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Conserved domains on  [gi|1210258420|dbj|BAZ77422|]
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succinylglutamate desuccinylase/aspartoacylase [Aulosira laxa NIES-50]

Protein Classification

aspartoacylase( domain architecture ID 10011780)

aspartoacylase catalyzes the hydrolysis of N-acetyl-l-aspartate to aspartate and acetate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK02259 PRK02259
aspartoacylase; Provisional
 3-291 8.56e-161

aspartoacylase; Provisional


:

Pssm-ID: 235019  Cd Length: 288  Bit Score: 449.33  E-value: 8.56e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   3 QIKRVVIVGGTHGNELTGIYLVKKFERSPDLIQRSSFETLTLIANPKAYAIGRRYTDTDLNRCFLPRDLENPHLSSYEAQ 82
Cdd:PRK02259    1 KINRVAIVGGTHGNEITGIYLVKKWQQQPNLINRKGLEVQTVIGNPEAIEAGRRYIDRDLNRSFRLDLLQNPDLSGYEQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420  83 RAKVIYQTFGFAGSQQADFVIDLHSSTANMGLSIILGNENLLNIQLAAYLASINPKVRVLYstTKNQERSH-LDSICQFG 161
Cdd:PRK02259   81 RAKELVQQLGPKGNSPCDFIIDLHSTTANMGLSLILYGRRPFDLALAAYLQSRLPLPIYLH--EKDEDQTGfLVELWPCG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420 162 CTLEVGAVAQGVLDAALFEETEAIIHAILDYLADHNQAKAPLINDTLTAYHNLGTIDYPRNELGEIQAMIHPRLQFRDYQ 241
Cdd:PRK02259  159 LVIEVGPVPQGVLDAEIFEQTELLIESILDYLEKYNQGKLPLPNEQLVVYRHLGSIDYPRDENGQIAAMIHPQLQGRDWQ 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1210258420 242 PLHPGEPIFLTFDGQEIPYEGDSIVYPVFINEAAYYEKGIAMCITEKREL 291
Cdd:PRK02259  239 PLKPGDPLFLTFDGKTIFYEGDSTVYPVFINEAAYYEKGIAMSLTKKEVI 288
 
Name Accession Description Interval E-value
PRK02259 PRK02259
aspartoacylase; Provisional
 3-291 8.56e-161

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 449.33  E-value: 8.56e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   3 QIKRVVIVGGTHGNELTGIYLVKKFERSPDLIQRSSFETLTLIANPKAYAIGRRYTDTDLNRCFLPRDLENPHLSSYEAQ 82
Cdd:PRK02259    1 KINRVAIVGGTHGNEITGIYLVKKWQQQPNLINRKGLEVQTVIGNPEAIEAGRRYIDRDLNRSFRLDLLQNPDLSGYEQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420  83 RAKVIYQTFGFAGSQQADFVIDLHSSTANMGLSIILGNENLLNIQLAAYLASINPKVRVLYstTKNQERSH-LDSICQFG 161
Cdd:PRK02259   81 RAKELVQQLGPKGNSPCDFIIDLHSTTANMGLSLILYGRRPFDLALAAYLQSRLPLPIYLH--EKDEDQTGfLVELWPCG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420 162 CTLEVGAVAQGVLDAALFEETEAIIHAILDYLADHNQAKAPLINDTLTAYHNLGTIDYPRNELGEIQAMIHPRLQFRDYQ 241
Cdd:PRK02259  159 LVIEVGPVPQGVLDAEIFEQTELLIESILDYLEKYNQGKLPLPNEQLVVYRHLGSIDYPRDENGQIAAMIHPQLQGRDWQ 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1210258420 242 PLHPGEPIFLTFDGQEIPYEGDSIVYPVFINEAAYYEKGIAMCITEKREL 291
Cdd:PRK02259  239 PLKPGDPLFLTFDGKTIFYEGDSTVYPVFINEAAYYEKGIAMSLTKKEVI 288
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
4-289 9.51e-96

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 285.20  E-value: 9.51e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   4 IKRVVIVGGTHGNELTGIYLVKKFERSPDLIQRS-SFETLTLIANPKAYAIGRRYTDTDLNRCFLPRDLENPhlSSYEAQ 82
Cdd:COG2988    24 IKAVVISGGIHGNETAPIELLDKLLQDLLLGERPlSFRLLLILGNPAAMRAGRRYLDEDLNRLFGGRHLQNP--ESYEAA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420  83 RAKVIYQTFG--FAGSQQADFVIDLHSSTANMGLSIIL---GNENLLNIQLAAYLASINPKVRVLYSTTKNQERSHLDSI 157
Cdd:COG2988   102 RAKELEQAVGpfFAAGGRVRLHIDLHTAIRNSGHERFAvypFRGRPFDLALLAYLAAAGPEAVVLHHAPGGTFSHFSAEL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420 158 CQF-GCTLEVGAV-AQGVLDAALFEETEAIIHAILDYLADHNQAKAPlindtLTAYHNLGTIDyprnELGeIQAMIHPRL 235
Cdd:COG2988   182 CGAqAFTLELGKVrPFGQNDLSRFAATEEALRALLSGAELPEHPAQD-----LDLYRVVQQII----KHG-DDFMLHPDL 251

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1210258420 236 QFRDYQPLHPGEPIFLTfDGQEIPYEGDsIVYPVFINEAAYYEKGIAMCITEKR 289
Cdd:COG2988   252 DTLNFTPLPPGTLLAED-GGKEYRVEGD-EERIVFPNEAVYYGQRAALLLTPKE 303
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 5-193 1.17e-91

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: 270.62  E-value: 1.17e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   5 KRVVIVGGTHGNELTGIYLVKKFERSPDLIQRSSFETLTLIANPKAYAIGRRYTDTDLNRCFLPRDLEN-PHLSSYEAQR 83
Cdd:cd06909     1 KRVAIVGGTHGNELTGVYLVKHWLKNPELIERKSFEVHPLLANPRAVEQCRRYIDTDLNRCFSLENLSSaPSSLPYEVRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420  84 AKVIYQTFGFAGSQQADFVIDLHSSTANMGLSIILGNENLLNIQLAAYLASINPKVRVLYSTTKNQERSHLDSICQFGCT 163
Cdd:cd06909    81 AREINQILGPKGNPACDFIIDLHNTTSNMGITLILSSSDDFTLKLAAYLQQRLPPVRVLLHESPSKESPFLRSVAKHGFT 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1210258420 164 LEVGAVAQGVLDAALFEETEAIIHAILDYL 193
Cdd:cd06909   161 IEVGPVPQGVLRADIFEQTRKLVKAILDFI 190
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 4-289 1.19e-78

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: 241.10  E-value: 1.19e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   4 IKRVVIVGGTHGNELTGIYLVKKFERSPDLIQRSSFETLTLIANPKAYAIGRRYTDTDLNRCFLPRDLENPHLSSYEAQR 83
Cdd:pfam04952   2 GPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALGASSDEPYRATR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420  84 AKVIYQTFGFAGSQQADFVIDLHSSTANMG-LSIILGNENLLNIQLAAYLASINPKVRVLYSTTKN--QERSHLDSICQF 160
Cdd:pfam04952  82 AERLADLFFPALLPRADIVLDLHTGTRGMGhLLFALAPIRDDPLHLLALLRAFGAPAVLKLHSKPSagFSAFSAEELGAP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420 161 GCTLEVGavAQGVLDAALFEETEAIIHAILDYLADHNQakAPLINDTLTAYHNLGTIDYPRNELGEIQAMIHPRL---QF 237
Cdd:pfam04952 162 GFTLELG--GAGPFGANLISRTAAGVLNVLRLIGVLNG--GPDAFEPPKLYRVLREIDRPRDIRAELAGLVEFALnlgDD 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1210258420 238 RDYQPLHPGEPIFLTFDGQEIPYEGDSIVYPVFINEAAYYEKGIAMCITEKR 289
Cdd:pfam04952 238 VDAGPLLPGGPLFAPFGGEETEYRAPEDGYPVFPNEAAYVGKGAALALVAKF 289
 
Name Accession Description Interval E-value
PRK02259 PRK02259
aspartoacylase; Provisional
 3-291 8.56e-161

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 449.33  E-value: 8.56e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   3 QIKRVVIVGGTHGNELTGIYLVKKFERSPDLIQRSSFETLTLIANPKAYAIGRRYTDTDLNRCFLPRDLENPHLSSYEAQ 82
Cdd:PRK02259    1 KINRVAIVGGTHGNEITGIYLVKKWQQQPNLINRKGLEVQTVIGNPEAIEAGRRYIDRDLNRSFRLDLLQNPDLSGYEQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420  83 RAKVIYQTFGFAGSQQADFVIDLHSSTANMGLSIILGNENLLNIQLAAYLASINPKVRVLYstTKNQERSH-LDSICQFG 161
Cdd:PRK02259   81 RAKELVQQLGPKGNSPCDFIIDLHSTTANMGLSLILYGRRPFDLALAAYLQSRLPLPIYLH--EKDEDQTGfLVELWPCG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420 162 CTLEVGAVAQGVLDAALFEETEAIIHAILDYLADHNQAKAPLINDTLTAYHNLGTIDYPRNELGEIQAMIHPRLQFRDYQ 241
Cdd:PRK02259  159 LVIEVGPVPQGVLDAEIFEQTELLIESILDYLEKYNQGKLPLPNEQLVVYRHLGSIDYPRDENGQIAAMIHPQLQGRDWQ 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1210258420 242 PLHPGEPIFLTFDGQEIPYEGDSIVYPVFINEAAYYEKGIAMCITEKREL 291
Cdd:PRK02259  239 PLKPGDPLFLTFDGKTIFYEGDSTVYPVFINEAAYYEKGIAMSLTKKEVI 288
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
4-289 9.51e-96

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 285.20  E-value: 9.51e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   4 IKRVVIVGGTHGNELTGIYLVKKFERSPDLIQRS-SFETLTLIANPKAYAIGRRYTDTDLNRCFLPRDLENPhlSSYEAQ 82
Cdd:COG2988    24 IKAVVISGGIHGNETAPIELLDKLLQDLLLGERPlSFRLLLILGNPAAMRAGRRYLDEDLNRLFGGRHLQNP--ESYEAA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420  83 RAKVIYQTFG--FAGSQQADFVIDLHSSTANMGLSIIL---GNENLLNIQLAAYLASINPKVRVLYSTTKNQERSHLDSI 157
Cdd:COG2988   102 RAKELEQAVGpfFAAGGRVRLHIDLHTAIRNSGHERFAvypFRGRPFDLALLAYLAAAGPEAVVLHHAPGGTFSHFSAEL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420 158 CQF-GCTLEVGAV-AQGVLDAALFEETEAIIHAILDYLADHNQAKAPlindtLTAYHNLGTIDyprnELGeIQAMIHPRL 235
Cdd:COG2988   182 CGAqAFTLELGKVrPFGQNDLSRFAATEEALRALLSGAELPEHPAQD-----LDLYRVVQQII----KHG-DDFMLHPDL 251

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1210258420 236 QFRDYQPLHPGEPIFLTfDGQEIPYEGDsIVYPVFINEAAYYEKGIAMCITEKR 289
Cdd:COG2988   252 DTLNFTPLPPGTLLAED-GGKEYRVEGD-EERIVFPNEAVYYGQRAALLLTPKE 303
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 5-193 1.17e-91

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: 270.62  E-value: 1.17e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   5 KRVVIVGGTHGNELTGIYLVKKFERSPDLIQRSSFETLTLIANPKAYAIGRRYTDTDLNRCFLPRDLEN-PHLSSYEAQR 83
Cdd:cd06909     1 KRVAIVGGTHGNELTGVYLVKHWLKNPELIERKSFEVHPLLANPRAVEQCRRYIDTDLNRCFSLENLSSaPSSLPYEVRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420  84 AKVIYQTFGFAGSQQADFVIDLHSSTANMGLSIILGNENLLNIQLAAYLASINPKVRVLYSTTKNQERSHLDSICQFGCT 163
Cdd:cd06909    81 AREINQILGPKGNPACDFIIDLHNTTSNMGITLILSSSDDFTLKLAAYLQQRLPPVRVLLHESPSKESPFLRSVAKHGFT 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1210258420 164 LEVGAVAQGVLDAALFEETEAIIHAILDYL 193
Cdd:cd06909   161 IEVGPVPQGVLRADIFEQTRKLVKAILDFI 190
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 4-289 1.19e-78

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: 241.10  E-value: 1.19e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   4 IKRVVIVGGTHGNELTGIYLVKKFERSPDLIQRSSFETLTLIANPKAYAIGRRYTDTDLNRCFLPRDLENPHLSSYEAQR 83
Cdd:pfam04952   2 GPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALGASSDEPYRATR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420  84 AKVIYQTFGFAGSQQADFVIDLHSSTANMG-LSIILGNENLLNIQLAAYLASINPKVRVLYSTTKN--QERSHLDSICQF 160
Cdd:pfam04952  82 AERLADLFFPALLPRADIVLDLHTGTRGMGhLLFALAPIRDDPLHLLALLRAFGAPAVLKLHSKPSagFSAFSAEELGAP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420 161 GCTLEVGavAQGVLDAALFEETEAIIHAILDYLADHNQakAPLINDTLTAYHNLGTIDYPRNELGEIQAMIHPRL---QF 237
Cdd:pfam04952 162 GFTLELG--GAGPFGANLISRTAAGVLNVLRLIGVLNG--GPDAFEPPKLYRVLREIDRPRDIRAELAGLVEFALnlgDD 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1210258420 238 RDYQPLHPGEPIFLTFDGQEIPYEGDSIVYPVFINEAAYYEKGIAMCITEKR 289
Cdd:pfam04952 238 VDAGPLLPGGPLFAPFGGEETEYRAPEDGYPVFPNEAAYVGKGAALALVAKF 289
COG3608 COG3608
Predicted deacylase [General function prediction only];
5-194 8.06e-17

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 79.12  E-value: 8.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   5 KRVVIVGGTHGNELTGIYLVKKFERSPDLIQRSSfeTLTL--IANPKAYAIGRRYT---DTDLNRCFlPRDLEnphlSSY 79
Cdd:COG3608    27 PTLLITAGIHGDELNGIEALRRLLRELDPGELRG--TVILvpVANPPGFLQGSRYLpidGRDLNRSF-PGDAD----GSL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420  80 EAQRAKVIYQTFgfagSQQADFVIDLHSSTANMGLS--IILGNENLLNIQLAAYLAsinpkVRVLYSTTKNQERShLDSI 157
Cdd:COG3608   100 AERIAHALFEEI----LPDADYVIDLHSGGIARDNLphVRAGPGDEELRALARAFG-----APVILDSPEGGDGS-LREA 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1210258420 158 CQ-FGC---TLEVGavAQGVLDAalfEETEAIIHAILDYLA 194
Cdd:COG3608   170 AAeAGIpalTLELG--GGGRFDE---ESIEAGVRGILNVLR 205
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 7-112 1.55e-15

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: 73.11  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   7 VVIVGGTHGNELTGIYLVKKFERSPDLIQRSSFETLTLIANPKAYAIGRRYTD---TDLNRCFLPRdlenpHLSSYEAQR 83
Cdd:cd06230     1 LLILAGVHGDEYEGVEAIRRLLAELDPSELKGTVVLVPVANPPAFEAGTRYTPldgLDLNRIFPGD-----PDGSPTERL 75

                          90       100
                  ....*....|....*....|....*....
gi 1210258420  84 AKVIYQTFGfagsQQADFVIDLHSSTANM 112
Cdd:cd06230    76 AHELTELIL----KHADALIDLHSGGTGR 100
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 7-167 3.09e-14

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: 69.40  E-value: 3.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   7 VVIVGGTHGNELTGIYLVKKF--ERSPDLIQRSSfetLTLI-ANPKAYAIGRRYTDTDLNRCFlPRDlenPHLSSYEAQR 83
Cdd:cd18430     1 LAVLGAVHGNETCGTRAVERLlaELPSGALQKGP---VTLVpANERAYAEGVRFCEEDLNRVF-PGD---PDPDTYERRL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420  84 AKVIYQTFgfagsQQADFVIDLHSSTANMGLSIILGNENLLNIQLAAYLASINPKvRVLYSTTKNQERSHL-DSIcqFGC 162
Cdd:cd18430    74 ANRLCPEL-----EGHDVVLDLHSTHSGGQPFAILDYGDKASRRLARSVGIPKGW-RVVYGRDLGYAHGGGkTEV--TGV 145


                  ....*
gi 1210258420 163 TLEVG 167
Cdd:cd18430   146 TVECG 150
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 5-108 3.40e-12

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: 349471  Cd Length: 211  Bit Score: 64.54  E-value: 3.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   5 KRVVIVGGTHGNELTGIY----LVKKFERSPDliQRSSFETLTLI---ANPKAYAIGRRYT---DTDLNRCFlPRDLENP 74
Cdd:cd06253    23 PRIAIVAGIHGDELNGLYvcsrLIRFLKELEE--GGYKLKGKVLVipaVNPLGINSGTRFWpfdNLDMNRMF-PGYNKGE 99

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1210258420  75 hlssyEAQR-AKVIYQTFgfagsQQADFVIDLHSS 108
Cdd:cd06253   100 -----TTERiAAALFEDL-----KGADYGIDLHSS 124
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 5-108 5.49e-11

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: 61.45  E-value: 5.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   5 KRVVIVGGTHGNELTGI----YLVKKFERSP-DLIQRssfeTLTLIANPKAYAIGRRYTDTDLNRCFLPRdlENPHLSSY 79
Cdd:cd03855    44 KSVVLSAGIHGNETAPIeildQLINDLIRGElALAHR----LLFIFGNPPAIRQGKRFIEENLNRLFSGR--HSKLPPSY 117

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1210258420  80 EAQRAKVIYQT---FgFAGSQQADFV-IDLHSS 108
Cdd:cd03855   118 ETARAAELEQAvadF-FAKASGEVRWhLDLHTA 149
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 5-111 5.68e-10

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: 57.94  E-value: 5.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   5 KRVVIVGGTHGNELTGIYLVKKFERSPDLIQRSSfetlTLIA----NPKAYAIGRRYT---DTDLNRCFlPRDlENPHLS 77
Cdd:cd06251    13 PTLLLTAAIHGDELNGIEVIQRLLEDLDPSKLRG----TLIAipvvNPLGFENNSRYLpddGRDLNRSF-PGS-EKGSLA 86

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1210258420  78 SYEAQRakvIYQTFgfagSQQADFVIDLHSSTAN 111
Cdd:cd06251    87 SRLAHL---LWNEI----VKKADYVIDLHTASTG 113
M14_ASTE_ASPA-like cd06910
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 6-110 6.88e-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: 51.97  E-value: 6.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   6 RVVIVGGTHGNELTGIYLVKKFERSPdliQRSSFETLTLI-ANPKAYA-------IGRRYTDTDLNRCFLPrDLENPHLS 77
Cdd:cd06910    26 HVMINALTHGNEICGAIALDWLLKNG---VRPLRGRLTFCfANVEAYErfdparpTASRFVDEDLNRVWGP-ELLDGPEQ 101

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1210258420  78 SYEAQRAKVIYQTFgfagsQQADFVIDLHSSTA 110
Cdd:cd06910   102 SIELRRARELRPVV-----DTVDYLLDIHSMQE 129
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 5-110 4.10e-07

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 50.57  E-value: 4.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   5 KRVVIVGGTHGNELTGIYLVKkferspDLIQRSSFETLTL-------IANPKAYAIGRRYTDTDLNRCFLPRDLENPHls 77
Cdd:PRK05324   48 KALVLSAGIHGNETAPIELLD------QLVRDLLAGELPLrarllviLGNPPAMRAGKRYLDEDLNRLFGGRHQQFPG-- 119

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1210258420  78 SYEAQRAKVIYQ---TFgFAGSQQAD-FVIDLHssTA 110
Cdd:PRK05324  120 SDEARRAAELEQaveDF-FAAGAERVrWHYDLH--TA 153
M14-like cd06242
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
 5-126 2.58e-06

Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of 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.


Pssm-ID: 349461 [Multi-domain]  Cd Length: 220  Bit Score: 47.68  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   5 KRVVIVGGTHGNELTG----IYLVKKFERSPDLiqRSSFETLTLI----ANPKAYAIGRRYT--DTDLNRCFLPrdlenp 74
Cdd:cd06242     2 PTVLLVGQQHGNEPAGreaaLALARDLAFGDDA--RELLEKVNVLvvprANPDGRAANTRGNanGVDLNRDHLL------ 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1210258420  75 hLSSYEAQRAKVIYQTFgfagsqQADFVIDLHSSTANMG------LSIILGNENLLNI 126
Cdd:cd06242    74 -LSTPETRALARVLRDY------RPEVVIDAHEFGGVTGdftlarYDVLWPRATNLNI 124
M14_ASTE_ASPA-like cd06255
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 9-108 3.25e-06

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


Pssm-ID: 349473  Cd Length: 223  Bit Score: 47.32  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   9 IVGGTHGNELTGIYLVKKFERSPDLIQRSSFETLTLIANPKAYAIGRRYT---DTDLNRCFlPRDLENPHlssyeAQR-A 84
Cdd:cd06255    28 INGAVHGDELNGPLAALELFRELDPAQLSGTLVATPIANPLAFQGRQKFSpqdGEDLDQSF-PGDPDGLI-----TERmA 101

                          90       100
                  ....*....|....*....|....
gi 1210258420  85 KVIYQTFgfagSQQADFVIDLHSS 108
Cdd:cd06255   102 HALFSEV----KEVADYLIDFHTG 121
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
 5-66 2.39e-05

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: 44.57  E-value: 2.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1210258420   5 KRVVIVGGTHGNELTGIYLVKKFERSpdLIQRSSFETLTLI----ANPKAYAIGRRYT--DTDLNRCF 66
Cdd:cd06904    24 ARILIIGGIHGDEPEGVSLVEHLLRW--LKNHPASGDFHIVvvpcLNPDGLAAGTRTNanGVDLNRNF 89
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 5-193 3.72e-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: 43.72  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   5 KRVVIVGGTHGNELTGIYLVKKFERSPDLIQRSSFETLTLIANPKAYAIGRRYTDTD----LNRCFlPrdlENPHLSSYE 80
Cdd:cd06254    12 PTLLITAGIHGGEYPGILAAIRLARELDPADVKGTLIIVHIANVSGFEARTPFVVPEdgknLNRVF-P---GDPDGTLTE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420  81 AQRAKVIYQTFGfagsqQADFVIDLHSSTANMGL-----SIILGNENLLNIQLAAYLAsINPKVRVLYSTTKNQ------ 149
Cdd:cd06254    88 RIAYFLTREIIS-----RADFLIDLHGGDANEALtpfvyYPGGASEEVNDISRAAAQA-LGLPYIVISSSEKGTgyysya 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1210258420 150 ERSHLDSIcqfgcTLEVGavAQGVLDAalfEETEAI---IHAILDYL 193
Cdd:cd06254   162 ALRGIPSI-----LVERG--GLGTCDE---EDVQAHkdgIKNLLRHL 198
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 7-107 1.84e-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: 349470  Cd Length: 224  Bit Score: 41.79  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   7 VVIVGGTHGNELTGIYLVKKferspdLIQRSSFETLT--LI----ANPKAYAIGRRYTDTD---LNRCFLPRdlenpHLS 77
Cdd:cd06252    37 VLLTGGNHGDEYEGPIALRR------LARDLDPEDVRgrLIivpaLNLPAVRAGTRTSPLDggnLNRAFPGD-----ADG 105

                          90       100       110
                  ....*....|....*....|....*....|
gi 1210258420  78 SYEAQRAKVIyQTFGFAgsqQADFVIDLHS 107
Cdd:cd06252   106 TPTERIAHFL-ETVLLP---RADAVIDLHS 131
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
 5-106 1.53e-03

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.


Pssm-ID: 349450 [Multi-domain]  Cd Length: 239  Bit Score: 39.21  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   5 KRVVIVGGTHGNELTGIYLVKKF--ERSPDLIQRSSFETLTLIaNPKAYAIGRRYTDT--DLNRCFLPRDlenphlssyE 80
Cdd:cd06231    43 PRVLISAGIHGDEPAGVEALLRFleSLAEKYLRRVNLLVLPCV-NPWGFERNTRENADgiDLNRSFLKDS---------P 112

                          90       100
                  ....*....|....*....|....*.
gi 1210258420  81 AQRAKVIyQTFgFAGSQQADFVIDLH 106
Cdd:cd06231   113 SPEVRAL-MEF-LASLGRFDLHLDLH 136
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 7-109 2.59e-03

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.


Pssm-ID: 349427 [Multi-domain]  Cd Length: 216  Bit Score: 38.59  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210258420   7 VVIVGGTHGNELTGI----YLVKKF-ERSPDLIQRSSFETLTLI----ANPKAYAI----GRRYTDT--DLNRCFlPRDL 71
Cdd:cd00596     1 ILITGGIHGNEVIGVelalALIEYLlENYGNDPLKRLLDNVELWivplVNPDGFARvidsGGRKNANgvDLNRNF-PYNW 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1210258420  72 ENPHLSSYEAQR-----------AKVIYQtfgFAGSQQADFVIDLHSST 109
Cdd:cd00596    80 GKDGTSGPSSPTyrgpapfsepeTQALRD---LAKSHRFDLAVSYHSSS 125
 
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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