|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
1-408 |
0e+00 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 795.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 1 MNNLLDRFFNYVSFDTQSKAGVRQIPSTDGQMKLARALQAELVELGFEQVTLSDHGCVMATLPSNVSWKAPTIGFISHLD 80
Cdd:PRK05469 1 MDKLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDENGYVMATLPANVDKDVPTIGFIAHMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 81 TAPDASGKNVNPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEIVTAMLRLKHN-N 159
Cdd:PRK05469 81 TAPDFSGKNVKPQIIENYDGGDIALGDGNEVLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYLIAHpE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 160 IPHGDIRIAFTPDEEVGKGAQFFDVEAFDAEWAYTVDGGGVGELECENFNAASVTIKIVGNNVHPGTAKGVMVNALSLAA 239
Cdd:PRK05469 161 IKHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALLLAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 240 RIHNELPPEQTPEHTEGYEGFYHLASMKGTVEKAEMHYIVRDFSREGFEARKKNIMDIAKKVGKGLHRdCYIEVTLDDSY 319
Cdd:PRK05469 241 DFHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKYGE-GRVELEIKDQY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 320 YNMRDEVAKHPHIIELAQQAMHDVGIEPIMCPIRGGTDGAQLSFRGLPCPNLFTGGYNFHGKHEFITLEGMEKAVSVIMR 399
Cdd:PRK05469 320 YNMREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVIVE 399
|
....*....
gi 2486361600 400 IAELTALKA 408
Cdd:PRK05469 400 IAELTAERA 408
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
4-403 |
0e+00 |
|
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; tripeptide aminopeptidase; tripeptidase) subfamily. PepT acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349887 [Multi-domain] Cd Length: 400 Bit Score: 695.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 4 LLDRFFNYVSFDTQSKAGVRQIPSTDGQMKLARALQAELVELGFEQVTLSDHGCVMATLPSNVSWKAPTIGFISHLDTAP 83
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDEHGYVTATLPANVDKDVPTIGFIAHMDTAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 84 DASGKNVNPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEIVTAMLRLKHN-NIPH 162
Cdd:cd03892 81 DNSGKNVKPQIIENYDGGDIVLNESGIVLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIEHpEIKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 163 GDIRIAFTPDEEVGKGAQFFDVEAFDAEWAYTVDGGGVGELECENFNAASVTIKIVGNNVHPGTAKGVMVNALSLAARIH 242
Cdd:cd03892 161 GDIRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLAADFH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 243 NELPPEQTPEHTEGYEGFYHLASMKGTVEKAEMHYIVRDFSREGFEARKKNIMDIAKKVGKGLHRDcYIEVTLDDSYYNM 322
Cdd:cd03892 241 SMLPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKYGEG-RVELEIKDQYYNM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 323 RDEVAKHPHIIELAQQAMHDVGIEPIMCPIRGGTDGAQLSFRGLPCPNLFTGGYNFHGKHEFITLEGMEKAVSVIMRIAE 402
Cdd:cd03892 320 KEKIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIVKIAE 399
|
.
gi 2486361600 403 L 403
Cdd:cd03892 400 L 400
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
4-403 |
0e+00 |
|
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: 556.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 4 LLDRFFNYVSFDTQSKAGVRQIPSTDGQMKLARALQAELVELGFEQVTLSDHGCVMATLPSNVSWKAPTIGFISHLDTAP 83
Cdd:cd05645 1 LLERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEKGTLIATLPANVDGDIPAIGFISHVDTSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 84 DASGKNVNPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEIVTAMLRLKHNNIPHG 163
Cdd:cd05645 81 DGSGKNVNPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKNIPHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 164 DIRIAFTPDEEVGKGAQFFDVEAFDAEWAYTVDGGGVGELECENFNAASVTIKIVGNNVHPGTAKGVMVNALSLAARIHN 243
Cdd:cd05645 161 DIEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAARIHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 244 ELPPEQTPEHTEGYEGFYHLASMKGTVEKAEMHYIVRDFSREGFEARKKNIMDIAKKVGKGLHRDCYIEVTLDDSYYNMR 323
Cdd:cd05645 241 EVPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVGKGLHPDCYIELVIEDSYYNFR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 324 DEVAKHPHIIELAQQAMHDVGIEPIMCPIRGGTDGAQLSFRGLPCPNLFTGGYNFHGKHEFITLEGMEKAVSVIMRIAEL 403
Cdd:cd05645 321 EKVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIVRIAEL 400
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
1-405 |
2.27e-177 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 498.42 E-value: 2.27e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 1 MNNLLDRFFNYVSFDTQSKAgvrqipstdgQMKLARALQAELVELGFEqVTLSDHGCVMATLPSNVSWKAPTIGFISHLD 80
Cdd:COG2195 2 PERLLERFLEYVKIPTPSDH----------EEALADYLVEELKELGLE-VEEDEAGNVIATLPATPGYNVPTIGLQAHMD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 81 TAPDASGKNVNPQIvenyRGGdialgigdevlspvmfpvlhqllgqtLITTDGKTLLGADDKAGIAEIVTAMLRLKHNNI 160
Cdd:COG2195 71 TVPQFPGDGIKPQI----DGG--------------------------LITADGTTTLGADDKAGVAAILAALEYLKEPEI 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 161 PHGDIRIAFTPDEEVG-KGAQFFDVEAFDAEWAYTVDGGGVGELECENFNAASVTIKIVGNNVHPGTAKGVMVNALSLAA 239
Cdd:COG2195 121 PHGPIEVLFTPDEEIGlRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIKLAA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 240 RIHNELPPEQTPEHTEGYEGFYHLASM-KGTVEKAEMHYIVRDFSREGFEARKKNIMDIAKKVGKGLHRdCYIEVTLDDS 318
Cdd:COG2195 201 RFLAALPLGRIPEETEGNEGFIHGGSAtNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGV-GVVEVEIEDQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 319 YYNMRDEvaKHPHIIELAQQAMHDVGIEPIMCPIRGGTDGAQLSFRGLPCPNLFTGGYNFHGKHEFITLEGMEKAVSVIM 398
Cdd:COG2195 280 YPNWKPE--PDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWELLV 357
|
....*..
gi 2486361600 399 RIAELTA 405
Cdd:COG2195 358 EILKLIA 364
|
|
| peptidase-T |
TIGR01882 |
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has ... |
3-408 |
7.15e-168 |
|
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: 476.31 E-value: 7.15e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 3 NLLDRFFNYVSFDTQSKAGVRQIPSTDGQMKLARALQAELVELGFEQVT-LSDHGCVMATLPSNVSWKAPTIGFISHLDT 81
Cdd:TIGR01882 4 ELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHyDEKNGYVIATIPSNTDKDVPTIGFLAHVDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 82 ApDASGKNVNPQIVENYRGGD-IALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEIVTAM-LRLKHNN 159
Cdd:TIGR01882 84 A-DFNGENVNPQIIENYDGESiIQLGDLEFTLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAAdYLINHPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 160 IPHGDIRIAFTPDEEVGKGAQFFDVEAFDAEWAYTVDGGGVGELECENFNAASVTIKIVGNNVHPGTAKGVMVNALSLAA 239
Cdd:TIGR01882 163 IKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAAQIAI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 240 RIHNELPPEQTPEHTEGYEGFYHLASMKGTVEKAEMHYIVRDFSREGFEARKKNIMDIAKKVGKGLHRDcYIEVTLDDSY 319
Cdd:TIGR01882 243 DLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEYGQD-RIKLDMNDQY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 320 YNMRDEVAKHPHIIELAQQAMHDVGIEPIMCPIRGGTDGAQLSFRGLPCPNLFTGGYNFHGKHEFITLEGMEKAVSVIMR 399
Cdd:TIGR01882 322 YNMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDVIVE 401
|
....*....
gi 2486361600 400 IAELTALKA 408
Cdd:TIGR01882 402 IAKLNEEQA 410
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
3-405 |
1.10e-165 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 470.56 E-value: 1.10e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 3 NLLDRFFNYVSFDTQSKAGVRQIPSTDGQMKLARALQAELVELGFEQVTLSDHGCVMATLPSNVSwKAPTIGFISHLDTA 82
Cdd:PRK13381 2 QLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDIVIDEHAIVTAKLPGNTP-GAPRIGFIAHLDTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 83 PDASGKNVNPQIVEnYRGGDIAL----GIgdeVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEIVTAMLRLKHN 158
Cdd:PRK13381 81 DVGLSPDIHPQILR-FDGGDLCLnaeqGI---WLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLENLTEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 159 NIPHGDIRIAFTPDEEVG-KGAQFFDVEAFDAEWAYTVDGGGVGELECENFNAASVTIKIVGNNVHPGTAKGVMVNALSL 237
Cdd:PRK13381 157 EVEHGDIVVAFVPDEEIGlRGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNPILM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 238 AARIHNELPPEQTPEHTEGYEGFYHLASMKGTVEKAEMHYIVRDFSREGFEARKKNIMDIAKKVGKgLHRDCYIEVTLDD 317
Cdd:PRK13381 237 ANDFISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINA-KYPTARVSLTLTD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 318 SYYNMRDEVAKHPHIIELAQQAMHDVGIEPIMCPIRGGTDGAQLSFRGLPCPNLFTGGYNFHGKHEFITLEGMEKAVSVI 397
Cdd:PRK13381 316 QYSNISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEVT 395
|
....*...
gi 2486361600 398 MRIAELTA 405
Cdd:PRK13381 396 ITICLLAA 403
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
24-402 |
3.94e-37 |
|
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: 138.53 E-value: 3.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 24 QIPSTDG-QMKLARALQAELVELGFE------QVTLSDHGCVMATLPSNVswKAPTIGFISHLDTAPDASGknVNPQIVE 96
Cdd:TIGR01883 11 QIDSESGkEKAILTYLKKQITKLGIPvsldevPAEVSNDNNLIARLPGTV--KFDTIFFCGHMDTVPPGAG--PEPVVED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 97 NYrggdialgigdevlspvmfpvlhqllgqtlITTDGKTLLGADDKAGIAEIVTAMLRLKHNNIPHGDIRIAFTPDEEVG 176
Cdd:TIGR01883 87 GI------------------------------FTSLGGTILGADDKAGVAAMLEAMDVLSTEETPHGTIEFIFTVKEELG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 177 -KGAQFFDVEAFDAEWAYTVDGGG-VGELECENFNAASVTIKIVGNNVHPGTAKGVMVNALSLAARIHNELPPEQTPEHT 254
Cdd:TIGR01883 137 lIGMRLFDESKITAAYGYCLDAPGeVGNIQLAAPTQVKVDATIAGKDAHAGLVPEDGISAISVARMAIHAMRLGRIDEET 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 255 EGYEGFYHlASMKGTVEKAEMHYIV--RDFSREGFEARKKNIMDIAKKVGKGLHRDCYIEVTLDDSYYNMRDEvakHPHi 332
Cdd:TIGR01883 217 TANIGSFS-GGVNTNIVQDEQLIVAeaRSLSFRKAEAQVQTMRERFEQAAEKYGATLEEETRLIYEGFKIHPQ---HPL- 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 333 IELAQQAMHDVGIEPIMCPIRGGTDGAQLSFRGLPCPNLFTGGYNFHGKHEFITLEGMEKAVSVIMRIAE 402
Cdd:TIGR01883 292 MNIFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETISIEQLVKLAELVIALAE 361
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
4-402 |
2.47e-35 |
|
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: 133.73 E-value: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 4 LLDRFFNYVSFDTQSKAgvrqipstdgQMKLARALQAELVELGFE-------QVTLSDHGCVMATLPSNVSwKAPTIGFI 76
Cdd:cd05683 5 LINTFLELVQIDSETLH----------EKEISKVLKKKFENLGLSvieddagKTTGGGAGNLICTLKADKE-EVPKILFT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 77 SHLDTApdASGKNV-NPQIVENYrggdialgigdevlspvmfpvlhqllgqtlITTDGKTLLGADDKAGIAEIVTAMLRL 155
Cdd:cd05683 74 SHMDTV--TPGINVkPPQIADGY------------------------------IYSDGTTILGADDKAGIAAILEAIRVI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 156 KHNNIPHGDIRIAFTPDEEVG-KGAQFFDVEAFDAEWAYTVDGGG-VGELECENFNAASVTIKIVGNNVHPGTAKGVMVN 233
Cdd:cd05683 122 KEKNIPHGQIQFVITVGEESGlVGAKALDPELIDADYGYALDSEGdVGTIIVGAPTQDKINAKIYGKTAHAGTSPEKGIS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 234 ALSLAARIHNELPPEQTPEHTEGYEGFYHLASMKGTVekAEMHYI---VRDFSREGFEARKKNIMDIAKKVGKGLHrdCY 310
Cdd:cd05683 202 AINIAAKAISNMKLGRIDEETTANIGKFQGGTATNIV--TDEVNIeaeARSLDEEKLDAQVKHMKETFETTAKEKG--AH 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 311 IEVTLDDSYYNMrdEVAKHPHIIELAQQAMHDVGIEPIMCPIRGGTDGAQLSFRGLPCPNLFTGGYNFHGKHEFITLEGM 390
Cdd:cd05683 278 AEVEVETSYPGF--KINEDEEVVKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDL 355
|
410
....*....|..
gi 2486361600 391 EKAVSVIMRIAE 402
Cdd:cd05683 356 YDTAVLVVEIIK 367
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
24-402 |
5.74e-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: 102.27 E-value: 5.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 24 QIPSTDGQ-MKLARALQAELVELGFE---QVTLSDHGCVMATLPSNVSwkAPTIGFISHLDTAP--DASGKNVNPqiven 97
Cdd:COG0624 23 RIPSVSGEeAAAAELLAELLEALGFEverLEVPPGRPNLVARRPGDGG--GPTLLLYGHLDVVPpgDLELWTSDP----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 98 yrggdialgigdevlspvmFPVlhqllgqtliTTDGKTLLG---ADDKAGIAEIVTAMLRLKHNNI-PHGDIRIAFTPDE 173
Cdd:COG0624 96 -------------------FEP----------TIEDGRLYGrgaADMKGGLAAMLAALRALLAAGLrLPGNVTLLFTGDE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 174 EVG-KGAQFF---DVEAFDAEWAYTVDGGGVGELECENFNAASVTIKIVGNNVHPGTAkGVMVNALSLAARIHNELppEQ 249
Cdd:COG0624 147 EVGsPGARALveeLAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAHSSRP-ELGVNAIEALARALAAL--RD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 250 TPEHTEGYEGFYH----LASMKGTV------EKAEMHYIVR---DFSREGFEARkknIMDIAKKVGKGLHrdcyIEVTLD 316
Cdd:COG0624 224 LEFDGRADPLFGRttlnVTGIEGGTavnvipDEAEAKVDIRllpGEDPEEVLAA---LRALLAAAAPGVE----VEVEVL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 317 DSYYN-MrdEVAKHPHIIELAQQAMHDV-GIEPIMCPIRGGTDGAQLSfRGLPCPNL---FTGGYNFHGKHEFITLEGME 391
Cdd:COG0624 297 GDGRPpF--ETPPDSPLVAAARAAIREVtGKEPVLSGVGGGTDARFFA-EALGIPTVvfgPGDGAGAHAPDEYVELDDLE 373
|
410
....*....|.
gi 2486361600 392 KAVSVIMRIAE 402
Cdd:COG0624 374 KGARVLARLLE 384
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
139-402 |
1.50e-19 |
|
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 88.56 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 139 ADDKAGIAEIVTAMLRLKHNNIPHGDIRIAFTPDEEVGKG-----AQFFDVEAFDAEWAYTVDGG------GVGELECEN 207
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEGLKKGTVKLLFQPDEEGGMGgaralIEDGLLEREKVDAVFGLHIGeptlleGGIAIGVVT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 208 FNAAS--VTIKIVGNNVH---PGTAKGVMVNALSLAARIHNELPPEQTPEHTEGYEgFYHLASMKGTV----EKAEMHYI 278
Cdd:pfam01546 113 GHRGSlrFRVTVKGKGGHastPHLGVNAIVAAARLILALQDIVSRNVDPLDPAVVT-VGNITGIPGGVnvipGEAELKGD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 279 VRDFSREGFEARKKNIMDIAKKVGKglHRDCYIEVTLDDSYYNMrdeVAKHPHIIELAQQAMHDVG---IEPIMCPIRGG 355
Cdd:pfam01546 192 IRLLPGEDLEELEERIREILEAIAA--AYGVKVEVEYVEGGAPP---LVNDSPLVAALREAAKELFglkVELIVSGSMGG 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2486361600 356 TDGAQLSFRGLPCPNLF-TGGYNFHGKHEFITLEGMEKAVSVIMRIAE 402
Cdd:pfam01546 267 TDAAFFLLGVPPTVVFFgPGSGLAHSPNEYVDLDDLEKGAKVLARLLL 314
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
24-401 |
1.32e-14 |
|
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.
Pssm-ID: 349944 [Multi-domain] Cd Length: 361 Bit Score: 74.64 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 24 QIPSTDGQMKLARALQAELVE---LGFEQVTLSDHGCVMATLPSNvswKAPTIGFISHLDTapdasgknVNPQIVENYRG 100
Cdd:cd08659 8 QIPSVNPPEAEVAEYLAELLAkrgYGIESTIVEGRGNLVATVGGG---DGPVLLLNGHIDT--------VPPGDGDKWSF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 101 GDIALGIGDEVLspvmfpvlhqlLGqtlittdgktlLGADD-KAGIAEIVTAMLRLKHNNIPH-GDIRIAFTPDEEVGK- 177
Cdd:cd08659 77 PPFSGRIRDGRL-----------YG-----------RGACDmKGGLAAMVAALIELKEAGALLgGRVALLATVDEEVGSd 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 178 GAQFFDveafDAEWAYTVDGGGVGE-LECENFNAA----SVTIKIVGNNVH---PGTAkgvmVNALSLAARIHNEL---- 245
Cdd:cd08659 135 GARALL----EAGYADRLDALIVGEpTGLDVVYAHkgslWLRVTVHGKAAHssmPELG----VNAIYALADFLAELrtlf 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 246 -PPEQTPEHTegyeGFYHLASM-KGTVE------KAEMHYIVR---DFSREGFEARkknIMDIAKKVGKGLHrdcyIEVT 314
Cdd:cd08659 207 eELPAHPLLG----PPTLNVGViNGGTQvnsipdEATLRVDIRlvpGETNEGVIAR---LEAILEEHEAKLT----VEVS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 315 LDDSYYNMRDEvaKHPhIIELAQQAMHDVGIEPIMCPIRGGTDGAQLSfRGLPCPNLFTGGYNFHGKH---EFITLEGME 391
Cdd:cd08659 276 LDGDPPFFTDP--DHP-LVQALQAAARALGGDPVVRPFTGTTDASYFA-KDLGFPVVVYGPGDLALAHqpdEYVSLEDLL 351
|
410
....*....|
gi 2486361600 392 KAVSVIMRIA 401
Cdd:cd08659 352 RAAEIYKEII 361
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
57-397 |
4.18e-12 |
|
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: 64.75 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 57 CVMATLPSNVswKAPTIGFISHLDTAPDASGKNVNPQIVEnyrggdialgigdevlspvmfpvlhqllgQTLITTDGKTL 136
Cdd:cd03873 1 NLIARLGGGE--GGKSVALGAHLDVVPAGEGDNRDPPFAE-----------------------------DTEEEGRLYGR 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 137 LGADDKAGIAEIVTAMLRLK-HNNIPHGDIRIAFTPDEEVGKGAQFFDVEAFDAEWAYTVDGGGVGELECENFNAASVTI 215
Cdd:cd03873 50 GALDDKGGVAAALEALKRLKeNGFKPKGTIVVAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDATAGPILQKGVVI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 216 KIVgnnvhpgtakgvmvnalslaarihnelppeqtpehtegyegfyhlasmkgtvekaemhyivrdfsregfearkknIM 295
Cdd:cd03873 130 RNP---------------------------------------------------------------------------LV 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 296 DIAKKVgkglHRDCYIEVTLDDsyynmrdevakhphiielaqqamhdvgiepimcPIRGGTDGAQLSFRGLPCPNLFTGG 375
Cdd:cd03873 135 DALRKA----AREVGGKPQRAS---------------------------------VIGGGTDGRLFAELGIPGVTLGPPG 177
|
330 340
....*....|....*....|...
gi 2486361600 376 -YNFHGKHEFITLEGMEKAVSVI 397
Cdd:cd03873 178 dKGAHSPNEFLNLDDLEKATKVY 200
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
206-309 |
2.37e-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: 60.05 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 206 ENFNAASVTIKIVGNNVHPGtAKGVMVNALSLAARIHNELP----------PEQTPEHTEGYEGFyhlaSMKGTVEKAEM 275
Cdd:pfam07687 2 GHKGLAGGHLTVKGKAGHSG-APGKGVNAIKLLARLLAELPaeygdigfdfPRTTLNITGIEGGT----ATNVIPAEAEA 76
|
90 100 110
....*....|....*....|....*....|....
gi 2486361600 276 HYIVRdfsREGFEARKKNIMDIAKKVGKGLHRDC 309
Cdd:pfam07687 77 KFDIR---LLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
57-200 |
4.61e-11 |
|
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 61.68 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 57 CVMATLPSNVSwkAPTIGFISHLDTAPDASGKNVNPQIVEnyrggdialgigdevlspvmfpvlhqllgQTLITTDGKTL 136
Cdd:cd18669 1 NVIARYGGGGG--GKRVLLGAHIDVVPAGEGDPRDPPFFV-----------------------------DTVEEGRLYGR 49
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486361600 137 LGADDKAGIAEIVTAMLRLK-HNNIPHGDIRIAFTPDEEVGKGA------QFFDVEAFDAEWAYTVDGGGV 200
Cdd:cd18669 50 GALDDKGGVAAALEALKLLKeNGFKLKGTVVVAFTPDEEVGSGAgkgllsKDALEEDLKVDYLFVGDATPA 120
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
139-402 |
2.23e-09 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 58.85 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 139 ADDKAGIAEIVTAMLRLKhnniPHGDIRI--AFTPDEEV-GKGA-QFFDVEAFDAEWAYTVDGGGVgelecENFNAAS-- 212
Cdd:PRK08651 113 SDMKGGIAALLAAFERLD----PAGDGNIelAIVPDEETgGTGTgYLVEEGKVTPDYVIVGEPSGL-----DNICIGHrg 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 213 ---VTIKIVGNNVHPGTAKgVMVNALSLAARIHNEL--------PPEQTPEHTEGYEgfyHLASMKGTVEKAEMHYIVRD 281
Cdd:PRK08651 184 lvwGVVKVYGKQAHASTPW-LGINAFEAAAKIAERLksslstikSKYEYDDERGAKP---TVTLGGPTVEGGTKTNIVPG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 282 F-------------SREGFEARKKNIMD-IAKKVGkglhrdcyIEVTLDDSYY---NMRDEVAKhphIIELAQQAMHDV- 343
Cdd:PRK08651 260 YcafsidrrlipeeTAEEVRDELEALLDeVAPELG--------IEVEFEITPFseaFVTDPDSE---LVKALREAIREVl 328
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 344 GIEPIMCPIRGGTDGAQLSFRGLPCPNLFTGGY-NFHGKHEFITLEGMEKAVSVIMRIAE 402
Cdd:PRK08651 329 GVEPKKTISLGGTDARFFGAKGIPTVVYGPGELeLAHAPDEYVEVKDVEKAAKVYEEVLK 388
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
138-402 |
1.44e-07 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 52.84 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 138 GADD-KAGIAEIVTAMLRLKHNNiPHGDIRIAFTPDEEV-GKGAQFFdVEAFDAEWAYTVDGGGvGELECENFNAASVTI 215
Cdd:PRK08652 84 GACDaKGGVAAILLALEELGKEF-EDLNVGIAFVSDEEEgGRGSALF-AERYRPKMAIVLEPTD-LKVAIAHYGNLEAYV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 216 KIVGNNVHpGTAKGVMVNALSLAARIHNELPpEQTPEHTEGYEGFYHLASMKGTVEkaemHYIVRDFSREGFEAR---KK 292
Cdd:PRK08652 161 EVKGKPSH-GACPESGVNAIEKAFEMLEKLK-ELLKALGKYFDPHIGIQEIIGGSP----EYSIPALCRLRLDARippEV 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 293 NIMDIAKKVGK-----GLHrdcYIEVTLDDSYYNMRDEvakhpHIIELAQQAMHDVGIEPIMCPIRGGTDGAQLSFRGLP 367
Cdd:PRK08652 235 EVEDVLDEIDPildeyTVK---YEYTEIWDGFELDEDE-----EIVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTK 306
|
250 260 270
....*....|....*....|....*....|....*...
gi 2486361600 368 cPNLFTGGyNF---HGKHEFITLEGMEKAVSVIMRIAE 402
Cdd:PRK08652 307 -TVVWGPG-ELdlcHTKFERIDVREVEKAKEFLKALNE 342
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
29-406 |
2.74e-06 |
|
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: 49.13 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 29 DGQMKLARALQAELVELGF--EQVTLSDHG-CVMATLPSnvsWKAPTIGFISHLDTapdasgknvnpqivenyrggdial 105
Cdd:cd03885 19 EGVDRVAELLAEELEALGFtvERRPLGEFGdHLIATFKG---TGGKRVLLIGHMDT------------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 106 gigdevlspvMFPvlHQLLGQTLITTDGKTLLG---ADDKAGIAEIVTAMLRLKHNN-IPHGDIRIAFTPDEEVGK--GA 179
Cdd:cd03885 72 ----------VFP--EGTLAFRPFTVDGDRAYGpgvADMKGGLVVILHALKALKAAGgRDYLPITVLLNSDEEIGSpgSR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 180 QFFDVEAFDAEWAYTVDGGGV-GELECENFNAASVTIKIVGNNVHPGTA--KGvmVNALSLAARIHNELppeqtpEHTEG 256
Cdd:cd03885 140 ELIEEEAKGADYVLVFEPARAdGNLVTARKGIGRFRLTVKGRAAHAGNApeKG--RSAIYELAHQVLAL------HALTD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 257 YEgfyhlasmKGTV----------------EKAEMHYIVRDFSREGFEARKKnimDIAKKVGKGLHRDCYIEVTLDDSyy 320
Cdd:cd03885 212 PE--------KGTTvnvgvisggtrvnvvpDHAEAQVDVRFATAEEADRVEE---ALRAIVATTLVPGTSVELTGGLN-- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 321 nmRDEVAKHPHIIEL---AQQAMHDVGIEPIMCPIRGGTDGAQLSFRGLP------CPnlftgGYNFHGKHEFITLEgme 391
Cdd:cd03885 279 --RPPMEETPASRRLlarAQEIAAELGLTLDWEATGGGSDANFTAALGVPtldglgPV-----GGGAHTEDEYLELD--- 348
|
410
....*....|....*
gi 2486361600 392 kavSVIMRIAELTAL 406
Cdd:cd03885 349 ---SLVPRIKLLARL 360
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
12-402 |
3.88e-06 |
|
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349889 [Multi-domain] Cd Length: 367 Bit Score: 48.36 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 12 VSFDTQSKAGvrqipstdgQMKLARALQAELVELGFE----QVTLSDHGCVMATLPSNVswkAPTIGFISHLDTAPDASG 87
Cdd:cd03894 7 VAFDTVSRNS---------NLALIEYVADYLAALGVKsrrvPVPEGGKANLLATLGPGG---EGGLLLSGHTDVVPVDGQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 88 K-NVNPqivenyrggdialgigdevlspvmFpvlhqllgqTLITTDGKtLLG---ADDKAGIAEIVTAMLRLKHNNiPHG 163
Cdd:cd03894 75 KwSSDP------------------------F---------TLTERDGR-LYGrgtCDMKGFLAAVLAAVPRLLAAK-LRK 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 164 DIRIAFTPDEEVG-KGAQFFdVEAFdAEWAYTVDGGGVGE-LECENFNA----ASVTIKIVGNNVH-PGTAKGVmvNALS 236
Cdd:cd03894 120 PLHLAFSYDEEVGcLGVRHL-IAAL-AARGGRPDAAIVGEpTSLQPVVAhkgiASYRIRVRGRAAHsSLPPLGV--NAIE 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 237 LAARIHNELPPEQTP----EHTEGYEGFY---HLASMKG-----TV-EKAEMHYIVRDFSREGFEARKKNIMDIAKKVGk 303
Cdd:cd03894 196 AAARLIGKLRELADRlapgLRDPPFDPPYptlNVGLIHGgnavnIVpAECEFEFEFRPLPGEDPEAIDARLRDYAEALL- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 304 gLHRDCYIEVTLDDSY--YNMRDEVAkhphIIELAQQAMHDVGIEPImcpiRGGTDGAQLSFRGLPCPNLFTGGYN-FHG 380
Cdd:cd03894 275 -EFPEAGIEVEPLFEVpgLETDEDAP----LVRLAAALAGDNKVRTV----AYGTEAGLFQRAGIPTVVCGPGSIAqAHT 345
|
410 420
....*....|....*....|..
gi 2486361600 381 KHEFITLEGMEKAVSVIMRIAE 402
Cdd:cd03894 346 PDEFVELEQLDRCEEFLRRLIA 367
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
129-300 |
8.55e-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: 47.90 E-value: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 129 ITTDGKTLlGADDKAGIAeivTAMLRLKHNNIPHGDIRIAFTPDEEVGK-GAQFFDVEAFDAEWAYTVDG---------- 197
Cdd:cd03890 97 LKATGTTL-GADNGIGVA---YALAILEDKDIEHPPLEVLFTVDEETGMtGALGLDPSLLKGKILLNLDSeeegeltvgc 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 198 -GGVG-----ELECENFNAASVTIKIV---------GNNVHPGTAkgvmvNALSLAARIHNELPPEQTpehtegyegfYH 262
Cdd:cd03890 173 aGGIDvtitlPIEREEAEGGYTGLKITvkglkgghsGVDIHKGRA-----NANKLMARLLYELAKELD----------FR 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2486361600 263 LASMKGTV------EKAEMHYIVRDFSREGFEARKKNIMDIAKK 300
Cdd:cd03890 238 LVSINGGTkrnaipREAVAVIAVPAEDVEALKKLIKKLEKALKA 281
|
|
| M42_glucanase_like |
cd05657 |
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ... |
24-202 |
1.78e-05 |
|
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: 46.50 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 24 QIPSTDGQMKLARA-LQAELVELGFEqVTLSDHGCVMATLPSNVSWKAPTIgfISHLDT--------------------- 81
Cdd:cd05657 11 AIPSPTGYTDEAVRyLKKELEGLGVE-TELTNKGALIATIPGKDSRKARAL--SAHVDTlgaivkeikpdgrlrltpigg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 82 --APDASGKNVN--PQIVENYRG------------GDI--------------------------ALGI--GDEVlspVMF 117
Cdd:cd05657 88 faWNSAEGENVTiiTRDGKTYTGtvlplkasvhvyGDApeaqertwdnmevrldekvkskedvlALGIrvGDFV---AFD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 118 PvlhqllgQTLITTDG----KTLlgaDDKAGIAEIVTAMLRLKHNNI-PHGDIRIAFTPDEEVGKGAQFFDVEAFDAEWA 192
Cdd:cd05657 165 P-------RPEVTESGfiksRHL---DDKASVAILLALARALKENKLkLPVDTHFLFSNYEEVGHGASFAPPEDTDELLA 234
|
250
....*....|
gi 2486361600 193 ytVDGGGVGE 202
Cdd:cd05657 235 --VDMGPVGP 242
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
132-361 |
5.22e-05 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 44.87 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 132 DGKtLLG---ADDKAGIAEIVTAMLRLKHNN-IPHGDIRIAFTPDEEVGK-GAQFFdveaFDAEWAYTVDGGGVGELECE 206
Cdd:PRK08588 90 DGK-LYGrgaTDMKSGLAALVIAMIELKEQGqLLNGTIRLLATAGEEVGElGAKQL----TEKGYADDLDALIIGEPSGH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 207 NFNAA---SVTIKIV--GNNVHPGT-AKGvmVNALSLAARIHNELPP--EQTPEHTEGYEGFYHLAS-MKG-----TV-E 271
Cdd:PRK08588 165 GIVYAhkgSMDYKVTstGKAAHSSMpELG--VNAIDPLLEFYNEQKEyfDSIKKHNPYLGGLTHVVTiINGgeqvnSVpD 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 272 KAEMHYIVRDFSREGFEARKKNIMDIAKKVGKGLHRDCYIEVTLDdsyynmRDEVAKHPH--IIELAQ-QAMHDVGIEPI 348
Cdd:PRK08588 243 EAELEFNIRTIPEYDNDQVISLLQEIINEVNQNGAAQLSLDIYSN------HRPVASDKDskLVQLAKdVAKSYVGQDIP 316
|
250
....*....|...
gi 2486361600 349 MCPIRGGTDGAQL 361
Cdd:PRK08588 317 LSAIPGATDASSF 329
|
|
| FrvX |
COG1363 |
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ... |
104-201 |
1.64e-04 |
|
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];
Pssm-ID: 440974 [Multi-domain] Cd Length: 353 Bit Score: 43.58 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486361600 104 ALGI--GDEVlspVMFPVLHQLLGQTLITtdGKTLlgaDDKAGIAEIVTAMLRLKHNNIPHgDIRIAFTPDEEVG-KGAQ 180
Cdd:COG1363 149 ALGIrvGDFV---VFDPEFEELTNSGFIK--SKAL---DDRAGCAVLLELLKALKDEDLPV-TVYFVFTVQEEVGlRGAS 219
|
90 100
....*....|....*....|.
gi 2486361600 181 FFdVEAFDAEWAYTVDGGGVG 201
Cdd:COG1363 220 TA-AYDIKPDEAIAVDVTPAG 239
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
139-204 |
1.06e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 41.14 E-value: 1.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486361600 139 ADDKAGIAEIVTAMLRLKHNNI-PHGDIRIAFTPDEEVGKGAQFFDV-----EAFDAEWAYTvDGGGvGELE 204
Cdd:PRK09133 140 SDDKADAAIWVATLIRLKREGFkPKRDIILALTGDEEGTPMNGVAWLaenhrDLIDAEFALN-EGGG-GTLD 209
|
|
| |
