|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
1-408 |
0e+00 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 810.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 1 MEKLTQRFIDYIKIDTQSDPESTTTPSTEKQWNLARKLVEELKQIGLKDVTIDENAYVMATLPSNVTHHVPTIGFIAHFD 80
Cdd:PRK05469 1 MDKLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDENGYVMATLPANVDKDVPTIGFIAHMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 81 TSPDFSGENVNPQFVENYDGNDIVLNKEqNIVLSPSYFEDLLLYKGQTLITTDGTTLLGADDKAGVAEIVTAMEYLVKHP 160
Cdd:PRK05469 81 TAPDFSGKNVKPQIIENYDGGDIALGDG-NEVLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYLIAHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 161 EIKHGKIRVGFTPDEEIGRGAHKFDVAKFGAEWAYTMDGSQVGELEYENFNAAGAKVLFKGKSVHPGYAKNKMVNSLLIA 240
Cdd:PRK05469 160 EIKHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALLLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 241 NEFVGALPESQVPERTSGREGFFHVTSISGDIENTVVQLIVRNHDRELFEKQKQLLHQIVDDLNQKH-NNAVSIEIKDQY 319
Cdd:PRK05469 240 ADFHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKYgEGRVELEIKDQY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 320 YNMREKVEPVFHIVEIAEQAMKDLGITPIIKPIRGGTDGSQLSFMGLPCPNIFAGGHNFHGKFEYVPVESMQKATQVIVK 399
Cdd:PRK05469 320 YNMREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVIVE 399
|
....*....
gi 1390593006 400 ITEITANRY 408
Cdd:PRK05469 400 IAELTAERA 408
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
4-402 |
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: 727.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 4 LTQRFIDYIKIDTQSDPESTTTPSTEKQWNLARKLVEELKQIGLKDVTIDENAYVMATLPSNVTHHVPTIGFIAHFDTSP 83
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDEHGYVTATLPANVDKDVPTIGFIAHMDTAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 84 DFSGENVNPQFVENYDGNDIVLNkEQNIVLSPSYFEDLLLYKGQTLITTDGTTLLGADDKAGVAEIVTAMEYLVKHPEIK 163
Cdd:cd03892 81 DNSGKNVKPQIIENYDGGDIVLN-ESGIVLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIEHPEIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 164 HGKIRVGFTPDEEIGRGAHKFDVAKFGAEWAYTMDGSQVGELEYENFNAAGAKVLFKGKSVHPGYAKNKMVNSLLIANEF 243
Cdd:cd03892 160 HGDIRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLAADF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 244 VGALPESQVPERTSGREGFFHVTSISGDIENTVVQLIVRNHDRELFEKQKQLLHQIVDDLNQKH-NNAVSIEIKDQYYNM 322
Cdd:cd03892 240 HSMLPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKYgEGRVELEIKDQYYNM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 323 REKVEPVFHIVEIAEQAMKDLGITPIIKPIRGGTDGSQLSFMGLPCPNIFAGGHNFHGKFEYVPVESMQKATQVIVKITE 402
Cdd:cd03892 320 KEKIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIVKIAE 399
|
|
| peptidase-T |
TIGR01882 |
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has ... |
2-407 |
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: 548.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 2 EKLTQRFIDYIKIDTQSDPESTTTPSTEKQWNLARKLVEELKQIGLKDVTIDE-NAYVMATLPSNVTHHVPTIGFIAHFD 80
Cdd:TIGR01882 3 EELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEkNGYVIATIPSNTDKDVPTIGFLAHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 81 TSpDFSGENVNPQFVENYDGNDIVLNKEQNIVLSPSYFEDLLLYKGQTLITTDGTTLLGADDKAGVAEIVTAMEYLVKHP 160
Cdd:TIGR01882 83 TA-DFNGENVNPQIIENYDGESIIQLGDLEFTLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAADYLINHP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 161 EIKHGKIRVGFTPDEEIGRGAHKFDVAKFGAEWAYTMDGSQVGELEYENFNAAGAKVLFKGKSVHPGYAKNKMVNSLLIA 240
Cdd:TIGR01882 162 EIKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAAQIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 241 NEFVGALPESQVPERTSGREGFFHVTSISGDIENTVVQLIVRNHDRELFEKQKQLLHQIVDDLNQKH-NNAVSIEIKDQY 319
Cdd:TIGR01882 242 IDLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEYgQDRIKLDMNDQY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 320 YNMREKVEPVFHIVEIAEQAMKDLGITPIIKPIRGGTDGSQLSFMGLPCPNIFAGGHNFHGKFEYVPVESMQKATQVIVK 399
Cdd:TIGR01882 322 YNMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDVIVE 401
|
....*...
gi 1390593006 400 ITEITANR 407
Cdd:TIGR01882 402 IAKLNEEQ 409
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
1-405 |
0e+00 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 533.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 1 MEKLTQRFIDYIKIDTQSDPEstttpstekqWNLARKLVEELKQIGLkDVTIDENAYVMATLPSNVTHHVPTIGFIAHFD 80
Cdd:COG2195 2 PERLLERFLEYVKIPTPSDHE----------EALADYLVEELKELGL-EVEEDEAGNVIATLPATPGYNVPTIGLQAHMD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 81 TSPDFSGENVNPQFvenyDGNdivlnkeqnivlspsyfedlllykgqtLITTDGTTLLGADDKAGVAEIVTAMEYLvKHP 160
Cdd:COG2195 71 TVPQFPGDGIKPQI----DGG---------------------------LITADGTTTLGADDKAGVAAILAALEYL-KEP 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 161 EIKHGKIRVGFTPDEEIG-RGAHKFDVAKFGAEWAYTMDGSQVGELEYENFNAAGAKVLFKGKSVHPGYAKNKMVNSLLI 239
Cdd:COG2195 119 EIPHGPIEVLFTPDEEIGlRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIKL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 240 ANEFVGALPESQVPERTSGREGFFHVTSI-SGDIENTVVQLIVRNHDRELFEKQKQLLHQIVDDLNQKHNNA-VSIEIKD 317
Cdd:COG2195 199 AARFLAALPLGRIPEETEGNEGFIHGGSAtNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGVGvVEVEIED 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 318 QYYNMREkvEPVFHIVEIAEQAMKDLGITPIIKPIRGGTDGSQLSFMGLPCPNIFAGGHNFHGKFEYVPVESMQKATQVI 397
Cdd:COG2195 279 QYPNWKP--EPDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWELL 356
|
....*...
gi 1390593006 398 VKITEITA 405
Cdd:COG2195 357 VEILKLIA 364
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
2-406 |
0e+00 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 515.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 2 EKLTQRFIDYIKIDTQSDPESTTTPSTEKQWNLARKLVEELKQIGLKDVTIDENAYVMATLPSNVTHhVPTIGFIAHFDT 81
Cdd:PRK13381 1 MQLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDIVIDEHAIVTAKLPGNTPG-APRIGFIAHLDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 82 SpDFSGE-NVNPQfVENYDGNDIVLNKEQNIVLSPSYFEDLLLYKGQTLITTDGTTLLGADDKAGVAEIVTAMEYLVKHp 160
Cdd:PRK13381 80 V-DVGLSpDIHPQ-ILRFDGGDLCLNAEQGIWLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLENLTEN- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 161 EIKHGKIRVGFTPDEEIG-RGAHKFDVAKFGAEWAYTMDGSQVGELEYENFNAAGAKVLFKGKSVHPGYAKNKMVNSLLI 239
Cdd:PRK13381 157 EVEHGDIVVAFVPDEEIGlRGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNPILM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 240 ANEFVGALPESQVPERTSGREGFFHVTSISGDIENTVVQLIVRNHDRELFEKQKQLLHQIVDDLNQKHNNA-VSIEIKDQ 318
Cdd:PRK13381 237 ANDFISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINAKYPTArVSLTLTDQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 319 YYNMREKVEPVFHIVEIAEQAMKDLGITPIIKPIRGGTDGSQLSFMGLPCPNIFAGGHNFHGKFEYVPVESMQKATQVIV 398
Cdd:PRK13381 317 YSNISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEVTI 396
|
....*...
gi 1390593006 399 KITEITAN 406
Cdd:PRK13381 397 TICLLAAK 404
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
4-402 |
4.22e-131 |
|
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: 382.88 E-value: 4.22e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 4 LTQRFIDYIKIDTQSDPESTTTPSTEKQWNLARKLVEELKQIGLKDVTIDENAYVMATLPSNVTHHVPTIGFIAHFDTSP 83
Cdd:cd05645 1 LLERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEKGTLIATLPANVDGDIPAIGFISHVDTSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 84 DFSGENVNPQFVENYDGNDIVLNKEQNiVLSPSYFEDLLLYKGQTLITTDGTTLLGADDKAGVAEIVTAMEYLVKHPeIK 163
Cdd:cd05645 81 DGSGKNVNPQIVENYRGGDIALGIGDE-VLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKN-IP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 164 HGKIRVGFTPDEEIGRGAHKFDVAKFGAEWAYTMDGSQVGELEYENFNAAGAKVLFKGKSVHPGYAKNKMVNSLLIANEF 243
Cdd:cd05645 159 HGDIEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAARI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 244 VGALPESQVPERTSGREGFFHVTSISGDIENTVVQLIVRNHDRELFEKQKQLLHQIVDDLNQKHNNA--VSIEIKDQYYN 321
Cdd:cd05645 239 HAEVPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVGKGLHPDcyIELVIEDSYYN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 322 MREKVEPVFHIVEIAEQAMKDLGITPIIKPIRGGTDGSQLSFMGLPCPNIFAGGHNFHGKFEYVPVESMQKATQVIVKIT 401
Cdd:cd05645 319 FREKVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIVRIA 398
|
.
gi 1390593006 402 E 402
Cdd:cd05645 399 E 399
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
2-403 |
3.54e-40 |
|
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: 146.83 E-value: 3.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 2 EKLTQRFIDYIKIDTQSDPEStttpstekqwNLARKLVEELKQIGLkDVTIDENAYV--------MATLPSNVtHHVPTI 73
Cdd:cd05683 3 DRLINTFLELVQIDSETLHEK----------EISKVLKKKFENLGL-SVIEDDAGKTtgggagnlICTLKADK-EEVPKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 74 GFIAHFDT-SPdfsGENVNPQFVENydgndivlnkeqnivlspsyfedlllykgqTLITTDGTTLLGADDKAGVAEIVTA 152
Cdd:cd05683 71 LFTSHMDTvTP---GINVKPPQIAD------------------------------GYIYSDGTTILGADDKAGIAAILEA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 153 MEYLvKHPEIKHGKIRVGFTPDEEIGR-GAHKFDVAKFGAEWAYTMDGS-QVGELEYENFNAAGAKVLFKGKSVHPGYAK 230
Cdd:cd05683 118 IRVI-KEKNIPHGQIQFVITVGEESGLvGAKALDPELIDADYGYALDSEgDVGTIIVGAPTQDKINAKIYGKTAHAGTSP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 231 NKMVNSLLIANEFVGALPESQVPERTSGREGFFHvtsiSGDIENTV---VQLI--VRNHDRELFEKQKQLLHQIVDDLNQ 305
Cdd:cd05683 197 EKGISAINIAAKAISNMKLGRIDEETTANIGKFQ----GGTATNIVtdeVNIEaeARSLDEEKLDAQVKHMKETFETTAK 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 306 KHNNAVSIEIKDQYYNMreKVEPVFHIVEIAEQAMKDLGITPIIKPIRGGTDGSQLSFMGLPCPNIFAGGHNFHGKFEYV 385
Cdd:cd05683 273 EKGAHAEVEVETSYPGF--KINEDEEVVKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERI 350
|
410
....*....|....*...
gi 1390593006 386 PVESMQKATQVIVKITEI 403
Cdd:cd05683 351 PIEDLYDTAVLVVEIIKE 368
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
3-402 |
7.09e-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: 140.45 E-value: 7.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 3 KLTQRFIDYIKIDTQSDPESTTTPSTEKQWNlarKLVEELKQIGLKDVTIDENAyVMATLPSnvTHHVPTIGFIAHFDTS 82
Cdd:TIGR01883 1 RLKKYFLELIQIDSESGKEKAILTYLKKQIT---KLGIPVSLDEVPAEVSNDNN-LIARLPG--TVKFDTIFFCGHMDTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 83 PDfsGENVNPQfVENydgndivlnkeqnivlspsyfedlllykgqTLITTDGTTLLGADDKAGVAEIVTAMEYLvKHPEI 162
Cdd:TIGR01883 75 PP--GAGPEPV-VED------------------------------GIFTSLGGTILGADDKAGVAAMLEAMDVL-STEET 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 163 KHGKIRVGFTPDEEIG-RGAHKFDVAKFGAEWAYTMD-GSQVGELEYENFNAAGAKVLFKGKSVHPGYAKNKMVNSLLIA 240
Cdd:TIGR01883 121 PHGTIEFIFTVKEELGlIGMRLFDESKITAAYGYCLDaPGEVGNIQLAAPTQVKVDATIAGKDAHAGLVPEDGISAISVA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 241 NEFVGALPESQVPERTSGREGFFhvtsiSGDIENTVVQ---LIVRNHDRELFEKQKQLLHQIVDDLNQ---KHNNAVSIE 314
Cdd:TIGR01883 201 RMAIHAMRLGRIDEETTANIGSF-----SGGVNTNIVQdeqLIVAEARSLSFRKAEAQVQTMRERFEQaaeKYGATLEEE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 315 IKDQYYNMreKVEPVFHIVEIAEQAMKDLGITPIIKPIRGGTDGSQLSFMGLPCPNIFAGGHNFHGKFEYVPVESMQKAT 394
Cdd:TIGR01883 276 TRLIYEGF--KIHPQHPLMNIFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETISIEQLVKLA 353
|
....*...
gi 1390593006 395 QVIVKITE 402
Cdd:TIGR01883 354 ELVIALAE 361
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
10-400 |
1.31e-25 |
|
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: 106.89 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 10 DYIKIDTQSDPEStttpstekqwNLARKLVEELKQIGLkDVTIDEN----AYVMATLPSNVTHhvPTIGFIAHFDTSP-- 83
Cdd:COG0624 20 ELVRIPSVSGEEA----------AAAELLAELLEALGF-EVERLEVppgrPNLVARRPGDGGG--PTLLLYGHLDVVPpg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 84 DFSGENVNPqfvenydgndivlnkeqnivlspsyFEdlllykgqtlITTDGTTLLG---ADDKAGVAEIVTAMEYLVKHP 160
Cdd:COG0624 87 DLELWTSDP-------------------------FE----------PTIEDGRLYGrgaADMKGGLAAMLAALRALLAAG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 161 EIKHGKIRVGFTPDEEIG-RGAHKF---DVAKFGAEWAYTMDGSQVGELEYENFNAAGAKVLFKGKSVHPGYAkNKMVNS 236
Cdd:COG0624 132 LRLPGNVTLLFTGDEEVGsPGARALveeLAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAHSSRP-ELGVNA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 237 LLIANEFVGALPESQVPERTSGREGF--FHVTSIS-GDIENTV-----VQLIVRNHDRELFEKQKQLLHQIVDdlnqKHN 308
Cdd:COG0624 211 IEALARALAALRDLEFDGRADPLFGRttLNVTGIEgGTAVNVIpdeaeAKVDIRLLPGEDPEEVLAALRALLA----AAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 309 NAVSIEIKDQYYNMREKVEPVFH-IVEIAEQAMKDL-GITPIIKPIRGGTDGSQLS-FMGLPCPNI-FAGGHNFHGKFEY 384
Cdd:COG0624 287 PGVEVEVEVLGDGRPPFETPPDSpLVAAARAAIREVtGKEPVLSGVGGGTDARFFAeALGIPTVVFgPGDGAGAHAPDEY 366
|
410
....*....|....*.
gi 1390593006 385 VPVESMQKATQVIVKI 400
Cdd:COG0624 367 VELDDLEKGARVLARL 382
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
140-400 |
2.77e-19 |
|
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: 87.79 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 140 ADDKAGVAEIVTAMEYLVKHPeIKHGKIRVGFTPDEEIGRG-----AHKFDVAKFGAEWAYTMDGSQVGELEYENFNAAG 214
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEG-LKKGTVKLLFQPDEEGGMGgaralIEDGLLEREKVDAVFGLHIGEPTLLEGGIAIGVV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 215 A--------KVLFKGKSVH---PGYAknkmVNSLLIANEFVGALPESQVPERTSGREGFFHVTSISGdIENTV------- 276
Cdd:pfam01546 112 TghrgslrfRVTVKGKGGHastPHLG----VNAIVAAARLILALQDIVSRNVDPLDPAVVTVGNITG-IPGGVnvipgea 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 277 -VQLIVRNHDRELFEKQKQLLHQIVDDLNQKHNNAVSIEIKDQYYNMREKVEPvfhIVEIAEQAMKDL-GITP--IIKPI 352
Cdd:pfam01546 187 eLKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEYVEGGAPPLVNDSP---LVAALREAAKELfGLKVelIVSGS 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1390593006 353 RGGTDGsqlSFMGLPCPNIF----AGGHNFHGKFEYVPVESMQKATQVIVKI 400
Cdd:pfam01546 264 MGGTDA---AFFLLGVPPTVvffgPGSGLAHSPNEYVDLDDLEKGAKVLARL 312
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
3-400 |
5.58e-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: 81.58 E-value: 5.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 3 KLTQRFIdyiKIDTQSDPESTTtpstekqwnlARKLVEELKQIGLK-DVTIDENAY-VMATLPSNVThhvPTIGFIAHFD 80
Cdd:cd08659 1 SLLQDLV---QIPSVNPPEAEV----------AEYLAELLAKRGYGiESTIVEGRGnLVATVGGGDG---PVLLLNGHID 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 81 TspdfsgenVNPQFVENYDgndivlnkeqnivLSPsyFE----DLLLYkgqtlittdGttlLGADD-KAGVAEIVTAMEY 155
Cdd:cd08659 65 T--------VPPGDGDKWS-------------FPP--FSgrirDGRLY---------G---RGACDmKGGLAAMVAALIE 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 156 LVKHPEIKHGKIRVGFTPDEEIG-RGAHKFDVAKFGAEWAYTMDG---------SQVGELEYEnfnaagakVLFKGKSVH 225
Cdd:cd08659 110 LKEAGALLGGRVALLATVDEEVGsDGARALLEAGYADRLDALIVGeptgldvvyAHKGSLWLR--------VTVHGKAAH 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 226 PGYaKNKMVNSLLIANEFVGALpESQVPERTSG---REGFFHVTSISGDIE-NTV-----VQLIVR---NHDRELFekqK 293
Cdd:cd08659 182 SSM-PELGVNAIYALADFLAEL-RTLFEELPAHpllGPPTLNVGVINGGTQvNSIpdeatLRVDIRlvpGETNEGV---I 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 294 QLLHQIVDdlnqKHNNAVSIEIkDQYYNMREKVEPVFHIVEIAEQAMKDLGITPIIKPIRGGTDGSQLS-FMGLPCPnIF 372
Cdd:cd08659 257 ARLEAILE----EHEAKLTVEV-SLDGDPPFFTDPDHPLVQALQAAARALGGDPVVRPFTGTTDASYFAkDLGFPVV-VY 330
|
410 420 430
....*....|....*....|....*....|
gi 1390593006 373 AGG--HNFHGKFEYVPVESMQKATQVIVKI 400
Cdd:cd08659 331 GPGdlALAHQPDEYVSLEDLLRAAEIYKEI 360
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
71-397 |
3.89e-13 |
|
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: 67.84 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 71 PTIGFIAHFDTSPDFSGENVNPQFVEnydgndivlnkeqnivlspsyfedlllykgQTLITTDGTTLLGADDKAGVAEIV 150
Cdd:cd03873 13 KSVALGAHLDVVPAGEGDNRDPPFAE------------------------------DTEEEGRLYGRGALDDKGGVAAAL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 151 TAMEYLVKHPEIKHGKIRVGFTPDEEIGRGAHKFDVAKFGAEwaytmdgsqvgeleyenfnaagakvlfkgksvhpgyak 230
Cdd:cd03873 63 EALKRLKENGFKPKGTIVVAFTADEEVGSGGGKGLLSKFLLA-------------------------------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 231 nkmvnsllianefvgalpesqvpertsgreGFFHVTSIsgdientvvqlivrnhdrelfekqkqllhqIVDDLNQKHNNA 310
Cdd:cd03873 105 ------------------------------EDLKVDAA------------------------------FVIDATAGPILQ 124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 311 VsieikdqyynmreKVEPVFHIVEIAEQAMKDLGITP-IIKPIRGGTDGSQLSFMGLPCPNIFAGGH-NFHGKFEYVPVE 388
Cdd:cd03873 125 K-------------GVVIRNPLVDALRKAAREVGGKPqRASVIGGGTDGRLFAELGIPGVTLGPPGDkGAHSPNEFLNLD 191
|
....*....
gi 1390593006 389 SMQKATQVI 397
Cdd:cd03873 192 DLEKATKVY 200
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
28-403 |
8.49e-13 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 69.02 E-value: 8.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 28 TEKQWNLARKLVEELKQIGLKDVTIDenaYVMATLPSnvthhvptigfiAHFDTSPDFSGENVNpqfvenydgndIVLNK 107
Cdd:PRK08652 1 TERAKELLKQLVKIPSPSGQEDEIAL---HIMEFLES------------LGYDVHIESDGEVIN-----------IVVNS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 108 EQNIVLSPSYfeDLLLYKgqTLITTDGTTLLG---ADDKAGVAEIVTAMEYLVKhpEIKHGKIRVGFTPDEEI-GRGAHK 183
Cdd:PRK08652 55 KAELFVEVHY--DTVPVR--AEFFVDGVYVYGtgaCDAKGGVAAILLALEELGK--EFEDLNVGIAFVSDEEEgGRGSAL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 184 FdVAKFGAEWAYTMDGSQvGELEYENFNAAGAKVLFKGKSVHpGYAKNKMVNSLLIANEFVGALpESQVPERTSGREGFF 263
Cdd:PRK08652 129 F-AERYRPKMAIVLEPTD-LKVAIAHYGNLEAYVEVKGKPSH-GACPESGVNAIEKAFEMLEKL-KELLKALGKYFDPHI 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 264 HVTSISGDIENTVVQLIVR-NHDRELFEKQK-----QLLHQIVDDLNQKHNNAvsiEIKDQYYnmrekVEPVFHIVEIAE 337
Cdd:PRK08652 205 GIQEIIGGSPEYSIPALCRlRLDARIPPEVEvedvlDEIDPILDEYTVKYEYT---EIWDGFE-----LDEDEEIVQLLE 276
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390593006 338 QAMKDLGITPIIKPIRGGTDGSQLSFMGLPcPNIFAGG--HNFHGKFEYVPVESMQKATQVIVKITEI 403
Cdd:PRK08652 277 KAMKEVGLEPEFTVMRSWTDAINFRYNGTK-TVVWGPGelDLCHTKFERIDVREVEKAKEFLKALNEI 343
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
127-389 |
2.27e-12 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 68.07 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 127 QTLITTDGTTLLG---ADDKAGVAEIVTAMEYLVKHPEIKHGKIRVGFTPDEEIGRGAHKFDVAKFGAewaytmdGSQVG 203
Cdd:PRK07338 112 QTLSWLDDGTLNGpgvADMKGGIVVMLAALLAFERSPLADKLGYDVLINPDEEIGSPASAPLLAELAR-------GKHAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 204 eLEYE----NFNAAGAK-------VLFKGKSVHPGYAKNKMVNSLLIANEFVGALpesqvpERTSG-REGF-FHVTSISG 270
Cdd:PRK07338 185 -LTYEpalpDGTLAGARkgsgnftIVVTGRAAHAGRAFDEGRNAIVAAAELALAL------HALNGqRDGVtVNVAKIDG 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 271 ----DI--ENTVVQLIVRNHDRELFEKQKQLLHQIVDDLNQKHNnaVSIEIKDQYYN----MREKVEPVFHIVeiaEQAM 340
Cdd:PRK07338 258 ggplNVvpDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHG--VSLHLHGGFGRppkpIDAAQQRLFEAV---QACG 332
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1390593006 341 KDLGITPIIKPIRGGTDGSQLSFMGLPCPNIF-AGGHNFHGKFEYVPVES 389
Cdd:PRK07338 333 AALGLTIDWKDSGGVCDGNNLAAAGLPVVDTLgVRGGNIHSEDEFVILDS 382
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
71-397 |
1.66e-11 |
|
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: 62.84 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 71 PTIGFIAHFDTSPDFSGENVNPQFVEnydgndivlnkeqnivlspsyfedlllykgQTLITTDGTTLLGADDKAGVAEIV 150
Cdd:cd18669 13 KRVLLGAHIDVVPAGEGDPRDPPFFV------------------------------DTVEEGRLYGRGALDDKGGVAAAL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 151 TAMEYLVKHPEIKHGKIRVGFTPDEEIGRGAHKFDVAKFGAewaytmdgsqvgeleyENFNAAGAkvlfkgksvhpgyak 230
Cdd:cd18669 63 EALKLLKENGFKLKGTVVVAFTPDEEVGSGAGKGLLSKDAL----------------EEDLKVDY--------------- 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 231 nkmvnsllianefvgalpesqvpertsgregffhvtSISGDIENTVVQlivrnhdrelfekqkqllhqivddlnqkhnna 310
Cdd:cd18669 112 ------------------------------------LFVGDATPAPQK-------------------------------- 123
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 311 vsieikdqyynmreKVEPVFHIVEIAEQAMKDLGITP-IIKPIRGGTDGSQLSFMGLPCPNIFAGGHNF-HGKFEYVPVE 388
Cdd:cd18669 124 --------------GVGIRTPLVDALSEAARKVFGKPqHAEGTGGGTDGRYLQELGIPGVTLGAGGGKGaHSPNERVNLE 189
|
....*....
gi 1390593006 389 SMQKATQVI 397
Cdd:cd18669 190 DLESALAVL 198
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
130-400 |
3.39e-10 |
|
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: 61.07 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 130 ITTDGTTLLG---ADDKAGVAEIVTAMEYLVKHPEIKHGKIRVGFTPDEEIG---------RGAHKFDVAkFGAEWAYTm 197
Cdd:cd03885 83 FTVDGDRAYGpgvADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGspgsrelieEEAKGADYV-LVFEPARA- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 198 DGSQV----GeleyenfnAAGAKVLFKGKSVHPGYAKNKMVNSLLIANEFVGALPESQVPER-TSgregfFHVTSIS-GD 271
Cdd:cd03885 161 DGNLVtarkG--------IGRFRLTVKGRAAHAGNAPEKGRSAIYELAHQVLALHALTDPEKgTT-----VNVGVISgGT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 272 IENTV-----VQLIVRNHDRELFEKQKQLLHQIVddlNQKHNNAVSIEIKdqyynmREKVEPVF-------HIVEIAEQA 339
Cdd:cd03885 228 RVNVVpdhaeAQVDVRFATAEEADRVEEALRAIV---ATTLVPGTSVELT------GGLNRPPMeetpasrRLLARAQEI 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1390593006 340 MKDLGITPIIKPIRGGTDGSQLSFMGLPCPNIF-AGGHNFHGKFEYVPVESMQKATQVIVKI 400
Cdd:cd03885 299 AAELGLTLDWEATGGGSDANFTAALGVPTLDGLgPVGGGAHTEDEYLELDSLVPRIKLLARL 360
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
207-306 |
4.98e-09 |
|
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: 53.50 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 207 YENFNAAGAKVLFKGKSVHPGYaKNKMVNSLLIANEFVGALPESQVPERTSGREGFFHVTSISGDIENTVV------QLI 280
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGA-PGKGVNAIKLLARLLAELPAEYGDIGFDFPRTTLNITGIEGGTATNVIpaeaeaKFD 79
|
90 100
....*....|....*....|....*.
gi 1390593006 281 VRnhdRELFEKQKQLLHQIVDDLNQK 306
Cdd:pfam07687 80 IR---LLPGEDLEELLEEIEAILEKE 102
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
146-362 |
6.61e-09 |
|
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: 57.22 E-value: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 146 VAEIVTAMEYLVKHPEIKHGKIRVGFTPDEEIGRGA-----------HKFDVAkFGaewAYTMDGSQVGELEYE--NFNA 212
Cdd:cd03886 94 TAMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPGGAkamieegvlenPGVDAA-FG---LHVWPGLPVGTVGVRsgALMA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 213 A--GAKVLFKGKSVHpGYAKNKMVNSLLIANEFVGALpESQVPERTSGREGF-FHVTSIS-GDIENT-----VVQLIVRN 283
Cdd:cd03886 170 SadEFEITVKGKGGH-GASPHLGVDPIVAAAQIVLAL-QTVVSRELDPLEPAvVTVGKFHaGTAFNVipdtaVLEGTIRT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 284 HDRELFEKQKQLLHQIVDDLNQKHNNAVSIEIKDQY---YNMREkvepvfhIVEIAEQAMKDLGI---TPIIKPIRGGTD 357
Cdd:cd03886 248 FDPEVREALEARIKRLAEGIAAAYGATVELEYGYGYpavINDPE-------LTELVREAAKELLGeeaVVEPEPVMGSED 320
|
....*
gi 1390593006 358 GSQLS 362
Cdd:cd03886 321 FAYYL 325
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
1-398 |
1.85e-08 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 55.77 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 1 MEKLTQRFIDYIKIDTQSdpestttPSTEKQWNLARKLVEELKQIGLkDVTIDE--NAYVMATLPSNVTHHV------PT 72
Cdd:PRK08651 5 MFDIVEFLKDLIKIPTVN-------PPGENYEEIAEFLRDTLEELGF-STEIIEvpNEYVKKHDGPRPNLIArrgsgnPH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 73 IGFIAHFDTSPDFSGENVNPQFVENYDGNDIvlnkeqnivlspsyfedlllYkGQtlittdGTTllgaDDKAGVAEIVTA 152
Cdd:PRK08651 77 LHFNGHYDVVPPGEGWSVNVPFEPKVKDGKV--------------------Y-GR------GAS----DMKGGIAALLAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 153 MEYLVkhpEIKHGKIRVGFTPDEEI-GRGA-HKFDVAKFGAEWAYtmdgsqVGE---LEYENFNAAG---AKVLFKGKSV 224
Cdd:PRK08651 126 FERLD---PAGDGNIELAIVPDEETgGTGTgYLVEEGKVTPDYVI------VGEpsgLDNICIGHRGlvwGVVKVYGKQA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 225 HPGYAKNKmVNSLLIANEFVGALPESqVPERTSGREGFFHVTS-------------------ISGDIENTVVQLIVRNHD 285
Cdd:PRK08651 197 HASTPWLG-INAFEAAAKIAERLKSS-LSTIKSKYEYDDERGAkptvtlggptveggtktniVPGYCAFSIDRRLIPEET 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 286 RELFEKQkqlLHQIVDDLNQKHNNAVSIEIKDQYynmrEK--VEPVFHIVE-IAEQAMKDLGITPIIKPIRGGTDGSQLS 362
Cdd:PRK08651 275 AEEVRDE---LEALLDEVAPELGIEVEFEITPFS----EAfvTDPDSELVKaLREAIREVLGVEPKKTISLGGTDARFFG 347
|
410 420 430
....*....|....*....|....*....|....*...
gi 1390593006 363 FMGLPCPNiFAGGH--NFHGKFEYVPVESMQKATQVIV 398
Cdd:PRK08651 348 AKGIPTVV-YGPGEleLAHAPDEYVEVKDVEKAAKVYE 384
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
140-361 |
6.38e-08 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 54.12 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 140 ADDKAGVAEIVTAMEYLVKHPEIKHGKIRVGFTPDEEIGR-GAHKFdvAKFGAewAYTMDGSQVGE-----LEYENFNAA 213
Cdd:PRK08588 99 TDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGElGAKQL--TEKGY--ADDLDALIIGEpsghgIVYAHKGSM 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 214 GAKVLFKGKSVH---PGYAKNKMVNSLLIANEFVGALpeSQVPERTSGREGFFHVTSI--SGDIENTV-----VQLIVR- 282
Cdd:PRK08588 175 DYKVTSTGKAAHssmPELGVNAIDPLLEFYNEQKEYF--DSIKKHNPYLGGLTHVVTIinGGEQVNSVpdeaeLEFNIRt 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 283 --NHDRELFekqKQLLHQIVDDLNQKHNNAVSIEIkdqYYNMRekvePVF-----HIVEIA-EQAMKDLGITPIIKPIRG 354
Cdd:PRK08588 253 ipEYDNDQV---ISLLQEIINEVNQNGAAQLSLDI---YSNHR----PVAsdkdsKLVQLAkDVAKSYVGQDIPLSAIPG 322
|
....*..
gi 1390593006 355 GTDGSQL 361
Cdd:PRK08588 323 ATDASSF 329
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
151-387 |
1.07e-06 |
|
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273857 [Multi-domain] Cd Length: 363 Bit Score: 50.42 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 151 TAMeYLVKHPEIKHGKIRVGFTPDEEIGRGAHKF--DVAKFGAEWAYTM-----DGSQVGELEYENFNAAGAK--VLFKG 221
Cdd:TIGR01891 101 TAK-LLKKLADLLEGTVRLIFQPAEEGGGGATKMieDGVLDDVDAILGLhpdpsIPAGTVGLRPGTIMAAADKfeVTIHG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 222 KSVHpGYAKNKMVNSLLIANEFVGALPesQVPERTSG--REGFFHVTSISGD-----IENTV-VQLIVRNHDRELFEKQK 293
Cdd:TIGR01891 180 KGAH-AARPHLGRDALDAAAQLVVALQ--QIVSRNVDpsRPAVVSVGIIEAGgapnvIPDKAsMSGTVRSLDPEVRDQII 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 294 QLLHQIVDDLNQKHNnaVSIEIKdqyynmREKVEPVFHIVEIAEQAMKDLGiTPIIKPIRGGTDgsqlsfmglpcPNIFA 373
Cdd:TIGR01891 257 DRIERIVEGAAAMYG--AKVELN------YDRGLPAVTNDPALTQILKEVA-RHVVGPENVAED-----------PEVTM 316
|
250
....*....|....
gi 1390593006 374 GGHNFHGKFEYVPV 387
Cdd:TIGR01891 317 GSEDFAYYSQKVPG 330
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
71-397 |
4.75e-06 |
|
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: 48.15 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 71 PTIGFIAHFDTSPDFSGEN--VNPqfvenYDGNDivlnkeqnivlspsyfEDLLLYkGQtlittdGTtllgADDKAGVAE 148
Cdd:cd08011 61 KRLLFNGHYDVVPAGDGEGwtVDP-----YSGKI----------------KDGKLY-GR------GS----SDMKGGIAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 149 IVTAMEYLVKHPEIKHGKIRVGFTPDEEIG--RGAH--------KFDVAKF----GAEWAYtmdgsqVGELeyenfNAAG 214
Cdd:cd08011 109 SIIAVARLADAKAPWDLPVVLTFVPDEETGgrAGTKyllekvriKPNDVLIgepsGSDNIR------IGEK-----GLVW 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 215 AKVLFKGKSVHPGYAKnKMVNSLLIANEFVGALPESqvpERTsgregfFHVTSISGDIE-NTVVQLIVRNHDREL----- 288
Cdd:cd08011 178 VIIEITGKPAHGSLPH-RGESAVKAAMKLIERLYEL---EKT------VNPGVIKGGVKvNLVPDYCEFSVDIRLppgis 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 289 FEKQKQLLHQIVDDLNQkhnnaVSIEIKdQYYNMREKvEPVFHIVEIAEQAMKD-LGITPIIKPIRGGTDGSQLSFMGLP 367
Cdd:cd08011 248 TDEVLSRIIDHLDSIEE-----VSFEIK-SFYSPTVS-NPDSEIVKKTEEAITEvLGIRPKEVISVGASDARFYRNAGIP 320
|
330 340 350
....*....|....*....|....*....|.
gi 1390593006 368 CPNIFAGG-HNFHGKFEYVPVESMQKATQVI 397
Cdd:cd08011 321 AIVYGPGRlGQMHAPNEYVEIDELIKVIKVH 351
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
140-238 |
8.34e-06 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 47.70 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 140 ADDKAGVAEIVTAMEYLVKHPEIKHGKIRVGFTPDEEIGRGAHKFDVAKFGAEWAYTMD---GSQVGELEYENFNAAGAK 216
Cdd:PRK06133 135 ADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGSPGSRELIAELAAQHDVVFScepGRAKDALTLATSGIATAL 214
|
90 100
....*....|....*....|..
gi 1390593006 217 VLFKGKSVHPGYAKNKMVNSLL 238
Cdd:PRK06133 215 LEVKGKASHAGAAPELGRNALY 236
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
121-185 |
1.61e-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: 46.74 E-value: 1.61e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1390593006 121 LLLYKGQTLITTDGTTLlGADDKAGVAEIVTAMEylvkHPEIKHGKIRVGFTPDEEIG-RGAHKFD 185
Cdd:cd03890 88 IKLRIDGDWLKATGTTL-GADNGIGVAYALAILE----DKDIEHPPLEVLFTVDEETGmTGALGLD 148
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
147-373 |
4.22e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (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).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 42.32 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 147 AEIVTAMEYLVKHPEIKHGKIRVGFTPDEEIGRGAHKF-------DV-AKFGAE-WAYTMDGSQVGELEYENFNAAGAKV 217
Cdd:cd08019 94 AMLLGAAKILNEIKDTIKGTVKLIFQPAEEVGEGAKQMieegvleDVdAVFGIHlWSDVPAGKISVEAGPRMASADIFKI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 218 LFKGKSVHpGYAKNKMVNSLLIANEFVGALpESQVPERTSGRE------GFFHVTSISGDIENTVVQLI-VRNHDRELFE 290
Cdd:cd08019 174 EVKGKGGH-GSMPHQGIDAVLAAASIVMNL-QSIVSREIDPLEpvvvtvGKLNSGTRFNVIADEAKIEGtLRTFNPETRE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 291 KQKQLLHQIVDDLNQKHNNAVSIEikdqYYNMREKVEPVFHIVEIAEQA-MKDLGiTPIIKPIRGGTDGSQLSFMGLPCP 369
Cdd:cd08019 252 KTPEIIERIAKHTAASYGAEAELT----YGAATPPVINDEKLSKIARQAaIKIFG-EDSLTEFEKTTGSEDFSYYLEEVP 326
|
....
gi 1390593006 370 NIFA 373
Cdd:cd08019 327 GVFA 330
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
328-396 |
1.44e-03 |
|
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.
Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 40.81 E-value: 1.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1390593006 328 PVFHIVEIAEQAM-KDLGITPIIKPirGGTDGSQLSFMGLPC--------PNIFAGGHNFHGKFEYVPVESMQKATQV 396
Cdd:cd05675 350 PLVDAMEAAVQAVdPGAPVVPYMSP--GGTDAKYFRRLGIPGygfaplflPPELDYTGLFHGVDERVPVESLYFGVRF 425
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
71-182 |
2.88e-03 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 39.76 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1390593006 71 PTIGFIAHFDTSPdfsgenVNPQFvENYDgndivlnkeqnivlsPsyFEdlllykgqtlITTDGTTLLG---ADDKAGVA 147
Cdd:PRK08554 64 PKLLFMAHFDVVP------VNPEE-WNTE---------------P--FK----------LTVKGDKAYGrgsADDKGNVA 109
|
90 100 110
....*....|....*....|....*....|....*..
gi 1390593006 148 EIVTAMEYLVKHPeiKHGKIRVGFTPDEEIG--RGAH 182
Cdd:PRK08554 110 SVMLALKELSKEP--LNGKVIFAFTGDEEIGgaMAMH 144
|
|
| |
