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Conserved domains on  [gi|1334692452|gb|PNV61178|]
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succinylglutamate desuccinylase [Clostridium sp. chh4-2]

Protein Classification

M14 family metallopeptidase( domain architecture ID 10154712)

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 cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 10-218 6.14e-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: 349471  Cd Length: 211  Bit Score: 297.59  E-value: 6.14e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  10 LPVDEKLKVKKNSLMPeslTGHEKRICVVTGTHGDELEGQYVCYELIRRINENKEH---LKGIVDIFPALNPLGIDSVTR 86
Cdd:cd06253     3 SPFREPLEVKGFRFGG---GNAEPRIAIVAGIHGDELNGLYVCSRLIRFLKELEEGgykLKGKVLVIPAVNPLGINSGTR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  87 GIPMFDLDMNRIFPGSESGSVPEYVASKIVEDIAGADLCIDIHASNIFLREIPQVRMSEGTAEKLLPYAKVLNIDYVWVY 166
Cdd:cd06253    80 FWPFDNLDMNRMFPGYNKGETTERIAAALFEDLKGADYGIDLHSSNDFLREIPQVRVIESGAQDLLPLAKFLGLDVVWVH 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1334692452 167 AAATVLEATLAHSLNTIGVPTLVVEMGVGMRITEDYCHQLTDGIFCVMKKMG 218
Cdd:cd06253   160 PASTVDTGTLAYNWNEWGTKALVLEMGVGMRIDKEYCEQLFEGILRFLLKMG 211
 
Name Accession Description Interval E-value
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 10-218 6.14e-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: 349471  Cd Length: 211  Bit Score: 297.59  E-value: 6.14e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  10 LPVDEKLKVKKNSLMPeslTGHEKRICVVTGTHGDELEGQYVCYELIRRINENKEH---LKGIVDIFPALNPLGIDSVTR 86
Cdd:cd06253     3 SPFREPLEVKGFRFGG---GNAEPRIAIVAGIHGDELNGLYVCSRLIRFLKELEEGgykLKGKVLVIPAVNPLGINSGTR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  87 GIPMFDLDMNRIFPGSESGSVPEYVASKIVEDIAGADLCIDIHASNIFLREIPQVRMSEGTAEKLLPYAKVLNIDYVWVY 166
Cdd:cd06253    80 FWPFDNLDMNRMFPGYNKGETTERIAAALFEDLKGADYGIDLHSSNDFLREIPQVRVIESGAQDLLPLAKFLGLDVVWVH 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1334692452 167 AAATVLEATLAHSLNTIGVPTLVVEMGVGMRITEDYCHQLTDGIFCVMKKMG 218
Cdd:cd06253   160 PASTVDTGTLAYNWNEWGTKALVLEMGVGMRIDKEYCEQLFEGILRFLLKMG 211
COG3608 COG3608
Predicted deacylase [General function prediction only];
33-306 1.88e-75

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 233.20  E-value: 1.88e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  33 KRICVVTGTHGDELEGQYVCYELIRRINENKehLKGIVDIFPALNPLGIDSVTRGIPMFDLDMNRIFPGSESGSVPEYVA 112
Cdd:COG3608    27 PTLLITAGIHGDELNGIEALRRLLRELDPGE--LRGTVILVPVANPPGFLQGSRYLPIDGRDLNRSFPGDADGSLAERIA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 113 SKIVEDI-AGADLCIDIHASNIFLREIPQVRMSEGtAEKLLPYAKVLNIDYVWVyaAATVLEATLAHSLNTIGVPTLVVE 191
Cdd:COG3608   105 HALFEEIlPDADYVIDLHSGGIARDNLPHVRAGPG-DEELRALARAFGAPVILD--SPEGGDGSLREAAAEAGIPALTLE 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 192 MGVGMRITEDYCHQLTDGIFCVMKKMGIWDGEVIEPKKPIISTDGQVGIINANEPGIFMPHVEHWDNIKKGDAIGVILNP 271
Cdd:COG3608   182 LGGGGRFDEESIEAGVRGILNVLRHLGMLDGEAPPPPLAPPVLARGSEWVRAPAGGLFEPLVELGDRVKKGDVLGRITDP 261

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1334692452 272 LqGTVAETLYAPFDGMVFTLREYPVVNSGSLIARI 306
Cdd:COG3608   262 F-GEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHI 295
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 33-306 8.98e-25

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: 100.89  E-value: 8.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  33 KRICVVTGTHGDELEGQYVCYELIRRINENKehLKGIVDIFPALNPLGIDSVTRGIPMfdlDMNRIFPGSESGSVPEY-- 110
Cdd:pfam04952   3 PTLLLSAGIHGNETNGVELLRRLLRQLDPGD--IAGERTLVPLANPPAFRAGSRYIPR---DLNRSFPGRALGASSDEpy 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 111 ---VASKIV-----EDIAGADLCIDIHASNIFLREIPQVRMSEGTA-EKLLPYAKVLNIDYVWV---YAAATVLEATLAH 178
Cdd:pfam04952  78 ratRAERLAdlffpALLPRADIVLDLHTGTRGMGHLLFALAPIRDDpLHLLALLRAFGAPAVLKlhsKPSAGFSAFSAEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 179 slntIGVPTLVVEMGVGMRITEDYCHQLTDGIFCVMKKMGIWDGEVIEPKKPIISTDGQVGI----INANEPGIFMPHVE 254
Cdd:pfam04952 158 ----LGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPPKLYRVLREIDrprdIRAELAGLVEFALN 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1334692452 255 HWDNIKKGDAI--GVILNPLQGTVAETLyAPFDGMVFTLREYPVVNSGSLIARI 306
Cdd:pfam04952 234 LGDDVDAGPLLpgGPLFAPFGGEETEYR-APEDGYPVFPNEAAYVGKGAALALV 286
 
Name Accession Description Interval E-value
M14_ASTE_ASPA-like cd06253
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 10-218 6.14e-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: 349471  Cd Length: 211  Bit Score: 297.59  E-value: 6.14e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  10 LPVDEKLKVKKNSLMPeslTGHEKRICVVTGTHGDELEGQYVCYELIRRINENKEH---LKGIVDIFPALNPLGIDSVTR 86
Cdd:cd06253     3 SPFREPLEVKGFRFGG---GNAEPRIAIVAGIHGDELNGLYVCSRLIRFLKELEEGgykLKGKVLVIPAVNPLGINSGTR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  87 GIPMFDLDMNRIFPGSESGSVPEYVASKIVEDIAGADLCIDIHASNIFLREIPQVRMSEGTAEKLLPYAKVLNIDYVWVY 166
Cdd:cd06253    80 FWPFDNLDMNRMFPGYNKGETTERIAAALFEDLKGADYGIDLHSSNDFLREIPQVRVIESGAQDLLPLAKFLGLDVVWVH 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1334692452 167 AAATVLEATLAHSLNTIGVPTLVVEMGVGMRITEDYCHQLTDGIFCVMKKMG 218
Cdd:cd06253   160 PASTVDTGTLAYNWNEWGTKALVLEMGVGMRIDKEYCEQLFEGILRFLLKMG 211
COG3608 COG3608
Predicted deacylase [General function prediction only];
33-306 1.88e-75

Predicted deacylase [General function prediction only];


Pssm-ID: 442826 [Multi-domain]  Cd Length: 296  Bit Score: 233.20  E-value: 1.88e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  33 KRICVVTGTHGDELEGQYVCYELIRRINENKehLKGIVDIFPALNPLGIDSVTRGIPMFDLDMNRIFPGSESGSVPEYVA 112
Cdd:COG3608    27 PTLLITAGIHGDELNGIEALRRLLRELDPGE--LRGTVILVPVANPPGFLQGSRYLPIDGRDLNRSFPGDADGSLAERIA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 113 SKIVEDI-AGADLCIDIHASNIFLREIPQVRMSEGtAEKLLPYAKVLNIDYVWVyaAATVLEATLAHSLNTIGVPTLVVE 191
Cdd:COG3608   105 HALFEEIlPDADYVIDLHSGGIARDNLPHVRAGPG-DEELRALARAFGAPVILD--SPEGGDGSLREAAAEAGIPALTLE 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 192 MGVGMRITEDYCHQLTDGIFCVMKKMGIWDGEVIEPKKPIISTDGQVGIINANEPGIFMPHVEHWDNIKKGDAIGVILNP 271
Cdd:COG3608   182 LGGGGRFDEESIEAGVRGILNVLRHLGMLDGEAPPPPLAPPVLARGSEWVRAPAGGLFEPLVELGDRVKKGDVLGRITDP 261

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1334692452 272 LqGTVAETLYAPFDGMVFTLREYPVVNSGSLIARI 306
Cdd:COG3608   262 F-GEEVEEVRAPVDGIVIGRRTNPLVNPGDALFHI 295
M14_ASTE_ASPA_like cd06230
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA) subfamily; The ...
 35-211 1.38e-39

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: 137.06  E-value: 1.38e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  35 ICVVTGTHGDELEGQYVCYELIRRINENKehLKGIVDIFPALNPLGIDSVTRGIPMFDLDMNRIFPGSESGSVPEYVASK 114
Cdd:cd06230     1 LLILAGVHGDEYEGVEAIRRLLAELDPSE--LKGTVVLVPVANPPAFEAGTRYTPLDGLDLNRIFPGDPDGSPTERLAHE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 115 IVEDIA-GADLCIDIHASNIFlREIPQVRM--SEGTAEKLLPYAKVLNIDYVWVYaaATVLEATLAHSLNTIGVPTLVVE 191
Cdd:cd06230    79 LTELILkHADALIDLHSGGTG-RLVPYAILdyDSDAREKSRELARAFGGTPVIWG--GDPPGGTPVAAARSAGIPAITVE 155

                         170       180
                  ....*....|....*....|
gi 1334692452 192 MGVGMRITEDYCHQLTDGIF 211
Cdd:cd06230   156 LGGGGRLRAERLERYLRGIR 175
M14_ASTE_ASPA-like cd06251
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 33-219 6.54e-27

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: 104.16  E-value: 6.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  33 KRICVVTGTHGDELEGQYVCYELIRRINenKEHLKGIVDIFPALNPLGIDSVTRGIPMFDLDMNRIFPGSESGSVPEYVA 112
Cdd:cd06251    13 PTLLLTAAIHGDELNGIEVIQRLLEDLD--PSKLRGTLIAIPVVNPLGFENNSRYLPDDGRDLNRSFPGSEKGSLASRLA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 113 SKIVEDI-AGADLCIDIHASNIFLREIPQVR--MSEGTAEKLlpyAKVLNIDYVwvyAAATVLEATLAHSLNTIGVPTLV 189
Cdd:cd06251    91 HLLWNEIvKKADYVIDLHTASTGRTNLPYVRadLRDPESRRM---AEAFGAPVI---VDDPGEDGSLRGAAVELGIPAIT 164

                         170       180       190
                  ....*....|....*....|....*....|
gi 1334692452 190 VEMGVGMRITEDYCHQLTDGIFCVMKKMGI 219
Cdd:cd06251   165 VELGEALRFDEDIIRRGVEGVLNVLRHLGM 194
AstE_AspA pfam04952
Succinylglutamate desuccinylase / Aspartoacylase family; This family includes ...
 33-306 8.98e-25

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: 100.89  E-value: 8.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  33 KRICVVTGTHGDELEGQYVCYELIRRINENKehLKGIVDIFPALNPLGIDSVTRGIPMfdlDMNRIFPGSESGSVPEY-- 110
Cdd:pfam04952   3 PTLLLSAGIHGNETNGVELLRRLLRQLDPGD--IAGERTLVPLANPPAFRAGSRYIPR---DLNRSFPGRALGASSDEpy 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 111 ---VASKIV-----EDIAGADLCIDIHASNIFLREIPQVRMSEGTA-EKLLPYAKVLNIDYVWV---YAAATVLEATLAH 178
Cdd:pfam04952  78 ratRAERLAdlffpALLPRADIVLDLHTGTRGMGHLLFALAPIRDDpLHLLALLRAFGAPAVLKlhsKPSAGFSAFSAEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 179 slntIGVPTLVVEMGVGMRITEDYCHQLTDGIFCVMKKMGIWDGEVIEPKKPIISTDGQVGI----INANEPGIFMPHVE 254
Cdd:pfam04952 158 ----LGAPGFTLELGGAGPFGANLISRTAAGVLNVLRLIGVLNGGPDAFEPPKLYRVLREIDrprdIRAELAGLVEFALN 233

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1334692452 255 HWDNIKKGDAI--GVILNPLQGTVAETLyAPFDGMVFTLREYPVVNSGSLIARI 306
Cdd:pfam04952 234 LGDDVDAGPLLpgGPLFAPFGGEETEYR-APEDGYPVFPNEAAYVGKGAALALV 286
M14_ASTE_ASPA-like cd06255
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 42-220 3.60e-24

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: 97.78  E-value: 3.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  42 HGDELEGQYVCYELIRRINENKehLKGIVDIFPALNPLGIDSVTRGIPMFDLDMNRIFPGSESGSVPEYVASKIVEDIAG 121
Cdd:cd06255    33 HGDELNGPLAALELFRELDPAQ--LSGTLVATPIANPLAFQGRQKFSPQDGEDLDQSFPGDPDGLITERMAHALFSEVKE 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 122 -ADLCIDIHASNIFLREIPQVR------MSEGTAEKLLPYAKVLNID---YVWVYAAATVLEATLAHSLN----TIGVPT 187
Cdd:cd06255   111 vADYLIDFHTGGTPFDANPYTVyklfpeSGPVEEKRLLRLARAFGVHancRVDVSGAGGELPGNTAGALDyqcmAQGIPA 190

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1334692452 188 LVVEMGVGMRITEDYCHQLTDGIFCVMKKMGIW 220
Cdd:cd06255   191 FMVELGGGGRAEEEAVRFAARGLRNLLRYLGML 223
M14_ASTE_ASPA-like cd06252
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 40-199 6.98e-18

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: 80.69  E-value: 6.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  40 GTHGDELEGQYVCYELIRRINEnkEHLKGIVDIFPALNPLGIDSVTRGIPMFDLDMNRIFPGSESGSVPEYVASKIVEDI 119
Cdd:cd06252    42 GNHGDEYEGPIALRRLARDLDP--EDVRGRLIIVPALNLPAVRAGTRTSPLDGGNLNRAFPGDADGTPTERIAHFLETVL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 120 -AGADLCIDIHASNIFLREIPQVRMS-EGTAE---KLLPYAKVLNIDYVWVYAA--ATVLEATLAHSLntiGVPTLVVEM 192
Cdd:cd06252   120 lPRADAVIDLHSGGSSLDFVPCAAVHlLPDPAqraRSLALAEAFGAPLSVVVDNvdAPGTLDSAAERA---GKIFVSTEL 196


                  ....*..
gi 1334692452 193 GVGMRIT 199
Cdd:cd06252   197 GGGGTVT 203
M14_ASTE_ASPA-like cd06254
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 33-216 5.43e-14

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: 69.15  E-value: 5.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  33 KRICVVTGTHGDELEGQYVCYELIRRINENKehLKGIVDIFPALNPLGIDSVTRGI-PMFDLDMNRIFPGSESGSVPEYV 111
Cdd:cd06254    12 PTLLITAGIHGGEYPGILAAIRLARELDPAD--VKGTLIIVHIANVSGFEARTPFVvPEDGKNLNRVFPGDPDGTLTERI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 112 ASKIVEDI-AGADLCIDIHASNIFLREIPQV----RMSEGTAEKLLPYAKVLNIDYVWVYAA--ATVLEATLAhslnTIG 184
Cdd:cd06254    90 AYFLTREIiSRADFLIDLHGGDANEALTPFVyypgGASEEVNDISRAAAQALGLPYIVISSSekGTGYYSYAA----LRG 165

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1334692452 185 VPTLVVEMGVGMRITEDYCHQLTDGIFCVMKK 216
Cdd:cd06254   166 IPSILVERGGLGTCDEEDVQAHKDGIKNLLRH 197
M14_ASTE_ASPA_like cd18174
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like; ...
 35-214 6.08e-13

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: 66.11  E-value: 6.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  35 ICVVTGTHGDELEGQYVCYELIRRINENKehLKGIVDIFPALNPLGIDSvtRGI---PMFDLDMNRIFPGSESGSVPEYV 111
Cdd:cd18174     1 LLVTAGVHGYEYASIEALQRLIKELDPAK--LSGTVIVVPIANIPAFEG--RSIyvnPLDGKNLNRSFPGDPDGTPTERL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452 112 ASKIVED-IAGADLCIDIHASNIFLREIPQVRMSEGTAEKL----LPYAKVLNIDYVWVYAAATvleATLAHSLNT---- 182
Cdd:cd18174    77 AHWLTTNvIARADYYIDLHGGDLNEDLRPFVYYYETGNAALdaasREMAEAFGLDHIVFYKARL---KASRGSLYTqaaa 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1334692452 183 --IGVPTLVVEMGVGMRITEDYCHQLTDGIFCVM 214
Cdd:cd18174   154 llRGIPAILVEAGGLGSRDEEDVARHVEGVLNVL 187
M14_MpaA-like cd06904
Peptidase M14-like domain of Escherichia coli Murein Peptide Amidase A and related proteins; ...
 23-100 3.13e-08

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: 53.05  E-value: 3.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  23 LMPESLTGHEKRICVVTGTHGDELEGQYVCYELIRRINENKEHLKGIVDIFPALNPLGIDSVTR----GIpmfdlDMNRI 98
Cdd:cd06904    14 LAYKFGPGSRARILIIGGIHGDEPEGVSLVEHLLRWLKNHPASGDFHIVVVPCLNPDGLAAGTRtnanGV-----DLNRN 88


                  ..
gi 1334692452  99 FP 100
Cdd:cd06904    89 FP 90
M14_ASTE_ASPA_like cd18430
Succinylglutamate desuccinylase/aspartoacylase; uncharacterized; A functionally ...
 35-131 3.81e-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: 46.28  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  35 ICVVTGTHGDELEGQYVCYELIRRINENKEhLKGIVDIFPAlNPLGIdsvTRGIPMFDLDMNRIFPGSESGSVPE-YVAS 113
Cdd:cd18430     1 LAVLGAVHGNETCGTRAVERLLAELPSGAL-QKGPVTLVPA-NERAY---AEGVRFCEEDLNRVFPGDPDPDTYErRLAN 75

                          90
                  ....*....|....*...
gi 1334692452 114 KIVEDIAGADLCIDIHAS 131
Cdd:cd18430    76 RLCPELEGHDVVLDLHST 93
M14_ASPA cd06909
Peptidase M14 Aspartoacylase (ASPA) subfamily; Aspartoacylase (ASPA) belongs to the ...
 33-129 3.09e-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: 44.12  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  33 KRICVVTGTHGDELEGQYvcyeLIRRINENKEHL--KGI-VDIFPAlNPLGIDSVTRGIpmfDLDMNRIFPGSESGSVPE 109
Cdd:cd06909     1 KRVAIVGGTHGNELTGVY----LVKHWLKNPELIerKSFeVHPLLA-NPRAVEQCRRYI---DTDLNRCFSLENLSSAPS 72

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1334692452 110 YV------ASKIVEDIAGA-----DLCIDIH 129
Cdd:cd06909    73 SLpyevrrAREINQILGPKgnpacDFIIDLH 103
M14_REP34-like cd06231
Peptidase M14-like domain similar to rapid encystment phenotype 34 (REP34); This family ...
 33-129 2.28e-04

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


Pssm-ID: 349450 [Multi-domain]  Cd Length: 239  Bit Score: 41.91  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  33 KRICVVTGTHGDELEGqyvCYELIRRINENKEH-LKGI-VDIFPALNPLGIDSVTR----GIpmfdlDMNRIF-PGSESg 105
Cdd:cd06231    43 PRVLISAGIHGDEPAG---VEALLRFLESLAEKyLRRVnLLVLPCVNPWGFERNTRenadGI-----DLNRSFlKDSPS- 113

                          90       100
                  ....*....|....*....|....*
gi 1334692452 106 svPEYVA-SKIVEDIAGADLCIDIH 129
Cdd:cd06231   114 --PEVRAlMEFLASLGRFDLHLDLH 136
AstE COG2988
Succinylglutamate desuccinylase [Amino acid transport and metabolism];
32-133 3.14e-04

Succinylglutamate desuccinylase [Amino acid transport and metabolism];


Pssm-ID: 442227  Cd Length: 305  Bit Score: 41.76  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334692452  32 EKRICVVTGTHGDELEGQYVCYELIRRInenkeHLKGIVDIFPAL----NPLGIDSVTRGIpmfDLDMNRIFPGSESGSV 107
Cdd:COG2988    24 IKAVVISGGIHGNETAPIELLDKLLQDL-----LLGERPLSFRLLlilgNPAAMRAGRRYL---DEDLNRLFGGRHLQNP 95

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1334692452 108 --PEYVASKIVEDIAGA--------DLCIDIHaSNI 133
Cdd:COG2988    96 esYEAARAKELEQAVGPffaaggrvRLHIDLH-TAI 130
M14_PaAOTO_like cd06250
Peptidase M14 Succinylglutamate desuccinylase (ASTE)/aspartoacylase (ASPA)-like subfamily; ...
 42-100 1.41e-03

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: 39.53  E-value: 1.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1334692452  42 HGDELEGQYVCYELIRRIN--ENKEHLKGIVDIFPALNPLGIDSVTRGIPM--FDLD----MNRIFP 100
Cdd:cd06250    37 HADELPGNLVIHHLLERLKalEAAGRIKGEIVLVPQANPIGLSQKIGGYHQgrFDLAtgdnFNRNFP 103
Peptidase_M14_like cd00596
M14 family of metallocarboxypeptidases and related proteins; The M14 family of ...
 37-100 1.84e-03

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


Pssm-ID: 349427 [Multi-domain]  Cd Length: 216  Bit Score: 38.98  E-value: 1.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1334692452  37 VVTGTHGDELEGQYVCYELIRRINEN--KEHLKGIVD-----IFPALNPLG----IDSVTRGiPMFDLDMNRIFP 100
Cdd:cd00596     3 ITGGIHGNEVIGVELALALIEYLLENygNDPLKRLLDnvelwIVPLVNPDGfarvIDSGGRK-NANGVDLNRNFP 76
 
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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