   64 ANLQAWSVLQQGPRRTRQAVIQGCMACQNQRCGRllTGRSSPDTE-GALTLEAAIMDGESLEYGAVAGMNGVRNAILVAD 142
Cdd:PLN02937  38 ACLAAAAILRQGSGGCIDAVSAAIQVLEDDPSTN--AGRGSNLTEdGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  143 AVLKYTKHS----------VLVGKSATKFARSLGYK--------EEYLTDARTRNVLKKWRsngcqpNFWRDVHPSPAEN 204
Cdd:PLN02937 116 LLAKEQMMGssllgrippmFLVGEGARQWAKSKGIDlpetveeaEKWLVTERAKEQWKKYK------TMLASAIAKSSCD 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358  205 CGPYSPLPEhmHQHPMHQEYAIIQGQH-------------DQLAFLALDAEGKFHVASQSSGAQFRIPGRVGDSAVPGAG 271
Cdd:PLN02937 190 SQSTSKLSE--LEAPRSNPSNGTGGGQssmctasdedcimDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSG 267
                        250       260       270
                 ....*....|....*....|....*....|..
gi 24657358  272 IYADNE-------VGGAVASGDGDVLMRHLPA 296
Cdd:PLN02937 268 CWASSKgpfgapfIVGCCVSGAGEYLMRGFAA 299
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
100-319 5.32e-09

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: 56.90  E-value: 5.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 100 TGR-SSPDTEGALTLEAAIMDGESLEYGAVAGMNGVRNAILVADAVLKY--TKHS-------VLVGKSATKFARSLGYke 169
Cdd:cd04514  60 AGYgSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKEqrKPLSlgrvppmFLVGEGAREWAKSKGI-- 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24657358 170 eyLTDarTrnvlkkwrsngcqpnfwrdVhpspaencGpysplpehmhqhpmhqeyAIiqgqhdqlaflALDAEGkfHVAS 249
Cdd:cd04514 138 --ITD--T-------------------V--------G------------------AI-----------AIDLYG--NIAA 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24657358 250 QSS--GAQFRIPGRVGDSAVPGAGIYA---DNEVGGAVA---SGDGDVLMRHLPAFLAVEAMRAGKEPDKAAELVVQR 319
Cdd:cd04514 156 GSSsgGIGLKHPGRVGPAALYGAGCWAeprDPDDKTSVAvvtSGTGEHIATTMLARRCAERLYHSTRREESDEDEILR 233
 
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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