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Conserved domains on  [gi|157831451]
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Chain A, AMINOPEPTIDASE

Protein Classification

M28 family metallopeptidase( domain architecture ID 10133839)

M28 family metallopeptidase similar to leucine aminopeptidase that catalyzes the release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M28_AAP cd03879
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ...
 3-287 1.48e-149

M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; Aeromonas (Vibrio) proteolytica aminopeptidase (AAP; leucine aminopeptidase from Vibrio proteolyticus; Bacterial leucyl aminopeptidase; E.C. 3.4.11.10) subfamily. AAP is a small (32kDa), heat stable leucine aminopeptidase and is active as a monomer. Similar forms of the enzyme have been isolated from Escherichia coli and Staphylococcus thermophilus. Leucine aminopeptidases, in general, play important roles in many biological processes such as protein catabolism, hormone degradation, regulation of migration and cell proliferation, as well as HIV infection and proliferation. AAP is a broad-specificity enzyme, utilizing two zinc(II) ions in its active site to remove N-terminal amino acids, with preference for large hydrophobic amino acids in the P1 position of the substrate, Leu being the most efficiently cleaved. It can accommodate all residues, except Pro, Asp and Glu in the P1' position.


:

Pssm-ID: 349875 [Multi-domain]  Cd Length: 286  Bit Score: 420.11  E-value: 1.48e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451   3 PITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTTSGAQASDWIASEWQALSASLP--NASVKQVSHSgYNQKSVVM 80
Cdd:cd03879    1 PITHQATVNSLLPQLSKSNMQDTLESLTSFNNRYYKSQTGVESAEWLLDQVQAIIASSGrsGATVEQFTHS-FPQPSIIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  81 TITGSEAPDEWIVIGGHLDSTIGSHTNeQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRGSQD 160
Cdd:cd03879   80 TIPGSEKSDEIVVIGAHQDSINGSNPS-NGRAPGADDDGSGTVTILEALRVLLESGFQPKNTIEFHWYAAEEGGLLGSQA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 161 LANQYKSEGKNVVSALQLDMTNYK--GSAQDVVFITDYTDSNFTQYLTQLMDEYLPsLTYGFDTCGYACSDHASWHNAGY 238
Cdd:cd03879  159 IATQYKSEGKNVKAMLQLDMTGYVkpGSAEDIGLITDYTDSNLTQFLKQLIDEYLP-IPYGDTKCGYACSDHASWTKAGY 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 157831451 239 PAAMPFESKFNDYNPRIHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMG 287
Cdd:cd03879  238 PAAFPFESAFEDYNPYIHTTNDTLDNSGLSFDHMLEFAKLALAFAVELG 286
 
Name Accession Description Interval E-value
M28_AAP cd03879
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ...
 3-287 1.48e-149

M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; Aeromonas (Vibrio) proteolytica aminopeptidase (AAP; leucine aminopeptidase from Vibrio proteolyticus; Bacterial leucyl aminopeptidase; E.C. 3.4.11.10) subfamily. AAP is a small (32kDa), heat stable leucine aminopeptidase and is active as a monomer. Similar forms of the enzyme have been isolated from Escherichia coli and Staphylococcus thermophilus. Leucine aminopeptidases, in general, play important roles in many biological processes such as protein catabolism, hormone degradation, regulation of migration and cell proliferation, as well as HIV infection and proliferation. AAP is a broad-specificity enzyme, utilizing two zinc(II) ions in its active site to remove N-terminal amino acids, with preference for large hydrophobic amino acids in the P1 position of the substrate, Leu being the most efficiently cleaved. It can accommodate all residues, except Pro, Asp and Glu in the P1' position.


Pssm-ID: 349875 [Multi-domain]  Cd Length: 286  Bit Score: 420.11  E-value: 1.48e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451   3 PITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTTSGAQASDWIASEWQALSASLP--NASVKQVSHSgYNQKSVVM 80
Cdd:cd03879    1 PITHQATVNSLLPQLSKSNMQDTLESLTSFNNRYYKSQTGVESAEWLLDQVQAIIASSGrsGATVEQFTHS-FPQPSIIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  81 TITGSEAPDEWIVIGGHLDSTIGSHTNeQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRGSQD 160
Cdd:cd03879   80 TIPGSEKSDEIVVIGAHQDSINGSNPS-NGRAPGADDDGSGTVTILEALRVLLESGFQPKNTIEFHWYAAEEGGLLGSQA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 161 LANQYKSEGKNVVSALQLDMTNYK--GSAQDVVFITDYTDSNFTQYLTQLMDEYLPsLTYGFDTCGYACSDHASWHNAGY 238
Cdd:cd03879  159 IATQYKSEGKNVKAMLQLDMTGYVkpGSAEDIGLITDYTDSNLTQFLKQLIDEYLP-IPYGDTKCGYACSDHASWTKAGY 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 157831451 239 PAAMPFESKFNDYNPRIHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMG 287
Cdd:cd03879  238 PAAFPFESAFEDYNPYIHTTNDTLDNSGLSFDHMLEFAKLALAFAVELG 286
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 38-290 1.38e-65

Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];


Pssm-ID: 441835 [Multi-domain]  Cd Length: 257  Bit Score: 205.75  E-value: 1.38e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  38 TTTSGAQASDWIASEWQALSASLPNASVKQVSHSGYNQKSVVMTITGSEAPDEWIVIGGHLDStIGShtneqsVAPGADD 117
Cdd:COG2234    9 GGTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDEVVVLGAHYDS-VGS------IGPGADD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 118 DASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRGSQDLANQYKSEGKNVVSALQLDMTNYKGSAQDVVFITDYT 197
Cdd:COG2234   82 NASGVAALLELARALAALGPKPKRTIRFVAFGAEEQGLLGSRYYAENLKAPLEKIVAVLNLDMIGRGGPRNYLYVDGDGG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 198 DSNFTQYLTQLMDEYLPSLT--YGFDTCGYACSDHASWHNAGYPAAMPFESKFnDYNPRIHTTQDTLANSDPTgsHAKKF 275
Cdd:COG2234  162 SPELADLLEAAAKAYLPGLGvdPPEETGGYGRSDHAPFAKAGIPALFLFTGAE-DYHPDYHTPSDTLDKIDLD--ALAKV 238

                        250
                 ....*....|....*
gi 157831451 276 TQLGLAYAIEMGSAT 290
Cdd:COG2234  239 AQLLAALVYELANAD 253
Peptidase_M28 pfam04389
Peptidase family M28;
78-281 5.84e-52

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 168.62  E-value: 5.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451   78 VVMTITGSeAPDEWIVIGGHLDSTigshtneqSVAPGADDDASGIAAVTEVIRVLSeNNFQPKRSIAFMAYAAEEVGLRG 157
Cdd:pfam04389   2 VIAKLPGK-APDEVVLLSAHYDSV--------GTGPGADDNASGVAALLELARVLA-AGQRPKRSVRFLFFDAEEAGLLG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  158 SQDLANQyKSEGKNVVSALQLDMTNYKGSAQDvVFITDYTDSNFTQYLTQLMDEYLPSL--TYGFDTCGYACSDHASWHN 235
Cdd:pfam04389  72 SHHFAKS-HPPLKKIRAVINLDMIGSGGPALL-FQSGPKGSSLLEKYLKAAAKPYGVTLaeDPFQERGGPGRSDHAPFIK 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157831451  236 AGYPAAMPfesKFNDYNPRIHTTQDTLANSDPTGSHAKKFTQLGLA 281
Cdd:pfam04389 150 AGIPGLDL---AFTDFGYRYHTPADTIDNIDPGTLQRIGDLVLALV 192
PRK09290 PRK09290
allantoate amidohydrolase; Reviewed
 78-162 4.87e-05

allantoate amidohydrolase; Reviewed


Pssm-ID: 236456 [Multi-domain]  Cd Length: 413  Bit Score: 44.38  E-value: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  78 VVMTITGSEAPDEWIVIGGHLDSTIGShtneqsvapGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEE----- 152
Cdd:PRK09290  62 LFGRLEGRDPDAPAVLTGSHLDTVPNG---------GRFDGPLGVLAGLEAVRTLNERGIRPRRPIEVVAFTNEEgsrfg 132

                         90
                 ....*....|
gi 157831451 153 VGLRGSQDLA 162
Cdd:PRK09290 133 PAMLGSRVFT 142
 
Name Accession Description Interval E-value
M28_AAP cd03879
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ...
 3-287 1.48e-149

M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; Aeromonas (Vibrio) proteolytica aminopeptidase (AAP; leucine aminopeptidase from Vibrio proteolyticus; Bacterial leucyl aminopeptidase; E.C. 3.4.11.10) subfamily. AAP is a small (32kDa), heat stable leucine aminopeptidase and is active as a monomer. Similar forms of the enzyme have been isolated from Escherichia coli and Staphylococcus thermophilus. Leucine aminopeptidases, in general, play important roles in many biological processes such as protein catabolism, hormone degradation, regulation of migration and cell proliferation, as well as HIV infection and proliferation. AAP is a broad-specificity enzyme, utilizing two zinc(II) ions in its active site to remove N-terminal amino acids, with preference for large hydrophobic amino acids in the P1 position of the substrate, Leu being the most efficiently cleaved. It can accommodate all residues, except Pro, Asp and Glu in the P1' position.


Pssm-ID: 349875 [Multi-domain]  Cd Length: 286  Bit Score: 420.11  E-value: 1.48e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451   3 PITQQATVTAWLPQVDASQITGTISSLESFTNRFYTTTSGAQASDWIASEWQALSASLP--NASVKQVSHSgYNQKSVVM 80
Cdd:cd03879    1 PITHQATVNSLLPQLSKSNMQDTLESLTSFNNRYYKSQTGVESAEWLLDQVQAIIASSGrsGATVEQFTHS-FPQPSIIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  81 TITGSEAPDEWIVIGGHLDSTIGSHTNeQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRGSQD 160
Cdd:cd03879   80 TIPGSEKSDEIVVIGAHQDSINGSNPS-NGRAPGADDDGSGTVTILEALRVLLESGFQPKNTIEFHWYAAEEGGLLGSQA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 161 LANQYKSEGKNVVSALQLDMTNYK--GSAQDVVFITDYTDSNFTQYLTQLMDEYLPsLTYGFDTCGYACSDHASWHNAGY 238
Cdd:cd03879  159 IATQYKSEGKNVKAMLQLDMTGYVkpGSAEDIGLITDYTDSNLTQFLKQLIDEYLP-IPYGDTKCGYACSDHASWTKAGY 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 157831451 239 PAAMPFESKFNDYNPRIHTTQDTLANSDPTGSHAKKFTQLGLAYAIEMG 287
Cdd:cd03879  238 PAAFPFESAFEDYNPYIHTTNDTLDNSGLSFDHMLEFAKLALAFAVELG 286
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 75-286 1.47e-66

M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases.


Pssm-ID: 349868 [Multi-domain]  Cd Length: 202  Bit Score: 206.43  E-value: 1.47e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  75 QKSVVMTITGSEAPDEWIVIGGHLDSTIgshtneqsVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVG 154
Cdd:cd02690    1 GYNVIATIKGSDKPDEVILIGAHYDSVP--------LSPGANDNASGVAVLLELARVLSKLQLKPKRSIRFAFWDAEELG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 155 LRGSQDLANQYKSEGKNVVSALQLDMTNYKGsaQDVVFITDY-TDSNFTQYLTQLMDEYLPSLTYGF--DTCGYACSDHA 231
Cdd:cd02690   73 LLGSKYYAEQLLSSLKNIRAALNLDMIGGAG--PDLYLQTAPgNDALVEKLLRALAHELENVVYTVVykEDGGTGGSDHR 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157831451 232 SWHNAGYPAAMPFESKFnDYNPRIHTTQDTLANSDptGSHAKKFTQLGLAYAIEM 286
Cdd:cd02690  151 PFLARGIPAASLIQSES-YNFPYYHTTQDTLENID--KDTLKRAGDILASFLYRL 202
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 38-290 1.38e-65

Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];


Pssm-ID: 441835 [Multi-domain]  Cd Length: 257  Bit Score: 205.75  E-value: 1.38e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  38 TTTSGAQASDWIASEWQALSASLPNASVKQVSHSGYNQKSVVMTITGSEAPDEWIVIGGHLDStIGShtneqsVAPGADD 117
Cdd:COG2234    9 GGTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDEVVVLGAHYDS-VGS------IGPGADD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 118 DASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRGSQDLANQYKSEGKNVVSALQLDMTNYKGSAQDVVFITDYT 197
Cdd:COG2234   82 NASGVAALLELARALAALGPKPKRTIRFVAFGAEEQGLLGSRYYAENLKAPLEKIVAVLNLDMIGRGGPRNYLYVDGDGG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 198 DSNFTQYLTQLMDEYLPSLT--YGFDTCGYACSDHASWHNAGYPAAMPFESKFnDYNPRIHTTQDTLANSDPTgsHAKKF 275
Cdd:COG2234  162 SPELADLLEAAAKAYLPGLGvdPPEETGGYGRSDHAPFAKAGIPALFLFTGAE-DYHPDYHTPSDTLDKIDLD--ALAKV 238

                        250
                 ....*....|....*
gi 157831451 276 TQLGLAYAIEMGSAT 290
Cdd:COG2234  239 AQLLAALVYELANAD 253
Peptidase_M28 pfam04389
Peptidase family M28;
78-281 5.84e-52

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 168.62  E-value: 5.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451   78 VVMTITGSeAPDEWIVIGGHLDSTigshtneqSVAPGADDDASGIAAVTEVIRVLSeNNFQPKRSIAFMAYAAEEVGLRG 157
Cdd:pfam04389   2 VIAKLPGK-APDEVVLLSAHYDSV--------GTGPGADDNASGVAALLELARVLA-AGQRPKRSVRFLFFDAEEAGLLG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  158 SQDLANQyKSEGKNVVSALQLDMTNYKGSAQDvVFITDYTDSNFTQYLTQLMDEYLPSL--TYGFDTCGYACSDHASWHN 235
Cdd:pfam04389  72 SHHFAKS-HPPLKKIRAVINLDMIGSGGPALL-FQSGPKGSSLLEKYLKAAAKPYGVTLaeDPFQERGGPGRSDHAPFIK 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157831451  236 AGYPAAMPfesKFNDYNPRIHTTQDTLANSDPTGSHAKKFTQLGLA 281
Cdd:pfam04389 150 AGIPGLDL---AFTDFGYRYHTPADTIDNIDPGTLQRIGDLVLALV 192
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 72-278 2.98e-38

M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Some proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.


Pssm-ID: 349874 [Multi-domain]  Cd Length: 206  Bit Score: 133.91  E-value: 2.98e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  72 GYNqksVVMTITGSEAPDEWIVIGGHLDST-IGSHTNEQSVAPGADDDASGIAAVTEVIRVLSENNfQPKRSIAFMAYAA 150
Cdd:cd03877    1 GHN---VVGVLEGSDLPDETIVIGAHYDHLgIGGGDSGDKIYNGADDNASGVAAVLELARYFAKQK-TPKRSIVFAAFTA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 151 EEVGLRGSQDLANQYKSEGKNVVSALQLDMTNyKGSAQDVVFITDYTDSNFTQYLTQLMDEYLPSLTY-GFDTCGYACSD 229
Cdd:cd03877   77 EEKGLLGSKYFAENPKFPLDKIVAMLNLDMIG-RLGRSKDVYLIGSGSSELENLLKKANKAAGRVLSKdPLPEWGFFRSD 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157831451 230 HASWHNAGYPA--AMPFEskFNDYnpriHTTQDTLANSDPtgSHAKKFTQL 278
Cdd:cd03877  156 HYPFAKAGVPAlyFFTGL--HDDY----HKPSDDYEKIDY--EGMARVVNL 198
Zinc_peptidase_like cd03873
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ...
 78-278 2.83e-36

Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).


Pssm-ID: 349870 [Multi-domain]  Cd Length: 200  Bit Score: 128.70  E-value: 2.83e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  78 VVMTITGSEaPDEWIVIGGHLDSTIGSHTNE-------------QSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIA 144
Cdd:cd03873    2 LIARLGGGE-GGKSVALGAHLDVVPAGEGDNrdppfaedteeegRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 145 FMAYAAEEVGLRGSQDLAN-QYKSEGKNVVSALQLDMTNYKGSAQDVVFITDytdsnFTQYLTQLMDEYLPSLTygFDTC 223
Cdd:cd03873   81 VAFTADEEVGSGGGKGLLSkFLLAEDLKVDAAFVIDATAGPILQKGVVIRNP-----LVDALRKAAREVGGKPQ--RASV 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157831451 224 GYACSDHASWHNAGYPAAMPFESkfndYNPRIHTTQDTLansdpTGSHAKKFTQL 278
Cdd:cd03873  154 IGGGTDGRLFAELGIPGVTLGPP----GDKGAHSPNEFL-----NLDDLEKATKV 199
M28_like cd05642
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 5-180 1.17e-30

M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.


Pssm-ID: 349894 [Multi-domain]  Cd Length: 347  Bit Score: 117.59  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451   5 TQQATVTAWLPQVDASQITGTISSLESFTNR--FYTTTSGAQ----ASDWIASEWQALSASlpNASVKQVSHSGYNQ--- 75
Cdd:cd05642    2 LPDDELQAILSEVDPKRIEATIRKLVSFGTRhtLSTQTDPTRgigaARDWIAEEFREYAAA--SGGRMTVEVPSYVQgpa 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  76 ---------KSVVMTITGSEAPDEWIVIGGHLDSTIGSHTNEQSVAPGADDDASGIAAVTEVIRVLSENnfQPKRSIAFM 146
Cdd:cd05642   80 sripfpvniSNVVATLKGSEDPDRVYVVSGHYDSRVSDVMDYESDAPGANDDASGVAVSMELARIFAKH--RPKATIVFT 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 157831451 147 AYAAEEVGLRGSQDLANQYKSEGKNVVSALQLDM 180
Cdd:cd05642  158 AVAGEEQGLYGSTFLAQTYRNNSVNVEGMLNNDI 191
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 25-240 3.11e-29

M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.


Pssm-ID: 349910 [Multi-domain]  Cd Length: 290  Bit Score: 112.45  E-value: 3.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  25 TISSLEsFTNRFYTTTSGAQASDWIASEWQALSASLPNAS------VKQVSHSGY-NQKSVVMTITGSEAPDEWIVIGGH 97
Cdd:cd05660    3 FLASDE-FEGRAPGSEGEKKTVDYLAEQFKELGLKPAGSDgsylqaVPLVSKIEYsTSHNVVAILPGSKLPDEYIVLSAH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  98 LDST-IGSHTNEQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRGSQDLANQYKSEGKNVVSAL 176
Cdd:cd05660   82 WDHLgIGPPIGGDEIYNGAVDNASGVAAVLELARVFAAQDQRPKRSIVFLAVTAEEKGLLGSRYYAANPIFPLDKIVANL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157831451 177 QLDMTNYKGSAQDVVFItDYTDSNFTQYLTQLMDEYLPSLTYGF--DTCGYACSDHASWHNAGYPA 240
Cdd:cd05660  162 NIDMIGRIGPTKDVLLI-GSGSSELENILKEAAKAVGRVVDYDPnpENGSFYRSDHYNFAKKGVPV 226
M28_Pgcp_like cd03883
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate ...
 78-267 1.61e-26

M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate carboxypeptidase (PGCP; blood plasma glutamate carboxypeptidase; EC 3.4.17.21) subfamily. PGCP is a 56kDa glutamate carboxypeptidase that is mainly produced in mammalian placenta and kidney, the majority of which is thought to be secreted into the bloodstream. Similar proteins are also found in other species, including bacteria. These proteins contain protease-associated (PA) domain inserts between the first and second strands of the central beta sheet in the protease-like domain. The PA domains may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. The exact physiological substrates of PGCP are unknown, although this enzyme may play an important role in the hydrolysis of circulating peptides. Its closest homolog encodes an important brain glutamate carboxypeptidase II (NAALADase) identical to the prostate-specific membrane antigen (PSMA), which serves as a marker for prostatic cancer metastasis. Hypermethylation of PGCP gene has been associated with human bronchial epithelial (HBE) cell immortalization and lung cancer. PGCP also provides an attractive target for serological analysis in hepatitis C virus (HCV)-induced hepatocellular carcinoma (HCC) patients.


Pssm-ID: 349879 [Multi-domain]  Cd Length: 425  Bit Score: 107.40  E-value: 1.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  78 VVMTITGSEAPDEWIVIGGHLDStigshtneQSVAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRG 157
Cdd:cd03883  229 VIAEITGSKYPDEVVLVGGHLDS--------WDVGTGAMDDGGGVAISWEALKLIKDLGLKPKRTIRVVLWTGEEQGLVG 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 158 SQDLANQYKSEGKNVVSALQLDMtnykGSAQDVVFitDYTDSNFTQYLTQLMDEYL-PSLTYGFDTCGYACSDHASWHNA 236
Cdd:cd03883  301 AKAYAEAHKDELENHVFAMESDI----GTFTPYGL--QFTGSDTARAIVKEVMKLLsPLGITQVLPKAGVGPDISFLKAA 374

                        170       180       190
                 ....*....|....*....|....*....|...
gi 157831451 237 GYPAA--MPFESKFNDYNpriHTTQDTLANSDP 267
Cdd:cd03883  375 GVPGAslIQDNSDYFDYH---HTAGDTMDVMDP 404
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 34-263 7.68e-22

M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.


Pssm-ID: 349893 [Multi-domain]  Cd Length: 281  Bit Score: 92.51  E-value: 7.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  34 NRFYTTTSGAQASDWIASEWQALSAslpNASVKQVSHSGYNQKSVVMTITGSEAPDEWIVIGGHLDSTIGShtneqsvaP 113
Cdd:cd05640   14 NPHDPSAFLAAAAEYIAQELVGSGY---NVTSHFFSHQEGVYANLIADLPGSYSQDKLILIGAHYDTVPGS--------P 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 114 GADDDASGIAAVTEVIRVLSENnfQPKRSIAFMAYAAEEV-----GLRGSQDLANQYKSEGKNVVSALQLDMTNYKGSAQ 188
Cdd:cd05640   83 GADDNASGVAALLELARLLATL--DPNHTLRFVAFDLEEYpffarGLMGSHAYAEDLLRPLTPIVGMLSLEMIGYYDPFP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 189 D-------------------VVFITDYTDSNFTQYLTQLMD-------EYLPSLTYGFDTCGYACSDHASWHNAGYPAAM 242
Cdd:cd05640  161 HsqaypagfelhfyphmgdfIAVVGRLRSRKLVRAFKRAFRmlsdfpvESLNLPFNGPGVPPFRRSDHSSFWDHGYPAIM 240

                        250       260
                 ....*....|....*....|.
gi 157831451 243 PFESKFNDyNPRIHTTQDTLA 263
Cdd:cd05640  241 VTDTAFYR-NPQYHLPCDTPD 260
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 16-264 2.87e-21

M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.


Pssm-ID: 349911 [Multi-domain]  Cd Length: 262  Bit Score: 90.32  E-value: 2.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  16 QVDASQITGTISSLeSFTNRFYTTTSGAQASDWIASEWQALSASlpnasVKQVSHSGYNqksvvmtITGSEAPDEW---- 91
Cdd:cd05661   10 RVDAENAYNHIRFL-SQAIGVAGTPEELKAARYIEQQLKSLGYE-----VEVQPFTSHN-------VIATKKPDNNknnn 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  92 --IVIGGHLDSTIGshtneqsvAPGADDDASGIAAVTEVIRVLSenNFQPKRSIAFMAYAAEEVGLRGSQDLANQY-KSE 168
Cdd:cd05661   77 diIIVTSHYDSVVK--------APGANDNASGTAVTLELARVFK--KVKTDKELRFIAFGAEENGLLGSKYYVASLsEDE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 169 GKNVVSALQLDM--TNYKgSAQDVVFITDYTDSNftqYLTQLMDEYLPSLTYGFDTCGYACSDHASWHNAGYPAAMPFES 246
Cdd:cd05661  147 IKRTIGVFNLDMvgTSDA-KAGDLYAYTIDGKPN---LVTDSGAAASKRLSGVLPLVQQGSSDHVPFHEAGIPAALFIHM 222

                        250       260
                 ....*....|....*....|
gi 157831451 247 KFNDY--NPRIHTTQDTLAN 264
Cdd:cd05661  223 DPETEpvEPWYHTPNDTVEN 242
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
 38-261 4.16e-19

M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ domain; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.


Pssm-ID: 349913 [Multi-domain]  Cd Length: 266  Bit Score: 84.43  E-value: 4.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  38 TTTSGA-QASDWIASEWQALSAslpnasVKQVSHSGYNQKSVVMTITG----------SEAPDEWIVIGGHLDStIGsHT 106
Cdd:cd05663   14 TGTKGEkLAADYIAQRFEELGL------EPGLDNGTYFQPFEFTTGTGrnvigvlpgkGDVADETVVVGAHYDH-LG-YG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 107 NEQSVAP--------GADDDASGIAAVTEVIRVLSEN-NFQP-KRSIAFMAYAAEEVGLRGSQDLANQYKSEGKNVVSAL 176
Cdd:cd05663   86 GEGSLARgdeslihnGADDNASGVAAMLELAAKLVDSdTSLAlSRNLVFIAFSGEELGLLGSKHFVKNPPFPIKNTVYMI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 177 QLDMTNYKGSAQDVVFITDYTDSnftqyLTQLMDEYlpSLTYGF----DTCGYACSDHASWHNAGYPAAMPFESKFNDYn 252
Cdd:cd05663  166 NMDMVGRLRDNKLIVQGTGTSPG-----WEQLVQAR--NKATGFklilDPTGYGPSDHTSFYLDDVPVLHFFTGAHSDY- 237


                 ....*....
gi 157831451 253 priHTTQDT 261
Cdd:cd05663  238 ---HRPSDD 243
M28_PSMA_like cd08022
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ...
 27-180 3.24e-18

M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase II or GCP-II)-like subfamily. PSMA is a homodimeric type II transmembrane protein containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). PSMA is over-expressed predominantly in prostate cancer (PCa) as well as in the neovasculature of most solid tumors, but not in the vasculature of the normal tissues. PSMA is considered a biomarker for PCa and possibly for use as an imaging and therapeutic target. The extracellular domain of PSMA possesses two unique enzymatic functions: N-acetylated, alpha-linked acidic dipeptidase (NAALADase) which cleaves terminal glutamate from the neurodipeptide N-acetyl-aspartyl-glutamate (NAAG), and folate hydrolase (FOLH) which cleaves the terminal glutamates from gamma-linked polyglutamates (carboxypeptidase). A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. Inhibition of GCP-II has been shown to be effective in preclinical models of neurological disorders associated with excessive activation of glutamatergic systems. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants.


Pssm-ID: 349942 [Multi-domain]  Cd Length: 287  Bit Score: 82.28  E-value: 3.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  27 SSLESFTNRFY--TTTSGAQASDWIASEWQalSASLPNASVKQVSHSGYNqksVVMTITGSEAPDEWIVIGGHLDSTIgs 104
Cdd:cd08022   15 EWLRYYTSGPHlaGTEGNLELAQWTEDKWR--EFGLDDVELEEYDVPIWN---VIGTIRGSEEPDEYIILGNHRDAWV-- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 105 htneqsvaPGADDDASGIAAVTEVIRVLSE---NNFQPKRSIAFMAYAAEEVGLRGSQDLANQYKSE-GKNVVSALQLDM 180
Cdd:cd08022   88 --------FGAGDPNSGTAVLLEVARALGTllkKGWRPRRTIIFASWDAEEYGLIGSTEWVEENADWlQERAVAYLNVDV 159
M28_like cd05662
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ...
 25-267 5.65e-18

M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins that do not contain a protease-associated (PA) domain.


Pssm-ID: 349912 [Multi-domain]  Cd Length: 268  Bit Score: 81.36  E-value: 5.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  25 TISSlESFTNRFYTTTSGAQASDWIASEWQALSAsLPNASVKQVSHS------GYNQKSVVMTITGSEAPDEWIVIGGHL 98
Cdd:cd05662    8 ILSS-DKFEGRKTGTKGAAKTRAYIIERFKQIGL-LPWGDRFEHPFSytkrfsTRQGVNVLAVIKGSEPPTKWRVVSAHY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  99 DStIGSHTNEqsVAPGADDDASGIAAVTEVIRVLSENnfQPKRSIAFMAYAAEEVGLRGSQDLANQYKSEGKNVVSALQL 178
Cdd:cd05662   86 DH-LGIRGGK--IYNGADDNASGVAALLALAEYFKKH--PPKHNVIFAATDAEEPGLRGSYAFVEALKVPRAQIELNINL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 179 DMTNYkgSAQDVVFITDytDSNFTQYLTQLMDEYLP----SLTYGFDTCG-----YACSDHASWHNAGypaaMPFESKFN 249
Cdd:cd05662  161 DMISR--PERNELYVEG--ASQFPQLTSILENVKGTcikaLHPKDTDGSIgsidwTRASDHYPFHKAK----IPWLYFGV 232

                        250
                 ....*....|....*...
gi 157831451 250 DYNPRIHTTQDTLANSDP 267
Cdd:cd05662  233 EDHPDYHKPTDDFETIDQ 250
M28_like cd08015
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 72-261 2.09e-15

M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.


Pssm-ID: 349937 [Multi-domain]  Cd Length: 218  Bit Score: 73.40  E-value: 2.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  72 GYNqksVVMTITGSEAPDEWIVIGGHLDSTigsHTneqsvAPGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAE 151
Cdd:cd08015    1 TYN---VIAEIPGSDKKDEVVILGAHLDSW---HG-----ATGATDNGAGTAVMMEAMRILKAIGSKPKRTIRVALWGSE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 152 EVGLRGSQDLANQY---------KSEGKNVVSALQLDmtNYKG-----SAQDVVFITDYtdsnFTQYLTQLMDEYLPSLT 217
Cdd:cd08015   70 EQGLHGSRAYVEKHfgdpptmqlQRDHKKISAYFNLD--NGTGrirgiYLQGNLAAYPI----FSAWLYPFHDLGATTVI 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 157831451 218 ygfdTCGYACSDHASWHNAGYPaAMPFESKFNDYNPRI-HTTQDT 261
Cdd:cd08015  144 ----ERNTGGTDHAAFDAVGIP-AFQFIQDPWDYWTRThHTNRDT 183
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 61-179 8.97e-14

M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic reticulum metallopeptidase 1 (ERMP1; Felix-ina, FXNA or Fxna peptidase; KIAA1815) subfamily. ERMP1 is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organization of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolyzed has not yet been determined. Another member of this subfamily is the 24-kDa vacuolar protein (VP24) which is probably involved in the formation of intravacuolar pigmented globules (cyanoplasts) in highly anthocyanin-containing vacuoles; however, the biological function of the C-terminal region which includes the putative transmembrane metallopeptidase domain is unknown.


Pssm-ID: 349872 [Multi-domain]  Cd Length: 307  Bit Score: 70.31  E-value: 8.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  61 PNASVKQVSHSGYNQKSVVMTITGSEAPDE-WIVIGGHLDSTIGShtneqsvaPGADDDASGIAAVTEVIRVLSENNFQP 139
Cdd:cd03875   65 FNFLSSGMTLVYFEVTNIVVRISGKNSNSLpALLLNAHFDSVPTS--------PGATDDGMGVAVMLEVLRYLSKSGHQP 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 157831451 140 KRSIAFMAYAAEEVGLRGSQDLANQYKSEgKNVVSALQLD 179
Cdd:cd03875  137 KRDIIFLFNGAEENGLLGAHAFITQHPWA-KNVRAFINLE 175
M28_like cd05643
M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), ...
 85-268 6.87e-11

M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They typically have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This protein subfamily conserves some of the metal-coordinating residues of the typically co-catalytic M28 family which might suggest binding of a single metal ion.


Pssm-ID: 349895 [Multi-domain]  Cd Length: 290  Bit Score: 61.65  E-value: 6.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  85 SEAPDEWIVIGGHLdstigshtneQSVAPGADDDASGIAAVTEVIRVLSE-NNFQPKRSIAFMaYAAEevgLRGSQDLAN 163
Cdd:cd05643   79 GKETPPEIAFVAHL----------CHPKPGANDNASGSALLLEVARVLAKlILNRPKRGICFL-WVPE---YTGTAAYFA 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 164 QYKSEGKNVVSALQLDMTnykGSAQDV---VFITDYTDSNFTQYL---TQLMDEY-----LPSLTYGFD--TCGyacSDH 230
Cdd:cd05643  145 QHPDRLKKIIAVINLDMV---GEDQTKtgsTLMLVPTPLSFPSYLneeLAQKLSNftgssLPAVRYGKEpyEGG---SDH 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 157831451 231 ASWHNAGYPAAMPFE--SKFndYnpriHTTQDTLANSDPT 268
Cdd:cd05643  219 DVFSDPGIPAVMFNTwpDRY--Y----HTSDDTPDKLDPE 252
M28_SGAP_like cd03876
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ...
 34-284 8.24e-11

M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family M28; Streptomyces griseus Aminopeptidase (SGAP, Leucine aminopeptidase (LAP), aminopeptidase S, Mername-AA022 peptidase) subfamily. SGAP is a di-zinc exopeptidase with high preference towards large hydrophobic amino-terminal residues, with Leu being the most efficiently cleaved. It can accommodate all except Pro and Glu residues in the P1' position. It is a monomeric (30 kDa), calcium-activated and calcium-stabilized enzyme; its activation by calcium correlates with substrate specificity and it has thermal stability only in the presence of calcium. Although SGAP contains a calcium binding site, it is not conserved in many members of this subfamily. SGAP is present in the extracellular fluid of S. griseus cultures.


Pssm-ID: 349873 [Multi-domain]  Cd Length: 289  Bit Score: 61.16  E-value: 8.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  34 NRFYTTtSGAQAS-DWIASEWQAlsASLPNASVKQVSHSGYNQKSVVMTITGSEaPDEWIVIGGHLDSTigshtneqSVA 112
Cdd:cd03876   24 NRAFGS-PGYNASvDYVKNELKA--AGYYDVTLQPFTSLYRTTYNVIAETKGGD-PNNVVMLGAHLDSV--------SAG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 113 PGADDDASGIAAVTEVIRVLSenNFQPKRSIAFMAYAAEEVGLRGSQDLANQYKSEGKNVVSA-LQLDMTnykGSAQDVV 191
Cdd:cd03876   92 PGINDNGSGSAALLEVALALA--KFKVKNAVRFAWWTAEEFGLLGSKFYVNNLSSEERSKIRLyLNFDMI---ASPNYGY 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 192 FITDYTDSNFTQY-------LTQLMDEYLPSLTYGF-DTCGYACSDHASWHNAGYPAAMPF-----------ESKFND-- 250
Cdd:cd03876  167 FIYDGDGSAFNLTgppgsaeIERLFEAYFTSLGLPStPTEFDGRSDYAPFIEAGIPAGGLFtgaegikteeqAALWGGta 246

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 157831451 251 ---YNPRIHTTQDTLANSDPT--GSHAKkftqlGLAYAI 284
Cdd:cd03876  247 gvaYDPCYHQACDTIDNINRTalLRNAD-----AIAHAV 280
M28_PMSA_TfR_like cd03874
M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor ...
 39-179 1.71e-10

M28 Zn-peptidase Transferrin Receptor-like family; Peptidase M28 family; Transferrin Receptor (TfR) and prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase or GCP-II) subfamily. TfR and PSMA are homodimeric type II transmembrane proteins containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). In TfR, it contains a binding site for the transferrin molecule and has 28% identity to membrane glutamate carboxypeptidase II (mGCP-II or PSMA). The PA domain is inserted between the first and second strands of the central beta sheet in the protease-like domain. TfR1 is widely expressed, and is a key player in the uptake of iron-loaded transferrin (Tf) into cells. The TfR1 homodimer binds two molecules of Tf and the complex is then internalized. TfR1 may also participate in cell growth and proliferation. TfR2 binds Tf but with a significantly lower affinity than TfR1. It is expressed chiefly in hepatocytes, hematopoietic cells, and duodenal crypt cells; its expression overlaps with that of hereditary hemochromatosis protein (HFE). TfR2 is involved in iron homeostasis; in humans, mutations in TfR2 are associated with a form of hemochromatosis (HFE3). PSMA is over-expressed predominantly in prostate cancer (PCa) as well as in the neovasculature of most solid tumors, but not in the vasculature of normal tissues. PSMA is considered a biomarker for PCa and possibly for use as an imaging and therapeutic target. The extracellular domain of PSMA possesses two unique enzymatic functions: N-acetylated, alpha-linked acidic dipeptidase (NAALADase) which cleaves terminal glutamate from the neurodipeptide N-acetyl-aspartyl-glutamate (NAAG), and folate hydrolase (FOLH) which cleaves the terminal glutamates from gamma-linked polyglutamates (carboxypeptidase). A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants. While related in sequence to peptidase M28 GCP-II, TfR lacks the metal ion coordination centers and protease activity.


Pssm-ID: 349871 [Multi-domain]  Cd Length: 278  Bit Score: 60.39  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  39 TTSGAQASDWIASEWQALSASlpnaSVKQVSHSG-YNqksVVMTITGSEAPDEWIVIGGHLDSTigshtneqsvAPGADD 117
Cdd:cd03874   27 TKGDAALAKYIENSFKNNGLF----EVELEEYSPiTN---VVGKIEGIEQPDRAIIIGAHRDSW----------GYGAGY 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157831451 118 DASGIAAVTEVIRVLSE----NNFQPKRSIAFMAYAAEEVGLRGSQDLANQYKSEGK-NVVSALQLD 179
Cdd:cd03874   90 PNSGTAVLLEIARLFQQlkkkFGWKPLRTIYFISWDGSEFGLAGSTELGEDRKASLKdEVYAYINID 156
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
 92-198 4.60e-07

M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).


Pssm-ID: 349948 [Multi-domain]  Cd Length: 198  Bit Score: 49.35  E-value: 4.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  92 IVIGGHLDsTIG--------SHTNEQSVA------PGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRG 157
Cdd:cd18669   15 VLLGAHID-VVPagegdprdPPFFVDTVEegrlygRGALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEEVGSGA 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157831451 158 SQDLANQYKSEGKNVVSA-LQLDMTNykGSAQDVVFITDYTD 198
Cdd:cd18669   94 GKGLLSKDALEEDLKVDYlFVGDATP--APQKGVGIRTPLVD 133
Peptidase_M20 pfam01546
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ...
 112-172 6.92e-07

Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.


Pssm-ID: 460247 [Multi-domain]  Cd Length: 315  Bit Score: 49.65  E-value: 6.92e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157831451  112 APGADDDASGIAAVTEVIRVLSENNFQpKRSIAFMAYAAEEVGLRGSQDLANQYKSEGKNV 172
Cdd:pfam01546  29 GRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGGMGGARALIEDGLLEREKV 88
M28_TfR cd09848
M28 Zn-peptidase Transferrin Receptor family; Peptidase M28 family; Transferrin Receptor (TfR) ...
 82-167 6.70e-06

M28 Zn-peptidase Transferrin Receptor family; Peptidase M28 family; Transferrin Receptor (TfR) subfamily. TfRs are homodimeric type II transmembrane proteins containing three distinct domains: protease-like, apical or protease-associated (PA), and helical domains. The protease-like domain is a large extracellular portion (ectodomain). In TfR, it contains a binding site for the transferrin molecule and has 28% identity to membrane glutamate carboxypeptidase II (mGCP-II or PSMA). The PA domain is inserted between the first and second strands of the central beta sheet in the protease-like domain. TfR1 is widely expressed, and is a key player in the uptake of iron-loaded transferrin (Tf) into cells. The TfR1 homodimer binds two molecules of Tf and the complex is then internalized. TfR1 may also participate in cell growth and proliferation. TfR2 binds Tf but with a significantly lower affinity than TfR1. It is expressed chiefly in hepatocytes, hematopoietic cells, and duodenal crypt cells; its expression overlaps with that of hereditary hemochromatosis protein (HFE). TfR2 is involved in iron homeostasis; in humans, mutations in TfR2 are associated with a form of hemochromatosis (HFE3). While related in sequence to peptidase M28 glutamate carboxypeptidase II (also called prostate-specific membrane antigen or PSMA), TfR lacks the metal ion coordination centers and protease activity of that group.


Pssm-ID: 349946 [Multi-domain]  Cd Length: 285  Bit Score: 46.60  E-value: 6.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  82 ITGSEAPDEWIVIGGHLDSTigshtneqsvAPGADDDASGIAAVTEVIRVLSE----NNFQPKRSIAFMAYAAEEVGLRG 157
Cdd:cd09848   63 IKGFVEPDRYVVIGAQRDAW----------GPGAAKSGVGTALLLELARTFSDmvknDGFKPRRSIVFASWSAGDFGSVG 132

                         90
                 ....*....|
gi 157831451 158 SQDLANQYKS 167
Cdd:cd09848  133 ATEWLEGYLS 142
M20_peptT_like cd05683
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ...
 70-161 7.54e-06

M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.


Pssm-ID: 349932 [Multi-domain]  Cd Length: 368  Bit Score: 46.67  E-value: 7.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  70 HSGYNQKSVVMTITGSEAPDEWIVIGGHLDSTIGSHTNEQSVAP------------GADDDAsGIAAVTEVIRVLSENNF 137
Cdd:cd05683   48 TTGGGAGNLICTLKADKEEVPKILFTSHMDTVTPGINVKPPQIAdgyiysdgttilGADDKA-GIAAILEAIRVIKEKNI 126

                         90       100
                 ....*....|....*....|....
gi 157831451 138 qPKRSIAFMAYAAEEVGLRGSQDL 161
Cdd:cd05683  127 -PHGQIQFVITVGEESGLVGAKAL 149
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 112-170 1.20e-05

Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440389 [Multi-domain]  Cd Length: 388  Bit Score: 46.03  E-value: 1.20e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157831451 112 APGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRGSQDLANQYKSEGK 170
Cdd:COG0624  107 GRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSPGARALVEELAEGLK 165
PRK09290 PRK09290
allantoate amidohydrolase; Reviewed
 78-162 4.87e-05

allantoate amidohydrolase; Reviewed


Pssm-ID: 236456 [Multi-domain]  Cd Length: 413  Bit Score: 44.38  E-value: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  78 VVMTITGSEAPDEWIVIGGHLDSTIGShtneqsvapGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEE----- 152
Cdd:PRK09290  62 LFGRLEGRDPDAPAVLTGSHLDTVPNG---------GRFDGPLGVLAGLEAVRTLNERGIRPRRPIEVVAFTNEEgsrfg 132

                         90
                 ....*....|
gi 157831451 153 VGLRGSQDLA 162
Cdd:PRK09290 133 PAMLGSRVFT 142
M20_bAS cd03884
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ...
 78-152 8.27e-05

M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.


Pssm-ID: 349880 [Multi-domain]  Cd Length: 398  Bit Score: 43.67  E-value: 8.27e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157831451  78 VVMTITGSEAPDEWIVIGGHLDSTIGShtneqsvapGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEE 152
Cdd:cd03884   54 LFGRLEGTDPDAPPVLTGSHLDTVPNG---------GRYDGILGVLAGLEALRALKEAGIRPRRPIEVVAFTNEE 119
FrvX COG1363
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ...
 117-181 4.23e-04

Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];


Pssm-ID: 440974 [Multi-domain]  Cd Length: 353  Bit Score: 41.27  E-value: 4.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157831451 117 DDASGIAAVTEVIRVLSENnfQPKRSIAFMAYAAEEVGLRGSQDLANQYksegkNVVSALQLDMT 181
Cdd:COG1363  179 DDRAGCAVLLELLKALKDE--DLPVTVYFVFTVQEEVGLRGASTAAYDI-----KPDEAIAVDVT 236
M42 cd05638
M42 Peptidases, also known as glutamyl aminopeptidase family; Peptidase M42 family proteins, ...
 106-189 6.91e-04

M42 Peptidases, also known as glutamyl aminopeptidase family; Peptidase M42 family proteins, also known as glutamyl aminopeptidases (GAP), are co-catalytic metallopeptidases, found in archaea and bacteria. They typically bind two zinc or cobalt atoms and include cellulase and endo-1,4-beta-glucanase (endoglucanase). Some of the enzymes exhibit typical aminopeptidase specificity, whereas others are also capable of N-terminal deblocking activity, i.e. hydrolyzing acylated N-terminal residues. GAP removes glutamyl residues from the N-terminus of peptide substrates, but is also effective against aspartyl and, to a lesser extent, seryl residues. Lactococcus lactis glutamyl aminopeptidase (PepA; aminopeptidase A) has high thermal stability and aids growth of the organism in milk. Pyrococcus horikoshii contain a thermostable de-blocking aminopeptidase member of this family, used commercially for N-terminal protein sequencing.


Pssm-ID: 193517 [Multi-domain]  Cd Length: 332  Bit Score: 40.52  E-value: 6.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 106 TNEQSVAPGADDDASGIAAVTEVIRVLSENNFQPKrsIAFMAYAAEEVGLRGSQDLANQYKSEgknvvSALQLDMT---- 181
Cdd:cd05638  162 LESKYIKSRALDDRVSVYILLELIKRLQDAELPAE--VYFVASVQEEVGLRGASTSTEAVEPD-----VALAVD*Gaagd 234


                 ....*...
gi 157831451 182 NYKGSAQD 189
Cdd:cd05638  235 GFAGQAKI 242
M20_ArgE_DapE-like cd08659
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ...
 43-164 1.03e-03

Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.


Pssm-ID: 349944 [Multi-domain]  Cd Length: 361  Bit Score: 39.98  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  43 AQASDWIAsewQALSASLPNASVKQVSHSGynqkSVVMTITGSEAPdeWIVIGGHLDS-TIGSHTNEQSVaP-------- 113
Cdd:cd08659   17 AEVAEYLA---ELLAKRGYGIESTIVEGRG----NLVATVGGGDGP--VLLLNGHIDTvPPGDGDKWSFP-Pfsgrirdg 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157831451 114 -----GADDDASGIAA-VTEVIRvLSENNFQPKRSIAFMAYAAEEVGLRGSQDLANQ 164
Cdd:cd08659   87 rlygrGACDMKGGLAAmVAALIE-LKEAGALLGGRVALLATVDEEVGSDGARALLEA 142
PRK12890 PRK12890
allantoate amidohydrolase; Reviewed
 15-152 1.11e-03

allantoate amidohydrolase; Reviewed


Pssm-ID: 237248 [Multi-domain]  Cd Length: 414  Bit Score: 40.27  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  15 PQVDASQITGTISSLESFT------NRFYTTTSGAQASDWIASEWQALSASLpnasvkQVSHSGynqkSVVMTITGSEAP 88
Cdd:PRK12890   4 PPINGERLLARLEELAAIGrdgpgwTRLALSDEERAARALLAAWMRAAGLEV------RRDAAG----NLFGRLPGRDPD 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157831451  89 DEWIVIGGHLDSTIGShtneqsvapGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEE 152
Cdd:PRK12890  74 LPPLMTGSHLDTVPNG---------GRYDGILGVLAGLEVVAALREAGIRPPHPLEVIAFTNEE 128
M20_yscS_like cd05675
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ...
 33-154 1.69e-03

M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.


Pssm-ID: 349924 [Multi-domain]  Cd Length: 431  Bit Score: 39.65  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  33 TNRFYTTTSGAQASDWIASEWQAlsASLPNASVKQVSHSGynQKSVVMTITGSEAPDEWIVIGGHLDsTIGSHTNEQSVA 112
Cdd:cd05675   13 TNSGDGTGSETRAAEVLAARLAE--AGIQTEIFVVESHPG--RANLVARIGGTDPSAGPLLLLGHID-VVPADASDWSVD 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157831451 113 P-------------GADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVG 154
Cdd:cd05675   88 PfsgeikdgyvygrGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAG 142
PRK10199 PRK10199
alkaline phosphatase isozyme conversion aminopeptidase; Provisional
 27-179 1.79e-03

alkaline phosphatase isozyme conversion aminopeptidase; Provisional


Pssm-ID: 182299 [Multi-domain]  Cd Length: 346  Bit Score: 39.34  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  27 SSLESFTNRF-YTTTSGAQasdwiasEWQALSASlpnasvkqvshsgynqkSVVMTITGSeAPDEwIVIGGHLDSTIgsh 105
Cdd:PRK10199  72 SDIRTFNSRYiYTARDNRK-------NWHNVTGS-----------------TVIAAHEGK-APQQ-IIIMAHLDTYA--- 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451 106 tnEQSVA-----------PGADDDASGIAAVTEVIRVLSenNFQPKRSIAFMAYAAEEVGLRGSQDLANQYK-SEGKNVV 173
Cdd:PRK10199 123 --PQSDAdvdanlggltlQGMDDNAAGLGVMLELAERLK--NVPTEYGIRFVATSGEEEGKLGAENLLKRMSdTEKKNTL 198


                 ....*.
gi 157831451 174 SALQLD 179
Cdd:PRK10199 199 LVINLD 204
M42_glucanase_like cd05657
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ...
 117-164 4.16e-03

M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1,4-beta-glucanase or endoglucanase)-like subfamily. Proteins in this subfamily are co-catalytic metallopeptidases, found in archaea and bacteria. They show similarity to cellulase and endo-1,4-beta-glucanase (endoglucanase) which typically bind two zinc or cobalt atoms. Some of the enzymes exhibit typical aminopeptidase specificity, whereas others are also capable of N-terminal deblocking activity, i.e. hydrolyzing acylated N-terminal residues. Many of these enzymes are assembled either as tetrahedral dodecamers or as octahedral tetracosameric structures, with the active site located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers.


Pssm-ID: 349907 [Multi-domain]  Cd Length: 337  Bit Score: 38.03  E-value: 4.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 157831451 117 DDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEVGLRGSQDLANQ 164
Cdd:cd05657  181 DDKASVAILLALARALKENKLKLPVDTHFLFSNYEEVGHGASFAPPED 228
PRK12893 PRK12893
Zn-dependent hydrolase;
78-165 4.20e-03

Zn-dependent hydrolase;


Pssm-ID: 237250 [Multi-domain]  Cd Length: 412  Bit Score: 38.32  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  78 VVMTITGSEAPDEWIVIGGHLDSTI-GshtneqsvapGADDDASGIAAVTEVIRVLSENNFQPKRSIAFMAYAAEEvGLR 156
Cdd:PRK12893  65 LFGRRAGTDPDAPPVLIGSHLDTQPtG----------GRFDGALGVLAALEVVRTLNDAGIRTRRPIEVVSWTNEE-GAR 133

                         90
                 ....*....|....*
gi 157831451 157 ------GSQDLANQY 165
Cdd:PRK12893 134 fapamlGSGVFTGAL 148
M20_yscS cd05674
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ...
 114-179 6.82e-03

M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.


Pssm-ID: 349923 [Multi-domain]  Cd Length: 471  Bit Score: 37.62  E-value: 6.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157831451 114 GADDDASGIAAVTEVIRVLSENNFQPKRSIafmaYAA----EEV-GLRGSQDLAN-QYKSEGKNVVSALqLD 179
Cdd:cd05674  109 GALDDKNSLIGILEAVELLLKRGFKPRRTI----ILAfghdEEVgGERGAGAIAElLLERYGVDGLAAI-LD 175
Peptidase_M42 pfam05343
M42 glutamyl aminopeptidase; These peptidases are found in Archaea and Bacteria. The example ...
 117-241 8.13e-03

M42 glutamyl aminopeptidase; These peptidases are found in Archaea and Bacteria. The example in Lactococcus lactis, PepA, aids growth on milk. Pyrococcus horikoshii contain a thermostable de-blocking aminopeptidase member of this family used commercially for N-terminal protein sequencing.


Pssm-ID: 428431 [Multi-domain]  Cd Length: 292  Bit Score: 37.17  E-value: 8.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157831451  117 DDASGIAAVTEVIRVLSENNFQPKrsIAFMAYAAEEVGLRGSQDLANQYKsegknVVSALQLDMT---------NYKGS- 186
Cdd:pfam05343 134 DDRAGVAVLLELLKELKDEDLPAD--VYFVATVQEEVGLRGAKTSAFKIK-----PDEAIAVDVTaagdtpgsdEYEAPl 206

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157831451  187 -------AQDVVFITDYTdsnFTQYLTQLMDEYlpSLTYGFDTCGYACSDHASWHNAGY--PAA 241
Cdd:pfam05343 207 gkgpairVKDASGIYHPK---LRKFLVELAKKN--NIPYQVDVYPGGGTDAGAAHLTGGgvPTA 265
 
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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