|
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: 803.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 1 MDKLLERFLNYVSLDTQSKAGVRQVPSTEGQWKLLHLLKEQLEEMGLINVTLSEKGTLMATLPANVPGDIPAIGFISHVD 80
Cdd:PRK05469 1 MDKLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDENGYVMATLPANVDKDVPTIGFIAHMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 81 TSPDCSGKNVNPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEIMTALAVLQQ-KN 159
Cdd:PRK05469 81 TAPDFSGKNVKPQIIENYDGGDIALGDGNEVLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYLIAhPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 160 IPHGDIRVAFTPDEEVGKGAKHFDVDAFDARWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVMVNALSLAA 239
Cdd:PRK05469 161 IKHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALLLAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 240 RIHAEVPADESPEMTEGYEGFYHLASMKGTVDRADMHYIIRDFDRKQFEARKRKMMEIAKKVGKGLhPDCYIELVIEDSY 319
Cdd:PRK05469 241 DFHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKY-GEGRVELEIKDQY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 320 YNMREKVVEHPHILDIAQQAMRDCDIEPELKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTLEGMEKAVQVIVR 399
Cdd:PRK05469 320 YNMREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVIVE 399
|
....*....
gi 446281586 400 IAELTAQRK 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: 734.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 4 LLERFLNYVSLDTQSKAGVRQVPSTEGQWKLLHLLKEQLEEMGLINVTLSEKGTLMATLPANVPGDIPAIGFISHVDTSP 83
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDEHGYVTATLPANVDKDVPTIGFIAHMDTAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 84 DCSGKNVNPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEIMTALAVLQQK-NIPH 162
Cdd:cd03892 81 DNSGKNVKPQIIENYDGGDIVLNESGIVLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIEHpEIKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 163 GDIRVAFTPDEEVGKGAKHFDVDAFDARWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVMVNALSLAARIH 242
Cdd:cd03892 161 GDIRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLAADFH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 243 AEVPADESPEMTEGYEGFYHLASMKGTVDRADMHYIIRDFDRKQFEARKRKMMEIAKKVGKGLhPDCYIELVIEDSYYNM 322
Cdd:cd03892 241 SMLPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKY-GEGRVELEIKDQYYNM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 323 REKVVEHPHILDIAQQAMRDCDIEPELKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTLEGMEKAVQVIVRIAE 402
Cdd:cd03892 320 KEKIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIVKIAE 399
|
.
gi 446281586 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: 652.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 4 LLERFLNYVSLDTQSKAGVRQVPSTEGQWKLLHLLKEQLEEMGLINVTLSEKGTLMATLPANVPGDIPAIGFISHVDTSP 83
Cdd:cd05645 1 LLERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEKGTLIATLPANVDGDIPAIGFISHVDTSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 84 DCSGKNVNPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEIMTALAVLQQKNIPHG 163
Cdd:cd05645 81 DGSGKNVNPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKNIPHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 164 DIRVAFTPDEEVGKGAKHFDVDAFDARWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVMVNALSLAARIHA 243
Cdd:cd05645 161 DIEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAARIHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 244 EVPADESPEMTEGYEGFYHLASMKGTVDRADMHYIIRDFDRKQFEARKRKMMEIAKKVGKGLHPDCYIELVIEDSYYNMR 323
Cdd:cd05645 241 EVPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVGKGLHPDCYIELVIEDSYYNFR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 324 EKVVEHPHILDIAQQAMRDCDIEPELKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTLEGMEKAVQVIVRIAEL 403
Cdd:cd05645 321 EKVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIVRIAEL 400
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
1-405 |
0e+00 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 507.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 1 MDKLLERFLNYVSLDTQSKAgvrqvpstegQWKLLHLLKEQLEEMGLiNVTLSEKGTLMATLPANVPGDIPAIGFISHVD 80
Cdd:COG2195 2 PERLLERFLEYVKIPTPSDH----------EEALADYLVEELKELGL-EVEEDEAGNVIATLPATPGYNVPTIGLQAHMD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 81 TSPDCSGKNVNPQIvenyRGGdialgigdevlspvmfpvlhqllgqtLITTDGKTLLGADDKAGIAEIMTALAVLQQKNI 160
Cdd:COG2195 71 TVPQFPGDGIKPQI----DGG--------------------------LITADGTTTLGADDKAGVAAILAALEYLKEPEI 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 161 PHGDIRVAFTPDEEVG-KGAKHFDVDAFDARWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVMVNALSLAA 239
Cdd:COG2195 121 PHGPIEVLFTPDEEIGlRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIKLAA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 240 RIHAEVPADESPEMTEGYEGFYHLASM-KGTVDRADMHYIIRDFDRKQFEARKRKMMEIAKKVGKGlHPDCYIELVIEDS 318
Cdd:COG2195 201 RFLAALPLGRIPEETEGNEGFIHGGSAtNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAK-YGVGVVEVEIEDQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 319 YYNMREKvvEHPHILDIAQQAMRDCDIEPELKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTLEGMEKAVQVIV 398
Cdd:COG2195 280 YPNWKPE--PDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWELLV 357
|
....*..
gi 446281586 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 ... |
2-407 |
4.71e-170 |
|
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: 482.09 E-value: 4.71e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 2 DKLLERFLNYVSLDTQSKAGVRQVPSTEGQWKLLHLLKEQLEEMGLINVTLSEK-GTLMATLPANVPGDIPAIGFISHVD 80
Cdd:TIGR01882 3 EELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEKnGYVIATIPSNTDKDVPTIGFLAHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 81 TSpDCSGKNVNPQIVENYRGGD-IALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEIMTALA-VLQQK 158
Cdd:TIGR01882 83 TA-DFNGENVNPQIIENYDGESiIQLGDLEFTLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAADyLINHP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 159 NIPHGDIRVAFTPDEEVGKGAKHFDVDAFDARWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVMVNALSLA 238
Cdd:TIGR01882 162 EIKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAAQIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 239 ARIHAEVPADESPEMTEGYEGFYHLASMKGTVDRADMHYIIRDFDRKQFEARKRKMMEIAKKVGKGLHPDcYIELVIEDS 318
Cdd:TIGR01882 242 IDLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEYGQD-RIKLDMNDQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 319 YYNMREKVVEHPHILDIAQQAMRDCDIEPELKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTLEGMEKAVQVIV 398
Cdd:TIGR01882 321 YYNMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDVIV 400
|
....*....
gi 446281586 399 RIAELTAQR 407
Cdd:TIGR01882 401 EIAKLNEEQ 409
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
2-406 |
9.38e-168 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 475.95 E-value: 9.38e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 2 DKLLERFLNYVSLDTQSKAGVRQVPSTEGQWKLLHLLKEQLEEMGLINVTLSEKGTLMATLPANVPgDIPAIGFISHVDT 81
Cdd:PRK13381 1 MQLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDIVIDEHAIVTAKLPGNTP-GAPRIGFIAHLDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 82 SPDCSGKNVNPQIVEnYRGGDIAL----GIgdeVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGIAEIMTALAVLQQ 157
Cdd:PRK13381 80 VDVGLSPDIHPQILR-FDGGDLCLnaeqGI---WLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLENLTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 158 KNIPHGDIRVAFTPDEEVG-KGAKHFDVDAFDARWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVMVNALS 236
Cdd:PRK13381 156 NEVEHGDIVVAFVPDEEIGlRGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNPIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 237 LAARIHAEVPADESPEMTEGYEGFYHLASMKGTVDRADMHYIIRDFDRKQFEARKRKMMEIAKKVGKgLHPDCYIELVIE 316
Cdd:PRK13381 236 MANDFISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINA-KYPTARVSLTLT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 317 DSYYNMREKVVEHPHILDIAQQAMRDCDIEPELKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTLEGMEKAVQV 396
Cdd:PRK13381 315 DQYSNISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEV 394
|
410
....*....|
gi 446281586 397 IVRIAELTAQ 406
Cdd:PRK13381 395 TITICLLAAK 404
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
2-402 |
1.59e-44 |
|
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: 158.38 E-value: 1.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 2 DKLLERFLNYVSLDTQSKagvrqvpsTEGQwkLLHLLKEQLEEMGL-------INVTLSEKGTLMATLPANVPGdIPAIG 74
Cdd:cd05683 3 DRLINTFLELVQIDSETL--------HEKE--ISKVLKKKFENLGLsvieddaGKTTGGGAGNLICTLKADKEE-VPKIL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 75 FISHVDT-SPdcsGKNV-NPQIVENYrggdialgigdevlspvmfpvlhqllgqtlITTDGKTLLGADDKAGIAEIMTAL 152
Cdd:cd05683 72 FTSHMDTvTP---GINVkPPQIADGY------------------------------IYSDGTTILGADDKAGIAAILEAI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 153 AVLQQKNIPHGDIRVAFTPDEEVG-KGAKHFDVDAFDARWAYTVDGGG-VGELEFENFNAASVNIKIVGNNVHPGTAKGV 230
Cdd:cd05683 119 RVIKEKNIPHGQIQFVITVGEESGlVGAKALDPELIDADYGYALDSEGdVGTIIVGAPTQDKINAKIYGKTAHAGTSPEK 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 231 MVNALSLAARIHAEVPADESPEMTEGYEGFYHLASMKGTVdrADMHYII---RDFDRKQFEARKRKMMEIAKKVGKGLHp 307
Cdd:cd05683 199 GISAINIAAKAISNMKLGRIDEETTANIGKFQGGTATNIV--TDEVNIEaeaRSLDEEKLDAQVKHMKETFETTAKEKG- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 308 dCYIELVIEDSYYNMreKVVEHPHILDIAQQAMRDCDIEPELKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTL 387
Cdd:cd05683 276 -AHAEVEVETSYPGF--KINEDEEVVKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPI 352
|
410
....*....|....*
gi 446281586 388 EGMEKAVQVIVRIAE 402
Cdd:cd05683 353 EDLYDTAVLVVEIIK 367
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
3-402 |
2.00e-38 |
|
peptidase T-like protein; This model represents a clade of enzymes closely related to Peptidase T, an aminotripeptidase found in bacteria. This clade consists of gram positive bacteria of which several additionally contain a Peptidase T gene.
Pssm-ID: 162579 [Multi-domain] Cd Length: 361 Bit Score: 142.00 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 3 KLLERFLNYVSLDTQSKAgvrqvpstegQWKLLHLLKEQLEEMGL------INVTLSEKGTLMATLPANVpgDIPAIGFI 76
Cdd:TIGR01883 1 RLKKYFLELIQIDSESGK----------EKAILTYLKKQITKLGIpvsldeVPAEVSNDNNLIARLPGTV--KFDTIFFC 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 77 SHVDTSPDcsGKNVNPQIVENYrggdialgigdevlspvmfpvlhqllgqtlITTDGKTLLGADDKAGIAEIMTALAVLQ 156
Cdd:TIGR01883 69 GHMDTVPP--GAGPEPVVEDGI------------------------------FTSLGGTILGADDKAGVAAMLEAMDVLS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 157 QKNIPHGDIRVAFTPDEEVG-KGAKHFDVDAFDARWAYTVDGGG-VGELEFENFNAASVNIKIVGNNVHPGTAKGVMVNA 234
Cdd:TIGR01883 117 TEETPHGTIEFIFTVKEELGlIGMRLFDESKITAAYGYCLDAPGeVGNIQLAAPTQVKVDATIAGKDAHAGLVPEDGISA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 235 LSLAAR-IHAEVPADESPEMTEGYEGFYHLASMKGTVDRADMHYIIRDFDRKQFEARKRKMME----IAKKVGKGLHPDc 309
Cdd:TIGR01883 197 ISVARMaIHAMRLGRIDEETTANIGSFSGGVNTNIVQDEQLIVAEARSLSFRKAEAQVQTMRErfeqAAEKYGATLEEE- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 310 yIELVIEDsyYNMREkvvEHPHIlDIAQQAMRDCDIEPELKPIRGGTDGAQLSFMGLPCPNLFTGGYNYHGKHEFVTLEG 389
Cdd:TIGR01883 276 -TRLIYEG--FKIHP---QHPLM-NIFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETISIEQ 348
|
410
....*....|...
gi 446281586 390 MEKAVQVIVRIAE 402
Cdd:TIGR01883 349 LVKLAELVIALAE 361
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
139-402 |
2.34e-19 |
|
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 87.79 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 139 ADDKAGIAEIMTALAVLQQKNIPHGDIRVAFTPDEEVGK-GAKHF------DVDAFDARWAYTVDGGGVGELEFE----N 207
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEGLKKGTVKLLFQPDEEGGMgGARALiedgllEREKVDAVFGLHIGEPTLLEGGIAigvvT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 208 FNAAS--VNIKIVGNNVHpGTAKGVMVNALSLAARIHAEVPADESPEMTEGYEG---FYHLASMKGTV----DRADMHYI 278
Cdd:pfam01546 113 GHRGSlrFRVTVKGKGGH-ASTPHLGVNAIVAAARLILALQDIVSRNVDPLDPAvvtVGNITGIPGGVnvipGEAELKGD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 279 IRDFDRKQFEARKRKMMEIAKKVGKGLhpDCYIELVIEDSYYNMrekVVEHPHILDIAQQAMRD---CDIEPELKPIRGG 355
Cdd:pfam01546 192 IRLLPGEDLEELEERIREILEAIAAAY--GVKVEVEYVEGGAPP---LVNDSPLVAALREAAKElfgLKVELIVSGSMGG 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446281586 356 TDGAqlsFMGLPCPNLF----TGGYNYHGKHEFVTLEGMEKAVQVIVRIAE 402
Cdd:pfam01546 267 TDAA---FFLLGVPPTVvffgPGSGLAHSPNEYVDLDDLEKGAKVLARLLL 314
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
24-402 |
8.12e-19 |
|
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: 87.25 E-value: 8.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 24 QVPSTEGQ-WKLLHLLKEQLEEMGlINVTLSE----KGTLMATLPANVPGdiPAIGFISHVDTSP--DCSGKNVNPqive 96
Cdd:COG0624 23 RIPSVSGEeAAAAELLAELLEALG-FEVERLEvppgRPNLVARRPGDGGG--PTLLLYGHLDVVPpgDLELWTSDP---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 97 nyrggdialgigdevlspvmFPVlhqllgqtliTTDGKTLLG---ADDKAGIAEIMTALAVLQQKNI-PHGDIRVAFTPD 172
Cdd:COG0624 96 --------------------FEP----------TIEDGRLYGrgaADMKGGLAAMLAALRALLAAGLrLPGNVTLLFTGD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 173 EEVG-KGAKHF---DVDAFDARWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAkGVMVNALSLAARIHAEVPAD 248
Cdd:COG0624 146 EEVGsPGARALveeLAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAHSSRP-ELGVNAIEALARALAALRDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 249 ESPEMTEGYEGF--YHLASMKGTV------DRADMHYIIR---DFDRKQFEARkrkMMEIAKKVGKGLHpdcyIEL-VIE 316
Cdd:COG0624 225 EFDGRADPLFGRttLNVTGIEGGTavnvipDEAEAKVDIRllpGEDPEEVLAA---LRALLAAAAPGVE----VEVeVLG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 317 DSYYNMREKvVEHPhILDIAQQAMRD-CDIEPELKPIRGGTDGAQLS-FMGLPCPNL-FTGGYNYHGKHEFVTLEGMEKA 393
Cdd:COG0624 298 DGRPPFETP-PDSP-LVAAARAAIREvTGKEPVLSGVGGGTDARFFAeALGIPTVVFgPGDGAGAHAPDEYVELDDLEKG 375
|
....*....
gi 446281586 394 VQVIVRIAE 402
Cdd:COG0624 376 ARVLARLLE 384
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
57-397 |
2.21e-14 |
|
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: 71.30 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 57 TLMATLPANvpGDIPAIGFISHVDTSPDCSGKNVNPQIVEnyrggdialgigdevlspvmfpvlhqllgQTLITTDGKTL 136
Cdd:cd03873 1 NLIARLGGG--EGGKSVALGAHLDVVPAGEGDNRDPPFAE-----------------------------DTEEEGRLYGR 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 137 LGADDKAGIAEIMTALAVLQQKN-IPHGDIRVAFTPDEEVGKGAKHFDVDAFDARWAYTVDGGGVGELEFENFNAASVNI 215
Cdd:cd03873 50 GALDDKGGVAAALEALKRLKENGfKPKGTIVVAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDATAGPILQKGVVI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 216 KIVgnnvhpgtakgvmvnalslaarihaevpadespemtegyegfyhlasmkgtvdradmhyiirdfdrkqfearkrkmm 295
Cdd:cd03873 130 RNP----------------------------------------------------------------------------- 132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 296 eiakkvgkglhpdcyielviedsyynmrekvvehphILDIAQQAMRDCDIEP-ELKPIRGGTDGAQLSFMGLPCPNLFTG 374
Cdd:cd03873 133 ------------------------------------LVDALRKAAREVGGKPqRASVIGGGTDGRLFAELGIPGVTLGPP 176
|
330 340
....*....|....*....|....
gi 446281586 375 G-YNYHGKHEFVTLEGMEKAVQVI 397
Cdd:cd03873 177 GdKGAHSPNEFLNLDDLEKATKVY 200
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
36-401 |
2.76e-13 |
|
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: 70.41 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 36 HLLKEQLEEMGL-INVTLSE-KGTLMATLPanvPGDIPAIGFISHVDTspdcsgknVNPQIVENYRGGDIALGIGDEVLs 113
Cdd:cd08659 21 EYLAELLAKRGYgIESTIVEgRGNLVATVG---GGDGPVLLLNGHIDT--------VPPGDGDKWSFPPFSGRIRDGRL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 114 pvmfpvlhqlLGqtlittdgktlLGADD-KAGIAEIMTALAVLQQKNIPH-GDIRVAFTPDEEVGK-GAKHFDvdafDAR 190
Cdd:cd08659 89 ----------YG-----------RGACDmKGGLAAMVAALIELKEAGALLgGRVALLATVDEEVGSdGARALL----EAG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 191 WAYTVDGGGVGE-LEFENFNAA----SVNIKIVGNNVH---PGTAkgvmVNALSLAARI-----HAEVPADESPEMTEgy 257
Cdd:cd08659 144 YADRLDALIVGEpTGLDVVYAHkgslWLRVTVHGKAAHssmPELG----VNAIYALADFlaelrTLFEELPAHPLLGP-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 258 egfyhlASMK-GTVDRADMHYIIRDFDRKQFEAR----------KRKMMEIAKKVGKGLHpdcyIELVIEDSYYNMREKv 326
Cdd:cd08659 218 ------PTLNvGVINGGTQVNSIPDEATLRVDIRlvpgetnegvIARLEAILEEHEAKLT----VEVSLDGDPPFFTDP- 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446281586 327 vEHPhILDIAQQAMRDCDIEPELKPIRGGTDGAQLS-FMGLPCpnLFTGGYNYHGKH---EFVTLEGMEKAVQVIVRIA 401
Cdd:cd08659 287 -DHP-LVQALQAAARALGGDPVVRPFTGTTDASYFAkDLGFPV--VVYGPGDLALAHqpdEYVSLEDLLRAAEIYKEII 361
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
57-397 |
1.31e-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: 63.22 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 57 TLMATLPANvpGDIPAIGFISHVDTSPDCSGKNVNPQIVEnyrggdialgigdevlspvmfpvlhqllgQTLITTDGKTL 136
Cdd:cd18669 1 NVIARYGGG--GGGKRVLLGAHIDVVPAGEGDPRDPPFFV-----------------------------DTVEEGRLYGR 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 137 LGADDKAGIAEIMTALAVLQQKN-IPHGDIRVAFTPDEEVGKGAKHFDVDAFDARWAYTVDGGGVGELEfenfNAASVNI 215
Cdd:cd18669 50 GALDDKGGVAAALEALKLLKENGfKLKGTVVVAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDAT----PAPQKGV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 216 KIvgnnvhpgtaKGVMVNALSLAARihaevpadespemtegyegfyhlasmkgtvdradmhyiirdfdrkqfearkrkmm 295
Cdd:cd18669 126 GI----------RTPLVDALSEAAR------------------------------------------------------- 140
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 296 eiakkvgkglhpdcyielviedsyynmreKVVEHPhildiaqqamrdcdiePELKPIRGGTDGAQLSFMGLPCPNLFTGG 375
Cdd:cd18669 141 -----------------------------KVFGKP----------------QHAEGTGGGTDGRYLQELGIPGVTLGAGG 175
|
330 340
....*....|....*....|...
gi 446281586 376 -YNYHGKHEFVTLEGMEKAVQVI 397
Cdd:cd18669 176 gKGAHSPNERVNLEDLESALAVL 198
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
205-309 |
4.35e-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: 59.28 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 205 FENFNAASVNIKIVGNNVHPGtAKGVMVNALSLAARIHAEVPAD----------ESPEMTEGYEGFyhlaSMKGTVDRAD 274
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSG-APGKGVNAIKLLARLLAELPAEygdigfdfprTTLNITGIEGGT----ATNVIPAEAE 75
|
90 100 110
....*....|....*....|....*....|....*
gi 446281586 275 MHYIIRdfdRKQFEARKRKMMEIAKKVGKGLHPDC 309
Cdd:pfam07687 76 AKFDIR---LLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
129-301 |
1.51e-09 |
|
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: 59.46 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 129 ITTDGKTLlGADDKAGIAeimTALAVLQQKNIPHGDIRVAFTPDEEVGK-GAKHFDVDAFDARWAYTVDG---------- 197
Cdd:cd03890 97 LKATGTTL-GADNGIGVA---YALAILEDKDIEHPPLEVLFTVDEETGMtGALGLDPSLLKGKILLNLDSeeegeltvgc 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 198 -GGVG-----ELEFENFNAASVNIKIV---------GNNVHPGTAkgvmvNALSLAARIHAEVPADESpemtegyegfYH 262
Cdd:cd03890 173 aGGIDvtitlPIEREEAEGGYTGLKITvkglkgghsGVDIHKGRA-----NANKLMARLLYELAKELD----------FR 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446281586 263 LASMK-GTVDRAdmhyIIRD------FDRKQFEARKRKMMEIAKKV 301
Cdd:cd03890 238 LVSINgGTKRNA----IPREavaviaVPAEDVEALKKLIKKLEKAL 279
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
1-400 |
1.55e-09 |
|
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: 59.14 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 1 MDKLLERFLNYVSlDTQSKAGVRQVPStegqwkllhLLKEQLEEMGlINVTLSEK----GTLMATLPanvPGDIPAIGFI 76
Cdd:cd03885 1 MLDLLERLVNIES-GTYDKEGVDRVAE---------LLAEELEALG-FTVERRPLgefgDHLIATFK---GTGGKRVLLI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 77 SHVDTspdcsgknvnpqivenyrggdialgigdevlspvMFPvlHQLLGQTLITTDGKTLLG---ADDKAGIAEIMTALA 153
Cdd:cd03885 67 GHMDT----------------------------------VFP--EGTLAFRPFTVDGDRAYGpgvADMKGGLVVILHALK 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 154 VLQQKN-IPHGDIRVAFTPDEEVGK--GAKHFDVDAFDARWAYTVDGGGV-GELEFENFNAASVNIKIVGNNVHPGTA-- 227
Cdd:cd03885 111 ALKAAGgRDYLPITVLLNSDEEIGSpgSRELIEEEAKGADYVLVFEPARAdGNLVTARKGIGRFRLTVKGRAAHAGNApe 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 228 KGvmVNALSLAAR----IHAEvpADESPEMT------EGyegfyhlasmkGTV-----DRADMHYIIRDFDRKQFEARKR 292
Cdd:cd03885 191 KG--RSAIYELAHqvlaLHAL--TDPEKGTTvnvgviSG-----------GTRvnvvpDHAEAQVDVRFATAEEADRVEE 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 293 KMMEIAKKVgkgLHPDCYIELVIEDSYYNMrekvVEHPH---ILDIAQQAMRDCDIEPELKPIRGGTDGAQLSFMGLP-- 367
Cdd:cd03885 256 ALRAIVATT---LVPGTSVELTGGLNRPPM----EETPAsrrLLARAQEIAAELGLTLDWEATGGGSDANFTAALGVPtl 328
|
410 420 430
....*....|....*....|....*....|....*..
gi 446281586 368 ----CPnlftgGYNYHGKHEFVTLEGMEKAVQVIVRI 400
Cdd:cd03885 329 dglgPV-----GGGAHTEDEYLELDSLVPRIKLLARL 360
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
34-402 |
8.23e-09 |
|
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: 56.83 E-value: 8.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 34 LLHLLKEQLEEMGL-INVTLSEKGT---LMATLPanvPGDIPAIGFISHVDTSPDCSGK-NVNPqivenyrggdialgig 108
Cdd:cd03894 20 LIEYVADYLAALGVkSRRVPVPEGGkanLLATLG---PGGEGGLLLSGHTDVVPVDGQKwSSDP---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 109 devlspvmFpvlhqllgqTLITTDGKtLLG---ADDKAGIAEIMTALAVLQQKNiPHGDIRVAFTPDEEVG-KGAKHFdV 184
Cdd:cd03894 81 --------F---------TLTERDGR-LYGrgtCDMKGFLAAVLAAVPRLLAAK-LRKPLHLAFSYDEEVGcLGVRHL-I 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 185 DAFDARwAYTVDGGGVGE-LEFENFNA----ASVNIKIVGNNVH-PGTAKGVmvNALSLAARI------HAE--VPADES 250
Cdd:cd03894 141 AALAAR-GGRPDAAIVGEpTSLQPVVAhkgiASYRIRVRGRAAHsSLPPLGV--NAIEAAARLigklreLADrlAPGLRD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 251 PEMTEGYEGFyHLASMKG-----TV-DRADMHYIIRDFDRKQFEARKRKMMEIAKKVGkgLHPDCYIELVIEDSY--YNM 322
Cdd:cd03894 218 PPFDPPYPTL-NVGLIHGgnavnIVpAECEFEFEFRPLPGEDPEAIDARLRDYAEALL--EFPEAGIEVEPLFEVpgLET 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 323 REkvvEHPhILDIAQQAMRDCDIEPelkpIRGGTDGAQLSFMGLPCPNLFTGGYNY-HGKHEFVTLEGMEKAVQVIVRIA 401
Cdd:cd03894 295 DE---DAP-LVRLAAALAGDNKVRT----VAYGTEAGLFQRAGIPTVVCGPGSIAQaHTPDEFVELEQLDRCEEFLRRLI 366
|
.
gi 446281586 402 E 402
Cdd:cd03894 367 A 367
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
139-402 |
6.66e-07 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 51.14 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 139 ADDKAGIAEIMtaLAVLQQKNIPHGDIRVAFTPDEEV-GKGAKHFdVDAFDARWAYTVdgggVGELEFENF--NAAS--- 212
Cdd:PRK08651 113 SDMKGGIAALL--AAFERLDPAGDGNIELAIVPDEETgGTGTGYL-VEEGKVTPDYVI----VGEPSGLDNicIGHRglv 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 213 -VNIKIVGNNVHPGTAKgVMVNALSLAARIHAE----VPADESP-EMTEGYEGFYHL----ASMKG-------------T 269
Cdd:PRK08651 186 wGVVKVYGKQAHASTPW-LGINAFEAAAKIAERlkssLSTIKSKyEYDDERGAKPTVtlggPTVEGgtktnivpgycafS 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 270 VDRAdmhyIIRDFDRKQFEAR-KRKMMEIAKKVGKGLHPDcyIELVIEDSYYNMREKVVEhpHILDIAQQAMRdcdIEPE 348
Cdd:PRK08651 265 IDRR----LIPEETAEEVRDElEALLDEVAPELGIEVEFE--ITPFSEAFVTDPDSELVK--ALREAIREVLG---VEPK 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446281586 349 LKPIRGGTDGAQLSFMGLPCPNLFTGGY-NYHGKHEFVTLEGMEKAVQVIVRIAE 402
Cdd:PRK08651 334 KTISLGGTDARFFGAKGIPTVVYGPGELeLAHAPDEYVEVKDVEKAAKVYEEVLK 388
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
140-402 |
3.24e-06 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 48.60 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 140 DDKAGIAEIMTALAVLQQKNiPHGDIRVAFTPDEEV-GKGAKHFdVDAFDARWAYTVDGGGvGELEFENFNAASVNIKIV 218
Cdd:PRK08652 87 DAKGGVAAILLALEELGKEF-EDLNVGIAFVSDEEEgGRGSALF-AERYRPKMAIVLEPTD-LKVAIAHYGNLEAYVEVK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 219 GNNVHpGTAKGVMVNALSLAARIHAEVPADEsPEMTEGYEGFYHLASMKGtvdrADMHYIIRDFDRKQFEAR---KRKMM 295
Cdd:PRK08652 164 GKPSH-GACPESGVNAIEKAFEMLEKLKELL-KALGKYFDPHIGIQEIIG----GSPEYSIPALCRLRLDARippEVEVE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 296 EIAKKVGKGLhpDCYI---ELV-IEDSYYNMREKvvehpHILDIAQQAMRDCDIEPELKPIRGGTDGAQLSFMGLPCPNL 371
Cdd:PRK08652 238 DVLDEIDPIL--DEYTvkyEYTeIWDGFELDEDE-----EIVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTKTVVW 310
|
250 260 270
....*....|....*....|....*....|..
gi 446281586 372 FTGGYNY-HGKHEFVTLEGMEKAVQVIVRIAE 402
Cdd:PRK08652 311 GPGELDLcHTKFERIDVREVEKAKEFLKALNE 342
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
132-180 |
1.22e-05 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 46.93 E-value: 1.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446281586 132 DGKTLLG---ADDKAGIAEIMTALAVLQQKNIP-HGDIRVAFTPDEEVG-KGAK 180
Cdd:PRK06133 125 DGDRAYGpgiADDKGGVAVILHALKILQQLGFKdYGTLTVLFNPDEETGsPGSR 178
|
|
| M42_glucanase_like |
cd05657 |
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ... |
38-202 |
1.07e-04 |
|
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: 43.80 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 38 LKEQLEEMGlINVTLSEKGTLMATLPAnvPGDIPAIGFISHVDT--------SPD---------------CSGKNVN--P 92
Cdd:cd05657 26 LKKELEGLG-VETELTNKGALIATIPG--KDSRKARALSAHVDTlgaivkeiKPDgrlrltpiggfawnsAEGENVTiiT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 93 QIVENYRG------------GDI--------------------------ALGI--GDEVlspVMFPvlhqllgQTLITTD 132
Cdd:cd05657 103 RDGKTYTGtvlplkasvhvyGDApeaqertwdnmevrldekvkskedvlALGIrvGDFV---AFDP-------RPEVTES 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446281586 133 G----KTLlgaDDKAGIAEIMTALAVLQQKNI-PHGDIRVAFTPDEEVGKGAKHF---DVDAFDArwaytVDGGGVGE 202
Cdd:cd05657 173 GfiksRHL---DDKASVAILLALARALKENKLkLPVDTHFLFSNYEEVGHGASFAppeDTDELLA-----VDMGPVGP 242
|
|
| FrvX |
COG1363 |
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ... |
104-201 |
3.87e-03 |
|
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];
Pssm-ID: 440974 [Multi-domain] Cd Length: 353 Bit Score: 38.95 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 104 ALGI--GDEVlspVMFPVLHQLLGQTLITtdGKTLlgaDDKAGIAEIMTALAVLQQKNIPHgDIRVAFTPDEEVG-KGAK 180
Cdd:COG1363 149 ALGIrvGDFV---VFDPEFEELTNSGFIK--SKAL---DDRAGCAVLLELLKALKDEDLPV-TVYFVFTVQEEVGlRGAS 219
|
90 100
....*....|....*....|...
gi 446281586 181 --HFDVDAfDArwAYTVDGGGVG 201
Cdd:COG1363 220 taAYDIKP-DE--AIAVDVTPAG 239
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
117-388 |
4.04e-03 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 39.18 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 117 FPVLHQLlgQTLITTDGKTLLG---ADDKAGIAEIMTALAVLQQKniPHGD---IRVAFTPDEEVGKGAKHfdvdAFDAR 190
Cdd:PRK07338 105 FPADHPF--QTLSWLDDGTLNGpgvADMKGGIVVMLAALLAFERS--PLADklgYDVLINPDEEIGSPASA----PLLAE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 191 WAYTVDGGGVGELEFENFNAA-----SVNIKIV--GNNVHPGTAKGVMVNALSLAARIHAEVPA--DESPEMTegyegfY 261
Cdd:PRK07338 177 LARGKHAALTYEPALPDGTLAgarkgSGNFTIVvtGRAAHAGRAFDEGRNAIVAAAELALALHAlnGQRDGVT------V 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446281586 262 HLASMKG------TVDRADMHYIIRDFDRKQFEARKRKMMEIAKKVGKGlhPDCYIELviedsyynmrekvveH------ 329
Cdd:PRK07338 251 NVAKIDGggplnvVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQR--HGVSLHL---------------Hggfgrp 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446281586 330 PHILDIAQQAM----RDC----DIEPELKPIRGGTDGAQLSFMGLpcPNLFT----GGyNYHGKHEFVTLE 388
Cdd:PRK07338 314 PKPIDAAQQRLfeavQACgaalGLTIDWKDSGGVCDGNNLAAAGL--PVVDTlgvrGG-NIHSEDEFVILD 381
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
139-176 |
8.96e-03 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 38.22 E-value: 8.96e-03
10 20 30
....*....|....*....|....*....|....*...
gi 446281586 139 ADDKAGIAEIMTALAVLQQKNIpHGDIRVAFTPDEEVG 176
Cdd:PRK08554 102 ADDKGNVASVMLALKELSKEPL-NGKVIFAFTGDEEIG 138
|
|
| |
