|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
2-409 |
0e+00 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 726.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 2 YENLLPRFLKYVKTETRSDATSTTTPSTQTQVAFAKELQKELEELGLSDVHYNEsNGFVIATLPSNVDHDVRSIGFIAHM 81
Cdd:PRK05469 1 MDKLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDE-NGYVMATLPANVDKDVPTIGFIAHM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 82 DTA-DFNAENVDPQIIENYDGeSTIKLDKEGkYTLNTKDFPNLKNYAGETLITTDGTTLLGSDDKSGIAEIMTAMEILLK 160
Cdd:PRK05469 80 DTApDFSGKNVKPQIIENYDG-GDIALGDGN-EVLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYLIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 161 NPTIKHGEIKVAFGPDEEIGVGADKFDVEDFNVDFAYTMDGGPVGELQYETFNAAQAEITIQGKNVHPGTAKDTMINALQ 240
Cdd:PRK05469 158 HPEIKHGDIRVAFTPDEEIGRGADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 241 LAVDFQNALPADEVPEKTEGTEGFFHLMSLSGSVEEAKMAYIIRDHDRSRFEERKAQLLAVQESLNARFDEPRVHVHLYD 320
Cdd:PRK05469 238 LAADFHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKYGEGRVELEIKD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 321 QYYNMKEIIEKDMSIIDLAKDAMKAVGITPMTEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRYEFVSLQSMMKATDVI 400
Cdd:PRK05469 318 QYYNMREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVI 397
|
....*....
gi 491368109 401 VKIAELNAQ 409
Cdd:PRK05469 398 VEIAELTAE 406
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
5-406 |
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: 668.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 5 LLPRFLKYVKTETRSDATSTTTPSTQTQVAFAKELQKELEELGLSDVHYNEsNGFVIATLPSNVDHDVRSIGFIAHMDTA 84
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDE-HGYVTATLPANVDKDVPTIGFIAHMDTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 85 DFN-AENVDPQIIENYDGEStIKLDKEGkYTLNTKDFPNLKNYAGETLITTDGTTLLGSDDKSGIAEIMTAMEILLKNPT 163
Cdd:cd03892 80 PDNsGKNVKPQIIENYDGGD-IVLNESG-IVLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIEHPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 164 IKHGEIKVAFGPDEEIGVGADKFDVEDFNVDFAYTMDGGPVGELQYETFNAAQAEITIQGKNVHPGTAKDTMINALQLAV 243
Cdd:cd03892 158 IKHGDIRVGFTPDEEIGRGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 244 DFQNALPADEVPEKTEGTEGFFHLMSLSGSVEEAKMAYIIRDHDRSRFEERKAQLLAVQESLNARFDEPRVHVHLYDQYY 323
Cdd:cd03892 238 DFHSMLPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKYGEGRVELEIKDQYY 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 324 NMKEIIEKDMSIIDLAKDAMKAVGITPMTEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRYEFVSLQSMMKATDVIVKI 403
Cdd:cd03892 318 NMKEKIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIVKI 397
|
...
gi 491368109 404 AEL 406
Cdd:cd03892 398 AEL 400
|
|
| peptidase-T |
TIGR01882 |
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has ... |
2-409 |
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: 603.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 2 YENLLPRFLKYVKTETRSDATSTTTPSTQTQVAFAKELQKELEELGLSDVHYNESNGFVIATLPSNVDHDVRSIGFIAHM 81
Cdd:TIGR01882 2 YEELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEKNGYVIATIPSNTDKDVPTIGFLAHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 82 DTADFNAENVDPQIIENYDGESTIKLDkEGKYTLNTKDFPNLKNYAGETLITTDGTTLLGSDDKSGIAEIMTAMEILLKN 161
Cdd:TIGR01882 82 DTADFNGENVNPQIIENYDGESIIQLG-DLEFTLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAADYLINH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 162 PTIKHGEIKVAFGPDEEIGVGADKFDVEDFNVDFAYTMDGGPVGELQYETFNAAQAEITIQGKNVHPGTAKDTMINALQL 241
Cdd:TIGR01882 161 PEIKHGTIRVAFTPDEEIGRGAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAAQI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 242 AVDFQNALPADEVPEKTEGTEGFFHLMSLSGSVEEAKMAYIIRDHDRSRFEERKAQLLAVQESLNARFDEPRVHVHLYDQ 321
Cdd:TIGR01882 241 AIDLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEYGQDRIKLDMNDQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 322 YYNMKEIIEKDMSIIDLAKDAMKAVGITPMTEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRYEFVSLQSMMKATDVIV 401
Cdd:TIGR01882 321 YYNMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDVIV 400
|
....*...
gi 491368109 402 KIAELNAQ 409
Cdd:TIGR01882 401 EIAKLNEE 408
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
3-409 |
1.14e-171 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 485.96 E-value: 1.14e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 3 ENLLPRFLKYVKTETRSDATSTTTPSTQTQVAFAKELQKELEELGLSDVhYNESNGFVIATLPSNVDhDVRSIGFIAHMD 82
Cdd:PRK13381 1 MQLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDI-VIDEHAIVTAKLPGNTP-GAPRIGFIAHLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 83 TADFNAE-NVDPQIIEnYDGEStIKLDKEGKYTLNTKDFPNLKNYAGETLITTDGTTLLGSDDKSGIAEIMTAMEILLKN 161
Cdd:PRK13381 79 TVDVGLSpDIHPQILR-FDGGD-LCLNAEQGIWLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLENLTEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 162 pTIKHGEIKVAFGPDEEIGV-GADKFDVEDFNVDFAYTMDGGPVGELQYETFNAAQAEITIQGKNVHPGTAKDTMINALQ 240
Cdd:PRK13381 157 -EVEHGDIVVAFVPDEEIGLrGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNPIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 241 LAVDFQNALPADEVPEKTEGTEGFFHLMSLSGSVEEAKMAYIIRDHDRSRFEERKAQLLAVQESLNARFDEPRVHVHLYD 320
Cdd:PRK13381 236 MANDFISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINAKYPTARVSLTLTD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 321 QYYNMKEIIEKDMSIIDLAKDAMKAVGITPMTEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRYEFVSLQSMMKATDVI 400
Cdd:PRK13381 316 QYSNISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEVT 395
|
....*....
gi 491368109 401 VKIAELNAQ 409
Cdd:PRK13381 396 ITICLLAAK 404
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
1-408 |
1.54e-168 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 476.08 E-value: 1.54e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 1 MYENLLPRFLKYVKTETRSDATStttpstqtqvAFAKELQKELEELGLsDVHYNEsNGFVIATLPSNVDHDVRSIGFIAH 80
Cdd:COG2195 1 NPERLLERFLEYVKIPTPSDHEE----------ALADYLVEELKELGL-EVEEDE-AGNVIATLPATPGYNVPTIGLQAH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 81 MDTA-DFNAENVDPQIienyDGEstikldkegkytlntkdfpnlknyagetLITTDGTTLLGSDDKSGIAEIMTAMEILl 159
Cdd:COG2195 69 MDTVpQFPGDGIKPQI----DGG----------------------------LITADGTTTLGADDKAGVAAILAALEYL- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 160 KNPTIKHGEIKVAFGPDEEIG-VGADKFDVEDFNVDFAYTMDGGPVGELQYETFNAAQAEITIQGKNVHPGTAKDTMINA 238
Cdd:COG2195 116 KEPEIPHGPIEVLFTPDEEIGlRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 239 LQLAVDFQNALPADEVPEKTEGTEGFFHLMSL-SGSVEEAKMAYIIRDHDRSRFEERKAQLLAVQESLNARFDEPRVHVH 317
Cdd:COG2195 196 IKLAARFLAALPLGRIPEETEGNEGFIHGGSAtNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGVGVVEVE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 318 LYDQYYNMKEiiEKDMSIIDLAKDAMKAVGITPMTEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRYEFVSLQSMMKAT 397
Cdd:COG2195 276 IEDQYPNWKP--EPDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAW 353
|
410
....*....|.
gi 491368109 398 DVIVKIAELNA 408
Cdd:COG2195 354 ELLVEILKLIA 364
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
5-406 |
5.83e-114 |
|
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: 338.97 E-value: 5.83e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 5 LLPRFLKYVKTETRSDATSTTTPSTQTQVAFAKELQKELEELGLSDVHYNESnGFVIATLPSNVDHDVRSIGFIAHMDTA 84
Cdd:cd05645 1 LLERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEK-GTLIATLPANVDGDIPAIGFISHVDTS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 85 -DFNAENVDPQIIENYDGESTIKldKEGKYTLNTKDFPNLKNYAGETLITTDGTTLLGSDDKSGIAEIMTAMEILLKNPt 163
Cdd:cd05645 80 pDGSGKNVNPQIVENYRGGDIAL--GIGDEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKN- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 164 IKHGEIKVAFGPDEEIGVGADKFDVEDFNVDFAYTMDGGPVGELQYETFNAAQAEITIQGKNVHPGTAKDTMINALQLAV 243
Cdd:cd05645 157 IPHGDIEVAFTPDEEVGKGAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 244 DFQNALPADEVPEKTEGTEGFFHLMSLSGSVEEAKMAYIIRDHDRSRFEERKAQLLAVQESLnARFDEPRVHVHLY--DQ 321
Cdd:cd05645 237 RIHAEVPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRK*KEIAKKV-GKGLHPDCYIELVieDS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 322 YYNMKEIIEKDMSIIDLAKDAMKAVGITPMTEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRYEFVSLQSMMKATDVIV 401
Cdd:cd05645 316 YYNFREKVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIV 395
|
....*
gi 491368109 402 KIAEL 406
Cdd:cd05645 396 RIAEL 400
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
35-405 |
3.08e-41 |
|
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: 149.52 E-value: 3.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 35 FAKELQKELEELGLSDV------HYNESNGFVIATLPSNVDHdVRSIGFIAHMDTadfnaenVDPqiienydGESTIKLD 108
Cdd:cd05683 25 ISKVLKKKFENLGLSVIeddagkTTGGGAGNLICTLKADKEE-VPKILFTSHMDT-------VTP-------GINVKPPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 109 KEGKYtlntkdfpnlknyagetlITTDGTTLLGSDDKSGIAEIMTAMEIlLKNPTIKHGEIKVAFGPDEEIG-VGADKFD 187
Cdd:cd05683 90 IADGY------------------IYSDGTTILGADDKAGIAAILEAIRV-IKEKNIPHGQIQFVITVGEESGlVGAKALD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 188 VEDFNVDFAYTMDG-GPVGELQYETFNAAQAEITIQGKNVHPGTAKDTMINALQLAVDFQNALPADEVPEKTEGTEGFFH 266
Cdd:cd05683 151 PELIDADYGYALDSeGDVGTIIVGAPTQDKINAKIYGKTAHAGTSPEKGISAINIAAKAISNMKLGRIDEETTANIGKFQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 267 LMSLSGSVeeAKMAYII---RDHDRSRFEERKAQLLAVQESLNARFD---EPRVHVhLYDQYYnmkeiIEKDMSIIDLAK 340
Cdd:cd05683 231 GGTATNIV--TDEVNIEaeaRSLDEEKLDAQVKHMKETFETTAKEKGahaEVEVET-SYPGFK-----INEDEEVVKLAK 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491368109 341 DAMKAVGITPMTEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRYEFVSLQSMMKATDVIVKIAE 405
Cdd:cd05683 303 RAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAVLVVEIIK 367
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
34-405 |
2.68e-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: 133.52 E-value: 2.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 34 AFAKELQKELEELGLsDVHYNE-----SNGF-VIATLPSNVDHDvrSIGFIAHMDTADfNAENVDPQIIENYdgestikl 107
Cdd:TIGR01883 21 AILTYLKKQITKLGI-PVSLDEvpaevSNDNnLIARLPGTVKFD--TIFFCGHMDTVP-PGAGPEPVVEDGI-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 108 dkegkytlntkdfpnlknyagetlITTDGTTLLGSDDKSGIAEIMTAMEILlKNPTIKHGEIKVAFGPDEEIG-VGADKF 186
Cdd:TIGR01883 89 ------------------------FTSLGGTILGADDKAGVAAMLEAMDVL-STEETPHGTIEFIFTVKEELGlIGMRLF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 187 DVEDFNVDFAYTMD-GGPVGELQYETFNAAQAEITIQGKNVHPGTAKDTMINALQLAVDFQNALPADEVPEKTEGTEGFF 265
Cdd:TIGR01883 144 DESKITAAYGYCLDaPGEVGNIQLAAPTQVKVDATIAGKDAHAGLVPEDGISAISVARMAIHAMRLGRIDEETTANIGSF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 266 -------------HLMSLSGSVEEAKMAYIIRdHDRSRFEERKAQLLAVQEslnarfDEPRVhvhLYDQYYnmkeiIEKD 332
Cdd:TIGR01883 224 sggvntnivqdeqLIVAEARSLSFRKAEAQVQ-TMRERFEQAAEKYGATLE------EETRL---IYEGFK-----IHPQ 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491368109 333 MSIIDLAKDAMKAVGITPMTEPVRGGTDGSKISYLGIPTPNIFAGGENMHGRYEFVSLQSMMKATDVIVKIAE 405
Cdd:TIGR01883 289 HPLMNIFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETISIEQLVKLAELVIALAE 361
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
36-405 |
1.65e-20 |
|
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: 92.26 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 36 AKELQKELEELGLS-DVHYNESN-GFVIATLPSNVDHdvRSIGFIAHMDT---ADFNAENVDPqiienydgestikldke 110
Cdd:COG0624 35 AELLAELLEALGFEvERLEVPPGrPNLVARRPGDGGG--PTLLLYGHLDVvppGDLELWTSDP----------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 111 gkytlntkdfpnlknYAGetliTTDGTTLLG---SDDKSGIAEIMTAMEILLKNPTIKHGEIKVAFGPDEEIG-VGADKF 186
Cdd:COG0624 96 ---------------FEP----TIEDGRLYGrgaADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGsPGARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 187 ---DVEDFNVDFAYTMDGGPVGELQYETFNAAQAEITIQGKNVHPGTAkDTMINALQLAVDFQNALPADEVPEKTEGTEG 263
Cdd:COG0624 157 veeLAEGLKADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAHSSRP-ELGVNAIEALARALAALRDLEFDGRADPLFG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 264 F--FHLMSLSGSV------EEAKMAYIIR---DHDRSRFEERkaqllaVQESLNARFDEPRVHVHLYDQYYNMKEiIEKD 332
Cdd:COG0624 236 RttLNVTGIEGGTavnvipDEAEAKVDIRllpGEDPEEVLAA------LRALLAAAAPGVEVEVEVLGDGRPPFE-TPPD 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491368109 333 MSIIDLAKDAMKAV-GITPMTEPVRGGTDGSKIS-YLGIPTPNI-FAGGENMHGRYEFVSLQSMMKATDVIVKIAE 405
Cdd:COG0624 309 SPLVAAARAAIREVtGKEPVLSGVGGGTDARFFAeALGIPTVVFgPGDGAGAHAPDEYVELDDLEKGARVLARLLE 384
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
142-405 |
1.04e-16 |
|
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: 80.47 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 142 SDDKSGIAEIMTAMEILLKNPtIKHGEIKVAFGPDEEIGVG-----ADKFDVEDFNVDFAYTMD----GGPVGELQYETF 212
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEG-LKKGTVKLLFQPDEEGGMGgaralIEDGLLEREKVDAVFGLHigepTLLEGGIAIGVV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 213 NA----AQAEITIQGKNVH---PGTAKDTMINALQLAVDFQnALPADEVPEKTEGTEGFFHLMSLSGSV----EEAKMAY 281
Cdd:pfam01546 112 TGhrgsLRFRVTVKGKGGHastPHLGVNAIVAAARLILALQ-DIVSRNVDPLDPAVVTVGNITGIPGGVnvipGEAELKG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 282 IIR---DHDRSRFEERkaqllaVQESLNARFDEPRVHVHLyDQYYNMKEIIEKDMSIIDLAKDAMKAV-GITP--MTEPV 355
Cdd:pfam01546 191 DIRllpGEDLEELEER------IREILEAIAAAYGVKVEV-EYVEGGAPPLVNDSPLVAALREAAKELfGLKVelIVSGS 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 491368109 356 RGGTDGSKISyLGIPtPNIF---AGGENMHGRYEFVSLQSMMKATDVIVKIAE 405
Cdd:pfam01546 264 MGGTDAAFFL-LGVP-PTVVffgPGSGLAHSPNEYVDLDDLEKGAKVLARLLL 314
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
142-405 |
3.71e-13 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 70.17 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 142 SDDKSGIAEIMTAMEILLKNptIKHGEIKVAFGPDEEIGVGADKFDVEDFNVDFAYTMDggPV-GELQYETFNAAQAEIT 220
Cdd:PRK08652 86 CDAKGGVAAILLALEELGKE--FEDLNVGIAFVSDEEEGGRGSALFAERYRPKMAIVLE--PTdLKVAIAHYGNLEAYVE 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 221 IQGKNVHpGTAKDTMINALQLAVDFQNALPADEvPEKTEGTEGFFHLMSLSGSVEEakmaYIIRDHDRSRFEER---KAQ 297
Cdd:PRK08652 162 VKGKPSH-GACPESGVNAIEKAFEMLEKLKELL-KALGKYFDPHIGIQEIIGGSPE----YSIPALCRLRLDARippEVE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 298 LLAVQESLNARFDEPRVHVHL---YDQYYnmkeiIEKDMSIIDLAKDAMKAVGITPMTEPVRGGTDGSKISYLGIPTPnI 374
Cdd:PRK08652 236 VEDVLDEIDPILDEYTVKYEYteiWDGFE-----LDEDEEIVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTKTV-V 309
|
250 260 270
....*....|....*....|....*....|...
gi 491368109 375 FAGGE--NMHGRYEFVSLQSMMKATDVIVKIAE 405
Cdd:PRK08652 310 WGPGEldLCHTKFERIDVREVEKAKEFLKALNE 342
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
36-404 |
2.32e-12 |
|
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: 67.71 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 36 AKELQKELEELGL---SDVHYNESNgfVIATLPSNvdhDVRSIGFIAHMDTadFNAENVDPQIIENYDGEstiklDKEGK 112
Cdd:cd08659 20 AEYLAELLAKRGYgieSTIVEGRGN--LVATVGGG---DGPVLLLNGHIDT--VPPGDGDKWSFPPFSGR-----IRDGR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 113 ytlntkdfpnlknyagetlittdgttLLG---SDDKSGIAEIMTAMEILLKNPTIKHGEIKVAFGPDEEIG-VGADKFDV 188
Cdd:cd08659 88 --------------------------LYGrgaCDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGsDGARALLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 189 EDFNVDFAYTMDGGPVGelqYETFNAA----QAEITIQGKNVHpGTAKDTMINALQLAVDFQNAL-----PADEVPEKTE 259
Cdd:cd08659 142 AGYADRLDALIVGEPTG---LDVVYAHkgslWLRVTVHGKAAH-SSMPELGVNAIYALADFLAELrtlfeELPAHPLLGP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 260 GTegfFHLMSLSGSVEeakmAYIIRDHDRSRF------EERKAQLLAVQESLnARFDEPRVHVHLYDQYYNMKEiIEKDM 333
Cdd:cd08659 218 PT---LNVGVINGGTQ----VNSIPDEATLRVdirlvpGETNEGVIARLEAI-LEEHEAKLTVEVSLDGDPPFF-TDPDH 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491368109 334 SIIDLAKDAMKAVGITPMTEPVRGGTDGSKIS-YLGIPTPnIFAGGEN--MHGRYEFVSLQSMMKATDVIVKIA 404
Cdd:cd08659 289 PLVQALQAAARALGGDPVVRPFTGTTDASYFAkDLGFPVV-VYGPGDLalAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
42-393 |
1.75e-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: 64.92 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 42 ELEELGLS-DVHYNESNG-FVIATLPsnvDHDVRSIGFIAHMDTAdfnaenvdpqiienydgestikldkegkytlntkd 119
Cdd:cd03885 31 ELEALGFTvERRPLGEFGdHLIATFK---GTGGKRVLLIGHMDTV----------------------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 120 FPnlKNYAGETLITTDGTTLLG---SDDKSGIAEIMTAMEILLKNPTIKHGEIKVAFGPDEEIGVGADKFDVEDF--NVD 194
Cdd:cd03885 73 FP--EGTLAFRPFTVDGDRAYGpgvADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRELIEEEakGAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 195 FAYTMD-GGPVGELQYETFNAAQAEITIQGKNVHPGTAKDTMINALQLAVDFQNALPADEVPEKteGTegffhlmSLS-G 272
Cdd:cd03885 151 YVLVFEpARADGNLVTARKGIGRFRLTVKGRAAHAGNAPEKGRSAIYELAHQVLALHALTDPEK--GT-------TVNvG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 273 SVEEAKMAYIIRDHDRSRFEER---KAQLLAVQESLNAR-----FDEPRVHVHLYDQYYNMkEIIEKDMSIIDLAKDAMK 344
Cdd:cd03885 222 VISGGTRVNVVPDHAEAQVDVRfatAEEADRVEEALRAIvattlVPGTSVELTGGLNRPPM-EETPASRRLLARAQEIAA 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 491368109 345 AVGITPMTEPVRGGTDGSKISYLGIPTPNIF-AGGENMHGRYEFVSLQSM 393
Cdd:cd03885 301 ELGLTLDWEATGGGSDANFTAALGVPTLDGLgPVGGGAHTEDEYLELDSL 350
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
60-210 |
4.83e-11 |
|
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: 61.67 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 60 VIATLPSNVDHdvRSIGFIAHMDTA-DFNAENVDPQIIEnydgestikldkegkytlntkdfpnlknyagETLITTDGTT 138
Cdd:cd03873 2 LIARLGGGEGG--KSVALGAHLDVVpAGEGDNRDPPFAE-------------------------------DTEEEGRLYG 48
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491368109 139 LLGSDDKSGIAEIMTAMEILLKNPTIKHGEIKVAFGPDEEIGVGADKF------DVEDFNVDFAYTMDGGPVGELQYE 210
Cdd:cd03873 49 RGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGSGGGKGllskflLAEDLKVDAAFVIDATAGPILQKG 126
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
60-204 |
1.85e-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: 57.06 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 60 VIATLPSNVDHdvRSIGFIAHMDTADFNAEnvdpqiienydgestikldkegkytLNTKDFPnlknyAGETLITTDGTTL 139
Cdd:cd18669 2 VIARYGGGGGG--KRVLLGAHIDVVPAGEG-------------------------DPRDPPF-----FVDTVEEGRLYGR 49
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491368109 140 LGSDDKSGIAEIMTAMEILLKNPTIKHGEIKVAFGPDEEIGVGADKF------DVEDFNVDFAYTMDGGPV 204
Cdd:cd18669 50 GALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEEVGSGAGKGllskdaLEEDLKVDYLFVGDATPA 120
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
142-400 |
6.03e-09 |
|
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: 57.40 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 142 SDDKSGIAEIMTAMEILLKNPTIKHGEIKVAFGPDEE-IGVGADKFDVEDFNVDFAYTMDGGP-------VGELqyetfN 213
Cdd:cd08011 100 SDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEEtGGRAGTKYLLEKVRIKPNDVLIGEPsgsdnirIGEK-----G 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 214 AAQAEITIQGKNVHPGTAKDTmINALQLAVDFQNALpADEVPEKTEGTEGFFHLMSLSGSVEEAKMAY-IIRDHDRSRFE 292
Cdd:cd08011 175 LVWVIIEITGKPAHGSLPHRG-ESAVKAAMKLIERL-YELEKTVNPGVIKGGVKVNLVPDYCEFSVDIrLPPGISTDEVL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 293 ERKAQLLAVQESLNARFdeprvhvhlyDQYYNMKEiIEKDMSIIDLAKDAMKAV-GITPMTEPVRGGTDGSKISYLGIPT 371
Cdd:cd08011 253 SRIIDHLDSIEEVSFEI----------KSFYSPTV-SNPDSEIVKKTEEAITEVlGIRPKEVISVGASDARFYRNAGIPA 321
|
250 260 270
....*....|....*....|....*....|
gi 491368109 372 PNIFAGG-ENMHGRYEFVSLQSMMKATDVI 400
Cdd:cd08011 322 IVYGPGRlGQMHAPNEYVEIDELIKVIKVH 351
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
142-401 |
6.40e-08 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 54.23 E-value: 6.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 142 SDDKSGIAEIMTAMEILlkNPTIKhGEIKVAFGPDEEI-GVGADKF-DVEDFNVDFAYTMDGGPVGELQYETFNAAQAEI 219
Cdd:PRK08651 113 SDMKGGIAALLAAFERL--DPAGD-GNIELAIVPDEETgGTGTGYLvEEGKVTPDYVIVGEPSGLDNICIGHRGLVWGVV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 220 TIQGKNVHPGTAKDTmINALQLAVDFQNAL---------------PADEVPEKTEGTEgffhlmSLSGSV------EEAK 278
Cdd:PRK08651 190 KVYGKQAHASTPWLG-INAFEAAAKIAERLksslstikskyeyddERGAKPTVTLGGP------TVEGGTktnivpGYCA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 279 MAYiirdhDRsRF--EERKAQllaVQESLNARFDE--PRVHVHLYDQYYNMKE--IIEKDMSIIDLAKDAM-KAVGITPM 351
Cdd:PRK08651 263 FSI-----DR-RLipEETAEE---VRDELEALLDEvaPELGIEVEFEITPFSEafVTDPDSELVKALREAIrEVLGVEPK 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 491368109 352 TEPVRGGTDGSKISYLGIPTPNIFAGGENM-HGRYEFVSLQSMMKATDVIV 401
Cdd:PRK08651 334 KTISLGGTDARFFGAKGIPTVVYGPGELELaHAPDEYVEVKDVEKAAKVYE 384
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
209-311 |
5.89e-07 |
|
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: 47.73 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 209 YETFNAAQAEITIQGKNVHPGtAKDTMINALQLAVDFQNALPAD----------EVPEKTEGTEGFfhlmSLSGSVEEAK 278
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSG-APGKGVNAIKLLARLLAELPAEygdigfdfprTTLNITGIEGGT----ATNVIPAEAE 75
|
90 100 110
....*....|....*....|....*....|...
gi 491368109 279 MAYIIRdhdRSRFEERKAQLLAVQESLNARFDE 311
Cdd:pfam07687 76 AKFDIR---LLPGEDLEELLEEIEAILEKELPE 105
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
143-239 |
4.89e-06 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 48.47 E-value: 4.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 143 DDKSGIAEIMTAMEIlLKNPTIK-HGEIKVAFGPDEEIG-VGADKFDVE---DFNVDFAYTmDGGPVGELQYETFNAAQA 217
Cdd:PRK06133 136 DDKGGVAVILHALKI-LQQLGFKdYGTLTVLFNPDEETGsPGSRELIAElaaQHDVVFSCE-PGRAKDALTLATSGIATA 213
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90 100
....*....|....*....|..
gi 491368109 218 EITIQGKNVHPGTAKDTMINAL 239
Cdd:PRK06133 214 LLEVKGKASHAGAAPELGRNAL 235
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| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
148-360 |
7.84e-06 |
|
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: 47.59 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 148 IAEIMTAMEILLKNPTIKHGEIKVAFGPDEEIGVGAdKFDVED-----FNVDFAY---TMDGGPVGELQYE--TFNAA-- 215
Cdd:cd03886 94 TAMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPGGA-KAMIEEgvlenPGVDAAFglhVWPGLPVGTVGVRsgALMASad 172
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 216 QAEITIQGKNVHPGTAKDTmINALQLAVDFQNAL---PADEVPEKTEG--TEGFFHlmslSGSV-----EEAKMAYIIRD 285
Cdd:cd03886 173 EFEITVKGKGGHGASPHLG-VDPIVAAAQIVLALqtvVSRELDPLEPAvvTVGKFH----AGTAfnvipDTAVLEGTIRT 247
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 286 HD---RSRFEERKAQLL-AVQESLNARFDeprvhVHLYDQY---YNMKEiiekdmsIIDLAKDAMKAVGI---TPMTEPV 355
Cdd:cd03886 248 FDpevREALEARIKRLAeGIAAAYGATVE-----LEYGYGYpavINDPE-------LTELVREAAKELLGeeaVVEPEPV 315
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....*
gi 491368109 356 RGGTD 360
Cdd:cd03886 316 MGSED 320
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| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
169-403 |
2.91e-05 |
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M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 45.73 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 169 IKVAFGPDEEIG--VGADKF----DVEDFNVDFAytMDGG-PVGELQYETFNAAQA----EITIQGKNVH-----PGTAK 232
Cdd:cd05646 131 IHLSFVPDEEIGghDGMEKFvkteEFKKLNVGFA--LDEGlASPTEEYRVFYGERSpwwvVITAPGTPGHgskllENTAG 208
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 233 DTMINALQLAVDF---QNALPADEvPEKTEGTEGFFHLMSLSGSV------EEAKMAYIIR---DHDRSRFEERKAQLLA 300
Cdd:cd05646 209 EKLRKVIESIMEFresQKQRLKSN-PNLTLGDVTTVNLTMLKGGVqmnvvpSEAEAGFDLRippTVDLEEFEKQIDEWCA 287
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 301 vQESLNARFDeprvhvhlYDQYYNMKEIIEKDMSII--DLAKDAMKAVGITPMTEPVRGGTDGSKISYLGIP-------- 370
Cdd:cd05646 288 -EAGRGVTYE--------FEQKSPEKDPTSLDDSNPwwAAFKKAVKEMGLKLKPEIFPAATDSRYIRALGIPalgfspmn 358
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250 260 270
....*....|....*....|....*....|....
gi 491368109 371 -TPNIfaggenMHGRYEFVSLQSMMKATDVIVKI 403
Cdd:cd05646 359 nTPIL------LHDHNEFLNEDVFLRGIEIYEKI 386
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| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
117-187 |
6.24e-04 |
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M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.
Pssm-ID: 349885 [Multi-domain] Cd Length: 474 Bit Score: 41.74 E-value: 6.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491368109 117 TKDFpnLKNYAGETLITTDGTTLlGSDDKSGIAEIMTAMEillkNPTIKHGEIKVAFGPDEEIG-VGADKFD 187
Cdd:cd03890 84 EKDP--IKLRIDGDWLKATGTTL-GADNGIGVAYALAILE----DKDIEHPPLEVLFTVDEETGmTGALGLD 148
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| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
149-246 |
1.01e-03 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. 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). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 41.10 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491368109 149 AEIMTAMEILLKNPTIKHGEIKVAFGPDEEIGVGADKFDVED---FNVDFAY---TMDGGPVGELQYE--TFNAAQAE-- 218
Cdd:cd08021 106 AMLLGAAKVLAENKDEIKGTVRFIFQPAEEVPPGGAKPMIEAgvlEGVDAVFglhLWSTLPTGTIAVRpgAIMAAPDEfd 185
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90 100 110
....*....|....*....|....*....|.
gi 491368109 219 ITIQGKNVH---PGTAKDTMINALQLAVDFQ 246
Cdd:cd08021 186 ITIKGKGGHgsmPHETVDPIVIAAQIVTALQ 216
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