|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 673.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 4 LVERFLTYVKVNTRSDANSQTTPTTVGQVVLAKMIETELHELGLADVHYNEqNGFLTARLPGNQ-PAAKSIGLIAHLDTA 82
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDE-HGYVTATLPANVdKDVPTIGFIAHMDTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 83 DF-SAENIRPQVITNYDGQDVLLNqEQGIVLSVAEFPNLKEYQGETLITTDGTTLLGADDKAGIVEILAAVEYFLAHPEV 161
Cdd:cd03892 80 PDnSGKNVKPQIIENYDGGDIVLN-ESGIVLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIEHPEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 162 ARGDVWLAFGPDEEIGRGADQFDAPNFPVAFAYTIDSGRVGHFEYETFNAAQAVITIDGTSVHPGTAYGSLVNAIKLGEQ 241
Cdd:cd03892 159 KHGDIRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 242 LDQSLPQKEVPEQTRGNEGFYLLNKFTGSIEKAELVYIIRDHDRENFQARKQFLEKQVQRLNALADKPRLTITFQDQYYN 321
Cdd:cd03892 239 FHSMLPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKYGEGRVELEIKDQYYN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 322 MKEIIENDWTPVELAVQAMESCDIEPIITPFRGGTDGSKISFMGIPTPNLFTGGENFHGQYEFITVESMAKAVQTIIAII 401
Cdd:cd03892 319 MKEKIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIVKIA 398
|
..
gi 1635061248 402 RL 403
Cdd:cd03892 399 EL 400
|
|
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
1-405 |
0e+00 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 663.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 1 MEKLVERFLTYVKVNTRSDANSQTTPTTVGQVVLAKMIETELHELGLADVHYNEqNGFLTARLPGN-QPAAKSIGLIAHL 79
Cdd:PRK05469 1 MDKLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDE-NGYVMATLPANvDKDVPTIGFIAHM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 80 DTA-DFSAENIRPQVITNYDGQDVLLNQEqGIVLSVAEFPNLKEYQGETLITTDGTTLLGADDKAGIVEILAAVEYFLAH 158
Cdd:PRK05469 80 DTApDFSGKNVKPQIIENYDGGDIALGDG-NEVLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYLIAH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 159 PEVARGDVWLAFGPDEEIGRGADQFDAPNFPVAFAYTIDSGRVGHFEYETFNAAQAVITIDGTSVHPGTAYGSLVNAIKL 238
Cdd:PRK05469 159 PEIKHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 239 GEQLDQSLPQKEVPEQTRGNEGFYLLNKFTGSIEKAELVYIIRDHDRENFQARKQFLEKQVQRLNALADKPRLTITFQDQ 318
Cdd:PRK05469 239 AADFHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKYGEGRVELEIKDQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 319 YYNMKEIIENDWTPVELAVQAMESCDIEPIITPFRGGTDGSKISFMGIPTPNLFTGGENFHGQYEFITVESMAKAVQTII 398
Cdd:PRK05469 319 YYNMREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVIV 398
|
....*..
gi 1635061248 399 AIIRLNA 405
Cdd:PRK05469 399 EIAELTA 405
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
2-406 |
0e+00 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 618.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 2 EKLVERFLTYVKVNTRSDANSQTTPTTVGQVVLAKMIETELHELGLADVhYNEQNGFLTARLPGNQPAAKSIGLIAHLDT 81
Cdd:PRK13381 1 MQLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDI-VIDEHAIVTAKLPGNTPGAPRIGFIAHLDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 82 ADFSAE-NIRPQVITnYDGQDVLLNQEQGIVLSVAEFPNLKEYQGETLITTDGTTLLGADDKAGIVEILAAVEYFLAHpE 160
Cdd:PRK13381 80 VDVGLSpDIHPQILR-FDGGDLCLNAEQGIWLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLENLTEN-E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 161 VARGDVWLAFGPDEEIG-RGADQFDAPNFPVAFAYTIDSGRVGHFEYETFNAAQAVITIDGTSVHPGTAYGSLVNAIKLG 239
Cdd:PRK13381 158 VEHGDIVVAFVPDEEIGlRGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNPILMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 240 EQLDQSLPQKEVPEQTRGNEGFYLLNKFTGSIEKAELVYIIRDHDRENFQARKQFLEKQVQRLNALADKPRLTITFQDQY 319
Cdd:PRK13381 238 NDFISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINAKYPTARVSLTLTDQY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 320 YNMKEIIENDWTPVELAVQAMESCDIEPIITPFRGGTDGSKISFMGIPTPNLFTGGENFHGQYEFITVESMAKAVQTIIA 399
Cdd:PRK13381 318 SNISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEVTIT 397
|
....*..
gi 1635061248 400 IIRLNAN 406
Cdd:PRK13381 398 ICLLAAK 404
|
|
| peptidase-T |
TIGR01882 |
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has ... |
2-405 |
0e+00 |
|
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: 509.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 2 EKLVERFLTYVKVNTRSDANSQTTPTTVGQVVLAKMIETELHELGLADVHYNEQNGFLTARLPGN-QPAAKSIGLIAHLD 80
Cdd:TIGR01882 3 EELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEKNGYVIATIPSNtDKDVPTIGFLAHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 81 TADFSAENIRPQVITNYDGQDVLLNQEQGIVLSVAEFPNLKEYQGETLITTDGTTLLGADDKAGIVEILAAVEYFLAHPE 160
Cdd:TIGR01882 83 TADFNGENVNPQIIENYDGESIIQLGDLEFTLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAADYLINHPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 161 VARGDVWLAFGPDEEIGRGADQFDAPNFPVAFAYTIDSGRVGHFEYETFNAAQAVITIDGTSVHPGTAYGSLVNAIKLGE 240
Cdd:TIGR01882 163 IKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAAQIAI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 241 QLDQSLPQKEVPEQTRGNEGFYLLNKFTGSIEKAELVYIIRDHDRENFQARKQFLEKQVQRLNALADKPRLTITFQDQYY 320
Cdd:TIGR01882 243 DLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEYGQDRIKLDMNDQYY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 321 NMKEIIENDWTPVELAVQAMESCDIEPIITPFRGGTDGSKISFMGIPTPNLFTGGENFHGQYEFITVESMAKAVQTIIAI 400
Cdd:TIGR01882 323 NMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDVIVEI 402
|
....*
gi 1635061248 401 IRLNA 405
Cdd:TIGR01882 403 AKLNE 407
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
1-405 |
1.97e-152 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 435.25 E-value: 1.97e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 1 MEKLVERFLTYVKVNTRSDAnsqttpttvgQVVLAKMIETELHELGLaDVHYNEqNGFLTARLPGNQP-AAKSIGLIAHL 79
Cdd:COG2195 2 PERLLERFLEYVKIPTPSDH----------EEALADYLVEELKELGL-EVEEDE-AGNVIATLPATPGyNVPTIGLQAHM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 80 DTA-DFSAENIRPQVitnyDGQdvllnqeqgivlsvaefpnlkeyqgetLITTDGTTLLGADDKAGIVEILAAVEYfLAH 158
Cdd:COG2195 70 DTVpQFPGDGIKPQI----DGG---------------------------LITADGTTTLGADDKAGVAAILAALEY-LKE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 159 PEVARGDVWLAFGPDEEIG-RGADQFDAPNFPVAFAYTIDSGRVGHFEYETFNAAQAVITIDGTSVHPGTAYGSLVNAIK 237
Cdd:COG2195 118 PEIPHGPIEVLFTPDEEIGlRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 238 LGEQLDQSLPQKEVPEQTRGNEGFYLLNKFT-GSIEKAELVYIIRDHDRENFQARKQFLEKQVQRLNALADKPRLTITFQ 316
Cdd:COG2195 198 LAARFLAALPLGRIPEETEGNEGFIHGGSATnAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGVGVVEVEIE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 317 DQYYNMKEiiENDWTPVELAVQAMESCDIEPIITPFRGGTDGSKISFMGIPTPNLFTGGENFHGQYEFITVESMAKAVQT 396
Cdd:COG2195 278 DQYPNWKP--EPDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWEL 355
|
....*....
gi 1635061248 397 IIAIIRLNA 405
Cdd:COG2195 356 LVEILKLIA 364
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
4-403 |
7.21e-102 |
|
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: 307.77 E-value: 7.21e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 4 LVERFLTYVKVNTRSDANSQTTPTTVGQVVLAKMIETELHELGLADVHYNEQnGFLTARLPGN-QPAAKSIGLIAHLDTA 82
Cdd:cd05645 1 LLERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEK-GTLIATLPANvDGDIPAIGFISHVDTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 83 -DFSAENIRPQVITNYDGQDVLLNQEQGiVLSVAEFPNLKEYQGETLITTDGTTLLGADDKAGIVEILAAVEYFLAHPeV 161
Cdd:cd05645 80 pDGSGKNVNPQIVENYRGGDIALGIGDE-VLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKN-I 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 162 ARGDVWLAFGPDEEIGRGADQFDAPNFPVAFAYTIDSGRVGHFEYETFNAAQAVITIDGTSVHPGTAYGSLVNAIKLGEQ 241
Cdd:cd05645 158 PHGDIEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 242 LDQSLPQKEVPEQTRGNEGFYLLNKFTGSIEKAELVYIIRDHDRENFQARKQFLEKQVQRL-NALADKPRLTITFQDQYY 320
Cdd:cd05645 238 IHAEVPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVgKGLHPDCYIELVIEDSYY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 321 NMKEIIENDWTPVELAVQAMESCDIEPIITPFRGGTDGSKISFMGIPTPNLFTGGENFHGQYEFITVESMAKAVQTIIAI 400
Cdd:cd05645 318 NFREKVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIVRI 397
|
...
gi 1635061248 401 IRL 403
Cdd:cd05645 398 AEL 400
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
2-402 |
5.78e-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: 5.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 2 EKLVERFLTYVKVNTRSDANSQttpttvgqvvLAKMIETELHELGL------ADVHYNEQNGFLTARLPGNQPAAKSIGL 75
Cdd:cd05683 3 DRLINTFLELVQIDSETLHEKE----------ISKVLKKKFENLGLsvieddAGKTTGGGAGNLICTLKADKEEVPKILF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 76 IAHLDTADfSAENIRPQVITNydgqdvllnqeqGIVLSvaefpnlkeyqgetlittDGTTLLGADDKAGIVEILAAVEYf 155
Cdd:cd05683 73 TSHMDTVT-PGINVKPPQIAD------------GYIYS------------------DGTTILGADDKAGIAAILEAIRV- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 156 LAHPEVARGDVWLAFGPDEEIGR-GADQFDAPNFPVAFAYTIDS-GRVGhfeyETFNAA--QAVI--TIDGTSVHPGTAY 229
Cdd:cd05683 121 IKEKNIPHGQIQFVITVGEESGLvGAKALDPELIDADYGYALDSeGDVG----TIIVGAptQDKInaKIYGKTAHAGTSP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 230 GSLVNAIKLGEQLDQSLPQKEVPEQTRGNEGfyllnKFTGSIEK---AELVYII---RDHDRENFQAR----KQFLEKQV 299
Cdd:cd05683 197 EKGISAINIAAKAISNMKLGRIDEETTANIG-----KFQGGTATnivTDEVNIEaeaRSLDEEKLDAQvkhmKETFETTA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 300 QRLNALADkprltITFQDQYYNMKeiIENDWTPVELAVQAMESCDIEPIITPFRGGTDGSKISFMGIPTPNLFTGGENFH 379
Cdd:cd05683 272 KEKGAHAE-----VEVETSYPGFK--INEDEEVVKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIH 344
|
410 420
....*....|....*....|...
gi 1635061248 380 GQYEFITVESMAKAVQTIIAIIR 402
Cdd:cd05683 345 TTNERIPIEDLYDTAVLVVEIIK 367
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
3-401 |
1.54e-27 |
|
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: 111.95 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 3 KLVERFLTYVKVNTRSDANSQttpttvgqvvLAKMIETELHELGLaDVHYNE-----QNGF-LTARLPGNQpAAKSIGLI 76
Cdd:TIGR01883 1 RLKKYFLELIQIDSESGKEKA----------ILTYLKKQITKLGI-PVSLDEvpaevSNDNnLIARLPGTV-KFDTIFFC 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 77 AHLDTADfSAENIRPQVitnydgqdvllnqEQGIvlsvaefpnlkeyqgetlITTDGTTLLGADDKAGIVEILAAVEYFl 156
Cdd:TIGR01883 69 GHMDTVP-PGAGPEPVV-------------EDGI------------------FTSLGGTILGADDKAGVAAMLEAMDVL- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 157 AHPEVARGDVWLAFGPDEEIG-RGADQFDAPNFPVAFAYTIDS-GRVGHFEYETFNAAQAVITIDGTSVHPGTAYGSLVN 234
Cdd:TIGR01883 116 STEETPHGTIEFIFTVKEELGlIGMRLFDESKITAAYGYCLDApGEVGNIQLAAPTQVKVDATIAGKDAHAGLVPEDGIS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 235 AIKLGEQLDQSLPQKEVPEQTRGNegfyllnkfTGSIEKAELVYIIRDHDRENFQARK---QFLEKQVQ----RLNALAD 307
Cdd:TIGR01883 196 AISVARMAIHAMRLGRIDEETTAN---------IGSFSGGVNTNIVQDEQLIVAEARSlsfRKAEAQVQtmreRFEQAAE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 308 K--PRLTITFQDQYYNMKeiIENDWTPVELAVQAMESCDIEPIITPFRGGTDGSKISFMGIPTPNLFTGGENFHGQYEFI 385
Cdd:TIGR01883 267 KygATLEEETRLIYEGFK--IHPQHPLMNIFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETI 344
|
410
....*....|....*.
gi 1635061248 386 TVESMAKAVQTIIAII 401
Cdd:TIGR01883 345 SIEQLVKLAELVIALA 360
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
34-402 |
1.04e-17 |
|
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: 84.17 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 34 LAKMIETELHELGL-ADVHYNEQN-GFLTARLPGNqPAAKSIGLIAHLDT---ADFSAENIRPqvitnydgqdvllnqeq 108
Cdd:COG0624 34 AAELLAELLEALGFeVERLEVPPGrPNLVARRPGD-GGGPTLLLYGHLDVvppGDLELWTSDP----------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 109 givlsvaeFPnlkeyqgetlITTDGTTLLG---ADDKAGIVEILAAVEYFLAHPEVARGDVWLAFGPDEEIG-RGADQF- 183
Cdd:COG0624 96 --------FE----------PTIEDGRLYGrgaADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGsPGARALv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 184 --DAPNFPVAFAYTIDSGRVGHFEYETFNAAQAVITIDGTSVHPGTaYGSLVNAI-KLGEQLdQSLpqKEVPEQTRGNEG 260
Cdd:COG0624 158 eeLAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAHSSR-PELGVNAIeALARAL-AAL--RDLEFDGRADPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 261 FYL----LNKFTGSI------EKAELVYIIRDHDRENFQARKQFLEKqvqRLNALADKPRLTITFQDQYYNMKEI-IEND 329
Cdd:COG0624 234 FGRttlnVTGIEGGTavnvipDEAEAKVDIRLLPGEDPEEVLAALRA---LLAAAAPGVEVEVEVLGDGRPPFETpPDSP 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1635061248 330 WtpVELAVQAMES-CDIEPIITPFRGGTDGSKIS-FMGIPTPNL-FTGGENFHGQYEFITVESMAKAVQTIIAIIR 402
Cdd:COG0624 311 L--VAAARAAIREvTGKEPVLSGVGGGTDARFFAeALGIPTVVFgPGDGAGAHAPDEYVELDDLEKGARVLARLLE 384
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
139-402 |
3.97e-12 |
|
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: 66.60 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 139 ADDKAGIVEILAAVEYFLAHPeVARGDVWLAFGPDEEIGRG-----ADQFDAPNFPVAFAYTIDSGR----VGHFEYETF 209
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEG-LKKGTVKLLFQPDEEGGMGgaralIEDGLLEREKVDAVFGLHIGEptllEGGIAIGVV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 210 NAAQAV----ITIDGTSVHpGTAYGSLVNAI-KLGEQLdQSLpQKEVPEQTRGNEGFYL----LNKFTGSI----EKAEL 276
Cdd:pfam01546 112 TGHRGSlrfrVTVKGKGGH-ASTPHLGVNAIvAAARLI-LAL-QDIVSRNVDPLDPAVVtvgnITGIPGGVnvipGEAEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 277 VYIIRDHDRENFQArkqfLEKQVQR-LNALADKPRLTITFqDQYYNMKEIIENDWTPVELAVQAMES---CDIEPIITPF 352
Cdd:pfam01546 189 KGDIRLLPGEDLEE----LEERIREiLEAIAAAYGVKVEV-EYVEGGAPPLVNDSPLVAALREAAKElfgLKVELIVSGS 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1635061248 353 RGGTDGSKISfMGIPtPNLF---TGGENFHGQYEFITVESMAKAVQTIIAIIR 402
Cdd:pfam01546 264 MGGTDAAFFL-LGVP-PTVVffgPGSGLAHSPNEYVDLDDLEKGAKVLARLLL 314
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
1-402 |
3.72e-10 |
|
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: 61.07 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 1 MEKLVERFltyVKVNTRSDansqttpTTVGQVVLAKMIETELHELGL-ADVHYNEQNG-FLTARLPGNQPaaKSIGLIAH 78
Cdd:cd03885 1 MLDLLERL---VNIESGTY-------DKEGVDRVAELLAEELEALGFtVERRPLGEFGdHLIATFKGTGG--KRVLLIGH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 79 LDTAdFSAEnirpqvitnydgqdvllnqeqgivlSVAEFPnlkeyqgetlITTDGTTLLG---ADDKAGIVEILAAVEYF 155
Cdd:cd03885 69 MDTV-FPEG-------------------------TLAFRP----------FTVDGDRAYGpgvADMKGGLVVILHALKAL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 156 LAHPEVARGDVWLAFGPDEEIG------------RGADqfdapnfpVAFAY-------TIDSGRVGhfeyetfnAAQAVI 216
Cdd:cd03885 113 KAAGGRDYLPITVLLNSDEEIGspgsrelieeeaKGAD--------YVLVFeparadgNLVTARKG--------IGRFRL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 217 TIDGTSVHPGTAYGSLVNAIK-LGEQLDQslpqkeVPEQTRGNEGFyLLNkfTGSIEKAELVYIIRDHDRENFQAR---- 291
Cdd:cd03885 177 TVKGRAAHAGNAPEKGRSAIYeLAHQVLA------LHALTDPEKGT-TVN--VGVISGGTRVNVVPDHAEAQVDVRfata 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 292 --KQFLEKQVQRLNALADKP--RLTITFQDQYYNMKEIIENDWTpVELAVQAMESCDIEPIITPFRGGTDGSKISFMGIP 367
Cdd:cd03885 248 eeADRVEEALRAIVATTLVPgtSVELTGGLNRPPMEETPASRRL-LARAQEIAAELGLTLDWEATGGGSDANFTAALGVP 326
|
410 420 430
....*....|....*....|....*....|....*..
gi 1635061248 368 TPNLFtG--GENFHGQYEFITVESMAKAVQTIIAIIR 402
Cdd:cd03885 327 TLDGL-GpvGGGAHTEDEYLELDSLVPRIKLLARLLM 362
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
61-203 |
4.99e-09 |
|
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: 55.89 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 61 ARLPGNQPAaKSIGLIAHLDTadfsaenirpqVITNydgqdvllnqeqgivlsvAEFPNLKEYQGETLITTDGTTLLGAD 140
Cdd:cd03873 4 ARLGGGEGG-KSVALGAHLDV-----------VPAG------------------EGDNRDPPFAEDTEEEGRLYGRGALD 53
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1635061248 141 DKAGIVEILAAVEYFLAHPEVARGDVWLAFGPDEEIGRGADQFDAPNFPVAFAYTIDSGRVGH 203
Cdd:cd03873 54 DKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVID 116
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
139-402 |
5.99e-09 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 57.31 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 139 ADDKAGIVEILAAVEYFlahPEVARGDVWLAFGPDEEI-GRGA----DQFDAPNFPVAFAYTIDSGRV--GHfeyetFNA 211
Cdd:PRK08651 113 SDMKGGIAALLAAFERL---DPAGDGNIELAIVPDEETgGTGTgylvEEGKVTPDYVIVGEPSGLDNIciGH-----RGL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 212 AQAVITIDGTSVHPGTAYgSLVNAI----KLGEQLDQSLPQKEVP---EQTRGNEGFYLLNKFTgsIEKAELVYIIRDH- 283
Cdd:PRK08651 185 VWGVVKVYGKQAHASTPW-LGINAFeaaaKIAERLKSSLSTIKSKyeyDDERGAKPTVTLGGPT--VEGGTKTNIVPGYc 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 284 ----DR-----ENfqaRKQFLEKQVQRLNALADKPRLTITFQDqyynmKEIIENDWT-PVELAVQAMESC-----DIEPI 348
Cdd:PRK08651 262 afsiDRrlipeET---AEEVRDELEALLDEVAPELGIEVEFEI-----TPFSEAFVTdPDSELVKALREAirevlGVEPK 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1635061248 349 ITPFRGGTDGSKISFMGIPTPNLFTGG-ENFHGQYEFITVESMAKAVQTIIAIIR 402
Cdd:PRK08651 334 KTISLGGTDARFFGAKGIPTVVYGPGElELAHAPDEYVEVKDVEKAAKVYEEVLK 388
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
206-308 |
6.83e-09 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 53.12 E-value: 6.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 206 YETFNAAQAVITIDGTSVHPGtAYGSLVNAIKLGEQLDQSLPQK----------EVPEQTRGNEGFyllnKFTGSIEKAE 275
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSG-APGKGVNAIKLLARLLAELPAEygdigfdfprTTLNITGIEGGT----ATNVIPAEAE 75
|
90 100 110
....*....|....*....|....*....|...
gi 1635061248 276 LVYIIRdhdRENFQARKQFLEKQVQRLNALADK 308
Cdd:pfam07687 76 AKFDIR---LLPGEDLEELLEEIEAILEKELPE 105
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
61-224 |
7.43e-08 |
|
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: 52.43 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 61 ARLPGNqPAAKSIGLIAHLDTADFSAEnirpqvitnydgqdvllnqeqgivlsvaeFPNLKEYQGETLITTDGTTLLGAD 140
Cdd:cd18669 4 ARYGGG-GGGKRVLLGAHIDVVPAGEG-----------------------------DPRDPPFFVDTVEEGRLYGRGALD 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 141 DKAGIVEILAAVEYFLAHPEVARGDVWLAFGPDEEIGRGADQFDAPNFPVAFAYTIDSgrvgHFEYETFNAAQAVITIDG 220
Cdd:cd18669 54 DKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEEVGSGAGKGLLSKDALEEDLKVDY----LFVGDATPAPQKGVGIRT 129
|
....
gi 1635061248 221 TSVH 224
Cdd:cd18669 130 PLVD 133
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
138-401 |
2.87e-06 |
|
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: 48.83 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 138 GADD-KAGIVEILAAVEYFLAHPEVARGDVWLAFGPDEEIG-RGADQFDA--PNFPVAFA-------YTIDSGRVGHFEY 206
Cdd:cd08659 92 GACDmKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGsDGARALLEagYADRLDALivgeptgLDVVYAHKGSLWL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 207 EtfnaaqavITIDGTSVH---PGTAygslVNAI-KLG------EQLDQSLPQKEVPEQTRGNEGFYLLNKFTGSI-EKAE 275
Cdd:cd08659 172 R--------VTVHGKAAHssmPELG----VNAIyALAdflaelRTLFEELPAHPLLGPPTLNVGVINGGTQVNSIpDEAT 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 276 LVYIIR---DHDRENFQAR-KQFLEKQVQRLNALADKPRLTITFQDQyynmkeiiENDWtpVELAVQAMESCDIEPIITP 351
Cdd:cd08659 240 LRVDIRlvpGETNEGVIARlEAILEEHEAKLTVEVSLDGDPPFFTDP--------DHPL--VQALQAAARALGGDPVVRP 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1635061248 352 FRGGTDGSKIS-FMGIPTPNLFTGGENF-HGQYEFITVESMAKAVQTIIAII 401
Cdd:cd08659 310 FTGTTDASYFAkDLGFPVVVYGPGDLALaHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
140-180 |
6.61e-05 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 44.93 E-value: 6.61e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1635061248 140 DDKAGIVEILAAVEYFLAHPEVARGDVWLAFGPDEEI-GRGA 180
Cdd:PRK08262 154 DDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVgGLGA 195
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
138-392 |
9.30e-05 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 44.31 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 138 GADD-KAGIVEILAAVEYFLAHPEVARGDVWLAFGPDEEIGR-GADQFDAPNF--PVAFAYTIDSGRVGHFEYETFNAAQ 213
Cdd:TIGR01910 102 GATDmKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEaGTLYLLQRGYfkDADGVLIPEPSGGDNIVIGHKGSIW 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 214 AVITIDGTSVH---PGTAYGSLVNAIKLGEQLdqslpQKEVPEQTRGNEGFYLLNKFT------------GSI-EKAELV 277
Cdd:TIGR01910 182 FKLRVKGKQAHasfPQFGVNAIMKLAKLITEL-----NELEEHIYARNSYGFIPGPITfnpgvikggdwvNSVpDYCEFS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 278 YIIRDHDRENFQARKQFLEKQVQRLNaladkprltitfQDQYYNMKEIIENDW------TPVELAVQAMESC-----DIE 346
Cdd:TIGR01910 257 IDVRIIPEENLDEVKQIIEDVVKALS------------KSDGWLYENEPVVKWsgpnetPPDSRLVKALEAIikkvrGIE 324
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1635061248 347 PIITPFRGGTDGSKISFMGIPTPNLFTG-GENFHGQYEFITVESMAK 392
Cdd:TIGR01910 325 PEVLVSTGGTDARFLRKAGIPSIVYGPGdLETAHQVNEYISIKNLVE 371
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
126-236 |
6.08e-04 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 41.87 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 126 ETLITTDGTTLLG---ADDKAGIVEILAAVEYFLAHPEVAR-G-DVWLAfgPDEEIG--RGADQFD--APNFPVAFAY-- 194
Cdd:PRK07338 112 QTLSWLDDGTLNGpgvADMKGGIVVMLAALLAFERSPLADKlGyDVLIN--PDEEIGspASAPLLAelARGKHAALTYep 189
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1635061248 195 -----TIDSGRVGHFEYEtfnaaqavITIDGTSVHPGTAYGSLVNAI 236
Cdd:PRK07338 190 alpdgTLAGARKGSGNFT--------IVVTGRAAHAGRAFDEGRNAI 228
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
132-180 |
6.77e-04 |
|
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: 41.86 E-value: 6.77e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1635061248 132 DGTTLLG---ADDKAGIVEILAAVEYFLAHPEVARGDVWLAFGPDEEIG--RGA 180
Cdd:cd05674 101 DGGYIWGrgaLDDKNSLIGILEAVELLLKRGFKPRRTIILAFGHDEEVGgeRGA 154
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
138-400 |
8.05e-04 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 41.28 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 138 GADD-KAGIVEILAAVEYFlaHPEVARGDVWLAFGPDEEI-GRGADQFdAPNFPVAFAYTIDSGRvGHFEYETFNAAQAV 215
Cdd:PRK08652 84 GACDaKGGVAAILLALEEL--GKEFEDLNVGIAFVSDEEEgGRGSALF-AERYRPKMAIVLEPTD-LKVAIAHYGNLEAY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 216 ITIDGTSVHpGTAYGSLVNAIKLGEQLDQSLPQKEvPEQTRGNEGFYLLNKFTGSIEkaelVYIIRDHDRENFQAR---K 292
Cdd:PRK08652 160 VEVKGKPSH-GACPESGVNAIEKAFEMLEKLKELL-KALGKYFDPHIGIQEIIGGSP----EYSIPALCRLRLDARippE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 293 QFLEKQVQRLNALADKprltITFQDQYYNMKE--IIENDWTPVELAVQAMESCDIEPIITPFRGGTDGskISFMGIPTPN 370
Cdd:PRK08652 234 VEVEDVLDEIDPILDE----YTVKYEYTEIWDgfELDEDEEIVQLLEKAMKEVGLEPEFTVMRSWTDA--INFRYNGTKT 307
|
250 260 270
....*....|....*....|....*....|...
gi 1635061248 371 LFTGGENF---HGQYEFITVESMAKAVQTIIAI 400
Cdd:PRK08652 308 VVWGPGELdlcHTKFERIDVREVEKAKEFLKAL 340
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
139-244 |
2.95e-03 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 39.61 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635061248 139 ADDKAGIVEILAAVEYFLAHPEVARGDVWLAFGPDEEIG---------RGADQFDapnfpVAFAY----TIDSGRVGhfe 205
Cdd:PRK06133 135 ADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGspgsreliaELAAQHD-----VVFSCepgrAKDALTLA--- 206
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1635061248 206 yeTFNAAQAVITIDGTSVHPGTAYGSLVNA-IKLGEQLDQ 244
Cdd:PRK06133 207 --TSGIATALLEVKGKASHAGAAPELGRNAlYELAHQLLQ 244
|
|
| |
