M14 family of metallocarboxypeptidases and related proteins; 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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304   10 IKKIAIFGGTHGNELTGVFLVTHWLRNGTEVHRAGLDVKPFITNPRAVEKCTRYIDCDLNRVFDLENLskEMSEDLPYEV 89
Cdd:PRK02259   2 INRVAIVGGTHGNEITGIYLVKKWQQQPNLINRKGLEVQTVIGNPEAIEAGRRYIDRDLNRSFRLDLL--QNPDLSGYEQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304   90 RRAQEINHLFGPKNSDDaYDIVFDLHNTTSNMGCTLILEDsRNDFLIQMFHYIKTCMaPLPcsVYLIEHPSLKYATTRSI 169
Cdd:PRK02259  80 LRAKELVQQLGPKGNSP-CDFIIDLHSTTANMGLSLILYG-RRPFDLALAAYLQSRL-PLP--IYLHEKDEDQTGFLVEL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304  170 AKYPVGIEVGPQPHGVLRADILDQMRKMIKHALDFIQHFNEGK-EFPPCSIDVYKIMEKVDYPRNESGDMAAVIHPNLQD 248
Cdd:PRK02259 155 WPCGLVIEVGPVPQGVLDAEIFEQTELLIESILDYLEKYNQGKlPLPNEQLVVYRHLGSIDYPRDENGQIAAMIHPQLQG 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19354304  249 QDWKPLHPGDPVFVSLDGKVIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTK 299
Cdd:PRK02259 235 RDWQPLKPGDPLFLTFDGKTIFYEGDSTVYPVFINEAAYYEKGIAMSLTKK 285

aspartoacylase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304   10 IKKIAIFGGTHGNELTGVFLVTHWLRNGTEVHRAGLDVKPFITNPRAVEKCTRYIDCDLNRVFDLENLskEMSEDLPYEV 89
Cdd:PRK02259   2 INRVAIVGGTHGNEITGIYLVKKWQQQPNLINRKGLEVQTVIGNPEAIEAGRRYIDRDLNRSFRLDLL--QNPDLSGYEQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304   90 RRAQEINHLFGPKNSDDaYDIVFDLHNTTSNMGCTLILEDsRNDFLIQMFHYIKTCMaPLPcsVYLIEHPSLKYATTRSI 169
Cdd:PRK02259  80 LRAKELVQQLGPKGNSP-CDFIIDLHSTTANMGLSLILYG-RRPFDLALAAYLQSRL-PLP--IYLHEKDEDQTGFLVEL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304  170 AKYPVGIEVGPQPHGVLRADILDQMRKMIKHALDFIQHFNEGK-EFPPCSIDVYKIMEKVDYPRNESGDMAAVIHPNLQD 248
Cdd:PRK02259 155 WPCGLVIEVGPVPQGVLDAEIFEQTELLIESILDYLEKYNQGKlPLPNEQLVVYRHLGSIDYPRDENGQIAAMIHPQLQG 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19354304  249 QDWKPLHPGDPVFVSLDGKVIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTK 299
Cdd:PRK02259 235 RDWQPLKPGDPLFLTFDGKTIFYEGDSTVYPVFINEAAYYEKGIAMSLTKK 285

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.).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304     9 PIKKIAIFGGTHGNELTGVFLVTHWLRNGTEVHRAGLDVKPFITNPRAVEKCTRYIDCDLNRVFDLENLSKemSEDLPYE 88
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALGA--SSDEPYR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304    89 VRRAQEINHLFGPKNSdDAYDIVFDLHNTTSNMGCTLILEDSRNDFLIQMFHYIKTCMAPLPCSVYLIEHPSLKYATTRS 168
Cdd:pfam04952  79 ATRAERLADLFFPALL-PRADIVLDLHTGTRGMGHLLFALAPIRDDPLHLLALLRAFGAPAVLKLHSKPSAGFSAFSAEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304   169 IAKYPVGIEVGPQphGVLRADILDQMRKMIKHALDFIQHFNEGKEFPPCSIdVYKIMEKVDYPRNESGDMAAVIHPNL-- 246
Cdd:pfam04952 158 LGAPGFTLELGGA--GPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPPK-LYRVLREIDRPRDIRAELAGLVEFALnl 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19354304   247 -QDQDWKPLHPGDPVFVSLDGKVIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTK 299
Cdd:pfam04952 235 gDDVDAGPLLPGGPLFAPFGGEETEYRAPEDGYPVFPNEAAYVGKGAALALVAK 288

aspartoacylase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304   10 IKKIAIFGGTHGNELTGVFLVTHWLRNGTEVHRAGLDVKPFITNPRAVEKCTRYIDCDLNRVFDLENLskEMSEDLPYEV 89
Cdd:PRK02259   2 INRVAIVGGTHGNEITGIYLVKKWQQQPNLINRKGLEVQTVIGNPEAIEAGRRYIDRDLNRSFRLDLL--QNPDLSGYEQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304   90 RRAQEINHLFGPKNSDDaYDIVFDLHNTTSNMGCTLILEDsRNDFLIQMFHYIKTCMaPLPcsVYLIEHPSLKYATTRSI 169
Cdd:PRK02259  80 LRAKELVQQLGPKGNSP-CDFIIDLHSTTANMGLSLILYG-RRPFDLALAAYLQSRL-PLP--IYLHEKDEDQTGFLVEL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304  170 AKYPVGIEVGPQPHGVLRADILDQMRKMIKHALDFIQHFNEGK-EFPPCSIDVYKIMEKVDYPRNESGDMAAVIHPNLQD 248
Cdd:PRK02259 155 WPCGLVIEVGPVPQGVLDAEIFEQTELLIESILDYLEKYNQGKlPLPNEQLVVYRHLGSIDYPRDENGQIAAMIHPQLQG 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 19354304  249 QDWKPLHPGDPVFVSLDGKVIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTK 299
Cdd:PRK02259 235 RDWQPLKPGDPLFLTFDGKTIFYEGDSTVYPVFINEAAYYEKGIAMSLTKK 285

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.).

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304     9 PIKKIAIFGGTHGNELTGVFLVTHWLRNGTEVHRAGLDVKPFITNPRAVEKCTRYIDCDLNRVFDLENLSKemSEDLPYE 88
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALGA--SSDEPYR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304    89 VRRAQEINHLFGPKNSdDAYDIVFDLHNTTSNMGCTLILEDSRNDFLIQMFHYIKTCMAPLPCSVYLIEHPSLKYATTRS 168
Cdd:pfam04952  79 ATRAERLADLFFPALL-PRADIVLDLHTGTRGMGHLLFALAPIRDDPLHLLALLRAFGAPAVLKLHSKPSAGFSAFSAEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304   169 IAKYPVGIEVGPQphGVLRADILDQMRKMIKHALDFIQHFNEGKEFPPCSIdVYKIMEKVDYPRNESGDMAAVIHPNL-- 246
Cdd:pfam04952 158 LGAPGFTLELGGA--GPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPPK-LYRVLREIDRPRDIRAELAGLVEFALnl 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19354304   247 -QDQDWKPLHPGDPVFVSLDGKVIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTK 299
Cdd:pfam04952 235 gDDVDAGPLLPGGPLFAPFGGEETEYRAPEDGYPVFPNEAAYVGKGAALALVAK 288

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304  13 IAIFGGTHGNELTGVFLVTHWLRNGTEVHRAG-LDVKPfITNPRAVEKCTRYID---CDLNRVFDLenlskemSEDLPYE 88
Cdd:cd06230   1 LLILAGVHGDEYEGVEAIRRLLAELDPSELKGtVVLVP-VANPPAFEAGTRYTPldgLDLNRIFPG-------DPDGSPT 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304  89 VRRAQEINHLFGPKnsddaYDIVFDLHNTTSNM-GCTLILEDSR--NDFLIQMFHYIKtcmaplPCSVYLIEHP--SLKY 163
Cdd:cd06230  73 ERLAHELTELILKH-----ADALIDLHSGGTGRlVPYAILDYDSdaREKSRELARAFG------GTPVIWGGDPpgGTPV 141

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19354304 164 ATTRSIAKYPVGIEVGpqPHGVLRADILDQMRKMIKH 200
Cdd:cd06230 142 AAARSAGIPAITVELG--GGGRLRAERLERYLRGIRN 176

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304  15 IFGGTHGNELTGVFLVTHWLRNGTEVHRAGLDVKpfITNPRAVEK-------CTRYIDCDLNRVFDLENLSkemSEDLPY 87
Cdd:cd06910  29 INALTHGNEICGAIALDWLLKNGVRPLRGRLTFC--FANVEAYERfdparptASRFVDEDLNRVWGPELLD---GPEQSI 103

                        90       100       110
                ....*....|....*....|....*....|.
gi 19354304  88 EVRRAQEINHLFgpknsdDAYDIVFDLHNTT 118
Cdd:cd06910 104 ELRRARELRPVV------DTVDYLLDIHSMQ 128

Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family includes Francisella tularensis protein rapid encystment phenotype 34 (REP34) which is a zinc-containing monomeric protein demonstrating carboxypeptidase B-like activity. REP34 possesses a novel topology with its substrate binding pocket deviating from the canonical M14 peptidases with a possible catalytic role for a conserved tyrosine and distinct S1' recognition site. Thus, REP34, identified as an active carboxypeptidase and a potential key F. tularensis effector protein, may help elucidate a mechanistic understanding of F. tularensis infection of phagocytic cells. A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family 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 cleavages. 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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304  11 KKIAIFGGTHGNELTGVFLVTHWLRNGTE--VHRAGLDVKPFItNPRAVEKCTRYIDC--DLNRVFDLENLSKEmsedlp 86
Cdd:cd06231  43 PRVLISAGIHGDEPAGVEALLRFLESLAEkyLRRVNLLVLPCV-NPWGFERNTRENADgiDLNRSFLKDSPSPE------ 115

                        90       100       110
                ....*....|....*....|....*....|..
gi 19354304  87 yevRRAQeINHLFgpknSDDAYDIVFDLHNTT 118
Cdd:cd06231 116 ---VRAL-MEFLA----SLGRFDLHLDLHEDW 139

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304   7 KEPIKKIAIFGGTHGNE----LTGVFLVTHWLRNGTevhragLDVKPFItNPRAVEKCTRYIDCDLNRVFDLENLSKems 82
Cdd:cd06243  13 REPGPTLLIIGGIQGDEpggfLAADLLADLYLVKGN------VIVVPRL-NFPSILRNHRGLNGDMNRKFAALDKKD--- 82

                        90       100       110
                ....*....|....*....|....*....|...
gi 19354304  83 edlpYEVRRAQEINHLFGPKNSddayDIVFDLH 115
Cdd:cd06243  83 ----PEYKTIQEIKSLIADFRP----DVVLHLH 107

Predicted deacylase [General function prediction only];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19354304   7 KEPIKKIAIFGGTHGNELTGVFLVTHWLRNGTEVHRAG-LDVKPFItNPRAVEKCTRY--IDC-DLNRVF-DLENLSkem 81
Cdd:COG3608  23 AGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELRGtVILVPVA-NPPGFLQGSRYlpIDGrDLNRSFpGDADGS--- 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19354304  82 sedlpYEVRRAQEINHLFGPKnsddaYDIVFDLHNTTSNM 121
Cdd:COG3608  99 -----LAERIAHALFEEILPD-----ADYVIDLHSGGIAR 128

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.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19354304   7 KEPIKKIAIFGGTHGNELTGVFLVTHWLRNGTEVHRAGLDVKPFITNPRAVEKCTRYI---DCDLNRVF 72
Cdd:cd06251   9 AKPGPTLLLTAAIHGDELNGIEVIQRLLEDLDPSKLRGTLIAIPVVNPLGFENNSRYLpddGRDLNRSF 77