NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|505385091|ref|WP_015572193|]
View 

MULTISPECIES: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase [Enterobacter]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 3-277 2.10e-116

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: 337.61  E-value: 2.10e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091   3 GIIATWRmALEGVTESASALAAGKPVAAAVVDAVAAVEDFPFYKSVGYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVD 82
Cdd:cd04513    1 LVINTWN-FTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  83 IANPVRVAHALSRQRYNSLLVGQGAREWALSQGFADKTMLTDRAMQHYRKRCRETLDKG--------------------- 141
Cdd:cd04513   80 IKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNfwknvvpdpskscsspkapsr 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 142 ---LSPYDGHDTVGIIGLDKQGSMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSETGAATATGVGEDLMKGCTSYEIVR 218
Cdd:cd04513  160 sesAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLPSYQAVE 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505385091 219 RMAQGMTPQQAADSVVFEledkLMSRFGRAGDLSVVCMNSKGEFGAATNIKTFSFVVAT 277
Cdd:cd04513  240 LMRQGMSPQEACEDAIRR----IAKKYPKDFEGAVVAVNKAGEYGAACNGEGFSYAVRT 294
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 3-277 2.10e-116

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: 337.61  E-value: 2.10e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091   3 GIIATWRmALEGVTESASALAAGKPVAAAVVDAVAAVEDFPFYKSVGYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVD 82
Cdd:cd04513    1 LVINTWN-FTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  83 IANPVRVAHALSRQRYNSLLVGQGAREWALSQGFADKTMLTDRAMQHYRKRCRETLDKG--------------------- 141
Cdd:cd04513   80 IKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNfwknvvpdpskscsspkapsr 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 142 ---LSPYDGHDTVGIIGLDKQGSMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSETGAATATGVGEDLMKGCTSYEIVR 218
Cdd:cd04513  160 sesAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLPSYQAVE 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505385091 219 RMAQGMTPQQAADSVVFEledkLMSRFGRAGDLSVVCMNSKGEFGAATNIKTFSFVVAT 277
Cdd:cd04513  240 LMRQGMSPQEACEDAIRR----IAKKYPKDFEGAVVAVNKAGEYGAACNGEGFSYAVRT 294
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 5-284 4.11e-74

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 230.38  E-value: 4.11e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091   5 IATWRMALEGVTESASA-LAAGKPVAAAVVDAVAAVEDFPFYkSVGYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVDI 83
Cdd:COG1446   27 EAAYRAGLRAALEAGYAvLEAGGSALDAVEAAVRVLEDDPLF-NAGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  84 ANPVRVAHALSRQRYNSLLVGQGAREWALSQGFA---DKTMLTDRAMQHYRKRCREtldKGLSPYDGHDTVGIIGLDKQG 160
Cdd:COG1446  106 KNPISLARAVMEKTPHVLLVGEGAERFAREQGLElvdPLYFFTEKRWKQWKKALEY---KPIINERKHGTVGAVALDANG 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 161 SMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSETGAATATGVGEDLMKGCTSYEIVRRMAQGMTPQQAADSVVfeleDK 240
Cdd:COG1446  183 NLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRTVVAHDIVERMRQGLSLQEAAEEVI----ER 258

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 505385091 241 LMSRFGraGDLSVVCMNSKGEFGAATNIKTFSFVVATARQPLTV 284
Cdd:COG1446  259 ILKKLG--GDGGLIAVDKDGNIAAPFNTEGMYRAYIDGDGELVV 300
Asparaginase_2 pfam01112
Asparaginase;
9-267 1.99e-59

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 192.80  E-value: 1.99e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091    9 RMALEGVTESA-SALAAGKPVAAAVVDAVAAVEDFPFYkSVGYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVDIANPV 87
Cdd:pfam01112  22 RAGLKEALEAGyAVLAAGGSALDAVEAAVRLLEDDPLF-NAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091   88 RVAHALSRQRYNSLLVGQGAREWALSQGFA---DKTMLTD-RAMQH--YRKR-CRETLDKGLSP-------YDGHDTVGI 153
Cdd:pfam01112 101 SLARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEeRLQELqkARKEnFQPNMALNVAPdplkecgDSKRGTVGA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  154 IGLDKQGSMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSETGAATATGVGEDLMKGCTSYEIVRRMAQGMTPQQAADSV 233
Cdd:pfam01112 181 VALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYDIVARMEYGLSLEEAADKV 260

                         250       260       270
                  ....*....|....*....|....*....|....
gi 505385091  234 VFEledkLMSRFGraGDLSVVCMNSKGEFGAATN 267
Cdd:pfam01112 261 ITE----MLKRVG--GDGGVIAVDAKGNIAAPFN 288
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 20-267 8.76e-32

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 120.58  E-value: 8.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  20 SALAAGKPVAAAVVDAVAAVEDFPFYKSvGYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVDIANPVRVAHALSRQRYN 99
Cdd:PLN02689  40 AALRSSLPALDVVELVVRELENDPLFNA-GRGSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPH 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 100 SLLVGQGAREWALSQGFADKT-----------ML-----TDRAMQHYRKRCRETLDKGLSPYDGH---DTVGIIGLDKQG 160
Cdd:PLN02689 119 IYLAFDGAEAFARQQGVETVDnsyfiteenveRLkqakeANSVQFDYRIPLDKPAKAAALAADGDaqpETVGCVAVDSDG 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 161 SMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSEtGAATATGVGEDLMKGCTSYEIVRRMA-QGMTPQQAADSVVFELED 239
Cdd:PLN02689 199 NCAAATSTGGLVNKMVGRIGDTPIIGAGTYANHL-CAVSATGKGEAIIRGTVARDVAAVMEyKGLPLQEAVDYVIKERLP 277

                        250       260
                 ....*....|....*....|....*...
gi 505385091 240 KlmsrfGRAGdlsVVCMNSKGEFGAATN 267
Cdd:PLN02689 278 E-----GPAG---LIAVSATGEVAMAFN 297
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 3-277 2.10e-116

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: 337.61  E-value: 2.10e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091   3 GIIATWRmALEGVTESASALAAGKPVAAAVVDAVAAVEDFPFYKSVGYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVD 82
Cdd:cd04513    1 LVINTWN-FTEAVEAAWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  83 IANPVRVAHALSRQRYNSLLVGQGAREWALSQGFADKTMLTDRAMQHYRKRCRETLDKG--------------------- 141
Cdd:cd04513   80 IKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNfwknvvpdpskscsspkapsr 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 142 ---LSPYDGHDTVGIIGLDKQGSMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSETGAATATGVGEDLMKGCTSYEIVR 218
Cdd:cd04513  160 sesAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLPSYQAVE 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505385091 219 RMAQGMTPQQAADSVVFEledkLMSRFGRAGDLSVVCMNSKGEFGAATNIKTFSFVVAT 277
Cdd:cd04513  240 LMRQGMSPQEACEDAIRR----IAKKYPKDFEGAVVAVNKAGEYGAACNGEGFSYAVRT 294
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 5-284 4.11e-74

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 230.38  E-value: 4.11e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091   5 IATWRMALEGVTESASA-LAAGKPVAAAVVDAVAAVEDFPFYkSVGYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVDI 83
Cdd:COG1446   27 EAAYRAGLRAALEAGYAvLEAGGSALDAVEAAVRVLEDDPLF-NAGKGAVLTRDGTVELDASIMDGATLRAGAVAGVTRI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  84 ANPVRVAHALSRQRYNSLLVGQGAREWALSQGFA---DKTMLTDRAMQHYRKRCREtldKGLSPYDGHDTVGIIGLDKQG 160
Cdd:COG1446  106 KNPISLARAVMEKTPHVLLVGEGAERFAREQGLElvdPLYFFTEKRWKQWKKALEY---KPIINERKHGTVGAVALDANG 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 161 SMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSETGAATATGVGEDLMKGCTSYEIVRRMAQGMTPQQAADSVVfeleDK 240
Cdd:COG1446  183 NLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRTVVAHDIVERMRQGLSLQEAAEEVI----ER 258

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 505385091 241 LMSRFGraGDLSVVCMNSKGEFGAATNIKTFSFVVATARQPLTV 284
Cdd:COG1446  259 ILKKLG--GDGGLIAVDKDGNIAAPFNTEGMYRAYIDGDGELVV 300
Asparaginase_2 pfam01112
Asparaginase;
9-267 1.99e-59

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 192.80  E-value: 1.99e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091    9 RMALEGVTESA-SALAAGKPVAAAVVDAVAAVEDFPFYkSVGYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVDIANPV 87
Cdd:pfam01112  22 RAGLKEALEAGyAVLAAGGSALDAVEAAVRLLEDDPLF-NAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091   88 RVAHALSRQRYNSLLVGQGAREWALSQGFA---DKTMLTD-RAMQH--YRKR-CRETLDKGLSP-------YDGHDTVGI 153
Cdd:pfam01112 101 SLARAVMEKTPHVMLSGEGAEQFAREMGLErvpPEDFLTEeRLQELqkARKEnFQPNMALNVAPdplkecgDSKRGTVGA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  154 IGLDKQGSMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSETGAATATGVGEDLMKGCTSYEIVRRMAQGMTPQQAADSV 233
Cdd:pfam01112 181 VALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYDIVARMEYGLSLEEAADKV 260

                         250       260       270
                  ....*....|....*....|....*....|....
gi 505385091  234 VFEledkLMSRFGraGDLSVVCMNSKGEFGAATN 267
Cdd:pfam01112 261 ITE----MLKRVG--GDGGVIAVDAKGNIAAPFN 288
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 2-273 1.08e-57

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: 186.23  E-value: 1.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091   2 WGIIATWRMALEGVTESASALaagkpvaaavvdavaavEDFPFYkSVGYGGLPTENGEVELDAAYMDGDTLAFGAVGNLV 81
Cdd:cd04512   31 REVLEKGGSALDAVEAAVRLL-----------------EDDPLF-NAGRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  82 DIANPVRVAHALSRQRYNSLLVGQGAREWALSQGfadktmltdramqhyrkrcretldkglspydgHDTVGIIGLDKQGS 161
Cdd:cd04512   93 GVKNPISLARAVMEKTPHVLLVGEGAERFAREHG--------------------------------HGTVGAVARDAQGN 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 162 MSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSETGAATATGVGEDLMKGCTSYEIVRRMAQGMTPQQAADSVVfeleDKL 241
Cdd:cd04512  141 LAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLVEFGGSAQEAAEAAI----DYL 216

                        250       260       270
                 ....*....|....*....|....*....|...
gi 505385091 242 MSRF-GRAGdlsVVCMNSKGEFGAATNIKTFSF 273
Cdd:cd04512  217 RRRVgGEGG---LIVVDPDGRLGAAHNTPGMAF 246
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 49-265 3.67e-51

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: 170.83  E-value: 3.67e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  49 GYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVDIANPVRVAHALSRQRYNSLLVGQGAREWALSQGF---ADKTMLTDR 125
Cdd:cd04702   62 GYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIpqvPPESLVTER 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 126 AMQHYRKRCRETLDKGLSPYDGHDTVGIIGLDKQGSMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSETGAATATGVGE 205
Cdd:cd04702  142 ARERLEKFKKEKGANVEDTQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGE 221

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 206 DLMKGCTSYEIVRRMAQGMTPQQAADSVVFELEDKLMsrfGRAGdlsVVCMNSKGEFGAA 265
Cdd:cd04702  222 SIMKVNLARLILFHMEQGKTAEEAAELALAYMKSRVK---GLGG---LIVVSKTGDWGAK 275
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 49-269 2.39e-43

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: 149.27  E-value: 2.39e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  49 GYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVDIANPVRVAHALSRQRYNSLLVGQGAREWALSQGFadktmltdramq 128
Cdd:cd14950   60 GVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIRLARKVMEKTDHVLIVGEGADELAKRLGG------------ 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 129 hyrkrcretldkglspydghDTVGIIGLDKQGSMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSEtGAATATGVGEDLM 208
Cdd:cd14950  128 --------------------DTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATNG-VAVSATGIGEVII 186

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505385091 209 KGCTSYEIVRRMAQGMTPQQAADSVVfeleDKLMSRFGRaGDLSVVCMNSKGEFGAATNIK 269
Cdd:cd14950  187 RSLPALRADELVSMGGDIEEAVRAVV----NKVTETFGK-DTAGIIGIDARGNIAAAFNTE 242
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 49-267 9.46e-41

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: 142.40  E-value: 9.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  49 GYGGLPTENGEVELDAAYMDGDTlAFGAVGNLVDIANPVRVAHALSRQRYNSLLVGQGAREWALSQGFADktmltdramq 128
Cdd:cd04703   56 GTGSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVARAVMETSPHVLLAGDGAVRFARRLGYPD---------- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 129 hyrkrcretldkglspydGHDTVGIIGLDkQGSMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDsETGAATATGVGEDLM 208
Cdd:cd04703  125 ------------------GCDTVGAVARD-GGKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAG-PKGAVAATGIGEEIA 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505385091 209 KGCTSYEIVRRMAQGMTPQQAAdsvvfeleDKLMSRFGRAGDLSVVCMNSKGEFGAATN 267
Cdd:cd04703  185 KRLLARRVYRWIETGLSLQAAA--------QRAIDEFDDGVAVGVIAVSRRGEAGIASN 235
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 49-285 1.35e-36

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: 133.17  E-value: 1.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  49 GYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVDIANPVRVAHALSRQRYNSL---------LVGQGAREWALSQGfadk 119
Cdd:cd04514   61 GYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKEQRKPLslgrvppmfLVGEGAREWAKSKG---- 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 120 tMLTdramqhyrkrcretldkglspydghDTVGIIGLDKQGSMSVATSTSGLFMKKRGRLGDSPIIGSGFY---CDSETG 196
Cdd:cd04514  137 -IIT-------------------------DTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWaepRDPDDK 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 197 AATA---TGVGEDLMKGCTSYEIVRRMAQGMTPQQAADSVVFE--LEDKLMSRFGR-----AGDLSVVCMNSKG---EFG 263
Cdd:cd04514  191 TSVAvvtSGTGEHIATTMLARRCAERLYHSTRREESDEDEILRsfIESDFMGHPGVknspsAGAIGVLAVKKTRsgvELY 270

                        250       260
                 ....*....|....*....|....*.
gi 505385091 264 AATNikTFSFVVA----TARQPLTVF 285
Cdd:cd04514  271 FAHN--TDSFALAsmssSDRKPKCVM 294
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 40-237 1.05e-35

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: 129.50  E-value: 1.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  40 EDFPFYKSvGYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVDIANPVRVAHALSRQRYNSLLVGQGAREWALSQGFadk 119
Cdd:cd04701   57 EDCPLFNA-GKGAVFTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGL--- 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 120 tmltdramqhyrkrcrETLDKGlspydghdTVGIIGLDKQGSMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSETGAAT 199
Cdd:cd04701  133 ----------------ELVPQG--------TVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWAVAVS 188

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 505385091 200 ATGVGEDLMKGCTSYEIVRRMA-QGMTPQQAADSVVFEL 237
Cdd:cd04701  189 GTGNGDSFIRVAAARDVAARMRyKGLSLAEAAKEVVGPG 227
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 20-267 8.76e-32

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 120.58  E-value: 8.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  20 SALAAGKPVAAAVVDAVAAVEDFPFYKSvGYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVDIANPVRVAHALSRQRYN 99
Cdd:PLN02689  40 AALRSSLPALDVVELVVRELENDPLFNA-GRGSVLTEDGTVEMEASIMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPH 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 100 SLLVGQGAREWALSQGFADKT-----------ML-----TDRAMQHYRKRCRETLDKGLSPYDGH---DTVGIIGLDKQG 160
Cdd:PLN02689 119 IYLAFDGAEAFARQQGVETVDnsyfiteenveRLkqakeANSVQFDYRIPLDKPAKAAALAADGDaqpETVGCVAVDSDG 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 161 SMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSEtGAATATGVGEDLMKGCTSYEIVRRMA-QGMTPQQAADSVVFELED 239
Cdd:PLN02689 199 NCAAATSTGGLVNKMVGRIGDTPIIGAGTYANHL-CAVSATGKGEAIIRGTVARDVAAVMEyKGLPLQEAVDYVIKERLP 277

                        250       260
                 ....*....|....*....|....*...
gi 505385091 240 KlmsrfGRAGdlsVVCMNSKGEFGAATN 267
Cdd:PLN02689 278 E-----GPAG---LIAVSATGEVAMAFN 297
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 11-253 1.48e-29

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 114.66  E-value: 1.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  11 ALEGVTESASA-LAAGKPVAAAVVDAVAAVEDFPFYKSvGYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVDIANPVRV 89
Cdd:PRK10226  31 ALSAIVETGQKmLEAGESALDVVTEAVRLLEECPLFNA-GIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPVLA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  90 AHALSRQRYNSLLVGQGAREWALSQGFAD------KTMLTDRAMQHYRKRCRETLDKGLSPYDGHD---TVGIIGLDKQG 160
Cdd:PRK10226 110 ARLVMEQSPHVMMIGEGAENFAFAHGMERvspeifSTPLRYEQLLAARAEGATVLDHSGAPLDEKQkmgTVGAVALDLDG 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 161 SMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSETGAATATGVGEDLMKGCTSYEIVRRMAQG-MTPQQAADSVVFEled 239
Cdd:PRK10226 190 NLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAALMDYGgLSLAEACERVVME--- 266

                        250
                 ....*....|....
gi 505385091 240 KLMSRFGRAGDLSV 253
Cdd:PRK10226 267 KLPALGGSGGLIAI 280
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 58-261 8.76e-28

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: 108.85  E-value: 8.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  58 GEVELDAAYMDGDTLAFGAVGNLVDIANPVRVAHALSrQRYNSLLVGQGAREWALSQGFADKTMLTDRAMQHYrkrcret 137
Cdd:cd14949   72 GQIRMSASLMDGQTQRFSGVINIENVKNPIEVAQKLQ-QEDDRVLSGEGATEFARENGFPEYNPETPQRRQEY------- 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 138 lDKGLSPYDGHDTVGIIGLDKQGSMSVATSTSGLFMKKRGRLGDSPIIgSGFYCdSETGAATATGVGEDLMKGCTSYEIV 217
Cdd:cd14949  144 -EEKKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNYA-NAFAGVSCTGIGEDIVSEALAAKIV 220

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 505385091 218 RRMAQGMTPQQAADSVVFELEDklmsrfgRAGDLSVVCMNSKGE 261
Cdd:cd14949  221 TRVTDGMSLQEAFEKSFAEAKP-------RDGFAGAIGIDSKGN 257
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 49-215 3.35e-22

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 96.09  E-value: 3.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091  49 GYGGLPTENGEVELDAAYMDGDTLAFGAVGNLVDIANPVRVAHALSR-QRYNS---------LLVGQGAREWALSQGF-- 116
Cdd:PLN02937  73 GRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKeQMMGSsllgrippmFLVGEGARQWAKSKGIdl 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385091 117 ------ADKTMLTDRAMQHYRK-------------------------------RCRETLDKGLSPYDGH------DTVGI 153
Cdd:PLN02937 153 petveeAEKWLVTERAKEQWKKyktmlasaiaksscdsqstsklseleaprsnPSNGTGGGQSSMCTASdedcimDTVGV 232

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505385091 154 IGLDKQGSMSVATSTSGLFMKKRGRLGDSPIIGSGFYCDSET--GAA-----TATGVGEDLMKGCTSYE 215
Cdd:PLN02937 233 ICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSGCWASSKGpfGAPfivgcCVSGAGEYLMRGFAARE 301
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH