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Conserved domains on  [gi|503561936|ref|WP_013796012|]
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M14 family metallopeptidase [Marinomonas posidonica]

Protein Classification

M14 family metallopeptidase( domain architecture ID 10161028)

M14 family metallopeptidase is a zinc-binding carboxypeptidase which hydrolyzes a single, C-terminal amino acid from a polypeptide chain, and has a recognition site for the free C-terminal carboxyl group

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
M14_ASTE_ASPA-like cd06910
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
24-232 2.82e-140

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


:

Pssm-ID: 349481  Cd Length: 208  Bit Score: 395.18  E-value: 2.82e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  24 DITPYKTGNGEIPYLYHFDSGVAGPHVMINALTHGNEVCGAIVVKELIDLAIQPRQGKLTLAFANVAAYLTFDSQHPDAS 103
Cdd:cd06910    1 DISPYKTGNTGIDYVHRFDSGQPGPHVMINALTHGNEICGAIALDWLLKNGVRPLRGRLTFCFANVEAYERFDPARPTAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 104 RFVDQDLNRVWTKEILDDlSQDSTELQRARQLRPIIDEVDVLLDLHSMHEKCPPLCVCGPQDKGLELALEQQSPAWIIRD 183
Cdd:cd06910   81 RFVDEDLNRVWGPELLDG-PEQSIELRRARELRPVVDTVDYLLDIHSMQEKVPPLALAGDKEKGRALARRVGSPAHLLID 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 503561936 184 EGHPEGCRMRDYADFGDPNSTKNALLVECGQHWESSAVTVARDVTARFL 232
Cdd:cd06910  160 AGHAEGLRLRDYAGFGDPSSPKNALLVECGQHWERSAVVVALDITLRFL 208
 
Name Accession Description Interval E-value
M14_ASTE_ASPA-like cd06910
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
24-232 2.82e-140

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349481  Cd Length: 208  Bit Score: 395.18  E-value: 2.82e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  24 DITPYKTGNGEIPYLYHFDSGVAGPHVMINALTHGNEVCGAIVVKELIDLAIQPRQGKLTLAFANVAAYLTFDSQHPDAS 103
Cdd:cd06910    1 DISPYKTGNTGIDYVHRFDSGQPGPHVMINALTHGNEICGAIALDWLLKNGVRPLRGRLTFCFANVEAYERFDPARPTAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 104 RFVDQDLNRVWTKEILDDlSQDSTELQRARQLRPIIDEVDVLLDLHSMHEKCPPLCVCGPQDKGLELALEQQSPAWIIRD 183
Cdd:cd06910   81 RFVDEDLNRVWGPELLDG-PEQSIELRRARELRPVVDTVDYLLDIHSMQEKVPPLALAGDKEKGRALARRVGSPAHLLID 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 503561936 184 EGHPEGCRMRDYADFGDPNSTKNALLVECGQHWESSAVTVARDVTARFL 232
Cdd:cd06910  160 AGHAEGLRLRDYAGFGDPSSPKNALLVECGQHWERSAVVVALDITLRFL 208
COG3608 COG3608
Predicted deacylase [General function prediction only];
34-325 1.17e-41

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 146.53  E-value: 1.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  34 EIPYlYHFDSGVAGPHVMINALTHGNEVCGAIVVKELID-LAIQPRQGKLTL-AFANVAAYLTFdsqhpdaSRF---VDQ 108
Cdd:COG3608   14 SLPV-TVFRGAGPGPTLLITAGIHGDELNGIEALRRLLReLDPGELRGTVILvPVANPPGFLQG-------SRYlpiDGR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 109 DLNRVWTkeildDLSQDSTELQRARQL-RPIIDEVDVLLDLHSMHEKCP--PLCVCGPQD-KGLELALEQQSPAwIIRDE 184
Cdd:COG3608   86 DLNRSFP-----GDADGSLAERIAHALfEEILPDADYVIDLHSGGIARDnlPHVRAGPGDeELRALARAFGAPV-ILDSP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 185 GHPEGCRMRDYADFGdpnstKNALLVECGQHWESSAVTVARDVTA--RFLMLHGLIQYKDLPSDWFQPIeskmnIVQVTE 262
Cdd:COG3608  160 EGGDGSLREAAAEAG-----IPALTLELGGGGRFDEESIEAGVRGilNVLRHLGMLDGEAPPPPLAPPV-----LARGSE 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503561936 263 PVVATSMDFHftDHYQGLEVFQKANSVIAY------QDGQQVTTPYENCVLVMPSVRQLRPGVTVVRLG 325
Cdd:COG3608  230 WVRAPAGGLF--EPLVELGDRVKKGDVLGRitdpfgEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHIA 296
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
46-250 3.71e-13

Succinylglutamate desuccinylase / Aspartoacylase family; This family includes Succinylglutamate desuccinylase EC:3.1.-.- that catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway. The family also include aspartoacylase EC:3.5.1.15 which cleaves acylaspartate into a fatty acid and aspartate. Mutations in Swiss:P45381 lead to Canavan disease. This family is probably structurally related to pfam00246 (Bateman A pers. obs.).


Pssm-ID: 428216 [Multi-domain]  Cd Length: 289  Bit Score: 68.53  E-value: 3.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936   46 AGPHVMINALTHGNEVCGAIVVKELI-DLAIQPRQGKLTLA-FANVAAYLTfdsqhpdASRFVDQDLNRVWTKEILDDLS 123
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLrQLDPGDIAGERTLVpLANPPAFRA-------GSRYIPRDLNRSFPGRALGASS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  124 QDSTELQRARQL-----RPIIDEVDVLLDLHS--MHEKCPPLCVCgPQDKGLELALE----QQSPAWIIRDEGHPEGCRM 192
Cdd:pfam04952  74 DEPYRATRAERLadlffPALLPRADIVLDLHTgtRGMGHLLFALA-PIRDDPLHLLAllraFGAPAVLKLHSKPSAGFSA 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  193 RDYADFGdpnstKNALLVECGQ--HWESSAVTVARDVTARFLMLHGLIQYKDLPSDWFQP 250
Cdd:pfam04952 153 FSAEELG-----APGFTLELGGagPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPPKL 207
PRK02259 PRK02259
aspartoacylase; Provisional
50-150 6.18e-09

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 56.04  E-value: 6.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  50 VMINALTHGNEVCGAIVVKELI--DLAIQPRQGKLTLAFANVAAYltfdsqhpDAS-RFVDQDLNRVWTKEILDDLSQDS 126
Cdd:PRK02259   5 VAIVGGTHGNEITGIYLVKKWQqqPNLINRKGLEVQTVIGNPEAI--------EAGrRYIDRDLNRSFRLDLLQNPDLSG 76
                         90       100
                 ....*....|....*....|....*....
gi 503561936 127 TELQRARQLRPII-----DEVDVLLDLHS 150
Cdd:PRK02259  77 YEQLRAKELVQQLgpkgnSPCDFIIDLHS 105
 
Name Accession Description Interval E-value
M14_ASTE_ASPA-like cd06910
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
24-232 2.82e-140

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349481  Cd Length: 208  Bit Score: 395.18  E-value: 2.82e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  24 DITPYKTGNGEIPYLYHFDSGVAGPHVMINALTHGNEVCGAIVVKELIDLAIQPRQGKLTLAFANVAAYLTFDSQHPDAS 103
Cdd:cd06910    1 DISPYKTGNTGIDYVHRFDSGQPGPHVMINALTHGNEICGAIALDWLLKNGVRPLRGRLTFCFANVEAYERFDPARPTAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 104 RFVDQDLNRVWTKEILDDlSQDSTELQRARQLRPIIDEVDVLLDLHSMHEKCPPLCVCGPQDKGLELALEQQSPAWIIRD 183
Cdd:cd06910   81 RFVDEDLNRVWGPELLDG-PEQSIELRRARELRPVVDTVDYLLDIHSMQEKVPPLALAGDKEKGRALARRVGSPAHLLID 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 503561936 184 EGHPEGCRMRDYADFGDPNSTKNALLVECGQHWESSAVTVARDVTARFL 232
Cdd:cd06910  160 AGHAEGLRLRDYAGFGDPSSPKNALLVECGQHWERSAVVVALDITLRFL 208
COG3608 COG3608
Predicted deacylase [General function prediction only];
34-325 1.17e-41

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 146.53  E-value: 1.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  34 EIPYlYHFDSGVAGPHVMINALTHGNEVCGAIVVKELID-LAIQPRQGKLTL-AFANVAAYLTFdsqhpdaSRF---VDQ 108
Cdd:COG3608   14 SLPV-TVFRGAGPGPTLLITAGIHGDELNGIEALRRLLReLDPGELRGTVILvPVANPPGFLQG-------SRYlpiDGR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 109 DLNRVWTkeildDLSQDSTELQRARQL-RPIIDEVDVLLDLHSMHEKCP--PLCVCGPQD-KGLELALEQQSPAwIIRDE 184
Cdd:COG3608   86 DLNRSFP-----GDADGSLAERIAHALfEEILPDADYVIDLHSGGIARDnlPHVRAGPGDeELRALARAFGAPV-ILDSP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 185 GHPEGCRMRDYADFGdpnstKNALLVECGQHWESSAVTVARDVTA--RFLMLHGLIQYKDLPSDWFQPIeskmnIVQVTE 262
Cdd:COG3608  160 EGGDGSLREAAAEAG-----IPALTLELGGGGRFDEESIEAGVRGilNVLRHLGMLDGEAPPPPLAPPV-----LARGSE 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503561936 263 PVVATSMDFHftDHYQGLEVFQKANSVIAY------QDGQQVTTPYENCVLVMPSVRQLRPGVTVVRLG 325
Cdd:COG3608  230 WVRAPAGGLF--EPLVELGDRVKKGDVLGRitdpfgEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHIA 296
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
50-224 3.21e-18

Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349486 [Multi-domain]  Cd Length: 168  Bit Score: 80.57  E-value: 3.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  50 VMINALTHGNEVCGAIVVKELID--LAIQPRQGKLTLAFANVAAYltfdsqhPDASRFVDQDLNRVWTKeildDLSQDST 127
Cdd:cd18430    1 LAVLGAVHGNETCGTRAVERLLAelPSGALQKGPVTLVPANERAY-------AEGVRFCEEDLNRVFPG----DPDPDTY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 128 ELQRARQLRPIIDEVDVLLDLHSMHEKCPPLCVCGPQDKGLELaleqqspawIIRDEGHPEGCRMRD----YADFGDPNS 203
Cdd:cd18430   70 ERRLANRLCPELEGHDVVLDLHSTHSGGQPFAILDYGDKASRR---------LARSVGIPKGWRVVYgrdlGYAHGGGKT 140
                        170       180
                 ....*....|....*....|.
gi 503561936 204 TKNALLVECGQHWESSAVTVA 224
Cdd:cd18430  141 EVTGVTVECGYHDSEEAAEVA 161
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
50-215 3.65e-14

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily belongs to the M14 family of metallocarboxypeptidases (MCPs), and includes ASTE, which catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) which cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349449 [Multi-domain]  Cd Length: 177  Bit Score: 69.65  E-value: 3.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  50 VMINALTHGNEVCGAIVVKELI-DLAIQPRQGKLTLAF-ANVAAYLTFDSQHPDasrfVDQDLNRVWTkeiLDDLSqdST 127
Cdd:cd06230    1 LLILAGVHGDEYEGVEAIRRLLaELDPSELKGTVVLVPvANPPAFEAGTRYTPL----DGLDLNRIFP---GDPDG--SP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 128 ELQRARQLRP-IIDEVDVLLDLHS----MHEKCPPLCVCGPQDKGLELALEQQSPAWIIRDEGHPEGCRMRDYADFGDPn 202
Cdd:cd06230   72 TERLAHELTElILKHADALIDLHSggtgRLVPYAILDYDSDAREKSRELARAFGGTPVIWGGDPPGGTPVAAARSAGIP- 150
                        170
                 ....*....|...
gi 503561936 203 stknALLVECGQH 215
Cdd:cd06230  151 ----AITVELGGG 159
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
50-150 1.52e-13

Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the Succinylglutamate desuccinylase/aspartoacylase subfamily of the M14 family of metallocarboxypeptidases. ASPA (also known as aminoacylase 2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349480  Cd Length: 190  Bit Score: 68.00  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  50 VMINALTHGNEVCGAIVVKELI-DLAIQPRQGKLTLAF-ANVAAYltfdsqhpDAS-RFVDQDLNRVWTKEILDDLSQDS 126
Cdd:cd06909    3 VAIVGGTHGNELTGVYLVKHWLkNPELIERKSFEVHPLlANPRAV--------EQCrRYIDTDLNRCFSLENLSSAPSSL 74
                         90       100       110
                 ....*....|....*....|....*....|
gi 503561936 127 T-ELQRARQLRPII-----DEVDVLLDLHS 150
Cdd:cd06909   75 PyEVRRAREINQILgpkgnPACDFIIDLHN 104
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
46-324 3.69e-13

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 68.72  E-value: 3.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  46 AGPHVMINALTHGNEVCGAIVVKELIDlaiQPRQGKLTLA------FANVAAYLtfdsqhpDASRFVDQDLNRVWTKEIL 119
Cdd:COG2988   23 GIKAVVISGGIHGNETAPIELLDKLLQ---DLLLGERPLSfrllliLGNPAAMR-------AGRRYLDEDLNRLFGGRHL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 120 DDlsQDSTELQRARQLRPIIDE-------VDVLLDLHS----MHekcPPLCVCGPQDKG---LELA--LEQQSP-AWIIr 182
Cdd:COG2988   93 QN--PESYEAARAKELEQAVGPffaaggrVRLHIDLHTairnSG---HERFAVYPFRGRpfdLALLayLAAAGPeAVVL- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 183 deghpegcrmrdyadFGDPNSTKNALLVEcgqHWESSAVTV------------ARDVTARFLMLHGLIQYKDLPSDWFQP 250
Cdd:COG2988  167 ---------------HHAPGGTFSHFSAE---LCGAQAFTLelgkvrpfgqndLSRFAATEEALRALLSGAELPEHPAQD 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503561936 251 IEskmnIVQVTEPVVATSMDFHFTDHYQGLEvFQ--KANSVIAYQDGQQVTTPYENCVLVMP---SVRQLRPGVTVVRL 324
Cdd:COG2988  229 LD----LYRVVQQIIKHGDDFMLHPDLDTLN-FTplPPGTLLAEDGGKEYRVEGDEERIVFPneaVYYGQRAALLLTPK 302
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
46-250 3.71e-13

Succinylglutamate desuccinylase / Aspartoacylase family; This family includes Succinylglutamate desuccinylase EC:3.1.-.- that catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway. The family also include aspartoacylase EC:3.5.1.15 which cleaves acylaspartate into a fatty acid and aspartate. Mutations in Swiss:P45381 lead to Canavan disease. This family is probably structurally related to pfam00246 (Bateman A pers. obs.).


Pssm-ID: 428216 [Multi-domain]  Cd Length: 289  Bit Score: 68.53  E-value: 3.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936   46 AGPHVMINALTHGNEVCGAIVVKELI-DLAIQPRQGKLTLA-FANVAAYLTfdsqhpdASRFVDQDLNRVWTKEILDDLS 123
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLrQLDPGDIAGERTLVpLANPPAFRA-------GSRYIPRDLNRSFPGRALGASS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  124 QDSTELQRARQL-----RPIIDEVDVLLDLHS--MHEKCPPLCVCgPQDKGLELALE----QQSPAWIIRDEGHPEGCRM 192
Cdd:pfam04952  74 DEPYRATRAERLadlffPALLPRADIVLDLHTgtRGMGHLLFALA-PIRDDPLHLLAllraFGAPAVLKLHSKPSAGFSA 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  193 RDYADFGdpnstKNALLVECGQ--HWESSAVTVARDVTARFLMLHGLIQYKDLPSDWFQP 250
Cdd:pfam04952 153 FSAEELG-----APGFTLELGGagPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPPKL 207
PRK02259 PRK02259
aspartoacylase; Provisional
50-150 6.18e-09

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 56.04  E-value: 6.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  50 VMINALTHGNEVCGAIVVKELI--DLAIQPRQGKLTLAFANVAAYltfdsqhpDAS-RFVDQDLNRVWTKEILDDLSQDS 126
Cdd:PRK02259   5 VAIVGGTHGNEITGIYLVKKWQqqPNLINRKGLEVQTVIGNPEAI--------EAGrRYIDRDLNRSFRLDLLQNPDLSG 76
                         90       100
                 ....*....|....*....|....*....
gi 503561936 127 TELQRARQLRPII-----DEVDVLLDLHS 150
Cdd:PRK02259  77 YEQLRAKELVQQLgpkgnSPCDFIIDLHS 105
M14_ASTE_ASPA-like cd06255
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
47-226 6.11e-06

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349473  Cd Length: 223  Bit Score: 46.55  E-value: 6.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  47 GPHVMINALTHGNEVCGAIVVKELIDlAIQPRQGKLTLAFANVAAYLTFDSQHpDASRFVDQDLNRVWTKEILDDLSQds 126
Cdd:cd06255   23 GPCLWINGAVHGDELNGPLAALELFR-ELDPAQLSGTLVATPIANPLAFQGRQ-KFSPQDGEDLDQSFPGDPDGLITE-- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 127 telQRARQLRPIIDEV-DVLLDLHSMHE----------KCPPLCVCGPQDKGLELAleqqspawiiRDEGHPEGCRMRDY 195
Cdd:cd06255   99 ---RMAHALFSEVKEVaDYLIDFHTGGTpfdanpytvyKLFPESGPVEEKRLLRLA----------RAFGVHANCRVDVS 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 503561936 196 ADFGDPNSTKN-------------ALLVECG--QHWESSAVTVARD 226
Cdd:cd06255  166 GAGGELPGNTAgaldyqcmaqgipAFMVELGggGRAEEEAVRFAAR 211
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
47-238 3.78e-05

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349469 [Multi-domain]  Cd Length: 195  Bit Score: 43.68  E-value: 3.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  47 GPHVMINALTHGNEVCGAIVVKELI-DLAIQPRQGKLTlAF--ANVAAYLTFDSQHPDASRfvdqDLNRVWtkeildDLS 123
Cdd:cd06251   12 GPTLLLTAAIHGDELNGIEVIQRLLeDLDPSKLRGTLI-AIpvVNPLGFENNSRYLPDDGR----DLNRSF------PGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 124 QDSTELQR-ARQLRP-IIDEVDVLLDLH--SMHEKCPPLC-VCGPQDKGLELALEQQSPawIIRDEGHPEGcRMRDYA-D 197
Cdd:cd06251   81 EKGSLASRlAHLLWNeIVKKADYVIDLHtaSTGRTNLPYVrADLRDPESRRMAEAFGAP--VIVDDPGEDG-SLRGAAvE 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 503561936 198 FGDPnstknALLVECGQHWESSAVTVARDVTA--RFLMLHGLI 238
Cdd:cd06251  158 LGIP-----AITVELGEALRFDEDIIRRGVEGvlNVLRHLGML 195
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
45-214 1.28e-04

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349472  Cd Length: 198  Bit Score: 42.18  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  45 VAGPHVMINALTHGNEVCGaivVKELIDLA--IQPRQ--GKLTLA-FANVAAYLTfdsqHPDASRFVD-QDLNRVWTKei 118
Cdd:cd06254    9 KPGPTLLITAGIHGGEYPG---ILAAIRLAreLDPADvkGTLIIVhIANVSGFEA----RTPFVVPEDgKNLNRVFPG-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 119 lddlSQDSTELQRARQL--RPIIDEVDVLLDLHS--MHEK-CPPLCVCG---PQ--DKGLELALEQQSPAwIIRDEGHPE 188
Cdd:cd06254   80 ----DPDGTLTERIAYFltREIISRADFLIDLHGgdANEAlTPFVYYPGgasEEvnDISRAAAQALGLPY-IVISSSEKG 154
                        170       180
                 ....*....|....*....|....*.
gi 503561936 189 GCRMRDYADFGDPnstknALLVECGQ 214
Cdd:cd06254  155 TGYYSYAALRGIP-----SILVERGG 175
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
50-154 5.29e-03

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 38.24  E-value: 5.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  50 VMINALTHGNE-----VCGAIVvkelIDLAiqprQGKLTLA------FANVAAYLTfdsqhpdASRFVDQDLNRV----W 114
Cdd:PRK05324  50 LVLSAGIHGNEtapieLLDQLV----RDLL----AGELPLRarllviLGNPPAMRA-------GKRYLDEDLNRLfggrH 114
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503561936 115 TKeilddlSQDSTELQRARQLRPII--------DEVDVLLDLH-----SMHEK 154
Cdd:PRK05324 115 QQ------FPGSDEARRAAELEQAVedffaagaERVRWHYDLHtairgSKHEQ 161
M14_CP_Csd4-like cd06243
Peptidase M14 carboxypeptidase Csd4 and similar proteins; This family includes peptidase M14 ...
34-149 5.64e-03

Peptidase M14 carboxypeptidase Csd4 and similar proteins; This family includes peptidase M14 carboxypeptidase Csd4 from H. pylori which has been shown to be DL-carboxypeptidase with a modified zinc binding site containing a glutamine residue in place of a conserved histidine. It is an archetype of a new carboxypeptidase subfamily with a domain arrangement that differs from this family of peptide-cleaving enzymes. Csd4 plays a role in trimming uncrosslinked peptidoglycan peptide chains by cleaving the amide bond between meso-diaminopimelate and iso-D-glutamic acid in truncated peptidoglycan side chains. It acts as a cell shape determinant, similar to Campylobacter jejuni Pgp1. The M14 family of metallocarboxypeptidases (MCPs), also known as funnelins, are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349462  Cd Length: 227  Bit Score: 37.72  E-value: 5.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  34 EIPYLYHFDSgVAGPHVMINALTHGNEVCGAIVVKELIDLAIqpRQGKL-TLAFANVAAYLTfdsqhpdASRFVDQDLNR 112
Cdd:cd06243    4 EKPFTRLEGR-EPGPTLLIIGGIQGDEPGGFLAADLLADLYL--VKGNViVVPRLNFPSILR-------NHRGLNGDMNR 73
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 503561936 113 VWtkeilDDLSQDSTELQRARQLRPIIDE--VDVLLDLH 149
Cdd:cd06243   74 KF-----AALDKKDPEYKTIQEIKSLIADfrPDVVLHLH 107
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
57-179 7.35e-03

Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 Succinylglutamate desuccinylase (ASTE, also known as N-succinyl-L-glutamate amidohydrolase, N2-succinylglutamate desuccinylase, and SGDS; EC 3.5.1.96) belongs to the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily of the M14 family of metallocarboxypeptidases. This group includes succinylglutamate desuccinylase that catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway. It hydrolyzes N-succinyl-L-glutamate to succinate and L-glutamate.


Pssm-ID: 349428  Cd Length: 239  Bit Score: 37.18  E-value: 7.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  57 HGNE-----VCGAIvvkeLIDLAiqprQGKLTLA------FANVAAYLTfdsqhpdASRFVDQDLNR----VWTKEildd 121
Cdd:cd03855   53 HGNEtapieILDQL----INDLI----RGELALAhrllfiFGNPPAIRQ-------GKRFIEENLNRlfsgRHSKL---- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936 122 lsQDSTELQRARQLRPIIDE--------VDVLLDLH-----SMHEK------CPPLCVCGPQ-----DKGLELALEQQSP 177
Cdd:cd03855  114 --PPSYETARAAELEQAVADffakasgeVRWHLDLHtairgSKHEQfavypfLEGRPHDREQldflgAAGIEAVLLSNSP 191

                 ..
gi 503561936 178 AW 179
Cdd:cd03855  192 GG 193
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
46-150 7.38e-03

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; uncharacterized subgroup; A functionally uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the M14 family of metallocarboxypeptidases. ASTE catalyzes the fifth and last step in arginine catabolism by the arginine succinyltransferase pathway, and aspartoacylase (ASPA, also known as aminoacylase 2, and ACY-2; EC:3.5.1.15) cleaves N-acetyl L-aspartic acid (NAA) into aspartate and acetate. NAA is abundant in the brain, and hydrolysis of NAA by ASPA may help maintain white matter. ASPA is an NAA scavenger in other tissues. Mutations in the gene encoding ASPA cause Canavan disease (CD), a fatal progressive neurodegenerative disorder involving dysmyelination and spongiform degeneration of white matter in children. This enzyme binds zinc which is necessary for activity. Measurement of elevated NAA levels in urine is used in the diagnosis of CD.


Pssm-ID: 349470  Cd Length: 224  Bit Score: 37.16  E-value: 7.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503561936  46 AGPHVMINALTHGNEVCGAIVVKELI-DLAIQPRQGKLTLA-FANVAAYLtfdsqhpdASRFV----DQDLNRVWtkeiL 119
Cdd:cd06252   33 SGPTVLLTGGNHGDEYEGPIALRRLArDLDPEDVRGRLIIVpALNLPAVR--------AGTRTspldGGNLNRAF----P 100
                         90       100       110
                 ....*....|....*....|....*....|...
gi 503561936 120 DDlsQDSTELQR-ARQL-RPIIDEVDVLLDLHS 150
Cdd:cd06252  101 GD--ADGTPTERiAHFLeTVLLPRADAVIDLHS 131
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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