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Conserved domains on  [gi|515628192|ref|WP_017060792|]
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MULTISPECIES: succinylglutamate desuccinylase/aspartoacylase family protein [Vibrio]

Protein Classification

succinylglutamate desuccinylase/aspartoacylase family protein( domain architecture ID 11466477)

succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) family protein which belongs to the ASTE/ASPA subfamily of the M14 family of metallocarboxypeptidases; ASTE cleaves N-succinyl-L-glutamate into succinate and L-glutamate (the last step in the arginine succinyltransferase (AST) pathway for the catabolism of arginine), and ASPA cleaves N-acetyl L-aspartic acid into aspartate and acetate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3608 COG3608
Predicted deacylase [General function prediction only];
26-317 7.33e-140

Predicted deacylase [General function prediction only];


:

Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 398.45  E-value: 7.33e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  26 ELQAAQLYTHSPLSIPIEIIHGRQAGPTLMVNAAIHGDELNGVEIARQLTNAIDPKKLKGTLIVVPIVNVFGFIHKSRYL 105
Cdd:COG3608    1 RLPLSRLASGTPVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELRGTVILVPVANPPGFLQGSRYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 106 P-DRRDLNRCFPGSEKGSLTSRIAYTFFENVAKHCDYILDLHTGAIHRTNLPQIRANLSNPETLRIAKAFATPVIIDSP- 183
Cdd:COG3608   81 PiDGRDLNRSFPGDADGSLAERIAHALFEEILPDADYVIDLHSGGIARDNLPHVRAGPGDEELRALARAFGAPVILDSPe 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 184 LRDGSLRSEAEKLGIPVLTYEGGEALRFDHLAIRAGYLGVHQVMKEIGMLRPNRKKLP--EPVLSKSTSWIRAESDGILR 261
Cdd:COG3608  161 GGDGSLREAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGMLDGEAPPPPlaPPVLARGSEWVRAPAGGLFE 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515628192 262 NMVRLGEQVEAGQTLAYISSPLGHQEGQVITTKGGIVIGQQTLPLVNEGDAVFHIA 317
Cdd:COG3608  241 PLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHIA 296
 
Name Accession Description Interval E-value
COG3608 COG3608
Predicted deacylase [General function prediction only];
26-317 7.33e-140

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 398.45  E-value: 7.33e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  26 ELQAAQLYTHSPLSIPIEIIHGRQAGPTLMVNAAIHGDELNGVEIARQLTNAIDPKKLKGTLIVVPIVNVFGFIHKSRYL 105
Cdd:COG3608    1 RLPLSRLASGTPVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELRGTVILVPVANPPGFLQGSRYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 106 P-DRRDLNRCFPGSEKGSLTSRIAYTFFENVAKHCDYILDLHTGAIHRTNLPQIRANLSNPETLRIAKAFATPVIIDSP- 183
Cdd:COG3608   81 PiDGRDLNRSFPGDADGSLAERIAHALFEEILPDADYVIDLHSGGIARDNLPHVRAGPGDEELRALARAFGAPVILDSPe 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 184 LRDGSLRSEAEKLGIPVLTYEGGEALRFDHLAIRAGYLGVHQVMKEIGMLRPNRKKLP--EPVLSKSTSWIRAESDGILR 261
Cdd:COG3608  161 GGDGSLREAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGMLDGEAPPPPlaPPVLARGSEWVRAPAGGLFE 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515628192 262 NMVRLGEQVEAGQTLAYISSPLGHQEGQVITTKGGIVIGQQTLPLVNEGDAVFHIA 317
Cdd:COG3608  241 PLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHIA 296
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 40-233 3.00e-102

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: 299.07  E-value: 3.00e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  40 IPIEIIHGRQAGPTLMVNAAIHGDELNGVEIARQLTNAIDPKKLKGTLIVVPIVNVFGFIHKSRYLPD-RRDLNRCFPGS 118
Cdd:cd06251    1 VPVLVARGAKPGPTLLLTAAIHGDELNGIEVIQRLLEDLDPSKLRGTLIAIPVVNPLGFENNSRYLPDdGRDLNRSFPGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 119 EKGSLTSRIAYTFFENVAKHCDYILDLHTGAIHRTNLPQIRANLSNPETLRIAKAFATPVIIDSPLRDGSLRSEAEKLGI 198
Cdd:cd06251   81 EKGSLASRLAHLLWNEIVKKADYVIDLHTASTGRTNLPYVRADLRDPESRRMAEAFGAPVIVDDPGEDGSLRGAAVELGI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 515628192 199 PVLTYEGGEALRFDHLAIRAGYLGVHQVMKEIGML 233
Cdd:cd06251  161 PAITVELGEALRFDEDIIRRGVEGVLNVLRHLGML 195
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 50-319 9.95e-71

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: 222.22  E-value: 9.95e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192   50 AGPTLMVNAAIHGDELNGVEIARQLTNAIDPKKLKGTLIVVPIVNVFGFIHKSRYLPdrRDLNRCFPGSEKG-------- 121
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRAGSRYIP--RDLNRSFPGRALGassdepyr 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  122 -SLTSRIAYTFFENVAKHCDYILDLHTGAIHRTNLPQIRANLSNPET--LRIAKAFATPVII--DSPLRDGSLRSEAEKL 196
Cdd:pfam04952  79 aTRAERLADLFFPALLPRADIVLDLHTGTRGMGHLLFALAPIRDDPLhlLALLRAFGAPAVLklHSKPSAGFSAFSAEEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  197 GIPVLTYEGGEALRFDHLAIRAGYLGVHQVMKEIGMLRP------NRKKLPEPVLSKSTSWIRAESDGILRNMVRLGEQV 270
Cdd:pfam04952 159 GAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGgpdafePPKLYRVLREIDRPRDIRAELAGLVEFALNLGDDV 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 515628192  271 EAGQTLA--YISSPLGHQEGQVITTKGGIVIGQQTLPLVNEGDAVFHIAYF 319
Cdd:pfam04952 239 DAGPLLPggPLFAPFGGEETEYRAPEDGYPVFPNEAAYVGKGAALALVAKF 289
PRK02259 PRK02259
aspartoacylase; Provisional
 58-147 3.75e-04

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 41.78  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  58 AAIHGDELNGVEIARQLT---NAIDPKKLKGTLIvvpIVNVFGFIHKSRYLpdRRDLNRCF--------PGSEKGSLTSR 126
Cdd:PRK02259   9 GGTHGNEITGIYLVKKWQqqpNLINRKGLEVQTV---IGNPEAIEAGRRYI--DRDLNRSFrldllqnpDLSGYEQLRAK 83

                         90       100
                 ....*....|....*....|..
gi 515628192 127 -IAYTFFENVAKHCDYILDLHT 147
Cdd:PRK02259  84 eLVQQLGPKGNSPCDFIIDLHS 105
 
Name Accession Description Interval E-value
COG3608 COG3608
Predicted deacylase [General function prediction only];
26-317 7.33e-140

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 398.45  E-value: 7.33e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  26 ELQAAQLYTHSPLSIPIEIIHGRQAGPTLMVNAAIHGDELNGVEIARQLTNAIDPKKLKGTLIVVPIVNVFGFIHKSRYL 105
Cdd:COG3608    1 RLPLSRLASGTPVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELRGTVILVPVANPPGFLQGSRYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 106 P-DRRDLNRCFPGSEKGSLTSRIAYTFFENVAKHCDYILDLHTGAIHRTNLPQIRANLSNPETLRIAKAFATPVIIDSP- 183
Cdd:COG3608   81 PiDGRDLNRSFPGDADGSLAERIAHALFEEILPDADYVIDLHSGGIARDNLPHVRAGPGDEELRALARAFGAPVILDSPe 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 184 LRDGSLRSEAEKLGIPVLTYEGGEALRFDHLAIRAGYLGVHQVMKEIGMLRPNRKKLP--EPVLSKSTSWIRAESDGILR 261
Cdd:COG3608  161 GGDGSLREAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGMLDGEAPPPPlaPPVLARGSEWVRAPAGGLFE 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515628192 262 NMVRLGEQVEAGQTLAYISSPLGHQEGQVITTKGGIVIGQQTLPLVNEGDAVFHIA 317
Cdd:COG3608  241 PLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHIA 296
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 40-233 3.00e-102

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: 299.07  E-value: 3.00e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  40 IPIEIIHGRQAGPTLMVNAAIHGDELNGVEIARQLTNAIDPKKLKGTLIVVPIVNVFGFIHKSRYLPD-RRDLNRCFPGS 118
Cdd:cd06251    1 VPVLVARGAKPGPTLLLTAAIHGDELNGIEVIQRLLEDLDPSKLRGTLIAIPVVNPLGFENNSRYLPDdGRDLNRSFPGS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 119 EKGSLTSRIAYTFFENVAKHCDYILDLHTGAIHRTNLPQIRANLSNPETLRIAKAFATPVIIDSPLRDGSLRSEAEKLGI 198
Cdd:cd06251   81 EKGSLASRLAHLLWNEIVKKADYVIDLHTASTGRTNLPYVRADLRDPESRRMAEAFGAPVIVDDPGEDGSLRGAAVELGI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 515628192 199 PVLTYEGGEALRFDHLAIRAGYLGVHQVMKEIGML 233
Cdd:cd06251  161 PAITVELGEALRFDEDIIRRGVEGVLNVLRHLGML 195
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 50-319 9.95e-71

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: 222.22  E-value: 9.95e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192   50 AGPTLMVNAAIHGDELNGVEIARQLTNAIDPKKLKGTLIVVPIVNVFGFIHKSRYLPdrRDLNRCFPGSEKG-------- 121
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDIAGERTLVPLANPPAFRAGSRYIP--RDLNRSFPGRALGassdepyr 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  122 -SLTSRIAYTFFENVAKHCDYILDLHTGAIHRTNLPQIRANLSNPET--LRIAKAFATPVII--DSPLRDGSLRSEAEKL 196
Cdd:pfam04952  79 aTRAERLADLFFPALLPRADIVLDLHTGTRGMGHLLFALAPIRDDPLhlLALLRAFGAPAVLklHSKPSAGFSAFSAEEL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  197 GIPVLTYEGGEALRFDHLAIRAGYLGVHQVMKEIGMLRP------NRKKLPEPVLSKSTSWIRAESDGILRNMVRLGEQV 270
Cdd:pfam04952 159 GAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGgpdafePPKLYRVLREIDRPRDIRAELAGLVEFALNLGDDV 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 515628192  271 EAGQTLA--YISSPLGHQEGQVITTKGGIVIGQQTLPLVNEGDAVFHIAYF 319
Cdd:pfam04952 239 DAGPLLPggPLFAPFGGEETEYRAPEDGYPVFPNEAAYVGKGAALALVAKF 289
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 41-228 6.05e-45

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: 152.74  E-value: 6.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  41 PIEIIHGRQAGPTLMVNAAIHGDELNGVEIARQLTNAIDPKKLKGTLIVVPIVNVFGFIHKSRYL-P-DRRDLNRCFPGS 118
Cdd:cd06254    1 PVTLINGAKPGPTLLITAGIHGGEYPGILAAIRLARELDPADVKGTLIIVHIANVSGFEARTPFVvPeDGKNLNRVFPGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 119 EKGSLTSRIAYTFFENVAKHCDYILDLHTGAIHRTNLP-QIRANLSNPETLRI----AKAFATPVIIDSPLRD-GSLRSE 192
Cdd:cd06254   81 PDGTLTERIAYFLTREIISRADFLIDLHGGDANEALTPfVYYPGGASEEVNDIsraaAQALGLPYIVISSSEKgTGYYSY 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515628192 193 AEKLGIPVLTYEGGEALRFDHLAIRAGYLGVHQVMK 228
Cdd:cd06254  161 AALRGIPSILVERGGLGTCDEEDVQAHKDGIKNLLR 196
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 54-226 3.13e-44

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: 150.15  E-value: 3.13e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  54 LMVNAAIHGDELNGVEIARQLTNAIDPKKLKGTLIVVPIVNVFGFIHKSRYLP-DRRDLNRCFPGSEKGSLTSRIAYTFF 132
Cdd:cd06230    1 LLILAGVHGDEYEGVEAIRRLLAELDPSELKGTVVLVPVANPPAFEAGTRYTPlDGLDLNRIFPGDPDGSPTERLAHELT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 133 ENVAKHCDYILDLHTGAIHRTNLPQI--RANLSNPETLRIAKAF-ATPVIIDSPLRDGSLRSEAEKLGIPVLTYEGGEAL 209
Cdd:cd06230   81 ELILKHADALIDLHSGGTGRLVPYAIldYDSDAREKSRELARAFgGTPVIWGGDPPGGTPVAAARSAGIPAITVELGGGG 160

                        170
                 ....*....|....*..
gi 515628192 210 RFDHLAIRAGYLGVHQV 226
Cdd:cd06230  161 RLRAERLERYLRGIRNV 177
M14_ASTE_ASPA-like cd06255
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 36-233 1.69e-42

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: 147.09  E-value: 1.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  36 SPLSIPIEIIHGRQAGPTLMVNAAIHGDELNGVEIARQLTNAIDPKKLKGTLIVVPIVNVFGFIHKSRYLP-DRRDLNRC 114
Cdd:cd06255    8 APVTIPVIVVRGAKPGPCLWINGAVHGDELNGPLAALELFRELDPAQLSGTLVATPIANPLAFQGRQKFSPqDGEDLDQS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 115 FPGSEKGSLTSRIAYTFFENVAKHCDYILDLHTGAIHRTNLPQIRANL---SNPET----LRIAKAF---ATPVIIDSPL 184
Cdd:cd06255   88 FPGDPDGLITERMAHALFSEVKEVADYLIDFHTGGTPFDANPYTVYKLfpeSGPVEekrlLRLARAFgvhANCRVDVSGA 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515628192 185 RD-------GSLRSEAEKLGIPVLTYEGGEALRFDHLAIRAGYLGVHQVMKEIGML 233
Cdd:cd06255  168 GGelpgntaGALDYQCMAQGIPAFMVELGGGGRAEEEAVRFAARGLRNLLRYLGML 223
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 40-233 1.06e-37

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: 134.62  E-value: 1.06e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  40 IPIEIIHGRqAGPTLMVNAAIHGDELNGVEIARQLTNAIDPKKLKGTLIVVPIVNVFGFIHKSRYLP-DRRDLNRCFPGS 118
Cdd:cd06252   24 IPITVINNG-SGPTVLLTGGNHGDEYEGPIALRRLARDLDPEDVRGRLIIVPALNLPAVRAGTRTSPlDGGNLNRAFPGD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 119 EKGSLTSRIAYTFFENVAKHCDYILDLHTG----------AIHRTNLPQIRAnlsnpETLRIAKAFATP--VIIDSPLRD 186
Cdd:cd06252  103 ADGTPTERIAHFLETVLLPRADAVIDLHSGgssldfvpcaAVHLLPDPAQRA-----RSLALAEAFGAPlsVVVDNVDAP 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 515628192 187 GSLRSEAEKLGIPVLTYEGGEALRFDHLAIRAGYLGVHQVMKEIGML 233
Cdd:cd06252  178 GTLDSAAERAGKIFVSTELGGGGTVTPAALRIAERGVLNVLIHLGVL 224
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 54-227 2.15e-34

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


Pssm-ID: 349484  Cd Length: 187  Bit Score: 124.66  E-value: 2.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  54 LMVNAAIHGDELNGVEIARQLTNAIDPKKLKGTLIVVPIVNVFGFIHKSRYL-P-DRRDLNRCFPGSEKGSLTSRIAYTF 131
Cdd:cd18174    1 LLVTAGVHGYEYASIEALQRLIKELDPAKLSGTVIVVPIANIPAFEGRSIYVnPlDGKNLNRSFPGDPDGTPTERLAHWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 132 FENVAKHCDYILDLHTGAI----------HRTNLPQIranlsNPETLRIAKAFATPVII-------DSPLRDGSLRSEAe 194
Cdd:cd18174   81 TTNVIARADYYIDLHGGDLnedlrpfvyyYETGNAAL-----DAASREMAEAFGLDHIVfykarlkASRGSLYTQAAAL- 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 515628192 195 KLGIPVLTYEGGEALRFDHLAIRAGYLGVHQVM 227
Cdd:cd18174  155 LRGIPAILVEAGGLGSRDEEDVARHVEGVLNVL 187
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 37-231 2.43e-31

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: 117.32  E-value: 2.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  37 PLSIPIEIIHGRQAGPTLMVNAAIHGDELNGVEIARQLTNAID-----PKKLKGTLIVVPIVNVFGFIHKSRYLP-DRRD 110
Cdd:cd06253    8 PLEVKGFRFGGGNAEPRIAIVAGIHGDELNGLYVCSRLIRFLKeleegGYKLKGKVLVIPAVNPLGINSGTRFWPfDNLD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 111 LNRCFPGSEKGSLTSRIAYTFFENVaKHCDYILDLHTGAIHRTNLPQIRANLSN-PETLRIAKAFATPVII--DSPLRDG 187
Cdd:cd06253   88 MNRMFPGYNKGETTERIAAALFEDL-KGADYGIDLHSSNDFLREIPQVRVIESGaQDLLPLAKFLGLDVVWvhPASTVDT 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 515628192 188 SLRSEAEKL-GIPVLTYEGGEALRFDHLAIRAGYLGVHQVMKEIG 231
Cdd:cd06253  167 GTLAYNWNEwGTKALVLEMGVGMRIDKEYCEQLFEGILRFLLKMG 211
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
 47-146 4.21e-12

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: 65.02  E-value: 4.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  47 GRQAGPTLMVNAAIHGDELNGVEIARQLTNAIDPKKLKG-TLIVVPIVNVFGFIHKSRYLPDRRDLNRCFpGSEKGSLTS 125
Cdd:cd06231   38 PRGDKPRVLISAGIHGDEPAGVEALLRFLESLAEKYLRRvNLLVLPCVNPWGFERNTRENADGIDLNRSF-LKDSPSPEV 116

                         90       100
                 ....*....|....*....|...
gi 515628192 126 RIAYTFfenVAKHCDY--ILDLH 146
Cdd:cd06231  117 RALMEF---LASLGRFdlHLDLH 136
M14_CP_Csd4-like cd06243
Peptidase M14 carboxypeptidase Csd4 and similar proteins; This family includes peptidase M14 ...
 36-148 4.84e-11

Peptidase M14 carboxypeptidase Csd4 and similar proteins; This family includes peptidase M14 carboxypeptidase Csd4 from H. pylori which has been shown to be DL-carboxypeptidase with a modified zinc binding site containing a glutamine residue in place of a conserved histidine. It is an archetype of a new carboxypeptidase subfamily with a domain arrangement that differs from this family of peptide-cleaving enzymes. Csd4 plays a role in trimming uncrosslinked peptidoglycan peptide chains by cleaving the amide bond between meso-diaminopimelate and iso-D-glutamic acid in truncated peptidoglycan side chains. It acts as a cell shape determinant, similar to Campylobacter jejuni Pgp1. The M14 family of metallocarboxypeptidases (MCPs), also known as funnelins, are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349462  Cd Length: 227  Bit Score: 61.99  E-value: 4.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  36 SPLSIPIEIIHGRQAGPTLMVNAAIHGDELNGVEIARQLtnaIDPKKLKGTLIVVPIVNVFGFIHKSRYLpdRRDLNRCF 115
Cdd:cd06243    1 EDIEKPFTRLEGREPGPTLLIIGGIQGDEPGGFLAADLL---ADLYLVKGNVIVVPRLNFPSILRNHRGL--NGDMNRKF 75

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515628192 116 pgseKGSLTSRIAYTFFENVAK-----HCDYILDLHTG 148
Cdd:cd06243   76 ----AALDKKDPEYKTIQEIKSliadfRPDVVLHLHDG 109
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
 31-214 6.85e-11

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: 61.14  E-value: 6.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  31 QLYTHSPLSIPIEIIH-GRQAGPTLMVNAAIHGDELNGVEIARQLTNAIDPKKLKG--TLIVVPIVNVFGFIHKSRYLPD 107
Cdd:cd06904    2 KVYGTSVKGRPILAYKfGPGSRARILIIGGIHGDEPEGVSLVEHLLRWLKNHPASGdfHIVVVPCLNPDGLAAGTRTNAN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 108 RRDLNRCFP------------------GSEKGSLT-SRIAYTFFEN------VAKHCDYILDLHTGAihrtnlPQIRAnl 162
Cdd:cd06904   82 GVDLNRNFPtknwepdarkpkdpryypGPKPASEPeTRALVELIERfkpdriISLHAPYLVNYDGPA------KSLLA-- 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515628192 163 snpetLRIAKAFATPVIIDSPLRDGSLRSEA-EKLGIPVLTYEGGEALRFDHL 214
Cdd:cd06904  154 -----EKLAQATGYPVVGDVGYTPGSLGTYAgIERNIPVITLELPEAVSIDEL 201
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
42-225 1.55e-08

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 55.47  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  42 IEIIHGRQAGPTLMVNAAIHGDELNGVE----IARQLTNAIDPKK---LKG-TLIVVPIVNVFGFIHKSRYLPDRRDLNR 113
Cdd:COG2866   56 LKIGDPAEGKPKVLLNAQQHGNEWTGTEallgLLEDLLDNYDPLIralLDNvTLYIVPMLNPDGAERNTRTNANGVDLNR 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 114 CFPgseKGSLTS---RIAYTFFENvaKHCDYILDLHT---------GAIHRTNLPQIRANlsNPETLRIAKAFATPVIID 181
Cdd:COG2866  136 DWP---APWLSEpetRALRDLLDE--HDPDFVLDLHGqgelfywfvGTTEPTGSFLAPSY--DEEREAFAEELNFEGIIL 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 515628192 182 SPLRDGSLRSEAEKLGIPVLTYEGGEALRFDHLAIRAGYLGVHQ 225
Cdd:COG2866  209 AGSAFLGAGAAGTLLISAPRQTFLFAAALDIGGGGDVSAGELVA 252
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
42-158 2.60e-07

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 51.39  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  42 IEIIHGRQAGPTLMVNAAIHGDELNGVEIARQLTNAIDPKKLKGTlivVPIVNVFG-----FIHKsRYLPdrRDLNRCFP 116
Cdd:COG2988   15 LELTPHAPGIKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLS---FRLLLILGnpaamRAGR-RYLD--EDLNRLFG 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515628192 117 GSEKGSLTSR---------IAYTFFENVAKHCDYILDLHTgAIHRTNLPQI 158
Cdd:COG2988   89 GRHLQNPESYeaarakeleQAVGPFFAAGGRVRLHIDLHT-AIRNSGHERF 138
M14-like cd06242
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
 51-113 4.10e-07

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: 49.99  E-value: 4.10e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515628192  51 GPTLMVNAAIHGDELNGVE----IARQLTNAIDPKKL--KGTLIVVPIVNVFGFIHKSRYLPDRRDLNR 113
Cdd:cd06242    1 KPTVLLVGQQHGNEPAGREaalaLARDLAFGDDARELleKVNVLVVPRANPDGRAANTRGNANGVDLNR 69
M14_ASTE_ASPA-like cd06256
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 44-206 7.33e-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: 7.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  44 IIH--GRQaGPTLMVNAAIHGDELNGVEIARQLTnaidpKKLKGTL---IVVPIVNVFGFIHKSRYLPDRRDLNRCFPGS 118
Cdd:cd06256   26 LIHlpGRR-PRPLFVSTLLHGNEPTGLRAVQRLL-----KTGQAPLprtLLLFIGNVDAAKAGVRRLPGQPDYNRCWPGP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 119 EKGSlTSRIAYTFFENVAKHCDY-ILDLH--TGaihrTNLPQIRANLSNPETLRIAKAFATPVIIDSPLRDGSLRSEAEK 195
Cdd:cd06256  100 FETP-EGRLAAAVLERLDTLRPFaSIDIHnnTG----KNPHYACVNRLDAAHLRLASLFSRTLVYFTRPLGVLSEALAAL 174

                        170
                 ....*....|.
gi 515628192 196 LgiPVLTYEGG 206
Cdd:cd06256  175 C--PAVTVECG 183
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 54-218 5.40e-06

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: 45.90  E-value: 5.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  54 LMVNAAIHGDELNGVEIARQLTNAIDPKKL-KGTLIVVPiVNVFGFIHKSRYLpdRRDLNRCFPGSEKG-SLTSRIAYTF 131
Cdd:cd18430    1 LAVLGAVHGNETCGTRAVERLLAELPSGALqKGPVTLVP-ANERAYAEGVRFC--EEDLNRVFPGDPDPdTYERRLANRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 132 FENVAKHCdYILDLHTgaIHRTNLPQIRANLSNPETLRIAKAFATPVIidSPLRDGSLRSEAEKLGIPV---LTYEGG-- 206
Cdd:cd18430   78 CPELEGHD-VVLDLHS--THSGGQPFAILDYGDKASRRLARSVGIPKG--WRVVYGRDLGYAHGGGKTEvtgVTVECGyh 152

                        170
                 ....*....|....*
gi 515628192 207 ---EALRFDHLAIRA 218
Cdd:cd18430  153 dseEAAEVAYRAILN 167
M14_PaAOTO_like cd06250
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like subfamily; ...
 36-148 8.73e-06

Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like subfamily; subgroup includes Pseudomonas aeruginosa AotO; An uncharacterized subgroup of the Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily which is part of the the M14 family of metallocarboxypeptidases. This subgroup includes Pseudomonas aeruginosa AotO and related proteins. 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. The gene encoding P. aeruginosa AotO was characterized as part of an operon encoding an arginine and ornithine transport system, however it is not essential for arginine and ornithine uptake.


Pssm-ID: 349468  Cd Length: 267  Bit Score: 46.46  E-value: 8.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  36 SPLSIPIEIIHGRQAGPTLMVNAAIHGDELNGV----EIARQLTNAIDPKKLKGTLIVVPIVN-------VFGFiHKSRY 104
Cdd:cd06250   12 TERSLTVFRFGGAGAGPKVYIQAALHADELPGNlvihHLLERLKALEAAGRIKGEIVLVPQANpiglsqkIGGY-HQGRF 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515628192 105 -LPDRRDLNRCFP---GSEKGSLTSRIAYTFFENVA----------------------KH--------CDYILDLHTG 148
Cdd:cd06250   91 dLATGDNFNRNFPdlaKAVAARVEERLGDDAAANVAliraalkealdalpprtelqrlKLtllrlaldADIVLDLHCD 168
M14_ASTE_ASPA-like cd06910
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 49-186 3.25e-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: 349481  Cd Length: 208  Bit Score: 44.26  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  49 QAGPTLMVNAAIHGDELNGVEIARQL-TNAIDPKKLKGTLIvvpIVNVFGFihkSRYLPDRRDLNRCF---------PGS 118
Cdd:cd06910   22 QPGPHVMINALTHGNEICGAIALDWLlKNGVRPLRGRLTFC---FANVEAY---ERFDPARPTASRFVdedlnrvwgPEL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192 119 EKGSLTS------RIAYTFFENVakhcDYILDLHTgaIHRTNLPQIranLSNPET--LRIAKAFATP--VIIDS------ 182
Cdd:cd06910   96 LDGPEQSielrraRELRPVVDTV----DYLLDIHS--MQEKVPPLA---LAGDKEkgRALARRVGSPahLLIDAghaegl 166


                 ....
gi 515628192 183 PLRD 186
Cdd:cd06910  167 RLRD 170
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 56-147 4.77e-05

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: 43.74  E-value: 4.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  56 VNAAIHGDELNGVEIARQLTNaiDPKKLKG-TLIVVP-IVNVFGFIHKSRYLpDrRDLNRCFPGSEKGSLTSRIAY---- 129
Cdd:cd06909    5 IVGGTHGNELTGVYLVKHWLK--NPELIERkSFEVHPlLANPRAVEQCRRYI-D-TDLNRCFSLENLSSAPSSLPYevrr 80

                         90       100
                 ....*....|....*....|....
gi 515628192 130 ------TFFENVAKHCDYILDLHT 147
Cdd:cd06909   81 areinqILGPKGNPACDFIIDLHN 104
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 54-150 4.80e-05

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: 43.99  E-value: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  54 LMVNAAIHGDELNGVEIARQLTNAI------DPKK--LKGT-LIVVPIVNVFGF----IHKSRYLPDRRDLNRCFP---- 116
Cdd:cd00596    1 ILITGGIHGNEVIGVELALALIEYLlenygnDPLKrlLDNVeLWIVPLVNPDGFarviDSGGRKNANGVDLNRNFPynwg 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515628192 117 ---GSEKGSLTSRIAYTFFE----NVAKHC-----DYILDLHTGAI 150
Cdd:cd00596   81 kdgTSGPSSPTYRGPAPFSEpetqALRDLAkshrfDLAVSYHSSSE 126
M14_ASTE cd03855
Peptidase M14 Succinylglutamate desuccinylase (ASTE) subfamily; Peptidase M14 ...
 42-157 2.32e-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: 42.19  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  42 IEIIHGRQAGPTLMVNAAIHGDELNGVEIARQLTNAIdpkkLKGTLIV-VPIVNVFG---FIHKS-RYLPDrrDLNRCFP 116
Cdd:cd03855   34 LELTPAASASKSVVLSAGIHGNETAPIEILDQLINDL----IRGELALaHRLLFIFGnppAIRQGkRFIEE--NLNRLFS 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515628192 117 GSEK---GSLTSRIA-------YTFFENVAKHCDYILDLHTgAIHRTNLPQ 157
Cdd:cd03855  108 GRHSklpPSYETARAaeleqavADFFAKASGEVRWHLDLHT-AIRGSKHEQ 157
PRK02259 PRK02259
aspartoacylase; Provisional
 58-147 3.75e-04

aspartoacylase; Provisional


Pssm-ID: 235019  Cd Length: 288  Bit Score: 41.78  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  58 AAIHGDELNGVEIARQLT---NAIDPKKLKGTLIvvpIVNVFGFIHKSRYLpdRRDLNRCF--------PGSEKGSLTSR 126
Cdd:PRK02259   9 GGTHGNEITGIYLVKKWQqqpNLINRKGLEVQTV---IGNPEAIEAGRRYI--DRDLNRSFrldllqnpDLSGYEQLRAK 83

                         90       100
                 ....*....|....*....|..
gi 515628192 127 -IAYTFFENVAKHCDYILDLHT 147
Cdd:PRK02259  84 eLVQQLGPKGNSPCDFIIDLHS 105
PRK05324 PRK05324
succinylglutamate desuccinylase; Provisional
 42-150 5.60e-04

succinylglutamate desuccinylase; Provisional


Pssm-ID: 235408  Cd Length: 329  Bit Score: 41.32  E-value: 5.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628192  42 IEIIHGRQAGPTLMVNAAIHGDELNGVEIARQLTNAIdpkkLKGTLIV-VPIVNVFG-----FIHKsRYLPDrrDLNRCF 115
Cdd:PRK05324  38 LELTPAAPSTKALVLSAGIHGNETAPIELLDQLVRDL----LAGELPLrARLLVILGnppamRAGK-RYLDE--DLNRLF 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 515628192 116 PGSEK---GSLTSRIAY-------TFFENVAKHCDYILDLHTgAI 150
Cdd:PRK05324 111 GGRHQqfpGSDEARRAAeleqaveDFFAAGAERVRWHYDLHT-AI 154
M14_CP_plant cd18172
Zinc carboxypeptidase, including SOL1, a carboxypeptidase D in plant; This family includes ...
 49-116 1.80e-03

Zinc carboxypeptidase, including SOL1, a carboxypeptidase D in plant; This family includes only plant members of the carboxypeptidase (CP) N/E-like subfamily of the M14 family of metallocarboxypeptidases (MCPs). It includes Arabidopsis thaliana SOL1 carboxypeptidase D which is known to possess enzymatic activity to remove the C-terminal arginine residue of CLE19 proprotein in vitro, and SOL1-dependent cleavage of the C-terminal arginine residue is necessary for CLE19 activity in vivo. The M14 family are zinc-binding 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. The N/E subfamily includes eight members, of which five (CPN, CPE, CPM, CPD, CPZ) are considered enzymatically active, while the other three are non-active (CPX1, PCX2, ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily, enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form; rather, they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition, all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation.


Pssm-ID: 349482 [Multi-domain]  Cd Length: 276  Bit Score: 39.70  E-value: 1.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515628192  49 QAGPTLMVNAAIHGDELNGVEIARQLTN-------AIDPKKLK----GTLIVVPIVNVFGFIHKSRYLPDRRDLNRCFP 116
Cdd:cd18172   49 ETEPAFKFVGNMHGDEPVGRELLLRLADwlcanykAKDPLAAKivenAHLHLVPTMNPDGFARRRRNNANNVDLNRDFP 127
 
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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