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Conserved domains on  [gi|818897695|gb|KKW32011|]
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hypothetical protein UY76_C0045G0011 [Candidatus Uhrbacteria bacterium GW2011_GWA2_52_8d]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M14_like super family cl11393
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 2-109 1.12e-14

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.


The actual alignment was detected with superfamily member cd06909:

Pssm-ID: 472171  Cd Length: 190  Bit Score: 71.09  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   2 VVFGGTHGDETMGMEVVKVLLgvfgihdvwgsatQESELIQG---DLYLGIGNPEAVKRGTRSVSgvRDLNRCFHEAFFE 78
Cdd:cd06909    4 AIVGGTHGNELTGVYLVKHWL-------------KNPELIERksfEVHPLLANPRAVEQCRRYID--TDLNRCFSLENLS 68

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 818897695  79 SPEALALPDQQRAAELKDLLA-----RADYFFDLHS 109
Cdd:cd06909   69 SAPSSLPYEVRRAREINQILGpkgnpACDFIIDLHN 104
AstE_AspA super family cl29314
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 2-283 1.21e-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.).


The actual alignment was detected with superfamily member pfam04952:

Pssm-ID: 428216 [Multi-domain]  Cd Length: 289  Bit Score: 69.69  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695    2 VVFGGTHGDETMGMEVVKVLLGvfgihdVWGSATQESELIQgdlyLGIGNPEAVKRGTRSVSgvRDLNRCF-----HEAF 76
Cdd:pfam04952   6 LLSAGIHGNETNGVELLRRLLR------QLDPGDIAGERTL----VPLANPPAFRAGSRYIP--RDLNRSFpgralGASS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   77 FESPEALALpdQQRAAEL-KDLLARADYFFDLHSVSTKQTVPFVGVTTFSAAHREICRYIPVryivdvnsilgQDVGIPR 155
Cdd:pfam04952  74 DEPYRATRA--ERLADLFfPALLPRADIVLDLHTGTRGMGHLLFALAPIRDDPLHLLALLRA-----------FGAPAVL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695  156 KMVEQTPTTCSW--VNRHGGVGLCYEMG-----YQNDIAsvpYALCVVVHLLEHVGVVDErfhqifsfssdQNFIVSEQQ 228
Cdd:pfam04952 141 KLHSKPSAGFSAfsAEELGAPGFTLELGgagpfGANLIS---RTAAGVLNVLRLIGVLNG-----------GPDAFEPPK 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818897695  229 VYRlvHCERNKFKNFHYADSRYTTSFL-----PVKTGELIGTYQ-------DKEEVRAYADGLLVFP 283
Cdd:pfam04952 207 LYR--VLREIDRPRDIRAELAGLVEFAlnlgdDVDAGPLLPGGPlfapfggEETEYRAPEDGYPVFP 271
 
Name Accession Description Interval E-value
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 2-109 1.12e-14

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: 71.09  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   2 VVFGGTHGDETMGMEVVKVLLgvfgihdvwgsatQESELIQG---DLYLGIGNPEAVKRGTRSVSgvRDLNRCFHEAFFE 78
Cdd:cd06909    4 AIVGGTHGNELTGVYLVKHWL-------------KNPELIERksfEVHPLLANPRAVEQCRRYID--TDLNRCFSLENLS 68

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 818897695  79 SPEALALPDQQRAAELKDLLA-----RADYFFDLHS 109
Cdd:cd06909   69 SAPSSLPYEVRRAREINQILGpkgnpACDFIIDLHN 104
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 2-283 1.21e-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: 69.69  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695    2 VVFGGTHGDETMGMEVVKVLLGvfgihdVWGSATQESELIQgdlyLGIGNPEAVKRGTRSVSgvRDLNRCF-----HEAF 76
Cdd:pfam04952   6 LLSAGIHGNETNGVELLRRLLR------QLDPGDIAGERTL----VPLANPPAFRAGSRYIP--RDLNRSFpgralGASS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   77 FESPEALALpdQQRAAEL-KDLLARADYFFDLHSVSTKQTVPFVGVTTFSAAHREICRYIPVryivdvnsilgQDVGIPR 155
Cdd:pfam04952  74 DEPYRATRA--ERLADLFfPALLPRADIVLDLHTGTRGMGHLLFALAPIRDDPLHLLALLRA-----------FGAPAVL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695  156 KMVEQTPTTCSW--VNRHGGVGLCYEMG-----YQNDIAsvpYALCVVVHLLEHVGVVDErfhqifsfssdQNFIVSEQQ 228
Cdd:pfam04952 141 KLHSKPSAGFSAfsAEELGAPGFTLELGgagpfGANLIS---RTAAGVLNVLRLIGVLNG-----------GPDAFEPPK 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818897695  229 VYRlvHCERNKFKNFHYADSRYTTSFL-----PVKTGELIGTYQ-------DKEEVRAYADGLLVFP 283
Cdd:pfam04952 207 LYR--VLREIDRPRDIRAELAGLVEFAlnlgdDVDAGPLLPGGPlfapfggEETEYRAPEDGYPVFP 271
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
1-109 1.49e-13

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 69.49  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   1 MVVFGGTHGDETMGMEVVKVLLgvfgihdvwgsatqeSELIQGDLYLG------IGNPEAVKRGTRSVSgvRDLNRCF-- 72
Cdd:COG2988   27 VVISGGIHGNETAPIELLDKLL---------------QDLLLGERPLSfrllliLGNPAAMRAGRRYLD--EDLNRLFgg 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 818897695  73 -HEAFFESPEalalpdQQRAAELKDLLA-------RADYFFDLHS 109
Cdd:COG2988   90 rHLQNPESYE------AARAKELEQAVGpffaaggRVRLHIDLHT 128
COG3608 COG3608
Predicted deacylase [General function prediction only];
1-299 1.95e-13

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 69.11  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   1 MVVFGGTHGDETMGMEVVKVLLgvfgihdvwgsATQESELIQGDLYL-GIGNPEAVKRGTR-SVSGVRDLNRCFHEAFFE 78
Cdd:COG3608   29 LLITAGIHGDELNGIEALRRLL-----------RELDPGELRGTVILvPVANPPGFLQGSRyLPIDGRDLNRSFPGDADG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695  79 SPEalalpdQQRAAEL-KDLLARADYFFDLHSVSTKQT-VPFVGVTTFSAAHREICRYIPVRYIVDvnsilgQDVGIPRK 156
Cdd:COG3608   98 SLA------ERIAHALfEEILPDADYVIDLHSGGIARDnLPHVRAGPGDEELRALARAFGAPVILD------SPEGGDGS 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695 157 MVEQTpttcswvNRHGGVGLCYEMGYQNDI--ASVPYALCVVVHLLEHVGVVDERFHQifsfSSDQNFIVSEQQVYrlvh 234
Cdd:COG3608  166 LREAA-------AEAGIPALTLELGGGGRFdeESIEAGVRGILNVLRHLGMLDGEAPP----PPLAPPVLARGSEW---- 230

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818897695 235 cernkfknfHYADS-----RYTTSFLPVKTGELIGTYQD-----KEEVRAYADGLLVFPSGPQTLRDNKSLFYLA 299
Cdd:COG3608  231 ---------VRAPAgglfePLVELGDRVKKGDVLGRITDpfgeeVEEVRAPVDGIVIGRRTNPLVNPGDALFHIA 296
PRK02259 PRK02259
aspartoacylase; Provisional
 2-109 4.92e-11

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 62.20  E-value: 4.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   2 VVFGGTHGDETMGMEVVKVLLgvfgihdvwgsatQESELIQGD----LYLgIGNPEAVKRGTRSVSgvRDLNRCFHEAFF 77
Cdd:PRK02259   6 AIVGGTHGNEITGIYLVKKWQ-------------QQPNLINRKglevQTV-IGNPEAIEAGRRYID--RDLNRSFRLDLL 69

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 818897695  78 ESPEALALpDQQRAAELKDLL-----ARADYFFDLHS 109
Cdd:PRK02259  70 QNPDLSGY-EQLRAKELVQQLgpkgnSPCDFIIDLHS 105
 
Name Accession Description Interval E-value
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 2-109 1.12e-14

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: 71.09  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   2 VVFGGTHGDETMGMEVVKVLLgvfgihdvwgsatQESELIQG---DLYLGIGNPEAVKRGTRSVSgvRDLNRCFHEAFFE 78
Cdd:cd06909    4 AIVGGTHGNELTGVYLVKHWL-------------KNPELIERksfEVHPLLANPRAVEQCRRYID--TDLNRCFSLENLS 68

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 818897695  79 SPEALALPDQQRAAELKDLLA-----RADYFFDLHS 109
Cdd:cd06909   69 SAPSSLPYEVRRAREINQILGpkgnpACDFIIDLHN 104
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 2-283 1.21e-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: 69.69  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695    2 VVFGGTHGDETMGMEVVKVLLGvfgihdVWGSATQESELIQgdlyLGIGNPEAVKRGTRSVSgvRDLNRCF-----HEAF 76
Cdd:pfam04952   6 LLSAGIHGNETNGVELLRRLLR------QLDPGDIAGERTL----VPLANPPAFRAGSRYIP--RDLNRSFpgralGASS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   77 FESPEALALpdQQRAAEL-KDLLARADYFFDLHSVSTKQTVPFVGVTTFSAAHREICRYIPVryivdvnsilgQDVGIPR 155
Cdd:pfam04952  74 DEPYRATRA--ERLADLFfPALLPRADIVLDLHTGTRGMGHLLFALAPIRDDPLHLLALLRA-----------FGAPAVL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695  156 KMVEQTPTTCSW--VNRHGGVGLCYEMG-----YQNDIAsvpYALCVVVHLLEHVGVVDErfhqifsfssdQNFIVSEQQ 228
Cdd:pfam04952 141 KLHSKPSAGFSAfsAEELGAPGFTLELGgagpfGANLIS---RTAAGVLNVLRLIGVLNG-----------GPDAFEPPK 206

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818897695  229 VYRlvHCERNKFKNFHYADSRYTTSFL-----PVKTGELIGTYQ-------DKEEVRAYADGLLVFP 283
Cdd:pfam04952 207 LYR--VLREIDRPRDIRAELAGLVEFAlnlgdDVDAGPLLPGGPlfapfggEETEYRAPEDGYPVFP 271
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
1-109 1.49e-13

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 69.49  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   1 MVVFGGTHGDETMGMEVVKVLLgvfgihdvwgsatqeSELIQGDLYLG------IGNPEAVKRGTRSVSgvRDLNRCF-- 72
Cdd:COG2988   27 VVISGGIHGNETAPIELLDKLL---------------QDLLLGERPLSfrllliLGNPAAMRAGRRYLD--EDLNRLFgg 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 818897695  73 -HEAFFESPEalalpdQQRAAELKDLLA-------RADYFFDLHS 109
Cdd:COG2988   90 rHLQNPESYE------AARAKELEQAVGpffaaggRVRLHIDLHT 128
COG3608 COG3608
Predicted deacylase [General function prediction only];
1-299 1.95e-13

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 69.11  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   1 MVVFGGTHGDETMGMEVVKVLLgvfgihdvwgsATQESELIQGDLYL-GIGNPEAVKRGTR-SVSGVRDLNRCFHEAFFE 78
Cdd:COG3608   29 LLITAGIHGDELNGIEALRRLL-----------RELDPGELRGTVILvPVANPPGFLQGSRyLPIDGRDLNRSFPGDADG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695  79 SPEalalpdQQRAAEL-KDLLARADYFFDLHSVSTKQT-VPFVGVTTFSAAHREICRYIPVRYIVDvnsilgQDVGIPRK 156
Cdd:COG3608   98 SLA------ERIAHALfEEILPDADYVIDLHSGGIARDnLPHVRAGPGDEELRALARAFGAPVILD------SPEGGDGS 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695 157 MVEQTpttcswvNRHGGVGLCYEMGYQNDI--ASVPYALCVVVHLLEHVGVVDERFHQifsfSSDQNFIVSEQQVYrlvh 234
Cdd:COG3608  166 LREAA-------AEAGIPALTLELGGGGRFdeESIEAGVRGILNVLRHLGMLDGEAPP----PPLAPPVLARGSEW---- 230

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818897695 235 cernkfknfHYADS-----RYTTSFLPVKTGELIGTYQD-----KEEVRAYADGLLVFPSGPQTLRDNKSLFYLA 299
Cdd:COG3608  231 ---------VRAPAgglfePLVELGDRVKKGDVLGRITDpfgeeVEEVRAPVDGIVIGRRTNPLVNPGDALFHIA 296
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 2-119 1.55e-12

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: 64.64  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   2 VVFGGTHGDETMGMEVVKVLLgvfgihdvwgSATQESELiQGDLyLGI--GNPEAVKRGTR-SVSGVRDLNRCFheaffe 78
Cdd:cd06230    2 LILAGVHGDEYEGVEAIRRLL----------AELDPSEL-KGTV-VLVpvANPPAFEAGTRyTPLDGLDLNRIF------ 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 818897695  79 SPEALALPDQQRAAELKDLLAR-ADYFFDLHSVSTKQTVPFV 119
Cdd:cd06230   64 PGDPDGSPTERLAHELTELILKhADALIDLHSGGTGRLVPYA 105
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 3-198 3.54e-11

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: 60.54  E-value: 3.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   3 VFGGTHGDETMGMEVVKVLLgvfgihdvwgSATQESELIQGDLYLGIGNPEAVKRGTRSVSgvRDLNRCFheAFFESPEA 82
Cdd:cd18430    3 VLGAVHGNETCGTRAVERLL----------AELPSGALQKGPVTLVPANERAYAEGVRFCE--EDLNRVF--PGDPDPDT 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695  83 LalpDQQRAAELKDLLARADYFFDLHSVSTkQTVPFVGVTTFSAAHREICRYIpvryivdvnsilgqDVGIPRKMVEQTP 162
Cdd:cd18430   69 Y---ERRLANRLCPELEGHDVVLDLHSTHS-GGQPFAILDYGDKASRRLARSV--------------GIPKGWRVVYGRD 130

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 818897695 163 TTCSWVnrHG---GVGLCYEMGYQNDIASVPYALCVVVH 198
Cdd:cd18430  131 LGYAHG--GGkteVTGVTVECGYHDSEEAAEVAYRAILN 167
PRK02259 PRK02259
aspartoacylase; Provisional
 2-109 4.92e-11

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 62.20  E-value: 4.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   2 VVFGGTHGDETMGMEVVKVLLgvfgihdvwgsatQESELIQGD----LYLgIGNPEAVKRGTRSVSgvRDLNRCFHEAFF 77
Cdd:PRK02259   6 AIVGGTHGNEITGIYLVKKWQ-------------QQPNLINRKglevQTV-IGNPEAIEAGRRYID--RDLNRSFRLDLL 69

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 818897695  78 ESPEALALpDQQRAAELKDLL-----ARADYFFDLHS 109
Cdd:PRK02259  70 QNPDLSGY-EQLRAKELVQQLgpkgnSPCDFIIDLHS 105
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 6-109 5.84e-09

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: 55.67  E-value: 5.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   6 GTHGDETMGMEVVKVLLgvfgihdvwgsatqeSELIQGDLYLG------IGNPEAVKRGTRSVSGvrDLNRCF---HEAF 76
Cdd:cd03855   51 GIHGNETAPIEILDQLI---------------NDLIRGELALAhrllfiFGNPPAIRQGKRFIEE--NLNRLFsgrHSKL 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 818897695  77 FESPEAlalpdqQRAAELK----DLLARAD----YFFDLHS 109
Cdd:cd03855  114 PPSYET------ARAAELEqavaDFFAKASgevrWHLDLHT 148
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 6-108 2.50e-08

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 54.42  E-value: 2.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   6 GTHGDETMGMEVVKVLLgvfgihdvwgsatqeSELIQGDLYLG------IGNPEAVKRGTRSVSGvrDLNRCF---HEAF 76
Cdd:PRK05324  55 GIHGNETAPIELLDQLV---------------RDLLAGELPLRarllviLGNPPAMRAGKRYLDE--DLNRLFggrHQQF 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 818897695  77 FESPEALalpdqqRAAELKDLLARadyFF-----------DLH 108
Cdd:PRK05324 118 PGSDEAR------RAAELEQAVED---FFaagaervrwhyDLH 151
M14_ASTE_ASPA-like cd06910
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 7-113 3.58e-08

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: 52.74  E-value: 3.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   7 THGDETMGMEVVKVLLgvfgihdvwgsatqESEL--IQGDLYLGIGNPEAVKR-----GTRSVSGVRDLNRCFheaffeS 79
Cdd:cd06910   33 THGNEICGAIALDWLL--------------KNGVrpLRGRLTFCFANVEAYERfdparPTASRFVDEDLNRVW------G 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 818897695  80 PEALALPDQ----QRAAELKDLLARADYFFDLHSVSTK 113
Cdd:cd06910   93 PELLDGPEQsielRRARELRPVVDTVDYLLDIHSMQEK 130
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 2-206 4.10e-08

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: 52.96  E-value: 4.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   2 VVFGGTHGDETMGMEVVKVLLgvfgihdvwgsATQESELIQGDLY-LGIGNPEAVKRGTRsVSGV--RDLNRCFheaffe 78
Cdd:cd06252   38 LLTGGNHGDEYEGPIALRRLA-----------RDLDPEDVRGRLIiVPALNLPAVRAGTR-TSPLdgGNLNRAF------ 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695  79 SPEALALPDQQRAAELKD-LLARADYFFDLHSV-STKQTVPFVGVT-TFSAAHREIC----RYIPVRYIVDVNSILGqdv 151
Cdd:cd06252  100 PGDADGTPTERIAHFLETvLLPRADAVIDLHSGgSSLDFVPCAAVHlLPDPAQRARSlalaEAFGAPLSVVVDNVDA--- 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 818897695 152 giprkmveqTPTTCSWVNRHGGVGLCYEMGYQN--DIASVPYALCVVVHLLEHVGVV 206
Cdd:cd06252  177 ---------PGTLDSAAERAGKIFVSTELGGGGtvTPAALRIAERGVLNVLIHLGVL 224
M14_ASTE_ASPA-like cd06256
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 8-128 5.50e-07

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: 49.22  E-value: 5.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   8 HGDETMGMEVVKVLLgvfgihdvwgsaTQESELIQGDLYLGIGNPEAVKRGTRSVSGVRDLNRCFHEAfFESPEalalpd 87
Cdd:cd06256   44 HGNEPTGLRAVQRLL------------KTGQAPLPRTLLLFIGNVDAAKAGVRRLPGQPDYNRCWPGP-FETPE------ 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 818897695  88 QQRAAELKDLLARADYF--FDLHSvSTKQTVPFVGVTTFSAAH 128
Cdd:cd06256  105 GRLAAAVLERLDTLRPFasIDIHN-NTGKNPHYACVNRLDAAH 146
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
1-164 2.59e-05

Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 45.06  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   1 MVVFGGTHGDETMGMEVVKVLLGVFgihdvwgsATQESELIQG-----DLY----LgigNPEAVKRGTRSVS-GVrDLNR 70
Cdd:COG2866   68 VLLNAQQHGNEWTGTEALLGLLEDL--------LDNYDPLIRAlldnvTLYivpmL---NPDGAERNTRTNAnGV-DLNR 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695  71 CFHEAFFESPEALALpdqqrAAELKDLlaRADYFFDLHS--------VSTKQTVPFVGVTTFSAAHREICRYIPVRYIVD 142
Cdd:COG2866  136 DWPAPWLSEPETRAL-----RDLLDEH--DPDFVLDLHGqgelfywfVGTTEPTGSFLAPSYDEEREAFAEELNFEGIIL 208

                        170       180
                 ....*....|....*....|..
gi 818897695 143 VNSILGQDVGIPRKMVEQTPTT 164
Cdd:COG2866  209 AGSAFLGAGAAGTLLISAPRQT 230
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 2-154 1.35e-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: 349469 [Multi-domain]  Cd Length: 195  Bit Score: 42.14  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695   2 VVFGGTHGDETMGMEVVKVLLG----------VFGIHDVwgsatqeseliqgdlylgigNPEAVKRGTRSVS-GVRDLNR 70
Cdd:cd06251   16 LLTAAIHGDELNGIEVIQRLLEdldpsklrgtLIAIPVV--------------------NPLGFENNSRYLPdDGRDLNR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818897695  71 CFheaffespealalPD------QQRAAEL--KDLLARADYFFDLHSVSTKQT-VPFVGVTTFSAAHREICRYIPVRYIV 141
Cdd:cd06251   76 SF-------------PGsekgslASRLAHLlwNEIVKKADYVIDLHTASTGRTnLPYVRADLRDPESRRMAEAFGAPVIV 142

                        170
                 ....*....|....*....
gi 818897695 142 DVNSILG------QDVGIP 154
Cdd:cd06251  143 DDPGEDGslrgaaVELGIP 161
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
 3-72 2.20e-03

Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A (MpaA) and related proteins. MpaA is a member of the M14 family of metallocarboxypeptidases (MCPs), however it has an exceptional type of activity, it hydrolyzes the gamma-D-glutamyl-meso-diaminopimelic acid (gamma-D-Glu-Dap) bond in murein peptides. MpaA is specific for cleavage of the gamma-D-Glu-Dap bond of free murein tripeptide; it may also cleave murein tetrapeptide. MpaA has a different substrate specificity and cellular role than endopeptidase I, ENP1 (ENP1 does not belong to this group). MpaA works on free murein peptide in the recycling pathway.


Pssm-ID: 349475 [Multi-domain]  Cd Length: 214  Bit Score: 38.80  E-value: 2.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818897695   3 VFGGTHGDEtmgMEvvkvllGVFGIHDVWGSATQESELiqGDLYLGI---GNPEAVKRGTR-SVSGVrDLNRCF 72
Cdd:cd06904   28 IIGGIHGDE---PE------GVSLVEHLLRWLKNHPAS--GDFHIVVvpcLNPDGLAAGTRtNANGV-DLNRNF 89
 
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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