|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
2-409 |
0e+00 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 814.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 2 KEDIIKRFTTYVKIDTQSNEDSETTPSTPGQLELANLLVNELNEIGMQEVTIDENGYVFATLPSNTDKEVPTIGFLAHLD 81
Cdd:PRK05469 1 MDKLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDENGYVMATLPANVDKDVPTIGFIAHMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 82 TATDFTGKHVNPQLIENFDGNDIVLNSErNVVLSEKEFPELPSYKGHTLITTDGTTLLGADNKAGIAEIMTAMDYLIKHP 161
Cdd:PRK05469 81 TAPDFSGKNVKPQIIENYDGGDIALGDG-NEVLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYLIAHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 162 EIKHGKIRVAFTPDEEIGRGPHKFDVQAFNADFAYTIDGGPLGELQYESFNAAAAKVTFKGNSVHPGTAKNKMINAGKMA 241
Cdd:PRK05469 160 EIKHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALLLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 242 AEFVSKFPEQESPEQTEGYEGFYHLISITGDVEKTRVYYIIRDFDRDSFENKKATMTKFVEEMKAKYGEDNVVLDMKDQY 321
Cdd:PRK05469 240 ADFHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKYGEGRVELEIKDQY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 322 YNMREKIEPVMEIVDVAKQAMRNLDIEPVIEPVRGGTDGSQLSYMGLPTPNIFTGGENFHGKFEYISVDNMEKATNVIVE 401
Cdd:PRK05469 320 YNMREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVIVE 399
|
....*...
gi 1896924906 402 ICRLFESK 409
Cdd:PRK05469 400 IAELTAER 407
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
5-405 |
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: 737.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 5 IIKRFTTYVKIDTQSNEDSETTPSTPGQLELANLLVNELNEIGMQEVTIDENGYVFATLPSNTDKEVPTIGFLAHLDTAT 84
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDEHGYVTATLPANVDKDVPTIGFIAHMDTAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 85 DFTGKHVNPQLIENFDGNDIVLNsERNVVLSEKEFPELPSYKGHTLITTDGTTLLGADNKAGIAEIMTAMDYLIKHPEIK 164
Cdd:cd03892 81 DNSGKNVKPQIIENYDGGDIVLN-ESGIVLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIEHPEIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 165 HGKIRVAFTPDEEIGRGPHKFDVQAFNADFAYTIDGGPLGELQYESFNAAAAKVTFKGNSVHPGTAKNKMINAGKMAAEF 244
Cdd:cd03892 160 HGDIRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLAADF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 245 VSKFPEQESPEQTEGYEGFYHLISITGDVEKTRVYYIIRDFDRDSFENKKATMTKFVEEMKAKYGEDNVVLDMKDQYYNM 324
Cdd:cd03892 240 HSMLPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKYGEGRVELEIKDQYYNM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 325 REKIEPVMEIVDVAKQAMRNLDIEPVIEPVRGGTDGSQLSYMGLPTPNIFTGGENFHGKFEYISVDNMEKATNVIVEICR 404
Cdd:cd03892 320 KEKIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIVKIAE 399
|
.
gi 1896924906 405 L 405
Cdd:cd03892 400 L 400
|
|
| peptidase-T |
TIGR01882 |
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has ... |
3-409 |
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: 630.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 3 EDIIKRFTTYVKIDTQSNEDSETTPSTPGQLELANLLVNELNEIGMQEVTIDE-NGYVFATLPSNTDKEVPTIGFLAHLD 81
Cdd:TIGR01882 3 EELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEkNGYVIATIPSNTDKDVPTIGFLAHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 82 TAtDFTGKHVNPQLIENFDGNDIVLNSERNVVLSEKEFPELPSYKGHTLITTDGTTLLGADNKAGIAEIMTAMDYLIKHP 161
Cdd:TIGR01882 83 TA-DFNGENVNPQIIENYDGESIIQLGDLEFTLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAADYLINHP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 162 EIKHGKIRVAFTPDEEIGRGPHKFDVQAFNADFAYTIDGGPLGELQYESFNAAAAKVTFKGNSVHPGTAKNKMINAGKMA 241
Cdd:TIGR01882 162 EIKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAAQIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 242 AEFVSKFPEQESPEQTEGYEGFYHLISITGDVEKTRVYYIIRDFDRDSFENKKATMTKFVEEMKAKYGEDNVVLDMKDQY 321
Cdd:TIGR01882 242 IDLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEYGQDRIKLDMNDQY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 322 YNMREKIEPVMEIVDVAKQAMRNLDIEPVIEPVRGGTDGSQLSYMGLPTPNIFTGGENFHGKFEYISVDNMEKATNVIVE 401
Cdd:TIGR01882 322 YNMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDVIVE 401
|
....*...
gi 1896924906 402 ICRLFESK 409
Cdd:TIGR01882 402 IAKLNEEQ 409
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
1-407 |
0e+00 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 531.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 1 MKEDIIKRFTTYVKIDTQSNEdsettpstpgQLELANLLVNELNEIGMqEVTIDENGYVFATLPSNTDKEVPTIGFLAHL 80
Cdd:COG2195 1 NPERLLERFLEYVKIPTPSDH----------EEALADYLVEELKELGL-EVEEDEAGNVIATLPATPGYNVPTIGLQAHM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 81 DTATDFTGKHVNPQLienfDGNdivlnsernvvlsekefpelpsykghtLITTDGTTLLGADNKAGIAEIMTAMDYLiKH 160
Cdd:COG2195 70 DTVPQFPGDGIKPQI----DGG---------------------------LITADGTTTLGADDKAGVAAILAALEYL-KE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 161 PEIKHGKIRVAFTPDEEIG-RGPHKFDVQAFNADFAYTIDGGPLGELQYESFNAAAAKVTFKGNSVHPGTAKNKMINAGK 239
Cdd:COG2195 118 PEIPHGPIEVLFTPDEEIGlRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 240 MAAEFVSKFPEQESPEQTEGYEGFYHLISIT-GDVEKTRVYYIIRDFDRDSFENKKATMTKFVEEMKAKYGEDNVVLDMK 318
Cdd:COG2195 198 LAARFLAALPLGRIPEETEGNEGFIHGGSATnAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGVGVVEVEIE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 319 DQYYNMREkiEPVMEIVDVAKQAMRNLDIEPVIEPVRGGTDGSQLSYMGLPTPNIFTGGENFHGKFEYISVDNMEKATNV 398
Cdd:COG2195 278 DQYPNWKP--EPDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWEL 355
|
....*....
gi 1896924906 399 IVEICRLFE 407
Cdd:COG2195 356 LVEILKLIA 364
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
3-405 |
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 1896924906 3 EDIIKRFTTYVKIDTQSNEDSETTPSTPGQLELANLLVNELNEIGMQEVTIDENGYVFATLPSNTDKEvPTIGFLAHLDT 82
Cdd:PRK13381 1 MQLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDIVIDEHAIVTAKLPGNTPGA-PRIGFIAHLDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 83 ATDFTGKHVNPQlIENFDGNDIVLNSERNVVLSEKEFPELPSYKGHTLITTDGTTLLGADNKAGIAEIMTAMDYLIKHpE 162
Cdd:PRK13381 80 VDVGLSPDIHPQ-ILRFDGGDLCLNAEQGIWLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLENLTEN-E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 163 IKHGKIRVAFTPDEEIG-RGPHKFDVQAFNADFAYTIDGGPLGELQYESFNAAAAKVTFKGNSVHPGTAKNKMINAGKMA 241
Cdd:PRK13381 158 VEHGDIVVAFVPDEEIGlRGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNPILMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 242 AEFVSKFPEQESPEQTEGYEGFYHLISITGDVEKTRVYYIIRDFDRDSFENKKATMTKFVEEMKAKYGEDNVVLDMKDQY 321
Cdd:PRK13381 238 NDFISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINAKYPTARVSLTLTDQY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 322 YNMREKIEPVMEIVDVAKQAMRNLDIEPVIEPVRGGTDGSQLSYMGLPTPNIFTGGENFHGKFEYISVDNMEKATNVIVE 401
Cdd:PRK13381 318 SNISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEVTIT 397
|
....
gi 1896924906 402 ICRL 405
Cdd:PRK13381 398 ICLL 401
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
5-405 |
6.42e-126 |
|
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: 369.40 E-value: 6.42e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 5 IIKRFTTYVKIDTQSNEDSETTPSTPGQLELANLLVNELNEIGMQEVTIDENGYVFATLPSNTDKEVPTIGFLAHLDTAT 84
Cdd:cd05645 1 LLERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEKGTLIATLPANVDGDIPAIGFISHVDTSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 85 DFTGKHVNPQLIENFDGNDIVLNSErNVVLSEKEFPELPSYKGHTLITTDGTTLLGADNKAGIAEIMTAMDYLIKHPeIK 164
Cdd:cd05645 81 DGSGKNVNPQIVENYRGGDIALGIG-DEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKN-IP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 165 HGKIRVAFTPDEEIGRGPHKFDVQAFNADFAYTIDGGPLGELQYESFNAAAAKVTFKGNSVHPGTAKNKMINAGKMAAEF 244
Cdd:cd05645 159 HGDIEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAARI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 245 VSKFPEQESPEQTEGYEGFYHLISITGDVEKTRVYYIIRDFDRDSFENKKATMTKFVEEM-KAKYGEDNVVLDMKDQYYN 323
Cdd:cd05645 239 HAEVPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVgKGLHPDCYIELVIEDSYYN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 324 MREKIEPVMEIVDVAKQAMRNLDIEPVIEPVRGGTDGSQLSYMGLPTPNIFTGGENFHGKFEYISVDNMEKATNVIVEIC 403
Cdd:cd05645 319 FREKVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIVRIA 398
|
..
gi 1896924906 404 RL 405
Cdd:cd05645 399 EL 400
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
2-404 |
5.01e-41 |
|
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: 149.14 E-value: 5.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 2 KEDIIKRFTTYVKIDTQSNEDSETTPstpgqlelanLLVNELNEIGMqEVTIDE--------NGYVFATLPSNTDkEVPT 73
Cdd:cd05683 2 EDRLINTFLELVQIDSETLHEKEISK----------VLKKKFENLGL-SVIEDDagkttgggAGNLICTLKADKE-EVPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 74 IGFLAHLDTATdfTGKHVNPQLIENfdgndivlnsernvvlsekefpelpsykghTLITTDGTTLLGADNKAGIAEIMTA 153
Cdd:cd05683 70 ILFTSHMDTVT--PGINVKPPQIAD------------------------------GYIYSDGTTILGADDKAGIAAILEA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 154 MDYlIKHPEIKHGKIRVAFTPDEEIGR-GPHKFDVQAFNADFAYTIDG-GPLGELQYESFNAAAAKVTFKGNSVHPGTAK 231
Cdd:cd05683 118 IRV-IKEKNIPHGQIQFVITVGEESGLvGAKALDPELIDADYGYALDSeGDVGTIIVGAPTQDKINAKIYGKTAHAGTSP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 232 NKMINAGKMAAEFVSKFPEQESPEQTEGYEGFYHLISITGDVekTRVYYII---RDFDRDSFENKKATMTKFVEEMKAKY 308
Cdd:cd05683 197 EKGISAINIAAKAISNMKLGRIDEETTANIGKFQGGTATNIV--TDEVNIEaeaRSLDEEKLDAQVKHMKETFETTAKEK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 309 GEdNVVLDMKDQYYNMreKIEPVMEIVDVAKQAMRNLDIEPVIEPVRGGTDGSQLSYMGLPTPNIFTGGENFHGKFEYIS 388
Cdd:cd05683 275 GA-HAEVEVETSYPGF--KINEDEEVVKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIP 351
|
410
....*....|....*.
gi 1896924906 389 VDNMEKATNVIVEICR 404
Cdd:cd05683 352 IEDLYDTAVLVVEIIK 367
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
1-406 |
1.79e-22 |
|
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: 98.03 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 1 MKEDIIKRFTTYVKIDTQSNEDsettpstpgqLELANLLVNELNEIGMqEVTIDEN----GYVFATLPSNTDKevPTIGF 76
Cdd:COG0624 10 HLDEALELLRELVRIPSVSGEE----------AAAAELLAELLEALGF-EVERLEVppgrPNLVARRPGDGGG--PTLLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 77 LAHLDT--ATDFTGKHVNPqlienFDGndivlnsernvvlsekefpelpsykghtliTTDGTTLLG---ADNKAGIAEIM 151
Cdd:COG0624 77 YGHLDVvpPGDLELWTSDP-----FEP------------------------------TIEDGRLYGrgaADMKGGLAAML 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 152 TAMDYLIKHPEIKHGKIRVAFTPDEEIG-RGPHKF---DVQAFNADFAYTIDGGPLGELQYESFNAAAAKVTFKGNSVHP 227
Cdd:COG0624 122 AALRALLAAGLRLPGNVTLLFTGDEEVGsPGARALveeLAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAHS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 228 GTAkNKMINAGKMAAEFVSKFpeQESPEQTEGYEGFYHL-ISIT----GDVEKT-----RVYYIIRDFDRDSFENKKATM 297
Cdd:COG0624 202 SRP-ELGVNAIEALARALAAL--RDLEFDGRADPLFGRTtLNVTgiegGTAVNVipdeaEAKVDIRLLPGEDPEEVLAAL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 298 TKFVEEMKAkygEDNVVLDMKDQYYN-MRekIEPVMEIVDVAKQAMRNLD-IEPVIEPVRGGTDGSQLS-YMGLPTPNI- 373
Cdd:COG0624 279 RALLAAAAP---GVEVEVEVLGDGRPpFE--TPPDSPLVAAARAAIREVTgKEPVLSGVGGGTDARFFAeALGIPTVVFg 353
|
410 420 430
....*....|....*....|....*....|...
gi 1896924906 374 FTGGENFHGKFEYISVDNMEKATNVIVEICRLF 406
Cdd:COG0624 354 PGDGAGAHAPDEYVELDDLEKGARVLARLLERL 386
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
141-402 |
6.89e-15 |
|
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: 75.08 E-value: 6.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 141 ADNKAGIAEIMTAMDYLIKHPeIKHGKIRVAFTPDEEIG-RGPHKF----DVQAFNADFAYTID----GGPLGELQYESF 211
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEG-LKKGTVKLLFQPDEEGGmGGARALiedgLLEREKVDAVFGLHigepTLLEGGIAIGVV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 212 NAAAA----KVTFKGNSVHpGTAKNKMINAGKMAAEFVSKFPEQESPEQTEGYEG---FYHLISITGDV----EKTRVYY 280
Cdd:pfam01546 112 TGHRGslrfRVTVKGKGGH-ASTPHLGVNAIVAAARLILALQDIVSRNVDPLDPAvvtVGNITGIPGGVnvipGEAELKG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 281 IIRDFDRDSFENKKATMTKFVEEMKAKYGEDnVVLDMKDQYYNMREKIEPVMEIVDVAKQAMRNLDIEPVIEPVRGGTDG 360
Cdd:pfam01546 191 DIRLLPGEDLEELEERIREILEAIAAAYGVK-VEVEYVEGGAPPLVNDSPLVAALREAAKELFGLKVELIVSGSMGGTDA 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1896924906 361 sqlSYMGLPTPNIF----TGGENFHGKFEYISVDNMEKATNVIVEI 402
Cdd:pfam01546 270 ---AFFLLGVPPTVvffgPGSGLAHSPNEYVDLDDLEKGAKVLARL 312
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
13-402 |
2.35e-14 |
|
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: 73.87 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 13 VKIDTqsnedsettpSTPGQLELANLLVNELNEIGMQ-EVTIDEN-GYVFATLPSNTDkevPTIGFLAHLDTatdftgkh 90
Cdd:cd08659 7 VQIPS----------VNPPEAEVAEYLAELLAKRGYGiESTIVEGrGNLVATVGGGDG---PVLLLNGHIDT-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 91 VNPQLIENFDgndivlnsernvvlsekefpeLPSYKGHTlitTDGTtLLG---ADNKAGIAEIMTAMDYLIKHPEIKHGK 167
Cdd:cd08659 66 VPPGDGDKWS---------------------FPPFSGRI---RDGR-LYGrgaCDMKGGLAAMVAALIELKEAGALLGGR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 168 IRVAFTPDEEIG-RGPHKFDVQAFNADFAYTIDGGPLGelqYESFNAA----AAKVTFKGNSVHpGTAKNKMINAGKMAA 242
Cdd:cd08659 121 VALLATVDEEVGsDGARALLEAGYADRLDALIVGEPTG---LDVVYAHkgslWLRVTVHGKAAH-SSMPELGVNAIYALA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 243 EFVSKFPEQ-ESPEQTEGYEGFYHLIS-ITGDVE------KTRVYYIIR---DFDRDSFenkKATMTKFVEEMKAKYged 311
Cdd:cd08659 197 DFLAELRTLfEELPAHPLLGPPTLNVGvINGGTQvnsipdEATLRVDIRlvpGETNEGV---IARLEAILEEHEAKL--- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 312 NVVLDMKDQYYnmrEKIEPVMEIVDVAKQAMRNLDIEPVIEPVRGGTDGSQLSYM-GLPTPNIFTGGENF-HGKFEYISV 389
Cdd:cd08659 271 TVEVSLDGDPP---FFTDPDHPLVQALQAAARALGGDPVVRPFTGTTDASYFAKDlGFPVVVYGPGDLALaHQPDEYVSL 347
|
410
....*....|...
gi 1896924906 390 DNMEKATNVIVEI 402
Cdd:cd08659 348 EDLLRAAEIYKEI 360
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
1-401 |
2.69e-13 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 70.79 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 1 MKEDIIKRFTTYVKIDTQSNEDSETTpstpgqlELANLLVNELNEIGMqEVTIDE---------NGYVFATLPSNTDKEv 71
Cdd:PRK08651 4 MMFDIVEFLKDLIKIPTVNPPGENYE-------EIAEFLRDTLEELGF-STEIIEvpneyvkkhDGPRPNLIARRGSGN- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 72 PTIGFLAHLDTATDFTG-KHVNPqlienFDGndivlnsernVVLSEKefpelpsykghtlITTDGTTllgaDNKAGIAEI 150
Cdd:PRK08651 75 PHLHFNGHYDVVPPGEGwSVNVP-----FEP----------KVKDGK-------------VYGRGAS----DMKGGIAAL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 151 MTAMDYLIkhpEIKHGKIRVAFTPDEEIGR--GPHKFDVQAFNADFAYTIDGGPLGELQYESFNAAAAKVTFKGNSVHPG 228
Cdd:PRK08651 123 LAAFERLD---PAGDGNIELAIVPDEETGGtgTGYLVEEGKVTPDYVIVGEPSGLDNICIGHRGLVWGVVKVYGKQAHAS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 229 TAK---NKMINAGKMAAEFVSKFPEQESPEQTEGYEGFYHLISITGDV----EKT-------RVYY---IIRDFDRDSFE 291
Cdd:PRK08651 200 TPWlgiNAFEAAAKIAERLKSSLSTIKSKYEYDDERGAKPTVTLGGPTveggTKTnivpgycAFSIdrrLIPEETAEEVR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 292 NKkatMTKFVEEMKAKYGEDnvvldmkdqyYNMREKI-------EPVMEIVDVAKQAMR-NLDIEPVIEPVRGGTDGSQL 363
Cdd:PRK08651 280 DE---LEALLDEVAPELGIE----------VEFEITPfseafvtDPDSELVKALREAIReVLGVEPKKTISLGGTDARFF 346
|
410 420 430
....*....|....*....|....*....|....*....
gi 1896924906 364 SYMGLPTPNIFTGG-ENFHGKFEYISVDNMEKATNVIVE 401
Cdd:PRK08651 347 GAKGIPTVVYGPGElELAHAPDEYVEVKDVEKAAKVYEE 385
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
142-409 |
7.91e-12 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 65.94 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 142 DNKAGIAEIMTAMDYLIKhpEIKHGKIRVAFTPDEEI-GRGPHKFdVQAFNADFAYTIDGGPLgELQYESFNAAAAKVTF 220
Cdd:PRK08652 87 DAKGGVAAILLALEELGK--EFEDLNVGIAFVSDEEEgGRGSALF-AERYRPKMAIVLEPTDL-KVAIAHYGNLEAYVEV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 221 KGNSVHpGTAKNKMINAGKMAAEFVSKFPEQEsPEQTEGYEGFYHLISITGDVEktrvYYIIRDFDRDSF------ENKK 294
Cdd:PRK08652 163 KGKPSH-GACPESGVNAIEKAFEMLEKLKELL-KALGKYFDPHIGIQEIIGGSP----EYSIPALCRLRLdarippEVEV 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 295 ATMTKFVEEMKAKYGEDNVVLDMKDQYYnmrekIEPVMEIVDVAKQAMRNLDIEPVIEPVRGGTDGSQLSYMGLPTPnIF 374
Cdd:PRK08652 237 EDVLDEIDPILDEYTVKYEYTEIWDGFE-----LDEDEEIVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTKTV-VW 310
|
250 260 270
....*....|....*....|....*....|....*..
gi 1896924906 375 TGGE--NFHGKFEYISVDNMEKATNVIVEICRLFESK 409
Cdd:PRK08652 311 GPGEldLCHTKFERIDVREVEKAKEFLKALNEILLES 347
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
208-312 |
8.99e-12 |
|
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: 61.21 E-value: 8.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 208 YESFNAAAAKVTFKGNSVHPGtAKNKMINAGKMAAEFVSKFPEQ----------ESPEQTEGYEGFyhliSITGDVEKTR 277
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSG-APGKGVNAIKLLARLLAELPAEygdigfdfprTTLNITGIEGGT----ATNVIPAEAE 75
|
90 100 110
....*....|....*....|....*....|....*
gi 1896924906 278 VYYIIRdfdRDSFENKKATMTKFVEEMKAKYGEDN 312
Cdd:pfam07687 76 AKFDIR---LLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
5-402 |
7.06e-11 |
|
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: 63.38 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 5 IIKRFTTYVKIDTQSnEDSEttpstpGQLELANLLVNELNEIGMQEVTIDEN---GYVFATLPsntDKEVPTIGFLAHLD 81
Cdd:cd03885 1 MLDLLERLVNIESGT-YDKE------GVDRVAELLAEELEALGFTVERRPLGefgDHLIATFK---GTGGKRVLLIGHMD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 82 TatdftgkhvnpqlienfdgndivlnsernvVLSEKEFPELPsykghtlITTDGTTLLG---ADNKAGIAEIMTAMDYLI 158
Cdd:cd03885 71 T------------------------------VFPEGTLAFRP-------FTVDGDRAYGpgvADMKGGLVVILHALKALK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 159 KHPEIKHGKIRVAFTPDEEIGR---GPHkFDVQAFNADFAYTID-GGPLGELQYESFNAAAAKVTFKGNSVHPGTAKNKM 234
Cdd:cd03885 114 AAGGRDYLPITVLLNSDEEIGSpgsREL-IEEEAKGADYVLVFEpARADGNLVTARKGIGRFRLTVKGRAAHAGNAPEKG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 235 INAGKMAAEFVSKFPEQESPEQ--TegyegfyhlISIT----GDV-----EKTRVYYIIRDFDRDSFENKKATMTKFVEE 303
Cdd:cd03885 193 RSAIYELAHQVLALHALTDPEKgtT---------VNVGvisgGTRvnvvpDHAEAQVDVRFATAEEADRVEEALRAIVAT 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 304 mkaKYGED-NVVLDMKDQYYNMrEKIEPVMEIVDVAKQAMRNLDIEPVIEPVRGGTDGSQLSYMGLPTPNIFtG--GENF 380
Cdd:cd03885 264 ---TLVPGtSVELTGGLNRPPM-EETPASRRLLARAQEIAAELGLTLDWEATGGGSDANFTAALGVPTLDGL-GpvGGGA 338
|
410 420
....*....|....*....|..
gi 1896924906 381 HGKFEYISVDNMEKATNVIVEI 402
Cdd:cd03885 339 HTEDEYLELDSLVPRIKLLARL 360
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
59-209 |
2.53e-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: 56.66 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 59 VFATLPSNTDKevPTIGFLAHLDTATDFTGkhvnpqlienfdgndivlnsernvvlsekeFPELPSYKGHTLITTDGTTL 138
Cdd:cd03873 2 LIARLGGGEGG--KSVALGAHLDVVPAGEG------------------------------DNRDPPFAEDTEEEGRLYGR 49
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896924906 139 LGADNKAGIAEIMTAMDYLIKHPEIKHGKIRVAFTPDEEIGRGPHKF------DVQAFNADFAYTIDGGPLGELQYE 209
Cdd:cd03873 50 GALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGSGGGKGllskflLAEDLKVDAAFVIDATAGPILQKG 126
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
59-229 |
8.19e-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: 55.13 E-value: 8.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 59 VFATLPSNTDKevPTIGFLAHLDtatdftgkhvnpqlienfdgndivlnsernVVLSEKEFPELPSYKGHTLITTDGTTL 138
Cdd:cd18669 2 VIARYGGGGGG--KRVLLGAHID------------------------------VVPAGEGDPRDPPFFVDTVEEGRLYGR 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 139 LGADNKAGIAEIMTAMDYLIKHPEIKHGKIRVAFTPDEEIGRGPHKF------DVQAFNADFAYTIDGGP-------LGE 205
Cdd:cd18669 50 GALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEEVGSGAGKGllskdaLEEDLKVDYLFVGDATPapqkgvgIRT 129
|
170 180
....*....|....*....|....*.
gi 1896924906 206 LQYESFNAAAAKV--TFKGNSVHPGT 229
Cdd:cd18669 130 PLVDALSEAARKVfgKPQHAEGTGGG 155
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
131-318 |
4.57e-06 |
|
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: 48.67 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 131 ITTDGTTLlGADNKAGIAEIMTAMDylikHPEIKHGKIRVAFTPDEEIG-RGPHKFDVQAFNADFAYTID---------- 199
Cdd:cd03890 97 LKATGTTL-GADNGIGVAYALAILE----DKDIEHPPLEVLFTVDEETGmTGALGLDPSLLKGKILLNLDseeegeltvg 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 200 --GG--PLGELQYESFNAAAAKVTFK--------GNS---VHPGTAknkmiNAGKMAAEFVSkfpeqespEQTEGYEgfY 264
Cdd:cd03890 172 caGGidVTITLPIEREEAEGGYTGLKitvkglkgGHSgvdIHKGRA-----NANKLMARLLY--------ELAKELD--F 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896924906 265 HLISITGDvekTRVYYIIRD------FDRDSFENKKATMTKFVEEMKAKYG--EDNVVLDMK 318
Cdd:cd03890 237 RLVSINGG---TKRNAIPREavaviaVPAEDVEALKKLIKKLEKALKAEYAgtDPNLKIEVE 295
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
147-364 |
3.13e-05 |
|
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: 45.67 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 147 IAEIMTAMDYLIKHPEIKHGKIRVAFTPDEEIGRGP---------HKFDVQAFnadFAYTIDGG-PLGELQYES--FNAA 214
Cdd:cd03886 94 TAMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPGGAkamieegvlENPGVDAA---FGLHVWPGlPVGTVGVRSgaLMAS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 215 AA--KVTFKGNSVHpGTAKNKMINAGKMAAEFVSK---FPEQESPEQTEgyegfyHLISI--------------TGDVEK 275
Cdd:cd03886 171 ADefEITVKGKGGH-GASPHLGVDPIVAAAQIVLAlqtVVSRELDPLEP------AVVTVgkfhagtafnvipdTAVLEG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 276 TrvyyiIRDFDRDSFENKKATMTKFVEEMKAKYGEDnVVLDMKDQYynmrekiePVM----EIVDVAKQAMRNLDIEPVI 351
Cdd:cd03886 244 T-----IRTFDPEVREALEARIKRLAEGIAAAYGAT-VELEYGYGY--------PAVindpELTELVREAAKELLGEEAV 309
|
250
....*....|....*.
gi 1896924906 352 ---EPVRGGTDGSQLS 364
Cdd:cd03886 310 vepEPVMGSEDFAYYL 325
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
129-245 |
2.30e-04 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 43.03 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 129 TLITTDGTTLLG---ADNKAGIAEIMTAMDYLIKHPEIKHGKIRVAFTPDEEIGrgphKFDVQAFNADFAYTIDGGPLGE 205
Cdd:PRK07338 113 TLSWLDDGTLNGpgvADMKGGIVVMLAALLAFERSPLADKLGYDVLINPDEEIG----SPASAPLLAELARGKHAALTYE 188
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1896924906 206 LQYESFNAAAAK-------VTFKGNSVHPGTAKNKMINAGKMAAEFV 245
Cdd:PRK07338 189 PALPDGTLAGARkgsgnftIVVTGRAAHAGRAFDEGRNAIVAAAELA 235
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
127-380 |
4.97e-04 |
|
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: 41.95 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 127 GHTLITTdgtTLLGadnkagiaeimTAMdYLIKHPEIKHGKIRVAFTPDEEIGRGPHKF-------DVQAFnadFAYTID 199
Cdd:TIGR01891 90 GHDLHTA---ILLG-----------TAK-LLKKLADLLEGTVRLIFQPAEEGGGGATKMiedgvldDVDAI---LGLHPD 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 200 GG-PLGELQYESFNAAAA----KVTFKGNSVH---PGTAKNKMINAGKMAAEFVSKFPEQESPEQtegyEGFYHLISITG 271
Cdd:TIGR01891 152 PSiPAGTVGLRPGTIMAAadkfEVTIHGKGAHaarPHLGRDALDAAAQLVVALQQIVSRNVDPSR----PAVVSVGIIEA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 272 ----DV--EKTRVYYIIRDFDRDsfenkkaTMTKFVEEMKAkygednvVLDMKDQYYNMR-----EKIEPVM----EIVD 336
Cdd:TIGR01891 228 ggapNVipDKASMSGTVRSLDPE-------VRDQIIDRIER-------IVEGAAAMYGAKvelnyDRGLPAVtndpALTQ 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1896924906 337 VAKQAMR------NLDIEPviEPVRGGTDGSQLSYMgLPTPNIFTGGENF 380
Cdd:TIGR01891 294 ILKEVARhvvgpeNVAEDP--EVTMGSEDFAYYSQK-VPGAFFFLGIGNE 340
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
217-402 |
2.59e-03 |
|
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: 39.75 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 217 KVTFKGNSVH---PGTAKNKMINAGKMA-------AEFVSKF-----PEQESPEQTEGYEGFYHLISITGDVEktrVYYI 281
Cdd:cd05650 192 KVNVKGKQCHastPENGINAFVAASNFAleldellHEKFDEKddlfnPPYSTFEPTKKEANVPNVNTIPGYDV---FYFD 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 282 IRDFDRDSFENKKATMTKFVEEMKAKYGEdNVVLDMkDQYYNMREKIEPVMEIVDVAKQAMRNL-DIEPVIEPVRGGTDG 360
Cdd:cd05650 269 CRVLPTYKLDEVLKFVNKIISDFENSYGA-GITYEI-VQKEQAPPATPEDSEIVVRLSKAIKKVrGREAKLIGIGGGTVA 346
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1896924906 361 SQLSYMGLPTPNIFTGGENFHGKFEYISVDNMEKATNVIVEI 402
Cdd:cd05650 347 AFLRKKGYPAVVWSTLDETAHQPNEYIRISHIVKDAKVFAEM 388
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
141-237 |
5.04e-03 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 38.84 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 141 ADNKAGIAEIMTAMDyLIKHPEIK-HGKIRVAFTPDEEIGRGPHKFDVQAFNADFAYTID---GGPLGELQYESFNAAAA 216
Cdd:PRK06133 135 ADDKGGVAVILHALK-ILQQLGFKdYGTLTVLFNPDEETGSPGSRELIAELAAQHDVVFScepGRAKDALTLATSGIATA 213
|
90 100
....*....|....*....|.
gi 1896924906 217 KVTFKGNSVHPGTAKNKMINA 237
Cdd:PRK06133 214 LLEVKGKASHAGAAPELGRNA 234
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
29-82 |
7.41e-03 |
|
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.
Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 38.27 E-value: 7.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1896924906 29 TPGQLELANLLVNELNEIGMqEVTIDENGYVFATLPSnTDKEVPTIGFLAHLDT 82
Cdd:cd03884 25 TDEDRAARDLFVEWMEEAGL-SVRVDAVGNLFGRLEG-TDPDAPPVLTGSHLDT 76
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
147-245 |
7.83e-03 |
|
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: 38.09 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896924906 147 IAEIMTAMDYLIKHPEIKHGKIRVAFTPDEEIGRGPHKFDVQAFNAD----FAYTIDGG-PLGELQYESFNAAAA----K 217
Cdd:cd08019 93 TAMLLGAAKILNEIKDTIKGTVKLIFQPAEEVGEGAKQMIEEGVLEDvdavFGIHLWSDvPAGKISVEAGPRMASadifK 172
|
90 100
....*....|....*....|....*...
gi 1896924906 218 VTFKGNSVHPGTAKNKmINAGKMAAEFV 245
Cdd:cd08019 173 IEVKGKGGHGSMPHQG-IDAVLAAASIV 199
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
141-179 |
8.31e-03 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 38.22 E-value: 8.31e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1896924906 141 ADNKAGIAEIMTAMDYLIKHPeiKHGKIRVAFTPDEEIG 179
Cdd:PRK08554 102 ADDKGNVASVMLALKELSKEP--LNGKVIFAFTGDEEIG 138
|
|
| |
