|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
5-412 |
0e+00 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 595.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 5 YQNFIEQlFIKYAKVNTRSDEDSQAVPTTQGQVELAKIVLQDLKKLGVADVVYDpKDSYVVASLPANTTADITPIGFIAH 84
Cdd:PRK05469 1 MDKLLER-FLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLD-ENGYVMATLPANVDKDVPTIGFIAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 85 LDTA-DFPAENVQPQVHENYDGQDVVLNEAKkIVLRVSEFPNLKNYRGQRLITNDGTTLLGVDDKAGVASILTAVKYLLE 163
Cdd:PRK05469 79 MDTApDFSGKNVKPQIIENYDGGDIALGDGN-EVLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYLIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 164 HPSLKHGPISFAFGPDEEIGRGAKRFDVSKFKVKFAYTLDNGLPGQLEAETFNAAQAKIKIKGTSVHPGNAFGLMVNAIT 243
Cdd:PRK05469 158 HPEIKHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 244 LANHIISLLPAGEVPEKSCGHQGFFLVTDFKATIAQADLKIIIRDFDQQKFNAKKKLLQQIVADLNRQFERPRITLELKD 323
Cdd:PRK05469 238 LAADFHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKYGEGRVELEIKD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 324 QYFNIGDVIQQHPYITELVLNVYHKLGLKVQVHPFRGGTDGNFLTAKGIPTPNLFNGGENFHGPYEFVTTEAMLTTSKTV 403
Cdd:PRK05469 318 QYYNMREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVI 397
|
....*....
gi 1864111725 404 IEIIKEHAQ 412
Cdd:PRK05469 398 VEIAELTAE 406
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
13-408 |
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: 591.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 13 FIKYAKVNTRSDEDSQAVPTTQGQVELAKIVLQDLKKLGVADVVYDPKdSYVVASLPANTTADITPIGFIAHLDTADF-P 91
Cdd:cd03892 5 FLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDEH-GYVTATLPANVDKDVPTIGFIAHMDTAPDnS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 92 AENVQPQVHENYDGQDVVLNEaKKIVLRVSEFPNLKNYRGQRLITNDGTTLLGVDDKAGVASILTAVKYLLEHPSLKHGP 171
Cdd:cd03892 84 GKNVKPQIIENYDGGDIVLNE-SGIVLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIEHPEIKHGD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 172 ISFAFGPDEEIGRGAKRFDVSKFKVKFAYTLDNGLPGQLEAETFNAAQAKIKIKGTSVHPGNAFGLMVNAITLANHIISL 251
Cdd:cd03892 163 IRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLAADFHSM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 252 LPAGEVPEKSCGHQGFFLVTDFKATIAQADLKIIIRDFDQQKFNAKKKLLQQIVADLNRQFERPRITLELKDQYFNIGDV 331
Cdd:cd03892 243 LPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKYGEGRVELEIKDQYYNMKEK 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864111725 332 IQQHPYITELVLNVYHKLGLKVQVHPFRGGTDGNFLTAKGIPTPNLFNGGENFHGPYEFVTTEAMLTTSKTVIEIIK 408
Cdd:cd03892 323 IEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIVKIAE 399
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
8-412 |
0e+00 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 547.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 8 FIEQLFIKYAKVNTRSDEDSQAVPTTQGQVELAKIVLQDLKKLGVADVVYDpKDSYVVASLPANTtADITPIGFIAHLDT 87
Cdd:PRK13381 2 QLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDIVID-EHAIVTAKLPGNT-PGAPRIGFIAHLDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 88 ADFPAE-NVQPQVHEnYDGQDVVLNEAKKIVLRVSEFPNLKNYRGQRLITNDGTTLLGVDDKAGVASILTAVKYLLEHpS 166
Cdd:PRK13381 80 VDVGLSpDIHPQILR-FDGGDLCLNAEQGIWLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLENLTEN-E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 167 LKHGPISFAFGPDEEIG-RGAKRFDVSKFKVKFAYTLDNGLPGQLEAETFNAAQAKIKIKGTSVHPGNAFGLMVNAITLA 245
Cdd:PRK13381 158 VEHGDIVVAFVPDEEIGlRGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNPILMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 246 NHIISLLPAGEVPEKSCGHQGFFLVTDFKATIAQADLKIIIRDFDQQKFNAKKKLLQQIVADLNRQFERPRITLELKDQY 325
Cdd:PRK13381 238 NDFISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINAKYPTARVSLTLTDQY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 326 FNIGDVIQQHPYITELVLNVYHKLGLKVQVHPFRGGTDGNFLTAKGIPTPNLFNGGENFHGPYEFVTTEAMLTTSKTVIE 405
Cdd:PRK13381 318 SNISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEVTIT 397
|
....*..
gi 1864111725 406 IIKEHAQ 412
Cdd:PRK13381 398 ICLLAAK 404
|
|
| peptidase-T |
TIGR01882 |
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has ... |
5-412 |
1.24e-163 |
|
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: 465.91 E-value: 1.24e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 5 YQNFIEQlFIKYAKVNTRSDEDSQAVPTTQGQVELAKIVLQDLKKLGVADVVYDPKDSYVVASLPANTTADITPIGFIAH 84
Cdd:TIGR01882 2 YEELLPR-FLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEKNGYVIATIPSNTDKDVPTIGFLAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 85 LDTADFPAENVQPQVHENYDGQDVVLNEAKKIVLRVSEFPNLKNYRGQRLITNDGTTLLGVDDKAGVASILTAVKYLLEH 164
Cdd:TIGR01882 81 VDTADFNGENVNPQIIENYDGESIIQLGDLEFTLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAADYLINH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 165 PSLKHGPISFAFGPDEEIGRGAKRFDVSKFKVKFAYTLDNGLPGQLEAETFNAAQAKIKIKGTSVHPGNAFGLMVNAITL 244
Cdd:TIGR01882 161 PEIKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAAQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 245 ANHIISLLPAGEVPEKSCGHQGFFLVTDFKATIAQADLKIIIRDFDQQKFNAKKKLLQQIVADLNRQFERPRITLELKDQ 324
Cdd:TIGR01882 241 AIDLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEYGQDRIKLDMNDQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 325 YFNIGDVIQQHPYITELVLNVYHKLGLKVQVHPFRGGTDGNFLTAKGIPTPNLFNGGENFHGPYEFVTTEAMLTTSKTVI 404
Cdd:TIGR01882 321 YYNMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDVIV 400
|
....*...
gi 1864111725 405 EIIKEHAQ 412
Cdd:TIGR01882 401 EIAKLNEE 408
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
9-411 |
3.77e-140 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 404.43 E-value: 3.77e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 9 IEQLFIKYAKVNTRSDEdsqavpttqgQVELAKIVLQDLKKLGVaDVVYDpKDSYVVASLPANTTADITPIGFIAHLDTA 88
Cdd:COG2195 5 LLERFLEYVKIPTPSDH----------EEALADYLVEELKELGL-EVEED-EAGNVIATLPATPGYNVPTIGLQAHMDTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 89 -DFPAENVQPQVhenyDGQdvvlneakkivlrvsefpnlknyrgqrLITNDGTTLLGVDDKAGVASILTAVKYLLeHPSL 167
Cdd:COG2195 73 pQFPGDGIKPQI----DGG---------------------------LITADGTTTLGADDKAGVAAILAALEYLK-EPEI 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 168 KHGPISFAFGPDEEIG-RGAKRFDVSKFKVKFAYTLDNGLPGQLEAETFNAAQAKIKIKGTSVHPGNAFGLMVNAITLAN 246
Cdd:COG2195 121 PHGPIEVLFTPDEEIGlRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIKLAA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 247 HIISLLPAGEVPEKSCGHQGFFLVTDF-KATIAQADLKIIIRDFDQQKFNAKKKLLQQIVADLNRQFERPRITLELKDQY 325
Cdd:COG2195 201 RFLAALPLGRIPEETEGNEGFIHGGSAtNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGVGVVEVEIEDQY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 326 FNIGDviQQHPYITELVLNVYHKLGLKVQVHPFRGGTDGNFLTAKGIPTPNLFNGGENFHGPYEFVTTEAMLTTSKTVIE 405
Cdd:COG2195 281 PNWKP--EPDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWELLVE 358
|
....*.
gi 1864111725 406 IIKEHA 411
Cdd:COG2195 359 ILKLIA 364
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
13-409 |
4.55e-103 |
|
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: 311.23 E-value: 4.55e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 13 FIKYAKVNTRSDEDSQAVPTTQGQVELAKIVLQDLKKLGVADVVYDPKDSyVVASLPANTTADITPIGFIAHLDTA-DFP 91
Cdd:cd05645 5 FLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEKGT-LIATLPANVDGDIPAIGFISHVDTSpDGS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 92 AENVQPQVHENYDGQDVVLNEAKKiVLRVSEFPNLKNYRGQRLITNDGTTLLGVDDKAGVASILTAVKYLLEHPsLKHGP 171
Cdd:cd05645 84 GKNVNPQIVENYRGGDIALGIGDE-VLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKN-IPHGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 172 ISFAFGPDEEIGRGAKRFDVSKFKVKFAYTLDNGLPGQLEAETFNAAQAKIKIKGTSVHPGNAFGLMVNAITLANHIISL 251
Cdd:cd05645 162 IEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAARIHAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 252 LPAGEVPEKSCGHQGFFLVTDFKATIAQADLKIIIRDFDQQKFNAKKKLLQQIVADLNRQFERP-RITLELKDQYFNIGD 330
Cdd:cd05645 242 VPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVGKGLHPDcYIELVIEDSYYNFRE 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864111725 331 VIQQHPYITELVLNVYHKLGLKVQVHPFRGGTDGNFLTAKGIPTPNLFNGGENFHGPYEFVTTEAMLTTSKTVIEIIKE 409
Cdd:cd05645 322 KVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIVRIAEL 400
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
38-409 |
1.15e-36 |
|
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: 137.58 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 38 ELAKIVLQDLKKLGVADVVYDPKDSY------VVASLPANTtADITPIGFIAHLDTADfPAENVQPQVHEnyDGqdvvln 111
Cdd:cd05683 24 EISKVLKKKFENLGLSVIEDDAGKTTgggagnLICTLKADK-EEVPKILFTSHMDTVT-PGINVKPPQIA--DG------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 112 eakkivlrvsefpnlknyrgqrLITNDGTTLLGVDDKAGVASILTAVKYLLEHpSLKHGPISFAFGPDEEIGR-GAKRFD 190
Cdd:cd05683 94 ----------------------YIYSDGTTILGADDKAGIAAILEAIRVIKEK-NIPHGQIQFVITVGEESGLvGAKALD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 191 VSKFKVKFAYTLD-NGLPGQLEAETFNAAQAKIKIKGTSVHPGNAFGLMVNAITLANHIISLLPAGEVPEKSCGHQGFF- 268
Cdd:cd05683 151 PELIDADYGYALDsEGDVGTIIVGAPTQDKINAKIYGKTAHAGTSPEKGISAINIAAKAISNMKLGRIDEETTANIGKFq 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 269 ------LVTDFKATIAQAdlkiiiRDFDQQKFNAK----KKLLQQIVADLNRQFErprITLELKDQYFNIGDviqqHPYI 338
Cdd:cd05683 231 ggtatnIVTDEVNIEAEA------RSLDEEKLDAQvkhmKETFETTAKEKGAHAE---VEVETSYPGFKINE----DEEV 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864111725 339 TELVLNVYHKLGLKVQVHPFRGGTDGNFLTAKGIPTPNLFNGGENFHGPYEFVTTEAMLTTSKTVIEIIKE 409
Cdd:cd05683 298 VKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAVLVVEIIKE 368
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
38-407 |
7.90e-33 |
|
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: 126.97 E-value: 7.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 38 ELAKIVLQDLKKLGVaDVVYDP------KDSYVVASLPAntTADITPIGFIAHLDTADfPAENVQPQVHENYdgqdvvln 111
Cdd:TIGR01883 21 AILTYLKKQITKLGI-PVSLDEvpaevsNDNNLIARLPG--TVKFDTIFFCGHMDTVP-PGAGPEPVVEDGI-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 112 eakkivlrvsefpnlknyrgqrlITNDGTTLLGVDDKAGVASILTAVKYLLEHpSLKHGPISFAFGPDEEIG-RGAKRFD 190
Cdd:TIGR01883 89 -----------------------FTSLGGTILGADDKAGVAAMLEAMDVLSTE-ETPHGTIEFIFTVKEELGlIGMRLFD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 191 VSKFKVKFAYTLDNGLPG---QLEAETfnaaQAKIK--IKGTSVHPGNAFGLMVNAITLANHIISLLPAGEVPEKSCGHQ 265
Cdd:TIGR01883 145 ESKITAAYGYCLDAPGEVgniQLAAPT----QVKVDatIAGKDAHAGLVPEDGISAISVARMAIHAMRLGRIDEETTANI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 266 GFFlVTDFKATIAQADLKIII--RDFDQQKFNAKkklLQQIVADLNRQFERPRITLELKDQYFNIGDVIQ-QHPYItELV 342
Cdd:TIGR01883 221 GSF-SGGVNTNIVQDEQLIVAeaRSLSFRKAEAQ---VQTMRERFEQAAEKYGATLEEETRLIYEGFKIHpQHPLM-NIF 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864111725 343 LNVYHKLGLKVQVHPFRGGTDGNFLTAKGIPTPNLFNGGENFHGPYEFVTTEAMLTTSKTVIEII 407
Cdd:TIGR01883 296 KKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETISIEQLVKLAELVIALA 360
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
29-409 |
9.76e-24 |
|
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 101.89 E-value: 9.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 29 AVPTTQGQV-ELAKIVLQDLKKLGVADVVYDPKDSY--VVASLPANTTADitPIGFIAHLDTAdfPAENVQPQVHENYDG 105
Cdd:COG0624 23 RIPSVSGEEaAAAELLAELLEALGFEVERLEVPPGRpnLVARRPGDGGGP--TLLLYGHLDVV--PPGDLELWTSDPFEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 106 qdvvlneakkivlRVsefpnlknyRGQRLItndGttlLGV-DDKAGVASILTAVKYLLEHPSLKHGPISFAFGPDEEIG- 183
Cdd:COG0624 99 -------------TI---------EDGRLY---G---RGAaDMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGs 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 184 RGAKRF---DVSKFKVKFAYTLDNGLPGQLEAETFNAAQAKIKIKGTSVHPGNaFGLMVNAITLANHIISLLPAGEVPEK 260
Cdd:COG0624 151 PGARALveeLAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAHSSR-PELGVNAIEALARALAALRDLEFDGR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 261 SCGHQGF--FLVTDFKATIA------QADLKIIIRDFDQQKFNAKKKLLQQIVADLNRQferPRITLELKDQYFNIGDVI 332
Cdd:COG0624 230 ADPLFGRttLNVTGIEGGTAvnvipdEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPG---VEVEVEVLGDGRPPFETP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 333 QQHPyITELVLNVYHKL-GLKVQVHPFRGGTDGNFLT-AKGIPTPNL-FNGGENFHGPYEFVTTEAMLTTSKTVIEIIKE 409
Cdd:COG0624 307 PDSP-LVAAARAAIREVtGKEPVLSGVGGGTDARFFAeALGIPTVVFgPGDGAGAHAPDEYVELDDLEKGARVLARLLER 385
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
145-409 |
1.51e-21 |
|
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 94.34 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 145 VDDKAGVASILTAVKYLLEHPsLKHGPISFAFGPDEEIG-RGAKRF----DVSKFKVKFAYTLDNGLPGQLEAE------ 213
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEG-LKKGTVKLLFQPDEEGGmGGARALiedgLLEREKVDAVFGLHIGEPTLLEGGiaigvv 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 214 TFNAAQA--KIKIKGTSVH---PGNAfglmVNAITLANHIISLLPAGEVPEKSCGHQG---FFLVTDFKATI----AQAD 281
Cdd:pfam01546 112 TGHRGSLrfRVTVKGKGGHastPHLG----VNAIVAAARLILALQDIVSRNVDPLDPAvvtVGNITGIPGGVnvipGEAE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 282 LKIIIRDFDQQKFNAKKKLLQQIVADLNRQFerpRITLELKDQYFNIGDVIQQHPyITELVLNVYHKL-GLKVQVH--PF 358
Cdd:pfam01546 188 LKGDIRLLPGEDLEELEERIREILEAIAAAY---GVKVEVEYVEGGAPPLVNDSP-LVAALREAAKELfGLKVELIvsGS 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1864111725 359 RGGTDGNFLTAKGIPTPNLFN-GGENFHGPYEFVTTEAMLTTSKTVIEIIKE 409
Cdd:pfam01546 264 MGGTDAAFFLLGVPPTVVFFGpGSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
131-391 |
4.93e-17 |
|
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: 81.87 E-value: 4.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 131 GQRLITNDGTTL--LGV-DDKAGVASILTAVKYLLEHPSLKHGPISFAFGPDEEIGRGAKRFDVSKF--KVKFAYTLDNG 205
Cdd:cd03885 79 AFRPFTVDGDRAygPGVaDMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRELIEEEakGADYVLVFEPA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 206 LP-GQLEAETFNAAQAKIKIKGTSVHPGNAFGLMVNAIT-LANHII----------------SLLPAGE----VPEkscg 263
Cdd:cd03885 159 RAdGNLVTARKGIGRFRLTVKGRAAHAGNAPEKGRSAIYeLAHQVLalhaltdpekgttvnvGVISGGTrvnvVPD---- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 264 hqgfflvtdfKATiAQADLKIIIRDfDQQKFNAKkklLQQIVAdlNRQFERPRITLELKDQY--FNIGDVIQQhpyITEL 341
Cdd:cd03885 235 ----------HAE-AQVDVRFATAE-EADRVEEA---LRAIVA--TTLVPGTSVELTGGLNRppMEETPASRR---LLAR 294
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1864111725 342 VLNVYHKLGLKVQVHPFRGGTDGNFLTAKGIPTpnlFNG----GENFHGPYEFV 391
Cdd:cd03885 295 AQEIAAELGLTLDWEATGGGSDANFTAALGVPT---LDGlgpvGGGAHTEDEYL 345
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
145-409 |
4.97e-15 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 76.18 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 145 VDDKAGVASILTAVKYLLEhpsLKHGPISFAFGPDEEI-GRGAKRFdVSKFKVKFAY-------TLDN---GLPGQLeae 213
Cdd:PRK08651 113 SDMKGGIAALLAAFERLDP---AGDGNIELAIVPDEETgGTGTGYL-VEEGKVTPDYvivgepsGLDNiciGHRGLV--- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 214 tfnaaQAKIKIKGTSVHPGNAFgLMVNAITLANHIISLL---------------PAGEVPEKSCGhqGFFLV-------- 270
Cdd:PRK08651 186 -----WGVVKVYGKQAHASTPW-LGINAFEAAAKIAERLksslstikskyeyddERGAKPTVTLG--GPTVEggtktniv 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 271 -TDFKATIaqaDLKIIIRDFDQQKFNAKKKLLQQIVADLNrqferPRITLELKDqYFNIGDVIQQHPYITELVLNVYHKL 349
Cdd:PRK08651 258 pGYCAFSI---DRRLIPEETAEEVRDELEALLDEVAPELG-----IEVEFEITP-FSEAFVTDPDSELVKALREAIREVL 328
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864111725 350 GLKVQVHPFRGGTDGNFLTAKGIPTPNLFNGG-ENFHGPYEFVTTEAMLTTSKTVIEIIKE 409
Cdd:PRK08651 329 GVEPKKTISLGGTDARFFGAKGIPTVVYGPGElELAHAPDEYVEVKDVEKAAKVYEEVLKR 389
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
213-313 |
9.83e-11 |
|
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: 58.51 E-value: 9.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 213 ETFNAAQAKIKIKGTSVHPGnAFGLMVNAITLANHIISLLPA----------GEVPEKSCGHQGFFlvtdFKATIAQADL 282
Cdd:pfam07687 2 GHKGLAGGHLTVKGKAGHSG-APGKGVNAIKLLARLLAELPAeygdigfdfpRTTLNITGIEGGTA----TNVIPAEAEA 76
|
90 100 110
....*....|....*....|....*....|.
gi 1864111725 283 KIIIRDFDQQKFNAKKKLLQQIVADLNRQFE 313
Cdd:pfam07687 77 KFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
64-407 |
6.34e-10 |
|
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: 60.39 E-value: 6.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 64 VVASLPantTADITPIGFIAHLDTadFPAENVQPQVHENYDGQDvvlneakkivlrvsefpnlknyRGQRLItndGttlL 143
Cdd:cd08659 45 LVATVG---GGDGPVLLLNGHIDT--VPPGDGDKWSFPPFSGRI----------------------RDGRLY---G---R 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 144 GVDD-KAGVASILTAVKYLLEHPSLKHGPISFAFGPDEEIG-RGAKRFdvskfkvkfaytLDNGLPGQLEA--------- 212
Cdd:cd08659 92 GACDmKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGsDGARAL------------LEAGYADRLDAlivgeptgl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 213 ETFNAA----QAKIKIKGTSVHpGNAFGLMVNAITLANHIISLL-----PAGEVPEKScghQGFFLVTDFKATI------ 277
Cdd:cd08659 160 DVVYAHkgslWLRVTVHGKAAH-SSMPELGVNAIYALADFLAELrtlfeELPAHPLLG---PPTLNVGVINGGTqvnsip 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 278 AQADLKIIIR---DFDQQKFnakKKLLQQIVADLNrqferPRITLELKDQYFNIGDVIQQHPYITeLVLNVYHKLGLKVQ 354
Cdd:cd08659 236 DEATLRVDIRlvpGETNEGV---IARLEAILEEHE-----AKLTVEVSLDGDPPFFTDPDHPLVQ-ALQAAARALGGDPV 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1864111725 355 VHPFRGGTDGNFLT-AKGIPT----PnlfnGGENF-HGPYEFVTTEAMLTTSKTVIEII 407
Cdd:cd08659 307 VRPFTGTTDASYFAkDLGFPVvvygP----GDLALaHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
146-401 |
1.17e-09 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 59.72 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 146 DDKAGVASILTAVKYLLEHPSLKHGPISFAFGPDEEIGR-GAKRFDVSKFKVKFAYTL--DNGLPGQLEAETFNAAQAKI 222
Cdd:TIGR01910 105 DMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEaGTLYLLQRGYFKDADGVLipEPSGGDNIVIGHKGSIWFKL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 223 KIKGTSVHPGNAfGLMVNAITLANHIISLL-----------PAGEVPekscgHQGFFLVT-----DFKATIA-QADLKII 285
Cdd:TIGR01910 185 RVKGKQAHASFP-QFGVNAIMKLAKLITELneleehiyarnSYGFIP-----GPITFNPGvikggDWVNSVPdYCEFSID 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 286 IRDFDQQKFNAKKKLLQQIVADLNRQfERPRITLELKDQYFNIGDVIQQHPYITELVLNVYHKLGLKVQVHPFRGGTDGN 365
Cdd:TIGR01910 259 VRIIPEENLDEVKQIIEDVVKALSKS-DGWLYENEPVVKWSGPNETPPDSRLVKALEAIIKKVRGIEPEVLVSTGGTDAR 337
|
250 260 270
....*....|....*....|....*....|....*..
gi 1864111725 366 FLTAKGIPTPNLFNG-GENFHGPYEFVTTEAMLTTSK 401
Cdd:TIGR01910 338 FLRKAGIPSIVYGPGdLETAHQVNEYISIKNLVESTK 374
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
70-230 |
1.19e-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: 57.44 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 70 ANTTADITPIGFIAHLDtadfpaenVQPQvhenydgQDVVLNEAKKIVLRVSEfpnlknyrgqrlitNDGTTLLGVDDKA 149
Cdd:cd18669 6 YGGGGGGKRVLLGAHID--------VVPA-------GEGDPRDPPFFVDTVEE--------------GRLYGRGALDDKG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 150 GVASILTAVKYLLEHPSLKHGPISFAFGPDEEIGRGAKRFDVSKFKVKFAYTLDNGlpgqLEAETFNAAQAKIKIKGTSV 229
Cdd:cd18669 57 GVAAALEALKLLKENGFKLKGTVVVAFTPDEEVGSGAGKGLLSKDALEEDLKVDYL----FVGDATPAPQKGVGIRTPLV 132
|
.
gi 1864111725 230 H 230
Cdd:cd18669 133 D 133
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
64-230 |
1.85e-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: 57.05 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 64 VVASLPAntTADITPIGFIAHLDtadfpaenVQPQvhenydgQDVVLNEAKKIVLRVsefpnlknyrgqrlITNDGTTLL 143
Cdd:cd03873 2 LIARLGG--GEGGKSVALGAHLD--------VVPA-------GEGDNRDPPFAEDTE--------------EEGRLYGRG 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 144 GVDDKAGVASILTAVKYLLEHPSLKHGPISFAFGPDEEIGRGAKRFDVSKFKVKFAYTLDNGLpgQLEAETFNAAQAKIK 223
Cdd:cd03873 51 ALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAF--VIDATAGPILQKGVV 128
|
....*..
gi 1864111725 224 IKGTSVH 230
Cdd:cd03873 129 IRNPLVD 135
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
151-373 |
2.81e-08 |
|
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: 55.30 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 151 VASILTAVKYLLEHPSLKHGPISFAFGPDEEIGRGAKRF----DVSKFKVKFAYTLDN--GLP-GQLEAE--TFNAA--Q 219
Cdd:cd03886 94 TAMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPGGAKAMieegVLENPGVDAAFGLHVwpGLPvGTVGVRsgALMASadE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 220 AKIKIKGTSVH---PGNAfglmVNAITLANHIIS---LLPAGEVPEKscgHQGFFLVTDFKA-----TIA-QADLKIIIR 287
Cdd:cd03886 174 FEITVKGKGGHgasPHLG----VDPIVAAAQIVLalqTVVSRELDPL---EPAVVTVGKFHAgtafnVIPdTAVLEGTIR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 288 DFDQQKFNAKKKLLQQIVADLNRQFERpRITLELKDQYfnigDVIQQHPYITELVLNVYHKLGLKVQVH---PFRGGTDG 364
Cdd:cd03886 247 TFDPEVREALEARIKRLAEGIAAAYGA-TVELEYGYGY----PAVINDPELTELVREAAKELLGEEAVVepePVMGSEDF 321
|
....*....
gi 1864111725 365 NFLTAKgIP 373
Cdd:cd03886 322 AYYLEK-VP 329
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
146-401 |
8.48e-08 |
|
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: 53.54 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 146 DDKAGVASILTAVKYLLEHPSLKHGPISFAFGPDEE-IGRGAKRFDVSKFKVKFAYTLdNGLPGQLEAETFN---AAQAK 221
Cdd:cd08011 101 DMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEEtGGRAGTKYLLEKVRIKPNDVL-IGEPSGSDNIRIGekgLVWVI 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 222 IKIKGTSVHPGNaFGLMVNAITLANHIISLLpaGEVpEKS-------CGHQgFFLVTDFKAtiAQADLKIIIrDFDQQKF 294
Cdd:cd08011 180 IEITGKPAHGSL-PHRGESAVKAAMKLIERL--YEL-EKTvnpgvikGGVK-VNLVPDYCE--FSVDIRLPP-GISTDEV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 295 NAK-KKLLQQIvadlnrqferPRITLELKdQYFNIGDVIQQHPYITELVLNVYHKLGLKVQVHPFRGGTDGNFLTAKGIP 373
Cdd:cd08011 252 LSRiIDHLDSI----------EEVSFEIK-SFYSPTVSNPDSEIVKKTEEAITEVLGIRPKEVISVGASDARFYRNAGIP 320
|
250 260
....*....|....*....|....*....
gi 1864111725 374 TPNLFNGG-ENFHGPYEFVTTEAMLTTSK 401
Cdd:cd08011 321 AIVYGPGRlGQMHAPNEYVEIDELIKVIK 349
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
143-391 |
2.27e-07 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 52.71 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 143 LGV-DDKAGVASILTAVKYLLEHPSLKHGPISFAFGPDEEIGRGAKRFDVSKFKVKFAYTLD---NGLPGQLEAETFNAA 218
Cdd:PRK06133 132 PGIaDDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGSPGSRELIAELAAQHDVVFScepGRAKDALTLATSGIA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 219 QAKIKIKGTSVHPGNAFGLMVNAITLANHII-----------------SLLPAGEV----PEkscghqgfflvtdfKATi 277
Cdd:PRK06133 212 TALLEVKGKASHAGAAPELGRNALYELAHQLlqlrdlgdpakgttlnwTVAKAGTNrnviPA--------------SAS- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 278 AQADLKI-IIRDFDQQKFNAKKKLLQQIVAD--LNRQFERPRITLELKDQYFNIGDVIQQhpyitelvlnVYHKLGLKVQ 354
Cdd:PRK06133 277 AQADVRYlDPAEFDRLEADLQEKVKNKLVPDteVTLRFERGRPPLEANAASRALAEHAQG----------IYGELGRRLE 346
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1864111725 355 VHPFR--GGTDGNFLTAKGipTPNLFNG----GENFHGPYEFV 391
Cdd:PRK06133 347 PIDMGtgGGTDAAFAAGSG--KAAVLEGfglvGFGAHSNDEYI 387
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
135-197 |
1.55e-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: 50.21 E-value: 1.55e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864111725 135 ITNDGTTLlGVDDKAGVASILTavkyLLEHPSLKHGPISFAFGPDEEIG-RGAKRFDVSKFKVK 197
Cdd:cd03890 97 LKATGTTL-GADNGIGVAYALA----ILEDKDIEHPPLEVLFTVDEETGmTGALGLDPSLLKGK 155
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
151-254 |
6.44e-06 |
|
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 47.80 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 151 VASILTAVKYLLEHPSLKHGPISFAFGPDEEIGRGAKR------FDvsKFKVKFAYTL--DNGLP-GQLE--AETFNAA- 218
Cdd:COG1473 106 TAMLLGAAKALAELRDELKGTVRLIFQPAEEGGGGAKAmiedglLD--RPDVDAIFGLhvWPGLPvGTIGvrPGPIMAAa 183
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1864111725 219 -QAKIKIKGTSVH---PGNAfglmVNAITLANHIISLLPA 254
Cdd:COG1473 184 dSFEITIKGKGGHaaaPHLG----IDPIVAAAQIVTALQT 219
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
152-249 |
9.47e-05 |
|
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: 44.25 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 152 ASILTAVKYLLEHPSLKHGPISFAFGPDEEIGRGAKRF-------DVSKFkvkFAYTLDNGLP-GQLEAE---TF-NAAQ 219
Cdd:cd08019 94 AMLLGAAKILNEIKDTIKGTVKLIFQPAEEVGEGAKQMieegvleDVDAV---FGIHLWSDVPaGKISVEagpRMaSADI 170
|
90 100 110
....*....|....*....|....*....|
gi 1864111725 220 AKIKIKGTSVHpGNAFGLMVNAITLANHII 249
Cdd:cd08019 171 FKIEVKGKGGH-GSMPHQGIDAVLAAASIV 199
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
93-409 |
1.69e-04 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 43.21 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 93 ENVQPQVHENYDGQ--DVVLNEAKKIVLRVsefpNLKNYRGQRLITNDGTTLLGV---DDKAGVASILTAVKYLleHPSL 167
Cdd:PRK08652 33 ESLGYDVHIESDGEviNIVVNSKAELFVEV----HYDTVPVRAEFFVDGVYVYGTgacDAKGGVAAILLALEEL--GKEF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 168 KHGPISFAFGPDEEI-GRGAKRFdVSKFKVKFAYTLDnglPGQLEA--ETFNAAQAKIKIKGTSVHpgNAFGLM-VNAIT 243
Cdd:PRK08652 107 EDLNVGIAFVSDEEEgGRGSALF-AERYRPKMAIVLE---PTDLKVaiAHYGNLEAYVEVKGKPSH--GACPESgVNAIE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 244 LANHIISLLPAGEvPEKSCGHQGFFLVT------DFKATIAQADLKIIIRDFDQQKFNAKKKLLQQIVADLNRQFErpri 317
Cdd:PRK08652 181 KAFEMLEKLKELL-KALGKYFDPHIGIQeiiggsPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYE---- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 318 TLELKDQYFNIGDViqqhpYITELVLNVYHKLGLKVQVHPFRGGTDGNFLTAKGIPTPnLFNGGE--NFHGPYEFVTTEA 395
Cdd:PRK08652 256 YTEIWDGFELDEDE-----EIVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTKTV-VWGPGEldLCHTKFERIDVRE 329
|
330
....*....|....*..
gi 1864111725 396 MLTTS---KTVIEIIKE 409
Cdd:PRK08652 330 VEKAKeflKALNEILLE 346
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
138-243 |
5.68e-04 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 41.86 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 138 DGTTLLG---VDDKAGVASILTAVKYLL-EHPSLKHGpISFAFGPDEEIG--RGAK---RFDVSKFKVK-FAYTLDNGLP 207
Cdd:cd05674 101 DGGYIWGrgaLDDKNSLIGILEAVELLLkRGFKPRRT-IILAFGHDEEVGgeRGAGaiaELLLERYGVDgLAAILDEGGA 179
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1864111725 208 GqLEAETFNAAQA------------KIKIKGTSVH-----PGNAFGLMVNAIT 243
Cdd:cd05674 180 V-LEGVFLGVPFAlpgvaekgymdvEITVHTPGGHssvppKHTGIGILSEAVA 231
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
145-207 |
1.86e-03 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 40.31 E-value: 1.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864111725 145 VDDKAGVASILTAVKYLLehpslKHG--P---ISFAFGPDEEI-GRGAKRFdVSKFK---VKFAYTLDNGLP 207
Cdd:PRK08262 153 LDDKGSLVAILEAAEALL-----AQGfqPrrtIYLAFGHDEEVgGLGARAI-AELLKergVRLAFVLDEGGA 218
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
145-183 |
2.21e-03 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 40.14 E-value: 2.21e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1864111725 145 VDDKAGVASILTAVKYLLEHPSlkHGPISFAFGPDEEIG 183
Cdd:PRK08554 102 ADDKGNVASVMLALKELSKEPL--NGKVIFAFTGDEEIG 138
|
|
| M42_glucanase_like |
cd05657 |
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ... |
146-186 |
3.71e-03 |
|
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1,4-beta-glucanase or endoglucanase)-like subfamily. Proteins in this subfamily are co-catalytic metallopeptidases, found in archaea and bacteria. They show similarity to cellulase and endo-1,4-beta-glucanase (endoglucanase) which typically bind two zinc or cobalt atoms. Some of the enzymes exhibit typical aminopeptidase specificity, whereas others are also capable of N-terminal deblocking activity, i.e. hydrolyzing acylated N-terminal residues. Many of these enzymes are assembled either as tetrahedral dodecamers or as octahedral tetracosameric structures, with the active site located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers.
Pssm-ID: 349907 [Multi-domain] Cd Length: 337 Bit Score: 39.18 E-value: 3.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1864111725 146 DDKAGVASILTAVKYLLEHPSLKHGPISFAFGPDEEIGRGA 186
Cdd:cd05657 181 DDKASVAILLALARALKENKLKLPVDTHFLFSNYEEVGHGA 221
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
138-249 |
5.04e-03 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. 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: 349916 [Multi-domain] Cd Length: 373 Bit Score: 38.66 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864111725 138 DG--TTLLGvddkagvasiltAVKYLLEHPSLKhGPISFAFGPDEEIGRGAKR------FDvsKFKVKFAYTLDNgLPGq 209
Cdd:cd05666 93 DGhtTMLLG------------AARYLAETRNFD-GTVHFIFQPAEEGGGGAKAmiedglFE--RFPCDAVYGLHN-MPG- 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1864111725 210 LEAETF---------NAAQAKIKIKGTSVHpgnafGLM----VNAITLANHII 249
Cdd:cd05666 156 LPAGKFavrpgpmmaSADTFEITIRGKGGH-----AAMphlgVDPIVAAAQLV 203
|
|
| FrvX |
COG1363 |
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ... |
146-208 |
5.11e-03 |
|
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];
Pssm-ID: 440974 [Multi-domain] Cd Length: 353 Bit Score: 38.57 E-value: 5.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864111725 146 DDKAGVASILTAVKYLLEHPsLKHgPISFAFGPDEEIG-RGAKrfdVSKFKVK--FAYTLDNGLPG 208
Cdd:COG1363 179 DDRAGCAVLLELLKALKDED-LPV-TVYFVFTVQEEVGlRGAS---TAAYDIKpdEAIAVDVTPAG 239
|
|
| |
