|
Name |
Accession |
Description |
Interval |
E-value |
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
38-402 |
4.48e-113 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 335.22 E-value: 4.48e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 38 IEEQIVIAEIPAPPFKEEKRATFILSKLEDLALENVEMDEEGNVFGLLRGVGNGPKIFVSAHLDTVFPEGTDTTVKRENG 117
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGLGDVERDGRGNVVGRLRGTGGGPALLFSAHLDTVFPGDTPATVRHEGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 118 ILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTVGEEGLGNLRGVRAFFNNHQDI-DGFISIDGPEiSRICYK 196
Cdd:cd03896 81 RIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEGLGDLRGARYLLSAHGARlDYFVVAEGTD-GVPHTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 197 GTGSYRYKVTYKGPGGHSFGAFGLPSAIHALGRAIAEIADIQTKADPKTTFTVGEISGGTSVNAIAAEAHMYVDLRSNDP 276
Cdd:cd03896 160 AVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAPYVPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 277 QELVKLEQQFLTIVEKACNDENarwntdKIKWKTEKIGDRPAATQPDDTPIVQIASAATEAMGIKPTLaGPSSTDSNVPM 356
Cdd:cd03896 240 AELADVQREVEAVVSKLAAKHL------RVKARVKPVGDRPGGEAQGTEPLVNAAVAAHREVGGDPRP-GSSSTDANPAN 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 517982453 357 SLGVPSVTLGKGGkSGGAHTLDEWFDPTDSYLGPQRTFLTIVGLVG 402
Cdd:cd03896 313 SLGIPAVTYGLGR-GGNAHRGDEYVLKDDMLKGAKAYLMLAAALCG 357
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
27-382 |
1.79e-68 |
|
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: 221.68 E-value: 1.79e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 27 LKFLKEDHENTIE--EQIViaEIPAPPFKEEKRATFILSKLEDLALEnVEMDEE----GNVFGLLRGVGNGPKIFVSAHL 100
Cdd:COG0624 4 LAAIDAHLDEALEllRELV--RIPSVSGEEAAAAELLAELLEALGFE-VERLEVppgrPNLVARRPGDGGGPTLLLYGHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 101 DTVFPEGTDT------TVKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTVGEEGLGNlrGVRAFFN 174
Cdd:COG0624 81 DVVPPGDLELwtsdpfEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSP--GARALVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 175 NHQD---IDGFISIDGPEISRICYKGTGSYRYKVTYKGPGGHSfGAFGL-PSAIHALGRAIAEIADIQ--TKADP---KT 245
Cdd:COG0624 159 ELAEglkADAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAHS-SRPELgVNAIEALARALAALRDLEfdGRADPlfgRT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 246 TFTVGEISGGTSVNAIAAEAHMYVDLRSNDPQELVKLEQQFLTIVEKACNDenarwntdkIKWKTEKIGD-RPAATQPDD 324
Cdd:COG0624 238 TLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPG---------VEVEVEVLGDgRPPFETPPD 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517982453 325 TPIVQIASAA-TEAMGIKPTLAG-PSSTDSNVPM-SLGVPSVTLGkGGKSGGAHTLDEWFD 382
Cdd:COG0624 309 SPLVAAARAAiREVTGKEPVLSGvGGGTDARFFAeALGIPTVVFG-PGDGAGAHAPDEYVE 368
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
44-380 |
8.80e-46 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 161.76 E-value: 8.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 44 IAEIPAPPFKEEKRATFILSKLEDLALEnVEMDEEGNVFGLLRG-VG-NGPKIFVSAHLDTV--FPeGTDTTVKRENGIL 119
Cdd:COG2195 12 YVKIPTPSDHEEALADYLVEELKELGLE-VEEDEAGNVIATLPAtPGyNVPTIGLQAHMDTVpqFP-GDGIKPQIDGGLI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 120 YAPGI----VDDTSGLAEMLSIIRAFKETKIePIGDIVFGGTVGEEGlgNLRGVRAFfnnhqDIDGF-----ISIDGPEI 190
Cdd:COG2195 90 TADGTttlgADDKAGVAAILAALEYLKEPEI-PHGPIEVLFTPDEEI--GLRGAKAL-----DVSKLgadfaYTLDGGEE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 191 SRICYKGTGSYRYKVTYKGPGGHS-FGAFGLPSAIHALGRAIAEIADIQTkaDPKTTFTVGEISGGTSVNAIAAEAHMYV 269
Cdd:COG2195 162 GELEYECAGAADAKITIKGKGGHSgDAKEKMINAIKLAARFLAALPLGRI--PEETEGNEGFIHGGSATNAIPREAEAVY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 270 DLRSNDPQELVKLEQQFLTIVEKacndENARWNTDKIKWKTEkiGDRPAATQPDDTPIVQIASAATEAMGIKPTL----A 345
Cdd:COG2195 240 IIRDHDREKLEARKAELEEAFEE----ENAKYGVGVVEVEIE--DQYPNWKPEPDSPIVDLAKEAYEELGIEPKIkpirG 313
|
330 340 350
....*....|....*....|....*....|....*
gi 517982453 346 GpssTDSNVPMSLGVPSVTLGKGGKsgGAHTLDEW 380
Cdd:COG2195 314 G---LDGGILSFKGLPTPNLGPGGH--NFHSPDER 343
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
96-385 |
2.58e-39 |
|
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: 143.26 E-value: 2.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 96 VSAHLDTVFPEGTDTT--VKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPiGDIVFGGTVGEEGLgnLRGVRAFF 173
Cdd:pfam01546 2 LRGHMDVVPDEETWGWpfKSTEDGKLYGRGHDDMKGGLLAALEALRALKEEGLKK-GTVKLLFQPDEEGG--MGGARALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 174 NNHQ----DIDGFISI--------DGPEISRICYKGTGSYRYKVTYKGPGGHSfGAFGL-PSAIHALGRAIAEIADI--- 237
Cdd:pfam01546 79 EDGLlereKVDAVFGLhigeptllEGGIAIGVVTGHRGSLRFRVTVKGKGGHA-STPHLgVNAIVAAARLILALQDIvsr 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 238 QTKADPKTTFTVGEISG-GTSVNAIAAEAHMYVDLRSNDPQELVKLEQQFLTIVEKACNDENARWntdKIKWKTekiGDR 316
Cdd:pfam01546 158 NVDPLDPAVVTVGNITGiPGGVNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKV---EVEYVE---GGA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517982453 317 PAATqpDDTPIVQ-IASAATEAMGIKP---TLAGPSSTDSNVpMSLGVPSVTLGKGGKSGGAHTLDEWFDPTD 385
Cdd:pfam01546 232 PPLV--NDSPLVAaLREAAKELFGLKVeliVSGSMGGTDAAF-FLLGVPPTVVFFGPGSGLAHSPNEYVDLDD 301
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
40-380 |
2.63e-37 |
|
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: 138.97 E-value: 2.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 40 EQIViaEIPAPPFKEEKRATFILSKLEDL--ALENVEMDEEGNVFGLLRGvGNGPKIFVSAHLDTVfPEGTDTT------ 111
Cdd:cd08659 4 QDLV--QIPSVNPPEAEVAEYLAELLAKRgyGIESTIVEGRGNLVATVGG-GDGPVLLLNGHIDTV-PPGDGDKwsfppf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 112 -VKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTVGEEGlgNLRGVRAFFNN--HQDIDGFIsIDGP 188
Cdd:cd08659 80 sGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEV--GSDGARALLEAgyADRLDALI-VGEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 189 EISRICYKGTGSYRYKVTYKGPGGHSFGAFGLPSAIHALGRAIAEIADIQTKAD-----PKTTFTVGEISGGTSVNAIAA 263
Cdd:cd08659 157 TGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPahpllGPPTLNVGVINGGTQVNSIPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 264 EAHMYVDLRSN---DPQELVKLeqqFLTIVEKACNDENARWNTDkikwktekiGDRPAATQPDDtPIVQIASAATEAMGI 340
Cdd:cd08659 237 EATLRVDIRLVpgeTNEGVIAR---LEAILEEHEAKLTVEVSLD---------GDPPFFTDPDH-PLVQALQAAARALGG 303
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 517982453 341 KPTLAG-PSSTD-SNVPMSLGVPSVTLGKgGKSGGAHTLDEW 380
Cdd:cd08659 304 DPVVRPfTGTTDaSYFAKDLGFPVVVYGP-GDLALAHQPDEY 344
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
35-379 |
1.74e-29 |
|
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: 117.55 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 35 ENTIEEQIVIAEIPAPPFKEEKRATFILSKLEDLALENVEMD-------EEGNVFGLLRGVG-NGPKIFVSAHLDTVFPE 106
Cdd:cd05683 3 DRLINTFLELVQIDSETLHEKEISKVLKKKFENLGLSVIEDDagkttggGAGNLICTLKADKeEVPKILFTSHMDTVTPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 107 GTDTTVKRENGILYAPGIV----DDTSGLAEMLSIIRAFKETKIePIGDIVFGGTVGEEGlgNLRGVRAFfnNHQDID-- 180
Cdd:cd05683 83 INVKPPQIADGYIYSDGTTilgaDDKAGIAAILEAIRVIKEKNI-PHGQIQFVITVGEES--GLVGAKAL--DPELIDad 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 181 -GFISIDGPEISRICYKGTGSYRYKVTYKGPGGHsfgAFGLP----SAIHALGRAIAEIADIQTkaDPKTTFTVGEISGG 255
Cdd:cd05683 158 yGYALDSEGDVGTIIVGAPTQDKINAKIYGKTAH---AGTSPekgiSAINIAAKAISNMKLGRI--DEETTANIGKFQGG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 256 TSVNAIAAEAHMYVDLRSNDPQELVKLEQQFLTIVEKACNDENArwntdKIKWKTEKIgdRPAATQPDDTPIVQIASAAT 335
Cdd:cd05683 233 TATNIVTDEVNIEAEARSLDEEKLDAQVKHMKETFETTAKEKGA-----HAEVEVETS--YPGFKINEDEEVVKLAKRAA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 517982453 336 EAMGIKP-TLAGPSSTDSNVPMSLGVPSVTLGKGGKSggAHTLDE 379
Cdd:cd05683 306 NNLGLEInTTYSGGGSDANIINGLGIPTVNLGIGYEN--IHTTNE 348
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
79-380 |
2.53e-29 |
|
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: 116.92 E-value: 2.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 79 GNVFGLLRGvGNGPKIFVSAHLDTVFPEGT--DTTVKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFGG 156
Cdd:cd03885 49 DHLIATFKG-TGGKRVLLIGHMDTVFPEGTlaFRPFTVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 157 TVGEEgLGNL----------RGVRAFFN-NHQDIDGFISIdgpeiSRicyKGTGsyRYKVTYKGPGGHSfgafglpSAIH 225
Cdd:cd03885 128 NSDEE-IGSPgsrelieeeaKGADYVLVfEPARADGNLVT-----AR---KGIG--RFRLTVKGRAAHA-------GNAP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 226 ALGR-AIAEIADI------QTKADPKTTFTVGEISGGTSVNAIAAEAHMYVDLRSNDPQELVKLEQQFLTIVEkacnden 298
Cdd:cd03885 190 EKGRsAIYELAHQvlalhaLTDPEKGTTVNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVA------- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 299 arwNTDKIKWKTEKIGD--RPAATQPDDT-PIVQIASAATEAMGIkpTLAGPSS---TDSNVPMSLGVPSV-TLGKGGks 371
Cdd:cd03885 263 ---TTLVPGTSVELTGGlnRPPMEETPASrRLLARAQEIAAELGL--TLDWEATgggSDANFTAALGVPTLdGLGPVG-- 335
|
....*....
gi 517982453 372 GGAHTLDEW 380
Cdd:cd03885 336 GGAHTEDEY 344
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
46-379 |
1.10e-24 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that 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: 349904 [Multi-domain] Cd Length: 343 Bit Score: 103.59 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 46 EIPAPPFKEEKRATFILSKLEDLALEnVEMDEEGNVFGLlRGVGnGPKIFVSAHLDTVfPegTDTTVKRENGILYAPGIV 125
Cdd:cd05653 12 SIYSPSGEEARAAKFLEEIMKELGLE-AWVDEAGNAVGG-AGSG-PPDVLLLGHIDTV-P--GEIPVRVEGGVLYGRGAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 126 DDTSGLAEMlsiIRAFKETKIEPIGDIVFGGTVGEEglGNLRGVRAFFNNHQDIDgFISIDGPE-ISRICYKGTGSYRYK 204
Cdd:cd05653 86 DAKGPLAAM---ILAASALNEELGARVVVAGLVDEE--GSSKGARELVRRGPRPD-YIIIGEPSgWDGITLGYRGSLLVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 205 VTYKGPGGHSFGAfgLPSAIHALGRAIAEI----ADIQTKADPKTTFTVGEISGGTSVNAIAAEAHMYVDLR---SNDPQ 277
Cdd:cd05653 160 IRCEGRSGHSSSP--ERNAAEDLIKKWLEVkkwaEGYNVGGRDFDSVVPTLIKGGESSNGLPQRAEATIDLRlppRLSPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 278 ELVKLEQQFLTivekacndenarwnTDKIKWktekIGDRPAATQPDDTPIVQIASAATEAMGIKPTLAGPSST-DSNV-P 355
Cdd:cd05653 238 EAIALATALLP--------------TCELEF----IDDTEPVKVSKNNPLARAFRRAIRKQGGKPRLKRKTGTsDMNVlA 299
|
330 340
....*....|....*....|....
gi 517982453 356 MSLGVPSVTLGKgGKSGGAHTLDE 379
Cdd:cd05653 300 PLWTVPIVAYGP-GDSTLDHTPNE 322
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
65-380 |
3.89e-21 |
|
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: 93.81 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 65 LEDLALE-NVEMDEEGNVFGLL--RGVGNGPKIFVSAHLDTVFPEG----TDT-TVKRENGILYAPGIVDDTSGLAEMLS 136
Cdd:cd03894 28 LAALGVKsRRVPVPEGGKANLLatLGPGGEGGLLLSGHTDVVPVDGqkwsSDPfTLTERDGRLYGRGTCDMKGFLAAVLA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 137 IIRAFKETKIEPigDIVFGGTVGEEGlgNLRGVRAFFNNHQD----IDGFIsIDGPEISR--ICYKGTGSYRykVTYKGP 210
Cdd:cd03894 108 AVPRLLAAKLRK--PLHLAFSYDEEV--GCLGVRHLIAALAArggrPDAAI-VGEPTSLQpvVAHKGIASYR--IRVRGR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 211 GGHSFGAFGLPSAIHALGRAIAEIADIQ-----TKAD-----PKTTFTVGEISGGTSVNAIAAEAHMYVDLR---SNDPQ 277
Cdd:cd03894 181 AAHSSLPPLGVNAIEAAARLIGKLRELAdrlapGLRDppfdpPYPTLNVGLIHGGNAVNIVPAECEFEFEFRplpGEDPE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 278 ElvkLEQQFLTIVEKACNDENARwntdkIkwKTEKIGDRPAATQPDDTPIVQIASAATeamGIKPTLAGPSSTDSNVPMS 357
Cdd:cd03894 261 A---IDARLRDYAEALLEFPEAG-----I--EVEPLFEVPGLETDEDAPLVRLAAALA---GDNKVRTVAYGTEAGLFQR 327
|
330 340
....*....|....*....|...
gi 517982453 358 LGVPSVTLGKGGKSgGAHTLDEW 380
Cdd:cd03894 328 AGIPTVVCGPGSIA-QAHTPDEF 349
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
36-389 |
2.59e-18 |
|
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.
Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 86.04 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 36 NTIEEqivIAEIPAPPF---------KEEKRAT-FILSKLEDLALEnVEMDEEGNVFGLLRGVGNG-PKIFVSAHLDTVf 104
Cdd:cd03884 3 DRLEE---LAAIGATPAggvtrlaltDEDRAARdLFVEWMEEAGLS-VRVDAVGNLFGRLEGTDPDaPPVLTGSHLDTV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 105 PEGtdttvKRENGILyapGIVddtSGLAemlsIIRAFKETKIEPIGDIVFGGTVGEEGL---GNLRGVRAFF-------- 173
Cdd:cd03884 78 PNG-----GRYDGIL---GVL---AGLE----ALRALKEAGIRPRRPIEVVAFTNEEGSrfpPSMLGSRAFAgtldleel 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 174 NNHQDIDGfISIdGPEISRICYKGT---------------------------------------GSYRYKVTYKGPGGHS 214
Cdd:cd03884 143 LSLRDADG-VSL-AEALKAIGYDGDrpasarrpgdikayvelhieqgpvleeeglpigvvtgiaGQRWLEVTVTGEAGHA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 215 fGAfgLP-----SAIHALGRAIAEIADIQTKADPKTTFTVGEIS---GgtSVNAIAAEAHMYVDLRSNDPQELVKLEQQF 286
Cdd:cd03884 221 -GT--TPmalrrDALLAAAELILAVEEIALEHGDDLVATVGRIEvkpN--AVNVIPGEVEFTLDLRHPDDAVLDAMVERI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 287 LTIVEKACNDEnarwntdKIKWKTEKIGDRPAAtqPDDTPIVQIASAATEAMGIKPTL----AGPSS--TDSNVPMS-LG 359
Cdd:cd03884 296 RAEAEAIAAER-------GVEVEVERLWDSPPV--PFDPELVAALEAAAEALGLSYRRmpsgAGHDAmfMARICPTAmIF 366
|
410 420 430
....*....|....*....|....*....|
gi 517982453 360 VPSvtlgKGGKSggaHTLDEWFDPTDSYLG 389
Cdd:cd03884 367 VPS----RDGIS---HNPAEYTSPEDLAAG 389
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
88-388 |
6.62e-18 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 84.55 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 88 VGNGPKIF-VSAHLDTVFPEGTDT------TVKRENGILYAPGIVDDTSGLAEM-LSIIRaFKETKIEPIGDIVFGGTVG 159
Cdd:PRK08588 55 IGSGSPVLaLSGHMDVVAAGDVDKwtydpfELTEKDGKLYGRGATDMKSGLAALvIAMIE-LKEQGQLLNGTIRLLATAG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 160 EEgLGNLrGVRAFFNNH--QDIDGFIsIDGPEISRICYKGTGSYRYKVTYKGPGGHSfgafGLPS----AIHALGRAIAE 233
Cdd:PRK08588 134 EE-VGEL-GAKQLTEKGyaDDLDALI-IGEPSGHGIVYAHKGSMDYKVTSTGKAAHS----SMPElgvnAIDPLLEFYNE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 234 I----ADIQTKAD--PKTTFTVGEISGGTSVNAIAAEAHMYVDLRS-----NDpqelvKLEQQFLTIVEKaCNDENArwn 302
Cdd:PRK08588 207 QkeyfDSIKKHNPylGGLTHVVTIINGGEQVNSVPDEAELEFNIRTipeydND-----QVISLLQEIINE-VNQNGA--- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 303 tdkIKWKTEKIGDRPAATQPDDTPIVQIA-SAATEAMGIKPTLAG-PSSTDSNVPMSLG--VPSVTLGKgGKSGGAHTLD 378
Cdd:PRK08588 278 ---AQLSLDIYSNHRPVASDKDSKLVQLAkDVAKSYVGQDIPLSAiPGATDASSFLKKKpdFPVIIFGP-GNNLTAHQVD 353
|
330
....*....|
gi 517982453 379 EWFDpTDSYL 388
Cdd:PRK08588 354 EYVE-KDMYL 362
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
27-382 |
8.36e-18 |
|
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: 83.98 E-value: 8.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 27 LKFLKEdhentieeqIVIAEIPAPPFKE-EKRATFILSKLEDLALEN--VEMDEEG-NVFGLLRGVGNGPKIFVSAHLDt 102
Cdd:cd08011 1 VKLLQE---------LVQIPSPNPPGDNtSAIAAYIKLLLEDLGYPVelHEPPEEIyGVVSNIVGGRKGKRLLFNGHYD- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 103 VFPEGTD-------TTVKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTVGEEGLGNLrGVRAFFNN 175
Cdd:cd08011 71 VVPAGDGegwtvdpYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRA-GTKYLLEK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 176 HQDIDGFISIDGPEISR-ICYKGTGSYRYKVTYKGPGGHSfgafGLP----SAIHALGRAIAEIADIQTkadpktTFTVG 250
Cdd:cd08011 150 VRIKPNDVLIGEPSGSDnIRIGEKGLVWVIIEITGKPAHG----SLPhrgeSAVKAAMKLIERLYELEK------TVNPG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 251 EISGGTSVNAIAAEAHMYVDLR---SNDPQELVKLEQQFLTIVEKACNDENARWNTDkikwktekigdrpaATQPDDtPI 327
Cdd:cd08011 220 VIKGGVKVNLVPDYCEFSVDIRlppGISTDEVLSRIIDHLDSIEEVSFEIKSFYSPT--------------VSNPDS-EI 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 517982453 328 VQ-IASAATEAMGIKP-TLAGPSSTDSNVPMSLGVPSVTLGKgGKSGGAHTLDEWFD 382
Cdd:cd08011 285 VKkTEEAITEVLGIRPkEVISVGASDARFYRNAGIPAIVYGP-GRLGQMHAPNEYVE 340
|
|
| PRK12893 |
PRK12893 |
Zn-dependent hydrolase; |
66-389 |
1.15e-15 |
|
Zn-dependent hydrolase;
Pssm-ID: 237250 [Multi-domain] Cd Length: 412 Bit Score: 78.00 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 66 EDLALEnVEMDEEGNVFGLLRGVGNG-PKIFVSAHLDTVfPEGtdttvKRENGILyapGIVddtSGLAemlsIIRAFKET 144
Cdd:PRK12893 51 EEAGLT-VSVDAIGNLFGRRAGTDPDaPPVLIGSHLDTQ-PTG-----GRFDGAL---GVL---AALE----VVRTLNDA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 145 KIEPIGDIVFGGTVGEEGLgnlR------GVRAFFNNH--------QDIDGfISIdGPEISRICYKGT------------ 198
Cdd:PRK12893 114 GIRTRRPIEVVSWTNEEGA---RfapamlGSGVFTGALplddalarRDADG-ITL-GEALARIGYRGTarvgrravdayl 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 199 ------------------------GSYRYKVTYKGPGGHSfGAFGLP---SAIHALGRAIAEIADIQTKADPKTTFTVGE 251
Cdd:PRK12893 189 elhieqgpvleaeglpigvvtgiqGIRWLEVTVEGQAAHA-GTTPMAmrrDALVAAARIILAVERIAAALAPDGVATVGR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 252 IS---GgtSVNAIAAEAHMYVDLRSNDPQELvkleQQFLTIVEKACNDENARWNtdkIKWKTEKIGDRPAATQPDDtpIV 328
Cdd:PRK12893 268 LRvepN--SRNVIPGKVVFTVDIRHPDDARL----DAMEAALRAACAKIAAARG---VQVTVETVWDFPPVPFDPA--LV 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517982453 329 QIASAATEAMGIK----PTLAG----------PSStdsnvpMsLGVPSvtlgKGGKSggaHTLDEWFDPTDSYLG 389
Cdd:PRK12893 337 ALVEAAAEALGLShmrmVSGAGhdamflarvaPAA------M-IFVPC----RGGIS---HNEAEDTEPADLAAG 397
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
199-294 |
1.44e-15 |
|
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: 71.99 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 199 GSYRYKVTYKGPGGHSfGAFGL-PSAIHALGRAIAEIADIQ---TKADPKTTFTVGEISGGTSVNAIAAEAHMYVDLRSN 274
Cdd:pfam07687 5 GLAGGHLTVKGKAGHS-GAPGKgVNAIKLLARLLAELPAEYgdiGFDFPRTTLNITGIEGGTATNVIPAEAEAKFDIRLL 83
|
90 100
....*....|....*....|
gi 517982453 275 DPQELVKLEQQFLTIVEKAC 294
Cdd:pfam07687 84 PGEDLEELLEEIEAILEKEL 103
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
57-385 |
3.81e-15 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 76.73 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 57 RATFIlSKLEDLALEnVEMDEEGNVFGLLRGVG-NGPKIFVSAHLDTVfPEGtdttvKRENGILyapGIVddtSGLAeml 135
Cdd:PRK09290 40 RDLFA-EWMEAAGLT-VRVDAVGNLFGRLEGRDpDAPAVLTGSHLDTV-PNG-----GRFDGPL---GVL---AGLE--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 136 sIIRAFKETKIE---PIGDIVFGGtvgEEG-------LGNlrgvRAFF--------NNHQDIDGfISIdGPEISRICYKG 197
Cdd:PRK09290 103 -AVRTLNERGIRprrPIEVVAFTN---EEGsrfgpamLGS----RVFTgaltpedaLALRDADG-VSF-AEALAAIGYDG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 198 T----------------------------------------GSYRYKVTYKGPGGHSfGAFGLPS---AIHALGRAIAEI 234
Cdd:PRK09290 173 DeavgaararrdikafvelhieqgpvleaeglpigvvtgivGQRRYRVTFTGEANHA-GTTPMALrrdALLAAAEIILAV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 235 ADIQTKADPKTTFTVGEIS---GgtSVNAIAAEAHMYVDLRSNDPQELVKLEQQFLTIVEKACNDEnarwntdKIKWKTE 311
Cdd:PRK09290 252 ERIAAAHGPDLVATVGRLEvkpN--SVNVIPGEVTFTLDIRHPDDAVLDALVAELRAAAEAIAARR-------GVEVEIE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 312 KIGDRPAAtqPDDTPIVQIASAATEAMGIK----PTLAGpssTDSN-----VPMS-LGVPSvtlgKGGKSggaHTLDEWF 381
Cdd:PRK09290 323 LISRRPPV--PFDPGLVAALEEAAERLGLSyrrlPSGAG---HDAQilaavVPTAmIFVPS----VGGIS---HNPAEFT 390
|
....
gi 517982453 382 DPTD 385
Cdd:PRK09290 391 SPED 394
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
77-379 |
2.93e-14 |
|
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.
Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 73.93 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 77 EEGNVFGLLRGVGNGPK-IFVSAHLDTVFPEGTDTTV-----KRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIG 150
Cdd:cd05675 50 GRANLVARIGGTDPSAGpLLLLGHIDVVPADASDWSVdpfsgEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 151 DIVFGGTVGEEGLGNLrGVRAFFNNHQDI----------DGFISIDGPEISRICY-----KGTGSYRYKVTykGPGGHSF 215
Cdd:cd05675 130 DLVFAFVADEEAGGEN-GAKWLVDNHPELfdgatfalneGGGGSLPVGKGRRLYPiqvaeKGIAWMKLTVR--GRAGHGS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 216 GAFGlPSAIHALGRAIAEIADIQ------------TKADPKTTFTVGE-------------------------------- 251
Cdd:cd05675 207 RPTD-DNAITRLAEALRRLGAHNfpvrltdetayfAQMAELAGGEGGAlmltavpvldpalaklgpsapllnamlrntas 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 252 ---ISGGTSVNAIAAEAHMYVDLRSNDPQElvklEQQFLTIVEKACNDenarwntDKIKWktEKIGDRPAATQPDDTPIV 328
Cdd:cd05675 286 ptmLDAGYATNVLPGRATAEVDCRILPGQS----EEEVLDTLDKLLGD-------PDVSV--EAVHLEPATESPLDSPLV 352
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517982453 329 QIASAATEAM----GIKPTLAgPSSTDSNVPMSLGVPsvTLG--------KGGKSGGAHTLDE 379
Cdd:cd05675 353 DAMEAAVQAVdpgaPVVPYMS-PGGTDAKYFRRLGIP--GYGfaplflppELDYTGLFHGVDE 412
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
46-388 |
2.29e-13 |
|
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: 71.09 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 46 EIPAPPFKEEKRATFILSKLEDLALENVEMDEEGNVFGLLRGVGNGPKIFVSAHLDTV-FPEGTDTTVKREN-GILYAPG 123
Cdd:cd03886 10 QHPELSFEEFRTAARIAEELRELGLEVRTGVGGTGVVATLKGGGPGPTVALRADMDALpIQEETGLPFASKHeGVMHACG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 124 ------IVddtSGLAEMLSIIRAfketkiEPIGDIVF---------GG--TVGEEGLGNLRGVRAFFNNHQDidgfisiD 186
Cdd:cd03886 90 hdghtaML---LGAAKLLAERRD------PLKGTVRFifqpaeegpGGakAMIEEGVLENPGVDAAFGLHVW-------P 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 187 GPEISRICYKG----TGSYRYKVTYKGPGGHsfGAFglP-----------SAIHALGRAIAEIADIQTKAdpktTFTVGE 251
Cdd:cd03886 154 GLPVGTVGVRSgalmASADEFEITVKGKGGH--GAS--PhlgvdpivaaaQIVLALQTVVSRELDPLEPA----VVTVGK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 252 ISGGTSVNAIAAEAHMYVDLRSNDPQELVKLEQQFLTIVEKACNDENARwntdkikWKTEKIGDRPaATQPDDTPIVQIA 331
Cdd:cd03886 226 FHAGTAFNVIPDTAVLEGTIRTFDPEVREALEARIKRLAEGIAAAYGAT-------VELEYGYGYP-AVINDPELTELVR 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517982453 332 SAATEAMGIKPTLAGPSSTDSN--VPMSLGVPS--VTLGKGGKSGGA---HTLDewFDPTDSYL 388
Cdd:cd03886 298 EAAKELLGEEAVVEPEPVMGSEdfAYYLEKVPGafFWLGAGEPDGENpglHSPT--FDFDEDAL 359
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
46-382 |
2.64e-13 |
|
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 fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349935 [Multi-domain] Cd Length: 379 Bit Score: 70.97 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 46 EIPAPPFKEEKRATFILSKLEDLALENVEMDE---EGNVFGLLRGVGNGPKIFVSAHLDTVFPEGTDT---TVKRENGIL 119
Cdd:cd08013 20 LSATGGAGEAEIATYVAAWLAHRGIEAHRIEGtpgRPSVVGVVRGTGGGKSLMLNGHIDTVTLDGYDGdplSGEIADGRV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 120 YAPGIVDDTSGL-AEMLSIIRAfkeTKIEPIGDIVFGGTVGEE--GLGN----LRGVRAffnnhqdiDGFIsIDGPEISR 192
Cdd:cd08013 100 YGRGTLDMKGGLaACMAALADA---KEAGLRGDVILAAVADEEdaSLGTqevlAAGWRA--------DAAI-VTEPTNLQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 193 ICYKGTGSYRYKVTYKGPGGH-SFGAFGLpSAIHALGRAIAEIADIQTK-----ADPKT---TFTVGEISGGTSVNAIAA 263
Cdd:cd08013 168 IIHAHKGFVWFEVDIHGRAAHgSRPDLGV-DAILKAGYFLVALEEYQQElperpVDPLLgraSVHASLIKGGEEPSSYPA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 264 EAHMYVDLRSNDPQELVKLEQQFLTIVEKACNDE-NARWNTDKIKWKtekigdRPAATQPDDTPIVQ-IASAATEAMGIK 341
Cdd:cd08013 247 RCTLTIERRTIPGETDESVLAELTAILGELAQTVpNFSYREPRITLS------RPPFEVPKEHPFVQlVAAHAAKVLGEA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 517982453 342 PTL-AGPSSTDSNVPMSLGVPSVTLGKGGksGGAHTLDEWFD 382
Cdd:cd08013 321 PQIrSETFWTDAALLAEAGIPSVVFGPSG--AGLHAKEEWVD 360
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
44-380 |
3.08e-13 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 70.16 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 44 IAEIPAPPFKEEKRATFILSKLEdlALENVEMDEEGNVFGLLRGVGNGPKIFVSAHLDTVFPEGTDTTVKRENGILYAPG 123
Cdd:cd05647 8 LVDIPSVSGNEKPIADEIEAALR--TLPHLEVIRDGNTVVARTERGLASRVILAGHLDTVPVAGNLPSRVEEDGVLYGCG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 124 IVDDTSGLAEMLSIIRAFKETkiEPIGDIVFGGTVGEEGLGNLRGVRAFFNNHQDidgFISID-----GPEISRICYKGT 198
Cdd:cd05647 86 ATDMKAGDAVQLKLAATLAAA--TLKHDLTLIFYDCEEVAAELNGLGRLAEEHPE---WLAADfavlgEPTDGTIEGGCQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 199 GSYRYKVTYKGPGGHSFGAFGLPSAIHALGRAIAEIADIQTKadpktTFTVG-----------EISGGTSVNAIAAEAHM 267
Cdd:cd05647 161 GTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLAAYEPR-----TVNIDgltyreglnavFISGGVAGNVIPDEARV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 268 YVDLRSNDPQELVKLEQQFLTIVEKACNDenarwntdkIKWKTEKIGDRPAATQPddtpivqIASAATEAMGIKPtLAGP 347
Cdd:cd05647 236 NLNYRFAPDKSLAEAIAHVREVFEGLGYE---------IEVTDLSPGALPGLDHP-------VARDLIEAVGGKV-RAKY 298
|
330 340 350
....*....|....*....|....*....|...
gi 517982453 348 SSTDSNVPMSLGVPSVTLGKGGKSgGAHTLDEW 380
Cdd:cd05647 299 GWTDVARFSALGIPAVNFGPGDPL-LAHKRDEQ 330
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
46-301 |
6.99e-12 |
|
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. 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 fungal, and have been inferred by similarity as being related to both ArgE and DapE.
Pssm-ID: 349903 [Multi-domain] Cd Length: 340 Bit Score: 66.14 E-value: 6.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 46 EIPAPPFKEEKRATFILSKLEDLAL--ENVEMDEEG--NVFGLLRGvGNGPKIFVSAHLDTVfPEGTDTTVKRENGILYA 121
Cdd:cd05652 10 EIPSISGNEAAVGDFLAEYLESLGFtvEKQPVENKDrfNVYAYPGS-SRQPRVLLTSHIDTV-PPFIPYSISDGGDTIYG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 122 PGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTVGEEGLGNlrGVRAFfnNHQDIDGF-ISIDG-PEISRICYKGTG 199
Cdd:cd05652 88 RGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGD--GMKAF--NDLGLNTWdAVIFGePTELKLASGHKG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 200 SYRYKVTYKGPGGHSfgafGLP----SAIHALGRAIAEIADIQTKADPK---TTFTVGEISGGTSVNAIAAEAHMYVDLR 272
Cdd:cd05652 164 MLGFKLTAKGKAGHS----GYPwlgiSAIEILVEALVKLIDADLPSSELlgpTTLNIGRISGGVAANVVPAAAEASVAIR 239
|
250 260 270
....*....|....*....|....*....|
gi 517982453 273 -SNDPQELVKLEQQFLTIVEKACNDENARW 301
Cdd:cd05652 240 lAAGPPEVKDIVKEAVAGILTDTEDIEVTF 269
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
47-379 |
9.44e-12 |
|
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. 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 bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349902 [Multi-domain] Cd Length: 341 Bit Score: 65.79 E-value: 9.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 47 IPAPPF-KEEKRATFILSKLedLALENVEMDEEG-NVFGLLRGVGNG-PKIFVSAHLDTVFPEGTDT----TVKRENGIL 119
Cdd:cd05651 10 IATPSFsREEHKTADLIENY--LEQKGIPFKRKGnNVWAENGHFDEGkPTLLLNSHHDTVKPNAGWTkdpfEPVEKGGKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 120 YAPGIVDDTSGLAEMLSIIRAFKETKiEPIGDIVFGGTVGEEGLGNlRGVRAFFNNHQDIDGFIsIDGPEISRICYKGTG 199
Cdd:cd05651 88 YGLGSNDAGASVVSLLATFLHLYSEG-PLNYNLIYAASAEEEISGK-NGIESLLPHLPPLDLAI-VGEPTEMQPAIAEKG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 200 SYRYKVTYKGPGGHSfgafGLPSAIHALGRAIAEIADIQT----KADP---KTTFTVGEISGGTSVNAIAAEAHMYVDLR 272
Cdd:cd05651 165 LLVLDCTARGKAGHA----ARNEGDNAIYKALDDIQWLRDfrfdKVSPllgPVKMTVTQINAGTQHNVVPDSCTFVVDIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 273 SNDPQELvkleQQFLTIVEKACNDEnarwntdkIKWKTEKIgdRPAATqPDDTPIVQiasaATEAMGIKPtLAGPSSTDS 352
Cdd:cd05651 241 TTEAYTN----EEIFEIIRGNLKSE--------IKPRSFRL--NSSAI-PPDHPIVQ----AAIAAGRTP-FGSPTLSDQ 300
|
330 340
....*....|....*....|....*..
gi 517982453 353 NVpmsLGVPSVTLGKgGKSGGAHTLDE 379
Cdd:cd05651 301 AL---MPFPSVKIGP-GDSSRSHTADE 323
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
80-382 |
1.04e-11 |
|
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. 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 bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 66.18 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 80 NVFGLLRGVGNGPK--IFvSAHLDTVfPEGTDTTVKR-------ENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIG 150
Cdd:cd03895 62 NVVGTHRPRGETGRslIL-NGHIDVV-PEGPVELWTRppfeatiVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 151 DIVFGGTVGEEGLGN------LRGVRAffnnhqdiDGFIsIDGPEISRICYKGTGSYRYKVTYKGPGGHSFGAFGLPSAI 224
Cdd:cd03895 140 DVHFQSVVEEECTGNgalaalMRGYRA--------DAAL-IPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 225 HALGRAIAEIADI------QTKADP-------KTTFTVGEISGGTSVNAIAAEAHMyvDLR-----SNDPQELV-KLEQq 285
Cdd:cd03895 211 EKAMHLIQALQELerewnaRKKSHPhfsdhphPINFNIGKIEGGDWPSSVPAWCVL--DCRigiypGESPEEARrEIEE- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 286 flTIVEKACNDENARWNTDKIKWktekIGDR-PAATQPDDTPIVQIASAATEAM-GIKPTL-AGPSSTDSNVpMSL--GV 360
Cdd:cd03895 288 --CVADAAATDPWLSNHPPEVEW----NGFQaEGYVLEPGSDAEQVLAAAHQAVfGTPPVQsAMTATTDGRF-FVLygDI 360
|
330 340
....*....|....*....|..
gi 517982453 361 PSVTLGKGGKsgGAHTLDEWFD 382
Cdd:cd03895 361 PALCYGPGSR--DAHGFDESVD 380
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
44-379 |
4.54e-11 |
|
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 bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 63.98 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 44 IAEIPAPPFKEEKRATFILSKLEDLALENVEMDEEGNVFGLLRgvGNGPKIFVSAHLDTV---------FP--EGtdttv 112
Cdd:cd05649 7 LIQIPSESGEEKGVVERIEEEMEKLGFDEVEIDPMGNVIGYIG--GGKKKILFDGHIDTVgignidnwkFDpyEG----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 113 KRENGILYAPGIVDDTSGLAEMLSIIRAFKE-TKIEPIGDIVFGGTVGEEglgNLRGV--RAFFNNHQDIDGFISIDGPE 189
Cdd:cd05649 80 YETDGKIYGRGTSDQKGGLASMVYAAKIMKDlGLRDFAYTILVAGTVQEE---DCDGVcwQYISKADKIKPDFVVSGEPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 190 ISRIcYKGT-GSYRYKVTYKGPGGHSFGAFGLPSAIHALGRAIAEIADI--QTKADP---KTTFTVGEI-SGGTSVNAIA 262
Cdd:cd05649 157 DGNI-YRGQrGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLnpNFPEAPflgRGTLTVTDIfSTSPSRCAVP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 263 AEAHMYVDLR--SNDPQELVKLEQQFLTIVEKAcNDENA--RWNTDKIKWKTEKI-GDR--PAATQPDDTPIVQIASAAT 335
Cdd:cd05649 236 DSCRISIDRRltVGETWEGCLEEIRALPAVKKY-GDDVAvsMYNYDRPSYTGEVYeSERyfPTWLLPEDHELVKALLEAY 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 517982453 336 EAMGIKPTLAGP---SSTDSNVPMSLGVPSVTLGKgGKSGGAHTLDE 379
Cdd:cd05649 315 KALFGARPLIDKwtfSTNGVSIMGRAGIPCIGFGP-GAENQAHAPNE 360
|
|
| Iap |
COG2234 |
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ... |
80-214 |
4.73e-11 |
|
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];
Pssm-ID: 441835 [Multi-domain] Cd Length: 257 Bit Score: 62.84 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 80 NVFGLLRGVGNGPK-IFVSAHLDTVfpegtdttvkrengILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTV 158
Cdd:COG2234 48 NVIAEIPGTDPPDEvVVLGAHYDSV--------------GSIGPGADDNASGVAALLELARALAALGPKPKRTIRFVAFG 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 159 GEEgLGnLRGVRAFFNNH----QDIDGFISIDGPeisricykGTGSYRYKVTYKGPGGHS 214
Cdd:COG2234 114 AEE-QG-LLGSRYYAENLkaplEKIVAVLNLDMI--------GRGGPRNYLYVDGDGGSP 163
|
|
| PRK12892 |
PRK12892 |
allantoate amidohydrolase; Reviewed |
64-391 |
8.19e-11 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 183817 [Multi-domain] Cd Length: 412 Bit Score: 63.19 E-value: 8.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 64 KLEDLALEnVEMDEEGNVFGLLRGVGNGPKIFVSAHLDTVFPEGtdttvkRENGILyapGIVddtSGLAemlsIIRAFKE 143
Cdd:PRK12892 48 WCEAAGLA-VRIDGIGNVFGRLPGPGPGPALLVGSHLDSQNLGG------RYDGAL---GVV---AGLE----AARALNE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 144 TKIEPIGDIVFGGTVGEEGL---GNLRGVRAFFN--NHQDID------------------GFISIDGPEISRICYKG--- 197
Cdd:PRK12892 111 HGIATRHPLDVVAWCDEEGSrftPGFLGSRAYAGrlDPADALaarcrsdgvplrdalaaaGLAGRPRPAADRARPKGyle 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 198 ----------------------TGSYRYKVTYKGPGGHSfGAFGLP---SAIHALGRAIAEIADIQTKADPKTTFTVGEI 252
Cdd:PRK12892 191 ahieqgpvleqaglpvgvvtgiVGIWQYRITVTGEAGHA-GTTPMAlrrDAGLAAAEMIAAIDEHFPRVCGPAVVTVGRV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 253 S---GGTSVnaIAAEAHMYVDLRSNDPQELvkleQQFLTIVEKACNDENARWNTdKIKWktEKIgdRPAATQPDDTPIVQ 329
Cdd:PRK12892 270 AldpGSPSI--IPGRVEFSFDARHPSPPVL----QRLVALLEALCREIARRRGC-RVSV--DRI--AEYAPAPCDAALVD 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517982453 330 IASAATEAMGIkPTLAGPS--STDSNVpMSLGVPSVTLGKGGKSGGAHTLDEWFDPTDSYLGPQ 391
Cdd:PRK12892 339 ALRAAAEAAGG-PYLEMPSgaGHDAQN-MARIAPSAMLFVPSKGGISHNPAEDTSPADLAQGAR 400
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
47-379 |
1.45e-10 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 62.65 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 47 IPAPPFKEEKRATFILSKLEDLALENVEMDEEGNVFGLlrgVGNGPK-IFVSAHLDTV---------FP--EGTDttvkr 114
Cdd:PRK13004 27 IPSESGDEKRVVKRIKEEMEKVGFDKVEIDPMGNVLGY---IGHGKKlIAFDAHIDTVgigdiknwdFDpfEGEE----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 115 ENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTVGEEglgnlrgvraffnnhqDIDG-----FISIDG-- 187
Cdd:PRK13004 99 DDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEE----------------DCDGlcwryIIEEDKik 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 188 PEISRIC-------YKGT-GSYRYKVTYKGPGGHSfgafGLP----SAIHALGRAIAEIADI--QTKADP---KTTFTVG 250
Cdd:PRK13004 163 PDFVVITeptdlniYRGQrGRMEIRVETKGVSCHG----SAPergdNAIYKMAPILNELEELnpNLKEDPflgKGTLTVS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 251 EI-SGGTSVNAIAAEAHMYVDLRSND--PQELVKLEQQFLTIVEKAcNDENARWNTDKIKWKTEKI-GDR--PAATQPDD 324
Cdd:PRK13004 239 DIfSTSPSRCAVPDSCAISIDRRLTVgeTWESVLAEIRALPAVKKA-NAKVSMYNYDRPSYTGLVYpTECyfPTWLYPED 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 517982453 325 TPIVQIASAA-TEAMGIKPTLAGPS-STDSNVPMS-LGVPSVTLGkGGKSGGAHTLDE 379
Cdd:PRK13004 318 HEFVKAAVEAyKGLFGKAPEVDKWTfSTNGVSIAGrAGIPTIGFG-PGKEPLAHAPNE 374
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
80-382 |
1.63e-10 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 62.34 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 80 NVFGLLRGVGNGpKIFVSAHLDTVFPEGT--DTTVKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGT 157
Cdd:PRK06133 89 MVVATFKGTGKR-RIMLIAHMDTVYLPGMlaKQPFRIDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 158 VGEE-GLGNLRGVRAFFNNHQDIdgFISIDGPEIS---RICYKGTGSYRYKVtyKGPGGHSFGAfglPSaihaLGR-AIA 232
Cdd:PRK06133 168 PDEEtGSPGSRELIAELAAQHDV--VFSCEPGRAKdalTLATSGIATALLEV--KGKASHAGAA---PE----LGRnALY 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 233 EIAD--IQTK----ADPKTT--FTVgeISGGTSVNAIAAEAHMYVDLRSNDPQELVKLEQQFLTIVEKACNDENarwntd 304
Cdd:PRK06133 237 ELAHqlLQLRdlgdPAKGTTlnWTV--AKAGTNRNVIPASASAQADVRYLDPAEFDRLEADLQEKVKNKLVPDT------ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 305 KIKWKTEKiGDRPAATQPDDTPIVQIASAATEAMGIKPTLAGPSS---TDSNVPMSLGVPSVTLGKGGKSGGAHTLDEWF 381
Cdd:PRK06133 309 EVTLRFER-GRPPLEANAASRALAEHAQGIYGELGRRLEPIDMGTgggTDAAFAAGSGKAAVLEGFGLVGFGAHSNDEYI 387
|
.
gi 517982453 382 D 382
Cdd:PRK06133 388 E 388
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
92-382 |
2.42e-10 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 61.72 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 92 PKIFVSAHLDTVFPEGT--DTTVKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTVGEEgLGNlRGV 169
Cdd:PRK07473 76 PGILIAGHMDTVHPVGTleKLPWRREGNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFTPDEE-VGT-PST 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 170 RAFFNNHQDIDGFISIdgPEISRiCYKG--TGSY---RYKVTYKGPGGHSFGAFGL-PSAIHALGRAIAEIaDIQTKADp 243
Cdd:PRK07473 154 RDLIEAEAARNKYVLV--PEPGR-PDNGvvTGRYaiaRFNLEATGRPSHAGATLSEgRSAIREMARQILAI-DAMTTED- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 244 kTTFTVGEISGGTSVNAIAAEAhmyvdlrSNDPQELVKLEQQFLTIVEK--ACNDEnarwnTDKIKWKTEKIGDRPaATQ 321
Cdd:PRK07473 229 -CTFSVGIVHGGQWVNCVATTC-------TGEALSMAKRQADLDRGVARmlALSGT-----EDDVTFTVTRGVTRP-VWE 294
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517982453 322 PDD--TPIVQIASAATEAMGIK-PTLAGPSSTDSNVPMSLGVPSVTlGKGGKSGGAHTLDEWFD 382
Cdd:PRK07473 295 PDAgtMALYEKARAIAGQLGLSlPHGSAGGGSDGNFTGAMGIPTLD-GLGVRGADYHTLNEHIE 357
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
46-379 |
2.60e-10 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 61.51 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 46 EIPAPPFKEEKRATFILSKLEDLALEnVEMDEEGNVFGLlRGVGnGPKIFVSAHLDTVfPegTDTTVKRENGILYAPGIV 125
Cdd:PRK04443 17 EIPSPSGEEAAAAEFLVEFMESHGRE-AWVDEAGNARGP-AGDG-PPLVLLLGHIDTV-P--GDIPVRVEDGVLWGRGSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 126 DDTSGLAEMLSiirAFKETKIEPIGDIVFGGTVGEEglGNLRGVRAFFNNHQDIDGFI-----SIDGPEISricYKG--T 198
Cdd:PRK04443 91 DAKGPLAAFAA---AAARLEALVRARVSFVGAVEEE--APSSGGARLVADRERPDAVIigepsGWDGITLG---YKGrlL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 199 GSYRYKVtykgPGGHSFGAfgLPSAI-HALG--RAIAEIADIQTKADP---KTTFTVGEISggTSVNAIAAEAHMYVDLR 272
Cdd:PRK04443 163 VTYVATS----ESFHSAGP--EPNAAeDAIEwwLAVEAWFEANDGRERvfdQVTPKLVDFD--SSSDGLTVEAEMTVGLR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 273 ---SNDPQELVKLEQQFLtivekacndenarwNTDKIKWKtekiGDRPAATQPDDTPIVQIASAATEAMGIKPTLAGPSS 349
Cdd:PRK04443 235 lppGLSPEEAREILDALL--------------PTGTVTFT----GAVPAYMVSKRTPLARAFRVAIREAGGTPRLKRKTG 296
|
330 340 350
....*....|....*....|....*....|...
gi 517982453 350 T-DSNV--PmSLGVPSVTLGKgGKSGGAHTLDE 379
Cdd:PRK04443 297 TsDMNVvaP-AWGCPMVAYGP-GDSDLDHTPDE 327
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
48-293 |
5.64e-10 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. 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: 349940 [Multi-domain] Cd Length: 372 Bit Score: 60.43 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 48 PAPPFKEEKRATFILSKLEDLALENVEMDEEGnVFGLLRGVGNGPKIFVSAHLDTV-FPEGTDTTVKREN-GILYAPGiv 125
Cdd:cd08019 12 PELSLKEERTSKRIKEELDKLGIPYVETGGTG-VIATIKGGKAGKTVALRADIDALpVEECTDLEYKSKNpGLMHACG-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 126 dDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTVGEE---------GLGNLRGVRAFFNNH--QDID-GFISID-GPEISr 192
Cdd:cd08019 89 -HDGHTAMLLGAAKILNEIKDTIKGTVKLIFQPAEEvgegakqmiEEGVLEDVDAVFGIHlwSDVPaGKISVEaGPRMA- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 193 icykgtGSYRYKVTYKGPGGHSfgafGLP-SAIHALGRAIAEIADIQT----KADP--KTTFTVGEISGGTSVNAIAAEA 265
Cdd:cd08019 167 ------SADIFKIEVKGKGGHG----SMPhQGIDAVLAAASIVMNLQSivsrEIDPlePVVVTVGKLNSGTRFNVIADEA 236
|
250 260
....*....|....*....|....*...
gi 517982453 266 HMYVDLRSNDPQELVKLEQQFLTIVEKA 293
Cdd:cd08019 237 KIEGTLRTFNPETREKTPEIIERIAKHT 264
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
94-298 |
1.70e-09 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 59.21 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 94 IFVSAHLDTVFPEGT--DTTVKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEP-IG-DIVFggTVGEEgLGNL--R 167
Cdd:PRK07338 95 VLLTGHMDTVFPADHpfQTLSWLDDGTLNGPGVADMKGGIVVMLAALLAFERSPLADkLGyDVLI--NPDEE-IGSPasA 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 168 GVRAFFNNHQDI---------DGFISidgpeISRicyKGTGSYRYKVTykGPGGHSFGAFglpsaihALGR-AIAEIADI 237
Cdd:PRK07338 172 PLLAELARGKHAaltyepalpDGTLA-----GAR---KGSGNFTIVVT--GRAAHAGRAF-------DEGRnAIVAAAEL 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517982453 238 QTKAD------PKTTFTVGEISGGTSVNAIAAEAHMYVDLRSNDPQELVKLEQQFLTIVEKACNDEN 298
Cdd:PRK07338 235 ALALHalngqrDGVTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHG 301
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
58-342 |
3.11e-09 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 58.39 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 58 ATFILSKLEDLALENVEMDEEGNVFGLLRG-VGNGPKIFVSAHLDTV--------------FpEGTDTTVKRENGILYAP 122
Cdd:PRK13381 34 AKLLADELRELGLEDIVIDEHAIVTAKLPGnTPGAPRIGFIAHLDTVdvglspdihpqilrF-DGGDLCLNAEQGIWLRT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 123 G-------------IV---------DDTSGLAEMLSIIRAFKETKIEPiGDIVFgGTVGEEGLGnLRGVRAFFNNHQDID 180
Cdd:PRK13381 113 AehpellnyqgediIFsdgtsvlgaDNKAAIAVVMTLLENLTENEVEH-GDIVV-AFVPDEEIG-LRGAKALDLARFPVD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 181 GFISIDGPEISRICYKGTGSYRYKVTYKGPGGHSFGAFGLpsAIHALGRAIAEIADIQTKADPKTT------FTVGEISG 254
Cdd:PRK13381 190 FAYTIDCCELGEVVYENFNAASAEITITGVTAHPMSAKGV--LVNPILMANDFISHFPRQETPEHTegregyIWVNDLQG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 255 GtsvnaiAAEAHMYVDLRSNDPQELVKLEQQFLTIVEKAcndeNARWNTDKIKWKTEKIGDRPAATQPDDTPIVQIASAA 334
Cdd:PRK13381 268 N------VNKAKLKLIIRDFDLDGFEARKQFIEEVVAKI----NAKYPTARVSLTLTDQYSNISNSIKDDRRAVDLAFDA 337
|
....*...
gi 517982453 335 TEAMGIKP 342
Cdd:PRK13381 338 MKELGIEP 345
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
72-387 |
3.54e-09 |
|
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation.
Pssm-ID: 349888 [Multi-domain] Cd Length: 426 Bit Score: 58.11 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 72 NVEMDEEGN----VFGLLRGVGNGPKIFVSAHLDTVfPEGTDT-------TVKRENGILYAPGIVDDTSGLAEMLSIIRA 140
Cdd:cd03893 40 TVEIVDTSNgapvVFAEFPGAPGAPTVLLYGHYDVQ-PAGDEDgwdsdpfELTERDGRLYGRGAADDKGPILAHLAALRA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 141 FKETKIEPIGDIVFGGTVGEE-GLGNLrgvRAFFNNHQDI---DGFISIDGPEISR----ICY--KGTGSYRYKVTYKGP 210
Cdd:cd03893 119 LMQQGGDLPVNVKFIIEGEEEsGSPSL---DQLVEAHRDLlaaDAIVISDSTWVGQeqptLTYglRGNANFDVEVKGLDH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 211 GGHSfGAFG--LPSAIHALGRAIA-------------------EIADIQTKADPKTTFTVGEISGGT------------- 256
Cdd:cd03893 196 DLHS-GLYGgvVPDPMTALAQLLAslrdetgrilvpglydavrELPEEEFRLDAGVLEEVEIIGGTTgsvaerlwtrpal 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 257 -------------SVNAIAAEAHMYVDLR---SNDPQELVKLEQQFLtivekacnDENARWNtDKIKWKTEKIGDrPAAT 320
Cdd:cd03893 275 tvlgidggfpgegSKTVIPPRARAKISIRlvpGQDPEEASRLLEAHL--------EKHAPSG-AKVTVSYVEGGM-PWRS 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517982453 321 QPDDtPIVQIASAATEAM-GIKPTLAGPSSTDSNVPMS---LGVPSVTLGKGGKSGGAHTLDEWFDPTDSY 387
Cdd:cd03893 345 DPSD-PAYQAAKDALRTAyGVEPPLTREGGSIPFISVLqefPQAPVLLIGVGDPDDNAHSPNESLRLGNYK 414
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
46-368 |
3.61e-09 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 57.85 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 46 EIPAPPFKEEKRATFILSKLEDLALE-NVEMDEEgnVFGLLrgVGNGPKIFVSAHLDTVFPEGTDTTvkrENGILYAPGI 124
Cdd:PRK08652 13 KIPSPSGQEDEIALHIMEFLESLGYDvHIESDGE--VINIV--VNSKAELFVEVHYDTVPVRAEFFV---DGVYVYGTGA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 125 VDDTSGLAEMLSIIRAFKETKIEPIGDIVFggtVGEEGLGNlRGVRAFFNNHQdiDGFISIDGPEISRICYKGTGSYRYK 204
Cdd:PRK08652 86 CDAKGGVAAILLALEELGKEFEDLNVGIAF---VSDEEEGG-RGSALFAERYR--PKMAIVLEPTDLKVAIAHYGNLEAY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 205 VTYKGPGGH-SFGAFGLpSAIHALGRAIAEIADI----QTKADPKTTFTvgEISGGTSVNAIAAEAHMYVDLRSNDPQEL 279
Cdd:PRK08652 160 VEVKGKPSHgACPESGV-NAIEKAFEMLEKLKELlkalGKYFDPHIGIQ--EIIGGSPEYSIPALCRLRLDARIPPEVEV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 280 VKLEQQFLTI-----VEKACNDENARWNTDkikwktekigdrpaatqpDDTPIVQIASAATEAMGIKPTLAG-PSSTDSN 353
Cdd:PRK08652 237 EDVLDEIDPIldeytVKYEYTEIWDGFELD------------------EDEEIVQLLEKAMKEVGLEPEFTVmRSWTDAI 298
|
330
....*....|....*
gi 517982453 354 VPMSLGVPSVTLGKG 368
Cdd:PRK08652 299 NFRYNGTKTVVWGPG 313
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
74-379 |
3.94e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 58.09 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 74 EMDEEGNVFGLLRGVGNGPKIFVSAHLDTVFPEGTDTT-----VKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEP 148
Cdd:PRK09133 84 PYPRKGNLVARLRGTDPKKPILLLAHMDVVEAKREDWTrdpfkLVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 149 IGDIVFGGTVGEEGlGNLRGVRAFFNNHQDI-----------DGFISIDGPEISRICYKGTGSYR-YKVTYKGPGGHSfg 216
Cdd:PRK09133 164 KRDIILALTGDEEG-TPMNGVAWLAENHRDLidaefalneggGGTLDEDGKPVLLTVQAGEKTYAdFRLEVTNPGGHS-- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 217 afGLPS---AIHALGRAIAEI--------------------ADIQT-------------KADPK---------------- 244
Cdd:PRK09133 241 --SRPTkdnAIYRLAAALSRLaayrfpvmlndvtrayfkqsAAIETgplaaamrafaanPADEAaiallsadpsynamlr 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 245 TTFTVGEISGGTSVNAIAAEAHMYVDLR--SNDPQELVKLEqqfltiVEKACNDENArwntdKIKWKTEkigDRPAATQP 322
Cdd:PRK09133 319 TTCVATMLEGGHAENALPQRATANVNCRifPGDTIEAVRAT------LKQVVADPAI-----KITRIGD---PSPSPASP 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517982453 323 DDTPIVQIASAATEAM----GIKPTLAgPSSTDSNVPMSLGVPS--VT-LGKGGKSGGAHTLDE 379
Cdd:PRK09133 385 LRPDIMKAVEKLTAAMwpgvPVIPSMS-TGATDGRYLRAAGIPTygVSgLFGDPDDTFAHGLNE 447
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
22-369 |
5.04e-09 |
|
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: 57.77 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 22 LVKEGLKFLKEDHENtieeQIVIAEIPAPPFkEEKRATFILSKLEDLALENVEMDEEGNVFGLLRGVGNG--PKIFVSAH 99
Cdd:cd05645 1 LLERFLEYVSLDTQS----KAGVRQVPSTEG-QWKLLKLLKKQLEELGLINVTLSEKGTLIATLPANVDGdiPAIGFISH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 100 LDTVfPEGTDTTVK-----RENGILYAPGI-------------------------------VDDTSGLAEMLSIIRAFKE 143
Cdd:cd05645 76 VDTS-PDGSGKNVNpqiveNYRGGDIALGIgdevlspvmfpvlhqllgqtlittdgktllgADDKAGLAEIFTALAVLKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 144 TKIePIGDIVFGGTVGEE-GLGnlrgvraffNNHQDIDGF-----ISIDGPEISRICYKGTGSYRYKVTYKGPGGHSFGA 217
Cdd:cd05645 155 KNI-PHGDIEVAFTPDEEvGKG---------AKHFDVEAFtakwaYTVDGGGVGELEFENFNAASVNIKIVGNNVHPGTA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 218 FGLP-SAIHALGRAIAEIADIQ---TKADPKTTFTVGEISGGTSVNAIAAEAHMYVdlRSNDPQELVKLEQQFLTIVEKA 293
Cdd:cd05645 225 KGVGvNALSLAARIHAEVPADEspeGTEGYEGFYHLASFKGTVDRAQIHYIIRDFD--RKQFEARKRK*KEIAKKVGKGL 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517982453 294 CNDENArwntdKIKWKTEKIGDRPAATQPDDtpIVQIASAATEAMGIKPTLAgPS--STDSNVPMSLGVPSVTLGKGG 369
Cdd:cd05645 303 HPDCYI-----ELVIEDSYYNFREKVVEHPH--ILDIAQQAARDCGITPELK-PIrgGTDGAQLSFHGLPCPNLFTGG 372
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
79-363 |
6.39e-09 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 57.49 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 79 GNVFGLLRGVGNGPK---IFVSAHLDTV--FPEGTD----TTVKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPI 149
Cdd:TIGR01880 56 GKPVVVLTWPGSNPElpsILLNSHTDVVpvFREHWThppfSAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 150 GDI--VFggtVGEEGLGNLRGVRAFFNNHQDID---GFISIDG----PEISRICYKGTGSYRYKVTYKGPGGHsfGAFGL 220
Cdd:TIGR01880 136 RTIhiSF---VPDEEIGGHDGMEKFAKTDEFKAlnlGFALDEGlaspDDVYRVFYAERVPWWVVVTAPGNPGH--GSKLM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 221 P-SAIHALGRAIAEIADIQT------KADPK------TTFTVGEISGGTSVNAIAAEAHMYVDLR---SNDPQELVKLEQ 284
Cdd:TIGR01880 211 EnTAMEKLEKSVESIRRFREsqfqllQSNPDlaigdvTSVNLTKLKGGVQSNVIPSEAEAGFDIRlapSVDFEEMENRLD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 285 QfltivEKACNDENarwntdkIKWKTEKIGDRPAATQPDDT-PIVQIASAATEAMG--IKPTLAgPSSTDSNVPMSLGVP 361
Cdd:TIGR01880 291 E-----WCADAGEG-------VTYEFSQHSGKPLVTPHDDSnPWWVAFKDAVKEMGctFKPEIL-PGSTDSRYIRAAGVP 357
|
..
gi 517982453 362 SV 363
Cdd:TIGR01880 358 AL 359
|
|
| PRK12890 |
PRK12890 |
allantoate amidohydrolase; Reviewed |
54-385 |
8.01e-09 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 237248 [Multi-domain] Cd Length: 414 Bit Score: 57.22 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 54 EEKRATFILSK-LEDLALEnVEMDEEGNVFGLLRG-VGNGPKIFVSAHLDTVfPEGtdttvkrengilyapGIVDDTSGL 131
Cdd:PRK12890 36 EERAARALLAAwMRAAGLE-VRRDAAGNLFGRLPGrDPDLPPLMTGSHLDTV-PNG---------------GRYDGILGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 132 AEMLSIIRAFKETKIEPIGDIVFGGTVGEEGL---GNLRGVRAFFN--------NHQDIDGfISIdGPEISRICYKG--- 197
Cdd:PRK12890 99 LAGLEVVAALREAGIRPPHPLEVIAFTNEEGVrfgPSMIGSRALAGtldveavlATRDDDG-TTL-AEALRRIGGDPdal 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 198 -------------------------------------TGSYRYKVTYKGPGGHS------------FGAFGLPSAIHALG 228
Cdd:PRK12890 177 pgalrppgavaaflelhieqgpvleaeglpigvvtaiQGIRRQAVTVEGEANHAgttpmdlrrdalVAAAELVTAMERRA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 229 RAIaeiadiqtkaDPKTTFTVGEIS-GGTSVNAIAAEAHMYVDLRSNDPQELVKLEQQFLTIVEKACNDENarwntdkIK 307
Cdd:PRK12890 257 RAL----------LHDLVATVGRLDvEPNAINVVPGRVVFTLDLRSPDDAVLEAAEAALLAELEAIAAARG-------VR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 308 WKTEKIGDRPAAtqPDDTPIVQIASAATEAMGIKPTL--------------AGPSStdsnvpMsLGVPSVtlgkGGKSgg 373
Cdd:PRK12890 320 IELERLSRSEPV--PCDPALVDAVEAAAARLGYPSRRmpsgaghdaaaiarIGPSA------M-IFVPCR----GGIS-- 384
|
410
....*....|..
gi 517982453 374 aHTLDEWFDPTD 385
Cdd:PRK12890 385 -HNPEEAMDPED 395
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
51-388 |
1.02e-08 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 56.33 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 51 PFKEEKRATFILSKLEDLALENVEMDEEGNVFGLlrgvgNGPKIFVSAHLDTV--FPEGtdttvKRENGILYAPGIVDDT 128
Cdd:PRK00466 25 PSGNETNATKFFEKISNELNLKLEILPDSNSFIL-----GEGDILLASHVDTVpgYIEP-----KIEGEVIYGRGAVDAK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 129 SGLAEMLSIIRAFKETKIEpigdIVFGGTVGEEglGNLRGVRAFFNNHQDIDGFISIDGPEISRICYKGTGSYRYKVTYK 208
Cdd:PRK00466 95 GPLISMIIAAWLLNEKGIK----VMVSGLADEE--STSIGAKELVSKGFNFKHIIVGEPSNGTDIVVEYRGSIQLDIMCE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 209 GPGGHSFGAfgLPSAIHALGRAIAEIADIQTKADpKTTFTVGEISGGTSVNAIAAEAHMYVDLRSNDPQelvkLEQQFLT 288
Cdd:PRK00466 169 GTPEHSSSA--KSNLIVDISKKIIEVYKQPENYD-KPSIVPTIIRAGESYNVTPAKLYLHFDVRYAINN----KRDDLIS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 289 IVekacndenarwnTDKIKWKTEKIGD--RPAATQPdDTPIVQIASAATEAMGIKPTLAGPSST-DSNVPMSLGVPSVTL 365
Cdd:PRK00466 242 EI------------KDKFQECGLKIVDetPPVKVSI-NNPVVKALMRALLKQNIKPRLVRKAGTsDMNILQKITTSIATY 308
|
330 340
....*....|....*....|....*....
gi 517982453 366 GKgGKSGGAHT------LDEWFDPTDSYL 388
Cdd:PRK00466 309 GP-GNSMLEHTnqekitLDEIYIAVKTYM 336
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
80-169 |
1.45e-08 |
|
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 54.36 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 80 NVFGLLRGVGNGPKIFVSAHLDTVFPEGTDTT------VKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIV 153
Cdd:cd18669 1 NVIARYGGGGGGKRVLLGAHIDVVPAGEGDPRdppffvDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90
....*....|....*.
gi 517982453 154 FGGTVGEEGLGNLRGV 169
Cdd:cd18669 81 VAFTPDEEVGSGAGKG 96
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
40-379 |
1.56e-08 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 56.20 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 40 EQIVIAEIPAPPFKEEKRA-TFILSKLEDLALEnVEM----DEEGNVFGLLRGVGNG-PK-IFVSAHLDTVFPEGTDT-- 110
Cdd:PRK08596 20 KTLVRFETPAPPARNTNEAqEFIAEFLRKLGFS-VDKwdvyPNDPNVVGVKKGTESDaYKsLIINGHMDVAEVSADEAwe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 111 ------TVKreNGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTVGEE--GLGNL----RGVRAFF----- 173
Cdd:PRK08596 99 tnpfepTIK--DGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEvgEAGTLqcceRGYDADFavvvd 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 174 --NNHQD-----IDGFISIDGPEISricYKGTgsyRYKVTYKgpGGHSFGAfglpSAIHALGRAIAEIADIQ-----TKA 241
Cdd:PRK08596 177 tsDLHMQgqggvITGWITVKSPQTF---HDGT---RRQMIHA--GGGLFGA----SAIEKMMKIIQSLQELErhwavMKS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 242 DP-----KTTFTVGEISGGTSVNAIAAEAHMYVD---LRSNDPQELVKLEQQFLTIVEKAcnDENARWNTDKIKW-KTEK 312
Cdd:PRK08596 245 YPgfppgTNTINPAVIEGGRHAAFIADECRLWITvhfYPNETYEQVIKEIEEYIGKVAAA--DPWLRENPPQFKWgGESM 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517982453 313 IGDR----PAATQPDDTPIVQIASAATEAMGIKPTLAG--PSSTDSNVPMSLGVPSVTLGKgGKSGGAHTLDE 379
Cdd:PRK08596 323 IEDRgeifPSLEIDSEHPAVKTLSSAHESVLSKNAILDmsTTVTDGGWFAEFGIPAVIYGP-GTLEEAHSVNE 394
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
65-342 |
1.77e-08 |
|
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: 56.01 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 65 LEDLALENVEMDEEGNVFGLLRG--VGNGPKIFVSAHLDTVfPEGTDTTVKRE-----NG---ILYAPGIV--------- 125
Cdd:cd03892 39 LKELGLEDVTLDEHGYVTATLPAnvDKDVPTIGFIAHMDTA-PDNSGKNVKPQiienyDGgdiVLNESGIVlspaefpel 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 126 -------------------DDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTVGEEgLGnlRGVRAFfnnhqDIDGF---- 182
Cdd:cd03892 118 knykgqtlittdgttllgaDDKAGIAEIMTALEYLIEHPEIKHGDIRVGFTPDEE-IG--RGADHF-----DVEKFgadf 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 183 -ISIDGPEISRICYKGTGSYRYKVTYKGPGGHSFGAFGlpSAIHALGRAIAEIADIQTKADPKTT------FTVGEISGG 255
Cdd:cd03892 190 aYTLDGGELGELEYENFNAASATITITGVNVHPGTAKG--KMVNALLLAADFHSMLPREETPEHTegyegfYHLLSMEGT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 256 TsvnaiaAEAHMYVDLRSNDPQELVKLEQQFLTIVEKAcndeNARWNTDKIKWK--------TEKIGDRPAatqpddtpI 327
Cdd:cd03892 268 V------EEAELSYIIRDFDRDGFEARKELIKEIAKKL----NAKYGEGRVELEikdqyynmKEKIEPHMH--------I 329
|
330
....*....|....*
gi 517982453 328 VQIASAATEAMGIKP 342
Cdd:cd03892 330 VDLAKEAMEALGIEP 344
|
|
| Peptidase_M28 |
pfam04389 |
Peptidase family M28; |
80-256 |
2.25e-08 |
|
Peptidase family M28;
Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 53.83 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 80 NVFGLLRGvGNGPK-IFVSAHLDTVFpegtdttvkrengilYAPGIVDDTSGLAEMLSIIRAFKETKiEPIGDIVFGGTV 158
Cdd:pfam04389 1 NVIAKLPG-KAPDEvVLLSAHYDSVG---------------TGPGADDNASGVAALLELARVLAAGQ-RPKRSVRFLFFD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 159 GEEgLGnLRGVRAFFNNHQD---IDGFISIDgpeisricykGTGSYRY-KVTYKGPGGHSfgafglpsaihALGRAIAEI 234
Cdd:pfam04389 64 AEE-AG-LLGSHHFAKSHPPlkkIRAVINLD----------MIGSGGPaLLFQSGPKGSS-----------LLEKYLKAA 120
|
170 180
....*....|....*....|..
gi 517982453 235 ADIQTKADPKTTFTVGEISGGT 256
Cdd:pfam04389 121 AKPYGVTLAEDPFQERGGPGRS 142
|
|
| FrvX |
COG1363 |
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ... |
46-103 |
2.52e-08 |
|
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];
Pssm-ID: 440974 [Multi-domain] Cd Length: 353 Bit Score: 55.13 E-value: 2.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 517982453 46 EIPAPPFKEEKRATFILSKLEDLALEnVEMDEEGNVFGLLRGVGNGPKIFVSAHLDTV 103
Cdd:COG1363 13 EAPGPSGFEDEVREYIKEELEPLGDE-VETDRLGNLIATKKGKGDGPKVMLAAHMDEI 69
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
44-282 |
1.18e-07 |
|
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: 53.68 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 44 IAEIPAPPFKEEKRATFILSKLEDLALEnVEMDEEGNVfgLLR-----GVGNGPKIFVSAHLDTVfPEGTDTTV------ 112
Cdd:cd03890 11 ISKIPRPSGNEKQISDFLVKFAKKLGLE-VIQDEVGNV--IIRkpatpGYENAPPVILQGHMDMV-CEKNADSEhdfekd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 113 ----KRENGILYAPGIV---DDTSGLAEMLSIIrafkETKIEPIGDIVFGGTVGEE-------GL--GNLRGvRAFFNnh 176
Cdd:cd03890 87 piklRIDGDWLKATGTTlgaDNGIGVAYALAIL----EDKDIEHPPLEVLFTVDEEtgmtgalGLdpSLLKG-KILLN-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 177 qdIDG------FISIDGpEISRICY------KGTGSYR-YKVTYKG-PGGHSfGA---FGLPSAIHALGRAIAEIADiqt 239
Cdd:cd03890 160 --LDSeeegelTVGCAG-GIDVTITlpiereEAEGGYTgLKITVKGlKGGHS-GVdihKGRANANKLMARLLYELAK--- 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 517982453 240 kadpKTTFTVGEISGGTSVNAIAAEAHMYVDLRSNDPQELVKL 282
Cdd:cd03890 233 ----ELDFRLVSINGGTKRNAIPREAVAVIAVPAEDVEALKKL 271
|
|
| M28_Fxna_like |
cd03875 |
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ... |
80-187 |
1.30e-07 |
|
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic reticulum metallopeptidase 1 (ERMP1; Felix-ina, FXNA or Fxna peptidase; KIAA1815) subfamily. ERMP1 is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organization of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolyzed has not yet been determined. Another member of this subfamily is the 24-kDa vacuolar protein (VP24) which is probably involved in the formation of intravacuolar pigmented globules (cyanoplasts) in highly anthocyanin-containing vacuoles; however, the biological function of the C-terminal region which includes the putative transmembrane metallopeptidase domain is unknown.
Pssm-ID: 349872 [Multi-domain] Cd Length: 307 Bit Score: 52.98 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 80 NVFGLLRGVGNGPK--IFVSAHLDTVFPegtdttvkrengilyAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGT 157
Cdd:cd03875 81 NIVVRISGKNSNSLpaLLLNAHFDSVPT---------------SPGATDDGMGVAVMLEVLRYLSKSGHQPKRDIIFLFN 145
|
90 100 110
....*....|....*....|....*....|...
gi 517982453 158 VGEEGLgnLRGVRAFFNNH---QDIDGFISIDG 187
Cdd:cd03875 146 GAEENG--LLGAHAFITQHpwaKNVRAFINLEA 176
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
38-295 |
4.34e-07 |
|
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: 51.50 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 38 IEEQIV-----IAEIPAPPFKEEKRATFILSKLEDLALEnVEMDEEGN-VFGLLRGVGNGPKIFVSAHLDTVfP--EGTD 109
Cdd:cd08021 8 LEDEMIqwrrhIHQYPELSFEEFETAAYIANELKKLGLE-VETNVGGTgVVATLKGGKPGKTVALRADMDAL-PieEETD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 110 TTVKREN-GILYAPGIVDDTS---GLAEMLSIIRAFKETKIEpigdIVF--------GGTVGEEGLGNLRGVRAFFNNHq 177
Cdd:cd08021 86 LPFKSKNpGVMHACGHDGHTAmllGAAKVLAENKDEIKGTVR----FIFqpaeevppGGAKPMIEAGVLEGVDAVFGLH- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 178 didgfISIDGPEISRICYKG---TGSYRYKVTYKGPGGHSfgafGLPS----AIHALGRAIAEIADIQT-KADPKTTF-- 247
Cdd:cd08021 161 -----LWSTLPTGTIAVRPGaimAAPDEFDITIKGKGGHG----SMPHetvdPIVIAAQIVTALQTIVSrRVDPLDPAvv 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 517982453 248 TVGEISGGTSVNAIAAEAHMYVDLRSNDPQELVKLEQQFLTIVEKACN 295
Cdd:cd08021 232 TIGTFQGGTSFNVIPDTVELKGTVRTFDEEVREQVPKRIERIVKGICE 279
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
80-164 |
5.03e-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: 50.12 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 80 NVFGLLRGVGNGPKIFVSAHLDTVfPEGTDTT-------VKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDI 152
Cdd:cd03873 1 NLIARLGGGEGGKSVALGAHLDVV-PAGEGDNrdppfaeDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTI 79
|
90
....*....|..
gi 517982453 153 VFGGTVGEEGLG 164
Cdd:cd03873 80 VVAFTADEEVGS 91
|
|
| M28_like |
cd03877 |
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ... |
80-175 |
1.37e-06 |
|
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 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. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Some proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.
Pssm-ID: 349874 [Multi-domain] Cd Length: 206 Bit Score: 48.78 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 80 NVFGLLRGvgNGPK---IFVSAHLDTVfpeGTDttvKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIgDIVFGG 156
Cdd:cd03877 3 NVVGVLEG--SDLPdetIVIGAHYDHL---GIG---GGDSGDKIYNGADDNASGVAAVLELARYFAKQKTPKR-SIVFAA 73
|
90
....*....|....*....
gi 517982453 157 TVGEEgLGnLRGVRAFFNN 175
Cdd:cd03877 74 FTAEE-KG-LLGSKYFAEN 90
|
|
| M28 |
cd02690 |
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ... |
80-186 |
2.75e-06 |
|
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: 47.72 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 80 NVFGLLRG-VGNGPKIFVSAHLDTVFPegtdttvkrengilyAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFgGTV 158
Cdd:cd02690 3 NVIATIKGsDKPDEVILIGAHYDSVPL---------------SPGANDNASGVAVLLELARVLSKLQLKPKRSIRF-AFW 66
|
90 100 110
....*....|....*....|....*....|..
gi 517982453 159 GEEGLGnLRGVRAFFNNH----QDIDGFISID 186
Cdd:cd02690 67 DAEELG-LLGSKYYAEQLlsslKNIRAALNLD 97
|
|
| M42_glucanase_like |
cd05657 |
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ... |
47-208 |
3.47e-06 |
|
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1,4-beta-glucanase or endoglucanase)-like subfamily. Proteins in this subfamily are co-catalytic metallopeptidases, found in archaea and bacteria. They show similarity to cellulase and endo-1,4-beta-glucanase (endoglucanase) which typically bind two zinc or cobalt atoms. Some of the enzymes exhibit typical aminopeptidase specificity, whereas others are also capable of N-terminal deblocking activity, i.e. hydrolyzing acylated N-terminal residues. Many of these enzymes are assembled either as tetrahedral dodecamers or as octahedral tetracosameric structures, with the active site located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers.
Pssm-ID: 349907 [Multi-domain] Cd Length: 337 Bit Score: 48.43 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 47 IPAPPFKEEKRATFILSKLEDLALEnVEMDEEGNVFGLLRGVGNGPKIFVSAHLDT------------------------ 102
Cdd:cd05657 12 IPSPTGYTDEAVRYLKKELEGLGVE-TELTNKGALIATIPGKDSRKARALSAHVDTlgaivkeikpdgrlrltpiggfaw 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 103 VFPEGTDTTVKRENG------ILY-------------------------------------APGI--------------- 124
Cdd:cd05657 91 NSAEGENVTIITRDGktytgtVLPlkasvhvygdapeaqertwdnmevrldekvkskedvlALGIrvgdfvafdprpevt 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 125 ---------VDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTVGEE-GLGnlrgvrAFFNNHQDIDGFISID----GPEI 190
Cdd:cd05657 171 esgfiksrhLDDKASVAILLALARALKENKLKLPVDTHFLFSNYEEvGHG------ASFAPPEDTDELLAVDmgpvGPGQ 244
|
250 260
....*....|....*....|....*
gi 517982453 191 SRICYK-------GTGSYRYKVTYK 208
Cdd:cd05657 245 NSDEYTvsicakdSGGPYDYHLRKR 269
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
35-176 |
5.89e-06 |
|
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. 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 bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349901 [Multi-domain] Cd Length: 389 Bit Score: 48.22 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 35 ENTIEEQIVIAEIPA--PPFK---EEKRATFILSKLEDLALENVEMDEEGNVFGLLR-------GVGNGPKIFVSAHLDT 102
Cdd:cd05650 1 EEIIELERDLIRIPAvnPESGgegEKEKADYLEKKLREYGFYTLERYDAPDERGIIRpnivakiPGGNDKTLWIISHLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 103 VfPEG------TDT-TVKRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPigDIVFG-GTVGEEGLGNLRGVRAFFN 174
Cdd:cd05650 81 V-PPGdlslweTDPwEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITP--KYNFGlLFVADEEDGSEYGIQYLLN 157
|
..
gi 517982453 175 NH 176
Cdd:cd05650 158 KF 159
|
|
| M20_Acy1-like |
cd05667 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
32-291 |
1.78e-05 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a 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. 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: 349917 [Multi-domain] Cd Length: 403 Bit Score: 46.65 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 32 EDHENTIEEQIV-----IAEIPAPPFKEEKRATFILSKLEDLALENVEMDEEGNVFGLLRGVGNGPKIFVSAHLDTV-FP 105
Cdd:cd05667 2 EAAIQQVEPKVIewrrdFHQNPELSNREFRTAALIAKELKSLGIEVRTGIAKTGVVGILKGGKPGPVIALRADMDALpVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 106 EGTD----TTVK-----RENGILYAPGivDDTSgLAEMLSIIRAFKETKIEPIGDIVF-------GGTVGEEGLGNLRGV 169
Cdd:cd05667 82 EKTGlpfaSKVKttylgQTVGVMHACG--HDAH-VAILLGAAEVLAANKDKIKGTVMFifqpaeeGPPEGEEGGAKLMLK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 170 RAFFNNHQD--IDGFISIDGPEISRICYKGTGSY----RYKVTYKGPGGHSFGAFG-----LPSA--IHALGRAIAEIAD 236
Cdd:cd05667 159 EGAFKDYKPeaIFGLHVGSGLPSGQLGYRSGPIMasadRFRITVKGKQTHGSRPWDgidpiMASAqiIQGLQTIISRRID 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 517982453 237 IqtkADPKTTFTVGEISGGTSVNAIAAEAHMYVDLRSNDPQELVKLEQQFLTIVE 291
Cdd:cd05667 239 L---TKEPAVISIGKINGGTRGNIIPEDAEMVGTIRTFDPEMREDIFARLKTIAE 290
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
73-260 |
2.96e-05 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 46.15 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 73 VEMDEEG--NVFGLLRGVGN-GPKIFVSAHLDTVfPEGT---------DTTVKreNGILYAPGIVDDTSGLAEMLSIIRA 140
Cdd:PRK06837 76 VEIDYSGapNVVGTYRPAGKtGRSLILQGHIDVV-PEGPldlwsrppfDPVIV--DGWMYGRGAADMKAGLAAMLFALDA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 141 FKETKIEPIGDIVFGGTVGEEGLGN------LRGVRAffnnhqdiDGFIsIDGPEISRICYKGTGSYRYKVTYKGPGGHS 214
Cdd:PRK06837 153 LRAAGLAPAARVHFQSVIEEESTGNgalstlQRGYRA--------DACL-IPEPTGEKLVRAQVGVIWFRLRVRGAPVHV 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517982453 215 FGAFGLPSAIHALGRAIAEIADIQT-----KADPK--------TTFTVGEISGG---TSVNA 260
Cdd:PRK06837 224 REAGTGANAIDAAYHLIQALRELEAewnarKASDPhfedvphpINFNVGIIKGGdwaSSVPA 285
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
60-362 |
3.15e-05 |
|
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: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 60 FILSKLEDLALEnVEMDEE--GNVFGLLRGVG---NGPKIFVSAHLDTV--FPEGTD----TTVKRENGILYAPGIVDDT 128
Cdd:cd05646 29 FLKRQADELGLP-VRVIEVvpGKPVVVLTWEGsnpELPSILLNSHTDVVpvFEEKWThdpfSAHKDEDGNIYARGAQDMK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 129 SGLAEMLSIIRAFKETKIEPIGDI--VFggtVGEEGLGNLRGVRAF-----FnnhQDIDGFISID----GPEIS-RICYK 196
Cdd:cd05646 108 CVGIQYLEAIRRLKASGFKPKRTIhlSF---VPDEEIGGHDGMEKFvkteeF---KKLNVGFALDeglaSPTEEyRVFYG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 197 GTGSYRYKVTYKGPGGHsfGAFGLP-SAIHALGRAIAEIADIQT------KADPKttFTVGE--------ISGGTSVNAI 261
Cdd:cd05646 182 ERSPWWVVITAPGTPGH--GSKLLEnTAGEKLRKVIESIMEFREsqkqrlKSNPN--LTLGDvttvnltmLKGGVQMNVV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 262 AAEAHMYVDLRSNDPQELVKLEQQFLTIVEKACNDenarwntdkIKWKTEKIGDRPAATQPDDT-PIVQIASAATEAMGI 340
Cdd:cd05646 258 PSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGRG---------VTYEFEQKSPEKDPTSLDDSnPWWAAFKKAVKEMGL 328
|
330 340
....*....|....*....|....
gi 517982453 341 --KPTLAgPSSTDSNVPMSLGVPS 362
Cdd:cd05646 329 klKPEIF-PAATDSRYIRALGIPA 351
|
|
| M28_like_PA |
cd05660 |
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ... |
80-163 |
4.06e-05 |
|
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 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. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.
Pssm-ID: 349910 [Multi-domain] Cd Length: 290 Bit Score: 45.04 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 80 NVFGLLRGVGNGPK-IFVSAHLDTvfpEGTDTTVkrENGILYaPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTV 158
Cdd:cd05660 61 NVVAILPGSKLPDEyIVLSAHWDH---LGIGPPI--GGDEIY-NGAVDNASGVAAVLELARVFAAQDQRPKRSIVFLAVT 134
|
....*.
gi 517982453 159 GEE-GL 163
Cdd:cd05660 135 AEEkGL 140
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
48-369 |
5.37e-05 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. 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. 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 in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349914 [Multi-domain] Cd Length: 399 Bit Score: 45.02 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 48 PAPPFKEEKRATFILSKLEDLALENVEMDEEGNVFGLLRGvGNGPKIFVSAHLD-------TVFPEGTDTTVKRENGI-- 118
Cdd:cd05664 14 PELSFQEHRTAAKIAEELRKLGFEVTTGIGGTGVVAVLRN-GEGPTVLLRADMDalpveenTGLPYASTVRMKDWDGKev 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 119 --LYAPGivDDTSgLAEMLSIIRAFKETKIEPIGDIVFGGTVGEEGLGnlrGVRAFFNnhqdiDGFIS-IDGPEI----- 190
Cdd:cd05664 93 pvMHACG--HDMH-VAALLGAARLLVEAKDAWSGTLIAVFQPAEETGG---GAQAMVD-----DGLYDkIPKPDVvlaqh 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 191 ------SRICYK----GTGSYRYKVTYKGPGGHsfGAfgLPSA-IHALGRAIAEIADIQT----KADPKT--TFTVGEIS 253
Cdd:cd05664 162 vmpgpaGTVGTRpgrfLSAADSLDITIFGRGGH--GS--MPHLtIDPVVMAASIVTRLQTivsrEVDPQEfaVVTVGSIQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 254 GGTSVNAIAAEAHMYVDLRSNDPqelvKLEQQFLTIVEKACNDENARWNTDKIKWKTEKigDRPAATQPDDTPIVQIASA 333
Cdd:cd05664 238 AGSAENIIPDEAELKLNVRTFDP----EVREKVLNAIKRIVRAECAASGAPKPPEFTYT--DSFPATVNDEDATARLAAA 311
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 517982453 334 ATEAMG------IKPTLAgpsSTD-SNVPMSLGVPSVTLGKGG 369
Cdd:cd05664 312 FREYFGedrvveVPPVSA---SEDfSILATAFGVPSVFWFIGG 351
|
|
| M42_Frv |
cd05656 |
M42 Peptidase, endoglucanases; Peptidase M42 family, Frv (Frv Operon Protein; Endo-1 ... |
46-103 |
7.31e-05 |
|
M42 Peptidase, endoglucanases; Peptidase M42 family, Frv (Frv Operon Protein; Endo-1 4-Beta-Glucanase; Cellulase Protein; Endoglucanase; Endo-1 4-Beta-Glucanase Homolog; Glucanase; EC. 3.2.1.4) subfamily. Frv is a co-catalytic metallopeptidase, found in archaea and bacteria, including Pyrococcus horikoshii tetrahedral shaped phTET1 (DAPPh1; FrvX; PhDAP aminopeptidase; PhTET aminopeptidase; deblocking aminopeptidase), phTET2 (DAPPh2) and phTET3 (DAPPh3), Haloarcula marismortui TET (HmTET) as well as Bacillus subtilis YsdC. All of these exhibit aminopeptidase and deblocking activities. The HmTET is a broad substrate aminopeptidase capable of degrading large peptides. PhTET2, which shares 24% identity with HmTET, is a cobalt-activated peptidase and possibly a deblocking aminopeptidase, assembled as a 12-subunit tetrahedral dodecamer, while PhTET1 can be alternatively assembled as a tetrahedral dodecamer or as an octahedral tetracosameric structure. The active site in such a self-compartmentalized complex is located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers. PhTET2 cleaves polypeptides by a nonprocessive mechanism, preferring N-terminal hydrophobic or uncharged polar amino acids. Streptococcus pneumoniae PepA (SpPepA) also forms dodecamer with tetrahedral architecture, and exhibits selective substrate specificity to acidic amino acids with the preference to glutamic acid, with the substrate binding S1 pocket containing an Arg allows electrostatic interactions with the N-terminal acidic residue in the substrate. The YsdC gene is conserved in a number of thermophiles, archaea and pathogenic bacterial species; the closest structural homolog is Thermotoga maritima FrwX (34% identity), which is annotated as either a cellulase or an endoglucanase, and is possibly involved in polysaccharide biosynthesis or degradation.
Pssm-ID: 349906 [Multi-domain] Cd Length: 337 Bit Score: 44.47 E-value: 7.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 517982453 46 EIPAPPFKEEKRATFILSKLEDLALEnVEMDEEGNVFGLLRGVGNGPKIFVSAHLDTV 103
Cdd:cd05656 8 EAPGPSGYEEEVRDVIKEELKPYVDE-VKVDGLGNLIARKKGKGEAPKVMIAAHMDEI 64
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
80-236 |
7.56e-05 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 44.75 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 80 NVFGLLRGVGNGPKIFVSAHLDTVfPEGTDTTV-----KRENGILYAPGIVDDTSGLAEMLSIIRAFKETKIEPIGDIVF 154
Cdd:PRK13013 73 NLVARRQGARDGDCVHFNSHHDVV-EVGHGWTRdpfggEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 155 GGTVGEE-----GLGNLRGVRAFFNNHqdIDGFISIDGPEISRICYKGTGSYRYKVTYKGPGGHSFGAFGLPSAIHALGR 229
Cdd:PRK13013 152 SGTADEEsggfgGVAYLAEQGRFSPDR--VQHVIIPEPLNKDRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGA 229
|
....*..
gi 517982453 230 AIAEIAD 236
Cdd:PRK13013 230 VLAEIEE 236
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
54-300 |
1.08e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of uncharacterized bacterial proteins predicted as putative amidohydrolases. 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: 349936 [Multi-domain] Cd Length: 371 Bit Score: 44.19 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 54 EEKRAT-FILSKLEDLALENVEMDEEGNVFGLLRGVGNGPKIFVSAHLDTV-FPEGTD----TTVKrenGILYAPGIVDD 127
Cdd:cd08014 17 QEYRTTaFVAERLRDLGLKPKEFPGGTGLVCDIGGKRDGRTVALRADMDALpIQEQTGlpyrSTVP---GVMHACGHDAH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 128 TS---GLAEMLSIIRAFKETKI----EPIGDIVFGGTVGEEGLGNLRGVRAFFNNHQDidgfisidgPEI--SRICYKG- 197
Cdd:cd08014 94 TAialGAALVLAALEEELPGRVrlifQPAEETMPGGALDMIRAGALDGVSAIFALHVD---------PRLpvGRVGVRYg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 198 ---TGSYRYKVTYKGPGGHSFGAFGLPSAIHALGRAIAEIADIQTKA-DPK--TTFTVGEISGGTSVNAIAAEAHMYVDL 271
Cdd:cd08014 165 pitAAADSLEIRIQGEGGHGARPHLTVDLVWAAAQVVTDLPQAISRRiDPRspVVLTWGSIEGGRAPNVIPDSVELSGTV 244
|
250 260
....*....|....*....|....*....
gi 517982453 272 RSNDPQELVKLEQQFLTIVEKACNDENAR 300
Cdd:cd08014 245 RTLDPDTWAQLPDLVEEIVAGICAPYGAK 273
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
72-280 |
2.85e-04 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 42.88 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 72 NVEMDEEGNVFGLLRGVGNGPKIFVSAHLDTVfPEG----TDT-TVKRENGILYAPGIVDDTSGLAEMLSIIRAfketki 146
Cdd:PRK08737 44 QVEVIDHGAGAVSLYAVRGTPKYLFNVHLDTV-PDSphwsADPhVMRRTDDRVIGLGVCDIKGAAAALLAAANA------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 147 ePIGDIVFGGTVGEEGlGNLRGVRAFFNNHQDIDGFIsIDGPEISRICYKGTGSYRYKVTYKGPGGHSFGAF-GLPSAIH 225
Cdd:PRK08737 117 -GDGDAAFLFSSDEEA-NDPRCVAAFLARGIPYEAVL-VAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKQdPSASALH 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517982453 226 ALGRAIAEIAD-IQTKADPK------TTFTVGEISGGTSVNAIAAEAHMYVDLR---SNDPQELV 280
Cdd:PRK08737 194 QAMRWGGQALDhVESLAHARfggltgLRFNIGRVEGGIKANMIAPAAELRFGFRplpSMDVDGLL 258
|
|
| M28_like_PA |
cd05661 |
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ... |
33-163 |
4.31e-04 |
|
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 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. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.
Pssm-ID: 349911 [Multi-domain] Cd Length: 262 Bit Score: 41.79 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 33 DHENTIEEQIVIAEIPAPPFK--EEKRATFILSKLEDLALE-NVEMDEEGNVFGLLR---GVGNGPKIFVSAHLDTVfpe 106
Cdd:cd05661 12 DAENAYNHIRFLSQAIGVAGTpeELKAARYIEQQLKSLGYEvEVQPFTSHNVIATKKpdnNKNNNDIIIVTSHYDSV--- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 517982453 107 gtdttvkrengiLYAPGIVDDTSGLAEMLSIIRAFKETKIE-PIGDIVFGGTvgEEGL 163
Cdd:cd05661 89 ------------VKAPGANDNASGTAVTLELARVFKKVKTDkELRFIAFGAE--ENGL 132
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
222-350 |
9.37e-04 |
|
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: 41.11 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 222 SAIHALGRAIAEIADIqtKADPKTTFTVGEI---SGGTSVNAIAAEAHMYVDLRSNDPQELVKLEQQFLTIVEKACNDEN 298
Cdd:cd08018 189 NAIEAASAIVNAVNAI--HLDPNIPWSVKMTklqAGGEATNIIPDKAKFALDLRAQSNEAMEELKEKVEHAIEAAAALYG 266
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 517982453 299 ArwntdKIKWKTEkiGDRPAATqPDDTPIVQIASAATEAMGiKPTLAGPSST 350
Cdd:cd08018 267 A-----SIEITEK--GGMPAAE-YDEEAVELMEEAITEVLG-EEKLAGPCVT 309
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
46-294 |
1.14e-03 |
|
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. 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 in 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.
Pssm-ID: 349920 [Multi-domain] Cd Length: 367 Bit Score: 40.71 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 46 EIPAPPFKEEKRATFILSKLEDLALENVEM--DEEGNVFGLLRGVGNGPKIFVSAHLDTVfpegtdtTVKRENGILYA-- 121
Cdd:cd05670 11 QIPELGLEEFKTQAYLLDVIAKLPQDNLEIktWCETGILVYVEGSNPERTIGYRADIDAL-------PIEEETGLPFAsk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 122 -PGIV-----DDTSGLAemLSIIRAFKETKiePIGDIVFGGTVGEEGLGNlrGVRAF----FNNHQdIDGFISI----DG 187
Cdd:cd05670 84 hPGVMhacghDGHMTIA--LGLLEYFAQHQ--PKDNLLFIFQPAEEGPGG--AKRMYesgvFGKWR-PDEIYGLhvnpDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 188 PEISRICYKGT---GSYRYKVTYKGPGGHsfGAFglP-SAIHALGRAIAEIADIQT----KADP--KTTFTVGEISGGTS 257
Cdd:cd05670 157 PVGTIATRSGTlfaGTSELHIDFIGKSGH--AAY--PhNANDMVVAAANFVTQLQTivsrNVDPidGAVVTIGKIHAGTA 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 517982453 258 VNAIAAEAHMYVDLRSNDPQELVKLEQQFLTIVEKAC 294
Cdd:cd05670 233 RNVIAGTAHLEGTIRTLTQEMMELVKQRVRDIAEGIE 269
|
|
| M42 |
cd05638 |
M42 Peptidases, also known as glutamyl aminopeptidase family; Peptidase M42 family proteins, ... |
44-103 |
1.35e-03 |
|
M42 Peptidases, also known as glutamyl aminopeptidase family; Peptidase M42 family proteins, also known as glutamyl aminopeptidases (GAP), are co-catalytic metallopeptidases, found in archaea and bacteria. They typically bind two zinc or cobalt atoms and include cellulase and endo-1,4-beta-glucanase (endoglucanase). Some of the enzymes exhibit typical aminopeptidase specificity, whereas others are also capable of N-terminal deblocking activity, i.e. hydrolyzing acylated N-terminal residues. GAP removes glutamyl residues from the N-terminus of peptide substrates, but is also effective against aspartyl and, to a lesser extent, seryl residues. Lactococcus lactis glutamyl aminopeptidase (PepA; aminopeptidase A) has high thermal stability and aids growth of the organism in milk. Pyrococcus horikoshii contain a thermostable de-blocking aminopeptidase member of this family, used commercially for N-terminal protein sequencing.
Pssm-ID: 193517 [Multi-domain] Cd Length: 332 Bit Score: 40.52 E-value: 1.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 44 IAEIPAPPFKEEKRATFILSKLEDLALEnVEMDEEGNVFGLLRGvGNGPKIFVSAHLDTV 103
Cdd:cd05638 6 LVEIPAISGYEAKIRNFIIEEIKDWVDE-VKVDGLGNLILTLKE-ENAPRVLIAAH*DEV 63
|
|
| M28_like_PA_PDZ_associated |
cd05663 |
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ... |
53-175 |
2.31e-03 |
|
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ domain; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 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. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.
Pssm-ID: 349913 [Multi-domain] Cd Length: 266 Bit Score: 39.36 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 53 KEEKRAT-FILSKLEDLALEnVEMDEEG-------------NVFGLLRGVGN--GPKIFVSAHLDTVFPEGTDTtVKREN 116
Cdd:cd05663 17 KGEKLAAdYIAQRFEELGLE-PGLDNGTyfqpfefttgtgrNVIGVLPGKGDvaDETVVVGAHYDHLGYGGEGS-LARGD 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517982453 117 GILYAPGIVDDTSGLAEMLSIIRAFKETKIEPI--GDIVFGGTVGEEgLGnLRGVRAFFNN 175
Cdd:cd05663 95 ESLIHNGADDNASGVAAMLELAAKLVDSDTSLAlsRNLVFIAFSGEE-LG-LLGSKHFVKN 153
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
54-235 |
2.63e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 39.83 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 54 EEKRATFILSKLEDLALENVEMDEE---GNVFGLLRGVGNG-PKIFVSAHLDTVFPEGTDTTV-----KRENGILYAPGI 124
Cdd:PRK07906 24 EREAAEYVAEKLAEVGLEPTYLESApgrANVVARLPGADPSrPALLVHGHLDVVPAEAADWSVhpfsgEIRDGYVWGRGA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517982453 125 VDDTSGLAEMLSIIRAFKETKIEPIGDIVFGGTVGEEGLGNLrGVRAFFNNHQD-----------IDGFiSIDGPEISRI 193
Cdd:PRK07906 104 VDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEAGGTY-GAHWLVDNHPElfegvteaiseVGGF-SLTVPGRDRL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517982453 194 cY------KGTGSYRykVTYKGPGGHsfGAFGLP-SAIHALGRAIAEIA 235
Cdd:PRK07906 182 -YlietaeKGLAWMR--LTARGRAGH--GSMVNDdNAVTRLAEAVARIG 225
|
|
| |
