|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
10-412 |
0e+00 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 654.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 10 DELRDNFLRYVAVSSESDPKAGRVPSSEGQRELAMLLARELEALGLVEIELNEHAILTALLPANVEGAPAVGWVAHLDTV 89
Cdd:PRK13381 1 MQLTDRFFRYLKVNSQSDAASGTLPSTPGQHELAKLLADELRELGLEDIVIDEHAIVTAKLPGNTPGAPRIGFIAHLDTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 90 PVSLSPDVKAQVIHYEGGDVLLNAQKDIWVRLEEHPELAAYAGQDIVFTDGTSVLGADNKAAVANVMTMLAVVTRENRPH 169
Cdd:PRK13381 81 DVGLSPDIHPQILRFDGGDLCLNAEQGIWLRTAEHPELLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLENLTENEVEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 170 GDIRVAFVPDEEIGLCGSKLLDLKKFKVDFAYTIDCCALGEIVWETFNACSVSIRIKGVTAHPMSAKGVLVNPLLVATDL 249
Cdd:PRK13381 161 GDIVVAFVPDEEIGLRGAKALDLARFPVDFAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGVLVNPILMANDF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 250 INRFDRLQTPEQTEGKEGYWWFTDCEANAAECRLTMNIRDFDRSRYDSRKAFVLEAVEAVRAQHPRAVIETELVDVYSNI 329
Cdd:PRK13381 241 ISHFPRQETPEHTEGREGYIWVNDLQGNVNKAKLKLIIRDFDLDGFEARKQFIEEVVAKINAKYPTARVSLTLTDQYSNI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 330 ADSLGDDRSPVELLYKAADNLGITTNTIAMRGGTDGSALSAKGLVTPNYFTGACNFHSYAEFLPLPSLHKSLEMTLELVR 409
Cdd:PRK13381 321 SNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEFLPVSSFVKSYEVTITICL 400
|
...
gi 2551629157 410 LTA 412
Cdd:PRK13381 401 LAA 403
|
|
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
10-414 |
0e+00 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 535.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 10 DELRDNFLRYVAVSSESDPKAGRVPSSEGQRELAMLLARELEALGLVEIELNEHAILTALLPANVEG-APAVGWVAHLDT 88
Cdd:PRK05469 2 DKLLERFLRYVKIDTQSDENSTTVPSTEGQWDLAKLLVEELKELGLQDVTLDENGYVMATLPANVDKdVPTIGFIAHMDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 89 VPVSLSPDVKAQVI-HYEGGDVLLNAQkDIWVRLEEHPELAAYAGQDIVFTDGTSVLGADNKAAVANVMTMLAV-VTREN 166
Cdd:PRK05469 82 APDFSGKNVKPQIIeNYDGGDIALGDG-NEVLSPAEFPELKNYIGQTLITTDGTTLLGADDKAGIAEIMTALEYlIAHPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 167 RPHGDIRVAFVPDEEIGLcGSKLLDLKKFKVDFAYTIDCCALGEIVWETFNACSVSIRIKGVTAHPMSAKGVLVNPLLVA 246
Cdd:PRK05469 161 IKHGDIRVAFTPDEEIGR-GADKFDVEKFGADFAYTVDGGPLGELEYENFNAASAKITIHGVNVHPGTAKGKMVNALLLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 247 TDLINRFDRLQTPEQTEGKEGYWWFTDCEANAAECRLTMNIRDFDRSRYDSRKAFVLEAVEAVRAQHPRAVIETELVDVY 326
Cdd:PRK05469 240 ADFHAMLPADETPETTEGYEGFYHLTSIKGTVEEAELSYIIRDFDREGFEARKALMQEIAKKVNAKYGEGRVELEIKDQY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 327 SNIADSLGDDRSPVELLYKAADNLGITTNTIAMRGGTDGSALSAKGLVTPNYFTGACNFHSYAEFLPLPSLHKSLEMTLE 406
Cdd:PRK05469 320 YNMREKIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFHGKFEFVSLESMEKAVEVIVE 399
|
....*...
gi 2551629157 407 LVRLTAGK 414
Cdd:PRK05469 400 IAELTAER 407
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
12-410 |
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: 527.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 12 LRDNFLRYVAVSSESDPKAGRVPSSEGQRELAMLLARELEALGLVEIELNEHAILTALLPANV-EGAPAVGWVAHLDTVP 90
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPSTEGQLELAKLLAKELKELGLEDVTLDEHGYVTATLPANVdKDVPTIGFIAHMDTAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 91 VSLSPDVKAQVIH-YEGGDVLLNAQkDIWVRLEEHPELAAYAGQDIVFTDGTSVLGADNKAAVANVMTMLAVVTRENR-P 168
Cdd:cd03892 81 DNSGKNVKPQIIEnYDGGDIVLNES-GIVLSPAEFPELKNYKGQTLITTDGTTLLGADDKAGIAEIMTALEYLIEHPEiK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 169 HGDIRVAFVPDEEIGlCGSKLLDLKKFKVDFAYTIDCCALGEIVWETFNACSVSIRIKGVTAHPMSAKGVLVNPLLVATD 248
Cdd:cd03892 160 HGDIRVGFTPDEEIG-RGADHFDVEKFGADFAYTLDGGELGELEYENFNAASATITITGVNVHPGTAKGKMVNALLLAAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 249 LINRFDRLQTPEQTEGKEGYWWFTDCEANAAECRLTMNIRDFDRSRYDSRKAFVLEAVEAVRAQHPRAVIETELVDVYSN 328
Cdd:cd03892 239 FHSMLPREETPEHTEGYEGFYHLLSMEGTVEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAKYGEGRVELEIKDQYYN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 329 IADSLGDDRSPVELLYKAADNLGITTNTIAMRGGTDGSALSAKGLVTPNYFTGACNFHSYAEFLPLPSLHKSLEMTLELV 408
Cdd:cd03892 319 MKEKIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRYEFVPVESMEKAVEVIVKIA 398
|
..
gi 2551629157 409 RL 410
Cdd:cd03892 399 EL 400
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
10-412 |
5.14e-132 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 383.63 E-value: 5.14e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 10 DELRDNFLRYVAVSSESDPkagrvpssegQRELAMLLARELEALGLvEIELNEHAILTALLPANVE-GAPAVGWVAHLDT 88
Cdd:COG2195 3 ERLLERFLEYVKIPTPSDH----------EEALADYLVEELKELGL-EVEEDEAGNVIATLPATPGyNVPTIGLQAHMDT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 89 VPVSLSPDVKAQVihyEGGdvllnaqkdiwvrleehpelaayagqdIVFTDGTSVLGADNKAAVANVMTMLAVVTRENRP 168
Cdd:COG2195 72 VPQFPGDGIKPQI---DGG---------------------------LITADGTTTLGADDKAGVAAILAALEYLKEPEIP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 169 HGDIRVAFVPDEEIGLCGSKLLDLKKFKVDFAYTIDCCALGEIVWETFNACSVSIRIKGVTAHPMSAKGVLVNPLLVATD 248
Cdd:COG2195 122 HGPIEVLFTPDEEIGLRGAKALDVSKLGADFAYTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIKLAAR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 249 LINRFDRLQTPEQTEGKEGYWWFTD-CEANAAECRLTMNIRDFDRSRYDSRKAFVLEAVEAVRAQHPRAVIETELVDVYS 327
Cdd:COG2195 202 FLAALPLGRIPEETEGNEGFIHGGSaTNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGVGVVEVEIEDQYP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 328 NIADSlgDDRSPVELLYKAADNLGITTNTIAMRGGTDGSALSAKGLVTPNYFTGACNFHSYAEFLPLPSLHKSLEMTLEL 407
Cdd:COG2195 282 NWKPE--PDSPIVDLAKEAYEELGIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWELLVEI 359
|
....*
gi 2551629157 408 VRLTA 412
Cdd:COG2195 360 LKLIA 364
|
|
| peptidase-T |
TIGR01882 |
peptidase T; This model represents a tripeptide aminopeptidase known as Peptidase T, which has ... |
10-412 |
7.90e-105 |
|
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: 316.07 E-value: 7.90e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 10 DELRDNFLRYVAVSSESDPKAGRVPSSEGQRELAMLLARELEALGLVEIELNEHA-ILTALLPANVE-GAPAVGWVAHLD 87
Cdd:TIGR01882 3 EELLPRFLTYVKVNTRSDENSDTCPSTPGQLTFGNMLVDDLKSLGLQDAHYDEKNgYVIATIPSNTDkDVPTIGFLAHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 88 TVPVSlSPDVKAQVI-HYEGGDVLLNAQKDIWVRLEEHPELAAYAGQDIVFTDGTSVLGADNKAAVANVMTMLAVVTreN 166
Cdd:TIGR01882 83 TADFN-GENVNPQIIeNYDGESIIQLGDLEFTLDPDQFPNLSGYKGQTLITTDGTTLLGADDKAGIAEIMTAADYLI--N 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 167 RP---HGDIRVAFVPDEEIGLcGSKLLDLKKFKVDFAYTIDCCALGEIVWETFNACSVSIRIKGVTAHPMSAKGVLVNPL 243
Cdd:TIGR01882 160 HPeikHGTIRVAFTPDEEIGR-GAHKFDVKDFNADFAYTVDGGPLGELEYETFSAAAAKITIQGNNVHPGTAKGKMINAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 244 LVATDLINRFDRLQTPEQTEGKEGYWWFTDCEANAAECRLTMNIRDFDRSRYDSRKAFVLEAVEAVRAQHPRAVIETELV 323
Cdd:TIGR01882 239 QIAIDLHNLLPEDDRPEYTEGREGFFHLLSIDGTVEEAKLHYIIRDFEKENFQERKELMKRIVEKMNNEYGQDRIKLDMN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 324 DVYSNIADSLGDDRSPVELLYKAADNLGITTNTIAMRGGTDGSALSAKGLVTPNYFTGACNFHSYAEFLPLPSLHKSLEM 403
Cdd:TIGR01882 319 DQYYNMAEKIEKVMEIVDIAKQAMENLGIEPKISPIRGGTDGSQLSYMGLPTPNIFAGGENMHGRFEYISVDNMVKAVDV 398
|
....*....
gi 2551629157 404 TLELVRLTA 412
Cdd:TIGR01882 399 IVEIAKLNE 407
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
12-410 |
3.33e-88 |
|
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: 273.10 E-value: 3.33e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 12 LRDNFLRYVAVSSESDPKAGRVPSSEGQRELAMLLARELEALGLVEIELNEHAILTALLPANVEGA-PAVGWVAHLDTVP 90
Cdd:cd05645 1 LLERFLEYVSLDTQSKAGVRQVPSTEGQWKLLKLLKKQLEELGLINVTLSEKGTLIATLPANVDGDiPAIGFISHVDTSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 91 VSLSPDVKAQVI-HYEGGDVLLNAQkDIWVRLEEHPELAAYAGQDIVFTDGTSVLGADNKAAVANVMTMLAVVTRENRPH 169
Cdd:cd05645 81 DGSGKNVNPQIVeNYRGGDIALGIG-DEVLSPVMFPVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKEKNIPH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 170 GDIRVAFVPDEEIGLcGSKLLDLKKFKVDFAYTIDCCALGEIVWETFNACSVSIRIKGVTAHPMSAKGVLVNPLLVATDL 249
Cdd:cd05645 160 GDIEVAFTPDEEVGK-GAKHFDVEAFTAKWAYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTAKGVGVNALSLAARI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 250 INRFDRLQTPEQTEGKEGYWWFTDCEANAAECRLTMNIRDFDRSRYDSRKAFVLEAVEAV-RAQHPRAVIETELVDVYSN 328
Cdd:cd05645 239 HAEVPADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVgKGLHPDCYIELVIEDSYYN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 329 IADSLGDDRSPVELLYKAADNLGITTNTIAMRGGTDGSALSAKGLVTPNYFTGACNFHSYAEFLPLPSLHKSLEMTLELV 408
Cdd:cd05645 319 FREKVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLEGLEKAVQVIVRIA 398
|
..
gi 2551629157 409 RL 410
Cdd:cd05645 399 EL 400
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
10-409 |
1.07e-39 |
|
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: 145.67 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 10 DELRDNFLRYVAVSSESdpkaGRvpssegQRELAMLLARELEALGLVEIELNEHAI-------LTALLPANVEGAPAVGW 82
Cdd:cd05683 3 DRLINTFLELVQIDSET----LH------EKEISKVLKKKFENLGLSVIEDDAGKTtgggagnLICTLKADKEEVPKILF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 83 VAHLDTVpvslSPdvkaqvihyegGDVLLNAQKDiwvrleehpelaayagQDIVFTDGTSVLGADNKAAVANVMTMLAVV 162
Cdd:cd05683 73 TSHMDTV----TP-----------GINVKPPQIA----------------DGYIYSDGTTILGADDKAGIAAILEAIRVI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 163 TRENRPHGDIRVAFVPDEEIGLCGSKLLDLKKFKVDFAYTIDCCA-LGEIVWETFNACSVSIRIKGVTAHPMSAKGVLVN 241
Cdd:cd05683 122 KEKNIPHGQIQFVITVGEESGLVGAKALDPELIDADYGYALDSEGdVGTIIVGAPTQDKINAKIYGKTAHAGTSPEKGIS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 242 PLLVATDLINRFDRLQTPEQTEGKEGYwwFTDCEAN---AAECRLTMNIRDFDRSRYDSRKAFVLEAVE-AVRAQHPRAV 317
Cdd:cd05683 202 AINIAAKAISNMKLGRIDEETTANIGK--FQGGTATnivTDEVNIEAEARSLDEEKLDAQVKHMKETFEtTAKEKGAHAE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 318 IETELvdVYSNIadSLGDDRSPVELLYKAADNLGITTNTIAMRGGTDGSALSAKGLVTPNYFTGACNFHSYAEFLPLPSL 397
Cdd:cd05683 280 VEVET--SYPGF--KINEDEEVVKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDL 355
|
410
....*....|..
gi 2551629157 398 HKSLEMTLELVR 409
Cdd:cd05683 356 YDTAVLVVEIIK 367
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
12-408 |
2.23e-31 |
|
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: 122.74 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 12 LRDNFLRYVAVSSESdpkagrvpssEGQRELAMLLARELEALGLVEIELNEHAI------LTALLPANVEgAPAVGWVAH 85
Cdd:TIGR01883 2 LKKYFLELIQIDSES----------GKEKAILTYLKKQITKLGIPVSLDEVPAEvsndnnLIARLPGTVK-FDTIFFCGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 86 LDTVPVSLSPdvKAQVihyEGGdvllnaqkdiwvrleehpelaayagqdIVFTDGTSVLGADNKAAVANVMTMLAVVTRE 165
Cdd:TIGR01883 71 MDTVPPGAGP--EPVV---EDG---------------------------IFTSLGGTILGADDKAGVAAMLEAMDVLSTE 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 166 NRPHGDIRVAFVPDEEIGLCGSKLLDLKKFKVDFAYTIDCCA-LGEIVWETFNACSVSIRIKGVTAHPMSAKGVLVNPLL 244
Cdd:TIGR01883 119 ETPHGTIEFIFTVKEELGLIGMRLFDESKITAAYGYCLDAPGeVGNIQLAAPTQVKVDATIAGKDAHAGLVPEDGISAIS 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 245 VATDLINRFDRLQTPEQTEGKEGYwwFTDCEANAAECRlTMNIRDFDRSRYDsRKAF-----VLEAVEAVRAQH-PRAVI 318
Cdd:TIGR01883 199 VARMAIHAMRLGRIDEETTANIGS--FSGGVNTNIVQD-EQLIVAEARSLSF-RKAEaqvqtMRERFEQAAEKYgATLEE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 319 ETELvdVYSniADSLGDDRSPVELLYKAADNLGITTNTIAMRGGTDGSALSAKGLVTPNYFTGACNFHSYAEFLPLPSLH 398
Cdd:TIGR01883 275 ETRL--IYE--GFKIHPQHPLMNIFKKAAKKIGLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETISIEQLV 350
|
410
....*....|
gi 2551629157 399 KSLEMTLELV 408
Cdd:TIGR01883 351 KLAELVIALA 360
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
32-409 |
5.31e-21 |
|
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 93.80 E-value: 5.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 32 RVPS-SEGQRELAMLLARELEALGL-VEIE--LNEHAILTALLPANvEGAPAVGWVAHLDTVPVslspdvkaqvihyegG 107
Cdd:COG0624 23 RIPSvSGEEAAAAELLAELLEALGFeVERLevPPGRPNLVARRPGD-GGGPTLLLYGHLDVVPP---------------G 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 108 DVllnaqkDIWvrleEHPELAAYAGQDIVFTDGTsvlgADNKAAVA-NVMTMLAVVTRENRPHGDIRVAFVPDEEIGLCG 186
Cdd:COG0624 87 DL------ELW----TSDPFEPTIEDGRLYGRGA----ADMKGGLAaMLAALRALLAAGLRLPGNVTLLFTGDEEVGSPG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 187 SK-LLD--LKKFKVDFAYTIDCCALGEIVwetfNAC----SVSIRIKGVTAHPmSAKGVLVNPLLVATDLINRFDRLQTP 259
Cdd:COG0624 153 ARaLVEelAEGLKADAAIVGEPTGVPTIV----TGHkgslRFELTVRGKAAHS-SRPELGVNAIEALARALAALRDLEFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 260 EQTEGKEGYwwfTDCEAN-----------AAECRLTMNIR-----DFDRsrydsrkafVLEAVEA-VRAQHPRAVIETEL 322
Cdd:COG0624 228 GRADPLFGR---TTLNVTgieggtavnviPDEAEAKVDIRllpgeDPEE---------VLAALRAlLAAAAPGVEVEVEV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 323 VDVYSNiADSLGDDRSPVELLYKAADNL-GITTNTIAMRGGTDGSALsAKGLVTPNYFTGA---CNFHSYAEFLPLPSLH 398
Cdd:COG0624 296 LGDGRP-PFETPPDSPLVAAARAAIREVtGKEPVLSGVGGGTDARFF-AEALGIPTVVFGPgdgAGAHAPDEYVELDDLE 373
|
410
....*....|.
gi 2551629157 399 KSLEMTLELVR 409
Cdd:COG0624 374 KGARVLARLLE 384
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
146-409 |
1.87e-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: 79.70 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 146 ADNKAAVANVMTMLAVVTRENRPHGDIRVAFVPDEEIGLCGSK----LLDLKKFKVDFAYtidccalGEIVWETFN---- 217
Cdd:pfam01546 33 DDMKGGLLAALEALRALKEEGLKKGTVKLLFQPDEEGGMGGARalieDGLLEREKVDAVF-------GLHIGEPTLlegg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 218 -----------ACSVSIRIKGVTAH-PMSAKGvlVNPLLVATDLINRFDRLQTPEQTEGKE-----GYWWFTDCEAN--A 278
Cdd:pfam01546 106 iaigvvtghrgSLRFRVTVKGKGGHaSTPHLG--VNAIVAAARLILALQDIVSRNVDPLDPavvtvGNITGIPGGVNviP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 279 AECRLTMNIRDFDrsryDSRKAFVLEAVEAVRAQHPRAVIETELVDVYSNIADSLGDDRSPVELLYKAADNL-GITTNTI 357
Cdd:pfam01546 184 GEAELKGDIRLLP----GEDLEELEERIREILEAIAAAYGVKVEVEYVEGGAPPLVNDSPLVAALREAAKELfGLKVELI 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2551629157 358 A--MRGGTDGSALSAKglVTPNYF---TGACNFHSYAEFLPLPSLHKSLEMTLELVR 409
Cdd:pfam01546 260 VsgSMGGTDAAFFLLG--VPPTVVffgPGSGLAHSPNEYVDLDDLEKGAKVLARLLL 314
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
32-372 |
9.13e-09 |
|
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: 56.54 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 32 RVPSSEG-QRELAMLLARELEALGL-VEIELNEHAiltallpANV------EGAPAVGWVAHLDTVPVslspdvkaqvih 103
Cdd:cd08659 8 QIPSVNPpEAEVAEYLAELLAKRGYgIESTIVEGR-------GNLvatvggGDGPVLLLNGHIDTVPP------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 104 yegGDVllnaqkDIWvrleEHPELAAYAGQDIVFTDGTsvlgADNKAAVANVMT-MLAVVTRENRPHGDIRVAFVPDEEI 182
Cdd:cd08659 69 ---GDG------DKW----SFPPFSGRIRDGRLYGRGA----CDMKGGLAAMVAaLIELKEAGALLGGRVALLATVDEEV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 183 GLCGSKLLDLKkfkvDFAYTIDCCALGE------------IVWetfnacsVSIRIKGVTAH-PMSAKGvlVNPLLVATDL 249
Cdd:cd08659 132 GSDGARALLEA----GYADRLDALIVGEptgldvvyahkgSLW-------LRVTVHGKAAHsSMPELG--VNAIYALADF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 250 INRFDRLQ--------------TPEQTEGkeGYWwftdceAN--AAECRLTMNIR---DFDRSRydsrkafVLEAVEAVR 310
Cdd:cd08659 199 LAELRTLFeelpahpllgpptlNVGVING--GTQ------VNsiPDEATLRVDIRlvpGETNEG-------VIARLEAIL 263
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551629157 311 AQHPRAViETELVDVYSNIADSLGDDRsPVELLYKAADNLGITTNTIAMRGGTDGSALSAKG 372
Cdd:cd08659 264 EEHEAKL-TVEVSLDGDPPFFTDPDHP-LVQALQAAARALGGDPVVRPFTGTTDASYFAKDL 323
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
35-409 |
1.19e-07 |
|
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349889 [Multi-domain] Cd Length: 367 Bit Score: 53.37 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 35 SSEGQRELAMLLARELEALG----LVEIELNEHAILTALLPAnvEGAPAVGWVAHLDTVPVslspdvkaqvihyEGGDvl 110
Cdd:cd03894 13 SRNSNLALIEYVADYLAALGvksrRVPVPEGGKANLLATLGP--GGEGGLLLSGHTDVVPV-------------DGQK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 111 lnaqkdiWvrleEHPELAAYAGQDIVFTDGTsvlgADNKAAVANVMTMLAVVTRENRpHGDIRVAFVPDEEIGLCGSKll 190
Cdd:cd03894 76 -------W----SSDPFTLTERDGRLYGRGT----CDMKGFLAAVLAAVPRLLAAKL-RKPLHLAFSYDEEVGCLGVR-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 191 DLKKFKVDFAYTIDCCALGE-----IVwetfNA----CSVSIRIKGVTAH-PMSAKGvlVNPLLVATDLINRFDRLQTPE 260
Cdd:cd03894 138 HLIAALAARGGRPDAAIVGEptslqPV----VAhkgiASYRIRVRGRAAHsSLPPLG--VNAIEAAARLIGKLRELADRL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 261 QTEGKEGYWW--FTDCEAN-----------AAECRLTMNIR---DFDRSRYDSRkafvLEAVEAVRAQHPRAVIETELVD 324
Cdd:cd03894 212 APGLRDPPFDppYPTLNVGlihggnavnivPAECEFEFEFRplpGEDPEAIDAR----LRDYAEALLEFPEAGIEVEPLF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 325 VYsniADSLGDDRSP-VELLYKAADNlgitTNTIAMRGGTDGSALSAKGLVTPNYFTGACN-FHSYAEFLPLPSLHKSLE 402
Cdd:cd03894 288 EV---PGLETDEDAPlVRLAAALAGD----NKVRTVAYGTEAGLFQRAGIPTVVCGPGSIAqAHTPDEFVELEQLDRCEE 360
|
....*..
gi 2551629157 403 MTLELVR 409
Cdd:cd03894 361 FLRRLIA 367
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
32-375 |
2.25e-07 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 52.45 E-value: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 32 RVPSSEGQR-ELAMLLARELEALGL-VEIELNEHAIltALLpanVEGAPAVGWVAHLDTVPVSLSPDVkaqvihyEGGdv 109
Cdd:PRK08652 13 KIPSPSGQEdEIALHIMEFLESLGYdVHIESDGEVI--NIV---VNSKAELFVEVHYDTVPVRAEFFV-------DGV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 110 llnaqkdiwvrleehpelaayagqdIVFTDGTSvlgaDNKAAVANVMTMLAVVTRENRpHGDIRVAFVPDEEIGLCGSKL 189
Cdd:PRK08652 79 -------------------------YVYGTGAC----DAKGGVAAILLALEELGKEFE-DLNVGIAFVSDEEEGGRGSAL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 190 LdLKKFKVDFAYTIDCCALgEIVWETFNACSVSIRIKGVTAH---PMSAkgvlVNPLLVATDLINRFDRLQtPEQTEGKE 266
Cdd:PRK08652 129 F-AERYRPKMAIVLEPTDL-KVAIAHYGNLEAYVEVKGKPSHgacPESG----VNAIEKAFEMLEKLKELL-KALGKYFD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 267 GYWWFTDCEANA------AECRLTMNIR---DFDRSRYDSRKAFVLEAVEavraqhpravIETELVDVYSNIadSLGDDR 337
Cdd:PRK08652 202 PHIGIQEIIGGSpeysipALCRLRLDARippEVEVEDVLDEIDPILDEYT----------VKYEYTEIWDGF--ELDEDE 269
|
330 340 350
....*....|....*....|....*....|....*...
gi 2551629157 338 SPVELLYKAADNLGITTNTIAMRGGTDGSALSAKGLVT 375
Cdd:PRK08652 270 EIVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTKT 307
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
34-414 |
2.38e-07 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 52.30 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 34 PSSEGQRELAMLLARELEALGL-VEI------ELNEHAILT-ALLPANVEGAPAVGWVAHLDTVPvslspdvkaqvihye 105
Cdd:PRK08651 23 PPGENYEEIAEFLRDTLEELGFsTEIievpneYVKKHDGPRpNLIARRGSGNPHLHFNGHYDVVP--------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 106 ggdvllnaQKDIWvrlEEHPELAAYAGQDIVFTDGTSvlgaDNKAAVAnvmTMLAVVTRENrPHGDIRV--AFVPDEEIG 183
Cdd:PRK08651 88 --------PGEGW---SVNVPFEPKVKDGKVYGRGAS----DMKGGIA---ALLAAFERLD-PAGDGNIelAIVPDEETG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 184 LCGSKLLDLK-KFKVDFAYTIDCCALGEIVWETFNACSVSIRIKGVTAH---PMSAkgvlVNPLLVATDLInrfDRLQTp 259
Cdd:PRK08651 149 GTGTGYLVEEgKVTPDYVIVGEPSGLDNICIGHRGLVWGVVKVYGKQAHastPWLG----INAFEAAAKIA---ERLKS- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 260 EQTEGKEGYWWFTDCEANA-------------------AECRLTMNIRDFDRSRYDSRKAFVLEAVEAVRAQHPRAVIet 320
Cdd:PRK08651 221 SLSTIKSKYEYDDERGAKPtvtlggptveggtktnivpGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVE-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 321 elVDVYSNIADSLGDDRSP-VELLYKAA-DNLGITTNTIAMRGGTDGSALSAKGLVTPNYFTGAC-NFHSYAEFLPLPSL 397
Cdd:PRK08651 299 --FEITPFSEAFVTDPDSElVKALREAIrEVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGELeLAHAPDEYVEVKDV 376
|
410
....*....|....*..
gi 2551629157 398 HKSLEMTLELVRLTAGK 414
Cdd:PRK08651 377 EKAAKVYEEVLKRLAKG 393
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
75-207 |
3.08e-07 |
|
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: 50.50 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 75 EGAPAVGWVAHLDTVPVslspdvkaqvihyeggdvllnaqkdiwvrLEEHPELAAYAGQDIVFTDGTSVLGADNKAAVAN 154
Cdd:cd03873 10 EGGKSVALGAHLDVVPA-----------------------------GEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAA 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2551629157 155 VMTMLAV-VTRENRPHGDIRVAFVPDEEIGLCG-----SKLLDLKKFKVDFAYTIDCCA 207
Cdd:cd03873 61 ALEALKRlKENGFKPKGTIVVAFTADEEVGSGGgkgllSKFLLAEDLKVDAAFVIDATA 119
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
214-313 |
5.67e-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: 5.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 214 ETFNACSVSIRIKGVTAHPmSAKGVLVNPLLVATDLINRFDRLQ----------TPEQTEGKEGYWwftdceANA--AEC 281
Cdd:pfam07687 2 GHKGLAGGHLTVKGKAGHS-GAPGKGVNAIKLLARLLAELPAEYgdigfdfprtTLNITGIEGGTA------TNVipAEA 74
|
90 100 110
....*....|....*....|....*....|..
gi 2551629157 282 RLTMNIRdfdRSRYDSRKAfVLEAVEAVRAQH 313
Cdd:pfam07687 75 EAKFDIR---LLPGEDLEE-LLEEIEAILEKE 102
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
75-204 |
2.26e-06 |
|
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: 47.81 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 75 EGAPAVGWVAHLDTVPVslspdvkaqvihyeggdvllnaqkdiwvrLEEHPELAAYAGQDIVFTDGTSVLGADNKAAVAN 154
Cdd:cd18669 10 GGGKRVLLGAHIDVVPA-----------------------------GEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAA 60
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2551629157 155 VMTMLAV-VTRENRPHGDIRVAFVPDEEIG-----LCGSKLLDLKKFKVDFAYTID 204
Cdd:cd18669 61 ALEALKLlKENGFKLKGTVVVAFTPDEEVGsgagkGLLSKDALEEDLKVDYLFVGD 116
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
75-226 |
7.36e-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: 47.90 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 75 EGAPAVGWVAHLDTVPVSLSpdvkaqvihyeggDVLLNAQKDiwvrleehPeLAAYAGQDIVFTDGTSvLGADNKAAVAn 154
Cdd:cd03890 58 ENAPPVILQGHMDMVCEKNA-------------DSEHDFEKD--------P-IKLRIDGDWLKATGTT-LGADNGIGVA- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 155 vmTMLAVVTRENRPHGDIRVAFVPDEEIGLCGSKLLDLKKFKVDFAYTIDC---------CALG-------EIVWETFNA 218
Cdd:cd03890 114 --YALAILEDKDIEHPPLEVLFTVDEETGMTGALGLDPSLLKGKILLNLDSeeegeltvgCAGGidvtitlPIEREEAEG 191
|
....*...
gi 2551629157 219 CSVSIRIK 226
Cdd:cd03890 192 GYTGLKIT 199
|
|
| Peptidase_M28 |
pfam04389 |
Peptidase family M28; |
145-188 |
1.84e-03 |
|
Peptidase family M28;
Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 39.19 E-value: 1.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2551629157 145 GA-DNKAAVANVMTMLAVVTRENRPHGDIRVAFVPDEEIGLCGSK 188
Cdd:pfam04389 29 GAdDNASGVAALLELARVLAAGQRPKRSVRFLFFDAEEAGLLGSH 73
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| M28 |
cd02690 |
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ... |
142-205 |
2.03e-03 |
|
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; 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. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases.
Pssm-ID: 349868 [Multi-domain] Cd Length: 202 Bit Score: 39.25 E-value: 2.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551629157 142 SVLGA-DNKAAVAnVMTMLA-VVTREN-RPHGDIRVAFVPDEEIGLCGSK--LLDLKKF--KVDFAYTIDC 205
Cdd:cd02690 29 LSPGAnDNASGVA-VLLELArVLSKLQlKPKRSIRFAFWDAEELGLLGSKyyAEQLLSSlkNIRAALNLDM 98
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|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
156-258 |
6.26e-03 |
|
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: 38.35 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551629157 156 MTML-----AVVTRENRPHGDIRVAFVPDEEIGLCGSKLLD---LKKFKVDFAYTIDC---CALGEIVWE--TFNA--CS 220
Cdd:cd03886 94 TAMLlgaakLLAERRDPLKGTVRFIFQPAEEGPGGAKAMIEegvLENPGVDAAFGLHVwpgLPVGTVGVRsgALMAsaDE 173
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90 100 110
....*....|....*....|....*....|....*...
gi 2551629157 221 VSIRIKGVTAHPmSAKGVLVNPLLVATDLINrfdRLQT 258
Cdd:cd03886 174 FEITVKGKGGHG-ASPHLGVDPIVAAAQIVL---ALQT 207
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