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Conserved domains on  [gi|312283655|ref|NP_001186022|]
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N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase precursor [Macaca mulatta]

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 ...
 29-332 5.36e-154

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: 433.91  E-value: 5.36e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  29 LVLNTWPFKNATEAAWRALASGGSALDAVESGCAMCETEQCDGSVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRI 108
Cdd:cd04513    1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 109 KNAIGVARKVLEHTTHTLLVGESATKFAESMGFVNEDLSTRASQALHSDWLARNCQPNYWRNVVPDPSKYCGPYKPLGIL 188
Cdd:cd04513   81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSCSSPKAPSRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 189 KQDIPIHketednrGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLP 268
Cdd:cd04513  161 ESAIPED-------NHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312283655 269 SYQAVKYMRGGEDPTIACQKVISKIQKYFP-DFFWAVICANGTGKLGAACNKlstfTQFSFMVFN 332
Cdd:cd04513  234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 29-332 5.36e-154

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: 433.91  E-value: 5.36e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  29 LVLNTWPFKNATEAAWRALASGGSALDAVESGCAMCETEQCDGSVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRI 108
Cdd:cd04513    1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 109 KNAIGVARKVLEHTTHTLLVGESATKFAESMGFVNEDLSTRASQALHSDWLARNCQPNYWRNVVPDPSKYCGPYKPLGIL 188
Cdd:cd04513   81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSCSSPKAPSRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 189 KQDIPIHketednrGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLP 268
Cdd:cd04513  161 ESAIPED-------NHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312283655 269 SYQAVKYMRGGEDPTIACQKVISKIQKYFP-DFFWAVICANGTGKLGAACNKlstfTQFSFMVFN 332
Cdd:cd04513  234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
35-326 2.43e-102

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 303.35  E-value: 2.43e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655   35 PFKNATEAAWRALASGGSALDAVESGCAMCEtEQCDGSVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGV 114
Cdd:pfam01112  24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  115 ARKVLEHTTHTLLVGESATKFAESMGFV---NEDLSTRASQALHSDWLARNCQPNYWRNVVPDPSKYCGPYKplgilkqd 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK-------- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  192 ipihketednrgHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLPSYQ 271
Cdd:pfam01112 175 ------------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYD 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 312283655  272 AVKYMRGGEDPTIACQKVISKIQKYFPDFFwAVICANGTGKLGAACNKLSTFTQF 326
Cdd:pfam01112 243 IVARMEYGLSLEEAADKVITEMLKRVGGDG-GVIAVDAKGNIAAPFNTEGMYRAY 296
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 37-318 3.79e-63

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 203.03  E-value: 3.79e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  37 KNATEAAWRALASGGSALDAVESGCAMCETeqcDG--SVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGV 114
Cdd:COG1446   35 RAALEAGYAVLEAGGSALDAVEAAVRVLED---DPlfNAGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 115 ARKVLEHTTHTLLVGESATKFAESMGFVNEDLSTRASQALHSDWLARNcqpnywrnvvpdpskycgPYKPLgilkqdipi 194
Cdd:COG1446  112 ARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKAL------------------EYKPI--------- 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 195 hketEDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYaddtagaaaatgdgdiL----------- 263
Cdd:COG1446  165 ----INERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTY----------------Adnevgavsatg 224

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 264 -----MRFLPSYQAVKYMRGGEDPTIACQKVISKIQKYFpDFFWAVICANGTGKLGAACN 318
Cdd:COG1446  225 hgeyfIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPFN 283
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 41-290 1.47e-25

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 104.26  E-value: 1.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  41 EAAWRALASGGSALDAVESGCAMceTEQC---DGSVGFGGSPDELGEttLDAMIMEGTTMDVGAVGDLRRIKNAIGVARK 117
Cdd:PRK10226  37 ETGQKMLEAGESALDVVTEAVRL--LEECplfNAGIGAVFTRDETHE--LDACVMDGNTLKAGAVAGVSHLRNPVLAARL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 118 VLEHTTHTLLVGESATKFAESMGF--VNEDL-ST--RASQALHsdwlARNCQpnywrNVVPDPSKycgpyKPLgilkqdi 192
Cdd:PRK10226 113 VMEQSPHVMMIGEGAENFAFAHGMerVSPEIfSTplRYEQLLA----ARAEG-----ATVLDHSG-----APL------- 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 193 pihketEDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLPSYQA 272
Cdd:PRK10226 172 ------DEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDI 245

                        250
                 ....*....|....*....
gi 312283655 273 VKYMR-GGEDPTIACQKVI 290
Cdd:PRK10226 246 AALMDyGGLSLAEACERVV 264
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 29-332 5.36e-154

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: 433.91  E-value: 5.36e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  29 LVLNTWPFKNATEAAWRALASGGSALDAVESGCAMCETEQCDGSVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRI 108
Cdd:cd04513    1 LVINTWNFTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 109 KNAIGVARKVLEHTTHTLLVGESATKFAESMGFVNEDLSTRASQALHSDWLARNCQPNYWRNVVPDPSKYCGPYKPLGIL 188
Cdd:cd04513   81 KNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWKNVVPDPSKSCSSPKAPSRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 189 KQDIPIHketednrGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLP 268
Cdd:cd04513  161 ESAIPED-------NHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLP 233

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312283655 269 SYQAVKYMRGGEDPTIACQKVISKIQKYFP-DFFWAVICANGTGKLGAACNKlstfTQFSFMVFN 332
Cdd:cd04513  234 SYQAVELMRQGMSPQEACEDAIRRIAKKYPkDFEGAVVAVNKAGEYGAACNG----EGFSYAVRT 294
Asparaginase_2 pfam01112
Asparaginase;
35-326 2.43e-102

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 303.35  E-value: 2.43e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655   35 PFKNATEAAWRALASGGSALDAVESGCAMCEtEQCDGSVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGV 114
Cdd:pfam01112  24 GLKEALEAGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  115 ARKVLEHTTHTLLVGESATKFAESMGFV---NEDLSTRASQALHSDWLARNCQPNYWRNVVPDPSKYCGPYKplgilkqd 191
Cdd:pfam01112 103 ARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK-------- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  192 ipihketednrgHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLPSYQ 271
Cdd:pfam01112 175 ------------RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYD 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 312283655  272 AVKYMRGGEDPTIACQKVISKIQKYFPDFFwAVICANGTGKLGAACNKLSTFTQF 326
Cdd:pfam01112 243 IVARMEYGLSLEEAADKVITEMLKRVGGDG-GVIAVDAKGNIAAPFNTEGMYRAY 296
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 37-318 3.79e-63

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 203.03  E-value: 3.79e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  37 KNATEAAWRALASGGSALDAVESGCAMCETeqcDG--SVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGV 114
Cdd:COG1446   35 RAALEAGYAVLEAGGSALDAVEAAVRVLED---DPlfNAGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRIKNPISL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 115 ARKVLEHTTHTLLVGESATKFAESMGFVNEDLSTRASQALHSDWLARNcqpnywrnvvpdpskycgPYKPLgilkqdipi 194
Cdd:COG1446  112 ARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKAL------------------EYKPI--------- 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 195 hketEDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYaddtagaaaatgdgdiL----------- 263
Cdd:COG1446  165 ----INERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTY----------------Adnevgavsatg 224

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 264 -----MRFLPSYQAVKYMRGGEDPTIACQKVISKIQKYFpDFFWAVICANGTGKLGAACN 318
Cdd:COG1446  225 hgeyfIRTVVAHDIVERMRQGLSLQEAAEEVIERILKKL-GGDGGLIAVDKDGNIAAPFN 283
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 39-318 2.26e-48

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: 163.12  E-value: 2.26e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  39 ATEAAWRALASGGSALDAVESGCAMCETeqcDG--SVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGVAR 116
Cdd:cd04512   26 ALEAGREVLEKGGSALDAVEAAVRLLED---DPlfNAGRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLAR 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 117 KVLEHTTHTLLVGESATKFAESMGfvnedlstrasqalhsdwlarncqpnywrnvvpdpskycgpykplgilkqdipihk 196
Cdd:cd04512  103 AVMEKTPHVLLVGEGAERFAREHG-------------------------------------------------------- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 197 etednrgHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLPSYQAVKYM 276
Cdd:cd04512  127 -------HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLV 199

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 312283655 277 RGGEDPTIACQKVISKIqKYFPDFFWAVICANGTGKLGAACN 318
Cdd:cd04512  200 EFGGSAQEAAEAAIDYL-RRRVGGEGGLIVVDPDGRLGAAHN 240
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 37-318 8.27e-42

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: 146.19  E-value: 8.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  37 KNATEAAWRALASGgSALDAVESGCAMCEteqcDGSV---GFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIG 113
Cdd:cd14950   25 REALERGYEALRRG-SALEAVVEAVAYME----DSGVfnaGVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 114 VARKVLEHTTHTLLVGESATKFAESMGFvnedlstrasqalhsdwlarncqpnywrnvvpdpskycgpykplgilkqdip 193
Cdd:cd14950  100 LARKVMEKTDHVLIVGEGADELAKRLGG---------------------------------------------------- 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 194 ihketednrghDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDIlMRFLPSYQAV 273
Cdd:cd14950  128 -----------DTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATNGVAVSATGIGEVI-IRSLPALRAD 195

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 312283655 274 KYMRGGEDPTIACQKVISKIQKYFPDFFWAVICANGTGKLGAACN 318
Cdd:cd14950  196 ELVSMGGDIEEAVRAVVNKVTETFGKDTAGIIGIDARGNIAAAFN 240
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 37-246 2.67e-39

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: 140.40  E-value: 2.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  37 KNATEAAWRALASGGSALDAVESG-CAMCETEQCDGsvGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGVA 115
Cdd:cd04702   26 KRAARAGYSVLKAGGSALDAVEAAvRALEDDPVFNA--GYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 116 RKVLEHTTHTLLVGESATKFAESMGFV---NEDLSTRASQALHSDWLARNCQPNywrnvvpdpskycgpykplgilkqdi 192
Cdd:cd04702  104 RLVMEKTPHCFLTGRGANKFAEEMGIPqvpPESLVTERARERLEKFKKEKGANV-------------------------- 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 312283655 193 pihkeTEDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAY 246
Cdd:cd04702  158 -----EDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGY 206
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 39-246 1.56e-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: 116.79  E-value: 1.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  39 ATEAAWRALASGGSALDAVESgcAMCETEQC------DGSVgfggsPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAI 112
Cdd:cd04701   31 ALEAGYAVLASGGSALDAVTA--AVRLLEDCplfnagKGAV-----FTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 113 GVARKVLEHTTHTLLVGESATKFAESMGfvnedlstrasqalhsdwlarncqpnywrnvvpdpskycGPYKPLGilkqdi 192
Cdd:cd04701  104 LLARAVLEKSPHVLLSGEGAEEFAREQG---------------------------------------LELVPQG------ 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 312283655 193 pihketednrghdTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAY 246
Cdd:cd04701  139 -------------TVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFW 179
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 41-290 1.47e-25

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 104.26  E-value: 1.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  41 EAAWRALASGGSALDAVESGCAMceTEQC---DGSVGFGGSPDELGEttLDAMIMEGTTMDVGAVGDLRRIKNAIGVARK 117
Cdd:PRK10226  37 ETGQKMLEAGESALDVVTEAVRL--LEECplfNAGIGAVFTRDETHE--LDACVMDGNTLKAGAVAGVSHLRNPVLAARL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 118 VLEHTTHTLLVGESATKFAESMGF--VNEDL-ST--RASQALHsdwlARNCQpnywrNVVPDPSKycgpyKPLgilkqdi 192
Cdd:PRK10226 113 VMEQSPHVMMIGEGAENFAFAHGMerVSPEIfSTplRYEQLLA----ARAEG-----ATVLDHSG-----APL------- 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 193 pihketEDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLPSYQA 272
Cdd:PRK10226 172 ------DEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDI 245

                        250
                 ....*....|....*....
gi 312283655 273 VKYMR-GGEDPTIACQKVI 290
Cdd:PRK10226 246 AALMDyGGLSLAEACERVV 264
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 37-293 4.33e-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: 4.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  37 KNATEAAWRALASGGSALDAVESGCAMCETEQCDGSvGFGGSPDELGETTLDAMIMEGTTmDVGAVGDLRRIKNAIGVAR 116
Cdd:cd04703   20 ERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNA-GTGSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVAR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 117 KVLEHTTHTLLVGESATKFAESMGFVnedlstrasqalhsdwlarncqpnywrnvvpdpskycgpykplgilkqdipihk 196
Cdd:cd04703   98 AVMETSPHVLLAGDGAVRFARRLGYP------------------------------------------------------ 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 197 etednRGHDTIGMVV-IHktGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAYADDTAGAAAATGDGDILMRFLpSYQAVKY 275
Cdd:cd04703  124 -----DGCDTVGAVArDG--GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKGAVAATGIGEEIAKRLL-ARRVYRW 195

                        250
                 ....*....|....*...
gi 312283655 276 MRGGEDPTIACQKVISKI 293
Cdd:cd04703  196 IETGLSLQAAAQRAIDEF 213
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 46-246 3.51e-22

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 95.16  E-value: 3.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  46 ALASGGSALDAVEsgCAMCETEQC-DGSVGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGVARKVLEHTTH 124
Cdd:PLN02689  41 ALRSSLPALDVVE--LVVRELENDpLFNAGRGSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPH 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 125 TLLVGESATKFAESMG--------FVNEDLSTRASQALHsdwlARNCQPNYwRNVVPDPSKYCGPYKPlgilkqdipihk 196
Cdd:PLN02689 119 IYLAFDGAEAFARQQGvetvdnsyFITEENVERLKQAKE----ANSVQFDY-RIPLDKPAKAAALAAD------------ 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 312283655 197 eteDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAY 246
Cdd:PLN02689 182 ---GDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTY 228
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 37-246 2.72e-21

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: 92.72  E-value: 2.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  37 KNATEAAWRALASGGSALDAVESgcAMCETEqcDGSV---GFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIG 113
Cdd:cd04514   25 KRACKAAAAVLKAGGSALDAVEA--AIKVLE--DSPLtnaGYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 114 VARKVLEHTTH---------TLLVGESATKFAESMGFVNedlstrasqalhsdwlarncqpnywrnvvpdpskycgpykp 184
Cdd:cd04514  101 LARLLLKEQRKplslgrvppMFLVGEGAREWAKSKGIIT----------------------------------------- 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312283655 185 lgilkqdipihketednrghDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAY 246
Cdd:cd04514  140 --------------------DTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCW 181
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 41-246 2.52e-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: 78.03  E-value: 2.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  41 EAAWRALASGgSALDAVESGCAMCETE-----------QCDGSVgfggspdelgetTLDAMIMEGTTMDVGAVGDLRRIK 109
Cdd:cd14949   32 EEVYEYLKSH-SALEAVVYAVSLLEDDplfnagtgsqiQSDGQI------------RMSASLMDGQTQRFSGVINIENVK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 110 NAIGVARKVLEHTtHTLLVGESATKFAESMGFvnedlstrasqalhsdwlarncqpnywrnvvpdpskycGPYKPLGILK 189
Cdd:cd14949   99 NPIEVAQKLQQED-DRVLSGEGATEFARENGF--------------------------------------PEYNPETPQR 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 312283655 190 QDIPIHKEtEDNRGHDTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPgAGAY 246
Cdd:cd14949  140 RQEYEEKK-LKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNY 194
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 37-246 1.26e-15

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 77.21  E-value: 1.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655  37 KNATEAAWRALASG-GSALDAVESGCAMCETEQCDGSvGFGGSPDELGETTLDAMIMEGTTMDVGAVGDLRRIKNAIGVA 115
Cdd:PLN02937  36 RRACLAAAAILRQGsGGCIDAVSAAIQVLEDDPSTNA-GRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIA 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 116 RKVLEHTTH----------TLLVGESATKFAESMGFVNEDLSTRASQalhsdWLARNCQPNYWRN-----VVPDPSKYCG 180
Cdd:PLN02937 115 ALLAKEQMMgssllgrippMFLVGEGARQWAKSKGIDLPETVEEAEK-----WLVTERAKEQWKKyktmlASAIAKSSCD 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312283655 181 PYKPLGILKQDIPIHKETEDNRGH--------------DTIGMVVIHKTGRIAAGTSTNGIKFKIHGRVGDSPVPGAGAY 246
Cdd:PLN02937 190 SQSTSKLSELEAPRSNPSNGTGGGqssmctasdedcimDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCW 269
 
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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