|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
4-410 |
0e+00 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 771.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 4 KLIERLITYAKIDTQSDFTSETTPSTAKQWDLIRHLETELKAIGLEDVETDEYGYLFATLPSNVDHDVPTIGLLAHVDTA 83
Cdd:PRK05469 3 KLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDENGYVMATLPANVDKDVPTIGFIAHMDTA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 84 TDFTGTNVNPQLVEHYEGGDIVLNEAlGVILSPRDFPELDGYVGHTLITTDGTTLLGADDKAGMAEIVTAVEYLLAHPEI 163
Cdd:PRK05469 83 PDFSGKNVKPQIIENYDGGDIALGDG-NEVLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYLIAHPEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 164 PHGPVRIAFTPDEEIGRGPHKFDVARFNADFAYTMDGGPLGELQYESFNAAGATVTFHGTNVHPGSAKNKMVNSMKLAMA 243
Cdd:PRK05469 162 KHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALLLAAD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 244 FHNRLPADEAPEHTSDYEGFFHLNGFSGDVETTTLQYIIRDHDRTKFEARKALLEKLVVEWKQKYGEARIDLKMDDQYYN 323
Cdd:PRK05469 242 FHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKYGEGRVELEIKDQYYN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 324 MAEKIEPVKHIVDTVADVMLELGIEPKIEPIRGGTDGSQLSYMGLPTPNIFTGGENYHGKFEYVSVNNMEKATHVIIQTL 403
Cdd:PRK05469 322 MREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVIVEIA 401
|
....*..
gi 2048237714 404 HTFAERA 410
Cdd:PRK05469 402 ELTAERA 408
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
5-400 |
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: 696.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 5 LIERLITYAKIDTQSDFTSETTPSTAKQWDLIRHLETELKAIGLEDVETDEYGYLFATLPSNVDHDVPTIGLLAHVDTAT 84
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDEHGYVTATLPANVDKDVPTIGFIAHMDTAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 85 DFTGTNVNPQLVEHYEGGDIVLNEaLGVILSPRDFPELDGYVGHTLITTDGTTLLGADDKAGMAEIVTAVEYLLAHPEIP 164
Cdd:cd03892 81 DNSGKNVKPQIIENYDGGDIVLNE-SGIVLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIEHPEIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 165 HGPVRIAFTPDEEIGRGPHKFDVARFNADFAYTMDGGPLGELQYESFNAAGATVTFHGTNVHPGSAKNKMVNSMKLAMAF 244
Cdd:cd03892 160 HGDIRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLAADF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 245 HNRLPADEAPEHTSDYEGFFHLNGFSGDVETTTLQYIIRDHDRTKFEARKALLEKLVVEWKQKYGEARIDLKMDDQYYNM 324
Cdd:cd03892 240 HSMLPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKYGEGRVELEIKDQYYNM 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2048237714 325 AEKIEPVKHIVDTVADVMLELGIEPKIEPIRGGTDGSQLSYMGLPTPNIFTGGENYHGKFEYVSVNNMEKATHVII 400
Cdd:cd03892 320 KEKIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIV 395
|
|
| peptidase-T |
TIGR01882 |
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has ... |
4-410 |
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: 576.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 4 KLIERLITYAKIDTQSDFTSETTPSTAKQWDLIRHLETELKAIGLEDVETDEY-GYLFATLPSNVDHDVPTIGLLAHVDT 82
Cdd:TIGR01882 4 ELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEKnGYVIATIPSNTDKDVPTIGFLAHVDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 83 AtDFTGTNVNPQLVEHYEGGDIVLNEALGVILSPRDFPELDGYVGHTLITTDGTTLLGADDKAGMAEIVTAVEYLLAHPE 162
Cdd:TIGR01882 84 A-DFNGENVNPQIIENYDGESIIQLGDLEFTLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAADYLINHPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 163 IPHGPVRIAFTPDEEIGRGPHKFDVARFNADFAYTMDGGPLGELQYESFNAAGATVTFHGTNVHPGSAKNKMVNSMKLAM 242
Cdd:TIGR01882 163 IKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAAQIAI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 243 AFHNRLPADEAPEHTSDYEGFFHLNGFSGDVETTTLQYIIRDHDRTKFEARKALLEKLVVEWKQKYGEARIDLKMDDQYY 322
Cdd:TIGR01882 243 DLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEYGQDRIKLDMNDQYY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 323 NMAEKIEPVKHIVDTVADVMLELGIEPKIEPIRGGTDGSQLSYMGLPTPNIFTGGENYHGKFEYVSVNNMEKATHVIIQT 402
Cdd:TIGR01882 323 NMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDVIVEI 402
|
....*...
gi 2048237714 403 LHTFAERA 410
Cdd:TIGR01882 403 AKLNEEQA 410
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
1-407 |
0e+00 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 508.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 1 MQSKLIERLITYAKIDTQSDftsettpstaKQWDLIRHLETELKAIGLEdVETDEYGYLFATLPSNVDHDVPTIGLLAHV 80
Cdd:COG2195 1 NPERLLERFLEYVKIPTPSD----------HEEALADYLVEELKELGLE-VEEDEAGNVIATLPATPGYNVPTIGLQAHM 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 81 DTATDFTGTNVNPQLvehyEGGdivlnealgvilsprdfpeldgyvghtLITTDGTTLLGADDKAGMAEIVTAVEYLLaH 160
Cdd:COG2195 70 DTVPQFPGDGIKPQI----DGG---------------------------LITADGTTTLGADDKAGVAAILAALEYLK-E 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 161 PEIPHGPVRIAFTPDEEIG-RGPHKFDVARFNADFAYTMDGGPLGELQYESFNAAGATVTFHGTNVHPGSAKNKMVNSMK 239
Cdd:COG2195 118 PEIPHGPIEVLFTPDEEIGlRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 240 LAMAFHNRLPADEAPEHTSDYEGFFHLNGF-SGDVETTTLQYIIRDHDRTKFEARKALLEKLVVEWKQKYGEARIDLKMD 318
Cdd:COG2195 198 LAARFLAALPLGRIPEETEGNEGFIHGGSAtNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGVGVVEVEIE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 319 DQYYNMaeKIEPVKHIVDTVADVMLELGIEPKIEPIRGGTDGSQLSYMGLPTPNIFTGGENYHGKFEYVSVNNMEKATHV 398
Cdd:COG2195 278 DQYPNW--KPEPDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWEL 355
|
....*....
gi 2048237714 399 IIQTLHTFA 407
Cdd:COG2195 356 LVEILKLIA 364
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
3-401 |
3.30e-173 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 489.82 E-value: 3.30e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 3 SKLIERLITYAKIDTQSDFTSETTPSTAKQWDLIRHLETELKAIGLEDVETDEYGYLFATLPSNVDhDVPTIGLLAHVDT 82
Cdd:PRK13381 1 MQLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDIVIDEHAIVTAKLPGNTP-GAPRIGFIAHLDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 83 ATDFTGTNVNPQLVeHYEGGDIVLNEALGVILSPRDFPELDGYVGHTLITTDGTTLLGADDKAGMAEIVTAVEYLLAHpE 162
Cdd:PRK13381 80 VDVGLSPDIHPQIL-RFDGGDLCLNAEQGIWLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLENLTEN-E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 163 IPHGPVRIAFTPDEEIG-RGPHKFDVARFNADFAYTMDGGPLGELQYESFNAAGATVTFHGTNVHPGSAKNKMVNSMKLA 241
Cdd:PRK13381 158 VEHGDIVVAFVPDEEIGlRGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNPILMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 242 MAFHNRLPADEAPEHTSDYEGFFHLNGFSGDVETTTLQYIIRDHDRTKFEARKALLEKLVVEWKQKYGEARIDLKMDDQY 321
Cdd:PRK13381 238 NDFISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINAKYPTARVSLTLTDQY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 322 YNMAEKIEPVKHIVDTVADVMLELGIEPKIEPIRGGTDGSQLSYMGLPTPNIFTGGENYHGKFEYVSVNNMEKATHVIIQ 401
Cdd:PRK13381 318 SNISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEVTIT 397
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
5-400 |
5.36e-124 |
|
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: 364.78 E-value: 5.36e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 5 LIERLITYAKIDTQSDFTSETTPSTAKQWDLIRHLETELKAIGLEDVETDEYGYLFATLPSNVDHDVPTIGLLAHVDTAT 84
Cdd:cd05645 1 LLERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEKGTLIATLPANVDGDIPAIGFISHVDTSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 85 DFTGTNVNPQLVEHYEGGDIVLNEALGViLSPRDFPELDGYVGHTLITTDGTTLLGADDKAGMAEIVTAVEYLLAHPeIP 164
Cdd:cd05645 81 DGSGKNVNPQIVENYRGGDIALGIGDEV-LSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKN-IP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 165 HGPVRIAFTPDEEIGRGPHKFDVARFNADFAYTMDGGPLGELQYESFNAAGATVTFHGTNVHPGSAKNKMVNSMKLAMAF 244
Cdd:cd05645 159 HGDIEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAARI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 245 HNRLPADEAPEHTSDYEGFFHLNGFSGDVETTTLQYIIRDHDRTKFEARKA-LLEKLVVEWKQKYGEARIDLKMDDQYYN 323
Cdd:cd05645 239 HAEVPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRk*KEIAKKVGKGLHPDCYIELVIEDSYYN 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2048237714 324 MAEKIEPVKHIVDTVADVMLELGIEPKIEPIRGGTDGSQLSYMGLPTPNIFTGGENYHGKFEYVSVNNMEKATHVII 400
Cdd:cd05645 319 FREKVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIV 395
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
2-400 |
1.85e-34 |
|
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: 131.42 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 2 QSKLIERLITYAKIDTQSDFTSETTPStakqwdlirhLETELKAIGLEDVETD-------EYGYLFATLPSNVDHdVPTI 74
Cdd:cd05683 2 EDRLINTFLELVQIDSETLHEKEISKV----------LKKKFENLGLSVIEDDagkttggGAGNLICTLKADKEE-VPKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 75 GLLAHVDTATdfTGTNVNPQLVEhyeggdivlnealgvilsprdfpelDGYvghtlITTDGTTLLGADDKAGMAEIVTAV 154
Cdd:cd05683 71 LFTSHMDTVT--PGINVKPPQIA-------------------------DGY-----IYSDGTTILGADDKAGIAAILEAI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 155 EYLlAHPEIPHGPVRIAFTPDEEIGR-GPHKFDVARFNADFAYTMDG-GPLGELQYESFNAAGATVTFHGTNVHPGSAKN 232
Cdd:cd05683 119 RVI-KEKNIPHGQIQFVITVGEESGLvGAKALDPELIDADYGYALDSeGDVGTIIVGAPTQDKINAKIYGKTAHAGTSPE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 233 KMVNSMKLAMAFHNRLPADEAPEHTSDYEGFFHlngfsGDVETTtlqyIIRDHDRTKFEARKALLEKLVVEWK------- 305
Cdd:cd05683 198 KGISAINIAAKAISNMKLGRIDEETTANIGKFQ-----GGTATN----IVTDEVNIEAEARSLDEEKLDAQVKhmketfe 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 306 ---QKYGeARIDLKMDDQYynMAEKIEPVKHIVDTVADVMLELGIEPKIEPIRGGTDGSQLSYMGLPTPNIFTGGENYHG 382
Cdd:cd05683 269 ttaKEKG-AHAEVEVETSY--PGFKINEDEEVVKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHT 345
|
410
....*....|....*...
gi 2048237714 383 KFEYVSVNNMEKATHVII 400
Cdd:cd05683 346 TNERIPIEDLYDTAVLVV 363
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
52-400 |
1.03e-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: 118.11 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 52 ETDEYGYLFATLPSNVDhdVPTIGLLAHVDTATDftGTNVNPQlVEhyeggdivlnealgvilsprdfpelDGYvghtlI 131
Cdd:TIGR01883 45 EVSNDNNLIARLPGTVK--FDTIFFCGHMDTVPP--GAGPEPV-VE-------------------------DGI-----F 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 132 TTDGTTLLGADDKAGMAEIVTAVEYlLAHPEIPHGPVRIAFTPDEEIG-RGPHKFDVARFNADFAYTMD-GGPLGELQYE 209
Cdd:TIGR01883 90 TSLGGTILGADDKAGVAAMLEAMDV-LSTEETPHGTIEFIFTVKEELGlIGMRLFDESKITAAYGYCLDaPGEVGNIQLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 210 SFNAAGATVTFHGTNVHPGSAKNKMVNSMKLA-MAFHnrlpadEAPEHTSDYEGFFHLNGFSGDVETTtlqyIIRDHDRT 288
Cdd:TIGR01883 169 APTQVKVDATIAGKDAHAGLVPEDGISAISVArMAIH------AMRLGRIDEETTANIGSFSGGVNTN----IVQDEQLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 289 KFEARKALLEKL---VVEWKQKYGEARID----LKMDDQYYNMAEKIEPVKHIVDTVADVMLELGIEPKIEPIRGGTDGS 361
Cdd:TIGR01883 239 VAEARSLSFRKAeaqVQTMRERFEQAAEKygatLEEETRLIYEGFKIHPQHPLMNIFKKAAKKIGLKTSEIFSGGGSDAN 318
|
330 340 350
....*....|....*....|....*....|....*....
gi 2048237714 362 QLSYMGLPTPNIFTGGENYHGKFEYVSVNNMEKATHVII 400
Cdd:TIGR01883 319 VLNEKGVPTVNLSAGYVHAHTEKETISIEQLVKLAELVI 357
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
1-408 |
1.29e-23 |
|
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: 101.50 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 1 MQSKLIERLITYAKIDTqsdftseTTPSTAkqwDLIRHLETELKAIGLE---DVETDEYGYLFATLPSNVDHdvPTIGLL 77
Cdd:COG0624 10 HLDEALELLRELVRIPS-------VSGEEA---AAAELLAELLEALGFEverLEVPPGRPNLVARRPGDGGG--PTLLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 78 AHVDT--ATDFTGTNVNPqlvehyeggdivlnealgviLSPRdfpELDGYV-GhtlittdgttlLGA-DDKAGMAEIVTA 153
Cdd:COG0624 78 GHLDVvpPGDLELWTSDP--------------------FEPT---IEDGRLyG-----------RGAaDMKGGLAAMLAA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 154 VEYLLAHPEIPHGPVRIAFTPDEEIG-RGPHKF---DVARFNADFAYTMDGGPLGELQYESFNAAGATVTFHGTNVHpGS 229
Cdd:COG0624 124 LRALLAAGLRLPGNVTLLFTGDEEVGsPGARALveeLAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAH-SS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 230 AKNKMVNSMKLAMAFHNRLPADEAPEHTSDYEGF--FHLNGFSGDVETTtlqyIIRDHDRTKFEAR----------KALL 297
Cdd:COG0624 203 RPELGVNAIEALARALAALRDLEFDGRADPLFGRttLNVTGIEGGTAVN----VIPDEAEAKVDIRllpgedpeevLAAL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 298 EKLVvewKQKYGEARIDLKMDDQYYNmAEKIEPVKHIVDTVADVMLEL-GIEPKIEPIRGGTDGSQLS-YMGLPTPNI-F 374
Cdd:COG0624 279 RALL---AAAAPGVEVEVEVLGDGRP-PFETPPDSPLVAAARAAIREVtGKEPVLSGVGGGTDARFFAeALGIPTVVFgP 354
|
410 420 430
....*....|....*....|....*....|....
gi 2048237714 375 TGGENYHGKFEYVSVNNMEKATHVIIQTLHTFAE 408
Cdd:COG0624 355 GDGAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
141-403 |
3.05e-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: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 141 ADDKAGMAEIVTAVEYLLAHPEIPhGPVRIAFTPDEEIG-RGPHKF----DVARFNADFAYTMD----GGPLGELQYESF 211
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEGLKK-GTVKLLFQPDEEGGmGGARALiedgLLEREKVDAVFGLHigepTLLEGGIAIGVV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 212 NA-AGA---TVTFHGTNVH---PGSAKNKMVNSMKLAMAFHNRLPADEAPEHTSDYEgFFHLNGFSGDV----ETTTLQY 280
Cdd:pfam01546 112 TGhRGSlrfRVTVKGKGGHastPHLGVNAIVAAARLILALQDIVSRNVDPLDPAVVT-VGNITGIPGGVnvipGEAELKG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 281 IIR---DHDRTKFEARkalLEKLVVEWKQKYGeARIDLKMDDQYYNMAEKIEPVKHIVDTVADVMLELGIEPKIEPIRGG 357
Cdd:pfam01546 191 DIRllpGEDLEELEER---IREILEAIAAAYG-VKVEVEYVEGGAPPLVNDSPLVAALREAAKELFGLKVELIVSGSMGG 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2048237714 358 TDGsqlSYMGLPTPNIF----TGGENYHGKFEYVSVNNMEKATHVIIQTL 403
Cdd:pfam01546 267 TDA---AFFLLGVPPTVvffgPGSGLAHSPNEYVDLDDLEKGAKVLARLL 313
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
141-407 |
1.61e-12 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 68.48 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 141 ADDKAGMAEIVTAVEYLlahPEIPHGPVRIAFTPDEEIGR--GPHKFDVARFNADFAYTMDGGPLGELQYESFNAAGATV 218
Cdd:PRK08651 113 SDMKGGIAALLAAFERL---DPAGDGNIELAIVPDEETGGtgTGYLVEEGKVTPDYVIVGEPSGLDNICIGHRGLVWGVV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 219 TFHGTNVH---PGSAKNKMVNSMKLAMAFHNRLPA--------DEAPEHTSDYEGFFHLNGFS------GDVETTTLQYI 281
Cdd:PRK08651 190 KVYGKQAHastPWLGINAFEAAAKIAERLKSSLSTikskyeydDERGAKPTVTLGGPTVEGGTktnivpGYCAFSIDRRL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 282 IRDHDRTKFEARkalLEKLVVEWKQKYGearIDLKMDDQYYNMAEKIEPVKHIVDTVADVMLE-LGIEPKIEPIRGGTDG 360
Cdd:PRK08651 270 IPEETAEEVRDE---LEALLDEVAPELG---IEVEFEITPFSEAFVTDPDSELVKALREAIREvLGVEPKKTISLGGTDA 343
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2048237714 361 SQLSYMGLPTPNIFTGG-ENYHGKFEYVSVNNMEKATHVIIQTLHTFA 407
Cdd:PRK08651 344 RFFGAKGIPTVVYGPGElELAHAPDEYVEVKDVEKAAKVYEEVLKRLA 391
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
140-403 |
9.25e-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: 62.70 E-value: 9.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 140 GADD-KAGMAEIVTAVEYLLAHPEIPHGPVRIAFTPDEEIG-RGPHKFDVARFNADFAYTMDGGPLGelqYESFNAA-GA 216
Cdd:cd08659 92 GACDmKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGsDGARALLEAGYADRLDALIVGEPTG---LDVVYAHkGS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 217 ---TVTFHGTNVHpGSAKNKMVNSMKLAMAFHNRLPADEAPEHTSDYEGFFHLNgfSGDVETTTLQYIIRDHDRTKFEAR 293
Cdd:cd08659 169 lwlRVTVHGKAAH-SSMPELGVNAIYALADFLAELRTLFEELPAHPLLGPPTLN--VGVINGGTQVNSIPDEATLRVDIR 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 294 ----------KALLEKLVvewKQKYGEARIDLKMDDQYYnmaEKIEPVKHIVDTVADVMLELGIEPKIEPIRGGTDGSQL 363
Cdd:cd08659 246 lvpgetnegvIARLEAIL---EEHEAKLTVEVSLDGDPP---FFTDPDHPLVQALQAAARALGGDPVVRPFTGTTDASYF 319
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2048237714 364 SYM-GLPTPnIFTGGENY--HGKFEYVSVNNMEKATHVIIQTL 403
Cdd:cd08659 320 AKDlGFPVV-VYGPGDLAlaHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
59-399 |
1.28e-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: 60.52 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 59 LFATLPSNVDHdvPTIGLLAHVDTATDFTGTNVNPQlvehyeggdivlnealgvilsprdfpeldgYVGHTLITTDGTTL 138
Cdd:cd03873 2 LIARLGGGEGG--KSVALGAHLDVVPAGEGDNRDPP------------------------------FAEDTEEEGRLYGR 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 139 LGADDKAGMAEIVTAVEYLLAHPEIPHGPVRIAFTPDEEIGRGPHKFDVARFNADFAYtmdggplgelqyesfnaagatv 218
Cdd:cd03873 50 GALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGSGGGKGLLSKFLLAEDL---------------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 219 tfhgtnvhpgsaknkmvnsmklamafhnrlpadeapehTSDYegffhlnGFSGDVEtttlqyiirdhdrtkfearkalle 298
Cdd:cd03873 108 --------------------------------------KVDA-------AFVIDAT------------------------ 118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 299 klvvewkqkygearidlkmddQYYNMAEKIEPVKHIVDTVADVMLELGIEPK-IEPIRGGTDGSQLSYMGLPTPNIFTGG 377
Cdd:cd03873 119 ---------------------AGPILQKGVVIRNPLVDALRKAAREVGGKPQrASVIGGGTDGRLFAELGIPGVTLGPPG 177
|
330 340
....*....|....*....|...
gi 2048237714 378 E-NYHGKFEYVSVNNMEKATHVI 399
Cdd:cd03873 178 DkGAHSPNEFLNLDDLEKATKVY 200
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
39-393 |
6.45e-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: 60.30 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 39 LETELKAIGL--EDVETDEYG-YLFATLPsnvDHDVPTIGLLAHVDTAtdftgtnvnpqlvehyeggdivlnealgvils 115
Cdd:cd03885 28 LAEELEALGFtvERRPLGEFGdHLIATFK---GTGGKRVLLIGHMDTV-------------------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 116 prdFPEldGYVGHTLITTDGTTLLG---ADDKAGMAEIVTAVEYLLAHPEIPHGPVRIAFTPDEEIGR---GPHKFDVAR 189
Cdd:cd03885 73 ---FPE--GTLAFRPFTVDGDRAYGpgvADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSpgsRELIEEEAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 190 fNADFAYTMD-GGPLGELQYESFNAAGATVTFHGTNVHPGSAKNKMVNSMkLAMAFH-NRLPA--DEAPEHTsdyegffh 265
Cdd:cd03885 148 -GADYVLVFEpARADGNLVTARKGIGRFRLTVKGRAAHAGNAPEKGRSAI-YELAHQvLALHAltDPEKGTT-------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 266 LNgfSGDVETTTLQYIIRDHDRTKFEAR------KALLEKLVVEWKQ--KYGEARIDLKMDDQYYNMaEKIEPVKHIVDT 337
Cdd:cd03885 218 VN--VGVISGGTRVNVVPDHAEAQVDVRfataeeADRVEEALRAIVAttLVPGTSVELTGGLNRPPM-EETPASRRLLAR 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2048237714 338 VADVMLELGIEPKIEPIRGGTDGSQLSYMGLPTPNIFtG--GENYHGKFEYVSVNNME 393
Cdd:cd03885 295 AQEIAAELGLTLDWEATGGGSDANFTAALGVPTLDGL-GpvGGGAHTEDEYLELDSLV 351
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
142-399 |
1.86e-09 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 58.62 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 142 DDKAGMAEIVTAVEYLLAHPEIPHgpVRIAFTPDEEI-GRGPHKFdVARFNADFAYTMDGGPLgELQYESFNAAGATVTF 220
Cdd:PRK08652 87 DAKGGVAAILLALEELGKEFEDLN--VGIAFVSDEEEgGRGSALF-AERYRPKMAIVLEPTDL-KVAIAHYGNLEAYVEV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 221 HGTNVHpGSAKNKMVNSMKLAMAFHNRLPADEaPEHTSDYEGFFHLNGFSGDVEtttlQYIIRDHDRTKFEAR------- 293
Cdd:PRK08652 163 KGKPSH-GACPESGVNAIEKAFEMLEKLKELL-KALGKYFDPHIGIQEIIGGSP----EYSIPALCRLRLDARippevev 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 294 ---KALLEKLVVEWKQKYGEARIDlkmdDQYYnmaekIEPVKHIVDTVADVMLELGIEPKIEPIRGGTDGSQLSYMGLPT 370
Cdd:PRK08652 237 edvLDEIDPILDEYTVKYEYTEIW----DGFE-----LDEDEEIVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTKT 307
|
250 260 270
....*....|....*....|....*....|.
gi 2048237714 371 PnIFTGGENY--HGKFEYVSVNNMEKATHVI 399
Cdd:PRK08652 308 V-VWGPGELDlcHTKFERIDVREVEKAKEFL 337
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
208-301 |
1.87e-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: 54.66 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 208 YESFNAAGATVTFHGTNVHPGsAKNKMVNSMKLAMAFHNRLPADEAPEHTSDYEGFFHLNGFSG------DVETTTLQYI 281
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSG-APGKGVNAIKLLARLLAELPAEYGDIGFDFPRTTLNITGIEGgtatnvIPAEAEAKFD 79
|
90 100
....*....|....*....|
gi 2048237714 282 IRdhdRTKFEARKALLEKLV 301
Cdd:pfam07687 80 IR---LLPGEDLEELLEEIE 96
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
59-202 |
2.33e-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: 56.67 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 59 LFATLPSNVDHdvPTIGLLAHVDTATDFTGTNVNPQlvehyeggdivlnealgvilsprdfpeldgYVGHTLITTDGTTL 138
Cdd:cd18669 2 VIARYGGGGGG--KRVLLGAHIDVVPAGEGDPRDPP------------------------------FFVDTVEEGRLYGR 49
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 139 LGADDKAGMAEIVTAVEYLLAHPEIPHGPVRIAFTPDEEIGRGPHKFDVAR------FNADFAYTMDGGP 202
Cdd:cd18669 50 GALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEEVGSGAGKGLLSKdaleedLKVDYLFVGDATP 119
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
141-399 |
1.51e-07 |
|
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: 52.77 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 141 ADDKAGMAEIVTAVEYLLAHPEIPHGPVRIAFTPDEE-IGRGPHKFDVARFNADFAYTMDGGPLGE------------LQ 207
Cdd:cd08011 100 SDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEEtGGRAGTKYLLEKVRIKPNDVLIGEPSGSdnirigekglvwVI 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 208 YESFNAAGatvtfHGTNVHPGsaknkmVNSMKLAMAFHNRLPADEAPEHTSDYEGFFHLNGFSGDVEtttLQYIIR---- 283
Cdd:cd08011 180 IEITGKPA-----HGSLPHRG------ESAVKAAMKLIERLYELEKTVNPGVIKGGVKVNLVPDYCE---FSVDIRlppg 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 284 ---DHDRTKFEARKALLEKLVVEWKQKYgearidlkmddQYYNMAEKIEPVKHIVDTVADVmleLGIEPKIEPIRGGTDG 360
Cdd:cd08011 246 istDEVLSRIIDHLDSIEEVSFEIKSFY-----------SPTVSNPDSEIVKKTEEAITEV---LGIRPKEVISVGASDA 311
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2048237714 361 SQLSYMGLPTPNIFTGG-ENYHGKFEYVSVNNMEKATHVI 399
Cdd:cd08011 312 RFYRNAGIPAIVYGPGRlGQMHAPNEYVEIDELIKVIKVH 351
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
147-364 |
6.72e-07 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 51.06 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 147 MAEIVTAVEYLLAHPEIPHGPVRIAFTPDEEIGRGPHK------FDVARFNADFAY-TMDGGPLGELQYES--FNAAGAT 217
Cdd:cd03886 94 TAMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPGGAKAmieegvLENPGVDAAFGLhVWPGLPVGTVGVRSgaLMASADE 173
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 218 --VTFHGTNVHpGSAKNKMVNSMKLAMAFHNRL---PADEAPEHTSDYEGFFHLNGfsGDV-----ETTTLQYIIRDHDR 287
Cdd:cd03886 174 feITVKGKGGH-GASPHLGVDPIVAAAQIVLALqtvVSRELDPLEPAVVTVGKFHA--GTAfnvipDTAVLEGTIRTFDP 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2048237714 288 TKFEARKALLEKLVVEWKQKYGeARIDLKMDDQYYNMAEKIEPVKHIVDTVADVmleLGIEPK--IEPIRGGTDGSQLS 364
Cdd:cd03886 251 EVREALEARIKRLAEGIAAAYG-ATVELEYGYGYPAVINDPELTELVREAAKEL---LGEEAVvePEPVMGSEDFAYYL 325
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|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
122-179 |
9.42e-06 |
|
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.
Pssm-ID: 349885 [Multi-domain] Cd Length: 474 Bit Score: 47.52 E-value: 9.42e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2048237714 122 LDGYVGHTLITTDGTTLlGADDKAGMAEIVTaveyLLAHPEIPHGPVRIAFTPDEEIG 179
Cdd:cd03890 88 IKLRIDGDWLKATGTTL-GADNGIGVAYALA----ILEDKDIEHPPLEVLFTVDEETG 140
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|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
145-223 |
4.68e-03 |
|
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349939 [Multi-domain] Cd Length: 365 Bit Score: 38.80 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 145 AGMAEIVTAVEYLLAHPEIPHGPVRIAFTPDEEIGRGPHKF--DVARFNADFAYTMDGGPLGELQYESFNAA---GATVT 219
Cdd:cd08018 90 AHMTMVLGAAELLKKIGLVKKGKLKFLFQPAEEKGTGALKMieDGVLDDVDYLFGVHLRPIQELPFGTAAPAiyhGASTF 169
|
....
gi 2048237714 220 FHGT 223
Cdd:cd08018 170 LEGT 173
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|
| COG4185 |
COG4185 |
Predicted ABC-type ATPase or kinase [General function prediction only]; |
15-106 |
4.83e-03 |
|
Predicted ABC-type ATPase or kinase [General function prediction only];
Pssm-ID: 443339 Cd Length: 197 Bit Score: 37.95 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 15 IDTQSDFTSETTPSTAKQWDLIRHL-----ETELKAIGLEDVETdeygylfatlpsNVD----------HDVPT------ 73
Cdd:COG4185 68 LAAGRSFAFETTLSGPSKLDLIREAkaagyRVRLIFVGLDSPEL------------AIArvaqrvaeggHDVPEdkirrr 135
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2048237714 74 --------IGLLAHVDTATDFTGTNVNPQLVEHYEGGDIVL 106
Cdd:COG4185 136 yprslanlAEALPLADRAYVFDNSGEKPRLVAEKEDGQIVL 176
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
141-230 |
6.75e-03 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 38.46 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2048237714 141 ADDKAGMAEIVTAVEYLLAHPEIPHGPVRIAFTPDEEIGRGPHKFDVARFNADFAYTMD---GGPLGELQYESFNAAGAT 217
Cdd:PRK06133 135 ADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGSPGSRELIAELAAQHDVVFScepGRAKDALTLATSGIATAL 214
|
90
....*....|...
gi 2048237714 218 VTFHGTNVHPGSA 230
Cdd:PRK06133 215 LEVKGKASHAGAA 227
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