|
Name |
Accession |
Description |
Interval |
E-value |
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
61-396 |
0e+00 |
|
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: 512.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 61 LISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQRVSSnpTVRDNVYAYLGSQRNTKVVLTSHIDTVNPFLPYYI 140
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKQPVEN--KDRFNVYAYPGSSRQPRVLLTSHIDTVPPFIPYSI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 141 E--GDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIGMKTVANKLNADWEVAIFGEPTENKLG 218
Cdd:cd05652 79 SdgGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGDGMKAFNDLGLNTWDAVIFGEPTELKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 219 VGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFLLRQCVKLMDTDLPKSKLLGPSTINIGTIEGGAAANILAAEAKAEVFI 298
Cdd:cd05652 159 SGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPSSELLGPTTLNIGRISGGVAANVVPAAAEASVAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 299 RVAEDIETIRDIAED-----LFDTEHSEIKVIQYSPPQYLDYDIPGMDTVVLAYATDIPYLSDrKMKIYLFGPGSIREAH 373
Cdd:cd05652 239 RLAAGPPEVKDIVKEavagiLTDTEDIEVTFTSGYGPVDLDCDVDGFETDVVAYGTDIPYLKG-DHKRYLYGPGSILVAH 317
|
330 340
....*....|....*....|...
gi 19075180 374 GPNEYVTFSQLFEGLNGYKRMVM 396
Cdd:cd05652 318 GPDEAITVSELEEAVEGYKKLIL 340
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
63-395 |
1.16e-74 |
|
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: 236.43 E-value: 1.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 63 SLHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQRVSSnptvRDNVYAYLGSQRNTKVVLTSHIDTVNP-------F 135
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEG----RGNLVATVGGGDGPVLLLNGHIDTVPPgdgdkwsF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 136 LPY--YIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIGMKTVANKLNA-DWEVAIFGEP 212
Cdd:cd08659 77 PPFsgRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLEAGYAdRLDALIVGEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 213 TENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFLLRQCVKL--MDTDLPKSKLLGPSTINIGTIEGGAAANILAA 290
Cdd:cd08659 157 TGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELrtLFEELPAHPLLGPPTLNVGVINGGTQVNSIPD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 291 EAKAEVFIR--VAEDIETIRDIAEDLFDTEHSEIKViQYSPPQYLDYDIPGMDTVVLA------------------YATD 350
Cdd:cd08659 237 EATLRVDIRlvPGETNEGVIARLEAILEEHEAKLTV-EVSLDGDPPFFTDPDHPLVQAlqaaaralggdpvvrpftGTTD 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 19075180 351 IPYLS-DRKMKIYLFGPGSIREAHGPNEYVTFSQLFEGLNGYKRMV 395
Cdd:cd08659 316 ASYFAkDLGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
59-395 |
4.68e-71 |
|
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: 227.85 E-value: 4.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 59 DNLISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQRVSSNptvRDNVYAYL-GSQRNTKVVLTSHIDTV----- 132
Cdd:COG0624 12 DEALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPPG---RPNLVARRpGDGGGPTLLLYGHLDVVppgdl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 133 -----NPFLPYyIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIGMKTV----ANKLNAD 203
Cdd:COG0624 89 elwtsDPFEPT-IEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSPGARALveelAEGLKAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 204 WevAIFGEPTE-NKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFLLRQCVKLMDTDLP--KSKLLGPSTINIGTIE 280
Cdd:COG0624 168 A--AIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDgrADPLFGRTTLNVTGIE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 281 GGAAANILAAEAKAEVFIRVA--EDIETIRDIAEDLFDTEHSEIKV-----IQYSPPQYLDYDIPGMDTVVLA------- 346
Cdd:COG0624 246 GGTAVNVIPDEAEAKVDIRLLpgEDPEEVLAALRALLAAAAPGVEVevevlGDGRPPFETPPDSPLVAAARAAirevtgk 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 19075180 347 --------YATDIPYLSDR-KMKIYLFGPGSIREAHGPNEYVTFSQLFEGLNGYKRMV 395
Cdd:COG0624 326 epvlsgvgGGTDARFFAEAlGIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLL 383
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
57-395 |
1.05e-46 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 164.39 E-value: 1.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 57 AGDNLISLHKSLVEIES---LGGNEVNVSDFLKSYLESKGLTVELQRV-----SSNPTVRDNVYAYLGSqRNTKVVLTSH 128
Cdd:PRK08651 4 MMFDIVEFLKDLIKIPTvnpPGENYEEIAEFLRDTLEELGFSTEIIEVpneyvKKHDGPRPNLIARRGS-GNPHLHFNGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 129 IDTV---------NPFLPYYIeGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQegdLSLLFVVGEEIDGIGMKTVANK 199
Cdd:PRK08651 83 YDVVppgegwsvnVPFEPKVK-DGKVYGRGASDMKGGIAALLAAFERLDPAGDGN---IELAIVPDEETGGTGTGYLVEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 200 LNADWEVAIFGEPT-ENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFLLRQCVKLM---DTDLPKSKL----LGP 271
Cdd:PRK08651 159 GKVTPDYVIVGEPSgLDNICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKsslSTIKSKYEYdderGAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 272 STINIG--TIEGGAAANILAAEAKAEVFIRV--AEDIETIRDIAEDLFDT------EHSEIKVIQYSPPQYLDYDIPGMD 341
Cdd:PRK08651 239 PTVTLGgpTVEGGTKTNIVPGYCAFSIDRRLipEETAEEVRDELEALLDEvapelgIEVEFEITPFSEAFVTDPDSELVK 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075180 342 TVVLAY---------------ATDIPYLSDRKMKIYLFGPGSIREAHGPNEYVTFSQLFEGLNGYKRMV 395
Cdd:PRK08651 319 ALREAIrevlgvepkktislgGTDARFFGAKGIPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVL 387
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
66-384 |
4.98e-46 |
|
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: 161.99 E-value: 4.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 66 KSLVEIESLGGN-EVNVSDFLKSYLESKGLTVELQRVSSNPtvRDNVYAYLGSQRNTKVVLTSHIDTV---------NPF 135
Cdd:cd03894 4 ARLVAFDTVSRNsNLALIEYVADYLAALGVKSRRVPVPEGG--KANLLATLGPGGEGGLLLSGHTDVVpvdgqkwssDPF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 136 LPYyIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGkvQEGDLSLLFVVGEEIDGIGMKTVANKLNADW---EVAIFGEP 212
Cdd:cd03894 82 TLT-ERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAK--LRKPLHLAFSYDEEVGCLGVRHLIAALAARGgrpDAAIVGEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 213 TENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEF---LLRQCVKLMDTDLPK---SKLLGP-STINIGTIEGGAAA 285
Cdd:cd03894 159 TSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAaarLIGKLRELADRLAPGlrdPPFDPPyPTLNVGLIHGGNAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 286 NILAAEAKAEVFIRV-----AEDI-ETIRDIAEDLFDTEHSEIKVIQYSPPQYLDYDI------------PGMDTVVLAY 347
Cdd:cd03894 239 NIVPAECEFEFEFRPlpgedPEAIdARLRDYAEALLEFPEAGIEVEPLFEVPGLETDEdaplvrlaaalaGDNKVRTVAY 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 19075180 348 ATDIPYLSDRKMKIYLFGPGSIREAHGPNEYVTFSQL 384
Cdd:cd03894 319 GTEAGLFQRAGIPTVVCGPGSIAQAHTPDEFVELEQL 355
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
62-386 |
5.45e-46 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 162.18 E-value: 5.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 62 ISLHKSLVEIESL---GGNEVNVSDFLKSYLESKGLTVELQRVSSN--PTVRDNVYAYLGSQRNTKVVLTSHIDTV---- 132
Cdd:TIGR01910 1 VELLKDLISIPSVnppGGNEETIANYIKDLLREFGFSTDVIEITDDrlKVLGKVVVKEPGNGNEKSLIFNGHYDVVpagd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 133 ------NPFLPYYIEGdKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIG-MKTVANKLNADWE 205
Cdd:TIGR01910 81 lelwktDPFKPVEKDG-KLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGtLYLLQRGYFKDAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 206 VAIFGEPTEN-KLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFL------LRQCVKLMDTDLPKSKLLGPSTINIGT 278
Cdd:TIGR01910 160 GVLIPEPSGGdNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLakliteLNELEEHIYARNSYGFIPGPITFNPGV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 279 IEGGAAANILAAEAKAEVFIRVA--EDIETIRDIAEDLFD------------TEHSEIKVIQYSPP--------QYLDYD 336
Cdd:TIGR01910 240 IKGGDWVNSVPDYCEFSIDVRIIpeENLDEVKQIIEDVVKalsksdgwlyenEPVVKWSGPNETPPdsrlvkalEAIIKK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 19075180 337 IPGMDTVVLAYA--TDIPYLSDRKMKIYLFGPGSIREAHGPNEYVTFSQLFE 386
Cdd:TIGR01910 320 VRGIEPEVLVSTggTDARFLRKAGIPSIVYGPGDLETAHQVNEYISIKNLVE 371
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
62-395 |
5.71e-43 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 154.27 E-value: 5.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 62 ISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQRVSSNptvRDNVYAYLGSqrNTKVV-LTSHIDTVNP------ 134
Cdd:PRK08588 5 IQILADIVKINSVNDNEIEVANYLQDLFAKHGIESKIVKVNDG---RANLVAEIGS--GSPVLaLSGHMDVVAAgdvdkw 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 135 -FLPY--YIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIGMKT-----VANKLNAdwev 206
Cdd:PRK08588 80 tYDPFelTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGELGAKQltekgYADDLDA---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 207 AIFGEPTENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFLLR---QCVKLMDTDLPKSKLLGPSTINIGTIEGGA 283
Cdd:PRK08588 156 LIIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEfynEQKEYFDSIKKHNPYLGGLTHVVTIINGGE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 284 AANILAAEAKAEVFIR---------VAEDIETI-------------RDIAEDLF----DTEHSEIKVIQYSPPQYLDYDI 337
Cdd:PRK08588 236 QVNSVPDEAELEFNIRtipeydndqVISLLQEIinevnqngaaqlsLDIYSNHRpvasDKDSKLVQLAKDVAKSYVGQDI 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 338 PgmdTVVLAYATDIPYLSDRK--MKIYLFGPGSIREAHGPNEYVTFSQLFEGLNGYKRMV 395
Cdd:PRK08588 316 P---LSAIPGATDASSFLKKKpdFPVIIFGPGNNLTAHQVDEYVEKDMYLKFIDIYKEII 372
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
62-395 |
1.14e-37 |
|
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: 138.98 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 62 ISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQRvssnptvrDNVYAYLGSQRNTK--VVLTSHIDTV------- 132
Cdd:cd05651 3 IELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRKG--------NNVWAENGHFDEGKptLLLNSHHDTVkpnagwt 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 133 -NPFLPYyIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKvQEGDLSLLFVVGEEIDGI-GMKTVANKLnADWEVAIFG 210
Cdd:cd05651 75 kDPFEPV-EKGGKLYGLGSNDAGASVVSLLATFLHLYSEGP-LNYNLIYAASAEEEISGKnGIESLLPHL-PPLDLAIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 211 EPTENKLGVGHKGNFRFDVYAHGKACHSGYPqEGFSAIEFLLRQCVKLMDTDLPK-SKLLGPSTINIGTIEGGAAANILA 289
Cdd:cd05651 152 EPTEMQPAIAEKGLLVLDCTARGKAGHAARN-EGDNAIYKALDDIQWLRDFRFDKvSPLLGPVKMTVTQINAGTQHNVVP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 290 AEAKAEVFIRVAE---DIETIRDIAEDLfdteHSEIKVIQY-SPPQYLDYDIPGMDTVVLAYATDI--PYLSDR------ 357
Cdd:cd05651 231 DSCTFVVDIRTTEaytNEEIFEIIRGNL----KSEIKPRSFrLNSSAIPPDHPIVQAAIAAGRTPFgsPTLSDQalmpfp 306
|
330 340 350
....*....|....*....|....*....|....*...
gi 19075180 358 KMKIylfGPGSIREAHGPNEYVTFSQLFEGLNGYKRMV 395
Cdd:cd05651 307 SVKI---GPGDSSRSHTADEFIELSEIEEGIDIYIELL 341
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
62-385 |
4.10e-37 |
|
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: 137.90 E-value: 4.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 62 ISLHKSLVEIESL---GGNEVNVSDFLKSYLESKGLTVELQrvsSNPTVRDNVYAYL-GSQRNTKVVLTSHIDTVnPF-- 135
Cdd:cd08011 1 VKLLQELVQIPSPnppGDNTSAIAAYIKLLLEDLGYPVELH---EPPEEIYGVVSNIvGGRKGKRLLFNGHYDVV-PAgd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 136 ------LPY--YIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGI-GMKTVANKLNADWEV 206
Cdd:cd08011 77 gegwtvDPYsgKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRaGTKYLLEKVRIKPND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 207 AIFGEPT-ENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFLLRQCVKLMDTDlpkskllgpSTINIGTIEGGAAA 285
Cdd:cd08011 157 VLIGEPSgSDNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELE---------KTVNPGVIKGGVKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 286 NILAAEAKAEVFIRVAEDIET--IRDIAEDLFDT-EHSEIKVIQYSPPQYLDYDIPGMD---------------TVVLAY 347
Cdd:cd08011 228 NLVPDYCEFSVDIRLPPGISTdeVLSRIIDHLDSiEEVSFEIKSFYSPTVSNPDSEIVKkteeaitevlgirpkEVISVG 307
|
330 340 350
....*....|....*....|....*....|....*...
gi 19075180 348 ATDIPYLSDRKMKIYLFGPGSIREAHGPNEYVTFSQLF 385
Cdd:cd08011 308 ASDARFYRNAGIPAIVYGPGRLGQMHAPNEYVEIDELI 345
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
124-396 |
4.36e-34 |
|
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: 128.62 E-value: 4.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 124 VLTSHIDTV-------NPFLPyyIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGkVQEGDLSLLFVVGEEIDGIGMKTV 196
Cdd:pfam01546 1 LLRGHMDVVpdeetwgWPFKS--TEDGKLYGRGHDDMKGGLLAALEALRALKEEG-LKKGTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 197 AN-----KLNADWEVAIF-GEPTEN------KLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFLLRQCVKLMDTDLP 264
Cdd:pfam01546 78 IEdglleREKVDAVFGLHiGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 265 KSKLLGPSTINIGT---IEGGaaanilaaeA-------KAEVFIRVAED------IETIRDIAEDLFD--TEHSEIKVIQ 326
Cdd:pfam01546 158 NVDPLDPAVVTVGNitgIPGG---------VnvipgeaELKGDIRLLPGedleelEERIREILEAIAAayGVKVEVEYVE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 327 YSPPQYLD---------------YDIPGMDTVV-LAYATDIPYLSDRKMKIY-LFGPGSIReAHGPNEYVTFSQLFEGLN 389
Cdd:pfam01546 229 GGAPPLVNdsplvaalreaakelFGLKVELIVSgSMGGTDAAFFLLGVPPTVvFFGPGSGL-AHSPNEYVDLDDLEKGAK 307
|
....*..
gi 19075180 390 GYKRMVM 396
Cdd:pfam01546 308 VLARLLL 314
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
61-387 |
2.68e-30 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 119.09 E-value: 2.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 61 LISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQRVssnptvrDNVYAYLGSQrNTKVVLTSHIDTVNPFLPYYI 140
Cdd:PRK08652 4 AKELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIESD-------GEVINIVVNS-KAELFVEVHYDTVPVRAEFFV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 141 EGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKvqEGDLSLLFVVGEEIDGIGMKTVANKLNAdwEVAIFGEPTENKLGVG 220
Cdd:PRK08652 76 DGVYVYGTGACDAKGGVAAILLALEELGKEFE--DLNVGIAFVSDEEEGGRGSALFAERYRP--KMAIVLEPTDLKVAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 221 HKGNFRFDVYAHGKACHSGYPQEGFSAIEFLLRQCVKLMDTDLPKSKLLGPStINIGTIEGGAAANILAAEAKAEVFIRV 300
Cdd:PRK08652 152 HYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPH-IGIQEIIGGSPEYSIPALCRLRLDARI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 301 --AEDIETIRDIAEDLFDTEHSEIKVIQYSPPQYLD------------YDIPGMDTV--VLAYATDIPYLSDRKMKIYLF 364
Cdd:PRK08652 231 ppEVEVEDVLDEIDPILDEYTVKYEYTEIWDGFELDedeeivqllekaMKEVGLEPEftVMRSWTDAINFRYNGTKTVVW 310
|
330 340
....*....|....*....|...
gi 19075180 365 GPGSIREAHGPNEYVTFSQLFEG 387
Cdd:PRK08652 311 GPGELDLCHTKFERIDVREVEKA 333
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
61-330 |
1.37e-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: 117.69 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 61 LISLHKSLVEIESLGGN--EVN-VSDFLKSYLESKGLTVELQRvssNPTVRDNVYAYLGSQRNTKVVLTSHIDTVNP--- 134
Cdd:cd03885 1 MLDLLERLVNIESGTYDkeGVDrVAELLAEELEALGFTVERRP---LGEFGDHLIATFKGTGGKRVLLIGHMDTVFPegt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 135 --FLPYYIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIGMKTVANKLNADWEVAIFGEP 212
Cdd:cd03885 78 laFRPFTVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRELIEEEAKGADYVLVFEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 213 T--ENKLGVGHKGNFRFDVYAHGKACHSG-YPQEGFSAIEFLLRQCVKLMD-TDLPKSkllgpSTINIGTIEGGAAANIL 288
Cdd:cd03885 158 AraDGNLVTARKGIGRFRLTVKGRAAHAGnAPEKGRSAIYELAHQVLALHAlTDPEKG-----TTVNVGVISGGTRVNVV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 19075180 289 AAEAKAEVFIRVAEDIE------TIRDIAEDLFDTE-HSEIKVIQYSPP 330
Cdd:cd03885 233 PDHAEAQVDVRFATAEEadrveeALRAIVATTLVPGtSVELTGGLNRPP 281
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
61-393 |
1.15e-27 |
|
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: 111.76 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 61 LISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLtVELQRVSsnptvrDNVYAYLGSQRNTKVVLTSHIDTV---NPFLP 137
Cdd:cd05647 1 PIELTAALVDIPSVSGNEKPIADEIEAALRTLPH-LEVIRDG------NTVVARTERGLASRVILAGHLDTVpvaGNLPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 138 YYIEGDKIHGRGSCDAKSSVAAQifamLELMSEGKVQEG--DLSLLFVVGEEIDGI--GMKTVANKLnADW---EVAIFG 210
Cdd:cd05647 74 RVEEDGVLYGCGATDMKAGDAVQ----LKLAATLAAATLkhDLTLIFYDCEEVAAElnGLGRLAEEH-PEWlaaDFAVLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 211 EPTENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEfllrqcvKLMDTdLPKSKLLGPSTINIG-----------TI 279
Cdd:cd05647 149 EPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIH-------KLAPI-LARLAAYEPRTVNIDgltyreglnavFI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 280 EGGAAANILAAEAKAEVFIRVAEDietiRDIAE------DLFDTEHSEIKVIQYSPPQyldydIPGMDTVVLA------- 346
Cdd:cd05647 221 SGGVAGNVIPDEARVNLNYRFAPD----KSLAEaiahvrEVFEGLGYEIEVTDLSPGA-----LPGLDHPVARdlieavg 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 19075180 347 ------YA-TDIPYLSDRKMKIYLFGPGSIREAHGPNEYVTFSQLFEGLNGYKR 393
Cdd:cd05647 292 gkvrakYGwTDVARFSALGIPAVNFGPGDPLLAHKRDEQVPVEQITACAAILRR 345
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
83-384 |
3.44e-27 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 111.43 E-value: 3.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 83 DFLKSYLESKGLTVELqrvSSNPT-VRDNVYAYLGSQRNTKVVLTSHID---------TVNPFLPYyIEGDKIHGRGSCD 152
Cdd:PRK07522 29 EWVRDYLAAHGVESEL---IPDPEgDKANLFATIGPADRGGIVLSGHTDvvpvdgqawTSDPFRLT-ERDGRLYGRGTCD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 153 AKSSVAAQIfAMLELMSEGKVQEGdLSLLFVVGEEIDGIG---MKTVANKLNADWEVAIFGEPTENKLGVGHKGNFRFDV 229
Cdd:PRK07522 105 MKGFIAAAL-AAVPELAAAPLRRP-LHLAFSYDEEVGCLGvpsMIARLPERGVKPAGCIVGEPTSMRPVVGHKGKAAYRC 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 230 YAHGKACHSGYPQEGFSAIEF---LLRQCVKLMDtdlpKSKLLGP---------STINIGTIEGGAAANILAAEAKAEVF 297
Cdd:PRK07522 183 TVRGRAAHSSLAPQGVNAIEYaarLIAHLRDLAD----RLAAPGPfdalfdppySTLQTGTIQGGTALNIVPAECEFDFE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 298 IRV-----AEDIET-IRDIAEDLFDTE--------HSEIKVIQYSPPQYLDYDIP----------GMDTVVLAYATD--- 350
Cdd:PRK07522 259 FRNlpgddPEAILArIRAYAEAELLPEmravhpeaAIEFEPLSAYPGLDTAEDAAaarlvraltgDNDLRKVAYGTEagl 338
|
330 340 350
....*....|....*....|....*....|....*....
gi 19075180 351 -----IPYLsdrkmkiyLFGPGSIREAHGPNEYVTFSQL 384
Cdd:PRK07522 339 fqragIPTV--------VCGPGSIEQAHKPDEFVELAQL 369
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
66-379 |
6.73e-27 |
|
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: 110.86 E-value: 6.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 66 KSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQR--------------VSSNPTVRDNVYAYLGSQRNT--KVVLTSHI 129
Cdd:cd03895 4 QDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDRWEidveklkhhpgfspVAVDYAGAPNVVGTHRPRGETgrSLILNGHI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 130 DTV----------NPFLPYyIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIGMK-TVAN 198
Cdd:cd03895 84 DVVpegpvelwtrPPFEAT-IVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNGALaALMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 199 KLNADweVAIFGEPTENKLGVGHKG--NFRFDVYahGKACHSGYPQEGFSAIE---FL---LRQCVKLMDTDLPKSKLLG 270
Cdd:cd03895 163 GYRAD--AALIPEPTELKLVRAQVGviWFRVKVR--GTPAHVAEASEGVNAIEkamHLiqaLQELEREWNARKKSHPHFS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 271 ----PSTINIGTIEGGAAANILAAEAKAEvfIRVA----EDIETIR-DIAEDLFDTEHSEIKV------IQYSPPQYLDY 335
Cdd:cd03895 239 dhphPINFNIGKIEGGDWPSSVPAWCVLD--CRIGiypgESPEEARrEIEECVADAAATDPWLsnhppeVEWNGFQAEGY 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075180 336 DIP----------------------------GMDTVVLAYATDIPYLsdrkmkiyLFGPGSiREAHGPNEYV 379
Cdd:cd03895 317 VLEpgsdaeqvlaaahqavfgtppvqsamtaTTDGRFFVLYGDIPAL--------CYGPGS-RDAHGFDESV 379
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
62-395 |
6.65e-25 |
|
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: 103.97 E-value: 6.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 62 ISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQRVssnptvrDNVYAYLGSQRNTkVVLTSHIDTVNPFLPYYIE 141
Cdd:cd05653 4 VELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEA-------GNAVGGAGSGPPD-VLLLGHIDTVPGEIPVRVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 142 GDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQegdLSLLFVVGEEIDGIGMKTVANK-LNADWevAIFGEPTeNKLGV- 219
Cdd:cd05653 76 GGVLYGRGAVDAKGPLAAMILAASALNEELGAR---VVVAGLVDEEGSSKGARELVRRgPRPDY--IIIGEPS-GWDGIt 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 220 -GHKGNFRFDVYAHGKACHSGYPQEG--FSAIEFLLR---------QCVKLMDTDLPkskllgpsTInigtIEGGAAANI 287
Cdd:cd05653 150 lGYRGSLLVKIRCEGRSGHSSSPERNaaEDLIKKWLEvkkwaegynVGGRDFDSVVP--------TL----IKGGESSNG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 288 LAAEAKAEVFIRVAEDIETIRDIAEDLFDTEHSEIKVIQYSPPQYLDYDIP-------------GMDTVVLAYAT-DIPY 353
Cdd:cd05653 218 LPQRAEATIDLRLPPRLSPEEAIALATALLPTCELEFIDDTEPVKVSKNNPlarafrrairkqgGKPRLKRKTGTsDMNV 297
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 19075180 354 LSDRKMK-IYLFGPGSIREAHGPNEYVTFSQLFEGLNGYKRMV 395
Cdd:cd05653 298 LAPLWTVpIVAYGPGDSTLDHTPNEHIELAEIERAAAVLKGAL 340
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
59-282 |
1.09e-24 |
|
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: 104.10 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 59 DNLISLHKSLVEIESL--------GGNEVNVSDFLKSYLESKGLtvELQRVSSNPTvRDNVYAYL-GSQRNTKVVLTSHI 129
Cdd:cd08013 1 DDPVSLTQTLVRINSSnpslsatgGAGEAEIATYVAAWLAHRGI--EAHRIEGTPG-RPSVVGVVrGTGGGKSLMLNGHI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 130 DTV-------NPFLPYYIEGdKIHGRGSCDAKSSVAAQIFAMLElmSEGKVQEGDLSLLFVVGEEIDGIGMKTVankLNA 202
Cdd:cd08013 78 DTVtldgydgDPLSGEIADG-RVYGRGTLDMKGGLAACMAALAD--AKEAGLRGDVILAAVADEEDASLGTQEV---LAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 203 DW--EVAIFGEPTENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAI----EFLLRqcVKLMDTDLPKSK---LLGPST 273
Cdd:cd08013 152 GWraDAAIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAIlkagYFLVA--LEEYQQELPERPvdpLLGRAS 229
|
....*....
gi 19075180 274 INIGTIEGG 282
Cdd:cd08013 230 VHASLIKGG 238
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
68-380 |
2.55e-24 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 102.82 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 68 LVEIESLGGNEVNVSDFLKSYLESKGLTVELQRVSsnptvrdNVYAYLGSQRNTK---VVLTSHIDTVNPFL-----PYy 139
Cdd:COG2195 12 YVKIPTPSDHEEALADYLVEELKELGLEVEEDEAG-------NVIATLPATPGYNvptIGLQAHMDTVPQFPgdgikPQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 140 IEGDKIHGRGS----CDAKSSVAAqIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIGMKTV-ANKLNADWEVAIFGEPtE 214
Cdd:COG2195 84 IDGGLITADGTttlgADDKAGVAA-ILAALEYLKEPEIPHGPIEVLFTPDEEIGLRGAKALdVSKLGADFAYTLDGGE-E 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 215 NKLGVGhkgNF---RFDVYAHGKACHSGY-PQEGFSAI----EFLlrqcvklmdTDLPKSKLLGPSTINIGTIEGGAAAN 286
Cdd:COG2195 162 GELEYE---CAgaaDAKITIKGKGGHSGDaKEKMINAIklaaRFL---------AALPLGRIPEETEGNEGFIHGGSATN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 287 ILAAEAKAEVFIR------VAEDIETIRDIAEDLF--------DTEHSEikviQYsPPQYLDYDIPGMDTVVLAYA---- 348
Cdd:COG2195 230 AIPREAEAVYIIRdhdrekLEARKAELEEAFEEENakygvgvvEVEIED----QY-PNWKPEPDSPIVDLAKEAYEelgi 304
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 19075180 349 ----------TDIPYLSDRKMKIYLFGPGsIREAHGPNEYVT 380
Cdd:COG2195 305 epkikpirggLDGGILSFKGLPTPNLGPG-GHNFHSPDERVS 345
|
|
| dapE-lys-deAc |
TIGR01902 |
N-acetyl-ornithine/N-acetyl-lysine deacetylase; This clade of mainly archaeal and related ... |
64-392 |
2.06e-23 |
|
N-acetyl-ornithine/N-acetyl-lysine deacetylase; This clade of mainly archaeal and related bacterial species contains two characterized enzymes, an deacetylase with specificity for both N-acetyl-ornithine and N-acetyl-lysine from Thermus, which is found within a lysine biosynthesis operon, and a fusion protein with acetyl-glutamate kinase (an enzyme of ornithine biosynthesis) from Lactobacillus. It is possible that all of the sequences within this clade have dual specificity, or that a mix of specificities have evolved within this clade.
Pssm-ID: 130957 [Multi-domain] Cd Length: 336 Bit Score: 99.93 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 64 LHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQRVssnptvrDNVYAYLGSQrNTKVVLTSHIDTVNPFLPYYIEGD 143
Cdd:TIGR01902 2 LLKDLLEIYSPSGKEANAAKFLEEISKDLGLKLIIDDA-------GNFILGKGDG-HKKILLAGHVDTVPGYIPVKIEGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 144 KIHGRGSCDAKSSVAAQIFAMLELmsegkvQEGDLSLLFV--VGEEIDGIGMKTVANKLNAdwEVAIFGEPTE-NKLGVG 220
Cdd:TIGR01902 74 LLYGRGAVDAKGPLIAMIFATWLL------NEKGIKVIVSglVDEESSSKGAREVIDKNYP--FYVIVGEPSGaEGITLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 221 HKGNFRFDVYAHGKACHSGYpqeGFSAIEFLLRQCVKLMDT-----DLPKSKLLgPSTINIGTIEggaaaniLAAEAKAE 295
Cdd:TIGR01902 146 YKGSLQLKIMCEGTPFHSSS---AGNAAELLIDYSKKIIEVykqpeNYDKPSIV-PTIIRFGESY-------NDTPAKLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 296 VFIRVA-----EDIETIRDIAEDlfdtEHSEIKVIQYSPPQYLDYDIPGMDTVVLAY--ATDIPYL------SDRKM--- 359
Cdd:TIGR01902 215 LHFDLRyppnnKPEEAIKEITDK----FPICLEIVDETPPYKVSRNNPLVRAFVRAIrkQGMKPRLkkktgtSDMNIlap 290
|
330 340 350
....*....|....*....|....*....|....*..
gi 19075180 360 ----KIYLFGPGSIREAHGPNEYVTFSQLFEGLNGYK 392
Cdd:TIGR01902 291 iwtvPMVAYGPGDSTLDHTPQEKISLAEYLIGIKTLM 327
|
|
| PRK06915 |
PRK06915 |
peptidase; |
62-386 |
8.41e-22 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 96.30 E-value: 8.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 62 ISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQR------------VSSNPTVRD--NVYAYL-GSQRNTKVVLT 126
Cdd:PRK06915 20 VKLLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIWEpsfkklkdhpyfVSPRTSFSDspNIVATLkGSGGGKSMILN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 127 SHIDTV----------NPFLPYYIEGdKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIG-MKT 195
Cdd:PRK06915 100 GHIDVVpegdvnqwdhHPYSGEVIGG-RIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEESGGAGtLAA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 196 VANKLNADweVAIFGEPTENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIE--FLLRQCVKLMD-------TDLPKS 266
Cdd:PRK06915 179 ILRGYKAD--GAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEksMFVIDHLRKLEekrndriTDPLYK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 267 KLLGPSTINIGTIEGGAAANILAAEAKAEVFIRVAEDiETIRDIAEDL-------------------------------- 314
Cdd:PRK06915 257 GIPIPIPINIGKIEGGSWPSSVPDSVILEGRCGIAPN-ETIEAAKEEFenwiaelndvdewfvehpvevewfgarwvpge 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19075180 315 FDTEHSEIKVIQySPPQYLDYDIP-------GMDTVVLAYATDIPylsdrkmkIYLFGPGSIREAHGPNEYVTFSQLFE 386
Cdd:PRK06915 336 LEENHPLMTTLE-HNFVEIEGNKPiieaspwGTDGGLLTQIAGVP--------TIVFGPGETKVAHYPNEYIEVDKMIA 405
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
59-282 |
4.32e-20 |
|
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: 90.97 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 59 DNLISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQRVSSNPTV-RDNVYAYLGSQRNT--KVVLTSHIDTVNP- 134
Cdd:cd05683 3 DRLINTFLELVQIDSETLHEKEISKVLKKKFENLGLSVIEDDAGKTTGGgAGNLICTLKADKEEvpKILFTSHMDTVTPg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 135 --FLPYYIEGDKIHGRGS----CDAKSSVAAqIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIGMKTV-ANKLNADWEVA 207
Cdd:cd05683 83 inVKPPQIADGYIYSDGTtilgADDKAGIAA-ILEAIRVIKEKNIPHGQIQFVITVGEESGLVGAKALdPELIDADYGYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 208 IFGEPTENKLGVGHKGNFRFDVYAHGKACHSG-YPQEGFSAI----EFLLRQCVKLMDTDlpkskllgpSTINIGTIEGG 282
Cdd:cd05683 162 LDSEGDVGTIIVGAPTQDKINAKIYGKTAHAGtSPEKGISAIniaaKAISNMKLGRIDEE---------TTANIGKFQGG 232
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
62-282 |
4.40e-20 |
|
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. 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 Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349886 [Multi-domain] Cd Length: 366 Bit Score: 90.64 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 62 ISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVElqRVSSNPTvrDNVYAYLGSQRNTkVVLTSHIDTV--------- 132
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCE--RLEFGGV--KNLWARRGTGGPH-LCFAGHTDVVppgdlegws 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 133 -NPFLPYYIEGdKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGI-GMKTVANKLNA-----DWe 205
Cdd:cd03891 76 sDPFSPTIKDG-MLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIdGTKKVLEWLKArgekiDY- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 206 vAIFGEPT-ENKLG----VGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFLLRQCVKLMDTDLPK-SKLLGPSTINIGTI 279
Cdd:cd03891 154 -CIVGEPTsEKKLGdtikIGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLDEgNEFFPPSSLQITNI 232
|
...
gi 19075180 280 EGG 282
Cdd:cd03891 233 DVG 235
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
66-249 |
7.84e-20 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 89.63 E-value: 7.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 66 KSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQRVssnptvrDNVYAYLGSQRNTkVVLTSHIDTVNPFLPYYIEGDKI 145
Cdd:PRK04443 13 KGLVEIPSPSGEEAAAAEFLVEFMESHGREAWVDEA-------GNARGPAGDGPPL-VLLLGHIDTVPGDIPVRVEDGVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 146 HGRGSCDAKSSVAAQIFAMLELMSEGKVQegdLSLLFVVGEEIDGIGMKT-VANKLNADWevAIFGEPTE-NKLGVGHKG 223
Cdd:PRK04443 85 WGRGSVDAKGPLAAFAAAAARLEALVRAR---VSFVGAVEEEAPSSGGARlVADRERPDA--VIIGEPSGwDGITLGYKG 159
|
170 180
....*....|....*....|....*.
gi 19075180 224 NFRFDVYAHGKACHSGYPQEgfSAIE 249
Cdd:PRK04443 160 RLLVTYVATSESFHSAGPEP--NAAE 183
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
66-279 |
8.42e-20 |
|
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: 90.17 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 66 KSLVEIESLGGNEVNVSDFLKSYLESKGL-TVELQRVSsnptvrdNVYAYLGSqRNTKVVLTSHIDTVN-------PFLP 137
Cdd:cd05649 5 RDLIQIPSESGEEKGVVERIEEEMEKLGFdEVEIDPMG-------NVIGYIGG-GKKKILFDGHIDTVGignidnwKFDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 138 Y--YIEGDKIHGRGSCDAKSSV-----AAQIFAMLELMSEGkvqeGDLSLLFVVGEEI-DGIGMKTVANKLNADWEVAIF 209
Cdd:cd05649 77 YegYETDGKIYGRGTSDQKGGLasmvyAAKIMKDLGLRDFA----YTILVAGTVQEEDcDGVCWQYISKADKIKPDFVVS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075180 210 GEPTENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFL--LRQCVKLMDTDLPKSKLLGPSTINIGTI 279
Cdd:cd05649 153 GEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMadIIQDIRQLNPNFPEAPFLGRGTLTVTDI 224
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
59-391 |
4.49e-19 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 88.07 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 59 DNLISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLT-VELQRVSsnptvrdNVYAYLGSQRnTKVVLTSHIDTVN---- 133
Cdd:PRK13004 15 ADMTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFDkVEIDPMG-------NVLGYIGHGK-KLIAFDAHIDTVGigdi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 134 ---PFLPY--YIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEI-DGIGMKTVANKLNADWEVA 207
Cdd:PRK13004 87 knwDFDPFegEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEEDcDGLCWRYIIEEDKIKPDFV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 208 IFGEPTENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFLLR--QCVKLMDTDLPKSKLLGPSTINIGTIEGGAAA 285
Cdd:PRK13004 167 VITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPilNELEELNPNLKEDPFLGKGTLTVSDIFSTSPS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 286 NILAAEAKAEVFIR---VAEDIET----IRDIAEdlfDTEH-SEIKVIQYSPPQYLDYDIPG------------------ 339
Cdd:PRK13004 247 RCAVPDSCAISIDRrltVGETWESvlaeIRALPA---VKKAnAKVSMYNYDRPSYTGLVYPTecyfptwlypedhefvka 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075180 340 -MDTVVLAYATD------------IPYLSDRKMKIYLFGPGSIREAHGPNEYVTFSQLFEGLNGY 391
Cdd:PRK13004 324 aVEAYKGLFGKApevdkwtfstngVSIAGRAGIPTIGFGPGKEPLAHAPNEYTWKEQLVKAAAMY 388
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
61-282 |
1.05e-17 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 84.30 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 61 LISLHKSLVEIESLGGNE---VNVSDFLKSYLESKGLTVElqRVSSNPTVRDNVYAYLGSQRNTKVVLTSHIDTVnpFL- 136
Cdd:PRK06133 39 YLDTLKELVSIESGSGDAeglKQVAALLAERLKALGAKVE--RAPTPPSAGDMVVATFKGTGKRRIMLIAHMDTV--YLp 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 137 ------PYYIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIGMKTVANKLNADWEVAIFG 210
Cdd:PRK06133 115 gmlakqPFRIDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGSPGSRELIAELAAQHDVVFSC 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075180 211 EPT--ENKLGVGHKGNFRFDVYAHGKACHSGY-PQEGFSAIEFLLRQCVKLMDTDLPKSKLlgpsTINIGTIEGG 282
Cdd:PRK06133 195 EPGraKDALTLATSGIATALLEVKGKASHAGAaPELGRNALYELAHQLLQLRDLGDPAKGT----TLNWTVAKAG 265
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
59-379 |
4.06e-17 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 82.50 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 59 DNLISLHKSLVEIESL---GGNEVNVSDFLKSYLESKGLTVELQRVSSNPT-----VRDNVYA-YLGSQRNTKVVLTSHI 129
Cdd:PRK13013 14 DDLVALTQDLIRIPTLnppGRAYREICEFLAARLAPRGFEVELIRAEGAPGdsetyPRWNLVArRQGARDGDCVHFNSHH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 130 D--------TVNPFlPYYIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIGmkTVANKLN 201
Cdd:PRK13013 94 DvvevghgwTRDPF-GGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFG--GVAYLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 202 ADW------EVAIFGEPT-ENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFL----------LRQCVKLMDTDLP 264
Cdd:PRK13013 171 QGRfspdrvQHVIIPEPLnKDRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMgavlaeieerLFPLLATRRTAMP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 265 -KSKLLGPSTINIGTIEGGAAANILAAEAKAE---------VFIR---VAEDIETIR----DIAEDL------FDTEHSE 321
Cdd:PRK13013 251 vVPEGARQSTLNINSIHGGEPEQDPDYTGLPApcvadrcriVIDRrflIEEDLDEVKaeitALLERLkrarpgFAYEIRD 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075180 322 IKVIQyspPQYLDYDIPGMDTV------VLAYATDI---PYLSDRKM-----KIY---LFGPGSIREAHGPNEYV 379
Cdd:PRK13013 331 LFEVL---PTMTDRDAPVVRSVaaaierVLGRQADYvvsPGTYDQKHidrigKLKnciAYGPGILDLAHQPDEWV 402
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
68-282 |
5.49e-17 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 81.97 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 68 LVEIESLGGNEVNVSDFLKSYLESKGLTVE--------LQR------VSSNPTVRDNVYAYLGSQRNT--KVVLTSHIDT 131
Cdd:PRK06837 29 LVRFPSTRGAEAPCQDFLARAFRERGYEVDrwsidpddLKShpgagpVEIDYSGAPNVVGTYRPAGKTgrSLILQGHIDV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 132 V----------NPFLPYyIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIG-MKTVANKL 200
Cdd:PRK06837 109 VpegpldlwsrPPFDPV-IVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEESTGNGaLSTLQRGY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 201 NADweVAIFGEPTENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIE--FLLRQCVKLMDTDLPKSK--------LLG 270
Cdd:PRK06837 188 RAD--ACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDaaYHLIQALRELEAEWNARKasdphfedVPH 265
|
250
....*....|..
gi 19075180 271 PSTINIGTIEGG 282
Cdd:PRK06837 266 PINFNVGIIKGG 277
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
68-393 |
2.63e-16 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 79.44 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 68 LVEIESLGGNEVNVSDFLKSYleSKGLTVELQRVSSNPTVrdnvyaYLGsqrNTKVVLTSHIDTVNPFLPYYIEGDKIHG 147
Cdd:PRK00466 19 LLSIYTPSGNETNATKFFEKI--SNELNLKLEILPDSNSF------ILG---EGDILLASHVDTVPGYIEPKIEGEVIYG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 148 RGSCDAKSSVAAQIFAMLELMSEG-KVQEGDLSllfvvGEEIDGIGMKTVANKlNADWEVAIFGEPTeNKLG--VGHKGN 224
Cdd:PRK00466 88 RGAVDAKGPLISMIIAAWLLNEKGiKVMVSGLA-----DEESTSIGAKELVSK-GFNFKHIIVGEPS-NGTDivVEYRGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 225 FRFDVYAHGKACHSGYPQEGfsAIEFLLRqcvKLMDTDLPKSKLLGPStINIGTIEGGAAANILAAEAKAEVFIRVAEDI 304
Cdd:PRK00466 161 IQLDIMCEGTPEHSSSAKSN--LIVDISK---KIIEVYKQPENYDKPS-IVPTIIRAGESYNVTPAKLYLHFDVRYAINN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 305 ETiRDIAEDLFDTEHS-EIKVIQYSPPQYLDYDIPGMDTVVLAYAT--------------DIPYLSDRKMKIYLFGPGSI 369
Cdd:PRK00466 235 KR-DDLISEIKDKFQEcGLKIVDETPPVKVSINNPVVKALMRALLKqnikprlvrkagtsDMNILQKITTSIATYGPGNS 313
|
330 340
....*....|....*....|....
gi 19075180 370 REAHGPNEYVTFSQLFEGLNGYKR 393
Cdd:PRK00466 314 MLEHTNQEKITLDEIYIAVKTYML 337
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
59-247 |
4.84e-16 |
|
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: 79.04 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 59 DNLISLHKSLVEIESL-----GGNEVNVSDFLKSYLESKGLTvELQRVSS-NPTV--RDNVYAYLGSQRNTKVVLTSHID 130
Cdd:cd05650 1 EEIIELERDLIRIPAVnpesgGEGEKEKADYLEKKLREYGFY-TLERYDApDERGiiRPNIVAKIPGGNDKTLWIISHLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 131 TV----------NPFLPYyIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEiDG--IGMKTVAN 198
Cdd:cd05650 80 TVppgdlslwetDPWEPV-VKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEE-DGseYGIQYLLN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19075180 199 KLN--ADWEVAI---FGEPTENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSA 247
Cdd:cd05650 158 KFDlfKKDDLIIvpdFGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINA 211
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
83-282 |
9.07e-16 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 78.20 E-value: 9.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 83 DFLKSYLESKGLTVElqRVSSNPTvrDNVYAYLGSQRNTkVVLTSHIDTV----------NPFLPYyIEGDKIHGRGSCD 152
Cdd:PRK13009 26 DLLAERLEALGFTCE--RMDFGDV--KNLWARRGTEGPH-LCFAGHTDVVppgdleawtsPPFEPT-IRDGMLYGRGAAD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 153 AKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGI-GMKTVANKLNA-----DWevAIFGEPT-ENKLG----VGH 221
Cdd:PRK13009 100 MKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAInGTVKVLEWLKArgekiDY--CIVGEPTsTERLGdvikNGR 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19075180 222 KGNFRFDVYAHGKACHSGYPQEGFSAIEFLLRQCVKLMDTDLPK-SKLLGPSTINIGTIEGG 282
Cdd:PRK13009 178 RGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEgNEFFPPTSLQITNIDAG 239
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
62-396 |
2.08e-15 |
|
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: 76.75 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 62 ISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLtVELQRVSsnptvRDNVYA-YLGSQRNTKVVLTSHIDTV----NPFL 136
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGL-GDVERDG-----RGNVVGrLRGTGGGPALLFSAHLDTVfpgdTPAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 137 PYYiEGDKIHGRGSCDAKSSVAAqIFAMLELMSE-GKVQEGDLSLLFVVGEE--IDGIGMKTVANKLNADWEVAIFGEPT 213
Cdd:cd03896 75 VRH-EGGRIYGPGIGDNKGSLAC-LLAMARAMKEaGAALKGDVVFAANVGEEglGDLRGARYLLSAHGARLDYFVVAEGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 214 ENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFLLRQCVKLMDTDLPKSkllgP-STINIGTIEGGAAANILAAEA 292
Cdd:cd03896 153 DGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAPYV----PkTTFAAIRGGGGTSVNRIANLC 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 293 KAEVFIRVAEDIETI----------RDIAEDLFDTeHSEIKVIQYSPpqylDYDIPGMDTVVLA---------------- 346
Cdd:cd03896 229 SMYLDIRSNPDAELAdvqreveavvSKLAAKHLRV-KARVKPVGDRP----GGEAQGTEPLVNAavaahrevggdprpgs 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 19075180 347 YATD-IPYLSdRKMKIYLFGPGSIREAHGPNEYVTFSQLFEGLNGYKRMVM 396
Cdd:cd03896 304 SSTDaNPANS-LGIPAVTYGLGRGGNAHRGDEYVLKDDMLKGAKAYLMLAA 353
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
219-318 |
2.74e-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: 71.22 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 219 VGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFLLRQCVKLMDTDLPKSKLLGPSTINIGTIEGGAAANILAAEAKAEVFI 298
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGFDFPRTTLNITGIEGGTATNVIPAEAEAKFDI 80
|
90 100
....*....|....*....|..
gi 19075180 299 RVA--EDIETIRDIAEDLFDTE 318
Cdd:pfam07687 81 RLLpgEDLEELLEEIEAILEKE 102
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
59-247 |
7.64e-15 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 75.66 E-value: 7.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 59 DNLISLHKSLVEIESL----GG-NEVNVSDFLKSYLESKGLT-VEL-----QRVSSNptVRDNVYAYL-GSQRNTKVVLT 126
Cdd:PRK13983 5 DEMIELLSELIAIPAVnpdfGGeGEKEKAEYLESLLKEYGFDeVERydapdPRVIEG--VRPNIVAKIpGGDGKRTLWII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 127 SHIDTV----------NPFLPYyIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEiDG--IGMK 194
Cdd:PRK13983 83 SHMDVVppgdlslwetDPFKPV-VKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEE-TGskYGIQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075180 195 TVANKLN-----ADW-EVAIFGEPTENKLGVGHKGN--FRFDVyaHGKACHSGYPQEGFSA 247
Cdd:PRK13983 161 YLLKKHPelfkkDDLiLVPDAGNPDGSFIEIAEKSIlwLKFTV--KGKQCHASTPENGINA 219
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
63-395 |
2.91e-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: 2.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 63 SLHKSLVEIES-----LGGNEVNVSDFLKSYLESKGLTVELQRVSSNPTvRDNVYAYLGSQRNTK--VVLTSHID----- 130
Cdd:cd05675 2 DLLQELIRIDTtnsgdGTGSETRAAEVLAARLAEAGIQTEIFVVESHPG-RANLVARIGGTDPSAgpLLLLGHIDvvpad 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 131 ----TVNPFlPYYIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGI-GMK-TVAN--KLNA 202
Cdd:cd05675 81 asdwSVDPF-SGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGEnGAKwLVDNhpELFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 203 DW-----EVAIFGEPTENK-----LGVGHKGNFRFDVYAHGKACHSGYPQEgFSAI----EFLLR--------------- 253
Cdd:cd05675 160 GAtfalnEGGGGSLPVGKGrrlypIQVAEKGIAWMKLTVRGRAGHGSRPTD-DNAItrlaEALRRlgahnfpvrltdeta 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 254 -----------QCVKLMDTDLPKS----KLLGPS----------TINIGTIEGGAAANILAAEAKAEVFIRV--AEDIET 306
Cdd:cd05675 239 yfaqmaelaggEGGALMLTAVPVLdpalAKLGPSapllnamlrnTASPTMLDAGYATNVLPGRATAEVDCRIlpGQSEEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 307 IRDIAEDLFDTEHSEIKVIQYSPPQYLDYDIPGMDT---VVLAY-------------ATDIPYLSDRKMKIYLFGP---- 366
Cdd:cd05675 319 VLDTLDKLLGDPDVSVEAVHLEPATESPLDSPLVDAmeaAVQAVdpgapvvpymspgGTDAKYFRRLGIPGYGFAPlflp 398
|
410 420 430
....*....|....*....|....*....|..
gi 19075180 367 ---GSIREAHGPNEYVTFSQLFEGLNGYKRMV 395
Cdd:cd05675 399 pelDYTGLFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
59-386 |
6.20e-13 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 69.68 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 59 DNLISLHKSLVEIESL---GGNEVNVSDFLKSYLESKGLTVELQRVSSNPtvrDNVYAYLGSQRNTK---VVLTSHID-- 130
Cdd:PRK08596 13 DELLELLKTLVRFETPappARNTNEAQEFIAEFLRKLGFSVDKWDVYPND---PNVVGVKKGTESDAyksLIINGHMDva 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 131 --------TVNPFLPYyIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIGMKtVANKLNA 202
Cdd:PRK08596 90 evsadeawETNPFEPT-IKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEVGEAGTL-QCCERGY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 203 DWEVAIFGEPTENK-LGVG---------------HKGNFRfdvyahgKACHSGYPQEGFSAIEFLLRQCVKLMDTD---- 262
Cdd:PRK08596 168 DADFAVVVDTSDLHmQGQGgvitgwitvkspqtfHDGTRR-------QMIHAGGGLFGASAIEKMMKIIQSLQELErhwa 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 263 LPKSK---LLGPSTINIGTIEGGaaanilaaeaKAEVFI-------------------RVAEDIET-------------- 306
Cdd:PRK08596 241 VMKSYpgfPPGTNTINPAVIEGG----------RHAAFIadecrlwitvhfypnetyeQVIKEIEEyigkvaaadpwlre 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 307 ------------IRDIAEdLF-----DTEHSEIKVIQYSPPQYLDYDIP-GMDTVVlayaTDIPYLSDRKMKIYLFGPGS 368
Cdd:PRK08596 311 nppqfkwggesmIEDRGE-IFpsleiDSEHPAVKTLSSAHESVLSKNAIlDMSTTV----TDGGWFAEFGIPAVIYGPGT 385
|
410
....*....|....*...
gi 19075180 369 IREAHGPNEYVTFSQLFE 386
Cdd:PRK08596 386 LEEAHSVNEKVEIEQLIE 403
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
61-384 |
1.39e-12 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 68.31 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 61 LISLHKSLVEIESLG--------GNEvNVSDFLKSYLESKGLTVELQRVssnPTVRD--NVYAYLGSQRNtKVVLTSHID 130
Cdd:PRK05111 7 FIEMYRALIATPSISatdpaldqSNR-AVIDLLAGWFEDLGFNVEIQPV---PGTRGkfNLLASLGSGEG-GLLLAGHTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 131 TV---------NPFLpyYIEGD-KIHGRGSCDAKSSVAAQIFAMLELmsEGKVQEGDLSLLFVVGEEIDGIGMKTVANKL 200
Cdd:PRK05111 82 TVpfdegrwtrDPFT--LTEHDgKLYGLGTADMKGFFAFILEALRDI--DLTKLKKPLYILATADEETSMAGARAFAEAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 201 NADWEVAIFGEPTENKLGVGHKGNFRFDVYAHGKACHSGYPQEGFSAIEFL---LRQCVKLMDT----------DLPKsk 267
Cdd:PRK05111 158 AIRPDCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMhdvIGELLQLRDElqeryhnpafTVPY-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 268 llgPsTINIGTIEGGAAANILAAEAKAEVFIR------VAEDIETIRDIAEDLFDTEHSEIKVIQYSPPqyldydIPGM- 340
Cdd:PRK05111 236 ---P-TLNLGHIHGGDAPNRICGCCELHFDIRplpgmtLEDLRGLLREALAPVSERWPGRITVAPLHPP------IPGYe 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075180 341 -----------------DTVVLAYATDIPYLSDRKMKIYLFGPGSIREAHGPNEYVTFSQL 384
Cdd:PRK05111 306 cpadhqlvrvvekllghKAEVVNYCTEAPFIQQLGCPTLVLGPGSIEQAHQPDEYLELSFI 366
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
110-395 |
1.42e-12 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 68.30 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 110 NVYAYLGSqrnTKVVLTSHIDTVnPFLPYY--------IEGDKIHGRGSCDAKSSVAAqifamleLMSEGKVQEGDLSLL 181
Cdd:PRK08737 56 SLYAVRGT---PKYLFNVHLDTV-PDSPHWsadphvmrRTDDRVIGLGVCDIKGAAAA-------LLAAANAGDGDAAFL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 182 FVVGEEI-DGIGMKTVANKlNADWEVAIFGEPTENKLGVGHKGNFRFDVYAHGKACHSGYPQE-GFSAIEFLLRQCVKLM 259
Cdd:PRK08737 125 FSSDEEAnDPRCVAAFLAR-GIPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKQDpSASALHQAMRWGGQAL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 260 D--TDLPKSKLLGPSTI--NIGTIEGGAAANILAAEAKAEVFIRV--AEDIE----TIRDIAEDlfDTEHSEIKviqYSP 329
Cdd:PRK08737 204 DhvESLAHARFGGLTGLrfNIGRVEGGIKANMIAPAAELRFGFRPlpSMDVDgllaTFAGFAEP--AAATFEET---FRG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 330 PQYLDYDIP-----GMDTVVLAYATDIP------------YLSDRKMKIYLFGPGSIREAHGPNEYVTFSQLFEGLNGYK 392
Cdd:PRK08737 279 PSLPSGDIAraeerRLAARDVADALDLPignavdfwteasLFSAAGYTALVYGPGDIAQAHTADEFVTLDQLQRYAESVH 358
|
...
gi 19075180 393 RMV 395
Cdd:PRK08737 359 RII 361
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
59-247 |
2.04e-11 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 65.44 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 59 DNLISLHKSLVEIESLGGN--EVNVSDFLKSYLESKGLTVE-----LQRVSSNPTVRDNVYAYLGSQRNTK--VVLTSHI 129
Cdd:cd05654 1 ERLEQLLKSLVSWPSVTGTegERSFADFLKEILKELPYFKEnpshvWQLLPPDDLGRRNVTALVKGKKPSKrtIILISHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 130 DTVN----------PFLP-----YYIE---------------GDKIHGRGSCDAKSSVAAQIfAMLELMSEGKVQEGDLS 179
Cdd:cd05654 81 DTVGiedygelkdiAFDPdeltkAFSEyveeldeevredllsGEWLFGRGTMDMKSGLAVHL-ALLEQASEDEDFDGNLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 180 LLFVVGEEIDGIGMKTVANKLNA-------DWEVAIFGEPTENKlgvgHKGNFRFDVYA------------HGKACHSGY 240
Cdd:cd05654 160 LMAVPDEEVNSRGMRAAVPALLElkkkhdlEYKLAINSEPIFPQ----YDGDQTRYIYTgsigkilpgflcYGKETHVGE 235
|
....*..
gi 19075180 241 PQEGFSA 247
Cdd:cd05654 236 PFAGINA 242
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
68-249 |
2.16e-09 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. 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: 349934 [Multi-domain] Cd Length: 423 Bit Score: 59.01 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 68 LVEIESLGGNevNVSDFLKSYLESKGLTVELQRVSSNPTVRDNVYAYLGSQRNTKV-VLTSHIDTV--NP----FLPYY- 139
Cdd:cd08012 27 LVPKEDNAGR--HVLEALTPYSTENGGPLVIDHVSYVKGRGNIIVEYPGTVDGKTVsFVGSHMDVVtaNPetweFDPFSl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 140 -IEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEE---IDGIGMKTVA-----NKLNAD---WEVA 207
Cdd:cd08012 105 sIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVVAVFIANEEnseIPGVGVDALVksgllDNLKSGplyWVDS 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19075180 208 IFGEPTenklgVGHKGNFRFDVYAHGKACHSGYPQEGFSAIE 249
Cdd:cd08012 185 ADSQPC-----IGTGGMVTWKLTATGKLFHSGLPHKAINALE 221
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
60-200 |
6.62e-09 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 57.48 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 60 NLISLHKSLVEIESL---GGNEVNVSD---FLKSYLESKGLTVELQRvssnptvRDNVYAYLG--SQRNTKVVLTSHIDT 131
Cdd:PRK08554 2 DVLELLSSLVSFETVndpSKGIKPSKEcpkFIKDTLESWGIESELIE-------KDGYYAVYGeiGEGKPKLLFMAHFDV 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075180 132 V---------NPFLPYyIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGkvQEGDLSLLFVVGEEIDGIGMKTVANKL 200
Cdd:PRK08554 75 VpvnpeewntEPFKLT-VKGDKAYGRGSADDKGNVASVMLALKELSKEP--LNGKVIFAFTGDEEIGGAMAMHIAEKL 149
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
110-192 |
6.69e-09 |
|
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 55.52 E-value: 6.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 110 NVYAYLGSQRNTKVVLT-SHIDTV---------NPFLPYYIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLS 179
Cdd:cd18669 1 NVIARYGGGGGGKRVLLgAHIDVVpagegdprdPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90
....*....|...
gi 19075180 180 LLFVVGEEIDGIG 192
Cdd:cd18669 81 VAFTPDEEVGSGA 93
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
84-207 |
1.53e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 56.30 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 84 FLKSYLESKGLTVELQRVSSNPTVrdnvYAYLGSQRNTKVVLTSHIDT----------VNPFLPYyIEGDKIHGRGSCDA 153
Cdd:PRK06446 30 YLKDTMEKLGIKANIERTKGHPVV----YGEINVGAKKTLLIYNHYDVqpvdplsewkRDPFSAT-IENGRIYARGASDN 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075180 154 KSSVAAQIFAMLELMSEGKvqeGDLSLLFVV--GEEIDGIGM----KTVANKLNAD---WEVA 207
Cdd:PRK06446 105 KGTLMARLFAIKHLIDKHK---LNVNVKFLYegEEEIGSPNLedfiEKNKNKLKADsviMEGA 164
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
81-240 |
2.21e-08 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases 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. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 55.81 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 81 VSDFLKSYLESKGLTVELQRVSSNPTVrdnvYAYLGSQRNTKVVLTSHIDTV----------NPFLPYyIEGDKIHGRGS 150
Cdd:cd05681 24 TADFLKEFLRRLGAEVEIFETDGNPIV----YAEFNSGDAKTLLFYNHYDVQpaeplelwtsDPFELT-IRNGKLYARGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 151 CDAKSSVAAQIFAMLELMSegkvQEGDL----SLLFVVGEEIDGIGM----KTVANKLNAD---WEVAIFGEPTENKLGV 219
Cdd:cd05681 99 ADDKGELMARLAALRALLQ----HLGELpvniKFLVEGEEEVGSPNLekfvAEHADLLKADgciWEGGGKNPKGRPQISL 174
|
170 180
....*....|....*....|...
gi 19075180 220 GHKGNFRFDVYAHG--KACHSGY 240
Cdd:cd05681 175 GVKGIVYVELRVKTadFDLHSSY 197
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
110-199 |
6.16e-08 |
|
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: 52.43 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 110 NVYAYLGSQRNTKVVLT-SHIDTV---------NPFLPYYIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLS 179
Cdd:cd03873 1 NLIARLGGGEGGKSVALgAHLDVVpagegdnrdPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
|
90 100
....*....|....*....|
gi 19075180 180 LLFVVGEEIDGIGMKTVANK 199
Cdd:cd03873 81 VAFTADEEVGSGGGKGLLSK 100
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
123-282 |
1.68e-07 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 53.04 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 123 VVLTSHIDTV----NPFLP-YYIEGDKIHGRGSCDAKSSVAAQIFAMLELmsEGKVQEGDLSLLFVVG--EEIDGIGMKT 195
Cdd:PRK07338 95 VLLTGHMDTVfpadHPFQTlSWLDDGTLNGPGVADMKGGIVVMLAALLAF--ERSPLADKLGYDVLINpdEEIGSPASAP 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 196 VANKLNADWEVAIFGEPT--ENKLGVGHKGNFRFDVYAHGKACHSGY-PQEGFSAIEFLLRQCVKLMDTDLPKSKLlgps 272
Cdd:PRK07338 173 LLAELARGKHAALTYEPAlpDGTLAGARKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAELALALHALNGQRDGV---- 248
|
170
....*....|
gi 19075180 273 TINIGTIEGG 282
Cdd:PRK07338 249 TVNVAKIDGG 258
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
48-240 |
2.32e-07 |
|
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: 52.33 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 48 LISHQSLLPAGDNLISLHKSLVEIESLggnevnvsdflksyLESKGLTVELQRVSSNPTVrdnVYAYLGSQRNTKVVLT- 126
Cdd:cd03893 7 LVAIPSVSAQPDRREELRRAAEWLADL--------------LRRLGFTVEIVDTSNGAPV---VFAEFPGAPGAPTVLLy 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 127 SHIDTV----------NPFLPYyIEGDKIHGRGSCDAKSSVAAQIFAMLELMSegkvQEGDLSLLFVV----GEEIDGIG 192
Cdd:cd03893 70 GHYDVQpagdedgwdsDPFELT-ERDGRLYGRGAADDKGPILAHLAALRALMQ----QGGDLPVNVKFiiegEEESGSPS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 193 MKTVANK----LNADWEV------AIFGEPTenkLGVGHKG--NFRFDVYAHGKACHSGY 240
Cdd:cd03893 145 LDQLVEAhrdlLAADAIVisdstwVGQEQPT---LTYGLRGnaNFDVEVKGLDHDLHSGL 201
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
123-282 |
3.21e-07 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 52.09 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 123 VVLTSHIDTVNPF-----LPYYIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGIGMKTVA 197
Cdd:PRK07473 78 ILIAGHMDTVHPVgtlekLPWRREGNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFTPDEEVGTPSTRDLI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 198 NKLNADWEVAIFGEPTENKLGV--GHKGNFRFDVYAHGKACHSG-YPQEGFSAIEFLLRQCVKL--MDTDlpkskllgPS 272
Cdd:PRK07473 158 EAEAARNKYVLVPEPGRPDNGVvtGRYAIARFNLEATGRPSHAGaTLSEGRSAIREMARQILAIdaMTTE--------DC 229
|
170
....*....|
gi 19075180 273 TINIGTIEGG 282
Cdd:PRK07473 230 TFSVGIVHGG 239
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
63-197 |
4.88e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 48.46 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 63 SLHKSLVEIESL--GGNEVNVSDFLKSYLESKGLTV-ELQRVSSNPTVRDNVYAYLGSQRNTKVVLTSHIDTV------- 132
Cdd:PRK09133 41 DLYKELIEINTTasTGSTTPAAEAMAARLKAAGFADaDIEVTGPYPRKGNLVARLRGTDPKKPILLLAHMDVVeakredw 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075180 133 --NPFLPYyIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEidGIGMKTVA 197
Cdd:PRK09133 121 trDPFKLV-EENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEE--GTPMNGVA 184
|
|
| FrvX |
COG1363 |
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ... |
59-132 |
9.47e-06 |
|
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];
Pssm-ID: 440974 [Multi-domain] Cd Length: 353 Bit Score: 47.04 E-value: 9.47e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19075180 59 DNLISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVELqrvssnpTVRDNVYAYL-GSQRNTKVVLTSHIDTV 132
Cdd:COG1363 2 DYLLELLKELTEAPGPSGFEDEVREYIKEELEPLGDEVET-------DRLGNLIATKkGKGDGPKVMLAAHMDEI 69
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
83-282 |
1.54e-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: 46.50 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 83 DFLKSYLESKGLTVE-LQRVSSNPTVrdnVYAYLGSQRNTK-VVLTSHIDTV---------NPFLPYYIEGDKIHGRGSC 151
Cdd:cd05646 28 EFLKRQADELGLPVRvIEVVPGKPVV---VLTWEGSNPELPsILLNSHTDVVpvfeekwthDPFSAHKDEDGNIYARGAQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 152 DAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGI-GMKTVA-----NKLNA----DWEVAifgEPTEN-KLGVG 220
Cdd:cd05646 105 DMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGHdGMEKFVkteefKKLNVgfalDEGLA---SPTEEyRVFYG 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19075180 221 HKGNFRFDVYAHGKACHSGYPQEGfSAIEFLLRQCVKLMD---------TDLPKSKLLGPSTINIGTIEGG 282
Cdd:cd05646 182 ERSPWWVVITAPGTPGHGSKLLEN-TAGEKLRKVIESIMEfresqkqrlKSNPNLTLGDVTTVNLTMLKGG 251
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
111-241 |
2.85e-05 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 46.09 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 111 VYAYLGSQRNTK-VVLTSHIDTV--NP-------FLPY--YIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDL 178
Cdd:cd05674 59 LYTWEGSDPSLKpLLLMAHQDVVpvNPetedqwtHPPFsgHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 179 SLLFVVGEEIDG-IGMKTVANKLNADWEV----AIF--GEPTENKL---------GVGHKG--NFRFDVYAHGKacHSGY 240
Cdd:cd05674 139 ILAFGHDEEVGGeRGAGAIAELLLERYGVdglaAILdeGGAVLEGVflgvpfalpGVAEKGymDVEITVHTPGG--HSSV 216
|
.
gi 19075180 241 P 241
Cdd:cd05674 217 P 217
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
123-272 |
1.03e-04 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 44.16 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 123 VVLTSHID------------TVNPFlPYYIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDG 190
Cdd:PRK08262 114 IVLMAHQDvvpvapgtegdwTHPPF-SGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVGG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 191 IGMKTVANKL-----NADWEV--------AIFGEPTENK--LGVGHKGNFRFDVYAHGKACHSGYPQEGfSAIEFLLRQC 255
Cdd:PRK08262 193 LGARAIAELLkergvRLAFVLdeggaiteGVLPGVKKPValIGVAEKGYATLELTARATGGHSSMPPRQ-TAIGRLARAL 271
|
170
....*....|....*..
gi 19075180 256 VKLMDTDLPkSKLLGPS 272
Cdd:PRK08262 272 TRLEDNPLP-MRLRGPV 287
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
74-282 |
1.41e-04 |
|
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: 43.74 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 74 LGGNEVNVSDFLKSYLESKGLTVElqrvssnpTVRDN--VYAYLGSQRNTKVV-LTSHID----TVNPFLPYYIEGDKI- 145
Cdd:cd03886 14 LSFEEFRTAARIAEELRELGLEVR--------TGVGGtgVVATLKGGGPGPTVaLRADMDalpiQEETGLPFASKHEGVm 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 146 HgrgSC--DAKSSV---AAQIFAMLELMSEGKVQegdlsLLFVVGEEIDGIGMKTVANKLNADWEV-AIFG---EPTenk 216
Cdd:cd03886 86 H---ACghDGHTAMllgAAKLLAERRDPLKGTVR-----FIFQPAEEGPGGAKAMIEEGVLENPGVdAAFGlhvWPG--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 217 LGVGH----KGNF-----RFDVYAHGKACHSGYPQEGFSAI----EFLLR-QCVKLMDTDLpksklLGPSTINIGTIEGG 282
Cdd:cd03886 155 LPVGTvgvrSGALmasadEFEITVKGKGGHGASPHLGVDPIvaaaQIVLAlQTVVSRELDP-----LEPAVVTVGKFHAG 229
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
83-305 |
2.50e-04 |
|
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: 42.86 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 83 DFLKSYLESKGLTVE-LQRVSSNPTVrdnVYAYLGSQRN-TKVVLTSHIDTV---------NPFLPYYIEGDKIHGRGSC 151
Cdd:TIGR01880 35 DFLIKQADELGLARKtIEFVPGKPVV---VLTWPGSNPElPSILLNSHTDVVpvfrehwthPPFSAFKDEDGNIYARGAQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 152 DAKSSVAAQIFAMLELMSEGKVQEGDLSLLFVVGEEIDGI-GMKTVA-----NKLNA----DWEVAifgEPTEN-KLGVG 220
Cdd:TIGR01880 112 DMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHdGMEKFAktdefKALNLgfalDEGLA---SPDDVyRVFYA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 221 HKGNFRFDVYAHGKACHSGYPQEGfSAIEFLLRQCVKLMDTDLPKSKLL--GP-------STINIGTIEGGAAANILAAE 291
Cdd:TIGR01880 189 ERVPWWVVVTAPGNPGHGSKLMEN-TAMEKLEKSVESIRRFRESQFQLLqsNPdlaigdvTSVNLTKLKGGVQSNVIPSE 267
|
250
....*....|....
gi 19075180 292 AKAEVFIRVAEDIE 305
Cdd:TIGR01880 268 AEAGFDIRLAPSVD 281
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
104-346 |
2.76e-04 |
|
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: 42.75 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 104 NPTVRDNVYAYLGSQRNTKVVLTSHIDTVNPFLPY--YIEGDKIHGRGScDAKSSVAaQIFAMLELMSEGKVQEGDLSLL 181
Cdd:cd05645 88 NPQIVENYRGGDIALGIGDEVLSPVMFPVLHQLLGqtLITTDGKTLLGA-DDKAGLA-EIFTALAVLKEKNIPHGDIEVA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 182 FVVGEEIdGIGMKTV-ANKLNADWEVAIFGEPTeNKLGVGHKGNFRFDVYAHGKACHSGY-PQEGFSAIEFLLRQCVKLM 259
Cdd:cd05645 166 FTPDEEV-GKGAKHFdVEAFTAKWAYTVDGGGV-GELEFENFNAASVNIKIVGNNVHPGTaKGVGVNALSLAARIHAEVP 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 260 DTDLPKSKLLGPSTINIGTIEGGAAANILAAEAKA----EVFIRVAEDIETIRDIAEDLFDTEHSEIkVIQYSPPQYLDY 335
Cdd:cd05645 244 ADESPEGTEGYEGFYHLASFKGTVDRAQIHYIIRDfdrkQFEARKRK*KEIAKKVGKGLHPDCYIEL-VIEDSYYNFREK 322
|
250
....*....|.
gi 19075180 336 DIPGMDTVVLA 346
Cdd:cd05645 323 VVEHPHILDIA 333
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
59-399 |
3.35e-04 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 42.62 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 59 DNLISLHKSLVEIES----------LGGNEVNVSDFLKSYLESKGLTVElqrvssnptVRDNVYAY--LGsQRNTKVVLT 126
Cdd:cd03888 8 DEILEDLKELVAIPSvrdeategapFGEGPRKALDKFLDLAKRLGFKTK---------NIDNYAGYaeYG-EGEEVLGIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 127 SHIDTV--------NPFLPYyIEGDKIHGRGSCDAKSSVAAQIFAMLELMSEG-----KVQ------------------- 174
Cdd:cd03888 78 GHLDVVpagegwttDPFKPV-IKDGKLYGRGTIDDKGPTIAALYALKILKDLGlplkkKIRlifgtdeetgwkciehyfe 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 175 -EGDLSLLF-------VVGEEIDGIGMKTVANKLNADWE----------------------VAIFGEPTENKLGVGHKGN 224
Cdd:cd03888 157 hEEYPDFGFtpdaefpVINGEKGIVTVDLTFKIDDDKGYrlisikggeatnmvpdkaeaviPGKDKEELALSAATDLKGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 225 FRFD-----VYAHGKACHSGYPQEGFSAIEFLL------------RQCVKLMDTDLP------------KSKLLGPSTIN 275
Cdd:cd03888 237 IEIDdggveLTVTGKSAHASAPEKGVNAITLLAkflaelnkdgndKDFIKFLAKNLHedyngkklginfEDEVMGELTLN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 276 IGTIEggaaanILAAEAKAEVFIRVAE--DIETIRDIAEDLFDTEHSEIKVIQYSPPQYLDYDIP-------------GM 340
Cdd:cd03888 317 PGIIT------LDDGKLELGLNVRYPVgtSAEDIIKQIEEALEKYGVEVEGHKHQKPLYVPKDSPlvktllkvyeeqtGK 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19075180 341 DTVVLA-----YATDIPylsdrkmKIYLFG---PGSIREAHGPNEYVTFSQLFEGLNGYKRMvMYNL 399
Cdd:cd03888 391 EGEPVAigggtYARELP-------NGVAFGpefPGQKDTMHQANEFIPIDDLIKALAIYAEA-IYEL 449
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
76-204 |
3.51e-03 |
|
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: 39.43 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075180 76 GNEVNVSDFLKSYLESKGLTVELQRVssnptvrDNVY----AYLGSQRNTKVVLTSHIDTV------------NPFLPYY 139
Cdd:cd03890 19 GNEKQISDFLVKFAKKLGLEVIQDEV-------GNVIirkpATPGYENAPPVILQGHMDMVceknadsehdfeKDPIKLR 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19075180 140 IEGDKIHGRGS---CDAKSSVAaqifAMLELMSEGKVQEGDLSLLFVVGEEidgIGMkTVANKLNADW 204
Cdd:cd03890 92 IDGDWLKATGTtlgADNGIGVA----YALAILEDKDIEHPPLEVLFTVDEE---TGM-TGALGLDPSL 151
|
|
| M42_glucanase_like |
cd05657 |
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ... |
60-131 |
3.65e-03 |
|
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: 39.18 E-value: 3.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19075180 60 NLISLHKSLVEIESLGGNEVNVSDFLKSYLESKGLTVELQRvssnptvRDNVYAYL-GSQRNTKVVLTSHIDT 131
Cdd:cd05657 1 YLLDLLKELLAIPSPTGYTDEAVRYLKKELEGLGVETELTN-------KGALIATIpGKDSRKARALSAHVDT 66
|
|
| |
