|
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: 798.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 1 MDKLLDRFFNYVSFDTQAKANVKSVPSTEGQRKLALALQHELQMLGFSQVSLSEHGCVMATLPANVSWLVPTIGFIAHLD 80
Cdd:PRK05469 1 MDKLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDENGYVMATLPANVDKDVPTIGFIAHMD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 81 TSPDFSGKNVNPQIVENYRGGDIALGMGDEVLSPVMFPVLHQLLGHTLITTDGKTLLGADDKAGIAEIITALVRLK-HSN 159
Cdd:PRK05469 81 TAPDFSGKNVKPQIIENYDGGDIALGDGNEVLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYLIaHPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 160 IPHGNIRIAFTPDEEVGKGARFFNVAEFNAQWAYTVDGGGVGELEFENFNAASVTIKIVGNNVHPGSAKGVMVNALSLAT 239
Cdd:PRK05469 161 IKHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALLLAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 240 RFHQELPTDETPECTDGYDGFYHLQSIKGTVERAEMHYIVRDFNRDGFEARKKNMVDIAKRVGKGLHRdCYIEIVIDDSY 319
Cdd:PRK05469 241 DFHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKYGE-GRVELEIKDQY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 320 YNMREHIIKHPHIIEIAQQAMHDCDITPIMKPIRGGTDGAQLSFLGLPCPNIFTGGYNYHGKHEFITLEGMEKAVAVIMR 399
Cdd:PRK05469 320 YNMREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVIVE 399
|
....*....
gi 893144778 400 IAELTAKRA 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: 679.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 4 LLDRFFNYVSFDTQAKANVKSVPSTEGQRKLALALQHELQMLGFSQVSLSEHGCVMATLPANVSWLVPTIGFIAHLDTSP 83
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDEHGYVTATLPANVDKDVPTIGFIAHMDTAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 84 DFSGKNVNPQIVENYRGGDIALGMGDEVLSPVMFPVLHQLLGHTLITTDGKTLLGADDKAGIAEIITALVRLK-HSNIPH 162
Cdd:cd03892 81 DNSGKNVKPQIIENYDGGDIVLNESGIVLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIeHPEIKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 163 GNIRIAFTPDEEVGKGARFFNVAEFNAQWAYTVDGGGVGELEFENFNAASVTIKIVGNNVHPGSAKGVMVNALSLATRFH 242
Cdd:cd03892 161 GDIRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLAADFH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 243 QELPTDETPECTDGYDGFYHLQSIKGTVERAEMHYIVRDFNRDGFEARKKNMVDIAKRVGKGLHRDcYIEIVIDDSYYNM 322
Cdd:cd03892 241 SMLPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKYGEG-RVELEIKDQYYNM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 323 REHIIKHPHIIEIAQQAMHDCDITPIMKPIRGGTDGAQLSFLGLPCPNIFTGGYNYHGKHEFITLEGMEKAVAVIMRIAE 402
Cdd:cd03892 320 KEKIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIVKIAE 399
|
.
gi 893144778 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: 549.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 4 LLDRFFNYVSFDTQAKANVKSVPSTEGQRKLALALQHELQMLGFSQVSLSEHGCVMATLPANVSWLVPTIGFIAHLDTSP 83
Cdd:cd05645 1 LLERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEKGTLIATLPANVDGDIPAIGFISHVDTSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 84 DFSGKNVNPQIVENYRGGDIALGMGDEVLSPVMFPVLHQLLGHTLITTDGKTLLGADDKAGIAEIITALVRLKHSNIPHG 163
Cdd:cd05645 81 DGSGKNVNPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKNIPHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 164 NIRIAFTPDEEVGKGARFFNVAEFNAQWAYTVDGGGVGELEFENFNAASVTIKIVGNNVHPGSAKGVMVNALSLATRFHQ 243
Cdd:cd05645 161 DIEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAARIHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 244 ELPTDETPECTDGYDGFYHLQSIKGTVERAEMHYIVRDFNRDGFEARKKNMVDIAKRVGKGLHRDCYIEIVIDDSYYNMR 323
Cdd:cd05645 241 EVPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVGKGLHPDCYIELVIEDSYYNFR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 324 EHIIKHPHIIEIAQQAMHDCDITPIMKPIRGGTDGAQLSFLGLPCPNIFTGGYNYHGKHEFITLEGMEKAVAVIMRIAEL 403
Cdd:cd05645 321 EKVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIVRIAEL 400
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
1-405 |
3.34e-170 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 480.32 E-value: 3.34e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 1 MDKLLDRFFNYVSFDTQAKAnvksvpstegQRKLALALQHELQMLGFsQVSLSEHGCVMATLPANVSWLVPTIGFIAHLD 80
Cdd:COG2195 2 PERLLERFLEYVKIPTPSDH----------EEALADYLVEELKELGL-EVEEDEAGNVIATLPATPGYNVPTIGLQAHMD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 81 TSPDFSGKNVNPQIvenyRGGdialgmgdevlspvmfpvlhqllghtLITTDGKTLLGADDKAGIAEIITALVRLKHSNI 160
Cdd:COG2195 71 TVPQFPGDGIKPQI----DGG--------------------------LITADGTTTLGADDKAGVAAILAALEYLKEPEI 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 161 PHGNIRIAFTPDEEVG-KGARFFNVAEFNAQWAYTVDGGGVGELEFENFNAASVTIKIVGNNVHPGSAKGVMVNALSLAT 239
Cdd:COG2195 121 PHGPIEVLFTPDEEIGlRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIKLAA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 240 RFHQELPTDETPECTDGYDGFYHLQSI-KGTVERAEMHYIVRDFNRDGFEARKKNMVDIAKRVGKGLHRdCYIEIVIDDS 318
Cdd:COG2195 201 RFLAALPLGRIPEETEGNEGFIHGGSAtNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGV-GVVEVEIEDQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 319 YYNMREHiiKHPHIIEIAQQAMHDCDITPIMKPIRGGTDGAQLSFLGLPCPNIFTGGYNYHGKHEFITLEGMEKAVAVIM 398
Cdd:COG2195 280 YPNWKPE--PDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWELLV 357
|
....*..
gi 893144778 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 ... |
2-408 |
4.14e-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: 4.14e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 2 DKLLDRFFNYVSFDTQAKANVKSVPSTEGQRKLALALQHELQMLGFSQVSLSE-HGCVMATLPANVSWLVPTIGFIAHLD 80
Cdd:TIGR01882 3 EELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEkNGYVIATIPSNTDKDVPTIGFLAHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 81 TSpDFSGKNVNPQIVENYRGGD-IALGMGDEVLSPVMFPVLHQLLGHTLITTDGKTLLGADDKAGIAEIITALVRL-KHS 158
Cdd:TIGR01882 83 TA-DFNGENVNPQIIENYDGESiIQLGDLEFTLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAADYLiNHP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 159 NIPHGNIRIAFTPDEEVGKGARFFNVAEFNAQWAYTVDGGGVGELEFENFNAASVTIKIVGNNVHPGSAKGVMVNALSLA 238
Cdd:TIGR01882 162 EIKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAAQIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 239 TRFHQELPTDETPECTDGYDGFYHLQSIKGTVERAEMHYIVRDFNRDGFEARKKNMVDIAKRVGKGLHRDcYIEIVIDDS 318
Cdd:TIGR01882 242 IDLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEYGQD-RIKLDMNDQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 319 YYNMREHIIKHPHIIEIAQQAMHDCDITPIMKPIRGGTDGAQLSFLGLPCPNIFTGGYNYHGKHEFITLEGMEKAVAVIM 398
Cdd:TIGR01882 321 YYNMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDVIV 400
|
410
....*....|
gi 893144778 399 RIAELTAKRA 408
Cdd:TIGR01882 401 EIAKLNEEQA 410
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
2-406 |
2.07e-158 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 452.07 E-value: 2.07e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 2 DKLLDRFFNYVSFDTQAKANVKSVPSTEGQRKLALALQHELQMLGFSQVSLSEHGCVMATLPANVSwLVPTIGFIAHLDT 81
Cdd:PRK13381 1 MQLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDIVIDEHAIVTAKLPGNTP-GAPRIGFIAHLDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 82 SpDFS-GKNVNPQIVEnYRGGDIALGMG-DEVLSPVMFPVLHQLLGHTLITTDGKTLLGADDKAGIAEIITALVRLKHSN 159
Cdd:PRK13381 80 V-DVGlSPDIHPQILR-FDGGDLCLNAEqGIWLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLENLTENE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 160 IPHGNIRIAFTPDEEVG-KGARFFNVAEFNAQWAYTVDGGGVGELEFENFNAASVTIKIVGNNVHPGSAKGVMVNALSLA 238
Cdd:PRK13381 158 VEHGDIVVAFVPDEEIGlRGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNPILMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 239 TRFHQELPTDETPECTDGYDGFYHLQSIKGTVERAEMHYIVRDFNRDGFEARKKNMVDIAKRVGKgLHRDCYIEIVIDDS 318
Cdd:PRK13381 238 NDFISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINA-KYPTARVSLTLTDQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 319 YYNMREHIIKHPHIIEIAQQAMHDCDITPIMKPIRGGTDGAQLSFLGLPCPNIFTGGYNYHGKHEFITLEGMEKAVAVIM 398
Cdd:PRK13381 317 YSNISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEVTI 396
|
....*...
gi 893144778 399 RIAELTAK 406
Cdd:PRK13381 397 TICLLAAK 404
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
2-402 |
6.65e-30 |
|
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: 118.71 E-value: 6.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 2 DKLLDRFFNYVSFDTQAK--ANVKSVpstegqrklalaLQHELQMLGFS-------QVSLSEHGCVMATLPANVSWlVPT 72
Cdd:cd05683 3 DRLINTFLELVQIDSETLheKEISKV------------LKKKFENLGLSvieddagKTTGGGAGNLICTLKADKEE-VPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 73 IGFIAHLDT-SPdfsGKNV-NPQIVENYrggdialgmgdevlspvmfpvlhqllghtlITTDGKTLLGADDKAGIAEIIT 150
Cdd:cd05683 70 ILFTSHMDTvTP---GINVkPPQIADGY------------------------------IYSDGTTILGADDKAGIAAILE 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 151 ALVRLKHSNIPHGNIRIAFTPDEEVG-KGARFFNVAEFNAQWAYTVDGGG-VGELEFENFNAASVTIKIVGNNVHPGSAK 228
Cdd:cd05683 117 AIRVIKEKNIPHGQIQFVITVGEESGlVGAKALDPELIDADYGYALDSEGdVGTIIVGAPTQDKINAKIYGKTAHAGTSP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 229 GVMVNALSLATRFHQELPTDETPECTDGYDGFYHLQSIKGTVerAEMHYI---VRDFNRDGFEARKKNMVDIAKRVGKGL 305
Cdd:cd05683 197 EKGISAINIAAKAISNMKLGRIDEETTANIGKFQGGTATNIV--TDEVNIeaeARSLDEEKLDAQVKHMKETFETTAKEK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 306 HrdCYIEIVIDDSYYNMreHIIKHPHIIEIAQQAMHDCDITPIMKPIRGGTDGAQLSFLGLPCPNIFTGGYNYHGKHEFI 385
Cdd:cd05683 275 G--AHAEVEVETSYPGF--KINEDEEVVKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERI 350
|
410
....*....|....*..
gi 893144778 386 TLEGMEKAVAVIMRIAE 402
Cdd:cd05683 351 PIEDLYDTAVLVVEIIK 367
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
25-402 |
3.08e-29 |
|
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: 116.96 E-value: 3.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 25 VPSTEG-QRKLALALQHELQMLGFSqVSLSEH-------GCVMATLPANVSWlvPTIGFIAHLDTSPDfsGKNVNPQIVE 96
Cdd:TIGR01883 12 IDSESGkEKAILTYLKKQITKLGIP-VSLDEVpaevsndNNLIARLPGTVKF--DTIFFCGHMDTVPP--GAGPEPVVED 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 97 NYrggdialgmgdevlspvmfpvlhqllghtlITTDGKTLLGADDKAGIAEIITALVRLKHSNIPHGNIRIAFTPDEEVG 176
Cdd:TIGR01883 87 GI------------------------------FTSLGGTILGADDKAGVAAMLEAMDVLSTEETPHGTIEFIFTVKEELG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 177 -KGARFFNVAEFNAQWAYTVDGGG-VGELEFENFNAASVTIKIVGNNVHPGSAKGVMVNALSLATRFHQELPTDETPECT 254
Cdd:TIGR01883 137 lIGMRLFDESKITAAYGYCLDAPGeVGNIQLAAPTQVKVDATIAGKDAHAGLVPEDGISAISVARMAIHAMRLGRIDEET 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 255 DgydgfYHLQSIKGTVE----RAEMHYIV--RDFNRDGFEARKKNMVDIAKRVGKGLHRDCYIEIVIDDSYYNMREhiiK 328
Cdd:TIGR01883 217 T-----ANIGSFSGGVNtnivQDEQLIVAeaRSLSFRKAEAQVQTMRERFEQAAEKYGATLEEETRLIYEGFKIHP---Q 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 893144778 329 HPHiIEIAQQAMHDCDITPIMKPIRGGTDGAQLSFLGLPCPNIFTGGYNYHGKHEFITLEGMEKAVAVIMRIAE 402
Cdd:TIGR01883 289 HPL-MNIFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETISIEQLVKLAELVIALAE 361
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
24-402 |
4.14e-18 |
|
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: 85.32 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 24 SVPSTEGQ-RKLALALQHELQMLGFS---QVSLSEHGCVMATLPANVSWlvPTIGFIAHLDTspdfsgknVNPqivenyr 99
Cdd:COG0624 23 RIPSVSGEeAAAAELLAELLEALGFEverLEVPPGRPNLVARRPGDGGG--PTLLLYGHLDV--------VPP------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 100 gGDIALGMGDevlsPvmFPVlhqllghtliTTDGKTLLG---ADDKAGIAEIITALVRLKHSNI-PHGNIRIAFTPDEEV 175
Cdd:COG0624 86 -GDLELWTSD----P--FEP----------TIEDGRLYGrgaADMKGGLAAMLAALRALLAAGLrLPGNVTLLFTGDEEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 176 G-KGARFF---NVAEFNAQWAYTVDGGGVGELEFENFNAASVTIKIVGNNVHpGSAKGVMVNALSLATRFHQELPTDETP 251
Cdd:COG0624 149 GsPGARALveeLAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAH-SSRPELGVNAIEALARALAALRDLEFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 252 ECTDGYDGFYHLQ--SIKGTV------ERAEMHYIVR---DFNRDGFEARkknMVDIAKRVGKGLHrdcyIEIVIDDSYY 320
Cdd:COG0624 228 GRADPLFGRTTLNvtGIEGGTavnvipDEAEAKVDIRllpGEDPEEVLAA---LRALLAAAAPGVE----VEVEVLGDGR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 321 N---MREHiikHPhIIEIAQQAMHD---CDITPIMKPirGGTDGAQLS-FLGLPCPNI-FTGGYNYHGKHEFITLEGMEK 392
Cdd:COG0624 301 PpfeTPPD---SP-LVAAARAAIREvtgKEPVLSGVG--GGTDARFFAeALGIPTVVFgPGDGAGAHAPDEYVELDDLEK 374
|
410
....*....|
gi 893144778 393 AVAVIMRIAE 402
Cdd:COG0624 375 GARVLARLLE 384
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
139-402 |
1.18e-17 |
|
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: 83.17 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 139 ADDKAGIAEIITALVRLKHSNIPHGNIRIAFTPDEEVGK-GARFF----NVAEFNAQWAYT--VDGGGVGELEFE----N 207
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEGLKKGTVKLLFQPDEEGGMgGARALiedgLLEREKVDAVFGlhIGEPTLLEGGIAigvvT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 208 FNAAS--VTIKIVGNNVHpGSAKGVMVNALSLATRFHQELPTDETPEcTDGYDG----FYHLQSIKGTV----ERAEMHY 277
Cdd:pfam01546 113 GHRGSlrFRVTVKGKGGH-ASTPHLGVNAIVAAARLILALQDIVSRN-VDPLDPavvtVGNITGIPGGVnvipGEAELKG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 278 IVRDFNRDGFEARKKNMVDIAKRVGKglHRDCYIEIVIDDSYYNMRehiIKHPHIIEIAQQAMHD---CDITPIMKPIRG 354
Cdd:pfam01546 191 DIRLLPGEDLEELEERIREILEAIAA--AYGVKVEVEYVEGGAPPL---VNDSPLVAALREAAKElfgLKVELIVSGSMG 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 893144778 355 GTDGAqlsFLGLPCPNIF----TGGYNYHGKHEFITLEGMEKAVAVIMRIAE 402
Cdd:pfam01546 266 GTDAA---FFLLGVPPTVvffgPGSGLAHSPNEYVDLDDLEKGAKVLARLLL 314
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
57-397 |
5.03e-15 |
|
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: 73.23 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 57 CVMATLPANVSwlVPTIGFIAHLDTSPDFSGKNVNPQIVEnyrggdialgmgdevlspvmfpvlhqllgHTLITTDGKTL 136
Cdd:cd03873 1 NLIARLGGGEG--GKSVALGAHLDVVPAGEGDNRDPPFAE-----------------------------DTEEEGRLYGR 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 137 LGADDKAGIAEIITALVRLK-HSNIPHGNIRIAFTPDEEVGKGARFFNVAEFnaqwaytvdgggvgELEFENFNAASVTI 215
Cdd:cd03873 50 GALDDKGGVAAALEALKRLKeNGFKPKGTIVVAFTADEEVGSGGGKGLLSKF--------------LLAEDLKVDAAFVI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 216 kivgnnvhpgsakgvmvnalslatrfhqelptDETPECTDGYDGfyhlqsikgtveraemhyivrdfnrdgfeARKKNMV 295
Cdd:cd03873 116 --------------------------------DATAGPILQKGV-----------------------------VIRNPLV 134
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 296 DIAKRVgkglHRDCYIEIVIDDsyynmrehiikhphiieiaqqamhdcditpimkPIRGGTDGAQLSFLGLPCPNIFTGG 375
Cdd:cd03873 135 DALRKA----AREVGGKPQRAS---------------------------------VIGGGTDGRLFAELGIPGVTLGPPG 177
|
330 340
....*....|....*....|...
gi 893144778 376 -YNYHGKHEFITLEGMEKAVAVI 397
Cdd:cd03873 178 dKGAHSPNEFLNLDDLEKATKVY 200
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
71-397 |
2.07e-12 |
|
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: 65.53 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 71 PTIGFIAHLDTSPDFSGKNVNPQIVENYRGGDIALGMGdevlspvmfpvlhqllghtlittdgktllGADDKAGIAEIIT 150
Cdd:cd18669 13 KRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRG-----------------------------ALDDKGGVAAALE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 151 ALVRLK-HSNIPHGNIRIAFTPDEEVGKGARFFNVAEFNAQWAYTVDGGGVGELEfenfnaasvtikivgnnvhPGSAKG 229
Cdd:cd18669 64 ALKLLKeNGFKLKGTVVVAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDAT-------------------PAPQKG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 230 VmvnalslATRFHQelptdetpectdgydgfyhlqsikgtveraemhyivrdfnrdgfearkknmVDIAKRVgkglHRDC 309
Cdd:cd18669 125 V-------GIRTPL---------------------------------------------------VDALSEA----ARKV 142
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 310 YIEIviddsyynmrehiikhphiieiaqqamhdcditPIMKPIRGGTDGAQLSFLGLPCPNIFTGG-YNYHGKHEFITLE 388
Cdd:cd18669 143 FGKP---------------------------------QHAEGTGGGTDGRYLQELGIPGVTLGAGGgKGAHSPNERVNLE 189
|
....*....
gi 893144778 389 GMEKAVAVI 397
Cdd:cd18669 190 DLESALAVL 198
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
56-401 |
8.11e-11 |
|
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: 63.09 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 56 GCVMATLPANVSwlvPTIGFIAHLDTspdfsgknVNPQIVENYRggdialgmgdevLSPvmfpvlhqllgHTLITTDGKt 135
Cdd:cd08659 43 GNLVATVGGGDG---PVLLLNGHIDT--------VPPGDGDKWS------------FPP-----------FSGRIRDGR- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 136 LLG---ADDKAGIAEIITALVRLKHSNIPH-GNIRIAFTPDEEVGK-GARFFnvaeFNAQWAYTVDGGGVGE-LEFENFN 209
Cdd:cd08659 88 LYGrgaCDMKGGLAAMVAALIELKEAGALLgGRVALLATVDEEVGSdGARAL----LEAGYADRLDALIVGEpTGLDVVY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 210 AA----SVTIKIVGNNVHpGSAKGVMVNALSLATRFHQELPTDETPECTDGYDGFYHLQS--IKGTVE------RAEMHY 277
Cdd:cd08659 164 AHkgslWLRVTVHGKAAH-SSMPELGVNAIYALADFLAELRTLFEELPAHPLLGPPTLNVgvINGGTQvnsipdEATLRV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 278 IVR---DFNRDGFEARkknMVDIAKRVGKGLHrdcyIEIVIDDSYYnmrEHIIKHPHIIEIAQQAMHDCDITPIMKPIRG 354
Cdd:cd08659 243 DIRlvpGETNEGVIAR---LEAILEEHEAKLT----VEVSLDGDPP---FFTDPDHPLVQALQAAARALGGDPVVRPFTG 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 893144778 355 GTDGAQLS-FLGLPCpnIFTGGYNYHGKH---EFITLEGMEKAVAVIMRIA 401
Cdd:cd08659 313 TTDASYFAkDLGFPV--VVYGPGDLALAHqpdEYVSLEDLLRAAEIYKEII 361
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
205-309 |
1.00e-09 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 55.43 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 205 FENFNAASVTIKIVGNNVHPGsAKGVMVNALSLATRFHQELPTD----------ETPECTDGYDGFyhlqSIKGTVERAE 274
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSG-APGKGVNAIKLLARLLAELPAEygdigfdfprTTLNITGIEGGT----ATNVIPAEAE 75
|
90 100 110
....*....|....*....|....*....|....*
gi 893144778 275 MHYIVRdfnRDGFEARKKNMVDIAKRVGKGLHRDC 309
Cdd:pfam07687 76 AKFDIR---LLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
25-402 |
8.86e-09 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 56.69 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 25 VPSTEGQR-KLALALQHELQMLGFSqVSLSEHGCVMATLPANVSWLVptigFIAHLDTSPdfsgknvnPQIVENYRGGdI 103
Cdd:PRK08652 14 IPSPSGQEdEIALHIMEFLESLGYD-VHIESDGEVINIVVNSKAELF----VEVHYDTVP--------VRAEFFVDGV-Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 104 ALGMGdevlspvmfpvlhqllghtlittdgktllGADDKAGIAEIITALVRLKHSNiPHGNIRIAFTPDEEV-GKGARFF 182
Cdd:PRK08652 80 VYGTG-----------------------------ACDAKGGVAAILLALEELGKEF-EDLNVGIAFVSDEEEgGRGSALF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 183 nVAEFNAQWAYTVDGGGvGELEFENFNAASVTIKIVGNNVHpGSAKGVMVNALSLATRFHQELPTDEtPECTDGYDGFYH 262
Cdd:PRK08652 130 -AERYRPKMAIVLEPTD-LKVAIAHYGNLEAYVEVKGKPSH-GACPESGVNAIEKAFEMLEKLKELL-KALGKYFDPHIG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 263 LQSIKGTVEraemHYIVRDFNRDGFEAR---KKNMVDIAKRVGK-----GLHRDcYIEIVidDSYYNMREHiikhpHIIE 334
Cdd:PRK08652 206 IQEIIGGSP----EYSIPALCRLRLDARippEVEVEDVLDEIDPildeyTVKYE-YTEIW--DGFELDEDE-----EIVQ 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 335 IAQQAMHDCDITPIMKPIRGGTDGAQLSFLGLPcPNIF-TGGYNY-HGKHEFITLEGMEKAVAVIMRIAE 402
Cdd:PRK08652 274 LLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTK-TVVWgPGELDLcHTKFERIDVREVEKAKEFLKALNE 342
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
126-402 |
4.44e-08 |
|
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: 54.52 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 126 HTLITTDGKtLLG---ADDKAGIAEIITALVRLKHSNiPHGNIRIAFTPDEEVG-KGARFFnvAEFNAQWAYTVDGGGVG 201
Cdd:cd03894 81 FTLTERDGR-LYGrgtCDMKGFLAAVLAAVPRLLAAK-LRKPLHLAFSYDEEVGcLGVRHL--IAALAARGGRPDAAIVG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 202 E-LEFENFNA----ASVTIKIVGNNVHpGSAKGVMVNALSLATRFHQEL----PTDETPECTDGYDGFY---HLQSIKG- 268
Cdd:cd03894 157 EpTSLQPVVAhkgiASYRIRVRGRAAH-SSLPPLGVNAIEAAARLIGKLrelaDRLAPGLRDPPFDPPYptlNVGLIHGg 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 269 ----TV-ERAEMHYIVRDFNRDGFEARKKNMVDIAKRVGkgLHRDCYIEIVIDDSY--YNMREHiikHPhIIEIAQQAmh 341
Cdd:cd03894 236 navnIVpAECEFEFEFRPLPGEDPEAIDARLRDYAEALL--EFPEAGIEVEPLFEVpgLETDED---AP-LVRLAAAL-- 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 893144778 342 dCDITPIMKpIRGGTDGAQLSFLGLPC----P-NIFTGgynyHGKHEFITLEGMEKAVAVIMRIAE 402
Cdd:cd03894 308 -AGDNKVRT-VAYGTEAGLFQRAGIPTvvcgPgSIAQA----HTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
138-399 |
6.48e-07 |
|
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.
Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 51.21 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 138 GA-DDKAGIAEIITALVRLKHSNI-PHGNIRIAFTPDEEVGK--GARF--------FNVAEF----NAQWAYTVDGGGVg 201
Cdd:cd05675 102 GAvDMKNMAAMMLAVLRHYKREGFkPKRDLVFAFVADEEAGGenGAKWlvdnhpelFDGATFalneGGGGSLPVGKGRR- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 202 eleFENFNAAS-----VTIKIVGNNVH---PGSAKGVmVNALSLATRFHQelpTDETPECTDGYDGFYHLQSIKGTVERA 273
Cdd:cd05675 181 ---LYPIQVAEkgiawMKLTVRGRAGHgsrPTDDNAI-TRLAEALRRLGA---HNFPVRLTDETAYFAQMAELAGGEGGA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 274 EM---------------------HYIVRD-FNRDGFEARKKNMVDIAKRVGkglHRDCYI------EIVIDD------SY 319
Cdd:cd05675 254 LMltavpvldpalaklgpsapllNAMLRNtASPTMLDAGYATNVLPGRATA---EVDCRIlpgqseEEVLDTldkllgDP 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 320 YNMREHIIKHPHII------------EIAQQAMHDCDITPIMKPirGGTDGAQLSFLGLPC--------PNIFTGGYNYH 379
Cdd:cd05675 331 DVSVEAVHLEPATEspldsplvdameAAVQAVDPGAPVVPYMSP--GGTDAKYFRRLGIPGygfaplflPPELDYTGLFH 408
|
330 340
....*....|....*....|
gi 893144778 380 GKHEFITLEGMEKAVAVIMR 399
Cdd:cd05675 409 GVDERVPVESLYFGVRFLDR 428
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
139-402 |
1.58e-06 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 49.99 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 139 ADDKAGIAEIITALVRLKhsNIPHGNIRIAFTPDEEV-GKGAR-FFNVAEFNAQWAYTVDGGGvgeleFENFNAAS---- 212
Cdd:PRK08651 113 SDMKGGIAALLAAFERLD--PAGDGNIELAIVPDEETgGTGTGyLVEEGKVTPDYVIVGEPSG-----LDNICIGHrglv 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 213 -VTIKIVGNNVHpGSAKGVMVNALSLATRFHQELPTDETP-----ECTDGYDGFYHLQSIKGTVERAEMHYIVRDF---- 282
Cdd:PRK08651 186 wGVVKVYGKQAH-ASTPWLGINAFEAAAKIAERLKSSLSTikskyEYDDERGAKPTVTLGGPTVEGGTKTNIVPGYcafs 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 283 ---------NRDGFEARKKNMVD-IAKRVGKGLHRDcyIEIVIDDSYYNMREHIIKhpHIIEIAQQAMhdcDITPIMKPI 352
Cdd:PRK08651 265 idrrlipeeTAEEVRDELEALLDeVAPELGIEVEFE--ITPFSEAFVTDPDSELVK--ALREAIREVL---GVEPKKTIS 337
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 893144778 353 RGGTDGAQLSFLGLPCPNIFTGGY-NYHGKHEFITLEGMEKAVAVIMRIAE 402
Cdd:PRK08651 338 LGGTDARFFGAKGIPTVVYGPGELeLAHAPDEYVEVKDVEKAAKVYEEVLK 388
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
29-176 |
1.96e-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: 49.51 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 29 EGQRKLALALQHELQMLGFS--QVSLSEHG-CVMATLPanvSWLVPTIGFIAHLDTspdfsgknvnpqivenyrggdial 105
Cdd:cd03885 19 EGVDRVAELLAEELEALGFTveRRPLGEFGdHLIATFK---GTGGKRVLLIGHMDT------------------------ 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 893144778 106 gmgdevlspvMFPvlHQLLGHTLITTDGKTLLG---ADDKAGIAEIITALVRLKHSN-IPHGNIRIAFTPDEEVG 176
Cdd:cd03885 72 ----------VFP--EGTLAFRPFTVDGDRAYGpgvADMKGGLVVILHALKALKAAGgRDYLPITVLLNSDEEIG 134
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
132-247 |
2.28e-05 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 46.16 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 132 DGKTLLG---ADDKAGIAEIITALVRLKHSNIP-HGNIRIAFTPDEEVG-KGARFFnVAEFNAQWAYTV--DGGGVGE-- 202
Cdd:PRK06133 125 DGDRAYGpgiADDKGGVAVILHALKILQQLGFKdYGTLTVLFNPDEETGsPGSREL-IAELAAQHDVVFscEPGRAKDal 203
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 893144778 203 -LEFENFNAASVTIKivGNNVHPGSAKGVMVNAL-SLAtrfHQELPT 247
Cdd:PRK06133 204 tLATSGIATALLEVK--GKASHAGAAPELGRNALyELA---HQLLQL 245
|
|
| M42_glucanase_like |
cd05657 |
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ... |
140-202 |
3.52e-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: 42.26 E-value: 3.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 893144778 140 DDKAGIAEIITALVRLKHSNI-PHGNIRIAFTPDEEVGKGARFF---NVAEFNAqwaytVDGGGVGE 202
Cdd:cd05657 181 DDKASVAILLALARALKENKLkLPVDTHFLFSNYEEVGHGASFAppeDTDELLA-----VDMGPVGP 242
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
129-299 |
9.78e-04 |
|
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: 41.35 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 129 ITTDGKTLlGADDKAGIAeiiTALVRLKHSNIPHGNIRIAFTPDEEVG------------KGARFFNV-----AEFNAQW 191
Cdd:cd03890 97 LKATGTTL-GADNGIGVA---YALAILEDKDIEHPPLEVLFTVDEETGmtgalgldpsllKGKILLNLdseeeGELTVGC 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 192 AYTVDGGGVGELEFENFNAASVTIKIV---------GNNVHPGSAkgvmvNALSLATRFHQELptdetPECTDgydgfYH 262
Cdd:cd03890 173 AGGIDVTITLPIEREEAEGGYTGLKITvkglkgghsGVDIHKGRA-----NANKLMARLLYEL-----AKELD-----FR 237
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 893144778 263 LQSIKGTVER------AEMHYIVRDFNRDGFEARKKNMVDIAK 299
Cdd:cd03890 238 LVSINGGTKRnaipreAVAVIAVPAEDVEALKKLIKKLEKALK 280
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
139-250 |
2.16e-03 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 40.14 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 139 ADDKAGIAEIITALVRLKHSNIpHGNIRIAFTPDEEVGkGARFFNVAEFNAQ---W-AYTVDGGGVGELEF-ENFNAASV 213
Cdd:PRK08554 102 ADDKGNVASVMLALKELSKEPL-NGKVIFAFTGDEEIG-GAMAMHIAEKLREegkLpKYMINADGIGMKPIiRRRKGFGV 179
|
90 100 110
....*....|....*....|....*....|....*..
gi 893144778 214 TIKIvgnnvhpgSAKGVMVNALSLATRFHQELPTDET 250
Cdd:PRK08554 180 TIRV--------PSEKVKVKGKLREQTFEIRTPVVET 208
|
|
| FrvX |
COG1363 |
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ... |
108-201 |
2.82e-03 |
|
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];
Pssm-ID: 440974 [Multi-domain] Cd Length: 353 Bit Score: 39.34 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 108 GDEVlspVMFPVLHQLLGHTLITtdGKTLlgaDDKAGIAEIITALVRLKHSNIPHgNIRIAFTPDEEVG-KGARFFnVAE 186
Cdd:COG1363 155 GDFV---VFDPEFEELTNSGFIK--SKAL---DDRAGCAVLLELLKALKDEDLPV-TVYFVFTVQEEVGlRGASTA-AYD 224
|
90
....*....|....*
gi 893144778 187 FNAQWAYTVDGGGVG 201
Cdd:COG1363 225 IKPDEAIAVDVTPAG 239
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
132-296 |
5.47e-03 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 38.71 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 132 DGKtLLG---ADDKAGIAEIITALVRLKHSN-IPHGNIRIAFTPDEEVGK-GARFFnvaeFNAQWAYTVDGGGVGELEFE 206
Cdd:PRK08588 90 DGK-LYGrgaTDMKSGLAALVIAMIELKEQGqLLNGTIRLLATAGEEVGElGAKQL----TEKGYADDLDALIIGEPSGH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 207 NFNAA---SVTIKIV--GNNVHpGSAKGVMVNALSLATRFHQELPT--DETPECTDGYDGFYHLQS-IKG-----TV-ER 272
Cdd:PRK08588 165 GIVYAhkgSMDYKVTstGKAAH-SSMPELGVNAIDPLLEFYNEQKEyfDSIKKHNPYLGGLTHVVTiINGgeqvnSVpDE 243
|
170 180
....*....|....*....|....*..
gi 893144778 273 AEMHYIVR---DFNRDGFEARKKNMVD 296
Cdd:PRK08588 244 AELEFNIRtipEYDNDQVISLLQEIIN 270
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
81-176 |
6.56e-03 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349933 [Multi-domain] Cd Length: 355 Bit Score: 38.52 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893144778 81 TSPDFSGKNVNPQIVeNYRGGDIAL--GMGDevlspvMFPVlHQLLGHT-----LITTDGKtLLG---ADDKAGIAEIIT 150
Cdd:cd08011 41 HEPPEEIYGVVSNIV-GGRKGKRLLfnGHYD------VVPA-GDGEGWTvdpysGKIKDGK-LYGrgsSDMKGGIAASII 111
|
90 100
....*....|....*....|....*..
gi 893144778 151 ALVRLKHS-NIPHGNIRIAFTPDEEVG 176
Cdd:cd08011 112 AVARLADAkAPWDLPVVLTFVPDEETG 138
|
|
| |
