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Conserved domains on  [gi|2111775711|gb|UCQ48439|]
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aminopeptidase [Edwardsiella ictaluri]

Protein Classification

Zn-dependent exopeptidase M28( domain architecture ID 11484609)

Zn-dependent exopeptidase M28, similar to alkaline phosphatase isozyme conversion aminopeptidase, may be an aminopeptidase or a carboxypeptidase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10199 PRK10199
alkaline phosphatase isozyme conversion aminopeptidase; Provisional
 1-338 0e+00

alkaline phosphatase isozyme conversion aminopeptidase; Provisional


:

Pssm-ID: 182299 [Multi-domain]  Cd Length: 346  Bit Score: 557.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711   1 MLSRCRYSLslAALCLGCALATPVSAQTHQPiGKIADQEVRHIATYFPGRMAGSPAELMMADYVNQRFRQMGYDSNLRDF 80
Cdd:PRK10199    1 MFSALRHRT--AALALGVCFILPVQAASPKP-GDFANTQARHIATFFPGRMTGSPAEMLSADYLRQQFQQMGYQSDIRTF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  81 KTRYLYRDSNGKNSWHNVTATSVIAAKVGHSAKQILIVAHLDTFTPQSDDDVNHNLGGLTLQGVDDNASGVGVMLELAER 160
Cdd:PRK10199   78 NSRYIYTARDNRKNWHNVTGSTVIAAHEGKAPQQIIIMAHLDTYAPQSDADVDANLGGLTLQGMDDNAAGLGVMLELAER 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 161 LRTVKTQVGIRFLALSAQELGGKGIENYLSRMTPEEKKNTLLVIGIDSLISGDKLLATS---NAQALAERSRDRLLQLAK 237
Cdd:PRK10199  158 LKNVPTEYGIRFVATSGEEEGKLGAENLLKRMSDTEKKNTLLVINLDNLIVGDKLYFNSgvnTPEAVRKLTRDRALAIAR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 238 RDGihIARGNSAMLDQSPPQNEGMA----LFSQAGLPLLLLSAAD---SQDPTRQTRHGGSLFAQGTSWHQPQYDNMKYL 310
Cdd:PRK10199  238 RHG--IAATTNPGLNKNYPKGTGCCndaeVFDKAGIPVLSVEATNwnlGNKDGYQQRAKTAAFPAGNSWHDVRLDNQQHI 315

                         330       340
                  ....*....|....*....|....*...
gi 2111775711 311 DRHLPGRIRARTREGVRILLPLLEQLAR 338
Cdd:PRK10199  316 DKALPGRIERRCRDVVRIMLPLVKELAK 343
 
Name Accession Description Interval E-value
PRK10199 PRK10199
alkaline phosphatase isozyme conversion aminopeptidase; Provisional
 1-338 0e+00

alkaline phosphatase isozyme conversion aminopeptidase; Provisional


Pssm-ID: 182299 [Multi-domain]  Cd Length: 346  Bit Score: 557.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711   1 MLSRCRYSLslAALCLGCALATPVSAQTHQPiGKIADQEVRHIATYFPGRMAGSPAELMMADYVNQRFRQMGYDSNLRDF 80
Cdd:PRK10199    1 MFSALRHRT--AALALGVCFILPVQAASPKP-GDFANTQARHIATFFPGRMTGSPAEMLSADYLRQQFQQMGYQSDIRTF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  81 KTRYLYRDSNGKNSWHNVTATSVIAAKVGHSAKQILIVAHLDTFTPQSDDDVNHNLGGLTLQGVDDNASGVGVMLELAER 160
Cdd:PRK10199   78 NSRYIYTARDNRKNWHNVTGSTVIAAHEGKAPQQIIIMAHLDTYAPQSDADVDANLGGLTLQGMDDNAAGLGVMLELAER 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 161 LRTVKTQVGIRFLALSAQELGGKGIENYLSRMTPEEKKNTLLVIGIDSLISGDKLLATS---NAQALAERSRDRLLQLAK 237
Cdd:PRK10199  158 LKNVPTEYGIRFVATSGEEEGKLGAENLLKRMSDTEKKNTLLVINLDNLIVGDKLYFNSgvnTPEAVRKLTRDRALAIAR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 238 RDGihIARGNSAMLDQSPPQNEGMA----LFSQAGLPLLLLSAAD---SQDPTRQTRHGGSLFAQGTSWHQPQYDNMKYL 310
Cdd:PRK10199  238 RHG--IAATTNPGLNKNYPKGTGCCndaeVFDKAGIPVLSVEATNwnlGNKDGYQQRAKTAAFPAGNSWHDVRLDNQQHI 315

                         330       340
                  ....*....|....*....|....*...
gi 2111775711 311 DRHLPGRIRARTREGVRILLPLLEQLAR 338
Cdd:PRK10199  316 DKALPGRIERRCRDVVRIMLPLVKELAK 343
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 96-338 1.86e-20

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: 89.04  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  96 HNVTATSVIAAKVG--HSAKQILIVAHLDTFtpqsdddvnhnlgGLTLQGVDDNASGVGVMLELAERLRT--VKTQVGIR 171
Cdd:COG2234    42 AGGDSRNVIAEIPGtdPPDEVVVLGAHYDSV-------------GSIGPGADDNASGVAALLELARALAAlgPKPKRTIR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 172 FLALSAQELGGKGIENYLSRMtPEEKKNTLLVIGIDSLISGDKLL-ATSNAQALAERSRDRLLQLAKR--DGIHIARGNS 248
Cdd:COG2234   109 FVAFGAEEQGLLGSRYYAENL-KAPLEKIVAVLNLDMIGRGGPRNyLYVDGDGGSPELADLLEAAAKAylPGLGVDPPEE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 249 AML----DQSPpqnegmalFSQAGLP-LLLLSAADSQDPTrqtrhggslfaqgtsWHQPQyDNMKYLDrhlpgriRARTR 323
Cdd:COG2234   188 TGGygrsDHAP--------FAKAGIPaLFLFTGAEDYHPD---------------YHTPS-DTLDKID-------LDALA 236

                         250
                  ....*....|....*
gi 2111775711 324 EGVRILLPLLEQLAR 338
Cdd:COG2234   237 KVAQLLAALVYELAN 251
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 50-223 1.97e-19

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: 86.47  E-value: 1.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  50 RMAGSPAELMMADYVNQRFRQMGYDSNLRDFKTrylyrdsngknswHNVTATSVIAAKVGHsAKQILIVAHLDT--FTPq 127
Cdd:cd05661    28 GVAGTPEELKAARYIEQQLKSLGYEVEVQPFTS-------------HNVIATKKPDNNKNN-NDIIIVTSHYDSvvKAP- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 128 sdddvnhnlggltlqGVDDNASGVGVMLELAERLRTVKTQVGIRFLALSAQELGGKGIENYLSRMTPEEKKNTLLVIGID 207
Cdd:cd05661    93 ---------------GANDNASGTAVTLELARVFKKVKTDKELRFIAFGAEENGLLGSKYYVASLSEDEIKRTIGVFNLD 157

                         170
                  ....*....|....*.
gi 2111775711 208 slisgdkLLATSNAQA 223
Cdd:cd05661   158 -------MVGTSDAKA 166
Peptidase_M28 pfam04389
Peptidase family M28;
103-318 1.61e-15

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 73.86  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 103 VIAAKVGHSAKQILIV-AHLDTfTPQSDddvnhnlggltlqGVDDNASGVGVMLELAERLRTVKT-QVGIRFLALSAQEL 180
Cdd:pfam04389   2 VIAKLPGKAPDEVVLLsAHYDS-VGTGP-------------GADDNASGVAALLELARVLAAGQRpKRSVRFLFFDAEEA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 181 GGKGIENYLSRmtPEEKKNTLLVIGIDSLISGDKLLATSNAQALAERSRDRLLQLAKRDGIHIA------RGNSAMLDQS 254
Cdd:pfam04389  68 GLLGSHHFAKS--HPPLKKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKPYGVTLAedpfqeRGGPGRSDHA 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2111775711 255 PpqnegmalFSQAGLPLLLLSAADSqdptrqtrhggslfaqGTSWHQPqYDNMKYLDRHLPGRI 318
Cdd:pfam04389 146 P--------FIKAGIPGLDLAFTDF----------------GYRYHTP-ADTIDNIDPGTLQRI 184
 
Name Accession Description Interval E-value
PRK10199 PRK10199
alkaline phosphatase isozyme conversion aminopeptidase; Provisional
 1-338 0e+00

alkaline phosphatase isozyme conversion aminopeptidase; Provisional


Pssm-ID: 182299 [Multi-domain]  Cd Length: 346  Bit Score: 557.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711   1 MLSRCRYSLslAALCLGCALATPVSAQTHQPiGKIADQEVRHIATYFPGRMAGSPAELMMADYVNQRFRQMGYDSNLRDF 80
Cdd:PRK10199    1 MFSALRHRT--AALALGVCFILPVQAASPKP-GDFANTQARHIATFFPGRMTGSPAEMLSADYLRQQFQQMGYQSDIRTF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  81 KTRYLYRDSNGKNSWHNVTATSVIAAKVGHSAKQILIVAHLDTFTPQSDDDVNHNLGGLTLQGVDDNASGVGVMLELAER 160
Cdd:PRK10199   78 NSRYIYTARDNRKNWHNVTGSTVIAAHEGKAPQQIIIMAHLDTYAPQSDADVDANLGGLTLQGMDDNAAGLGVMLELAER 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 161 LRTVKTQVGIRFLALSAQELGGKGIENYLSRMTPEEKKNTLLVIGIDSLISGDKLLATS---NAQALAERSRDRLLQLAK 237
Cdd:PRK10199  158 LKNVPTEYGIRFVATSGEEEGKLGAENLLKRMSDTEKKNTLLVINLDNLIVGDKLYFNSgvnTPEAVRKLTRDRALAIAR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 238 RDGihIARGNSAMLDQSPPQNEGMA----LFSQAGLPLLLLSAAD---SQDPTRQTRHGGSLFAQGTSWHQPQYDNMKYL 310
Cdd:PRK10199  238 RHG--IAATTNPGLNKNYPKGTGCCndaeVFDKAGIPVLSVEATNwnlGNKDGYQQRAKTAAFPAGNSWHDVRLDNQQHI 315

                         330       340
                  ....*....|....*....|....*...
gi 2111775711 311 DRHLPGRIRARTREGVRILLPLLEQLAR 338
Cdd:PRK10199  316 DKALPGRIERRCRDVVRIMLPLVKELAK 343
Iap COG2234
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ...
 96-338 1.86e-20

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: 89.04  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  96 HNVTATSVIAAKVG--HSAKQILIVAHLDTFtpqsdddvnhnlgGLTLQGVDDNASGVGVMLELAERLRT--VKTQVGIR 171
Cdd:COG2234    42 AGGDSRNVIAEIPGtdPPDEVVVLGAHYDSV-------------GSIGPGADDNASGVAALLELARALAAlgPKPKRTIR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 172 FLALSAQELGGKGIENYLSRMtPEEKKNTLLVIGIDSLISGDKLL-ATSNAQALAERSRDRLLQLAKR--DGIHIARGNS 248
Cdd:COG2234   109 FVAFGAEEQGLLGSRYYAENL-KAPLEKIVAVLNLDMIGRGGPRNyLYVDGDGGSPELADLLEAAAKAylPGLGVDPPEE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 249 AML----DQSPpqnegmalFSQAGLP-LLLLSAADSQDPTrqtrhggslfaqgtsWHQPQyDNMKYLDrhlpgriRARTR 323
Cdd:COG2234   188 TGGygrsDHAP--------FAKAGIPaLFLFTGAEDYHPD---------------YHTPS-DTLDKID-------LDALA 236

                         250
                  ....*....|....*
gi 2111775711 324 EGVRILLPLLEQLAR 338
Cdd:COG2234   237 KVAQLLAALVYELAN 251
M28_like_PA cd05661
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ...
 50-223 1.97e-19

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: 86.47  E-value: 1.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  50 RMAGSPAELMMADYVNQRFRQMGYDSNLRDFKTrylyrdsngknswHNVTATSVIAAKVGHsAKQILIVAHLDT--FTPq 127
Cdd:cd05661    28 GVAGTPEELKAARYIEQQLKSLGYEVEVQPFTS-------------HNVIATKKPDNNKNN-NDIIIVTSHYDSvvKAP- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 128 sdddvnhnlggltlqGVDDNASGVGVMLELAERLRTVKTQVGIRFLALSAQELGGKGIENYLSRMTPEEKKNTLLVIGID 207
Cdd:cd05661    93 ---------------GANDNASGTAVTLELARVFKKVKTDKELRFIAFGAEENGLLGSKYYVASLSEDEIKRTIGVFNLD 157

                         170
                  ....*....|....*.
gi 2111775711 208 slisgdkLLATSNAQA 223
Cdd:cd05661   158 -------MVGTSDAKA 166
M28_like_PA_PDZ_associated cd05663
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ...
 49-272 4.91e-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: 85.20  E-value: 4.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  49 GRMAGSPAELMMADYVNQRFRQMGYdsNLRDFKTRYLYRDSNGKNSWHNVTAtsVIAAKVGHSAKQILIVAHLD------ 122
Cdd:cd05663    11 GRLTGTKGEKLAADYIAQRFEELGL--EPGLDNGTYFQPFEFTTGTGRNVIG--VLPGKGDVADETVVVGAHYDhlgygg 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 123 --TFTPQSDDDVnHNlggltlqGVDDNASGVGVMLELAERLRTVKTQV----GIRFLALSAQELGGKGIENYLSRMtPEE 196
Cdd:cd05663    87 egSLARGDESLI-HN-------GADDNASGVAAMLELAAKLVDSDTSLalsrNLVFIAFSGEELGLLGSKHFVKNP-PFP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 197 KKNTLLVIGIDSL--ISGDKL----LATSNA--QALAERSRDRLLQLA-KRDGihiaRGNSamlDQSPpqnegmalFSQA 267
Cdd:cd05663   158 IKNTVYMINMDMVgrLRDNKLivqgTGTSPGweQLVQARNKATGFKLIlDPTG----YGPS---DHTS--------FYLD 222


                  ....*
gi 2111775711 268 GLPLL 272
Cdd:cd05663   223 DVPVL 227
Peptidase_M28 pfam04389
Peptidase family M28;
103-318 1.61e-15

Peptidase family M28;


Pssm-ID: 461288 [Multi-domain]  Cd Length: 192  Bit Score: 73.86  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 103 VIAAKVGHSAKQILIV-AHLDTfTPQSDddvnhnlggltlqGVDDNASGVGVMLELAERLRTVKT-QVGIRFLALSAQEL 180
Cdd:pfam04389   2 VIAKLPGKAPDEVVLLsAHYDS-VGTGP-------------GADDNASGVAALLELARVLAAGQRpKRSVRFLFFDAEEA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 181 GGKGIENYLSRmtPEEKKNTLLVIGIDSLISGDKLLATSNAQALAERSRDRLLQLAKRDGIHIA------RGNSAMLDQS 254
Cdd:pfam04389  68 GLLGSHHFAKS--HPPLKKIRAVINLDMIGSGGPALLFQSGPKGSSLLEKYLKAAAKPYGVTLAedpfqeRGGPGRSDHA 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2111775711 255 PpqnegmalFSQAGLPLLLLSAADSqdptrqtrhggslfaqGTSWHQPqYDNMKYLDRHLPGRI 318
Cdd:pfam04389 146 P--------FIKAGIPGLDLAFTDF----------------GYRYHTP-ADTIDNIDPGTLQRI 184
M28_like_PA cd05660
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ...
 40-209 7.83e-14

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: 70.85  E-value: 7.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  40 VRHIAT-YFPGRMAGSPAELMMADYVNQRFRQMGY------DSNLRDFKtryLYRDSNGKNSwHNVTAtsVIAAKvGHSA 112
Cdd:cd05660     1 VKFLASdEFEGRAPGSEGEKKTVDYLAEQFKELGLkpagsdGSYLQAVP---LVSKIEYSTS-HNVVA--ILPGS-KLPD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 113 KQILIVAHLDTF--TPQSDDDVNHNlggltlqGVDDNASGVGVMLELAERLRT--VKTQVGIRFLALSAQELGGKGiENY 188
Cdd:cd05660    74 EYIVLSAHWDHLgiGPPIGGDEIYN-------GAVDNASGVAAVLELARVFAAqdQRPKRSIVFLAVTAEEKGLLG-SRY 145

                         170       180
                  ....*....|....*....|.
gi 2111775711 189 LSRMTPEEKKNTLLVIGIDSL 209
Cdd:cd05660   146 YAANPIFPLDKIVANLNIDMI 166
M28 cd02690
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ...
 101-312 3.79e-12

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: 64.29  E-value: 3.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 101 TSVIAAKVGHSAKQ--ILIVAHLDTFTPQSdddvnhnlggltlqGVDDNASGVGVMLELAERLRTVKTQV--GIRFLALS 176
Cdd:cd02690     2 YNVIATIKGSDKPDevILIGAHYDSVPLSP--------------GANDNASGVAVLLELARVLSKLQLKPkrSIRFAFWD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 177 AQELGGKGIENYLSRMtPEEKKNTLLVIGIDSLISGDKLLATSNAQALAERSRDRLLQLAKR------DGIHIARGNSAM 250
Cdd:cd02690    68 AEELGLLGSKYYAEQL-LSSLKNIRAALNLDMIGGAGPDLYLQTAPGNDALVEKLLRALAHElenvvyTVVYKEDGGTGG 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2111775711 251 LDQSPpqnegmalFSQAGLPLLLLSAADSQDPTRqtrhggslfaqgtsWHQPQyDNMKYLDR 312
Cdd:cd02690   147 SDHRP--------FLARGIPAASLIQSESYNFPY--------------YHTTQ-DTLENIDK 185
M28_like cd03877
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ...
 96-207 1.61e-11

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: 62.65  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  96 HNVTAtsVIAAKvGHSAKQILIVAHLDT--FTPQSDDDVNHNlggltlqGVDDNASGVGVMLELAERLR-TVKTQVGIRF 172
Cdd:cd03877     2 HNVVG--VLEGS-DLPDETIVIGAHYDHlgIGGGDSGDKIYN-------GADDNASGVAAVLELARYFAkQKTPKRSIVF 71

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2111775711 173 LALSAQELGGKGiENYLSRMTPEEKKNTLLVIGID 207
Cdd:cd03877    72 AAFTAEEKGLLG-SKYFAENPKFPLDKIVAMLNLD 105
M28_like cd05640
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 61-179 3.71e-11

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: 62.85  E-value: 3.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  61 ADYVNQRFRQMGYDSNLRDFktrylyrdSNGKNSWHNVTATSVIAAKVGhsaKQILIVAHLDTfTPQSdddvnhnlgglt 140
Cdd:cd05640    26 AEYIAQELVGSGYNVTSHFF--------SHQEGVYANLIADLPGSYSQD---KLILIGAHYDT-VPGS------------ 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2111775711 141 lQGVDDNASGVGVMLELAERLRTVKTQVGIRFLALSAQE 179
Cdd:cd05640    82 -PGADDNASGVAALLELARLLATLDPNHTLRFVAFDLEE 119
M28_like cd05662
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ...
 47-207 5.72e-11

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: 62.10  E-value: 5.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  47 FPGRMAGSPAELMMADYVNQRFRQMGYDSNLRDFKTRYLYRDSNGKNSWHNVTAtsVIAAKvGHSAKQILIVAHLDtftp 126
Cdd:cd05662    14 FEGRKTGTKGAAKTRAYIIERFKQIGLLPWGDRFEHPFSYTKRFSTRQGVNVLA--VIKGS-EPPTKWRVVSAHYD---- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 127 qsdddvnhNLG---GLTLQGVDDNASGVGVMLELAERLRTVKTQVGIRFLALSAQELGGKGiENYLSRMTPEEKKNTLLV 203
Cdd:cd05662    87 --------HLGirgGKIYNGADDNASGVAALLALAEYFKKHPPKHNVIFAATDAEEPGLRG-SYAFVEALKVPRAQIELN 157


                  ....
gi 2111775711 204 IGID 207
Cdd:cd05662   158 INLD 161
M28_like cd08656
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ...
 36-181 1.12e-09

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: 349943 [Multi-domain]  Cd Length: 287  Bit Score: 58.30  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  36 ADQEVRHIATYFPgRMAGSPAELMMADYVNQRFRQMGYdsnlrdfKTRYLYRDSNGKNSwHNVTATSVIAAKVGHSAKQI 115
Cdd:cd08656     4 AYQYVQNQVDFGP-RVPNTAAHKACGEYLAGKLEAFGA-------KVYNQYADLIAYDG-TILKARNIIGAYNPESKKRV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2111775711 116 LIVAHLDTfTPQSDDDVNHNLGGLTLQGVDDNASGVGVMLELAERLRTVKTQVGIRFLALSAQELG 181
Cdd:cd08656    75 LLCAHWDS-RPYADNDADPKKHHTPILGANDGASGVGALLEIARQIQQQAPAIGIDIIFFDAEDYG 139
M28_SGAP_like cd03876
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ...
 38-211 6.06e-09

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: 56.15  E-value: 6.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  38 QEVRHIAtYFPG--RMAGSPAELMMADYVNQRFRQMG-YDSNLRDFKtrYLYRDSngknswHNVTATSviaaKVGHSAKQ 114
Cdd:cd03876    12 QQLQDIA-DANGgnRAFGSPGYNASVDYVKNELKAAGyYDVTLQPFT--SLYRTT------YNVIAET----KGGDPNNV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 115 ILIVAHLDTFT--PqsdddvnhnlggltlqGVDDNASGVGVMLELAERLRTVKTQVGIRFLALSAQELGGKGIENYLSRM 192
Cdd:cd03876    79 VMLGAHLDSVSagP----------------GINDNGSGSAALLEVALALAKFKVKNAVRFAWWTAEEFGLLGSKFYVNNL 142

                         170
                  ....*....|....*....
gi 2111775711 193 TPEEKKNTLLVIGIDSLIS 211
Cdd:cd03876   143 SSEERSKIRLYLNFDMIAS 161
PepD2 COG2195
Di- or tripeptidase [Amino acid transport and metabolism];
57-162 2.72e-06

Di- or tripeptidase [Amino acid transport and metabolism];


Pssm-ID: 441798 [Multi-domain]  Cd Length: 364  Bit Score: 48.51  E-value: 2.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  57 ELMMADYVNQRFRQMGYDsnlrdfktryLYRDSNGknswhNVTATsvIAAKVGHSAKQILIVAHLDT---FT-----PQS 128
Cdd:COG2195    22 EEALADYLVEELKELGLE----------VEEDEAG-----NVIAT--LPATPGYNVPTIGLQAHMDTvpqFPgdgikPQI 84

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2111775711 129 DDDVNHNlGGLTLQGVDDNAsGVGVMLELAERLR 162
Cdd:COG2195    85 DGGLITA-DGTTTLGADDKA-GVAAILAALEYLK 116
ArgE COG0624
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ...
 54-205 4.89e-06

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: 47.96  E-value: 4.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  54 SPAELMMADYVNQRFRQMGYDSNLRDFKTRYlyrdsngknswhnvtaTSVIAAKVGH-SAKQILIVAHLDT--------- 123
Cdd:COG0624    28 SGEEAAAAELLAELLEALGFEVERLEVPPGR----------------PNLVARRPGDgGGPTLLLYGHLDVvppgdlelw 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 124 ----FTPQSDDDVnhnLGGLtlqGVDDNASGVGVMLELAERLR--TVKTQVGIRFLALSAQELGGKGIENYLSRMtPEEK 197
Cdd:COG0624    92 tsdpFEPTIEDGR---LYGR---GAADMKGGLAAMLAALRALLaaGLRLPGNVTLLFTGDEEVGSPGARALVEEL-AEGL 164


                  ....*...
gi 2111775711 198 KNTLLVIG 205
Cdd:COG0624   165 KADAAIVG 172
M28_nicalin_like cd03882
M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin ...
 112-216 2.02e-05

M28 Zn-Peptidase Nicalin, Nicastrin-like protein; Peptidase M28 family, Nicalin (nicastrin-like protein) subfamily. Nicalin is distantly related to Nicastrin, a component of the Alzheimer's disease-associated gamma-secretase, and forms a complex with Nomo (nodal modulator) pM5. Similar to Nicastrin, Nicalin lacks the amino-acid conservation required for catalytically active aminopeptidases. Functional studies in zebrafish embryos and cultured human cells reveal that nicalin and Nomo collaborate to antagonize the Nodal/TGFbeta signaling pathway. Thus, nicastrin and nicalin are both associated with protein complexes involved in cell fate decisions during early embryonic development.


Pssm-ID: 349878  Cd Length: 296  Bit Score: 45.44  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 112 AKQILIVAHLDTFTPQSdddvNHNLGGltlqgvDDNASGVGVMLELAERLR----TVKTQVG--IRFLALSAQELGGKGI 185
Cdd:cd03882    89 LPTIVIVAHYDTFGVAP----WLSSGA------DSNGSGVAALLELMRLFSrlysNPRTRAKynLLFLLTGGGKLNYQGT 158

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2111775711 186 ENYLSRMTPEEKKNTLLVIGIDSLISGDKLL 216
Cdd:cd03882   159 KHWLESNLDHFLDNVEFVLCLDSIGSKDSDL 189
M28_like cd05643
M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), ...
 40-173 2.24e-05

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: 45.47  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  40 VRHIATYFpgRMAGSPAELMMADYVNQRFRQMGYD----SNLRDFKTRYLYRDSNgkNSWHNVTAT-----SVIAAKVGH 110
Cdd:cd05643     5 VSFISRYH--RVQGSRGYVKAAEEVKELLEELGLEakliSDIYDGGERILTPQSP--ISWELIEGElnetlPILYAIIGK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2111775711 111 SAKQ-ILIVAHLdtFTPQsdddvnhnlggltlQGVDDNASGVGVMLELA---ERLRTVKTQVGIRFL 173
Cdd:cd05643    81 ETPPeIAFVAHL--CHPK--------------PGANDNASGSALLLEVArvlAKLILNRPKRGICFL 131
M28_Fxna_like cd03875
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ...
 30-181 6.45e-04

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: 41.03  E-value: 6.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  30 QPIGKIADQEVRHIATYFPgRMAGSPAELMMADYVNQRFRQMGYDSNLRD---------FKTRYLYRDSNGKNSWHNVTA 100
Cdd:cd03875     3 GFSLERAWEDLQVLISIGP-HPYGSHNNDKVRDYLLARVEEIKERANANGlevevqddtGSGSFNFLSSGMTLVYFEVTN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 101 TSV-IAAKVGHSAKQILIVAHLDTfTPQSdddvnhnlggltlQGVDDNASGVGVMLELAERLRTVKTQ--VGIRFLALSA 177
Cdd:cd03875    82 IVVrISGKNSNSLPALLLNAHFDS-VPTS-------------PGATDDGMGVAVMLEVLRYLSKSGHQpkRDIIFLFNGA 147


                  ....
gi 2111775711 178 QELG 181
Cdd:cd03875   148 EENG 151
M28_AAP cd03879
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ...
 71-206 1.91e-03

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: 39.53  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  71 MGYDSNLRDFKTRYlYRDSNGKNS-------WHNVTATS----VIAAKVGHSAKQ----------------ILIVAHLDT 123
Cdd:cd03879    21 QDTLESLTSFNNRY-YKSQTGVESaewlldqVQAIIASSgrsgATVEQFTHSFPQpsiiatipgseksdeiVVIGAHQDS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 124 ftpqsdddVNHNLGGLTLQ-GVDDNASGVGVMLElAERL---------RTVKtqvgirFLALSAQE---LGGKGI-ENYL 189
Cdd:cd03879   100 --------INGSNPSNGRApGADDDGSGTVTILE-ALRVllesgfqpkNTIE------FHWYAAEEgglLGSQAIaTQYK 164

                         170       180
                  ....*....|....*....|....*...
gi 2111775711 190 SR-----------MTPEEKKNTLLVIGI 206
Cdd:cd03879   165 SEgknvkamlqldMTGYVKPGSAEDIGL 192
M20_ArgE_DapE-like cd08659
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ...
 54-191 3.85e-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: 38.82  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711  54 SPAELMMADYVNQRFRQMGYDSNLRDFKTRYlyrdsngknswhnvtatSVIAAKVGHSAKQILIVAHLDTFTPQ------ 127
Cdd:cd08659    13 NPPEAEVAEYLAELLAKRGYGIESTIVEGRG-----------------NLVATVGGGDGPVLLLNGHIDTVPPGdgdkws 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 128 ----SDDDVNHNLGGLtlqGVDDNASGVGVMLELAERLRT--VKTQVGIRFLALSAQELGGKGIENYLSR 191
Cdd:cd08659    76 fppfSGRIRDGRLYGR---GACDMKGGLAAMVAALIELKEagALLGGRVALLATVDEEVGSDGARALLEA 142
M20_18_42 cd18669
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ...
 103-245 4.73e-03

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: 37.80  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2111775711 103 VIAAKVGHSAKQILIVAHLDT----------FTPQSDDDVNHNLGGLtlqGVDDNASGVGVMLELAERLR--TVKTQVGI 170
Cdd:cd18669     3 IARYGGGGGGKRVLLGAHIDVvpagegdprdPPFFVDTVEEGRLYGR---GALDDKGGVAAALEALKLLKenGFKLKGTV 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2111775711 171 RFLALSAQELGGKGIENYLSRmtpEEKKNTLlviGIDSLISGDKLLATSNAQALAERSRDRLLQLAKRDGIHIAR 245
Cdd:cd18669    80 VVAFTPDEEVGSGAGKGLLSK---DALEEDL---KVDYLFVGDATPAPQKGVGIRTPLVDALSEAARKVFGKPQH 148
M28_like cd05642
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ...
 143-181 9.80e-03

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: 37.47  E-value: 9.80e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2111775711 143 GVDDNASGVGVMLELAERLRTVKTQVGIRFLALSAQELG 181
Cdd:cd05642   127 GANDDASGVAVSMELARIFAKHRPKATIVFTAVAGEEQG 165
 
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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