|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
1-405 |
0e+00 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 671.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 1 MKVLDRLVSYVKVDTQSSEESGTHPSTEKQFVLARQLERELRELGADDVRLSEHCYVYARIPSNLSAEenmhTPTLGLIA 80
Cdd:PRK05469 2 DKLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDENGYVMATLPANVDKD----VPTIGFIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 81 HMDTSPSASGKDVKPRVIKSYDGSPIPLGHGAI-LDPGIFPQLLSAKGDDLLVTDGSTLLGADDKAGVAEIMQCIEELLS 159
Cdd:PRK05469 78 HMDTAPDFSGKNVKPQIIENYDGGDIALGDGNEvLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYLIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 160 QPERRHGEICIAFTPDEEIGSGADFFDLAGFGAEVAYTVDGGTLGGIEYENFNAASAVLTIHGVNVHPGSAKDKMLNALL 239
Cdd:PRK05469 158 HPEIKHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 240 IAMEFNALLPP-CTPANTEGYEGFFHLMSMKGDESLAELRYIIRDHDREKFEEKKRQFQSAADRLNEKYrsGGAALEAKL 318
Cdd:PRK05469 238 LAADFHAMLPAdETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKY--GEGRVELEI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 319 TDSYYNMKEKLEPYPYLIDCAKEAFRSCGVKPETLPIRGGTDGAKLSFMGLPCPNLSTGGENYHGIYEYLNINSMEKMVE 398
Cdd:PRK05469 316 KDQYYNMREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVE 395
|
....*..
gi 496507077 399 VLKKLTE 405
Cdd:PRK05469 396 VIVEIAE 402
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
3-405 |
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: 633.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 3 VLDRLVSYVKVDTQSSEESGTHPSTEKQFVLARQLERELRELGADDVRLSEHCYVYARIPSNLSAeenmHTPTLGLIAHM 82
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDEHGYVTATLPANVDK----DVPTIGFIAHM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 83 DTSPSASGKDVKPRVIKSYDGSPIPLGHGAI-LDPGIFPQLLSAKGDDLLVTDGSTLLGADDKAGVAEIMQCIEELLSQP 161
Cdd:cd03892 77 DTAPDNSGKNVKPQIIENYDGGDIVLNESGIvLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIEHP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 162 ERRHGEICIAFTPDEEIGSGADFFDLAGFGAEVAYTVDGGTLGGIEYENFNAASAVLTIHGVNVHPGSAKDKMLNALLIA 241
Cdd:cd03892 157 EIKHGDIRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 242 MEFNALLPPC-TPANTEGYEGFFHLMSMKGDESLAELRYIIRDHDREKFEEKKRQFQSAADRLNEKYrsGGAALEAKLTD 320
Cdd:cd03892 237 ADFHSMLPREeTPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKY--GEGRVELEIKD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 321 SYYNMKEKLEPYPYLIDCAKEAFRSCGVKPETLPIRGGTDGAKLSFMGLPCPNLSTGGENYHGIYEYLNINSMEKMVEVL 400
Cdd:cd03892 315 QYYNMKEKIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVI 394
|
....*
gi 496507077 401 KKLTE 405
Cdd:cd03892 395 VKIAE 399
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
1-406 |
6.95e-160 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 454.12 E-value: 6.95e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 1 MKVLDRLVSYVKVDTQSSEEsgthpstekqFVLARQLERELRELGADdVRLSEHCYVYARIPSNLsaeeNMHTPTLGLIA 80
Cdd:COG2195 3 ERLLERFLEYVKIPTPSDHE----------EALADYLVEELKELGLE-VEEDEAGNVIATLPATP----GYNVPTIGLQA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 81 HMDTSPSASGKDVKPRViksyDGspiplghgaildpgifpqllsakgdDLLVTDGSTLLGADDKAGVAEIMQCIEELLSq 160
Cdd:COG2195 68 HMDTVPQFPGDGIKPQI----DG-------------------------GLITADGTTTLGADDKAGVAAILAALEYLKE- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 161 PERRHGEICIAFTPDEEIG-SGADFFDLAGFGAEVAYTVDGGTLGGIEYENFNAASAVLTIHGVNVHPGSAKDKMLNALL 239
Cdd:COG2195 118 PEIPHGPIEVLFTPDEEIGlRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 240 IAMEFNALLPPC-TPANTEGYEGFFHLMSM-KGDESLAELRYIIRDHDREKFEEKKRQFQSAADRLNEKYrsGGAALEAK 317
Cdd:COG2195 198 LAARFLAALPLGrIPEETEGNEGFIHGGSAtNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKY--GVGVVEVE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 318 LTDSYYNMKEklEPYPYLIDCAKEAFRSCGVKPETLPIRGGTDGAKLSFMGLPCPNLSTGGENYHGIYEYLNINSMEKMV 397
Cdd:COG2195 276 IEDQYPNWKP--EPDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAW 353
|
....*....
gi 496507077 398 EVLKKLTEE 406
Cdd:COG2195 354 ELLVEILKL 362
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
1-406 |
6.31e-153 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 438.20 E-value: 6.31e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 1 MKVLDRLVSYVKVDTQSSEESGTHPSTEKQFVLARQLERELRELGADDVRLSEHCYVYARIPSNLSAEenmhtPTLGLIA 80
Cdd:PRK13381 1 MQLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDIVIDEHAIVTAKLPGNTPGA-----PRIGFIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 81 HMDTSPSASGKDVKPRVIKsYDGSPIPLG--HGAILDPGIFPQLLSAKGDDLLVTDGSTLLGADDKAGVAEIMQCIEeLL 158
Cdd:PRK13381 76 HLDTVDVGLSPDIHPQILR-FDGGDLCLNaeQGIWLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLE-NL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 159 SQPERRHGEICIAFTPDEEIGS-GADFFDLAGFGAEVAYTVDGGTLGGIEYENFNAASAVLTIHGVNVHPGSAKDKMLNA 237
Cdd:PRK13381 154 TENEVEHGDIVVAFVPDEEIGLrGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 238 LLIAMEFNALLPPC-TPANTEGYEGFFHLMSMKGDESLAELRYIIRDHDREKFEEKKRQFQSAADRLNEKYrsGGAALEA 316
Cdd:PRK13381 234 ILMANDFISHFPRQeTPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINAKY--PTARVSL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 317 KLTDSYYNMKEKLEPYPYLIDCAKEAFRSCGVKPETLPIRGGTDGAKLSFMGLPCPNLSTGGENYHGIYEYLNINSMEKM 396
Cdd:PRK13381 312 TLTDQYSNISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKS 391
|
410
....*....|
gi 496507077 397 VEVLKKLTEE 406
Cdd:PRK13381 392 YEVTITICLL 401
|
|
| peptidase-T |
TIGR01882 |
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has ... |
2-405 |
2.46e-151 |
|
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: 434.32 E-value: 2.46e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 2 KVLDRLVSYVKVDTQSSEESGTHPSTEKQFVLARQLERELRELGADDVRLSEHC-YVYARIPSNLSAEenmhTPTLGLIA 80
Cdd:TIGR01882 4 ELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEKNgYVIATIPSNTDKD----VPTIGFLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 81 HMDTSpSASGKDVKPRVIKSYDG-SPIPLGHGAI-LDPGIFPQLLSAKGDDLLVTDGSTLLGADDKAGVAEIMQCIEELL 158
Cdd:TIGR01882 80 HVDTA-DFNGENVNPQIIENYDGeSIIQLGDLEFtLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAADYLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 159 SQPERRHGEICIAFTPDEEIGSGADFFDLAGFGAEVAYTVDGGTLGGIEYENFNAASAVLTIHGVNVHPGSAKDKMLNAL 238
Cdd:TIGR01882 159 NHPEIKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 239 LIAMEFNALLPPC-TPANTEGYEGFFHLMSMKGDESLAELRYIIRDHDREKFEEKKRQFQSAADRLNEKYrsGGAALEAK 317
Cdd:TIGR01882 239 QIAIDLHNLLPEDdRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEY--GQDRIKLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 318 LTDSYYNMKEKLEPYPYLIDCAKEAFRSCGVKPETLPIRGGTDGAKLSFMGLPCPNLSTGGENYHGIYEYLNINSMEKMV 397
Cdd:TIGR01882 317 MNDQYYNMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAV 396
|
....*...
gi 496507077 398 EVLKKLTE 405
Cdd:TIGR01882 397 DVIVEIAK 404
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
3-406 |
3.10e-112 |
|
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: 334.73 E-value: 3.10e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 3 VLDRLVSYVKVDTQSSEESGTHPSTEKQFVLARQLERELRELGADDVRLSEHCYVYARIPSNLSAEenmhTPTLGLIAHM 82
Cdd:cd05645 1 LLERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEKGTLIATLPANVDGD----IPAIGFISHV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 83 DTSPSASGKDVKPRVIKSYDGSPIPLGHG-AILDPGIFPQLLSAKGDDLLVTDGSTLLGADDKAGVAEIMQCIEELLSQP 161
Cdd:cd05645 77 DTSPDGSGKNVNPQIVENYRGGDIALGIGdEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 162 eRRHGEICIAFTPDEEIGSGADFFDLAGFGAEVAYTVDGGTLGGIEYENFNAASAVLTIHGVNVHPGSAKDKMLNALLIA 241
Cdd:cd05645 157 -IPHGDIEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 242 MEFNALLPPC-TPANTEGYEGFFHLMSMKGDESLAELRYIIRDHDREKFEEKKRQFQSAADRLNEKYRSGGAAlEAKLTD 320
Cdd:cd05645 236 ARIHAEVPADeSPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVGKGLHPDCYI-ELVIED 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 321 SYYNMKEKLEPYPYLIDCAKEAFRSCGVKPETLPIRGGTDGAKLSFMGLPCPNLSTGGENYHGIYEYLNINSMEKMVEVL 400
Cdd:cd05645 315 SYYNFREKVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVI 394
|
....*.
gi 496507077 401 KKLTEE 406
Cdd:cd05645 395 VRIAEL 400
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
2-405 |
4.83e-35 |
|
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: 132.75 E-value: 4.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 2 KVLDRLVSYVKVDTQSSEESGthpstekqfvLARQLERELRELG----ADDVRLSEHC--YVYARIPSNLSaeenmhTPT 75
Cdd:TIGR01883 1 RLKKYFLELIQIDSESGKEKA----------ILTYLKKQITKLGipvsLDEVPAEVSNdnNLIARLPGTVK------FDT 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 76 LGLIAHMDTSPSASGkdVKPRViksydgspiplghgailDPGIFpqllsakgddllVTDGSTLLGADDKAGVAEIMQCIe 155
Cdd:TIGR01883 65 IFFCGHMDTVPPGAG--PEPVV-----------------EDGIF------------TSLGGTILGADDKAGVAAMLEAM- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 156 ELLSQPERRHGEICIAFTPDEEIG-SGADFFDLAGFGAEVAYTVD-GGTLGGIEYENFNAASAVLTIHGVNVHPGSAKDK 233
Cdd:TIGR01883 113 DVLSTEETPHGTIEFIFTVKEELGlIGMRLFDESKITAAYGYCLDaPGEVGNIQLAAPTQVKVDATIAGKDAHAGLVPED 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 234 MLNALLIAMEFNALLPPC-----TPANTEGYEGffhlmsMKGDESLAELRYIIRDHDREKFEEKKRQFQSAADRLNEKYR 308
Cdd:TIGR01883 193 GISAISVARMAIHAMRLGrideeTTANIGSFSG------GVNTNIVQDEQLIVAEARSLSFRKAEAQVQTMRERFEQAAE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 309 SGGAALEAKLTDSYYNMkeKLEPYPYLIDCAKEAFRSCGVKPETLPIRGGTDGAKLSFMGLPCPNLSTGGENYHGIYEYL 388
Cdd:TIGR01883 267 KYGATLEEETRLIYEGF--KIHPQHPLMNIFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETI 344
|
410
....*....|....*..
gi 496507077 389 NINSMEKMVEVLKKLTE 405
Cdd:TIGR01883 345 SIEQLVKLAELVIALAE 361
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
5-406 |
3.70e-24 |
|
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: 102.53 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 5 DRLVS----YVKVDTQSSEESGTHPSTEKQFVlarQLERELRELGADDVRLSEHCYVYARIPSNLSaeenmHTPTLGLIA 80
Cdd:cd05683 3 DRLINtfleLVQIDSETLHEKEISKVLKKKFE---NLGLSVIEDDAGKTTGGGAGNLICTLKADKE-----EVPKILFTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 81 HMDT-SPsasGKDVKPRVIKsydgspiplghgaildpgifpqllsakgDDLLVTDGSTLLGADDKAGVAEIMQCIEELLS 159
Cdd:cd05683 75 HMDTvTP---GINVKPPQIA----------------------------DGYIYSDGTTILGADDKAGIAAILEAIRVIKE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 160 QPErRHGEICIAFTPDEEIG-SGADFFDLAGFGAEVAYTVDG-GTLGGIEYENFNAASAVLTIHGVNVHPGSAKDKMLNA 237
Cdd:cd05683 124 KNI-PHGQIQFVITVGEESGlVGAKALDPELIDADYGYALDSeGDVGTIIVGAPTQDKINAKIYGKTAHAGTSPEKGISA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 238 LLIAMEFNALLP-----PCTPANTEGYEGffhlmsmkGDES--LAELRYII---RDHDREKFEEKKRQFQSAADRLNEKY 307
Cdd:cd05683 203 INIAAKAISNMKlgridEETTANIGKFQG--------GTATniVTDEVNIEaeaRSLDEEKLDAQVKHMKETFETTAKEK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 308 rsgGAALEAKLTDSY--YNMKEKLEpypyLIDCAKEAFRSCGVKPETLPIRGGTDGAKLSFMGLPCPNLSTGGENYHGIY 385
Cdd:cd05683 275 ---GAHAEVEVETSYpgFKINEDEE----VVKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTN 347
|
410 420
....*....|....*....|.
gi 496507077 386 EYLNINSMEKMVEVLKKLTEE 406
Cdd:cd05683 348 ERIPIEDLYDTAVLVVEIIKE 368
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
3-407 |
2.00e-21 |
|
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: 94.95 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 3 VLDRLVSYVKVDTQSSEESGthpstekqfvLARQLERELRELGADDVRLS---EHCYVYARIPSNLSAeenmhtPTLGLI 79
Cdd:COG0624 14 ALELLRELVRIPSVSGEEAA----------AAELLAELLEALGFEVERLEvppGRPNLVARRPGDGGG------PTLLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 80 AHMDTspsasgkdVKPRVIKSYDGSPIPLghgaildpgifpqllsakgddllVTDGSTLLG---ADDKAGVAEIMQCIEE 156
Cdd:COG0624 78 GHLDV--------VPPGDLELWTSDPFEP-----------------------TIEDGRLYGrgaADMKGGLAAMLAALRA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 157 LLSQPERRHGEICIAFTPDEEIGS-GADFF---DLAGFGAEVAYTVDGGTLGGIEYENFNAASAVLTIHGVNVHpGSAKD 232
Cdd:COG0624 127 LLAAGLRLPGNVTLLFTGDEEVGSpGARALveeLAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAH-SSRPE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 233 KMLNALLIAMEF-------------NALLPPCTpANTEGYEGffhlmsmkGDE-----SLAELRYIIR---DHDREKFEE 291
Cdd:COG0624 206 LGVNAIEALARAlaalrdlefdgraDPLFGRTT-LNVTGIEG--------GTAvnvipDEAEAKVDIRllpGEDPEEVLA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 292 K-KRQFQSAADRLNEKYRSGGAALEAKLTDsyynmkeklEPYPyLIDCAKEAFRS-CGVKPETLPIRGGTDGAKLS-FMG 368
Cdd:COG0624 277 AlRALLAAAAPGVEVEVEVLGDGRPPFETP---------PDSP-LVAAARAAIREvTGKEPVLSGVGGGTDARFFAeALG 346
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 496507077 369 LPCPNLSTG-GENYHGIYEYLNINSMEKMVEVLKKLTEEM 407
Cdd:COG0624 347 IPTVVFGPGdGAGAHAPDEYVELDDLEKGARVLARLLERL 386
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
141-406 |
2.61e-13 |
|
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: 70.07 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 141 ADDKAGVAEIMQCIEELLSQPERRhGEICIAFTPDEEIGSG-------ADFFDLAGFGAEVAYTVDGGTL----GGIEYE 209
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEGLKK-GTVKLLFQPDEEGGMGgaralieDGLLEREKVDAVFGLHIGEPTLleggIAIGVV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 210 NFNAASA--VLTIHGVNVH---PGSAKdkmlNALLIAMEF-NALLPPCTPANTEGYEGFFHLMSMKGDE-------SLAE 276
Cdd:pfam01546 112 TGHRGSLrfRVTVKGKGGHastPHLGV----NAIVAAARLiLALQDIVSRNVDPLDPAVVTVGNITGIPggvnvipGEAE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 277 LRYIIRDHDREKFEEKKRQFQSAADRLNEKYrsgGAALEAKLTDSYYNMKEKLEPypyLIDCAKEAFRS-CGVKPETL-- 353
Cdd:pfam01546 188 LKGDIRLLPGEDLEELEERIREILEAIAAAY---GVKVEVEYVEGGAPPLVNDSP---LVAALREAAKElFGLKVELIvs 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 496507077 354 PIRGGTDGAklsFMGLPCPN----LSTGGENYHGIYEYLNINSMEKMVEVLKKLTEE 406
Cdd:pfam01546 262 GSMGGTDAA---FFLLGVPPtvvfFGPGSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
3-394 |
2.62e-11 |
|
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: 64.53 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 3 VLDRLVSYVKVdtqsseESGTHPSTEKQFVlARQLERELRELGADDVR--LSEHC-YVYARIPSNLSaeenmhtPTLGLI 79
Cdd:cd03885 1 MLDLLERLVNI------ESGTYDKEGVDRV-AELLAEELEALGFTVERrpLGEFGdHLIATFKGTGG-------KRVLLI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 80 AHMDTS-PSASGKDVKPRViksyDGspiplghGAILDPGIfpqllsakgddllvtdgstllgADDKAGVAEIMQCIEELL 158
Cdd:cd03885 67 GHMDTVfPEGTLAFRPFTV----DG-------DRAYGPGV----------------------ADMKGGLVVILHALKALK 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 159 SQPERRHGEICIAFTPDEEIGS------------GADffdlAGFGAEVAytVDGGTL-----GGIEYenfnaasaVLTIH 221
Cdd:cd03885 114 AAGGRDYLPITVLLNSDEEIGSpgsrelieeeakGAD----YVLVFEPA--RADGNLvtarkGIGRF--------RLTVK 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 222 GVNVHPGSAKDKMLNALL----IAMEFNALLPPC-------------TPANTegyegffhlmsmKGDESLAE--LRYiIR 282
Cdd:cd03885 180 GRAAHAGNAPEKGRSAIYelahQVLALHALTDPEkgttvnvgvisggTRVNV------------VPDHAEAQvdVRF-AT 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 283 DHDREKFEEKKRQFQSAADRlnekyrsGGAALEAKLTDSYYNMkEKLEPYPYLIDCAKEAFRSCGVKPETLPIRGGTDGA 362
Cdd:cd03885 247 AEEADRVEEALRAIVATTLV-------PGTSVELTGGLNRPPM-EETPASRRLLARAQEIAAELGLTLDWEATGGGSDAN 318
|
410 420 430
....*....|....*....|....*....|....*
gi 496507077 363 KLSFMGLpcPNL-STG--GENYHGIYEYLNINSME 394
Cdd:cd03885 319 FTAALGV--PTLdGLGpvGGGAHTEDEYLELDSLV 351
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
11-403 |
3.13e-10 |
|
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.
Pssm-ID: 349944 [Multi-domain] Cd Length: 361 Bit Score: 61.16 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 11 VKVDTQSSEESGThpstekQFVLARQLERelRELGADDVRLSEHCYVYARIPSNlsaeenmHTPTLGLIAHMDTspsasg 90
Cdd:cd08659 7 VQIPSVNPPEAEV------AEYLAELLAK--RGYGIESTIVEGRGNLVATVGGG-------DGPVLLLNGHIDT------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 91 kdVKPRVIKSYDGSPiplghgaildpgifpqlLSAK-GDDLLVTDGStllgADDKAGVAEIMQCIEELLSQPERRHGEIC 169
Cdd:cd08659 66 --VPPGDGDKWSFPP-----------------FSGRiRDGRLYGRGA----CDMKGGLAAMVAALIELKEAGALLGGRVA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 170 IAFTPDEEIGS-GADFFDLAGFGAEVAYTVDG---------GTLGGIEYEnfnaasavLTIHGVNVHpGSAKDKMLNALL 239
Cdd:cd08659 123 LLATVDEEVGSdGARALLEAGYADRLDALIVGeptgldvvyAHKGSLWLR--------VTVHGKAAH-SSMPELGVNAIY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 240 IAMEF-NAL--LPPCTPANTEGYEGFFHLMSMKG--------DEslAELRYIIRDHDREKFEEKKRQFQSAADRLNEKYR 308
Cdd:cd08659 194 ALADFlAELrtLFEELPAHPLLGPPTLNVGVINGgtqvnsipDE--ATLRVDIRLVPGETNEGVIARLEAILEEHEAKLT 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 309 sggaaLEAKLTDSYYNMKEKLEPypyLIDCAKEAFRSCGVKPETLPIRGGTDGAKLS-FMGLPC----P-NLSTGgenyH 382
Cdd:cd08659 272 -----VEVSLDGDPPFFTDPDHP---LVQALQAAARALGGDPVVRPFTGTTDASYFAkDLGFPVvvygPgDLALA----H 339
|
410 420
....*....|....*....|.
gi 496507077 383 GIYEYLNINSMEKMVEVLKKL 403
Cdd:cd08659 340 QPDEYVSLEDLLRAAEIYKEI 360
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
208-308 |
5.01e-10 |
|
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: 56.59 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 208 YENFNAASAVLTIHGVNVHPGsAKDKMLNALLIAMEF-----------NALLPPCTPANTEGYEGFfhlmSMKGDESLAE 276
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSG-APGKGVNAIKLLARLlaelpaeygdiGFDFPRTTLNITGIEGGT----ATNVIPAEAE 75
|
90 100 110
....*....|....*....|....*....|..
gi 496507077 277 LRYIIRDHDREKFEEKKRQFQSAADRLNEKYR 308
Cdd:pfam07687 76 AKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
74-199 |
6.65e-10 |
|
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: 58.21 E-value: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 74 PTLGLIAHMDTspsasgkdvkprviksydgspIPLGHGAILDPGIFPqllsakgDDLLVTDGSTLLGADDKAGVAEIMQC 153
Cdd:cd03873 13 KSVALGAHLDV---------------------VPAGEGDNRDPPFAE-------DTEEEGRLYGRGALDDKGGVAAALEA 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 496507077 154 IEELLSQPERRHGEICIAFTPDEEIGSGADFFDLAGFGAEVAYTVD 199
Cdd:cd03873 65 LKRLKENGFKPKGTIVVAFTADEEVGSGGGKGLLSKFLLAEDLKVD 110
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
74-400 |
1.08e-09 |
|
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 57.83 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 74 PTLGLIAHMDTspsasgkdvkprviksydgspIPLGHGAILDPGIFPqllsakgDDLLVTDGSTLLGADDKAGVAEIMQC 153
Cdd:cd18669 13 KRVLLGAHIDV---------------------VPAGEGDPRDPPFFV-------DTVEEGRLYGRGALDDKGGVAAALEA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 154 IEELLSQPERRHGEICIAFTPDEEIGSGADFFDLAGFGAevaytvdggtlggieyENFNAASAVLTIHGVNVHpgsakdk 233
Cdd:cd18669 65 LKLLKENGFKLKGTVVVAFTPDEEVGSGAGKGLLSKDAL----------------EEDLKVDYLFVGDATPAP------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 234 mlnalliamefnallppctpantegyegffhlmsmkgdeslaelryiirdhdrekfeekkrqfqsaadrlnekyrSGGAA 313
Cdd:cd18669 122 ---------------------------------------------------------------------------QKGVG 126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 314 LEAKltdsyynmkeklepypyLIDCAKEAFRSCGVKPETL-PIRGGTDGAKLSFMGLPCPNLSTGGE-NYHGIYEYLNIN 391
Cdd:cd18669 127 IRTP-----------------LVDALSEAARKVFGKPQHAeGTGGGTDGRYLQELGIPGVTLGAGGGkGAHSPNERVNLE 189
|
....*....
gi 496507077 392 SMEKMVEVL 400
Cdd:cd18669 190 DLESALAVL 198
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
3-239 |
1.05e-08 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 56.56 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 3 VLDRLVSYVKVDTQSSEESGThpsteKQfvLARQLERELRELGADdVRlsehcyvyaRIPSNLSAEENMHTPTLG----- 77
Cdd:PRK06133 39 YLDTLKELVSIESGSGDAEGL-----KQ--VAALLAERLKALGAK-VE---------RAPTPPSAGDMVVATFKGtgkrr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 78 --LIAHMDTSPSASGKDVKPRVIKSydgspiplghGAILDPGIfpqllsakgddllvtdgstllgADDKAGVAEIMQCIE 155
Cdd:PRK06133 102 imLIAHMDTVYLPGMLAKQPFRIDG----------DRAYGPGI----------------------ADDKGGVAVILHALK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 156 ELLSQPERRHGEICIAFTPDEEIGSGADFFDLAGFGAEVAYTV--------DGGTLG--GIeyenfnaASAVLTIHGVNV 225
Cdd:PRK06133 150 ILQQLGFKDYGTLTVLFNPDEETGSPGSRELIAELAAQHDVVFscepgrakDALTLAtsGI-------ATALLEVKGKAS 222
|
250
....*....|....
gi 496507077 226 HPGSAKDKMLNALL 239
Cdd:PRK06133 223 HAGAAPELGRNALY 236
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
1-409 |
1.86e-06 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 49.77 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 1 MKVLDRLVSYVKVDTQSSEESGTHPSTEkqfvlARQLERELRELGADDVRLSEHCYVYAripsnLSAEENMHTPTLGLIA 80
Cdd:PRK08554 1 MDVLELLSSLVSFETVNDPSKGIKPSKE-----CPKFIKDTLESWGIESELIEKDGYYA-----VYGEIGEGKPKLLFMA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 81 HMDTSPSASGKdvkprviKSYDgspiplghgaildpgifPQLLSAKGDDLLvTDGStllgADDKAGVAEIMQCIEELLSQ 160
Cdd:PRK08554 71 HFDVVPVNPEE-------WNTE-----------------PFKLTVKGDKAY-GRGS----ADDKGNVASVMLALKELSKE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 161 PERrhGEICIAFTPDEEIGsGADFFDLA-----------------------------GFGAEV-AYTVDGGTLGGIEYEN 210
Cdd:PRK08554 122 PLN--GKVIFAFTGDEEIG-GAMAMHIAeklreegklpkyminadgigmkpiirrrkGFGVTIrVPSEKVKVKGKLREQT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 211 FNAASAVL-TIH------GVNVHPGSAKDKML---NALLIAMEFNALLPPCTPANT--------EGYEGffhlmsmKGDE 272
Cdd:PRK08554 199 FEIRTPVVeTRHaayflpGVDTHPLIAASHFLresNVLAVSLEGKFLKGNVVPGEVtltylepgEGEEV-------EVDL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 273 SLAEL--------RYIIRdhdREK--------------FEEKKRQFQ---SAADRLNEKY-RSGGAALEAKLTDSYYNMK 326
Cdd:PRK08554 272 GLTRLlkaivplvRAPIK---AEKysdygvsitpnvysFAEGKHVLKldiRAMSYSKEDIeRTLKEVLEFNLPEAEVEIR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 327 EK-------LEPYPYLIDCAKEAFRSCGVKPETLPIRGGTDGAKLSFMGLPCPNLSTGGENYHGIYEYLNINSMEKMVEV 399
Cdd:PRK08554 349 TNekagylfTPPDEEIVKVALRVLKELGEDAEPVEGPGASDSRYFTPYGVKAIDFGPKGGNIHGPNEYVEIDSLKKMPEV 428
|
490
....*....|
gi 496507077 400 LKKLTEEMIG 409
Cdd:PRK08554 429 YKRIALRLLG 438
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
142-405 |
1.17e-05 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 47.06 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 142 DDKAGVAEIMQCIEELLSQPERRhgEICIAFTPDEEIGS-GADFFdLAGFGAEVAYTVDGgTLGGIEYENFNAASAVLTI 220
Cdd:PRK08652 87 DAKGGVAAILLALEELGKEFEDL--NVGIAFVSDEEEGGrGSALF-AERYRPKMAIVLEP-TDLKVAIAHYGNLEAYVEV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 221 HGVNVHpGSAKDKMLNALLIAMEFNALLPPCTPANTEGYEGFFHLMSMKGDES------LAELRYIIRDHDREKFEEKKR 294
Cdd:PRK08652 163 KGKPSH-GACPESGVNAIEKAFEMLEKLKELLKALGKYFDPHIGIQEIIGGSPeysipaLCRLRLDARIPPEVEVEDVLD 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 295 QFQSAADRLNEKYRSggaaleAKLTDSYYnmkekLEPYPYLIDCAKEAFRSCGVKPETLPIRGGTDGAKLSFMGLPCPNL 374
Cdd:PRK08652 242 EIDPILDEYTVKYEY------TEIWDGFE-----LDEDEEIVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTKTVVW 310
|
250 260 270
....*....|....*....|....*....|..
gi 496507077 375 STGGENY-HGIYEYLNINSMEKMVEVLKKLTE 405
Cdd:PRK08652 311 GPGELDLcHTKFERIDVREVEKAKEFLKALNE 342
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
134-244 |
8.72e-04 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 41.10 E-value: 8.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 134 DGSTLLG---ADDKAGVAEIMQCIEELLSQPERRHGEICIAFTPDEEIGS--GADFFDLAGFGAEVAYTVD----GGTLG 204
Cdd:PRK07338 118 DDGTLNGpgvADMKGGIVVMLAALLAFERSPLADKLGYDVLINPDEEIGSpaSAPLLAELARGKHAALTYEpalpDGTLA 197
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 496507077 205 GIEyenfnAASAVLTI--HGVNVHPGSAKDKMLNALLIAMEF 244
Cdd:PRK07338 198 GAR-----KGSGNFTIvvTGRAAHAGRAFDEGRNAIVAAAEL 234
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
128-248 |
1.79e-03 |
|
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: 40.20 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 128 DDLLVTDGSTLlGADDKAGVAEIMQcieeLLSQPERRHGEICIAFTPDEEIG-SGADFFDL------------------- 187
Cdd:cd03890 94 GDWLKATGTTL-GADNGIGVAYALA----ILEDKDIEHPPLEVLFTVDEETGmTGALGLDPsllkgkillnldseeegel 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496507077 188 ----AGfGAEVAYTVDggtlggIEYENFNAASAVLTIH---------GVNVHPGSAK-DKMLNALL--IAMEFNALL 248
Cdd:cd03890 169 tvgcAG-GIDVTITLP------IEREEAEGGYTGLKITvkglkgghsGVDIHKGRANaNKLMARLLyeLAKELDFRL 238
|
|
| M42_glucanase_like |
cd05657 |
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ... |
142-205 |
3.18e-03 |
|
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1,4-beta-glucanase or endoglucanase)-like subfamily. Proteins in this subfamily are co-catalytic metallopeptidases, found in archaea and bacteria. They show similarity to cellulase and endo-1,4-beta-glucanase (endoglucanase) which typically bind two zinc or cobalt atoms. Some of the enzymes exhibit typical aminopeptidase specificity, whereas others are also capable of N-terminal deblocking activity, i.e. hydrolyzing acylated N-terminal residues. Many of these enzymes are assembled either as tetrahedral dodecamers or as octahedral tetracosameric structures, with the active site located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers.
Pssm-ID: 349907 [Multi-domain] Cd Length: 337 Bit Score: 39.18 E-value: 3.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496507077 142 DDKAGVAEIMQCIEELLSQPERRHGEICIAFTPDEEIGSGADFFdLAGFGAE-VAytVDGGTLGG 205
Cdd:cd05657 181 DDKASVAILLALARALKENKLKLPVDTHFLFSNYEEVGHGASFA-PPEDTDElLA--VDMGPVGP 242
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
134-217 |
5.91e-03 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 38.78 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496507077 134 DGSTLLG---ADDKAGVAEIMQCIEELLS---QPERrhgEICIAFTPDEEIG--SGADF---FDLAGFGAE-VAYTVDGG 201
Cdd:cd05674 101 DGGYIWGrgaLDDKNSLIGILEAVELLLKrgfKPRR---TIILAFGHDEEVGgeRGAGAiaeLLLERYGVDgLAAILDEG 177
|
90
....*....|....*.
gi 496507077 202 tLGGIEYENFNAASAV 217
Cdd:cd05674 178 -GAVLEGVFLGVPFAL 192
|
|
| |
