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Conserved domains on  [gi|719787450|ref|XP_010223280|]
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PREDICTED: aspartoacylase isoform X2 [Tinamus guttatus]

Protein Classification

M14 family metallopeptidase( domain architecture ID 27772)

M14 family metallopeptidase is a zinc-binding carboxypeptidase (CP) which hydrolyzes single, C-terminal amino acids from polypeptide chains, and has a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity.

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 ...
 12-300 2.20e-125

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 PRK02259:

Pssm-ID: 472171  Cd Length: 288  Bit Score: 359.96  E-value: 2.20e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  12 VRKVAIFGGTHGNELSGIYLVKHWQEHGAEIQRTGVEVKPFICNPRAVKKCTRYIDCDLNRVFDLDSLgTVVEDTPYEVR 91
Cdd:PRK02259   2 INRVAIVGGTHGNEITGIYLVKKWQQQPNLINRKGLEVQTVIGNPEAIEAGRRYIDRDLNRSFRLDLL-QNPDLSGYEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  92 RAQEINRIFGPKGSDDaFDLIFDLHNTTSNMGCTLILENsRDDFTIQMSHYIKNALapePVPILLIEHPTLKYATTRSVA 171
Cdd:PRK02259  81 RAKELVQQLGPKGNSP-CDFIIDLHSTTANMGLSLILYG-RRPFDLALAAYLQSRL---PLPIYLHEKDEDQTGFLVELW 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450 172 KHPIGVEVGPQPQGVIRADILEKMRKIVRHGLDFVQLFNKGQ-EFPPCTIEVYKIMEKVDYPRNKNDEVIAIIHPKLQDQ 250
Cdd:PRK02259 156 PCGLVIEVGPVPQGVLDAEIFEQTELLIESILDYLEKYNQGKlPLPNEQLVVYRHLGSIDYPRDENGQIAAMIHPQLQGR 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 719787450 251 DWQPLNKGDPLFLTLDGEVIEYKGDNTVYPAFINEAAYYEKKHAFVKTVK 300
Cdd:PRK02259 236 DWQPLKPGDPLFLTFDGKTIFYEGDSTVYPVFINEAAYYEKGIAMSLTKK 285
 
Name Accession Description Interval E-value
PRK02259 PRK02259
aspartoacylase; Provisional
 12-300 2.20e-125

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 359.96  E-value: 2.20e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  12 VRKVAIFGGTHGNELSGIYLVKHWQEHGAEIQRTGVEVKPFICNPRAVKKCTRYIDCDLNRVFDLDSLgTVVEDTPYEVR 91
Cdd:PRK02259   2 INRVAIVGGTHGNEITGIYLVKKWQQQPNLINRKGLEVQTVIGNPEAIEAGRRYIDRDLNRSFRLDLL-QNPDLSGYEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  92 RAQEINRIFGPKGSDDaFDLIFDLHNTTSNMGCTLILENsRDDFTIQMSHYIKNALapePVPILLIEHPTLKYATTRSVA 171
Cdd:PRK02259  81 RAKELVQQLGPKGNSP-CDFIIDLHSTTANMGLSLILYG-RRPFDLALAAYLQSRL---PLPIYLHEKDEDQTGFLVELW 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450 172 KHPIGVEVGPQPQGVIRADILEKMRKIVRHGLDFVQLFNKGQ-EFPPCTIEVYKIMEKVDYPRNKNDEVIAIIHPKLQDQ 250
Cdd:PRK02259 156 PCGLVIEVGPVPQGVLDAEIFEQTELLIESILDYLEKYNQGKlPLPNEQLVVYRHLGSIDYPRDENGQIAAMIHPQLQGR 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 719787450 251 DWQPLNKGDPLFLTLDGEVIEYKGDNTVYPAFINEAAYYEKKHAFVKTVK 300
Cdd:PRK02259 236 DWQPLKPGDPLFLTFDGKTIFYEGDSTVYPVFINEAAYYEKGIAMSLTKK 285
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 13-206 3.61e-108

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: 312.22  E-value: 3.61e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  13 RKVAIFGGTHGNELSGIYLVKHWQEHGAEIQRTGVEVKPFICNPRAVKKCTRYIDCDLNRVFDLDSLGTVVEDTPYEVRR 92
Cdd:cd06909    1 KRVAIVGGTHGNELTGVYLVKHWLKNPELIERKSFEVHPLLANPRAVEQCRRYIDTDLNRCFSLENLSSAPSSLPYEVRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  93 AQEINRIFGPKGsDDAFDLIFDLHNTTSNMGCTLILEnSRDDFTIQMSHYIKNALapEPVPILLIEHPTLKYATTRSVAK 172
Cdd:cd06909   81 AREINQILGPKG-NPACDFIIDLHNTTSNMGITLILS-SSDDFTLKLAAYLQQRL--PPVRVLLHESPSKESPFLRSVAK 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 719787450 173 HPIGVEVGPQPQGVIRADILEKMRKIVRHGLDFV 206
Cdd:cd06909  157 HGFTIEVGPVPQGVLRADIFEQTRKLVKAILDFI 190
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 11-301 1.62e-81

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: 248.42  E-value: 1.62e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450   11 PVRKVAIFGGTHGNELSGIYLVKHWQEHGAEIQRTGVEVKPFICNPRAVKKCTRYIDCDLNRVFDLDSLGTvVEDTPYEV 90
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALGA-SSDEPYRA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450   91 RRAQEINRIFGPKGSdDAFDLIFDLHNTTSNMGCTLILENSRDDFTIQMSHYIKNALAPEPVPILLIEHPTLKYATTRSV 170
Cdd:pfam04952  80 TRAERLADLFFPALL-PRADIVLDLHTGTRGMGHLLFALAPIRDDPLHLLALLRAFGAPAVLKLHSKPSAGFSAFSAEEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  171 AKHPIGVEVGpqPQGVIRADILEKMRKIVRHGLDFVQLFNKGQEFPPcTIEVYKIMEKVDYPRNKNDEVIAIIHPKL--- 247
Cdd:pfam04952 159 GAPGFTLELG--GAGPFGANLISRTAAGVLNVLRLIGVLNGGPDAFE-PPKLYRVLREIDRPRDIRAELAGLVEFALnlg 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 719787450  248 QDQDWQPLNKGDPLFLTLDGEVIEYKGDNTVYPAFINEAAYYEKKHAFVKTVKV 301
Cdd:pfam04952 236 DDVDAGPLLPGGPLFAPFGGEETEYRAPEDGYPVFPNEAAYVGKGAALALVAKF 289
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
8-295 1.34e-60

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 195.07  E-value: 1.34e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450   8 HSPPVRKVAIFGGTHGNELSGIYLVKHWQEHGAEIQRT-GVEVKPFICNPRAVKKCTRYIDCDLNRVFDLDSLgtvVEDT 86
Cdd:COG2988   20 HAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPlSFRLLLILGNPAAMRAGRRYLDEDLNRLFGGRHL---QNPE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  87 PYEVRRAQEINRIFGPK-GSDDAFDLIFDLHNTTSNMGCTLI--LENSRDDFTIQMSHYIKnALAPEPVpiLLIEHPTlK 163
Cdd:COG2988   97 SYEAARAKELEQAVGPFfAAGGRVRLHIDLHTAIRNSGHERFavYPFRGRPFDLALLAYLA-AAGPEAV--VLHHAPG-G 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450 164 YATTRSVAKHPIG---VEVGPQ-PQGVIRADILEKMRKIVRHGLDFVQLfnkgQEFPPCTIEVYKIMEKVDyprnKNDEv 239
Cdd:COG2988  173 TFSHFSAELCGAQaftLELGKVrPFGQNDLSRFAATEEALRALLSGAEL----PEHPAQDLDLYRVVQQII----KHGD- 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 719787450 240 IAIIHPKLQDQDWQPLNKGDPLFLTlDGEVIEYKGDN--TVYPafiNEAAYYEKKHAF 295
Cdd:COG2988  244 DFMLHPDLDTLNFTPLPPGTLLAED-GGKEYRVEGDEerIVFP---NEAVYYGQRAAL 297
 
Name Accession Description Interval E-value
PRK02259 PRK02259
aspartoacylase; Provisional
 12-300 2.20e-125

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 359.96  E-value: 2.20e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  12 VRKVAIFGGTHGNELSGIYLVKHWQEHGAEIQRTGVEVKPFICNPRAVKKCTRYIDCDLNRVFDLDSLgTVVEDTPYEVR 91
Cdd:PRK02259   2 INRVAIVGGTHGNEITGIYLVKKWQQQPNLINRKGLEVQTVIGNPEAIEAGRRYIDRDLNRSFRLDLL-QNPDLSGYEQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  92 RAQEINRIFGPKGSDDaFDLIFDLHNTTSNMGCTLILENsRDDFTIQMSHYIKNALapePVPILLIEHPTLKYATTRSVA 171
Cdd:PRK02259  81 RAKELVQQLGPKGNSP-CDFIIDLHSTTANMGLSLILYG-RRPFDLALAAYLQSRL---PLPIYLHEKDEDQTGFLVELW 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450 172 KHPIGVEVGPQPQGVIRADILEKMRKIVRHGLDFVQLFNKGQ-EFPPCTIEVYKIMEKVDYPRNKNDEVIAIIHPKLQDQ 250
Cdd:PRK02259 156 PCGLVIEVGPVPQGVLDAEIFEQTELLIESILDYLEKYNQGKlPLPNEQLVVYRHLGSIDYPRDENGQIAAMIHPQLQGR 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 719787450 251 DWQPLNKGDPLFLTLDGEVIEYKGDNTVYPAFINEAAYYEKKHAFVKTVK 300
Cdd:PRK02259 236 DWQPLKPGDPLFLTFDGKTIFYEGDSTVYPVFINEAAYYEKGIAMSLTKK 285
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 13-206 3.61e-108

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: 312.22  E-value: 3.61e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  13 RKVAIFGGTHGNELSGIYLVKHWQEHGAEIQRTGVEVKPFICNPRAVKKCTRYIDCDLNRVFDLDSLGTVVEDTPYEVRR 92
Cdd:cd06909    1 KRVAIVGGTHGNELTGVYLVKHWLKNPELIERKSFEVHPLLANPRAVEQCRRYIDTDLNRCFSLENLSSAPSSLPYEVRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  93 AQEINRIFGPKGsDDAFDLIFDLHNTTSNMGCTLILEnSRDDFTIQMSHYIKNALapEPVPILLIEHPTLKYATTRSVAK 172
Cdd:cd06909   81 AREINQILGPKG-NPACDFIIDLHNTTSNMGITLILS-SSDDFTLKLAAYLQQRL--PPVRVLLHESPSKESPFLRSVAK 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 719787450 173 HPIGVEVGPQPQGVIRADILEKMRKIVRHGLDFV 206
Cdd:cd06909  157 HGFTIEVGPVPQGVLRADIFEQTRKLVKAILDFI 190
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 11-301 1.62e-81

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: 248.42  E-value: 1.62e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450   11 PVRKVAIFGGTHGNELSGIYLVKHWQEHGAEIQRTGVEVKPFICNPRAVKKCTRYIDCDLNRVFDLDSLGTvVEDTPYEV 90
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRAGSRYIPRDLNRSFPGRALGA-SSDEPYRA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450   91 RRAQEINRIFGPKGSdDAFDLIFDLHNTTSNMGCTLILENSRDDFTIQMSHYIKNALAPEPVPILLIEHPTLKYATTRSV 170
Cdd:pfam04952  80 TRAERLADLFFPALL-PRADIVLDLHTGTRGMGHLLFALAPIRDDPLHLLALLRAFGAPAVLKLHSKPSAGFSAFSAEEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  171 AKHPIGVEVGpqPQGVIRADILEKMRKIVRHGLDFVQLFNKGQEFPPcTIEVYKIMEKVDYPRNKNDEVIAIIHPKL--- 247
Cdd:pfam04952 159 GAPGFTLELG--GAGPFGANLISRTAAGVLNVLRLIGVLNGGPDAFE-PPKLYRVLREIDRPRDIRAELAGLVEFALnlg 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 719787450  248 QDQDWQPLNKGDPLFLTLDGEVIEYKGDNTVYPAFINEAAYYEKKHAFVKTVKV 301
Cdd:pfam04952 236 DDVDAGPLLPGGPLFAPFGGEETEYRAPEDGYPVFPNEAAYVGKGAALALVAKF 289
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
8-295 1.34e-60

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 195.07  E-value: 1.34e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450   8 HSPPVRKVAIFGGTHGNELSGIYLVKHWQEHGAEIQRT-GVEVKPFICNPRAVKKCTRYIDCDLNRVFDLDSLgtvVEDT 86
Cdd:COG2988   20 HAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPlSFRLLLILGNPAAMRAGRRYLDEDLNRLFGGRHL---QNPE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  87 PYEVRRAQEINRIFGPK-GSDDAFDLIFDLHNTTSNMGCTLI--LENSRDDFTIQMSHYIKnALAPEPVpiLLIEHPTlK 163
Cdd:COG2988   97 SYEAARAKELEQAVGPFfAAGGRVRLHIDLHTAIRNSGHERFavYPFRGRPFDLALLAYLA-AAGPEAV--VLHHAPG-G 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450 164 YATTRSVAKHPIG---VEVGPQ-PQGVIRADILEKMRKIVRHGLDFVQLfnkgQEFPPCTIEVYKIMEKVDyprnKNDEv 239
Cdd:COG2988  173 TFSHFSAELCGAQaftLELGKVrPFGQNDLSRFAATEEALRALLSGAEL----PEHPAQDLDLYRVVQQII----KHGD- 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 719787450 240 IAIIHPKLQDQDWQPLNKGDPLFLTlDGEVIEYKGDN--TVYPafiNEAAYYEKKHAF 295
Cdd:COG2988  244 DFMLHPDLDTLNFTPLPPGTLLAED-GGKEYRVEGDEerIVFP---NEAVYYGQRAAL 297
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 15-201 3.40e-24

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: 96.61  E-value: 3.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  15 VAIFGGTHGNELSGIYLVKHWQEHGAEIQRTG-VEVKPfICNPRAVKKCTRYID---CDLNRVFDLDSLGTvvedtpYEV 90
Cdd:cd06230    1 LLILAGVHGDEYEGVEAIRRLLAELDPSELKGtVVLVP-VANPPAFEAGTRYTPldgLDLNRIFPGDPDGS------PTE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  91 RRAQEINRIFGPKGsddafDLIFDLHNTTSNM-GCTLILENSRD--DFTIQMSHYIKNAlapepvPILLIEHP--TLKYA 165
Cdd:cd06230   74 RLAHELTELILKHA-----DALIDLHSGGTGRlVPYAILDYDSDarEKSRELARAFGGT------PVIWGGDPpgGTPVA 142

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 719787450 166 TTRSVAKHPIGVEVGpqPQGVIRADILEKMRKIVRH 201
Cdd:cd06230  143 AARSAGIPAITVELG--GGGRLRAERLERYLRGIRN 176
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 15-189 7.05e-12

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: 62.85  E-value: 7.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  15 VAIFGGTHGNELSGIYLVKHWQ---EHGAEIQRTgveVKPFICNPRAVKKCTRYIDCDLNRVFDLDSlgtvvEDTPYEVR 91
Cdd:cd18430    1 LAVLGAVHGNETCGTRAVERLLaelPSGALQKGP---VTLVPANERAYAEGVRFCEEDLNRVFPGDP-----DPDTYERR 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  92 RAQEINRIFgpkgsdDAFDLIFDLHNTTSNmGCTLILENSRDDFTiqmsHYIKNALAPEPvPILLIEHPTLKYATTRSVA 171
Cdd:cd18430   73 LANRLCPEL------EGHDVVLDLHSTHSG-GQPFAILDYGDKAS----RRLARSVGIPK-GWRVVYGRDLGYAHGGGKT 140

                        170       180
                 ....*....|....*....|.
gi 719787450 172 K-HPIGVEVGPQ--PQGVIRA 189
Cdd:cd18430  141 EvTGVTVECGYHdsEEAAEVA 161
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 10-122 3.83e-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: 349471  Cd Length: 211  Bit Score: 52.60  E-value: 3.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  10 PPVRKVAIFGGTHGNELSGIY----LVKHWQEHGAE-IQRTG-VEVKPFiCNPRAVKKCTRYI---DCDLNRVFDLDSLG 80
Cdd:cd06253   20 NAEPRIAIVAGIHGDELNGLYvcsrLIRFLKELEEGgYKLKGkVLVIPA-VNPLGINSGTRFWpfdNLDMNRMFPGYNKG 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 719787450  81 TVVEdtpyevRRAQEINRIFgpKGsddaFDLIFDLHNttSNM 122
Cdd:cd06253   99 ETTE------RIAAALFEDL--KG----ADYGIDLHS--SND 126
M14_ASTE_ASPA-like cd06910
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 15-119 8.63e-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: 349481  Cd Length: 208  Bit Score: 48.88  E-value: 8.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  15 VAIFGGTHGNELSGIYLVKHWQEHGaeiqrtgveVKPFI-------CNPRAVKK-------CTRYIDCDLNRVFDLDSLg 80
Cdd:cd06910   27 VMINALTHGNEICGAIALDWLLKNG---------VRPLRgrltfcfANVEAYERfdparptASRFVDEDLNRVWGPELL- 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 719787450  81 tvveDTP---YEVRRAQEINRIFgpkgsdDAFDLIFDLHNTT 119
Cdd:cd06910   97 ----DGPeqsIELRRARELRPVV------DTVDYLLDIHSMQ 128
COG3608 COG3608
Predicted deacylase [General function prediction only];
13-158 1.60e-06

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 48.69  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  13 RKVAIFGGTHGNELSGIY----LVKHWQEhgAEIQRTgVEVKPfICNPRAVKKCTRY--IDC-DLNRVFDLDSLGTVVEd 85
Cdd:COG3608   27 PTLLITAGIHGDELNGIEalrrLLRELDP--GELRGT-VILVP-VANPPGFLQGSRYlpIDGrDLNRSFPGDADGSLAE- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  86 tpyevRRAQEINRIFGPKgsddaFDLIFDLHNTTSNM------GCTLILENSRD-------DFTIQMSHYIKNAL----A 148
Cdd:COG3608  102 -----RIAHALFEEILPD-----ADYVIDLHSGGIARdnlphvRAGPGDEELRAlarafgaPVILDSPEGGDGSLreaaA 171

                        170
                 ....*....|
gi 719787450 149 PEPVPILLIE 158
Cdd:COG3608  172 EAGIPALTLE 181
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 6-96 1.12e-04

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: 42.58  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450   6 VAHSPPVRKVAIFGGTHGNELSGIYLVKHW---QEHGAEI--QRTGVevkpFICNPRAVKKCTRYIDCDLNRVFDLDSlg 80
Cdd:cd03855   37 TPAASASKSVVLSAGIHGNETAPIEILDQLindLIRGELAlaHRLLF----IFGNPPAIRQGKRFIEENLNRLFSGRH-- 110

                         90
                 ....*....|....*.
gi 719787450  81 TVVEDTpYEVRRAQEI 96
Cdd:cd03855  111 SKLPPS-YETARAAEL 125
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
 9-119 2.30e-04

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: 41.91  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450   9 SPPVRKVAIFGGTHGNELSGIYLVKHWQEHGAEIQRTGVE--VKPfICNPRAVKKCTRYIDC--DLNRVFDLDSlgtvve 84
Cdd:cd06231   39 RGDKPRVLISAGIHGDEPAGVEALLRFLESLAEKYLRRVNllVLP-CVNPWGFERNTRENADgiDLNRSFLKDS------ 111

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 719787450  85 dTPYEVRRAQEINRifgpkgSDDAFDLIFDLHNTT 119
Cdd:cd06231  112 -PSPEVRALMEFLA------SLGRFDLHLDLHEDW 139
M14_ASTE_ASPA-like cd06256
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 22-121 1.57e-03

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


Pssm-ID: 349474  Cd Length: 204  Bit Score: 39.20  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  22 HGNELSGIYLVKHW-QEHGAEIQRTgveVKPFICNPRAVKKCTRYID--CDLNRVFdldslgtVVEDTPYEVRRAQEINR 98
Cdd:cd06256   44 HGNEPTGLRAVQRLlKTGQAPLPRT---LLLFIGNVDAAKAGVRRLPgqPDYNRCW-------PGPFETPEGRLAAAVLE 113

                         90       100
                 ....*....|....*....|...
gi 719787450  99 IFGPKGsddAFDLIfDLHNTTSN 121
Cdd:cd06256  114 RLDTLR---PFASI-DIHNNTGK 132
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
 13-74 2.34e-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: 38.41  E-value: 2.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 719787450  13 RKVAIFGGTHGNELSGIYLVKHWqehgAEIQRTGVEVKPFIC------NPRAVKKCTRY----IdcDLNRVF 74
Cdd:cd06904   24 ARILIIGGIHGDEPEGVSLVEHL----LRWLKNHPASGDFHIvvvpclNPDGLAAGTRTnangV--DLNRNF 89
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 11-121 3.68e-03

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


Pssm-ID: 349469 [Multi-domain]  Cd Length: 195  Bit Score: 37.90  E-value: 3.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  11 PVRKVAIFGGTHGNELSGIYLVKHWQEHGAEIQRTGVEVKPFICNPRAVKKCTRYI---DCDLNRVFDLDSLGTVVEdtp 87
Cdd:cd06251   11 PGPTLLLTAAIHGDELNGIEVIQRLLEDLDPSKLRGTLIAIPVVNPLGFENNSRYLpddGRDLNRSFPGSEKGSLAS--- 87

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 719787450  88 yevRRAQEI-NRIFgpkgsdDAFDLIFDLHNTTSN 121
Cdd:cd06251   88 ---RLAHLLwNEIV------KKADYVIDLHTASTG 113
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 15-116 4.22e-03

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


Pssm-ID: 349470  Cd Length: 224  Bit Score: 37.94  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 719787450  15 VAIFGGTHGNELSG-IYLVKHWQEHGAEiQRTG-VEVKPFIcNPRAVKKCTRY--ID-CDLNRVFDLDSLGTVVEDTPYE 89
Cdd:cd06252   37 VLLTGGNHGDEYEGpIALRRLARDLDPE-DVRGrLIIVPAL-NLPAVRAGTRTspLDgGNLNRAFPGDADGTPTERIAHF 114

                         90       100
                 ....*....|....*....|....*..
gi 719787450  90 VRRaqeinRIFgPKGsddafDLIFDLH 116
Cdd:cd06252  115 LET-----VLL-PRA-----DAVIDLH 130
 
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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