NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|145275202|ref|NP_001077395|]
View 

isoaspartyl peptidase/L-asparaginase [Homo sapiens]

Protein Classification

isoaspartyl peptidase/L-asparaginase( domain architecture ID 10140429)

isoaspartyl peptidase/L-asparaginase degrades proteins which are compromised via the formation of L-isoaspartyl residues by removing beta-linked aspartyl residues from the N-terminus; the enzyme also shows activity as an L-asparaginase

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 2-291 0e+00

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: 530.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   2 NPIVVVHGGgAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASI 81
Cdd:cd04702    1 KPVIVVHGG-AGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  82 MDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTD 161
Cdd:cd04702   80 MDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEKGANVED 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 162 CQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQG 241
Cdd:cd04702  160 TQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNLARLILFHMEQG 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 145275202 242 KTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDG 291
Cdd:cd04702  240 KTAEEAAELALAYMKSRVKGLGGLIVVSKTGDWGAKFTSKRMAWAAVKDG 289
 
Name Accession Description Interval E-value
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 2-291 0e+00

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: 530.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   2 NPIVVVHGGgAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASI 81
Cdd:cd04702    1 KPVIVVHGG-AGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  82 MDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTD 161
Cdd:cd04702   80 MDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEKGANVED 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 162 CQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQG 241
Cdd:cd04702  160 TQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNLARLILFHMEQG 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 145275202 242 KTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDG 291
Cdd:cd04702  240 KTAEEAAELALAYMKSRVKGLGGLIVVSKTGDWGAKFTSKRMAWAAVKDG 289
Asparaginase_2 pfam01112
Asparaginase;
4-299 1.54e-128

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 368.45  E-value: 1.54e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202    4 IVVVHGG-GAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIM 82
Cdd:pfam01112   1 VLVIHGGaGSILRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   83 DGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEK---------- 152
Cdd:pfam01112  81 DGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARkenfqpnmal 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  153 -HEKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLA 231
Cdd:pfam01112 161 nVAPDPLKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLA 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145275202  232 RLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDP 299
Cdd:pfam01112 241 YDIVARMEYGLSLEEAADKVITEMLKRVGGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGIGDVLIY 308
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 1-300 3.00e-117

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 339.78  E-value: 3.00e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   1 MNPIVVVHGGGAGPI-----SKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEV 75
Cdd:COG1446    3 MSRRALIIHGGAGTIarsamTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  76 EMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEK 155
Cdd:COG1446   83 ELDASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 156 GAQKtdcQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTL 235
Cdd:COG1446  163 PIIN---ERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRTVVAHDIV 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145275202 236 FHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAK-DGKLHFGIDPD 300
Cdd:COG1446  240 ERMRQGLSLQEAAEEVIERILKKLGGDGGLIAVDKDGNIAAPFNTEGMYRAYIDgDGELVVAIYKD 305
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 5-299 5.98e-85

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 258.10  E-value: 5.98e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   5 VVVHGGgAGPISK----DRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDAS 80
Cdd:PLN02689   6 IALHGG-AGDIDPnlprERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEAS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  81 IMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKH------- 153
Cdd:PLN02689  85 IMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAKEansvqfd 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 154 ---------EKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYAdNDIGAVSTTGHGES 224
Cdd:PLN02689 165 yripldkpaKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYA-NHLCAVSATGKGEA 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145275202 225 ILKVNLARLTLFHIE-QGKTVEEAADLSLgymKSRV-KGLGGLIVVSKTGDWVAKWTSTSMPWAAAK-DGKLHFGIDP 299
Cdd:PLN02689 244 IIRGTVARDVAAVMEyKGLPLQEAVDYVI---KERLpEGPAGLIAVSATGEVAMAFNTTGMFRACATeDGFMEVGIWP 318
 
Name Accession Description Interval E-value
ASRGL1_like cd04702
Metazoan L-Asparaginase type 2; ASRGL1 and similar proteins constitute a subfamily of the ...
 2-291 0e+00

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: 530.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   2 NPIVVVHGGgAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASI 81
Cdd:cd04702    1 KPVIVVHGG-AGSIPDDRIKGSREGVKRAARAGYSVLKAGGSALDAVEAAVRALEDDPVFNAGYGSVLNADGEVEMDASI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  82 MDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTD 161
Cdd:cd04702   80 MDGKTLRAGAVSAVRNIANPISLARLVMEKTPHCFLTGRGANKFAEEMGIPQVPPESLVTERARERLEKFKKEKGANVED 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 162 CQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQG 241
Cdd:cd04702  160 TQRGHGTVGAVAIDCEGNVACATSTGGITNKMVGRVGDSPIIGSGGYADNLVGAVSTTGHGESIMKVNLARLILFHMEQG 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 145275202 242 KTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDG 291
Cdd:cd04702  240 KTAEEAAELALAYMKSRVKGLGGLIVVSKTGDWGAKFTSKRMAWAAVKDG 289
Asparaginase_2 pfam01112
Asparaginase;
4-299 1.54e-128

Asparaginase;


Pssm-ID: 426055  Cd Length: 308  Bit Score: 368.45  E-value: 1.54e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202    4 IVVVHGG-GAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIM 82
Cdd:pfam01112   1 VLVIHGGaGSILRTKEREEAYRAGLKEALEAGYAVLAAGGSALDAVEAAVRLLEDDPLFNAGKGSVLTSDGEVEMDASIM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   83 DGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEK---------- 152
Cdd:pfam01112  81 DGKTLRAGAVAGVSRIKNPISLARAVMEKTPHVMLSGEGAEQFAREMGLERVPPEDFLTEERLQELQKARkenfqpnmal 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  153 -HEKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLA 231
Cdd:pfam01112 161 nVAPDPLKECGDSKRGTVGAVALDSEGNLAAGTSTGGMTNKRPGRVGDSPIIGAGTYADNATGAVSATGHGEDIIRETLA 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145275202  232 RLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDP 299
Cdd:pfam01112 241 YDIVARMEYGLSLEEAADKVITEMLKRVGGDGGVIAVDAKGNIAAPFNTEGMYRAYHTGDGIGDVLIY 308
Ntn_Asparaginase_2_like cd04512
L-Asparaginase type 2-like enzymes of the NTN-hydrolase superfamily; This family includes ...
 4-286 1.23e-121

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: 348.79  E-value: 1.23e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   4 IVVVHGGgAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMD 83
Cdd:cd04512    1 SLIVHGG-AGTIEDEDAEAYREGLLRALEAGREVLEKGGSALDAVEAAVRLLEDDPLFNAGRGSVLNEDGEVEMDAAIMD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  84 GKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGvpeipgeklvternkkrlekekhekgaqktdcq 163
Cdd:cd04512   80 GKTLNAGAVAGVKGVKNPISLARAVMEKTPHVLLVGEGAERFAREHG--------------------------------- 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 164 knLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQGKT 243
Cdd:cd04512  127 --HGTVGAVARDAQGNLAAATSTGGMVNKRPGRVGDSPIIGAGTYADNETGAVSATGHGESIIRTVLAKRIADLVEFGGS 204

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 145275202 244 VEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWA 286
Cdd:cd04512  205 AQEAAEAAIDYLRRRVGGEGGLIVVDPDGRLGAAHNTPGMAFA 247
IaaA COG1446
Isoaspartyl peptidase or L-asparaginase, Ntn-hydrolase superfamily [Amino acid transport and ...
 1-300 3.00e-117

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


Pssm-ID: 441055  Cd Length: 305  Bit Score: 339.78  E-value: 3.00e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   1 MNPIVVVHGGGAGPI-----SKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEV 75
Cdd:COG1446    3 MSRRALIIHGGAGTIarsamTPEVEAAYRAGLRAALEAGYAVLEAGGSALDAVEAAVRVLEDDPLFNAGKGAVLTRDGTV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  76 EMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEK 155
Cdd:COG1446   83 ELDASIMDGATLRAGAVAGVTRIKNPISLARAVMEKTPHVLLVGEGAERFAREQGLELVDPLYFFTEKRWKQWKKALEYK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 156 GAQKtdcQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTL 235
Cdd:COG1446  163 PIIN---ERKHGTVGAVALDANGNLAAATSTGGMTNKRPGRVGDSPIIGAGTYADNEVGAVSATGHGEYFIRTVVAHDIV 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145275202 236 FHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAK-DGKLHFGIDPD 300
Cdd:COG1446  240 ERMRQGLSLQEAAEEVIERILKKLGGDGGLIAVDKDGNIAAPFNTEGMYRAYIDgDGELVVAIYKD 305
Asparaginase_2 cd04701
Bacterial/fungal L-Asparaginase type 2; L-Asparaginase hydrolyzes L-asparagine to L-aspartate ...
 5-283 1.12e-87

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: 263.17  E-value: 1.12e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   5 VVVHGGgAGPISK-----DRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDA 79
Cdd:cd04701    2 LAIHGG-AGTISRanltpERYAAYRAALRRALEAGYAVLASGGSALDAVTAAVRLLEDCPLFNAGKGAVFTRDGTNELEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  80 SIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPgeklvternkkrlekekhekgaqk 159
Cdd:cd04701   81 SIMDGRTKRAGAVAGLRRVRNPILLARAVLEKSPHVLLSGEGAEEFAREQGLELVP------------------------ 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 160 tdcqknLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIE 239
Cdd:cd04701  137 ------QGTVGAVALDSDGNLAAATSTGGLTNKLPGRIGDTPIIGAGFWAEEWAVAVSGTGNGDSFIRVAAARDVAARMR 210

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 145275202 240 -QGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSM 283
Cdd:cd04701  211 yKGLSLAEAAKEVVGPGGELGEGEGGIIAIDARGNVAMPFNCGGM 255
PLN02689 PLN02689
Bifunctional isoaspartyl peptidase/L-asparaginase
 5-299 5.98e-85

Bifunctional isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215372  Cd Length: 318  Bit Score: 258.10  E-value: 5.98e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   5 VVVHGGgAGPISK----DRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDAS 80
Cdd:PLN02689   6 IALHGG-AGDIDPnlprERQEEAEAALRRCLDLGIAALRSSLPALDVVELVVRELENDPLFNAGRGSVLTEDGTVEMEAS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  81 IMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKH------- 153
Cdd:PLN02689  85 IMDGRTRRCGAVSGLTTVVNPISLARLVMEKTPHIYLAFDGAEAFARQQGVETVDNSYFITEENVERLKQAKEansvqfd 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 154 ---------EKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYAdNDIGAVSTTGHGES 224
Cdd:PLN02689 165 yripldkpaKAAALAADGDAQPETVGCVAVDSDGNCAAATSTGGLVNKMVGRIGDTPIIGAGTYA-NHLCAVSATGKGEA 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145275202 225 ILKVNLARLTLFHIE-QGKTVEEAADLSLgymKSRV-KGLGGLIVVSKTGDWVAKWTSTSMPWAAAK-DGKLHFGIDP 299
Cdd:PLN02689 244 IIRGTVARDVAAVMEyKGLPLQEAVDYVI---KERLpEGPAGLIAVSATGEVAMAFNTTGMFRACATeDGFMEVGIWP 318
Asparaginase_2_like_2 cd14950
Uncharacterized archaebacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 4-290 8.00e-73

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: 224.77  E-value: 8.00e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   4 IVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGgSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMD 83
Cdd:cd14950    1 ALVVHGGAGSWKNSDDEEKALRALREALERGYEALRRG-SALEAVVEAVAYMEDSGVFNAGVGSVLNLEGEVEMDAGIMD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  84 GKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAamgvpeipgeklvternkkrlekekhekgaqktdcQ 163
Cdd:cd14950   80 GRTLRVGAVAAVRAVKNPIRLARKVMEKTDHVLIVGEGADELAK-----------------------------------R 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 164 KNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDiGAVSTTGHGESILKVNLARLTLFHIEQGKT 243
Cdd:cd14950  125 LGGDTVGAVALDKDGNLAAATSTGGVWLKLPGRVGDSPIPGAGFYATNG-VAVSATGIGEVIIRSLPALRADELVSMGGD 203

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 145275202 244 VEEAADLSLGYMKSRV-KGLGGLIVVSKTGDWVAKWTSTSMPWAAAKD 290
Cdd:cd14950  204 IEEAVRAVVNKVTETFgKDTAGIIGIDARGNIAAAFNTEAMPRGYIDD 251
Glycosylasparaginase cd04513
Glycosylasparaginase and similar proteins; Glycosylasparaginase catalyzes the hydrolysis of ...
 34-274 4.00e-64

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: 203.95  E-value: 4.00e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  34 GYGILREGGSAVDAVEGAVVALEDDPE-FNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKT 112
Cdd:cd04513   15 AWEVLQKGGSALDAVEAGCSVCEDDQCdGSVGYGGSPDENGETTLDAAIMDGDTMDVGAVAALRRIKNAISVARAVMEHT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 113 PHCFLTDQGAAQFAAAMGVPEipgEKLVTERNKKRLEKEKhekgaqKTDCQKNL-------------------------- 166
Cdd:cd04513   95 PHSLLVGEGATEFAVSMGFKE---ENLLTEESRKMWKKWL------KENCQPNFwknvvpdpskscsspkapsrsesaip 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 167 ----GTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQGK 242
Cdd:cd04513  166 ednhDTIGMIALDANGNIAAGTSTSGAAFKIPGRVGDSPIPGAGLYADNEVGAAAATGDGDIMMRFLPSYQAVELMRQGM 245

                        250       260       270
                 ....*....|....*....|....*....|....
gi 145275202 243 TVEEAADLSLGYMKSRVKGL--GGLIVVSKTGDW 274
Cdd:cd04513  246 SPQEACEDAIRRIAKKYPKDfeGAVVAVNKAGEY 279
Asparaginase_2_like_1 cd04703
Uncharacterized subfamily of the L-Asparaginase type 2-like enzymes, an Ntn-hydrolase family; ...
 3-288 1.65e-60

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: 192.86  E-value: 1.65e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   3 PIVVVHGGGAGPISKDRkervhqGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIM 82
Cdd:cd04703    1 MAVLVHGGAGSDPERQD------GLERAAEAGLAELQNGGDALDAVVAAVRVLEDDPRFNAGTGSVLRDDGSIQMDAAVM 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  83 DGKDlSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPeipgeklvternkkrlekekhekgaqkTDC 162
Cdd:cd04703   75 TSGG-AFGAVAAIEGVKNPVLVARAVMETSPHVLLAGDGAVRFARRLGYP---------------------------DGC 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 163 qknlGTVGAVALDcKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDiGAVSTTGHGESILKVNLARLTLFHIEQGK 242
Cdd:cd04703  127 ----DTVGAVARD-GGKFAAAVSTGGTSPALRGRVGDVPIIGAGFYAGPK-GAVAATGIGEEIAKRLLARRVYRWIETGL 200

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 145275202 243 TVEEAADLSLGYMKSRVkgLGGLIVVSKTGdWVAKWTSTSMPWAAA 288
Cdd:cd04703  201 SLQAAAQRAIDEFDDGV--AVGVIAVSRRG-EAGIASNTAMAWAIA 243
PRK10226 PRK10226
isoaspartyl peptidase; Provisional
 1-290 3.40e-55

isoaspartyl peptidase; Provisional


Pssm-ID: 182319  Cd Length: 313  Bit Score: 181.69  E-value: 3.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   1 MNPIVVVHGGGAGPISK-----DRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEV 75
Cdd:PRK10226   1 MGKAVIAIHGGAGAISRaqmslQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  76 EMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVT-ERNKKRLEKEKH- 153
Cdd:PRK10226  81 ELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFAHGMERVSPEIFSTpLRYEQLLAARAEg 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 154 ----EKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVn 229
Cdd:PRK10226 161 atvlDHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRA- 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145275202 230 larLTLFHIeqgKTVEEAADLSLGYMKSRV--------KGLGGLIVVSKTGDWVAKWTSTSM--PWAAAKD 290
Cdd:PRK10226 240 ---LAAYDI---AALMDYGGLSLAEACERVvmeklpalGGSGGLIAIDHEGNVALPFNTEGMyrAWGYAGD 304
Asparaginase_2_like_3 cd14949
Uncharacterized bacterial subfamily of the L-Asparaginase type 2-like enzymes, an ...
 3-295 5.61e-55

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: 180.11  E-value: 5.61e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   3 PIVVVHGGgAGPISKDRKE--RVHQG-MVRAATVGYGILREGgSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDA 79
Cdd:cd14949    1 PKLIIHGG-FGSESSTNGEtkAAKQEaLAEIVEEVYEYLKSH-SALEAVVYAVSLLEDDPLFNAGTGSQIQSDGQIRMSA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  80 SIMDGKDLSAGAVSAVQCIANPIKLARLVMEKtPHCFLTDQGAAQFAAAMGVPEIpgEKLVTERnkKRLEKEKHEKGAQK 159
Cdd:cd14949   79 SLMDGQTQRFSGVINIENVKNPIEVAQKLQQE-DDRVLSGEGATEFARENGFPEY--NPETPQR--RQEYEEKKLKSGGT 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 160 tdcqknlGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLgAGGYAdNDIGAVSTTGHGESILKVNLARLTLFHIE 239
Cdd:cd14949  154 -------GTVGCVALDSDGKLAAATSTGGKGFEIPGRVSDSATV-AGNYA-NAFAGVSCTGIGEDIVSEALAAKIVTRVT 224

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145275202 240 QGKTVEEAADLSLGYMKSRvKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHF 295
Cdd:cd14949  225 DGMSLQEAFEKSFAEAKPR-DGFAGAIGIDSKGNIYHGDTHPVMVYASYDGEKIGV 279
Taspase1_like cd04514
Taspase 1 (threonine aspartase 1) and similar proteins; Taspase1 catalyzes the cleavage of the ...
 3-232 5.95e-52

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: 173.23  E-value: 5.95e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   3 PIVVVHGGgAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIM 82
Cdd:cd04514    1 FFVAVHAG-AGYHSPSNEKAYKRACKRACKAAAAVLKAGGSALDAVEAAIKVLEDSPLTNAGYGSNLTEDGTVECDASIM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  83 DGKDLSAGAVSAVQCIANPIKLARLVMEK---------TPHCFLTDQGAAQFAAAMGVPeipgeklvternkkrlekekh 153
Cdd:cd04514   80 DGSSGRFGAVGAVSGVKNPIQLARLLLKEqrkplslgrVPPMFLVGEGAREWAKSKGII--------------------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 154 ekgaqkTDcqknlgTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYA---DNDIG---AVSTTGHGESILK 227
Cdd:cd04514  139 ------TD------TVGAIAIDLYGNIAAGSSSGGIGLKHPGRVGPAALYGAGCWAeprDPDDKtsvAVVTSGTGEHIAT 206


                 ....*
gi 145275202 228 VNLAR 232
Cdd:cd04514  207 TMLAR 211
PLN02937 PLN02937
Putative isoaspartyl peptidase/L-asparaginase
 5-232 1.72e-32

Putative isoaspartyl peptidase/L-asparaginase


Pssm-ID: 215506 [Multi-domain]  Cd Length: 414  Bit Score: 124.21  E-value: 1.72e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202   5 VVVHGGgAGPISKDRKERVHQGMVRAATVGYGILREG-GSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMD 83
Cdd:PLN02937  14 VAVHVG-AGYHAPSNEKALRSAMRRACLAAAAILRQGsGGCIDAVSAAIQVLEDDPSTNAGRGSNLTEDGHVECDASIMD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202  84 GKDLSAGAVSAVQCIANPIKLARLVME----------KTPHCFLTDQGAAQFAAAMGV--PEIPGEK---LVTERNKKR- 147
Cdd:PLN02937  93 GDSGAFGAVGAVPGVRNAIQIAALLAKeqmmgssllgRIPPMFLVGEGARQWAKSKGIdlPETVEEAekwLVTERAKEQw 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145275202 148 --------------------------LEKEKHEK-----GAQKTDCQKN-----LGTVGAVALDCKGNVAYATSTGGIVN 191
Cdd:PLN02937 173 kkyktmlasaiaksscdsqstsklseLEAPRSNPsngtgGGQSSMCTASdedciMDTVGVICVDSEGNIASGASSGGIAM 252

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 145275202 192 KMVGRVGDSPCLGAGGYADND-------IGAVSTTGHGESILKVNLAR 232
Cdd:PLN02937 253 KVSGRVGLAAMYGSGCWASSKgpfgapfIVGCCVSGAGEYLMRGFAAR 300
 
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