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Conserved domains on  [gi|893705440|ref|WP_048934076|]
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MULTISPECIES: M14 family metallopeptidase [Ralstonia]

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; ...
22-229 1.14e-138

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: 390.94  E-value: 1.14e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  22 DIRWWKTGTHGVDYVHTFDSGVPGPHVMINALTHGNELCGAIAVDALLAAGVRPARGQLTLSFANVEAYERFDINDPDAT 101
Cdd:cd06910    1 DISPYKTGNTGIDYVHRFDSGQPGPHVMINALTHGNEICGAIALDWLLKNGVRPLRGRLTFCFANVEAYERFDPARPTAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 102 RFIDEDLNRVWSADKLDGPGNTLELRRARELRPVIDTVDYLLDIHSMHEKAEPLMLTGPLEKGVALGRQVGAPSHLMIDA 181
Cdd:cd06910   81 RFVDEDLNRVWGPELLDGPEQSIELRRARELRPVVDTVDYLLDIHSMQEKVPPLALAGDKEKGRALARRVGSPAHLLIDA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 893705440 182 GHAAGRRLRDYAGFGDAASPKNALLIECGQHFERVSRDVALDACARFL 229
Cdd:cd06910  161 GHAEGLRLRDYAGFGDPSSPKNALLVECGQHWERSAVVVALDITLRFL 208
 
Name Accession Description Interval E-value
M14_ASTE_ASPA-like cd06910
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
22-229 1.14e-138

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: 390.94  E-value: 1.14e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  22 DIRWWKTGTHGVDYVHTFDSGVPGPHVMINALTHGNELCGAIAVDALLAAGVRPARGQLTLSFANVEAYERFDINDPDAT 101
Cdd:cd06910    1 DISPYKTGNTGIDYVHRFDSGQPGPHVMINALTHGNEICGAIALDWLLKNGVRPLRGRLTFCFANVEAYERFDPARPTAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 102 RFIDEDLNRVWSADKLDGPGNTLELRRARELRPVIDTVDYLLDIHSMHEKAEPLMLTGPLEKGVALGRQVGAPSHLMIDA 181
Cdd:cd06910   81 RFVDEDLNRVWGPELLDGPEQSIELRRARELRPVVDTVDYLLDIHSMQEKVPPLALAGDKEKGRALARRVGSPAHLLIDA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 893705440 182 GHAAGRRLRDYAGFGDAASPKNALLIECGQHFERVSRDVALDACARFL 229
Cdd:cd06910  161 GHAEGLRLRDYAGFGDPSSPKNALLVECGQHWERSAVVVALDITLRFL 208
COG3608 COG3608
Predicted deacylase [General function prediction only];
36-322 3.29e-36

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 132.28  E-value: 3.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  36 VHTFDSGVPGPHVMINALTHGNELCGAIAVDALLAAgVRPA--RGQLTL-SFANVEAYERFdindpdaTRFI---DEDLN 109
Cdd:COG3608   17 VTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRE-LDPGelRGTVILvPVANPPGFLQG-------SRYLpidGRDLN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 110 RVWSADKlDGpgnTLELRRAREL-RPVIDTVDYLLDIHSMHEKAE--PLMLTGPL-EKGVALGRQVGAPshLMIDAGHAA 185
Cdd:COG3608   89 RSFPGDA-DG---SLAERIAHALfEEILPDADYVIDLHSGGIARDnlPHVRAGPGdEELRALARAFGAP--VILDSPEGG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 186 GRRLRDYAgfgdAASPKNALLIECGQH--FERVSRDVALDACARFLVALGTVDASVVSqwfgiAPALEVRCIRVTDPVVA 263
Cdd:COG3608  163 DGSLREAA----AEAGIPALTLELGGGgrFDEESIEAGVRGILNVLRHLGMLDGEAPP-----PPLAPPVLARGSEWVRA 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 893705440 264 KSTA-FRFaddYRGMETIASAGTVIAT------DGELQFVTPYDNCVLLQPSLRHLAPGVTVVRLG 322
Cdd:COG3608  234 PAGGlFEP---LVELGDRVKKGDVLGRitdpfgEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHIA 296
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
44-147 3.51e-10

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: 60.06  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440   44 PGPHVMINALTHGNELCGAIAVDAL---LAAGVRPARGQLTLsFANVEAYERfdindpdATRFIDEDLNRVWSADKLDGP 120
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLlrqLDPGDIAGERTLVP-LANPPAFRA-------GSRYIPRDLNRSFPGRALGAS 72
                          90       100       110
                  ....*....|....*....|....*....|...
gi 893705440  121 G-NTLELRRAREL-----RPVIDTVDYLLDIHS 147
Cdd:pfam04952  73 SdEPYRATRAERLadlffPALLPRADIVLDLHT 105
PRK02259 PRK02259
aspartoacylase; Provisional
48-147 1.76e-08

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 54.88  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  48 VMINALTHGNELCGAIAVDALLAAG--VRPARGQLTLSFANVEAYERfdindpdATRFIDEDLNRVWSADKLDGPGNT-L 124
Cdd:PRK02259   5 VAIVGGTHGNEITGIYLVKKWQQQPnlINRKGLEVQTVIGNPEAIEA-------GRRYIDRDLNRSFRLDLLQNPDLSgY 77
                         90       100
                 ....*....|....*....|....*...
gi 893705440 125 ELRRARELRPVI-----DTVDYLLDIHS 147
Cdd:PRK02259  78 EQLRAKELVQQLgpkgnSPCDFIIDLHS 105
 
Name Accession Description Interval E-value
M14_ASTE_ASPA-like cd06910
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
22-229 1.14e-138

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: 390.94  E-value: 1.14e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  22 DIRWWKTGTHGVDYVHTFDSGVPGPHVMINALTHGNELCGAIAVDALLAAGVRPARGQLTLSFANVEAYERFDINDPDAT 101
Cdd:cd06910    1 DISPYKTGNTGIDYVHRFDSGQPGPHVMINALTHGNEICGAIALDWLLKNGVRPLRGRLTFCFANVEAYERFDPARPTAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 102 RFIDEDLNRVWSADKLDGPGNTLELRRARELRPVIDTVDYLLDIHSMHEKAEPLMLTGPLEKGVALGRQVGAPSHLMIDA 181
Cdd:cd06910   81 RFVDEDLNRVWGPELLDGPEQSIELRRARELRPVVDTVDYLLDIHSMQEKVPPLALAGDKEKGRALARRVGSPAHLLIDA 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 893705440 182 GHAAGRRLRDYAGFGDAASPKNALLIECGQHFERVSRDVALDACARFL 229
Cdd:cd06910  161 GHAEGLRLRDYAGFGDPSSPKNALLVECGQHWERSAVVVALDITLRFL 208
COG3608 COG3608
Predicted deacylase [General function prediction only];
36-322 3.29e-36

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 132.28  E-value: 3.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  36 VHTFDSGVPGPHVMINALTHGNELCGAIAVDALLAAgVRPA--RGQLTL-SFANVEAYERFdindpdaTRFI---DEDLN 109
Cdd:COG3608   17 VTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRE-LDPGelRGTVILvPVANPPGFLQG-------SRYLpidGRDLN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 110 RVWSADKlDGpgnTLELRRAREL-RPVIDTVDYLLDIHSMHEKAE--PLMLTGPL-EKGVALGRQVGAPshLMIDAGHAA 185
Cdd:COG3608   89 RSFPGDA-DG---SLAERIAHALfEEILPDADYVIDLHSGGIARDnlPHVRAGPGdEELRALARAFGAP--VILDSPEGG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 186 GRRLRDYAgfgdAASPKNALLIECGQH--FERVSRDVALDACARFLVALGTVDASVVSqwfgiAPALEVRCIRVTDPVVA 263
Cdd:COG3608  163 DGSLREAA----AEAGIPALTLELGGGgrFDEESIEAGVRGILNVLRHLGMLDGEAPP-----PPLAPPVLARGSEWVRA 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 893705440 264 KSTA-FRFaddYRGMETIASAGTVIAT------DGELQFVTPYDNCVLLQPSLRHLAPGVTVVRLG 322
Cdd:COG3608  234 PAGGlFEP---LVELGDRVKKGDVLGRitdpfgEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHIA 296
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
48-228 4.46e-19

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: 82.88  E-value: 4.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  48 VMINALTHGNELCGAIAVDALLAAGVRPA--RGQLTLSFANVEAYERfdindpdATRFIDEDLNRVWSADKldgPGNTLE 125
Cdd:cd18430    1 LAVLGAVHGNETCGTRAVERLLAELPSGAlqKGPVTLVPANERAYAE-------GVRFCEEDLNRVFPGDP---DPDTYE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 126 LRRARELRPVIDTVDYLLDIHSMHEKAEPL-MLTGPLEKGVALGRQVGAPSHL-MIDaghaaGRRLRDYAGFGdaASPKN 203
Cdd:cd18430   71 RRLANRLCPELEGHDVVLDLHSTHSGGQPFaILDYGDKASRRLARSVGIPKGWrVVY-----GRDLGYAHGGG--KTEVT 143
                        170       180
                 ....*....|....*....|....*
gi 893705440 204 ALLIECGQHFERVSRDVALDACARF 228
Cdd:cd18430  144 GVTVECGYHDSEEAAEVAYRAILNT 168
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
45-296 1.62e-15

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 75.65  E-value: 1.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  45 GPHVMINALTHGNELCGAIAVDALLAAgvrPARGQLTLS------FANVEAYERfdindpdATRFIDEDLNRVWSADKLD 118
Cdd:COG2988   24 IKAVVISGGIHGNETAPIELLDKLLQD---LLLGERPLSfrllliLGNPAAMRA-------GRRYLDEDLNRLFGGRHLQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 119 GPGNtLELRRARELRPVID-------TVDYLLDIH-----SMHEKaeplMLTGPLEKGVALGRQVGAPSHLMIDAG---H 183
Cdd:COG2988   94 NPES-YEAARAKELEQAVGpffaaggRVRLHIDLHtairnSGHER----FAVYPFRGRPFDLALLAYLAAAGPEAVvlhH 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 184 AAGrrlRDYAGFGDAASPKNALLIECGqhfeRVSRDVALDAcARFLVALGTVDASVVSQWFGIAPALEVRCIRVTDPVVA 263
Cdd:COG2988  169 APG---GTFSHFSAELCGAQAFTLELG----KVRPFGQNDL-SRFAATEEALRALLSGAELPEHPAQDLDLYRVVQQIIK 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 893705440 264 KSTAFR--FADDYRGMETIAsAGTVIATDGELQFV 296
Cdd:COG2988  241 HGDDFMlhPDLDTLNFTPLP-PGTLLAEDGGKEYR 274
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
48-147 4.11e-15

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: 72.63  E-value: 4.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  48 VMINALTHGNELCGAIAVDALLAAGVRPARGQLTLSF--ANVEAYERfdindpdATRFIDEDLNRVWSADKLDGP--GNT 123
Cdd:cd06909    3 VAIVGGTHGNELTGVYLVKHWLKNPELIERKSFEVHPllANPRAVEQ-------CRRYIDTDLNRCFSLENLSSApsSLP 75
                         90       100
                 ....*....|....*....|....*....
gi 893705440 124 LELRRAREL----RPVIDT-VDYLLDIHS 147
Cdd:cd06909   76 YEVRRAREInqilGPKGNPaCDFIIDLHN 104
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
48-226 8.65e-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: 68.49  E-value: 8.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  48 VMINALTHGNELCGAIAVDALLAAGVRPA-RGQLTL-SFANVEAYERfdindpdATRFIDE---DLNRVWSADkldgPGN 122
Cdd:cd06230    1 LLILAGVHGDEYEGVEAIRRLLAELDPSElKGTVVLvPVANPPAFEA-------GTRYTPLdglDLNRIFPGD----PDG 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 123 TLELRRARELRP-VIDTVDYLLDIHSMHEKAEP--LMLTGPL---EKGVALGRQVGAPSHLMIDaGHAAGRRLRDYAGFG 196
Cdd:cd06230   70 SPTERLAHELTElILKHADALIDLHSGGTGRLVpyAILDYDSdarEKSRELARAFGGTPVIWGG-DPPGGTPVAAARSAG 148
                        170       180       190
                 ....*....|....*....|....*....|
gi 893705440 197 DAaspknALLIECGQHFERVSRDVALDACA 226
Cdd:cd06230  149 IP-----AITVELGGGGRLRAERLERYLRG 173
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
44-147 3.51e-10

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: 60.06  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440   44 PGPHVMINALTHGNELCGAIAVDAL---LAAGVRPARGQLTLsFANVEAYERfdindpdATRFIDEDLNRVWSADKLDGP 120
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLlrqLDPGDIAGERTLVP-LANPPAFRA-------GSRYIPRDLNRSFPGRALGAS 72
                          90       100       110
                  ....*....|....*....|....*....|...
gi 893705440  121 G-NTLELRRAREL-----RPVIDTVDYLLDIHS 147
Cdd:pfam04952  73 SdEPYRATRAERLadlffPALLPRADIVLDLHT 105
PRK02259 PRK02259
aspartoacylase; Provisional
48-147 1.76e-08

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 54.88  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  48 VMINALTHGNELCGAIAVDALLAAG--VRPARGQLTLSFANVEAYERfdindpdATRFIDEDLNRVWSADKLDGPGNT-L 124
Cdd:PRK02259   5 VAIVGGTHGNEITGIYLVKKWQQQPnlINRKGLEVQTVIGNPEAIEA-------GRRYIDRDLNRSFRLDLLQNPDLSgY 77
                         90       100
                 ....*....|....*....|....*...
gi 893705440 125 ELRRARELRPVI-----DTVDYLLDIHS 147
Cdd:PRK02259  78 EQLRAKELVQQLgpkgnSPCDFIIDLHS 105
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
48-151 4.18e-06

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 47.87  E-value: 4.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  48 VMINALTHGNE-----LCGAIAVDalLAAGVRPARGQLTLSFANVEAyerfdINDpdATRFIDEDLNRVWSADKLDGPGn 122
Cdd:PRK05324  50 LVLSAGIHGNEtapieLLDQLVRD--LLAGELPLRARLLVILGNPPA-----MRA--GKRYLDEDLNRLFGGRHQQFPG- 119
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 893705440 123 TLELRRARELRPVIDT--------VDYLLDIH-----SMHEK 151
Cdd:PRK05324 120 SDEARRAAELEQAVEDffaagaerVRWHYDLHtairgSKHEQ 161
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
44-233 4.82e-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: 349469 [Multi-domain]  Cd Length: 195  Bit Score: 46.38  E-value: 4.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  44 PGPHVMINALTHGNELCGaIAVDALLAAGVRPA--RGQLT-LSFANVEAYERFDINDPDATRfideDLNRVWSADKldgP 120
Cdd:cd06251   11 PGPTLLLTAAIHGDELNG-IEVIQRLLEDLDPSklRGTLIaIPVVNPLGFENNSRYLPDDGR----DLNRSFPGSE---K 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 121 GNTLELRRARELRPVIDTVDYLLDIH--SMHEKAEPLML-TGPLEKGVALGRQVGAPshlMIDAGHAAGRRLRDYAgfGD 197
Cdd:cd06251   83 GSLASRLAHLLWNEIVKKADYVIDLHtaSTGRTNLPYVRaDLRDPESRRMAEAFGAP---VIVDDPGEDGSLRGAA--VE 157
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 893705440 198 AASPknALLIECGQH--FERVSRDVALDACARFLVALG 233
Cdd:cd06251  158 LGIP--AITVELGEAlrFDEDIIRRGVEGVLNVLRHLG 193
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
43-154 2.29e-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: 349472  Cd Length: 198  Bit Score: 44.49  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  43 VPGPHVMINALTHGNELCGAIAVdALLAAGVRPAR--GQLTL-SFANVEAYE--RFDINdpdatrFIDED-LNRVWsadk 116
Cdd:cd06254    9 KPGPTLLITAGIHGGEYPGILAA-IRLARELDPADvkGTLIIvHIANVSGFEarTPFVV------PEDGKnLNRVF---- 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 893705440 117 ldgPGN---TLELRRAREL-RPVIDTVDYLLDIHS--MHEKAEP 154
Cdd:cd06254   78 ---PGDpdgTLTERIAYFLtREIISRADFLIDLHGgdANEALTP 118
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
50-222 2.87e-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: 349484  Cd Length: 187  Bit Score: 44.15  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  50 INALTHGNELCGAIAVDALlAAGVRPA--RGQLTLS-FANVEAYER--FDINDPDatrfiDEDLNRVWSADKlDGpgnTL 124
Cdd:cd18174    3 VTAGVHGYEYASIEALQRL-IKELDPAklSGTVIVVpIANIPAFEGrsIYVNPLD-----GKNLNRSFPGDP-DG---TP 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 125 ELRRAREL-RPVIDTVDYLLDIHS--MHEKAEP--LMLTGPLEKGVALGRQV----GAPsHLMIDAGHAAGRRLRDYAGF 195
Cdd:cd18174   73 TERLAHWLtTNVIARADYYIDLHGgdLNEDLRPfvYYYETGNAALDAASREMaeafGLD-HIVFYKARLKASRGSLYTQA 151
                        170       180
                 ....*....|....*....|....*..
gi 893705440 196 GDAASPKNALLIECGQHFERVSRDVAL 222
Cdd:cd18174  152 AALLRGIPAILVEAGGLGSRDEEDVAR 178
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
55-151 6.43e-05

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: 43.73  E-value: 6.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  55 HGNE-----LCGAIaVDALlaagvrpARGQLTLS------FANVEAYERfdindpdATRFIDEDLNRVWSADKLDGPgNT 123
Cdd:cd03855   53 HGNEtapieILDQL-INDL-------IRGELALAhrllfiFGNPPAIRQ-------GKRFIEENLNRLFSGRHSKLP-PS 116
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 893705440 124 LELRRARELRPVID--------TVDYLLDIH-----SMHEK 151
Cdd:cd03855  117 YETARAAELEQAVAdffakasgEVRWHLDLHtairgSKHEQ 157
M14_ASTE_ASPA-like cd06256
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
45-147 6.92e-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: 349474  Cd Length: 204  Bit Score: 43.05  E-value: 6.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  45 GPHVMINALTHGNELCGAIAVDALLAAGVRPARGQLTLSFANVEAYERfdindpdATRFID--EDLNRVWSadkldGPGN 122
Cdd:cd06256   34 PRPLFVSTLLHGNEPTGLRAVQRLLKTGQAPLPRTLLLFIGNVDAAKA-------GVRRLPgqPDYNRCWP-----GPFE 101
                         90       100
                 ....*....|....*....|....*..
gi 893705440 123 TLELRRARELRPVIDT--VDYLLDIHS 147
Cdd:cd06256  102 TPEGRLAAAVLERLDTlrPFASIDIHN 128
M14_ASTE_ASPA-like cd06255
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
44-234 5.29e-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: 349473  Cd Length: 223  Bit Score: 40.77  E-value: 5.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  44 PGPHVMINALTHGNELCGAIAVDALLaAGVRPARGQLTLSF---AN---VEAYERFdindpdaTRFIDEDLNRVWSADKl 117
Cdd:cd06255   22 PGPCLWINGAVHGDELNGPLAALELF-RELDPAQLSGTLVAtpiANplaFQGRQKF-------SPQDGEDLDQSFPGDP- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440 118 DGPGNTlelRRA----RELRPVidtVDYLLDIHSMH----EKAEPLMLTGPLEKGVA------LGRQVGAPSHLMIDAGH 183
Cdd:cd06255   93 DGLITE---RMAhalfSEVKEV---ADYLIDFHTGGtpfdANPYTVYKLFPESGPVEekrllrLARAFGVHANCRVDVSG 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 893705440 184 AAGRRLRDYAGFGD---AASPKNALLIECG--QHFERVSRDVALDACARFLVALGT 234
Cdd:cd06255  167 AGGELPGNTAGALDyqcMAQGIPAFMVELGggGRAEEEAVRFAARGLRNLLRYLGM 222
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
44-186 5.47e-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: 37.55  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893705440  44 PGPHVMINALTHGNELCGAIAVdALLAAGVRPA--RGQLT-LSFANVEAYErfdindpDATRF--IDE-DLNRVWSADKL 117
Cdd:cd06252   33 SGPTVLLTGGNHGDEYEGPIAL-RRLARDLDPEdvRGRLIiVPALNLPAVR-------AGTRTspLDGgNLNRAFPGDAD 104
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 893705440 118 DGPGNTLelrrARELRPVI-DTVDYLLDIHSMHEKAE--PLMLTGPLEKGVALGRQV------GAPSHLMIDAGHAAG 186
Cdd:cd06252  105 GTPTERI----AHFLETVLlPRADAVIDLHSGGSSLDfvPCAAVHLLPDPAQRARSLalaeafGAPLSVVVDNVDAPG 178
 
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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