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Conserved domains on  [gi|322414761|gb|EFY05561|]
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succinylglutamate desuccinylase/aspartoacylase family protein [Phascolarctobacterium succinatutens YIT 12067]

Protein Classification

M14 family metallopeptidase( domain architecture ID 10154713)

M14 family metallopeptidase is a zinc-binding carboxypeptidase which hydrolyzes a single, C-terminal amino acid from a polypeptide chain, and has a recognition site for the free C-terminal carboxyl group

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 32-228 2.96e-105

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: 306.05  E-value: 2.96e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  32 PLTIINGDQDGPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVAaGCLIMMHPVNIQGFWARREMIVPEDGKNLNRVFPG 111
Cdd:cd06254    1 PVTLINGAKPGPTLLITAGIHGGEYPGILAAIRLARELDPADVK-GTLIIVHIANVSGFEARTPFVVPEDGKNLNRVFPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761 112 DPMGTLADKTAYLISNNFFSIADFYVDMHSGDIHESLHPYVYYPGQPTPEVEKKSRSVARVLDMEYMVRSLA--TGGAYN 189
Cdd:cd06254   80 DPDGTLTERIAYFLTREIISRADFLIDLHGGDANEALTPFVYYPGGASEEVNDISRAAAQALGLPYIVISSSekGTGYYS 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 322414761 190 YAASTGLPSILIERGGAGLCLHEDIEAYKDDIRNILRKL 228
Cdd:cd06254  160 YAALRGIPSILVERGGLGTCDEEDVQAHKDGIKNLLRHL 198
 
Name Accession Description Interval E-value
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 32-228 2.96e-105

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: 306.05  E-value: 2.96e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  32 PLTIINGDQDGPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVAaGCLIMMHPVNIQGFWARREMIVPEDGKNLNRVFPG 111
Cdd:cd06254    1 PVTLINGAKPGPTLLITAGIHGGEYPGILAAIRLARELDPADVK-GTLIIVHIANVSGFEARTPFVVPEDGKNLNRVFPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761 112 DPMGTLADKTAYLISNNFFSIADFYVDMHSGDIHESLHPYVYYPGQPTPEVEKKSRSVARVLDMEYMVRSLA--TGGAYN 189
Cdd:cd06254   80 DPDGTLTERIAYFLTREIISRADFLIDLHGGDANEALTPFVYYPGGASEEVNDISRAAAQALGLPYIVISSSekGTGYYS 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 322414761 190 YAASTGLPSILIERGGAGLCLHEDIEAYKDDIRNILRKL 228
Cdd:cd06254  160 YAALRGIPSILVERGGLGTCDEEDVQAHKDGIKNLLRHL 198
COG3608 COG3608
Predicted deacylase [General function prediction only];
21-316 2.32e-79

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 243.60  E-value: 2.32e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  21 YLPVPD----TNVKIPLTIINGDQDGPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVAaGCLIMMHPVNIQGFWAR-RE 95
Cdd:COG3608    1 RLPLSRlasgTPVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELR-GTVILVPVANPPGFLQGsRY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  96 MivPEDGKNLNRVFPGDPMGTLADKTAYLISNNFFSIADFYVDMHSGDIHESLHPYVYYPgqPTPEvekKSRSVARVLDM 175
Cdd:COG3608   80 L--PIDGRDLNRSFPGDADGSLAERIAHALFEEILPDADYVIDLHSGGIARDNLPHVRAG--PGDE---ELRALARAFGA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761 176 EYMVRS--LATGGAYNYAASTGLPSILIERGGAGLCLHEDIEAYKDDIRNILRKLKMFSLPVKPRHHS-PRDVENLIYLE 252
Cdd:COG3608  153 PVILDSpeGGDGSLREAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGMLDGEAPPPPLApPVLARGSEWVR 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 322414761 253 ALETGCWLHHIHSGDFVEEGQVLGRITDVFGNTLTTYYAEQTGVILYVCPALASPKGTILVAYG 316
Cdd:COG3608  233 APAGGLFEPLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHIA 296
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 41-313 6.28e-27

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: 107.05  E-value: 6.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761   41 DGPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVaAGCLIMMHPVNIQGFwARREMIVPEDgknLNRVFPGDPMG----- 115
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDI-AGERTLVPLANPPAF-RAGSRYIPRD---LNRSFPGRALGassde 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  116 ----TLADKTAYLISNNFFSIADFYVDMHSGDIHESLHPYVYYPGQPTPEVEKKsrsVARVLDMEYMVRSL---ATGGAY 188
Cdd:pfam04952  76 pyraTRAERLADLFFPALLPRADIVLDLHTGTRGMGHLLFALAPIRDDPLHLLA---LLRAFGAPAVLKLHskpSAGFSA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  189 NYAASTGLPSILIERGGAGLCLHEDIEAYKDDIRNILRKLKMFSLPV----KPRHHSPRDVENLIYLEALETGCWLH-HI 263
Cdd:pfam04952 153 FSAEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPdafePPKLYRVLREIDRPRDIRAELAGLVEfAL 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 322414761  264 HSGDFVEEGQVLGRITDV--FGNTLTTYYAEQTGVILYVCPALASPKGTILV 313
Cdd:pfam04952 233 NLGDDVDAGPLLPGGPLFapFGGEETEYRAPEDGYPVFPNEAAYVGKGAALA 284
Zn_pept smart00631
Zn_pept domain;
33-196 1.63e-05

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 45.79  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761    33 LTIINGDQDG-PTLLITAGIHGGEYPGIAAAM--------ELGRD-IEPEHVAAGCLIMMHPVNIQGF---------WA- 92
Cdd:smart00631  39 LKISNGGSHDkPAIFIDAGIHAREWIGPATALylinqlleNYGRDpRVTNLLDKTDIYIVPVLNPDGYeythtgdrlWRk 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761    93 RREMIVPEDGKNLNRVFP-----------GDPMGTLADK-------TAYLISNNFFsiaDFYVDMHSGDiHESLHPYvYY 154
Cdd:smart00631 119 NRSPNSNCRGVDLNRNFPfhwgetgnpcsETYAGPSPFSepetkavRDFIRSNRRF---KLYIDLHSYS-QLILYPY-GY 193

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 322414761   155 PGQPTPEVEKKSRSVARVLDMEYmvrSLATGGAYNYAASTGL 196
Cdd:smart00631 194 TKNDLPPNVDDLDAVAKALAKAL---ASVHGTRYTYGISNGA 232
 
Name Accession Description Interval E-value
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 32-228 2.96e-105

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: 306.05  E-value: 2.96e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  32 PLTIINGDQDGPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVAaGCLIMMHPVNIQGFWARREMIVPEDGKNLNRVFPG 111
Cdd:cd06254    1 PVTLINGAKPGPTLLITAGIHGGEYPGILAAIRLARELDPADVK-GTLIIVHIANVSGFEARTPFVVPEDGKNLNRVFPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761 112 DPMGTLADKTAYLISNNFFSIADFYVDMHSGDIHESLHPYVYYPGQPTPEVEKKSRSVARVLDMEYMVRSLA--TGGAYN 189
Cdd:cd06254   80 DPDGTLTERIAYFLTREIISRADFLIDLHGGDANEALTPFVYYPGGASEEVNDISRAAAQALGLPYIVISSSekGTGYYS 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 322414761 190 YAASTGLPSILIERGGAGLCLHEDIEAYKDDIRNILRKL 228
Cdd:cd06254  160 YAALRGIPSILVERGGLGTCDEEDVQAHKDGIKNLLRHL 198
COG3608 COG3608
Predicted deacylase [General function prediction only];
21-316 2.32e-79

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 243.60  E-value: 2.32e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  21 YLPVPD----TNVKIPLTIINGDQDGPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVAaGCLIMMHPVNIQGFWAR-RE 95
Cdd:COG3608    1 RLPLSRlasgTPVSLPVTVFRGAGPGPTLLITAGIHGDELNGIEALRRLLRELDPGELR-GTVILVPVANPPGFLQGsRY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  96 MivPEDGKNLNRVFPGDPMGTLADKTAYLISNNFFSIADFYVDMHSGDIHESLHPYVYYPgqPTPEvekKSRSVARVLDM 175
Cdd:COG3608   80 L--PIDGRDLNRSFPGDADGSLAERIAHALFEEILPDADYVIDLHSGGIARDNLPHVRAG--PGDE---ELRALARAFGA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761 176 EYMVRS--LATGGAYNYAASTGLPSILIERGGAGLCLHEDIEAYKDDIRNILRKLKMFSLPVKPRHHS-PRDVENLIYLE 252
Cdd:COG3608  153 PVILDSpeGGDGSLREAAAEAGIPALTLELGGGGRFDEESIEAGVRGILNVLRHLGMLDGEAPPPPLApPVLARGSEWVR 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 322414761 253 ALETGCWLHHIHSGDFVEEGQVLGRITDVFGNTLTTYYAEQTGVILYVCPALASPKGTILVAYG 316
Cdd:COG3608  233 APAGGLFEPLVELGDRVKKGDVLGRITDPFGEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHIA 296
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 45-225 3.20e-58

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: 185.52  E-value: 3.20e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  45 LLITAGIHGGEYPGIAAAMELGRDIEPEHVAaGCLIMMHPVNIQGFWARREMIVPEDGKNLNRVFPGDPMGTLADKTAYL 124
Cdd:cd18174    1 LLVTAGVHGYEYASIEALQRLIKELDPAKLS-GTVIVVPIANIPAFEGRSIYVNPLDGKNLNRSFPGDPDGTPTERLAHW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761 125 ISNNFFSIADFYVDMHSGDIHESLHPYVYYPGQPTPEVEKKSRSVARVLDMEYMV-------RSLATGGAYNYAASTGLP 197
Cdd:cd18174   80 LTTNVIARADYYIDLHGGDLNEDLRPFVYYYETGNAALDAASREMAEAFGLDHIVfykarlkASRGSLYTQAAALLRGIP 159

                        170       180
                 ....*....|....*....|....*...
gi 322414761 198 SILIERGGAGLCLHEDIEAYKDDIRNIL 225
Cdd:cd18174  160 AILVEAGGLGSRDEEDVARHVEGVLNVL 187
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 29-230 1.19e-39

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: 138.86  E-value: 1.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  29 VKIPLTIINGdQDGPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVAaGCLIMMHPVNIQGFWARREmIVPEDGKNLNRV 108
Cdd:cd06252   22 IPIPITVINN-GSGPTVLLTGGNHGDEYEGPIALRRLARDLDPEDVR-GRLIIVPALNLPAVRAGTR-TSPLDGGNLNRA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761 109 FPGDPMGTLADKTAYLISNNFFSIADFYVDMHSGDIHESLHPYVYYPGQPTPEVEKKSRSVARVLDMEYMV--RSLATGG 186
Cdd:cd06252   99 FPGDADGTPTERIAHFLETVLLPRADAVIDLHSGGSSLDFVPCAAVHLLPDPAQRARSLALAEAFGAPLSVvvDNVDAPG 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 322414761 187 AYN-YAASTGLPSILIERGGAGLCLHEDIEAYKDDIRNILRKLKM 230
Cdd:cd06252  179 TLDsAAERAGKIFVSTELGGGGTVTPAALRIAERGVLNVLIHLGV 223
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 31-230 4.61e-36

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: 128.81  E-value: 4.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  31 IPLTIINGDQDGPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVAaGCLIMMHPVNIQGFWARREMIvPEDGKNLNRVFP 110
Cdd:cd06251    1 VPVLVARGAKPGPTLLLTAAIHGDELNGIEVIQRLLEDLDPSKLR-GTLIAIPVVNPLGFENNSRYL-PDDGRDLNRSFP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761 111 GDPMGTLADKTAYLISNNFFSIADFYVDMHSGDIHESLHPYVYYPGqPTPEVEKKSRS--VARVLDMEYMVRSLAtggay 188
Cdd:cd06251   79 GSEKGSLASRLAHLLWNEIVKKADYVIDLHTASTGRTNLPYVRADL-RDPESRRMAEAfgAPVIVDDPGEDGSLR----- 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 322414761 189 NYAASTGLPSILIERGGAGLCLHEDIEAYKDDIRNILRKLKM 230
Cdd:cd06251  153 GAAVELGIPAITVELGEALRFDEDIIRRGVEGVLNVLRHLGM 194
M14_ASTE_ASPA-like cd06255
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 29-230 2.27e-35

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: 127.83  E-value: 2.27e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  29 VKIPLTIINGDQDGPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVAaGCLIMMHPVNIQGFWARREmIVPEDGKNLNRV 108
Cdd:cd06255   10 VTIPVIVVRGAKPGPCLWINGAVHGDELNGPLAALELFRELDPAQLS-GTLVATPIANPLAFQGRQK-FSPQDGEDLDQS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761 109 FPGDPMGTLADKTAYLISNNFFSIADFYVDMHSGDIHESLHPYVYY--PGQPTPEVEKKSRSVARVLDME---YMVRSLA 183
Cdd:cd06255   88 FPGDPDGLITERMAHALFSEVKEVADYLIDFHTGGTPFDANPYTVYklFPESGPVEEKRLLRLARAFGVHancRVDVSGA 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 322414761 184 TG-------GAYNY-AASTGLPSILIERGGAGLCLHEDIEAYKDDIRNILRKLKM 230
Cdd:cd06255  168 GGelpgntaGALDYqCMAQGIPAFMVELGGGGRAEEEAVRFAARGLRNLLRYLGM 222
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 45-224 1.50e-34

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: 124.35  E-value: 1.50e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  45 LLITAGIHGGEYPGIAAAMELGRDIEPEHVAaGCLIMMHPVNIQGFWARREMIvPEDGKNLNRVFPGDPMGTLADKTAYL 124
Cdd:cd06230    1 LLILAGVHGDEYEGVEAIRRLLAELDPSELK-GTVVLVPVANPPAFEAGTRYT-PLDGLDLNRIFPGDPDGSPTERLAHE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761 125 ISNNFFSIADFYVDMHSGDIHESL-HPYVYYPGQPTPevekKSRSVARVLDME--YMVRSLATGGAYNYAASTGLPSILI 201
Cdd:cd06230   79 LTELILKHADALIDLHSGGTGRLVpYAILDYDSDARE----KSRELARAFGGTpvIWGGDPPGGTPVAAARSAGIPAITV 154

                        170       180
                 ....*....|....*....|...
gi 322414761 202 ERGGAGLCLHEDIEAYKDDIRNI 224
Cdd:cd06230  155 ELGGGGRLRAERLERYLRGIRNV 177
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 41-313 6.28e-27

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: 107.05  E-value: 6.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761   41 DGPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVaAGCLIMMHPVNIQGFwARREMIVPEDgknLNRVFPGDPMG----- 115
Cdd:pfam04952   1 PGPTLLLSAGIHGNETNGVELLRRLLRQLDPGDI-AGERTLVPLANPPAF-RAGSRYIPRD---LNRSFPGRALGassde 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  116 ----TLADKTAYLISNNFFSIADFYVDMHSGDIHESLHPYVYYPGQPTPEVEKKsrsVARVLDMEYMVRSL---ATGGAY 188
Cdd:pfam04952  76 pyraTRAERLADLFFPALLPRADIVLDLHTGTRGMGHLLFALAPIRDDPLHLLA---LLRAFGAPAVLKLHskpSAGFSA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  189 NYAASTGLPSILIERGGAGLCLHEDIEAYKDDIRNILRKLKMFSLPV----KPRHHSPRDVENLIYLEALETGCWLH-HI 263
Cdd:pfam04952 153 FSAEELGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPdafePPKLYRVLREIDRPRDIRAELAGLVEfAL 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 322414761  264 HSGDFVEEGQVLGRITDV--FGNTLTTYYAEQTGVILYVCPALASPKGTILV 313
Cdd:pfam04952 233 NLGDDVDAGPLLPGGPLFapFGGEETEYRAPEDGYPVFPNEAAYVGKGAALA 284
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 38-228 9.01e-11

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: 60.69  E-value: 9.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  38 GDQDGPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVAAGCL---IMMHP-VNIQGFWARREMiVPEDGKNLNRVFPGDP 113
Cdd:cd06253   18 GGNAEPRIAIVAGIHGDELNGLYVCSRLIRFLKELEEGGYKLkgkVLVIPaVNPLGINSGTRF-WPFDNLDMNRMFPGYN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761 114 MGTLADKTAYLIsnnFFSI--ADFYVDMHSGDIHESLHPYV--YYPGQPtpevekKSRSVARVLDMEY-MVRSLAT--GG 186
Cdd:cd06253   97 KGETTERIAAAL---FEDLkgADYGIDLHSSNDFLREIPQVrvIESGAQ------DLLPLAKFLGLDVvWVHPASTvdTG 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 322414761 187 AYNYAAST-GLPSILIErGGAGLCLHEDI-EAYKDDIRNILRKL 228
Cdd:cd06253  168 TLAYNWNEwGTKALVLE-MGVGMRIDKEYcEQLFEGILRFLLKM 210
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 45-199 5.28e-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: 5.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  45 LLITAGIHGGEYPGIAAAMELGRDIEPEHVAAGCLIMMhPVNIQGFwARREMIVPEdgkNLNRVFPGDPMGT-----LAD 119
Cdd:cd18430    1 LAVLGAVHGNETCGTRAVERLLAELPSGALQKGPVTLV-PANERAY-AEGVRFCEE---DLNRVFPGDPDPDtyerrLAN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761 120 KTAYLISNNffsiaDFYVDMHSgdIHESLHPYVYYPGqptpeVEKKSRSVARVLDMEyMVRSLATGGAYNYAASTGLPSI 199
Cdd:cd18430   76 RLCPELEGH-----DVVLDLHS--THSGGQPFAILDY-----GDKASRRLARSVGIP-KGWRVVYGRDLGYAHGGGKTEV 142
Zn_pept smart00631
Zn_pept domain;
33-196 1.63e-05

Zn_pept domain;


Pssm-ID: 214748 [Multi-domain]  Cd Length: 277  Bit Score: 45.79  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761    33 LTIINGDQDG-PTLLITAGIHGGEYPGIAAAM--------ELGRD-IEPEHVAAGCLIMMHPVNIQGF---------WA- 92
Cdd:smart00631  39 LKISNGGSHDkPAIFIDAGIHAREWIGPATALylinqlleNYGRDpRVTNLLDKTDIYIVPVLNPDGYeythtgdrlWRk 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761    93 RREMIVPEDGKNLNRVFP-----------GDPMGTLADK-------TAYLISNNFFsiaDFYVDMHSGDiHESLHPYvYY 154
Cdd:smart00631 119 NRSPNSNCRGVDLNRNFPfhwgetgnpcsETYAGPSPFSepetkavRDFIRSNRRF---KLYIDLHSYS-QLILYPY-GY 193

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 322414761   155 PGQPTPEVEKKSRSVARVLDMEYmvrSLATGGAYNYAASTGL 196
Cdd:smart00631 194 TKNDLPPNVDDLDAVAKALAKAL---ASVHGTRYTYGISNGA 232
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
 38-110 7.15e-04

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: 40.34  E-value: 7.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 322414761  38 GDQDGPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVAAGCLIMMHP-VNIQGFWARREmiVPEDGKNLNRVFP 110
Cdd:cd06904   19 GPGSRARILIIGGIHGDEPEGVSLVEHLLRWLKNHPASGDFHIVVVPcLNPDGLAAGTR--TNANGVDLNRNFP 90
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
42-160 2.60e-03

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 39.06  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  42 GPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVAAGC---LIMMHPVNIQGfwARREmiVPEDgknLNRVFPGDPmgtLA 118
Cdd:COG2988   24 IKAVVISGGIHGNETAPIELLDKLLQDLLLGERPLSFrllLILGNPAAMRA--GRRY--LDED---LNRLFGGRH---LQ 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 322414761 119 DKTAY-------LIS--NNFFSIA---DFYVDMHSGdIHESLHP-YVYYPGQPTP 160
Cdd:COG2988   94 NPESYeaarakeLEQavGPFFAAGgrvRLHIDLHTA-IRNSGHErFAVYPFRGRP 147
MpaA COG2866
Murein tripeptide amidase MpaA [Cell wall/membrane/envelope biogenesis];
33-230 3.55e-03

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


Pssm-ID: 442113 [Multi-domain]  Cd Length: 337  Bit Score: 38.90  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761  33 LTIINGDQDGPTLLITAGIHGGEYPGIAAAMELGRDI------EPEHVAAGCLIMMHP-VNIQG-FWARREMIvpeDGKN 104
Cdd:COG2866   56 LKIGDPAEGKPKVLLNAQQHGNEWTGTEALLGLLEDLldnydpLIRALLDNVTLYIVPmLNPDGaERNTRTNA---NGVD 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322414761 105 LNRVFPGDP-----MGTLADKTAyliSNNFfsiaDFYVDMHSGDIheslhpyVYYPGQPTPEVEKKSRSVARVLDMEYMV 179
Cdd:COG2866  133 LNRDWPAPWlsepeTRALRDLLD---EHDP----DFVLDLHGQGE-------LFYWFVGTTEPTGSFLAPSYDEEREAFA 198

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 322414761 180 RSLATGGAYNYAASTGLPSILIERGGAGLCLHEDIEAYKDDIRNILRKLKM 230
Cdd:COG2866  199 EELNFEGIILAGSAFLGAGAAGTLLISAPRQTFLFAAALDIGGGGDVSAGE 249
M14-like cd06241
Peptidase M14-like domain; uncharacterized subgroup; Peptidase M14-like domain of a ...
 43-69 3.95e-03

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 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: 349460 [Multi-domain]  Cd Length: 215  Bit Score: 38.01  E-value: 3.95e-03
                         10        20
                 ....*....|....*....|....*..
gi 322414761  43 PTLLITAGIHGGEYPGIAAAMELGRDI 69
Cdd:cd06241    2 PVVLIQAGIHPGEVEGKEASLMLLRDI 28
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
 33-109 4.91e-03

Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family includes Francisella tularensis protein rapid encystment phenotype 34 (REP34) which is a zinc-containing monomeric protein demonstrating carboxypeptidase B-like activity. REP34 possesses a novel topology with its substrate binding pocket deviating from the canonical M14 peptidases with a possible catalytic role for a conserved tyrosine and distinct S1' recognition site. Thus, REP34, identified as an active carboxypeptidase and a potential key F. tularensis effector protein, may help elucidate a mechanistic understanding of F. tularensis infection of phagocytic cells. A functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.


Pssm-ID: 349450 [Multi-domain]  Cd Length: 239  Bit Score: 38.06  E-value: 4.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 322414761  33 LTIINGDQDGPTLLITAGIHGGEYPGIAAAMELGRDIEPEHVAAGCLIMMHPVNIQGFWA-RREMIvpeDGKNLNRVF 109
Cdd:cd06231   33 LKSPNPRGDKPRVLISAGIHGDEPAGVEALLRFLESLAEKYLRRVNLLVLPCVNPWGFERnTRENA---DGIDLNRSF 107
 
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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