|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
2-406 |
0e+00 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 746.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 2 KEKVLERFLKYVAFDTTADPKNSNCPSSEGQRVFAKYLVEELKGLGLEDANVDENSYVMATLKGNVEG-VPTIGFISHLD 80
Cdd:PRK05469 1 MDKLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDENGYVMATLPANVDKdVPTIGFIAHMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 81 TAPDVTGKDVKPRIIENYDGKDIVLNEElNVVTSTKDYPEMKTLAGQDIIVTDGTTLLGADDKAGIAEIVTAIEYLVNNP 160
Cdd:PRK05469 81 TAPDFSGKNVKPQIIENYDGGDIALGDG-NEVLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYLIAHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 161 EIKHGDIKIGFTPDEEVGRGADLFDVEKFGAKYAYTIDGGILGELQYENFNAAAATITIQGRNVHPGSAKNKLVNALHIA 240
Cdd:PRK05469 160 EIKHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALLLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 241 AEISEMFPASERPETTEVYEGFYHLNDINGNVESATMIYIIRDHDKAKFEERKAFMTSAIEKINEKY-EGRVKLDLNDQY 319
Cdd:PRK05469 240 ADFHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKYgEGRVELEIKDQY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 320 YNMKEKVEPVKFVVDIVEEAMKETEIAPLIVPIRGGTDGARLSFMGLPCPNIFTGGLNFHSKNECISVQAMEKGANLIVK 399
Cdd:PRK05469 320 YNMREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVIVE 399
|
....*..
gi 821175516 400 IAEKYTE 406
Cdd:PRK05469 400 IAELTAE 406
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
5-403 |
0e+00 |
|
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; tripeptide aminopeptidase; tripeptidase) subfamily. PepT 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: 349887 [Multi-domain] Cd Length: 400 Bit Score: 690.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 5 VLERFLKYVAFDTTADPKNSNCPSSEGQRVFAKYLVEELKGLGLEDANVDENSYVMATLKGNV-EGVPTIGFISHLDTAP 83
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDEHGYVTATLPANVdKDVPTIGFIAHMDTAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 84 DVTGKDVKPRIIENYDGKDIVLNEElNVVTSTKDYPEMKTLAGQDIIVTDGTTLLGADDKAGIAEIVTAIEYLVNNPEIK 163
Cdd:cd03892 81 DNSGKNVKPQIIENYDGGDIVLNES-GIVLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIEHPEIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 164 HGDIKIGFTPDEEVGRGADLFDVEKFGAKYAYTIDGGILGELQYENFNAAAATITIQGRNVHPGSAKNKLVNALHIAAEI 243
Cdd:cd03892 160 HGDIRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLAADF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 244 SEMFPASERPETTEVYEGFYHLNDINGNVESATMIYIIRDHDKAKFEERKAFMTSAIEKINEKY-EGRVKLDLNDQYYNM 322
Cdd:cd03892 240 HSMLPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKYgEGRVELEIKDQYYNM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 323 KEKVEPVKFVVDIVEEAMKETEIAPLIVPIRGGTDGARLSFMGLPCPNIFTGGLNFHSKNECISVQAMEKGANLIVKIAE 402
Cdd:cd03892 320 KEKIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIVKIAE 399
|
.
gi 821175516 403 K 403
Cdd:cd03892 400 L 400
|
|
| peptidase-T |
TIGR01882 |
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has ... |
3-407 |
0e+00 |
|
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has a substrate preference for hydrophobic peptides. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 130937 [Multi-domain] Cd Length: 410 Bit Score: 510.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 3 EKVLERFLKYVAFDTTADPKNSNCPSSEGQRVFAKYLVEELKGLGLEDANVDE-NSYVMATLKGNVE-GVPTIGFISHLD 80
Cdd:TIGR01882 3 EELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEkNGYVIATIPSNTDkDVPTIGFLAHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 81 TApDVTGKDVKPRIIENYDGKDIVLNEELNVVTSTKDYPEMKTLAGQDIIVTDGTTLLGADDKAGIAEIVTAIEYLVNNP 160
Cdd:TIGR01882 83 TA-DFNGENVNPQIIENYDGESIIQLGDLEFTLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAADYLINHP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 161 EIKHGDIKIGFTPDEEVGRGADLFDVEKFGAKYAYTIDGGILGELQYENFNAAAATITIQGRNVHPGSAKNKLVNALHIA 240
Cdd:TIGR01882 162 EIKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAAQIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 241 AEISEMFPASERPETTEVYEGFYHLNDINGNVESATMIYIIRDHDKAKFEERKAFMTSAIEKINEKY-EGRVKLDLNDQY 319
Cdd:TIGR01882 242 IDLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEYgQDRIKLDMNDQY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 320 YNMKEKVEPVKFVVDIVEEAMKETEIAPLIVPIRGGTDGARLSFMGLPCPNIFTGGLNFHSKNECISVQAMEKGANLIVK 399
Cdd:TIGR01882 322 YNMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDVIVE 401
|
....*...
gi 821175516 400 IAEKYTEV 407
Cdd:TIGR01882 402 IAKLNEEQ 409
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
1-404 |
1.05e-176 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 496.88 E-value: 1.05e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 1 MKEKVLERFLKYVAFDTTADPknsncpssegQRVFAKYLVEELKGLGLEdANVDENSYVMATLKGNVE-GVPTIGFISHL 79
Cdd:COG2195 1 NPERLLERFLEYVKIPTPSDH----------EEALADYLVEELKELGLE-VEEDEAGNVIATLPATPGyNVPTIGLQAHM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 80 DTAPDVTGKDVKPRIienyDGkdivlneelnvvtstkdypemktlagqDIIVTDGTTLLGADDKAGIAEIVTAIEYLVnN 159
Cdd:COG2195 70 DTVPQFPGDGIKPQI----DG---------------------------GLITADGTTTLGADDKAGVAAILAALEYLK-E 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 160 PEIKHGDIKIGFTPDEEVG-RGADLFDVEKFGAKYAYTIDGGILGELQYENFNAAAATITIQGRNVHPGSAKNKLVNALH 238
Cdd:COG2195 118 PEIPHGPIEVLFTPDEEIGlRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 239 IAAEISEMFPASERPETTEVYEGFYHLNDI-NGNVESATMIYIIRDHDKAKFEERKAFMTSAIEKINEKY-EGRVKLDLN 316
Cdd:COG2195 198 LAARFLAALPLGRIPEETEGNEGFIHGGSAtNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYgVGVVEVEIE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 317 DQYYNMKEkvEPVKFVVDIVEEAMKETEIAPLIVPIRGGTDGARLSFMGLPCPNIFTGGLNFHSKNECISVQAMEKGANL 396
Cdd:COG2195 278 DQYPNWKP--EPDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWEL 355
|
....*...
gi 821175516 397 IVKIAEKY 404
Cdd:COG2195 356 LVEILKLI 363
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
3-402 |
4.46e-172 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 486.73 E-value: 4.46e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 3 EKVLERFLKYVAFDTTADPKNSNCPSSEGQRVFAKYLVEELKGLGLEDANVDENSYVMATLKGNVEGVPTIGFISHLDTA 82
Cdd:PRK13381 1 MQLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDIVIDEHAIVTAKLPGNTPGAPRIGFIAHLDTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 83 PDVTGKDVKPRIIEnYDGKDIVLNEELNVVTSTKDYPEMKTLAGQDIIVTDGTTLLGADDKAGIAEIVTAIEYLVNNpEI 162
Cdd:PRK13381 81 DVGLSPDIHPQILR-FDGGDLCLNAEQGIWLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLENLTEN-EV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 163 KHGDIKIGFTPDEEVG-RGADLFDVEKFGAKYAYTIDGGILGELQYENFNAAAATITIQGRNVHPGSAKNKLVNALHIAA 241
Cdd:PRK13381 159 EHGDIVVAFVPDEEIGlRGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNPILMAN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 242 EISEMFPASERPETTEVYEGFYHLNDINGNVESATMIYIIRDHDKAKFEERKAFMTSAIEKINEKY-EGRVKLDLNDQYY 320
Cdd:PRK13381 239 DFISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINAKYpTARVSLTLTDQYS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 321 NMKEKVEPVKFVVDIVEEAMKETEIAPLIVPIRGGTDGARLSFMGLPCPNIFTGGLNFHSKNECISVQAMEKGANLIVKI 400
Cdd:PRK13381 319 NISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEVTITI 398
|
..
gi 821175516 401 AE 402
Cdd:PRK13381 399 CL 400
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
5-402 |
8.56e-124 |
|
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; tripeptide aminopeptidase; tripeptidase) subfamily and similar proteins. PepT acts only on tripeptide substrates, and is thus termed 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: 349897 [Multi-domain] Cd Length: 400 Bit Score: 364.01 E-value: 8.56e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 5 VLERFLKYVAFDTTADPKNSNCPSSEGQRVFAKYLVEELKGLGLEDANVDENSYVMATLKGNVEG-VPTIGFISHLDTAP 83
Cdd:cd05645 1 LLERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEKGTLIATLPANVDGdIPAIGFISHVDTSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 84 DVTGKDVKPRIIENYDGKDIVLNEElNVVTSTKDYPEMKTLAGQDIIVTDGTTLLGADDKAGIAEIVTAIEYLVNNPeIK 163
Cdd:cd05645 81 DGSGKNVNPQIVENYRGGDIALGIG-DEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKN-IP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 164 HGDIKIGFTPDEEVGRGADLFDVEKFGAKYAYTIDGGILGELQYENFNAAAATITIQGRNVHPGSAKNKLVNALHIAAEI 243
Cdd:cd05645 159 HGDIEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAARI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 244 SEMFPASERPETTEVYEGFYHLNDINGNVESATMIYIIRDHDKAKFEERKAFMTSAIEKINEKY--EGRVKLDLNDQYYN 321
Cdd:cd05645 239 HAEVPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVGKGLhpDCYIELVIEDSYYN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 322 MKEKVEPVKFVVDIVEEAMKETEIAPLIVPIRGGTDGARLSFMGLPCPNIFTGGLNFHSKNECISVQAMEKGANLIVKIA 401
Cdd:cd05645 319 FREKVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIVRIA 398
|
.
gi 821175516 402 E 402
Cdd:cd05645 399 E 399
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
2-402 |
1.13e-39 |
|
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: 145.29 E-value: 1.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 2 KEKVLERFLKYVAFDTtadpknsncpSSEGQRVFAKYLVEELKGLGLEDANVD-------ENSYVMATLKGNVEGVPTIG 74
Cdd:cd05683 2 EDRLINTFLELVQIDS----------ETLHEKEISKVLKKKFENLGLSVIEDDagkttggGAGNLICTLKADKEEVPKIL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 75 FISHLDTApdVTGKDVKPRIIENydgkdivlneelnvvtstkdypemktlagqDIIVTDGTTLLGADDKAGIAEIVTAIE 154
Cdd:cd05683 72 FTSHMDTV--TPGINVKPPQIAD------------------------------GYIYSDGTTILGADDKAGIAAILEAIR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 155 YLVNNpEIKHGDIKIGFTPDEEVGR-GADLFDVEKFGAKYAYTIDG-GILGELQYENFNAAAATITIQGRNVHPGSAKNK 232
Cdd:cd05683 120 VIKEK-NIPHGQIQFVITVGEESGLvGAKALDPELIDADYGYALDSeGDVGTIIVGAPTQDKINAKIYGKTAHAGTSPEK 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 233 LVNALHIAAE-ISEMFPASERPETTEvyegfyHLNDINGNveSATMI-----YII---RDHDKAKFEERKAFMTSAIEKI 303
Cdd:cd05683 199 GISAINIAAKaISNMKLGRIDEETTA------NIGKFQGG--TATNIvtdevNIEaeaRSLDEEKLDAQVKHMKETFETT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 304 NEKYEGRVKLDLNDQY--YNMKEKVEpvkfVVDIVEEAMKETEIAPLIVPIRGGTDGARLSFMGLPCPNIFTGGLNFHSK 381
Cdd:cd05683 271 AKEKGAHAEVEVETSYpgFKINEDEE----VVKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTT 346
|
410 420
....*....|....*....|.
gi 821175516 382 NECISVQAMEKGANLIVKIAE 402
Cdd:cd05683 347 NERIPIEDLYDTAVLVVEIIK 367
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
4-402 |
3.28e-38 |
|
peptidase T-like protein; This model represents a clade of enzymes closely related to Peptidase T, an aminotripeptidase found in bacteria. This clade consists of gram positive bacteria of which several additionally contain a Peptidase T gene.
Pssm-ID: 162579 [Multi-domain] Cd Length: 361 Bit Score: 141.23 E-value: 3.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 4 KVLERFLKYVAFDTTadpknsncpsSEGQRVFAKYLVEELKGLGL---EDANVDENSY---VMATLKGNVEgVPTIGFIS 77
Cdd:TIGR01883 1 RLKKYFLELIQIDSE----------SGKEKAILTYLKKQITKLGIpvsLDEVPAEVSNdnnLIARLPGTVK-FDTIFFCG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 78 HLDTAPDvtGKDVKPrIIENydgkdivlneelnvvtstkdypemktlagqDIIVTDGTTLLGADDKAGIAEIVTAIEYLv 157
Cdd:TIGR01883 70 HMDTVPP--GAGPEP-VVED------------------------------GIFTSLGGTILGADDKAGVAAMLEAMDVL- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 158 NNPEIKHGDIKIGFTPDEEVG-RGADLFDVEKFGAKYAYTID-GGILGELQYENFNAAAATITIQGRNVHPGSAKNKLVN 235
Cdd:TIGR01883 116 STEETPHGTIEFIFTVKEELGlIGMRLFDESKITAAYGYCLDaPGEVGNIQLAAPTQVKVDATIAGKDAHAGLVPEDGIS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 236 ALHIAAE-ISEMFPASERPETTEVYEGFYHLNDINGNVESATMIYIIRDHDKAKFEERKAFMTSAIEKINEKYEGRVKLD 314
Cdd:TIGR01883 196 AISVARMaIHAMRLGRIDEETTANIGSFSGGVNTNIVQDEQLIVAEARSLSFRKAEAQVQTMRERFEQAAEKYGATLEEE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 315 LNDQYYNMkeKVEPVKFVVDIVEEAMKETEIAPLIVPIRGGTDGARLSFMGLPCPNIFTGGLNFHSKNECISVQAMEKGA 394
Cdd:TIGR01883 276 TRLIYEGF--KIHPQHPLMNIFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETISIEQLVKLA 353
|
....*...
gi 821175516 395 NLIVKIAE 402
Cdd:TIGR01883 354 ELVIALAE 361
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
1-406 |
2.87e-24 |
|
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: 103.04 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 1 MKEKVLERFLKYVAFDTtadpknsncPSSEGQRVfAKYLVEELKGLGLE---DANVDENSYVMATLKGNVEGvPTIGFIS 77
Cdd:COG0624 10 HLDEALELLRELVRIPS---------VSGEEAAA-AELLAELLEALGFEverLEVPPGRPNLVARRPGDGGG-PTLLLYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 78 HLDTAPDVTGKD-----VKPRIIenyDGKdivlneelnvvtstkdypemktLAGqdiivtdgttlLGA-DDKAGIAEIVT 151
Cdd:COG0624 79 HLDVVPPGDLELwtsdpFEPTIE---DGR----------------------LYG-----------RGAaDMKGGLAAMLA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 152 AIEYLVNNPEIKHGDIKIGFTPDEEVG-RGADLF---DVEKFGAKYAYTIDGGILGELQYENFNAAAATITIQGRNVHpG 227
Cdd:COG0624 123 ALRALLAAGLRLPGNVTLLFTGDEEVGsPGARALveeLAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAH-S 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 228 SAKNKLVNALHIAAE-ISEMfpaSERPETTEVYEGFYHLNdIN-GNVESATMIYIIRDHDKAKF------EERKAFMTSA 299
Cdd:COG0624 202 SRPELGVNAIEALARaLAAL---RDLEFDGRADPLFGRTT-LNvTGIEGGTAVNVIPDEAEAKVdirllpGEDPEEVLAA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 300 IEKINEKYEGRVKLDLNdqyyNMKEKVEPVKF-----VVDIVEEAMKE-TEIAPLIVPIRGGTDGARLS-FMGLPCPNIF 372
Cdd:COG0624 278 LRALLAAAAPGVEVEVE----VLGDGRPPFETppdspLVAAARAAIREvTGKEPVLSGVGGGTDARFFAeALGIPTVVFG 353
|
410 420 430
....*....|....*....|....*....|....*
gi 821175516 373 TGGL-NFHSKNECISVQAMEKGANLIVKIAEKYTE 406
Cdd:COG0624 354 PGDGaGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
140-403 |
4.64e-21 |
|
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: 92.80 E-value: 4.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 140 ADDKAGIAEIVTAIEYLVNNPeIKHGDIKIGFTPDEEVGRG-----ADLFDVEKFGAKYAYTI---DGGIL-GELQYENF 210
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEG-LKKGTVKLLFQPDEEGGMGgaralIEDGLLEREKVDAVFGLhigEPTLLeGGIAIGVV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 211 NAAAAT----ITIQGRNVH---PGSAKNKLVNALHIAAEISEMFPASERPETTEVYEgFYHLNDING--NV--ESATMIY 279
Cdd:pfam01546 112 TGHRGSlrfrVTVKGKGGHastPHLGVNAIVAAARLILALQDIVSRNVDPLDPAVVT-VGNITGIPGgvNVipGEAELKG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 280 IIRDHDKAKFEERKAFMTSAIEKINEKYEGRVKLDLNDQYYNMKEKVEPVkfvVDIVEEAMKET---EIAPLIVPIRGGT 356
Cdd:pfam01546 191 DIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEYVEGGAPPLVNDSPL---VAALREAAKELfglKVELIVSGSMGGT 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 821175516 357 DGArlsFMGLPCPNIF----TGGLNFHSKNECISVQAMEKGANLIVKIAEK 403
Cdd:pfam01546 268 DAA---FFLLGVPPTVvffgPGSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
36-401 |
4.16e-17 |
|
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: 81.96 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 36 AKYLVEELK--GLGLEDANVDENSYVMATLKGNVEgvPTIGFISHLDTapdVTGKDVKPRIIENYDGKDivlneelnvvt 113
Cdd:cd08659 20 AEYLAELLAkrGYGIESTIVEGRGNLVATVGGGDG--PVLLLNGHIDT---VPPGDGDKWSFPPFSGRI----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 114 stkdypemktlaGQDIIVTDGTtllgADDKAGIAEIVTAIEYLVNNPEIKHGDIKIGFTPDEEVG-RGADLFdVEkfgAK 192
Cdd:cd08659 84 ------------RDGRLYGRGA----CDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGsDGARAL-LE---AG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 193 YAYTIDGGILGE-----LQYENFNAAAATITIQGRNVHpGSAKNKLVNALHIAAE-ISEMFPASERPETTEVYEGFYHLN 266
Cdd:cd08659 144 YADRLDALIVGEptgldVVYAHKGSLWLRVTVHGKAAH-SSMPELGVNAIYALADfLAELRTLFEELPAHPLLGPPTLNV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 267 D-INGNVEsatmIYIIRDHDKAKFEERKAFMTSA------IEKINEKYEGRVKLDLNdQYYNMKEKVEPVKFVVDIVEEA 339
Cdd:cd08659 223 GvINGGTQ----VNSIPDEATLRVDIRLVPGETNegviarLEAILEEHEAKLTVEVS-LDGDPPFFTDPDHPLVQALQAA 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 821175516 340 MKETEIAPLIVPIRGGTDGARLS-FMGLPCPNIFTGGLNF-HSKNECISVQAMEKGANLIVKIA 401
Cdd:cd08659 298 ARALGGDPVVRPFTGTTDASYFAkDLGFPVVVYGPGDLALaHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
88-406 |
4.16e-12 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 66.71 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 88 KDVKPRIIENYDGKDIVLNEELNVVTSTK-DYPEMKTLAGQDIIVTDGTtllGADD-KAGIAEIVTAIEYLvnNPEIKHG 165
Cdd:PRK08652 35 LGYDVHIESDGEVINIVVNSKAELFVEVHyDTVPVRAEFFVDGVYVYGT---GACDaKGGVAAILLALEEL--GKEFEDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 166 DIKIGFTPDEEV-GRGADLFdVEKFGAKYAYTIDGGILgELQYENFNAAAATITIQGRNVH---PGSAKNKLVNALHIAA 241
Cdd:PRK08652 110 NVGIAFVSDEEEgGRGSALF-AERYRPKMAIVLEPTDL-KVAIAHYGNLEAYVEVKGKPSHgacPESGVNAIEKAFEMLE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 242 EISEMFPASerpetTEVYEGFYHLNDINGNVESatmiYIIRDHDKAKFEERKAFMTSA------IEKINEKYEGRVKLDL 315
Cdd:PRK08652 188 KLKELLKAL-----GKYFDPHIGIQEIIGGSPE----YSIPALCRLRLDARIPPEVEVedvldeIDPILDEYTVKYEYTE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 316 NDQYYNMKEKVEpvkfVVDIVEEAMKETEIAPLIVPIRGGTDGARLSFMGLPcPNIF-TGGLNF-HSKNECISVQAMEKG 393
Cdd:PRK08652 259 IWDGFELDEDEE----IVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTK-TVVWgPGELDLcHTKFERIDVREVEKA 333
|
330
....*....|...
gi 821175516 394 ANLIVKIAEKYTE 406
Cdd:PRK08652 334 KEFLKALNEILLE 346
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
207-308 |
1.50e-10 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. 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: 400158 [Multi-domain] Cd Length: 107 Bit Score: 57.74 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 207 YENFNAAAATITIQGRNVHPGsAKNKLVNALHIAAE-ISEM---------FPASERPETTEVYEGFyhlnDINGNVESAT 276
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSG-APGKGVNAIKLLARlLAELpaeygdigfDFPRTTLNITGIEGGT----ATNVIPAEAE 75
|
90 100 110
....*....|....*....|....*....|..
gi 821175516 277 MIYIIRDHDKAKFEERKAFMTSAIEKINEKYE 308
Cdd:pfam07687 76 AKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
146-357 |
4.08e-10 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 61.08 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 146 IAEIVTAIEYLVNNPEIKHGDIKIGFTPDEEVGRGA------DLFDVEKFGAKYAYTIDGGI-LGELQYE--NFNAAAAT 216
Cdd:cd03886 94 TAMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPGGAkamieeGVLENPGVDAAFGLHVWPGLpVGTVGVRsgALMASADE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 217 --ITIQGRNVHpGSAKNKLVNALHIAAEI--------SEMFPASERPETTevyegfyhLNDING----NV--ESATMIYI 280
Cdd:cd03886 174 feITVKGKGGH-GASPHLGVDPIVAAAQIvlalqtvvSRELDPLEPAVVT--------VGKFHAgtafNVipDTAVLEGT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 281 IRDHDKAKFEERKAFMTSAIEKINEKYEGRVKLDLNDQY---YNMKEkvepvkfVVDIVEEAMKETEIAPLIV---PIRG 354
Cdd:cd03886 245 IRTFDPEVREALEARIKRLAEGIAAAYGATVELEYGYGYpavINDPE-------LTELVREAAKELLGEEAVVepePVMG 317
|
...
gi 821175516 355 GTD 357
Cdd:cd03886 318 SED 320
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
99-200 |
1.49e-09 |
|
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: 57.44 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 99 DGKDIVLNEELNVVTSTKDYPEMKTLAGQDIIVTDGTTLLGADDKAGIAEIVTAIEYLVNNPEIKHGDIKIGFTPDEEVG 178
Cdd:cd18669 11 GGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEEVG 90
|
90 100
....*....|....*....|....*...
gi 821175516 179 RGA------DLFDVEKFGAKYAYTIDGG 200
Cdd:cd18669 91 SGAgkgllsKDALEEDLKVDYLFVGDAT 118
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
59-200 |
8.94e-09 |
|
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: 55.12 E-value: 8.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 59 VMATLKGNVEGvPTIGFISHLDTAPdvtgkdvkpriienydgkdivlneeLNVVTSTKDYPEMKTLAGQDIIvtdgtTLL 138
Cdd:cd03873 2 LIARLGGGEGG-KSVALGAHLDVVP-------------------------AGEGDNRDPPFAEDTEEEGRLY-----GRG 50
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 821175516 139 GADDKAGIAEIVTAIEYLVNNPEIKHGDIKIGFTPDEEVGRGA------DLFDVEKFGAKYAYTIDGG 200
Cdd:cd03873 51 ALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGSGGgkgllsKFLLAEDLKVDAAFVIDAT 118
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
23-400 |
1.34e-08 |
|
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.
Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 56.06 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 23 NSNCPSS--EGQRVFAKYLVEELKGLGLE---DANVDENSYVMATLKGnvEGVPTIGFISHLDTApdvtgkdvkpriien 97
Cdd:cd03885 10 NIESGTYdkEGVDRVAELLAEELEALGFTverRPLGEFGDHLIATFKG--TGGKRVLLIGHMDTV--------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 98 ydgkdivlneelnvvtstkdYPEmKTLAGQDIIVtDGTTLLG---ADDKAGIAEIVTAIEYLVNNPEIKHGDIKIGFTPD 174
Cdd:cd03885 73 --------------------FPE-GTLAFRPFTV-DGDRAYGpgvADMKGGLVVILHALKALKAAGGRDYLPITVLLNSD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 175 EEVGR--GADLFdvEKFGAKYAYTID---GGILGELQYENFNAAAATITIQGRNVHPGSAKNKLVNAL----HIAAEISE 245
Cdd:cd03885 131 EEIGSpgSRELI--EEEAKGADYVLVfepARADGNLVTARKGIGRFRLTVKGRAAHAGNAPEKGRSAIyelaHQVLALHA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 246 MfpASERPETTevyegfyhlndIN-GNVESATMIYIIRDHDKAKF-------EERKAFMTSAIEKINEKYEGRVKLDLND 317
Cdd:cd03885 209 L--TDPEKGTT-----------VNvGVISGGTRVNVVPDHAEAQVdvrfataEEADRVEEALRAIVATTLVPGTSVELTG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 318 QYYNM-KEKVEPVKFVVDIVEEAMKETEIAPLIVPIRGGTDGARLSFMGLpcPNIFTGGL---NFHSKNECISVQAMEKG 393
Cdd:cd03885 276 GLNRPpMEETPASRRLLARAQEIAAELGLTLDWEATGGGSDANFTAALGV--PTLDGLGPvggGAHTEDEYLELDSLVPR 353
|
....*..
gi 821175516 394 ANLIVKI 400
Cdd:cd03885 354 IKLLARL 360
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
30-237 |
2.57e-08 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 55.41 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 30 EGQRVFAKYLVEELKGLG----LEDANVDENSYVMATLKGNveGVPTIGFISHLDTApdvtgkdvkpriienydgkdivl 105
Cdd:PRK06133 57 EGLKQVAALLAERLKALGakveRAPTPPSAGDMVVATFKGT--GKRRIMLIAHMDTV----------------------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 106 neelnvvtstkdYPEmKTLAGQDIIVtDGTTLLG---ADDKAGIAEIVTAIEYLVNNPEIKHGDIKIGFTPDEEVGRGAD 182
Cdd:PRK06133 112 ------------YLP-GMLAKQPFRI-DGDRAYGpgiADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGSPGS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 821175516 183 LFDVEKFGAKYAYTID---GGILGELQYENFNAAAATITIQGRNVHPGSAKNKLVNAL 237
Cdd:PRK06133 178 RELIAELAAQHDVVFScepGRAKDALTLATSGIATALLEVKGKASHAGAAPELGRNAL 235
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
1-403 |
6.09e-07 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 51.14 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 1 MKEKVLERFLKYVAFDTTADPKnsncpssEGQRVFAKYLVEELKGLGLEdanvdensyvmatlkgnvegvptigfiSHLD 80
Cdd:PRK08651 4 MMFDIVEFLKDLIKIPTVNPPG-------ENYEEIAEFLRDTLEELGFS---------------------------TEII 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 81 TAPDVTGKDVKPR----IIENYDG-KDIVLNEELNVVtSTKDyPEMKT-----LAGQDIIVTDGTTllgaDDKAGIAEIV 150
Cdd:PRK08651 50 EVPNEYVKKHDGPrpnlIARRGSGnPHLHFNGHYDVV-PPGE-GWSVNvpfepKVKDGKVYGRGAS----DMKGGIAALL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 151 TAIEYLVnnpEIKHGDIKIGFTPDEEV-GRGAD-LFDVEKFGAKYAYTIDGGILGELQYENFNAAAATITIQGRNVH--- 225
Cdd:PRK08651 124 AAFERLD---PAGDGNIELAIVPDEETgGTGTGyLVEEGKVTPDYVIVGEPSGLDNICIGHRGLVWGVVKVYGKQAHast 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 226 PGSAKNKLVNALHIAAEISEMFPASERP-ETTEVYEGFYHLNDINGNVESATMIYIIRD------------HDKAK--FE 290
Cdd:PRK08651 201 PWLGINAFEAAAKIAERLKSSLSTIKSKyEYDDERGAKPTVTLGGPTVEGGTKTNIVPGycafsidrrlipEETAEevRD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 291 ERKAFMTSAIEKINEKYEGRVKLDLNDQYynmkekVEPVKFVVDIVEEAMKETE-IAPLIVPIRGGTDGARLSFMGLPCP 369
Cdd:PRK08651 281 ELEALLDEVAPELGIEVEFEITPFSEAFV------TDPDSELVKALREAIREVLgVEPKKTISLGGTDARFFGAKGIPTV 354
|
410 420 430
....*....|....*....|....*....|....*
gi 821175516 370 NIFTGGL-NFHSKNECISVQAMEKGANLIVKIAEK 403
Cdd:PRK08651 355 VYGPGELeLAHAPDEYVEVKDVEKAAKVYEEVLKR 389
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
140-361 |
2.75e-06 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 49.11 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 140 ADDKAGIAEIVTAIEYLVNNPEIKHGDIKIGFTPDEEVGR-GADLFdVEKfgaKYAYTIDGGILGE-----LQYENFNAA 213
Cdd:PRK08588 99 TDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGElGAKQL-TEK---GYADDLDALIIGEpsghgIVYAHKGSM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 214 AATITIQGRNVH---PGSAKNKLVNALHIAAEISEMFpaSERPETTEVYEGFYHLND-INGNV------ESATMIYIIR- 282
Cdd:PRK08588 175 DYKVTSTGKAAHssmPELGVNAIDPLLEFYNEQKEYF--DSIKKHNPYLGGLTHVVTiINGGEqvnsvpDEAELEFNIRt 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 283 ----DHDKAkfeerKAFMTSAIEKINEKYEGRVKLDLndqYYNMKekvePV------KFVVDIVEEAMKETEIAPLIVPI 352
Cdd:PRK08588 253 ipeyDNDQV-----ISLLQEIINEVNQNGAAQLSLDI---YSNHR----PVasdkdsKLVQLAKDVAKSYVGQDIPLSAI 320
|
....*....
gi 821175516 353 RGGTDGARL 361
Cdd:PRK08588 321 PGATDASSF 329
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
83-392 |
1.22e-05 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE 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 subfamily are mostly archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349933 [Multi-domain] Cd Length: 355 Bit Score: 47.00 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 83 PDVTGKDVKPRIIENYDGKDIVLNEELNVVTSTKD----YPEMKTLAGQDIIVTDGTtllgADDKAGIAEIVTAIEYLVN 158
Cdd:cd08011 43 PPEEIYGVVSNIVGGRKGKRLLFNGHYDVVPAGDGegwtVDPYSGKIKDGKLYGRGS----SDMKGGIAASIIAVARLAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 159 NPEIKHGDIKIGFTPDEE-VGRGADLFDVEKFGAKYAYTIDGGILGEL--QYENFNAAAATITIQGRNVHpGSAKNKLVN 235
Cdd:cd08011 119 AKAPWDLPVVLTFVPDEEtGGRAGTKYLLEKVRIKPNDVLIGEPSGSDniRIGEKGLVWVIIEITGKPAH-GSLPHRGES 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 236 ALHIAAEISEMFPASERPETTEVYEGFYHLNDINGNVESATMIYIIRDHDKakfEERKAFMTSAIEKInEKYEGRVKldl 315
Cdd:cd08011 198 AVKAAMKLIERLYELEKTVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGIST---DEVLSRIIDHLDSI-EEVSFEIK--- 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821175516 316 ndQYYNMKEKvEPVKFVVDIVEEAMKET-EIAPLIVPIRGGTDGARLSFMGLPCPNIFTGGL-NFHSKNECISVQAMEK 392
Cdd:cd08011 271 --SFYSPTVS-NPDSEIVKKTEEAITEVlGIRPKEVISVGASDARFYRNAGIPAIVYGPGRLgQMHAPNEYVEIDELIK 346
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
128-339 |
1.33e-05 |
|
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.
Pssm-ID: 349885 [Multi-domain] Cd Length: 474 Bit Score: 47.13 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 128 DIIVTDGTTLlGADDKAGIAEIVTAIEylvnNPEIKHGDIKIGFTPDEEVG-RGADLFDVEKFGAKYAYTID-------- 198
Cdd:cd03890 95 DWLKATGTTL-GADNGIGVAYALAILE----DKDIEHPPLEVLFTVDEETGmTGALGLDPSLLKGKILLNLDseeegelt 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 199 ----GGILG----ELQYENFNAA--AATITIQG-RNVHPGSAKNK-LVNALHIAAEIsemfpASERPETTEvyegfYHLN 266
Cdd:cd03890 170 vgcaGGIDVtitlPIEREEAEGGytGLKITVKGlKGGHSGVDIHKgRANANKLMARL-----LYELAKELD-----FRLV 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821175516 267 DING----NV--ESATMIYIIrdhDKAKFEERKAFMTSAIEKINEKYEGRVKldlndqyyNMKEKVEPVKFVVDIVEEA 339
Cdd:cd03890 240 SINGgtkrNAipREAVAVIAV---PAEDVEALKKLIKKLEKALKAEYAGTDP--------NLKIEVEKVETPKVVLSEA 307
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
127-396 |
1.36e-04 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 43.80 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 127 QDIIVTDGTTLLG---ADDKAGIAEIVTAIEYLVNNPeikHGDiKIGF----TPDEEVG--RGADLFdvekfgAKYAYTI 197
Cdd:PRK07338 112 QTLSWLDDGTLNGpgvADMKGGIVVMLAALLAFERSP---LAD-KLGYdvliNPDEEIGspASAPLL------AELARGK 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 198 DGGILGELQYENFNAAAA-------TITIQGRNVHPGSAKNKLVNALHIAAEISEMFPA--SERPETTeVYEGFyhlndI 268
Cdd:PRK07338 182 HAALTYEPALPDGTLAGArkgsgnfTIVVTGRAAHAGRAFDEGRNAIVAAAELALALHAlnGQRDGVT-VNVAK-----I 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 269 NG----NV--ESATMIYIIRdhdkAKFEERKAFMTSAIEKINEKYEGR--VKLDLNDQYYnmkekvEPVKfVVDIVEEAM 340
Cdd:PRK07338 256 DGggplNVvpDNAVLRFNIR----PPTPEDAAWAEAELKKLIAQVNQRhgVSLHLHGGFG------RPPK-PIDAAQQRL 324
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 821175516 341 KET--EIAPLI-VPIR-----GGTDGARLSFMGLpcPNIFT----GGlNFHSKNECISVQAMEKGANL 396
Cdd:PRK07338 325 FEAvqACGAALgLTIDwkdsgGVCDGNNLAAAGL--PVVDTlgvrGG-NIHSEDEFVILDSLVERAQL 389
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
23-400 |
3.34e-04 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE 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 subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349901 [Multi-domain] Cd Length: 389 Bit Score: 42.45 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 23 NSNCPSS--EGQRVFAKYLVEELKGLG--------LEDANVDENSYVMATL-KGNVEgvpTIGFISHLDTAP--DVTGKD 89
Cdd:cd05650 14 PAVNPESggEGEKEKADYLEKKLREYGfytlerydAPDERGIIRPNIVAKIpGGNDK---TLWIISHLDTVPpgDLSLWE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 90 VKPRIIENYDGKDIVLNEELN---VVTSTkdypemktLAGQDIIvTDGTT-------LLGADDKAGIAeivTAIEYLVNN 159
Cdd:cd05650 91 TDPWEPVVKDGKIYGRGVEDNqqgIVSSL--------LALKAII-KNGITpkynfglLFVADEEDGSE---YGIQYLLNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 160 PEIkhgdikigFTPDeevgrgaDLFDVEKFGAKYAYTIDGGILGELQYEnfnaaaatITIQGRNVH---PGSAKNKLVNA 236
Cdd:cd05650 159 FDL--------FKKD-------DLIIVPDFGTEDGEFIEIAEKSILWIK--------VNVKGKQCHastPENGINAFVAA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 237 LHIAAEISEMF------------PASERPETTEVYEGFYHLNDINGNVEsatmIYI-IRDHDKAKFEERKAFMTSAIEKI 303
Cdd:cd05650 216 SNFALELDELLhekfdekddlfnPPYSTFEPTKKEANVPNVNTIPGYDV----FYFdCRVLPTYKLDEVLKFVNKIISDF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821175516 304 NEKYEGRVKLDLNDQYYNMKEKVEPVKFVVDIVEEAMKETEIAPLIVPIRGGTDGARLSFMGLPCPNIFTGGLNFHSKNE 383
Cdd:cd05650 292 ENSYGAGITYEIVQKEQAPPATPEDSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNE 371
|
410
....*....|....*..
gi 821175516 384 CISVQAMEKGANLIVKI 400
Cdd:cd05650 372 YIRISHIVKDAKVFAEM 388
|
|
| M42_glucanase_like |
cd05657 |
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ... |
141-181 |
1.54e-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: 40.34 E-value: 1.54e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 821175516 141 DDKAGIAEIVTAIEYLVNNPEIKHGDIKIGFTPDEEVGRGA 181
Cdd:cd05657 181 DDKASVAILLALARALKENKLKLPVDTHFLFSNYEEVGHGA 221
|
|
| |
