|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
1-401 |
0e+00 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 670.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 1 MKVQERFLKYVTFDTQSDENSQTTPSSLKQLKLAKYLVDELKNIGVTNAYVDEFGIVYGSLLANCEANCPKIGFIAHMDT 80
Cdd:PRK05469 2 DKLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDENGYVMATLPANVDKDVPTIGFIAHMDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 81 SPDMSGENVKPRIIENYDGSDIILNEKlNIHMGPNDFESLNRNIGENLIVTDGTTLLGADDKAGIAEIMTMLETIIQ-KN 159
Cdd:PRK05469 82 APDFSGKNVKPQIIENYDGGDIALGDG-NEVLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYLIAhPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 160 LPHGDIKIAFTPDEEVGRGTDHFNVKAFDADFAYTVDGGEVEFIDYENFNAASAVLDIQGLSIHPGSAKGKMINALLVGM 239
Cdd:PRK05469 161 IKHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALLLAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 240 EFHSMLPVEQNPAYTEGYEGFNHLTDMHGECEHAHMSYIIRNHDETLFEQQKEDFKRIADYLNKKYPENTITLQITDSYA 319
Cdd:PRK05469 241 DFHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKYGEGRVELEIKDQYY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 320 NMRQIIEQNMNIIELVKKSMEEIGLQPASAAIRGGTDGARLTYEGLPCPNLGTGGYNYHGKYEYVSINEMEKSVALLLKI 399
Cdd:PRK05469 321 NMREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVIVEI 400
|
..
gi 495962659 400 VE 401
Cdd:PRK05469 401 AE 402
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
3-402 |
0e+00 |
|
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; tripeptide aminopeptidase; tripeptidase) subfamily. PepT acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349887 [Multi-domain] Cd Length: 400 Bit Score: 640.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 3 VQERFLKYVTFDTQSDENSQTTPSSLKQLKLAKYLVDELKNIGVTNAYVDEFGIVYGSLLANCEANCPKIGFIAHMDTSP 82
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDEHGYVTATLPANVDKDVPTIGFIAHMDTAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 83 DMSGENVKPRIIENYDGSDIILNEKlNIHMGPNDFESLNRNIGENLIVTDGTTLLGADDKAGIAEIMTMLETIIQK-NLP 161
Cdd:cd03892 81 DNSGKNVKPQIIENYDGGDIVLNES-GIVLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIEHpEIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 162 HGDIKIAFTPDEEVGRGTDHFNVKAFDADFAYTVDGGEVEFIDYENFNAASAVLDIQGLSIHPGSAKGKMINALLVGMEF 241
Cdd:cd03892 160 HGDIRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLAADF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 242 HSMLPVEQNPAYTEGYEGFNHLTDMHGECEHAHMSYIIRNHDETLFEQQKEDFKRIADYLNKKYPENTITLQITDSYANM 321
Cdd:cd03892 240 HSMLPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKYGEGRVELEIKDQYYNM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 322 RQIIEQNMNIIELVKKSMEEIGLQPASAAIRGGTDGARLTYEGLPCPNLGTGGYNYHGKYEYVSINEMEKSVALLLKIVE 401
Cdd:cd03892 320 KEKIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIVKIAE 399
|
.
gi 495962659 402 N 402
Cdd:cd03892 400 L 400
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
1-402 |
4.67e-165 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 467.22 E-value: 4.67e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 1 MKVQERFLKYVTFDTQSDEnsqttpsslkQLKLAKYLVDELKNIGVtNAYVDEFGIVYGSLLANCEANCPKIGFIAHMDT 80
Cdd:COG2195 3 ERLLERFLEYVKIPTPSDH----------EEALADYLVEELKELGL-EVEEDEAGNVIATLPATPGYNVPTIGLQAHMDT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 81 SPDMSGENVKPRIienyDGsdiilneklnihmgpndfeslnrnigeNLIVTDGTTLLGADDKAGIAEIMTMLETIIQKNL 160
Cdd:COG2195 72 VPQFPGDGIKPQI----DG---------------------------GLITADGTTTLGADDKAGVAAILAALEYLKEPEI 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 161 PHGDIKIAFTPDEEVG-RGTDHFNVKAFDADFAYTVDGGEVEFIDYENFNAASAVLDIQGLSIHPGSAKGKMINALLVGM 239
Cdd:COG2195 121 PHGPIEVLFTPDEEIGlRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIKLAA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 240 EFHSMLPVEQNPAYTEGYEGFNHLTDMH-GECEHAHMSYIIRNHDETLFEQQKEDFKRIADYLNKKYPENTITLQITDSY 318
Cdd:COG2195 201 RFLAALPLGRIPEETEGNEGFIHGGSATnAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGVGVVEVEIEDQY 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 319 ANMRqiIEQNMNIIELVKKSMEEIGLQPASAAIRGGTDGARLTYEGLPCPNLGTGGYNYHGKYEYVSINEMEKSVALLLK 398
Cdd:COG2195 281 PNWK--PEPDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWELLVE 358
|
....
gi 495962659 399 IVEN 402
Cdd:COG2195 359 ILKL 362
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
1-405 |
8.43e-162 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 460.54 E-value: 8.43e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 1 MKVQERFLKYVTFDTQSDENSQTTPSSLKQLKLAKYLVDELKNIGVTNAYVDEFGIVYGSLLANCEaNCPKIGFIAHMDT 80
Cdd:PRK13381 1 MQLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDIVIDEHAIVTAKLPGNTP-GAPRIGFIAHLDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 81 SPDMSGENVKPRIIEnYDGSDIILNEKLNIHMGPNDFESLNRNIGENLIVTDGTTLLGADDKAGIAEIMTMLETIIQKNL 160
Cdd:PRK13381 80 VDVGLSPDIHPQILR-FDGGDLCLNAEQGIWLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLENLTENEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 161 PHGDIKIAFTPDEEVG-RGTDHFNVKAFDADFAYTVDGGEVEFIDYENFNAASAVLDIQGLSIHPGSAKGKMINALLVGM 239
Cdd:PRK13381 159 EHGDIVVAFVPDEEIGlRGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNPILMAN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 240 EFHSMLPVEQNPAYTEGYEGFNHLTDMHGECEHAHMSYIIRNHDETLFEQQKEDFKRIADYLNKKYPENTITLQITDSYA 319
Cdd:PRK13381 239 DFISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINAKYPTARVSLTLTDQYS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 320 NMRQIIEQNMNIIELVKKSMEEIGLQPASAAIRGGTDGARLTYEGLPCPNLGTGGYNYHGKYEYVSINEMEKSVALLLKI 399
Cdd:PRK13381 319 NISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEVTITI 398
|
....*.
gi 495962659 400 VENSLK 405
Cdd:PRK13381 399 CLLAAK 404
|
|
| peptidase-T |
TIGR01882 |
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has ... |
2-401 |
2.69e-161 |
|
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: 459.75 E-value: 2.69e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 2 KVQERFLKYVTFDTQSDENSQTTPSSLKQLKLAKYLVDELKNIGVTNAYVDEF-GIVYGSLLANCEANCPKIGFIAHMDT 80
Cdd:TIGR01882 4 ELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEKnGYVIATIPSNTDKDVPTIGFLAHVDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 81 SpDMSGENVKPRIIENYDGSDIILNEKLNIHMGPNDFESLNRNIGENLIVTDGTTLLGADDKAGIAEIMTMLETIIQK-N 159
Cdd:TIGR01882 84 A-DFNGENVNPQIIENYDGESIIQLGDLEFTLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAADYLINHpE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 160 LPHGDIKIAFTPDEEVGRGTDHFNVKAFDADFAYTVDGGEVEFIDYENFNAASAVLDIQGLSIHPGSAKGKMINALLVGM 239
Cdd:TIGR01882 163 IKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAAQIAI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 240 EFHSMLPVEQNPAYTEGYEGFNHLTDMHGECEHAHMSYIIRNHDETLFEQQKEDFKRIADYLNKKYPENTITLQITDSYA 319
Cdd:TIGR01882 243 DLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEYGQDRIKLDMNDQYY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 320 NMRQIIEQNMNIIELVKKSMEEIGLQPASAAIRGGTDGARLTYEGLPCPNLGTGGYNYHGKYEYVSINEMEKSVALLLKI 399
Cdd:TIGR01882 323 NMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDVIVEI 402
|
..
gi 495962659 400 VE 401
Cdd:TIGR01882 403 AK 404
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
5-401 |
2.90e-120 |
|
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: 354.76 E-value: 2.90e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 5 ERFLKYVTFDTQSDENSQTTPSSLKQLKLAKYLVDELKNIGVTNAYVDEFGIVYGSLLANCEANCPKIGFIAHMDTSPDM 84
Cdd:cd05645 3 ERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEKGTLIATLPANVDGDIPAIGFISHVDTSPDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 85 SGENVKPRIIENYDGSDIILNEKLNIhMGPNDFESLNRNIGENLIVTDGTTLLGADDKAGIAEIMTMLETIIQKNLPHGD 164
Cdd:cd05645 83 SGKNVNPQIVENYRGGDIALGIGDEV-LSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKNIPHGD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 165 IKIAFTPDEEVGRGTDHFNVKAFDADFAYTVDGGEVEFIDYENFNAASAVLDIQGLSIHPGSAKGKMINALLVGMEFHSM 244
Cdd:cd05645 162 IEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAARIHAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 245 LPVEQNPAYTEGYEGFNHLTDMHGECEHAHMSYIIRNHDETLFEQQKEDFKRIADYLNKK-YPENTITLQITDSYANMRQ 323
Cdd:cd05645 242 VPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVGKGlHPDCYIELVIEDSYYNFRE 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495962659 324 IIEQNMNIIELVKKSMEEIGLQPASAAIRGGTDGARLTYEGLPCPNLGTGGYNYHGKYEYVSINEMEKSVALLLKIVE 401
Cdd:cd05645 322 KVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIVRIAE 399
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
22-401 |
3.90e-33 |
|
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: 127.57 E-value: 3.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 22 QTTPSSLKQLKLAKYLVDELKNIGVTNAYVD-------EFGIVYGSLLANcEANCPKIGFIAHMDT-SPdmsGENVKPRI 93
Cdd:cd05683 14 QIDSETLHEKEISKVLKKKFENLGLSVIEDDagkttggGAGNLICTLKAD-KEEVPKILFTSHMDTvTP---GINVKPPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 94 IENydgsdiilneklnihmgpndfeslnrnigeNLIVTDGTTLLGADDKAGIAEIMTMLETIIQKNLPHGDIKIAFTPDE 173
Cdd:cd05683 90 IAD------------------------------GYIYSDGTTILGADDKAGIAAILEAIRVIKEKNIPHGQIQFVITVGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 174 EVGR-GTDHFNVKAFDADFAYTVDG-GEVEFIDYENFNAASAVLDIQGLSIHPGSAKGKMINALLVGMEFHSMLPVEQNP 251
Cdd:cd05683 140 ESGLvGAKALDPELIDADYGYALDSeGDVGTIIVGAPTQDKINAKIYGKTAHAGTSPEKGISAINIAAKAISNMKLGRID 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 252 AYTEGYEG-FNHLTDMHGECEHAHMSYIIRNHDETLFEQQKEDFKRIADYLNKKYPENtITLQITDSYANMRqiIEQNMN 330
Cdd:cd05683 220 EETTANIGkFQGGTATNIVTDEVNIEAEARSLDEEKLDAQVKHMKETFETTAKEKGAH-AEVEVETSYPGFK--INEDEE 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495962659 331 IIELVKKSMEEIGLQPASAAIRGGTDGARLTYEGLPCPNLGTGGYNYHGKYEYVSINEMEKSVALLLKIVE 401
Cdd:cd05683 297 VVKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAVLVVEIIK 367
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
2-401 |
3.72e-32 |
|
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: 124.66 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 2 KVQERFLKYVTFDTQSDensqttpsslKQLKLAKYLVDELKNIGVTNAYVDEFGIVYG--SLLANCEA--NCPKIGFIAH 77
Cdd:TIGR01883 1 RLKKYFLELIQIDSESG----------KEKAILTYLKKQITKLGIPVSLDEVPAEVSNdnNLIARLPGtvKFDTIFFCGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 78 MDTSPDmsGENVKPrIIENydgsdiilneklnihmgpndfeslnrnigeNLIVTDGTTLLGADDKAGIAEIMTMLETIIQ 157
Cdd:TIGR01883 71 MDTVPP--GAGPEP-VVED------------------------------GIFTSLGGTILGADDKAGVAAMLEAMDVLST 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 158 KNLPHGDIKIAFTPDEEVG-RGTDHFNVKAFDADFAYTVD-GGEVEFIDYENFNAASAVLDIQGLSIHPGSAKGKMINAL 235
Cdd:TIGR01883 118 EETPHGTIEFIFTVKEELGlIGMRLFDESKITAAYGYCLDaPGEVGNIQLAAPTQVKVDATIAGKDAHAGLVPEDGISAI 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 236 LVG-MEFHSMLPV---EQNPAYTEGYE-GFNHLTDMHGECEHAHMSYIIRNHDETLFEQQKEDFKRIADylnkKYpENTI 310
Cdd:TIGR01883 198 SVArMAIHAMRLGridEETTANIGSFSgGVNTNIVQDEQLIVAEARSLSFRKAEAQVQTMRERFEQAAE----KY-GATL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 311 TLQITDSYANMRqiIEQNMNIIELVKKSMEEIGLQPASAAIRGGTDGARLTYEGLPCPNLGTGGYNYHGKYEYVSINEME 390
Cdd:TIGR01883 273 EEETRLIYEGFK--IHPQHPLMNIFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETISIEQLV 350
|
410
....*....|.
gi 495962659 391 KSVALLLKIVE 401
Cdd:TIGR01883 351 KLAELVIALAE 361
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
11-402 |
5.85e-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: 96.49 E-value: 5.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 11 VTFDTQSDENsqttpsslkqLKLAKYLVDELKNIGVTnAYVDEFGIVYGSLLA--NCEANCPKIGFIAHMDTSP-----D 83
Cdd:COG0624 22 VRIPSVSGEE----------AAAAELLAELLEALGFE-VERLEVPPGRPNLVArrPGDGGGPTLLLYGHLDVVPpgdleL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 84 MSGENVKPRIIENYdgsdiilneklnIHmGPndfeslnrnigenlivtdGTtllgADDKAGIAEIMTMLETIIQKNL-PH 162
Cdd:COG0624 91 WTSDPFEPTIEDGR------------LY-GR------------------GA----ADMKGGLAAMLAALRALLAAGLrLP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 163 GDIKIAFTPDEEVG-RGTDHF---NVKAFDADFAYTVDGGEVEFIDYENFNAASAVLDIQGLSIHpGSAKGKMINALLVG 238
Cdd:COG0624 136 GNVTLLFTGDEEVGsPGARALveeLAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAH-SSRPELGVNAIEAL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 239 MEFHS-----MLPVEQNPAYteGYEGFNhLTDMHGE------CEHAHMSYIIRnhdeTLFEQQKED-FKRIADYLNKKYP 306
Cdd:COG0624 215 ARALAalrdlEFDGRADPLF--GRTTLN-VTGIEGGtavnviPDEAEAKVDIR----LLPGEDPEEvLAALRALLAAAAP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 307 ENTITLQ-ITDSYANMRqiIEQNMNIIELVKKSMEEI-GLQPASAAIRGGTDGARLTYE-GLPCPNLGTGGY-NYHGKYE 382
Cdd:COG0624 288 GVEVEVEvLGDGRPPFE--TPPDSPLVAAARAAIREVtGKEPVLSGVGGGTDARFFAEAlGIPTVVFGPGDGaGAHAPDE 365
|
410 420
....*....|....*....|
gi 495962659 383 YVSINEMEKSVALLLKIVEN 402
Cdd:COG0624 366 YVELDDLEKGARVLARLLER 385
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
139-402 |
8.46e-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: 74.69 E-value: 8.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 139 ADDKAGIAEIMTMLETIIQKNLPHGDIKIAFTPDEEVGRG-----TDHFNVKAFDADFAYTVDGGE------VEFIDYEN 207
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEGLKKGTVKLLFQPDEEGGMGgaralIEDGLLEREKVDAVFGLHIGEptllegGIAIGVVT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 208 FNAASA--VLDIQGLSIHpGSAKGKMINALLVGMEF----HSMLPVEQNPAYTEGYEgFNHLTDMHGE----CEHAHMSY 277
Cdd:pfam01546 113 GHRGSLrfRVTVKGKGGH-ASTPHLGVNAIVAAARLilalQDIVSRNVDPLDPAVVT-VGNITGIPGGvnviPGEAELKG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 278 IIRNHDETLFEQQKEDFKRIADYLNKKYPEnTITLQITDSYANMRqiiEQNMNIIELVKKSMEE-IGLQPASAAI--RGG 354
Cdd:pfam01546 191 DIRLLPGEDLEELEERIREILEAIAAAYGV-KVEVEYVEGGAPPL---VNDSPLVAALREAAKElFGLKVELIVSgsMGG 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 495962659 355 TDgARLTYEGLPCP--NLGTGGYNYHGKYEYVSINEMEKSVALLLKIVEN 402
Cdd:pfam01546 267 TD-AAFFLLGVPPTvvFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
140-401 |
1.01e-13 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 71.71 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 140 DDKAGIAEIMTMLETIIQKNlPHGDIKIAFTPDEEV-GRGTDHFnVKAFDADFAYTVDGGEVEfIDYENFNAASAVLDIQ 218
Cdd:PRK08652 87 DAKGGVAAILLALEELGKEF-EDLNVGIAFVSDEEEgGRGSALF-AERYRPKMAIVLEPTDLK-VAIAHYGNLEAYVEVK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 219 GLSIHpGSAKGKMINALLVGMEFHSMLPvEQNPAYTEGYEGFNHLTDMHGECEHAHMSYIIRNHDETLF--EQQKEDFKR 296
Cdd:PRK08652 164 GKPSH-GACPESGVNAIEKAFEMLEKLK-ELLKALGKYFDPHIGIQEIIGGSPEYSIPALCRLRLDARIppEVEVEDVLD 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 297 IADYLNKKYPENTITLQITDSYanmrqIIEQNMNIIELVKKSMEEIGLQPASAAIRGGTDGARLTYEGLPCPNLGTGGYN 376
Cdd:PRK08652 242 EIDPILDEYTVKYEYTEIWDGF-----ELDEDEEIVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTKTVVWGPGELD 316
|
250 260
....*....|....*....|....*.
gi 495962659 377 Y-HGKYEYVSINEMEKSVALLLKIVE 401
Cdd:PRK08652 317 LcHTKFERIDVREVEKAKEFLKALNE 342
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
205-309 |
3.89e-09 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 53.89 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 205 YENFNAASAVLDIQGLSIHPGsAKGKMINALLVGMEFHSMLPVEQNP-AYTEGYEGFNhLTDMHGE------CEHAHMSY 277
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSG-APGKGVNAIKLLARLLAELPAEYGDiGFDFPRTTLN-ITGIEGGtatnviPAEAEAKF 78
|
90 100 110
....*....|....*....|....*....|..
gi 495962659 278 IIRNhdeTLFEQQKEDFKRIADYLNKKYPENT 309
Cdd:pfam07687 79 DIRL---LPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
32-405 |
8.40e-09 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 56.92 E-value: 8.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 32 KLAKYLVDELKNIG-------VTNAYVDEFGIVYGSLLANCEANCPKIGFIAHMDTspdmsgenVKPriienydgsdiil 104
Cdd:PRK08651 30 EIAEFLRDTLEELGfsteiieVPNEYVKKHDGPRPNLIARRGSGNPHLHFNGHYDV--------VPP------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 105 neklniHMGPNDFESLNRNIGENLIVTDGTTllgaDDKAGIAEIMTMLETIiqKNLPHGDIKIAFTPDEEV-GRGTDHF- 182
Cdd:PRK08651 89 ------GEGWSVNVPFEPKVKDGKVYGRGAS----DMKGGIAALLAAFERL--DPAGDGNIELAIVPDEETgGTGTGYLv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 183 NVKAFDADFAYTVDGGEVEFIDYENFNAASAVLDIQGLSIHPGSAK-------------GKMINALLVGMEFHSM-LPVE 248
Cdd:PRK08651 157 EEGKVTPDYVIVGEPSGLDNICIGHRGLVWGVVKVYGKQAHASTPWlginafeaaakiaERLKSSLSTIKSKYEYdDERG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 249 QNPAYTEGYEGFNHLTDMH---GECEhahMSYIIRNHDETLFEQQKEDFKRIADYLNKKYPENtITLQITDSY-ANMrqi 324
Cdd:PRK08651 237 AKPTVTLGGPTVEGGTKTNivpGYCA---FSIDRRLIPEETAEEVRDELEALLDEVAPELGIE-VEFEITPFSeAFV--- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 325 IEQNMNIIELVKKSMEE-IGLQPASAAIRGGTDGARLTYEGLPCPNLGTGGY-NYHGKYEYVSINEMEKSValllKIVEN 402
Cdd:PRK08651 310 TDPDSELVKALREAIREvLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGELeLAHAPDEYVEVKDVEKAA----KVYEE 385
|
...
gi 495962659 403 SLK 405
Cdd:PRK08651 386 VLK 388
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
24-401 |
1.64e-08 |
|
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.
Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 56.06 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 24 TPSSLKQ--LKLAKYLVDELKNIG--VTNAYVDEFGivyGSLLA-NCEANCPKIGFIAHMDTspdmsgenVKPRiienyd 98
Cdd:cd03885 13 SGTYDKEgvDRVAELLAEELEALGftVERRPLGEFG---DHLIAtFKGTGGKRVLLIGHMDT--------VFPE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 99 GSdiilneklnihmgpndfeslnrnIGENLIVTDGTTLLG---ADDKAGIAEIMTMLETIIQKN-LPHGDIKIAFTPDEE 174
Cdd:cd03885 76 GT-----------------------LAFRPFTVDGDRAYGpgvADMKGGLVVILHALKALKAAGgRDYLPITVLLNSDEE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 175 VGR--GTDHFNVKAFDADFAYTVDGGEVEfidyENFNAA-----SAVLDIQGLSIHPGSAKGKMINALL----VGMEFHS 243
Cdd:cd03885 133 IGSpgSRELIEEEAKGADYVLVFEPARAD----GNLVTArkgigRFRLTVKGRAAHAGNAPEKGRSAIYelahQVLALHA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 244 MLPVEQ----NPAYTEGYEGFNHLTDmhgeceHAHMSYIIRNHDETLFEQQKEDFKRIADylNKKYPENTITLQITDSYA 319
Cdd:cd03885 209 LTDPEKgttvNVGVISGGTRVNVVPD------HAEAQVDVRFATAEEADRVEEALRAIVA--TTLVPGTSVELTGGLNRP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 320 NMRQIiEQNMNIIELVKKSMEEIGLQPASAAIRGGTDGARLTYEGLP--CpNLGTGGYNYHGKYEYVSINEMEKSVALLL 397
Cdd:cd03885 281 PMEET-PASRRLLARAQEIAAELGLTLDWEATGGGSDANFTAALGVPtlD-GLGPVGGGAHTEDEYLELDSLVPRIKLLA 358
|
....
gi 495962659 398 KIVE 401
Cdd:cd03885 359 RLLM 362
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
34-400 |
2.38e-08 |
|
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: 55.38 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 34 AKYLVDELKNIGVTnayVDEFGIVY-GSLLANCE-ANCPKIGFIAHMDTspdmsgenVKPRIIENYDGSdiilneklnih 111
Cdd:cd08659 20 AEYLAELLAKRGYG---IESTIVEGrGNLVATVGgGDGPVLLLNGHIDT--------VPPGDGDKWSFP----------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 112 mgPndFEslnRNIGENLIVTDGTtllgADDKAGIAEIMTMLETIIQKNLPH-GDIKIAFTPDEEVG-RGTDHF--NVKAF 187
Cdd:cd08659 78 --P--FS---GRIRDGRLYGRGA----CDMKGGLAAMVAALIELKEAGALLgGRVALLATVDEEVGsDGARALleAGYAD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 188 DADFA-------YTVDGGEVEFIDYEnfnaasavLDIQGLSIHpGSAKGKMINALLVGMEF-----HSMLPVEQNPAYTe 255
Cdd:cd08659 147 RLDALivgeptgLDVVYAHKGSLWLR--------VTVHGKAAH-SSMPELGVNAIYALADFlaelrTLFEELPAHPLLG- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 256 gyeGFNH-LTDMHG---------ECEhahMSYIIRnhdeTLFEQQKEDF-KRIADYLNKKYPENTITLQITDSYAnmrQI 324
Cdd:cd08659 217 ---PPTLnVGVINGgtqvnsipdEAT---LRVDIR----LVPGETNEGViARLEAILEEHEAKLTVEVSLDGDPP---FF 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495962659 325 IEQNMNIIELVKKSMEEIGLQPASAAIRGGTDGARLT-YEGLPCPNLGTGGYNY-HGKYEYVSINEMEKSVALLLKIV 400
Cdd:cd08659 284 TDPDHPLVQALQAAARALGGDPVVRPFTGTTDASYFAkDLGFPVVVYGPGDLALaHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
70-396 |
6.85e-08 |
|
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: 52.43 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 70 PKIGFIAHMDTSPDMSGENVKPRIIEnydgsdiilneklnihmgpndfeslnrnigENLIVTDGTTLLGADDKAGIAEIM 149
Cdd:cd03873 13 KSVALGAHLDVVPAGEGDNRDPPFAE------------------------------DTEEEGRLYGRGALDDKGGVAAAL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 150 TMLETIIQKNL-PHGDIKIAFTPDEEVGRGTDHFNVKAFDADFAYTVDggevefidyenfnaasavldiQGLSIHPGSAK 228
Cdd:cd03873 63 EALKRLKENGFkPKGTIVVAFTADEEVGSGGGKGLLSKFLLAEDLKVD---------------------AAFVIDATAGP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 229 gkminallvgmefhsmlpveqnpaytegyegfnhltdmhgeceHAHMSYIIRNHdetlfeqqkedfkriadylnkkypen 308
Cdd:cd03873 122 -------------------------------------------ILQKGVVIRNP-------------------------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 309 titlqitdsyanmrqiieqnmnIIELVKKSMEEIGLQPASAA-IRGGTDGARLTYEGLPCPNLGTGG-YNYHGKYEYVSI 386
Cdd:cd03873 133 ----------------------LVDALRKAAREVGGKPQRASvIGGGTDGRLFAELGIPGVTLGPPGdKGAHSPNEFLNL 190
|
330
....*....|
gi 495962659 387 NEMEKSVALL 396
Cdd:cd03873 191 DDLEKATKVY 200
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
70-200 |
3.31e-07 |
|
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: 50.51 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 70 PKIGFIAHMDTSPDMSGENVKPRIIENYDGSDIILneklnihmgpndfeslnrnigenlivtdgtTLLGADDKAGIAEIM 149
Cdd:cd18669 13 KRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLY------------------------------GRGALDDKGGVAAAL 62
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 495962659 150 TMLETIIQKNL-PHGDIKIAFTPDEEVGRGTDHFNV------KAFDADFAYTVDGGEV 200
Cdd:cd18669 63 EALKLLKENGFkLKGTVVVAFTPDEEVGSGAGKGLLskdaleEDLKVDYLFVGDATPA 120
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
132-176 |
5.23e-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: 48.29 E-value: 5.23e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 495962659 132 DGTTLlGADDKAGIAEIMTMLETiiqKNLPHGDIKIAFTPDEEVG 176
Cdd:cd03890 100 TGTTL-GADNGIGVAYALAILED---KDIEHPPLEVLFTVDEETG 140
|
|
| FrvX |
COG1363 |
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ... |
140-198 |
1.04e-03 |
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Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];
Pssm-ID: 440974 [Multi-domain] Cd Length: 353 Bit Score: 40.88 E-value: 1.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495962659 140 DDKAGIAEIMTMLETIIQKNLPHgDIKIAFTPDEEVG-RGTdHFNVKAFDADFAYTVDGG 198
Cdd:COG1363 179 DDRAGCAVLLELLKALKDEDLPV-TVYFVFTVQEEVGlRGA-STAAYDIKPDEAIAVDVT 236
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| M42_glucanase_like |
cd05657 |
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ... |
140-178 |
1.50e-03 |
|
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1,4-beta-glucanase or endoglucanase)-like subfamily. Proteins in this subfamily are co-catalytic metallopeptidases, found in archaea and bacteria. They show similarity to cellulase and endo-1,4-beta-glucanase (endoglucanase) which typically bind two zinc or cobalt atoms. Some of the enzymes exhibit typical aminopeptidase specificity, whereas others are also capable of N-terminal deblocking activity, i.e. hydrolyzing acylated N-terminal residues. Many of these enzymes are assembled either as tetrahedral dodecamers or as octahedral tetracosameric structures, with the active site located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers.
Pssm-ID: 349907 [Multi-domain] Cd Length: 337 Bit Score: 40.34 E-value: 1.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 495962659 140 DDKAGIAEIMTMLETIIQKNL-PHGDIKIAFTPDEEVGRG 178
Cdd:cd05657 181 DDKASVAILLALARALKENKLkLPVDTHFLFSNYEEVGHG 220
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