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Conserved domains on  [gi|564389084|ref|XP_006253173|]
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N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase isoform X1 [Rattus norvegicus]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
29-350 4.32e-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: 435.07  E-value: 4.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  29 LVVNTWPFKNATEAvsvislrgdifatqrktvtAWWTLVSGGSALDAVEKGCAMCEKEQCGGTVGFGGSPDEVGETTLDA 108
Cdd:cd04513    1 LVINTWNFTEAVEA-------------------AWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDA 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 109 MIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHSDWLSRNCQPNYWR 188
Cdd:cd04513   62 AIMDGDTMDVGAVAALRRIKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 189 NVIPDPSKYCgpykppDFLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDM 268
Cdd:cd04513  142 NVVPDPSKSC------SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNE 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 269 AGAAAATGDGDTLLRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYPK-FFGAVICANVTGSYGAACNRlptfTQFSFM 347
Cdd:cd04513  216 VGAAAATGDGDIMMRFLPSYQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAACNG----EGFSYA 291

                 ...
gi 564389084 348 VYN 350
Cdd:cd04513  292 VRT 294
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
29-350 4.32e-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: 435.07  E-value: 4.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  29 LVVNTWPFKNATEAvsvislrgdifatqrktvtAWWTLVSGGSALDAVEKGCAMCEKEQCGGTVGFGGSPDEVGETTLDA 108
Cdd:cd04513    1 LVINTWNFTEAVEA-------------------AWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDA 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 109 MIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHSDWLSRNCQPNYWR 188
Cdd:cd04513   62 AIMDGDTMDVGAVAALRRIKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 189 NVIPDPSKYCgpykppDFLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDM 268
Cdd:cd04513  142 NVVPDPSKSC------SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNE 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 269 AGAAAATGDGDTLLRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYPK-FFGAVICANVTGSYGAACNRlptfTQFSFM 347
Cdd:cd04513  216 VGAAAATGDGDIMMRFLPSYQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAACNG----EGFSYA 291

                 ...
gi 564389084 348 VYN 350
Cdd:cd04513  292 VRT 294
Asparaginase_2 pfam01112
Asparaginase;
61-336 3.46e-93

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 280.62  E-value: 3.46e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084   61 TAWWTLVSGGSALDAVEKGCAMCEkEQCGGTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEH 140
Cdd:pfam01112  31 AGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLARAVMEK 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  141 TTHTLLVGDSATKFAVSMGFT---SEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPSKYCGPYKppdfleqnnrahkev 217
Cdd:pfam01112 110 TPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK--------------- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  218 dihsHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEYMRGG 297
Cdd:pfam01112 175 ----RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYDIVARMEYG 250
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 564389084  298 DDPARACQKVISRIQKYYPKfFGAVICANVTGSYGAACN 336
Cdd:pfam01112 251 LSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFN 288
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
61-339 5.85e-54

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


Pssm-ID: 224363  Cd Length: 307  Bit Score: 179.86  E-value: 5.85e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  61 TAWWTLVSGGSALDAVEKGCAMCEKeqCGGT-VGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLE 139
Cdd:COG1446   33 AGYQLLSAGGSALDAVVEAVRVLED--SPLFnAGTGSVLNIDGKVEMDASIMDGATLRAGAVAAVEGVKNPILAARAVME 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 140 HTTHTLLVGDSATKFAVSMGF-TSEDLSTNTSRALHSDWLSRNcqpnywRNVIPDPSKycgpykppdfleqnNRAHKEVD 218
Cdd:COG1446  111 KTPHVLLVGEGAVAFAREMGLpREYDPFTEERRAEWLQAERDA------KKQVLDHSK--------------TYEEPEDP 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 219 IHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEYMRGGD 298
Cdd:COG1446  171 DSKHGTVGAVALDADGNLAAATSTGGVFLKRPGRVGDSPIPGAGFYAENGAGAVSCTGVGEVIIRNALAFDIAARVRYGL 250
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 564389084 299 DPARACQKVISRIQKYYPKFFGAvICANVTGSYGAACNRLP 339
Cdd:COG1446  251 SLDAACERVVEEALKALGGDGGL-IAVDAKGNVAAAFNTKG 290
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
66-262 3.28e-25

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 104.02  E-value: 3.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  66 LVSGGSALDAVE---------------KGCAMCEKeqcgGTVgfggspdevgetTLDAMIMDGTAMDVGAVGGLRRIKNA 130
Cdd:PLN02689  42 LRSSLPALDVVElvvrelendplfnagRGSVLTED----GTV------------EMEASIMDGRTRRCGAVSGLTTVVNP 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 131 IGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHsDWLSRNCQPNywrNVIPDpskycgpYKPPDFLEQN 210
Cdd:PLN02689 106 ISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENV-ERLKQAKEAN---SVQFD-------YRIPLDKPAK 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564389084 211 NRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 262
Cdd:PLN02689 175 AAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAG 226
 
Name Accession Description Interval E-value
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
29-350 4.32e-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: 435.07  E-value: 4.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  29 LVVNTWPFKNATEAvsvislrgdifatqrktvtAWWTLVSGGSALDAVEKGCAMCEKEQCGGTVGFGGSPDEVGETTLDA 108
Cdd:cd04513    1 LVINTWNFTEAVEA-------------------AWEVLQKGGSALDAVEAGCSVCEDDQCDGSVGYGGSPDENGETTLDA 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 109 MIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHSDWLSRNCQPNYWR 188
Cdd:cd04513   62 AIMDGDTMDVGAVAALRRIKNAISVARAVMEHTPHSLLVGEGATEFAVSMGFKEENLLTEESRKMWKKWLKENCQPNFWK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 189 NVIPDPSKYCgpykppDFLEQNNRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDM 268
Cdd:cd04513  142 NVVPDPSKSC------SSPKAPSRSESAIPEDNHDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNE 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 269 AGAAAATGDGDTLLRFLPSYQAVEYMRGGDDPARACQKVISRIQKYYPK-FFGAVICANVTGSYGAACNRlptfTQFSFM 347
Cdd:cd04513  216 VGAAAATGDGDIMMRFLPSYQAVELMRQGMSPQEACEDAIRRIAKKYPKdFEGAVVAVNKAGEYGAACNG----EGFSYA 291

                 ...
gi 564389084 348 VYN 350
Cdd:cd04513  292 VRT 294
Asparaginase_2 pfam01112
Asparaginase;
61-336 3.46e-93

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 280.62  E-value: 3.46e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084   61 TAWWTLVSGGSALDAVEKGCAMCEkEQCGGTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEH 140
Cdd:pfam01112  31 AGYAVLAAGGSALDAVEAAVRLLE-DDPLFNAGKGSVLTSDGEVEMDASIMDGKTLRAGAVAGVSRIKNPISLARAVMEK 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  141 TTHTLLVGDSATKFAVSMGFT---SEDLSTNTSRALHSDWLSRNCQPNYWRNVIPDPSKYCGPYKppdfleqnnrahkev 217
Cdd:pfam01112 110 TPHVMLSGEGAEQFAREMGLErvpPEDFLTEERLQELQKARKENFQPNMALNVAPDPLKECGDSK--------------- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  218 dihsHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEYMRGG 297
Cdd:pfam01112 175 ----RGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLAYDIVARMEYG 250
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 564389084  298 DDPARACQKVISRIQKYYPKfFGAVICANVTGSYGAACN 336
Cdd:pfam01112 251 LSLEEAADKVITEMLKRVGG-DGGVIAVDAKGNIAAPFN 288
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
61-339 5.85e-54

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


Pssm-ID: 224363  Cd Length: 307  Bit Score: 179.86  E-value: 5.85e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  61 TAWWTLVSGGSALDAVEKGCAMCEKeqCGGT-VGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLE 139
Cdd:COG1446   33 AGYQLLSAGGSALDAVVEAVRVLED--SPLFnAGTGSVLNIDGKVEMDASIMDGATLRAGAVAAVEGVKNPILAARAVME 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 140 HTTHTLLVGDSATKFAVSMGF-TSEDLSTNTSRALHSDWLSRNcqpnywRNVIPDPSKycgpykppdfleqnNRAHKEVD 218
Cdd:COG1446  111 KTPHVLLVGEGAVAFAREMGLpREYDPFTEERRAEWLQAERDA------KKQVLDHSK--------------TYEEPEDP 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 219 IHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEYMRGGD 298
Cdd:COG1446  171 DSKHGTVGAVALDADGNLAAATSTGGVFLKRPGRVGDSPIPGAGFYAENGAGAVSCTGVGEVIIRNALAFDIAARVRYGL 250
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 564389084 299 DPARACQKVISRIQKYYPKFFGAvICANVTGSYGAACNRLP 339
Cdd:COG1446  251 SLDAACERVVEEALKALGGDGGL-IAVDAKGNVAAAFNTKG 290
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
61-336 5.98e-46

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: 157.34  E-value: 5.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  61 TAWWTLVSGGSALDAVEKGCAMCEKEqcgGT--VGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVL 138
Cdd:cd04512   29 AGREVLEKGGSALDAVEAAVRLLEDD---PLfnAGRGSVLNEDGEVEMDAAIMDGKTLNAGAVAGVKGVKNPISLARAVM 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 139 EHTTHTLLVGDSATKFAVSMGftsedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnrahkevd 218
Cdd:cd04512  106 EKTPHVLLVGEGAERFAREHG----------------------------------------------------------- 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 219 ihsHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEYMRGGD 298
Cdd:cd04512  127 ---HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLVEFGG 203
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 564389084 299 DPARACQKVISRIqKYYPKFFGAVICANVTGSYGAACN 336
Cdd:cd04512  204 SAQEAAEAAIDYL-RRRVGGEGGLIVVDPDGRLGAAHN 240
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
57-336 4.14e-38

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: 136.94  E-value: 4.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  57 RKTVTAWWTLVSGGSALDAVEKGCAMCEKEqcgG--TVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVA 134
Cdd:cd14950   25 REALERGYEALRRGSALEAVVEAVAYMEDS---GvfNAGVGSVLNLEGEVEMDAGIMDGRTLRVGAVAAVRAVKNPIRLA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 135 RKVLEHTTHTLLVGDSATKFAVSMGFtsedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnrah 214
Cdd:cd14950  102 RKVMEKTDHVLIVGEGADELAKRLGG------------------------------------------------------ 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 215 kevdihshDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGaYADDMAGAAAATGDGDTLLRFLPSYQAVEYM 294
Cdd:cd14950  128 --------DTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAG-FYATNGVAVSATGIGEVIIRSLPALRADELV 198
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 564389084 295 RGGDDPARACQKVISRIQKYYPKFFGAVICANVTGSYGAACN 336
Cdd:cd14950  199 SMGGDIEEAVRAVVNKVTETFGKDTAGIIGIDARGNIAAAFN 240
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
66-262 2.00e-35

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: 130.77  E-value: 2.00e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  66 LVSGGSALDAVEKGCAMCEKEQCGGTvGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTHTL 145
Cdd:cd04702   36 LKAGGSALDAVEAAVRALEDDPVFNA-GYGSVLNADGEVEMDASIMDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCF 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 146 LVGDSATKFAVSMGFT---SEDLSTNTSRALHSDWLSRNCQPNywrnvipdpsKYCGpykppdfleqnnrahkevdiHSH 222
Cdd:cd04702  115 LTGRGANKFAEEMGIPqvpPESLVTERARERLEKFKKEKGANV----------EDTQ--------------------RGH 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 564389084 223 DTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 262
Cdd:cd04702  165 GTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSG 204
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
66-262 9.36e-30

Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzyme undergoes an autoproteolytic cleavage into alpha and beta subunits to expose a threonine residue which becomes the N-terminal residue of the beta subunit. The threonine residue plays a central role in hydrolase activity. Some asparaginases can also hydrolyze L-glutamine and are termed glutaminase-asparaginase. This is a member of the Ntn-hydrolase superfamily, and this subfamily covers mostly bacterial and fungal enzymes.


Pssm-ID: 271337  Cd Length: 264  Bit Score: 114.87  E-value: 9.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  66 LVSGGSALDAVEKgcAMCEKEQCG-GTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTHT 144
Cdd:cd04701   39 LASGGSALDAVTA--AVRLLEDCPlFNAGKGAVFTRDGTNELEASIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHV 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 145 LLVGDSATKFAVSMGftsedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnrahkeVDIHSHDT 224
Cdd:cd04701  117 LLSGEGAEEFAREQG---------------------------------------------------------LELVPQGT 139
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564389084 225 IGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 262
Cdd:cd04701  140 VGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAG 177
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
66-337 2.66e-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: 102.34  E-value: 2.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  66 LVSGGSALDAVEKGCAMCEKEQC--GGTvgfGGSPDEVGETTLDAMIMDGTAmDVGAVGGLRRIKNAIGVARKVLEHTTH 143
Cdd:cd04703   30 LQNGGDALDAVVAAVRVLEDDPRfnAGT---GSVLRDDGSIQMDAAVMTSGG-AFGAVAAIEGVKNPVLVARAVMETSPH 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 144 TLLVGDSATKFAVSMGFTsedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnrahkevdiHSHD 223
Cdd:cd04703  106 VLLAGDGAVRFARRLGYP----------------------------------------------------------DGCD 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 224 TIGMVV-IHktGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLpSYQAVEYMRGGDDPAR 302
Cdd:cd04703  128 TVGAVArDG--GKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPKGAVAATGIGEEIAKRLL-ARRVYRWIETGLSLQA 204
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564389084 303 ACQKVISRIQKYYPkffGAVICANVTGSYGAACNR 337
Cdd:cd04703  205 AAQRAIDEFDDGVA---VGVIAVSRRGEAGIASNT 236
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
66-262 3.28e-25

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 104.02  E-value: 3.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  66 LVSGGSALDAVE---------------KGCAMCEKeqcgGTVgfggspdevgetTLDAMIMDGTAMDVGAVGGLRRIKNA 130
Cdd:PLN02689  42 LRSSLPALDVVElvvrelendplfnagRGSVLTED----GTV------------EMEASIMDGRTRRCGAVSGLTTVVNP 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 131 IGVARKVLEHTTHTLLVGDSATKFAVSMGFTSEDLSTNTSRALHsDWLSRNCQPNywrNVIPDpskycgpYKPPDFLEQN 210
Cdd:PLN02689 106 ISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENV-ERLKQAKEAN---SVQFD-------YRIPLDKPAK 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564389084 211 NRAHKEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 262
Cdd:PLN02689 175 AAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAG 226
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
66-308 3.45e-25

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 103.88  E-value: 3.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  66 LVSGGSALDAVEKGCAMCEkeQC---GGTVGFGGSPDEVGEttLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTT 142
Cdd:PRK10226  43 LEAGESALDVVTEAVRLLE--ECplfNAGIGAVFTRDETHE--LDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSP 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 143 HTLLVGDSATKFAVSMGFTSedlstntsralhsdwlsrncqpnywrnviPDPSKYCGPYKPPDFLEQNNRAHKEVDiHSH 222
Cdd:PRK10226 119 HVMMIGEGAENFAFAHGMER-----------------------------VSPEIFSTPLRYEQLLAARAEGATVLD-HSG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 223 ---------DTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAGAYADDMAGAAAATGDGDTLLRFLPSYQAVEY 293
Cdd:PRK10226 169 apldekqkmGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAAL 248
                        250
                 ....*....|....*.
gi 564389084 294 MR-GGDDPARACQKVI 308
Cdd:PRK10226 249 MDyGGLSLAEACERVV 264
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
66-262 2.19e-19

Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the mix lineage leukemia (MLL) nuclear protein and transcription factor TFIIA. Taspase1 is a threonine aspartase, a member of the Ntn hydrolase superfamily and the type 2 asparaginase family. A threonine residue acts as the active site nucleophile in both endopeptidease and protease activities to cleave polypeptide substrates after an aspartate residue. The Taspase1 proenzyme undergoes autoproteolysis into alpha and beta subunits. The N-terminal residue of the beta subunit is a threonine which is the active catalytic residue. The active enzyme is a heterotetramer.


Pssm-ID: 271336  Cd Length: 313  Bit Score: 87.33  E-value: 2.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  66 LVSGGSALDAVEKGCAMCEKEQCGGTvGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTH-- 143
Cdd:cd04514   35 LKAGGSALDAVEAAIKVLEDSPLTNA-GYGSNLTEDGTVECDASIMDGSSGRFGAVGAVSGVKNPIQLARLLLKEQRKpl 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 144 -------TLLVGDSATKFAVSMGFTSedlstntsralhsdwlsrncqpnywrnvipdpskycgpykppdfleqnnrahke 216
Cdd:cd04514  114 slgrvppMFLVGEGAREWAKSKGIIT------------------------------------------------------ 139
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564389084 217 vdihshDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 262
Cdd:cd04514  140 ------DTVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAG 179
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
60-262 3.27e-16

Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; The wider family of Asparaginase 2-like enzymes includes Glycosylasparaginase, Taspase 1, and L-Asparaginase type 2. Glycosylasparaginase catalyzes the hydrolysis of the glycosylamide bond of asparagine-linked glycoprotein. Taspase1 catalyzes the cleavage of the Mix Lineage Leukemia (MLL) nuclear protein and transcription factor TFIIA. L-Asparaginase type 2 hydrolyzes L-asparagine to L-aspartate and ammonia. The proenzymes of this family undergo autoproteolytic cleavage before a threonine to generate alpha and beta subunits. The threonine becomes the N-terminal residue of the beta subunit and is the catalytic residue.


Pssm-ID: 271340  Cd Length: 280  Bit Score: 77.65  E-value: 3.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  60 VTAWWTLVSGGSALDAVEKGCAMCEKEQC--GGTvgfgGS---PDevGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVA 134
Cdd:cd14949   31 VEEVYEYLKSHSALEAVVYAVSLLEDDPLfnAGT----GSqiqSD--GQIRMSASLMDGQTQRFSGVINIENVKNPIEVA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 135 RKVLEHTtHTLLVGDSATKFAVSMGFtsedlstntsralhsdwlsrncqpnywrnvipdpskycGPYKPPDFLEQNNRAH 214
Cdd:cd14949  105 QKLQQED-DRVLSGEGATEFARENGF--------------------------------------PEYNPETPQRRQEYEE 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564389084 215 KEVDIHSHDTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPgAG 262
Cdd:cd14949  146 KKLKSGGTGTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AG 192
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
70-262 3.23e-12

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 67.20  E-value: 3.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084  70 GSALDAVEKGCAMCEKEQCGgTVGFGGSPDEVGETTLDAMIMDGTAMDVGAVGGLRRIKNAIGVARKVLEHTTH------ 143
Cdd:PLN02937  51 GGCIDAVSAAIQVLEDDPST-NAGRGSNLTEDGHVECDASIMDGDSGAFGAVGAVPGVRNAIQIAALLAKEQMMgssllg 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564389084 144 ----TLLVGDSATKFAVSMGFtseDLSTNTSRALHsdWLSRNCQPNYWR-------NVIP-------DPSKYCGPYKPPD 205
Cdd:PLN02937 130 rippMFLVGEGARQWAKSKGI---DLPETVEEAEK--WLVTERAKEQWKkyktmlaSAIAksscdsqSTSKLSELEAPRS 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564389084 206 FLEQNNRAHKEVDIHSH------DTIGMVVIHKTGHTAAGTSTNGLKFKIPGRVGDSPIPGAG 262
Cdd:PLN02937 205 NPSNGTGGGQSSMCTASdedcimDTVGVICVDSEGNIASGASSGGIAMKVSGRVGLAAMYGSG 267
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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