|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
1-378 |
0e+00 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 711.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 1 MQLPGFIDIYGGLISTSSISSSDPSWDEGNSEVIAKLATWFEDLGFETQVVEVE--KGKHNLIAKMGKGEGGLLLAGHTD 78
Cdd:PRK05111 2 MKLPSFIEMYRALIATPSISATDPALDQSNRAVIDLLAGWFEDLGFNVEIQPVPgtRGKFNLLASLGSGEGGLLLAGHTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 79 TVPFDEGRWNYDPHALTEANDRFYGLGTADMKGFFAFILEAVKKTDWSQQTKPLYVLATCDEETTMLGARHFTEDAPFKP 158
Cdd:PRK05111 82 TVPFDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAEATAIRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 159 DYCIIGEPTSLVPIRAHKGHVANAIRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIKAYHHPGFDIPNPTLNLG 238
Cdd:PRK05111 162 DCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQERYHNPAFTVPYPTLNLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 239 HIHGGDSANRICGCCELHYDVRPLPGISIDGLDNMLREALKEVEAKWPGRIEIKPLHEPIPGYECDHEHPFIEGMERICE 318
Cdd:PRK05111 242 HIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSERWPGRITVAPLHPPIPGYECPADHQLVRVVEKLLG 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549778073 319 QPSETVNYCTEAPFLQQL-CPTLVLGPGSIDQAHQPDEFLAFEFIDPTIKILDRAIHQYCF 378
Cdd:PRK05111 322 HKAEVVNYCTEAPFIQQLgCPTLVLGPGSIEQAHQPDEYLELSFIKPTRELLRQLIHHFCL 382
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
27-374 |
7.40e-166 |
|
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: 468.23 E-value: 7.40e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 27 DEGNSEVIAKLATWFEDLGFETQVVEV-EKGKHNLIAKMG-KGEGGLLLAGHTDTVPFDEGRWNYDPHALTEANDRFYGL 104
Cdd:cd03894 14 RNSNLALIEYVADYLAALGVKSRRVPVpEGGKANLLATLGpGGEGGLLLSGHTDVVPVDGQKWSSDPFTLTERDGRLYGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 105 GTADMKGFFAFILEAVKKTDWSQQTKPLYVLATCDEETTMLGARHFTEDA---PFKPDYCIIGEPTSLVPIRAHKGHVAN 181
Cdd:cd03894 94 GTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALaarGGRPDAAIVGEPTSLQPVVAHKGIASY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 182 AIRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIKAYHHPGFDIPNPTLNLGHIHGGDSANRICGCCELHYDVRP 261
Cdd:cd03894 174 RIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPFDPPYPTLNVGLIHGGNAVNIVPAECEFEFEFRP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 262 LPGISIDGLDNMLREALKEVEAKWPGRIEIKPLHEPiPGYECDHEHPFIEGMERICEQ-PSETVNYCTEAPFLQQL-CPT 339
Cdd:cd03894 254 LPGEDPEAIDARLRDYAEALLEFPEAGIEVEPLFEV-PGLETDEDAPLVRLAAALAGDnKVRTVAYGTEAGLFQRAgIPT 332
|
330 340 350
....*....|....*....|....*....|....*
gi 549778073 340 LVLGPGSIDQAHQPDEFLAFEFIDPTIKILDRAIH 374
Cdd:cd03894 333 VVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
30-373 |
2.70e-146 |
|
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130947 [Multi-domain] Cd Length: 364 Bit Score: 418.46 E-value: 2.70e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 30 NSEVIAKLATWFEDLGFETQVVEVEKG--KHNLIAKMG-KGEGGLLLAGHTDTVPFDEGRWNYDPHALTEANDRFYGLGT 106
Cdd:TIGR01892 17 NVDLIDWAQAYLEALGFSVEVQPFPDGaeKSNLVAVIGpSGAGGLALSGHTDVVPYDDAAWTRDPFRLTEKDGRLYGRGT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 107 ADMKGFFAFILEAVKKTDWSQQTKPLYVLATCDEETTMLGARHFTEDAPFKPDYCIIGEPTSLVPIRAHKGHVANAIRVT 186
Cdd:TIGR01892 97 CDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIEAGAGRPRHAIIGEPTRLIPVRAHKGYASAEVTVR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 187 GHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIKAYHHPGFDIPNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGIS 266
Cdd:TIGR01892 177 GRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDLDEGFTPPYTTLNIGVIQGGKAVNIIPGACEFVFEWRPIPGMD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 267 IDGLDNMLREALKEVEAKWPGRIEIKPLHEPIPGYECDHEHPFIEGMERICEQPSETVNYCTEAPFLQQL-CPTLVLGPG 345
Cdd:TIGR01892 257 PEELLQLLETIAQALVRDEPGFEVQIEVVSTDPGVNTEPDAELVAFLEELSGNAPEVVSYGTEAPQFQELgAEAVVCGPG 336
|
330 340
....*....|....*....|....*...
gi 549778073 346 SIDQAHQPDEFLAFEFIDPTIKILDRAI 373
Cdd:TIGR01892 337 DIRQAHQPDEYVEIEDLVRCRAVLARLV 364
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
27-377 |
2.15e-103 |
|
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: 310.28 E-value: 2.15e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 27 DEGNSEVIAKLATWFEDLGFETQVVEVEKGKHNLIAKM--GKGEGGLLLAGHTDTVPFDEG-RWNYDPHALTEANDRFYG 103
Cdd:COG0624 28 SGEEAAAAELLAELLEALGFEVERLEVPPGRPNLVARRpgDGGGPTLLLYGHLDVVPPGDLeLWTSDPFEPTIEDGRLYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 104 LGTADMKGFFAFILEAVK--KTDWSQQTKPLYVLATCDEETTMLGARHFTEDAP--FKPDYCIIGEPTS-LVPIRAHKGH 178
Cdd:COG0624 108 RGAADMKGGLAAMLAALRalLAAGLRLPGNVTLLFTGDEEVGSPGARALVEELAegLKADAAIVGEPTGvPTIVTGHKGS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 179 VANAIRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIKayhHPGFDipNPTLNLGHIHGGDSANRICGCCELHYD 258
Cdd:COG0624 188 LRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRA---DPLFG--RTTLNVTGIEGGTAVNVIPDEAEAKVD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 259 VRPLPGISIDGLDNMLREALKEVEAkwPGRIEIKPLHEPIPGYECDHEHPFIEGMERICEQ------PSETVNYCTEAPF 332
Cdd:COG0624 263 IRLLPGEDPEEVLAALRALLAAAAP--GVEVEVEVLGDGRPPFETPPDSPLVAAARAAIREvtgkepVLSGVGGGTDARF 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 549778073 333 LQQL--CPTLVLGPGSIDQAHQPDEFLAFEFIDPTIKILDRAIHQYC 377
Cdd:COG0624 341 FAEAlgIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
30-360 |
4.13e-86 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 265.90 E-value: 4.13e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 30 NSEVIAKLATWFEDLGFETQVVEVEKG-KHNLIAKMG-KGEGGLLLAGHTDTVPFDEGRWNYDPHALTEANDRFYGLGTA 107
Cdd:PRK07522 24 NLALIEWVRDYLAAHGVESELIPDPEGdKANLFATIGpADRGGIVLSGHTDVVPVDGQAWTSDPFRLTERDGRLYGRGTC 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 108 DMKGFFAFILEAVKKTDWSQQTKPLYVLATCDEETTMLGARHFTED---APFKPDYCIIGEPTSLVPIRAHKGHVANAIR 184
Cdd:PRK07522 104 DMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPSMIARlpeRGVKPAGCIVGEPTSMRPVVGHKGKAAYRCT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 185 VTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIKAYHH-PGFDIPNPTLNLGHIHGGDSANRICGCCELHYDVRPLP 263
Cdd:PRK07522 184 VRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLAAPGPFdALFDPPYSTLQTGTIQGGTALNIVPAECEFDFEFRNLP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 264 GISIDGLDNMLREA-----LKEVEAKWPG-RIEIKPLHEpIPGYECDHEHPFIEGMERICEQPS-ETVNYCTEAPFLQQL 336
Cdd:PRK07522 264 GDDPEAILARIRAYaeaelLPEMRAVHPEaAIEFEPLSA-YPGLDTAEDAAAARLVRALTGDNDlRKVAYGTEAGLFQRA 342
|
330 340
....*....|....*....|....*
gi 549778073 337 -CPTLVLGPGSIDQAHQPDEFLAFE 360
Cdd:PRK07522 343 gIPTVVCGPGSIEQAHKPDEFVELA 367
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
31-373 |
7.91e-75 |
|
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: 236.04 E-value: 7.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 31 SEVIAKLATWFEDLGFETQVVEVEkGKHNLIAKMGKGEG-GLLLAGHTDTVPF-DEGRWNYDPHALTEANDRFYGLGTAD 108
Cdd:cd08659 17 AEVAEYLAELLAKRGYGIESTIVE-GRGNLVATVGGGDGpVLLLNGHIDTVPPgDGDKWSFPPFSGRIRDGRLYGRGACD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 109 MKG-----FFAFIleAVKKTDWSQQTkPLYVLATCDEETTMLGARHFTEDAPFK-PDYCIIGEPTSLVPIRAHKGHVANA 182
Cdd:cd08659 96 MKGglaamVAALI--ELKEAGALLGG-RVALLATVDEEVGSDGARALLEAGYADrLDALIVGEPTGLDVVYAHKGSLWLR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 183 IRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIkayHHPgfDIPNPTLNLGHIHGGDSANRICGCCELHYDVRPL 262
Cdd:cd08659 173 VTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELP---AHP--LLGPPTLNVGVINGGTQVNSIPDEATLRVDIRLV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 263 PGISIDGLDNMLREALKEVEAKwpgrIEIKPLHEPIPGYECDHEHPFI-----EGMERICEQPSETVNYCTEAPFLQQL- 336
Cdd:cd08659 248 PGETNEGVIARLEAILEEHEAK----LTVEVSLDGDPPFFTDPDHPLVqalqaAARALGGDPVVRPFTGTTDASYFAKDl 323
|
330 340 350
....*....|....*....|....*....|....*...
gi 549778073 337 -CPTLVLGPGSIDQAHQPDEFLAFEFIDPTIKILDRAI 373
Cdd:cd08659 324 gFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
32-373 |
1.93e-63 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 207.54 E-value: 1.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 32 EVIAKLATWFEDLGFETQVVEVEKG--------KHNLIAKMGKGEGGLLLAGHTDTVPFDEGRWNYDPHALTEANDRFYG 103
Cdd:PRK08651 30 EIAEFLRDTLEELGFSTEIIEVPNEyvkkhdgpRPNLIARRGSGNPHLHFNGHYDVVPPGEGWSVNVPFEPKVKDGKVYG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 104 LGTADMKGFFAFILEAVKKTDwSQQTKPLYVLATCDEETTMLGARHFTEDAPFKPDYCIIGEPTSLVPI-RAHKGHVANA 182
Cdd:PRK08651 110 RGASDMKGGIAALLAAFERLD-PAGDGNIELAIVPDEETGGTGTGYLVEEGKVTPDYVIVGEPSGLDNIcIGHRGLVWGV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 183 IRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIKAYHHPGFDIPNPTLNLG--HIHGGDSANRICGCCELHYDVR 260
Cdd:PRK08651 189 VKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYEYDDERGAKPTVTLGgpTVEGGTKTNIVPGYCAFSIDRR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 261 PLPGISIDGLDNMLREALKEVEAKWPGRIEIKPLhEPIPGYECDHEHPFIEGMERICEQ-----PSETVnyCTEA----P 331
Cdd:PRK08651 269 LIPEETAEEVRDELEALLDEVAPELGIEVEFEIT-PFSEAFVTDPDSELVKALREAIREvlgvePKKTI--SLGGtdarF 345
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 549778073 332 FLQQLCPTLVLGPGSIDQAHQPDEFLAFEFIDPTIKILDRAI 373
Cdd:PRK08651 346 FGAKGIPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVL 387
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
72-375 |
4.33e-60 |
|
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: 196.41 E-value: 4.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 72 LLAGHTDTVPfDEGRWNyDPHALTEaNDRFYGLGTADMKGFFAFILEAVKKTDWSQQTK-PLYVLATCDEETTMLGARHF 150
Cdd:pfam01546 1 LLRGHMDVVP-DEETWG-WPFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLKKgTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 151 TED---APFKPDYCI---IGEPTSLV------PIRAHKGHVANAIRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDD 218
Cdd:pfam01546 78 IEDgllEREKVDAVFglhIGEPTLLEggiaigVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 219 LIKAYHHPGFDIpnptLNLGHIHGGDsaNRICGCCELHYDVRPLPGISIDGLDNMLREALKEVEAKWPGRIEIKPlHEPI 298
Cdd:pfam01546 158 NVDPLDPAVVTV----GNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEY-VEGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 299 PGYECDHeHPFIEGMERICEQ--------PSETVNYCTEAPF-LQQLCPTLV-LGPGSiDQAHQPDEFLAFEFIDPTIKI 368
Cdd:pfam01546 231 APPLVND-SPLVAALREAAKElfglkvelIVSGSMGGTDAAFfLLGVPPTVVfFGPGS-GLAHSPNEYVDLDDLEKGAKV 308
|
....*..
gi 549778073 369 LDRAIHQ 375
Cdd:pfam01546 309 LARLLLK 315
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
31-373 |
2.37e-54 |
|
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: 182.97 E-value: 2.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 31 SEVIAKLATWFEDLGFETQVVEVEKGKHNLIAKMGKGEGG--LLLAGHTDTVPFDEGR-WNYDPHALTEANDRFYGLGTA 107
Cdd:cd08011 21 SAIAAYIKLLLEDLGYPVELHEPPEEIYGVVSNIVGGRKGkrLLFNGHYDVVPAGDGEgWTVDPYSGKIKDGKLYGRGSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 108 DMKGFFAFILEAV-----KKTDWSQqtkPLYVLATCDEETT-MLGARHFTEDAPFKPDYCIIGEPTSLVPIR-AHKGHVA 180
Cdd:cd08011 101 DMKGGIAASIIAVarladAKAPWDL---PVVLTFVPDEETGgRAGTKYLLEKVRIKPNDVLIGEPSGSDNIRiGEKGLVW 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 181 NAIRVTGHSGHSSNPALGVNAIEvmhevlfALMKLRDDLIKAyhhpgfdipNPTLNLGHIHGGDSANRICGCCELHYDVR 260
Cdd:cd08011 178 VIIEITGKPAHGSLPHRGESAVK-------AAMKLIERLYEL---------EKTVNPGVIKGGVKVNLVPDYCEFSVDIR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 261 PLPGISIDGLDNMLREALKEVEAKWPgriEIKPLHEPipgYECDHEHPFIEgmeRICEQPSETVNY---------CTEAP 331
Cdd:cd08011 242 LPPGISTDEVLSRIIDHLDSIEEVSF---EIKSFYSP---TVSNPDSEIVK---KTEEAITEVLGIrpkevisvgASDAR 312
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 549778073 332 FLQQL-CPTLVLGPGSIDQAHQPDEFLAFEFIDPTIKILDRAI 373
Cdd:cd08011 313 FYRNAgIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
29-368 |
1.30e-45 |
|
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: 160.64 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 29 GNSEVIAK-LATWFEDLGFETQVVEVEKGK-----HNLIAKMGKGEGGLL-LAGHTDTVPF-DEGRWNYDPHALTEANDR 100
Cdd:TIGR01910 18 GNEETIANyIKDLLREFGFSTDVIEITDDRlkvlgKVVVKEPGNGNEKSLiFNGHYDVVPAgDLELWKTDPFKPVEKDGK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 101 FYGLGTADMKGFFAFILEAVKKTDWSQQTKP--LYVLATCDEETTMLGARHFTEDAPFK-PDYCIIGEPTSLVPI-RAHK 176
Cdd:TIGR01910 98 LYGRGATDMKGGLVALLYALKAIREAGIKPNgnIILQSVVDEESGEAGTLYLLQRGYFKdADGVLIPEPSGGDNIvIGHK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 177 GHVANAIRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDlIKAYHHPGFDIPNPTLNLGHIHGGDSANRICGCCELH 256
Cdd:TIGR01910 178 GSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEEH-IYARNSYGFIPGPITFNPGVIKGGDWVNSVPDYCEFS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 257 YDVRPLPGISIDGLDNMLREALKEVEAKWPGRIEIKPLHEPIPGYECDHEHPFIEGMERIC------EQPSETVNYCTEA 330
Cdd:TIGR01910 257 IDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYENEPVVKWSGPNETPPDSRLVKALEAIIkkvrgiEPEVLVSTGGTDA 336
|
330 340 350
....*....|....*....|....*....|....*....
gi 549778073 331 PFL-QQLCPTLVLGPGSIDQAHQPDEFLAFEFIDPTIKI 368
Cdd:TIGR01910 337 RFLrKAGIPSIVYGPGDLETAHQVNEYISIKNLVESTKV 375
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
29-363 |
2.10e-44 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 157.35 E-value: 2.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 29 GNSEVIAK-LATWFEDLGFETQVVEVEKGKHNLIAKMGKGEGGLLLAGHTDTV-PFDEGRWNYDPHALTEANDRFYGLGT 106
Cdd:PRK08588 19 DNEIEVANyLQDLFAKHGIESKIVKVNDGRANLVAEIGSGSPVLALSGHMDVVaAGDVDKWTYDPFELTEKDGKLYGRGA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 107 ADMK-GFFAFILEAVkktDWSQQTKPLY----VLATCDEETTMLGARHFTEDAPFKP-DYCIIGEPTSLVPIRAHKGHVA 180
Cdd:PRK08588 99 TDMKsGLAALVIAMI---ELKEQGQLLNgtirLLATAGEEVGELGAKQLTEKGYADDlDALIIGEPSGHGIVYAHKGSMD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 181 NAIRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIKAYHHPGFDIPNPTLnlghIHGGDSANRICGCCELHYDVR 260
Cdd:PRK08588 176 YKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYFDSIKKHNPYLGGLTHVVTI----INGGEQVNSVPDEAELEFNIR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 261 PLPGISIDGLDNMLREALKEVEAKWPGRIEIKPLHEPIPGYEcDHEHPFIEGMERICEQ------PSETVNYCTEAP-FL 333
Cdd:PRK08588 252 TIPEYDNDQVISLLQEIINEVNQNGAAQLSLDIYSNHRPVAS-DKDSKLVQLAKDVAKSyvgqdiPLSAIPGATDASsFL 330
|
330 340 350
....*....|....*....|....*....|....*.
gi 549778073 334 QQL--CPTLVLGPGSIDQAHQPDEFLA----FEFID 363
Cdd:PRK08588 331 KKKpdFPVIIFGPGNNLTAHQVDEYVEkdmyLKFID 366
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
31-357 |
1.00e-40 |
|
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: 146.65 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 31 SEVIAKLATWFEDLGF--ETQVVEvEKGKHNLIAKMGKGEG-GLLLAGHTDTVPfdegrwNYDPHALTEANDRFYGLGTA 107
Cdd:cd05652 19 AAVGDFLAEYLESLGFtvEKQPVE-NKDRFNVYAYPGSSRQpRVLLTSHIDTVP------PFIPYSISDGGDTIYGRGSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 108 DMKGFFAFILEAVKKTDWSQQTKP-----LYVLAtcdEETTMLGARHFTEDAPFKPDYCIIGEPTSLVPIRAHKGHVANA 182
Cdd:cd05652 92 DAKGSVAAQIIAVEELLAEGEVPEgdlglLFVVG---EETGGDGMKAFNDLGLNTWDAVIFGEPTELKLASGHKGMLGFK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 183 IRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLrddlikayhhpgfDIP------NPTLNLGHIHGGDSANRICGCCELH 256
Cdd:cd05652 169 LTAKGKAGHSGYPWLGISAIEILVEALVKLIDA-------------DLPssellgPTTLNIGRISGGVAANVVPAAAEAS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 257 YDVRplPGISIDGLDNMLREALKEVeAKWPGRIEIKPLHEPIPGYeCDHEhpfIEGMEriceqpSETVNYCTEAPFLQQL 336
Cdd:cd05652 236 VAIR--LAAGPPEVKDIVKEAVAGI-LTDTEDIEVTFTSGYGPVD-LDCD---VDGFE------TDVVAYGTDIPYLKGD 302
|
330 340
....*....|....*....|.
gi 549778073 337 CPTLVLGPGSIDQAHQPDEFL 357
Cdd:cd05652 303 HKRYLYGPGSILVAHGPDEAI 323
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
29-377 |
3.28e-39 |
|
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: 143.39 E-value: 3.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 29 GNSEVIAKLATWFEDLGFETQVVEVEKGKHNLIAKMgKGEGG---LLLAGHTDTVPFDegrwNYDPHALTE--ANDRFYG 103
Cdd:cd08013 27 GEAEIATYVAAWLAHRGIEAHRIEGTPGRPSVVGVV-RGTGGgksLMLNGHIDTVTLD----GYDGDPLSGeiADGRVYG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 104 LGTADMKGFFAFILEAVKKTdwsqQTKPL----YVLATCDEETTMLGarhfTED---APFKPDYCIIGEPTSLVPIRAHK 176
Cdd:cd08013 102 RGTLDMKGGLAACMAALADA----KEAGLrgdvILAAVADEEDASLG----TQEvlaAGWRADAAIVTEPTNLQIIHAHK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 177 GHVANAIRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIKAYHHPgfDIPNPTLNLGHIHGGDSANRICGCCELH 256
Cdd:cd08013 174 GFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALEEYQQELPERPVDP--LLGRASVHASLIKGGEEPSSYPARCTLT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 257 YDVRPLPGISIDGLDNMLREALKEVEAKWPG------RIEIKPlhepiPGYECDHEHPFIEGMERICEQ------PSETV 324
Cdd:cd08013 252 IERRTIPGETDESVLAELTAILGELAQTVPNfsyrepRITLSR-----PPFEVPKEHPFVQLVAAHAAKvlgeapQIRSE 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 549778073 325 NYCTEAPFLQQL-CPTLVLGPgSIDQAHQPDEFLAFEFIDPTIKILDRAIHQYC 377
Cdd:cd08013 327 TFWTDAALLAEAgIPSVVFGP-SGAGLHAKEEWVDVESIRQLREVLSAVVREFC 379
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
45-360 |
3.18e-36 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 135.33 E-value: 3.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 45 GFETQVVEVEKGKHNLIAKmgKGEGGLLLAGHTDTVPfDEGRWNYDPHALTEANDRFYGLGTADMKGFFAFILEAVKKTD 124
Cdd:PRK08737 42 GFQVEVIDHGAGAVSLYAV--RGTPKYLFNVHLDTVP-DSPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANAGD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 125 wsqqtKPLYVLATCDEET-TMLGARHFTEDApfkPDY--CIIGEPTSLVPIRAHKGHVANAIRVTGHSGHSSNP-ALGVN 200
Cdd:PRK08737 119 -----GDAAFLFSSDEEAnDPRCVAAFLARG---IPYeaVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKqDPSAS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 201 AIevmHEVLFALMKLRDDLIKAYHHPGFDIPNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGISIDGLDNMLR----E 276
Cdd:PRK08737 191 AL---HQAMRWGGQALDHVESLAHARFGGLTGLRFNIGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFAgfaeP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 277 ALKEVEAKWPGrieikPLHEPIPGYECDHEHPFIEGMERICEQP-SETVNYCTEAP-FLQQLCPTLVLGPGSIDQAHQPD 354
Cdd:PRK08737 268 AAATFEETFRG-----PSLPSGDIARAEERRLAARDVADALDLPiGNAVDFWTEASlFSAAGYTALVYGPGDIAQAHTAD 342
|
....*.
gi 549778073 355 EFLAFE 360
Cdd:PRK08737 343 EFVTLD 348
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
55-377 |
3.99e-32 |
|
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: 124.73 E-value: 3.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 55 KGKHNLIAKM-GKGEGG--LLLAGHTDTVPFDEGR-WNYDPHALTEANDRFYGLGTADMKGFFA---FILEAVKKTDWsQ 127
Cdd:cd03895 58 AGAPNVVGTHrPRGETGrsLILNGHIDVVPEGPVElWTRPPFEATIVDGWMYGRGAGDMKAGLAanlFALDALRAAGL-Q 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 128 QTKPLYVLATCDEETTMLGA-----RHFTEDApfkpdyCIIGEPTSLVPIRAHKGHVANAIRVTGHSGHSSNPALGVNAI 202
Cdd:cd03895 137 PAADVHFQSVVEEECTGNGAlaalmRGYRADA------ALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 203 EVMHEVLFALMKLRDDL-IKAYHHPGF-DIPNP-TLNLGHIHGGDSANRICGCCELHYDVRPLPGISIDGLDNMLREALK 279
Cdd:cd03895 211 EKAMHLIQALQELEREWnARKKSHPHFsDHPHPiNFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 280 EVEAKWPGRIEIKPLHEPI----PGYECDHEHPFIEGMERICEQ-----PSETVNYC-TEAPFLQQL--CPTLVLGPGSI 347
Cdd:cd03895 291 DAAATDPWLSNHPPEVEWNgfqaEGYVLEPGSDAEQVLAAAHQAvfgtpPVQSAMTAtTDGRFFVLYgdIPALCYGPGSR 370
|
330 340 350
....*....|....*....|....*....|
gi 549778073 348 DqAHQPDEFLAFEFIDPTIKILDRAIHQYC 377
Cdd:cd03895 371 D-AHGFDESVDLESLRKITKTIALFIAEWC 399
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
27-355 |
5.19e-31 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 121.59 E-value: 5.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 27 DEGnsEVIAKLATWFEDLGFETqvVEVEkGKHNLIAKMGKGEGGLLLAGHTDTVPF-DEGRWNYDPHALTEANDRFYGLG 105
Cdd:PRK13004 33 DEK--RVVKRIKEEMEKVGFDK--VEID-PMGNVLGYIGHGKKLIAFDAHIDTVGIgDIKNWDFDPFEGEEDDGRIYGRG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 106 TADMKGFFAFILEAVK--KTDWSQQTKPLYVLATCDEET-TMLGARHFTEDAPFKPDYCIIGEPTSLVPIRAHKGHVANA 182
Cdd:PRK13004 108 TSDQKGGMASMVYAAKiiKDLGLDDEYTLYVTGTVQEEDcDGLCWRYIIEEDKIKPDFVVITEPTDLNIYRGQRGRMEIR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 183 IRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLikaYHHP----GfdipnpTLNLGHIHGGD-SANRICGCCELHY 257
Cdd:PRK13004 188 VETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNL---KEDPflgkG------TLTVSDIFSTSpSRCAVPDSCAISI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 258 DVRPLPGISIDGLDNMLReALKEVEaKWPGRIEI----KPLH--EPIPGyEC-------DHEHPF----IEGMERICEQP 320
Cdd:PRK13004 259 DRRLTVGETWESVLAEIR-ALPAVK-KANAKVSMynydRPSYtgLVYPT-ECyfptwlyPEDHEFvkaaVEAYKGLFGKA 335
|
330 340 350
....*....|....*....|....*....|....*....
gi 549778073 321 SETVNY--CTEAPFLQQL--CPTLVLGPGSIDQAHQPDE 355
Cdd:PRK13004 336 PEVDKWtfSTNGVSIAGRagIPTIGFGPGKEPLAHAPNE 374
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
28-260 |
1.54e-30 |
|
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: 119.62 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 28 EGNSEVIAKLATWFEDLGFETQVVEVEKGKHNLIAKM-GKGEGGLLLAGHTDTVpFDEGrwNYDPHALTEANDRFYGLGT 106
Cdd:cd03885 19 EGVDRVAELLAEELEALGFTVERRPLGEFGDHLIATFkGTGGKRVLLIGHMDTV-FPEG--TLAFRPFTVDGDRAYGPGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 107 ADMKGFFAFILEAVK--KTDWSQQTKPLYVLATCDEETTMLGARHFTEDAPFKPDYCIIGEPT----SLVPIRahKGHVA 180
Cdd:cd03885 96 ADMKGGLVVILHALKalKAAGGRDYLPITVLLNSDEEIGSPGSRELIEEEAKGADYVLVFEPAradgNLVTAR--KGIGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 181 NAIRVTGHSGHSSN-PALGVNAIEVMHEVLFALMKLRDdlikayhhpgfDIPNPTLNLGHIHGGDSANRICGCCELHYDV 259
Cdd:cd03885 174 FRLTVKGRAAHAGNaPEKGRSAIYELAHQVLALHALTD-----------PEKGTTVNVGVISGGTRVNVVPDHAEAQVDV 242
|
.
gi 549778073 260 R 260
Cdd:cd03885 243 R 243
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
32-355 |
1.79e-30 |
|
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: 119.83 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 32 EVIAKLATWFEDLGFETqvVEVEkGKHNLIAKMGKGEGGLLLAGHTDTVPF-DEGRWNYDPHALTEANDRFYGLGTADMK 110
Cdd:cd05649 19 GVVERIEEEMEKLGFDE--VEID-PMGNVIGYIGGGKKKILFDGHIDTVGIgNIDNWKFDPYEGYETDGKIYGRGTSDQK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 111 GFFAFILEAV---KKTDWSQQTKPLYVLATCDEET-TMLGARHFTEDAPFKPDYCIIGEPTSLVPIRAHKGHVANAIRVT 186
Cdd:cd05649 96 GGLASMVYAAkimKDLGLRDFAYTILVAGTVQEEDcDGVCWQYISKADKIKPDFVVSGEPTDGNIYRGQRGRMEIRVDTK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 187 GHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIkayHHPgfDIPNPTLNLGHIHGGD-SANRICGCCELHYD------- 258
Cdd:cd05649 176 GVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFP---EAP--FLGRGTLTVTDIFSTSpSRCAVPDSCRISIDrrltvge 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 259 --------VRPLPGISIDGLDNMLREALKEvEAKWPGriEIKPLHEPIPGYECDHEHPFI----EGMERICEQPSETVNY 326
Cdd:cd05649 251 twegcleeIRALPAVKKYGDDVAVSMYNYD-RPSYTG--EVYESERYFPTWLLPEDHELVkallEAYKALFGARPLIDKW 327
|
330 340 350
....*....|....*....|....*....|...
gi 549778073 327 --CTEAPFLQ--QLCPTLVLGPGSIDQAHQPDE 355
Cdd:cd05649 328 tfSTNGVSIMgrAGIPCIGFGPGAENQAHAPNE 360
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
29-373 |
6.07e-28 |
|
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: 112.06 E-value: 6.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 29 GNSEVIAK-LATWFEDLGFETQVVEVEkgkhNLIAKMGKGEGGLLLAGHTDTVPfdeGRWNydphaLTEANDRFYGLGTA 107
Cdd:cd05653 18 GEEARAAKfLEEIMKELGLEAWVDEAG----NAVGGAGSGPPDVLLLGHIDTVP---GEIP-----VRVEGGVLYGRGAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 108 DMKG-FFAFILEAVKKTDWSQQTkpLYVLATCDEETTMLGARHFTEDAPfKPDYCIIGEPTSLVPIR-AHKGHVANAIRV 185
Cdd:cd05653 86 DAKGpLAAMILAASALNEELGAR--VVVAGLVDEEGSSKGARELVRRGP-RPDYIIIGEPSGWDGITlGYRGSLLVKIRC 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 186 TGHSGHSSNPalGVNAIEVMHEVLFALMKLrddlikAYHHPGFDIPNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGi 265
Cdd:cd05653 163 EGRSGHSSSP--ERNAAEDLIKKWLEVKKW------AEGYNVGGRDFDSVVPTLIKGGESSNGLPQRAEATIDLRLPPR- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 266 sidgldNMLREALKEVEAKWPG-RIEIKPLHEPipgYECDHEHPFIEGMER-ICEQPSE--------TVNYCTEAPFLQq 335
Cdd:cd05653 234 ------LSPEEAIALATALLPTcELEFIDDTEP---VKVSKNNPLARAFRRaIRKQGGKprlkrktgTSDMNVLAPLWT- 303
|
330 340 350
....*....|....*....|....*....|....*...
gi 549778073 336 lCPTLVLGPGSIDQAHQPDEFLAFEFIDPTIKILDRAI 373
Cdd:cd05653 304 -VPIVAYGPGDSTLDHTPNEHIELAEIERAAAVLKGAL 340
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
173-286 |
4.79e-27 |
|
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: 103.19 E-value: 4.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 173 RAHKGHVANAIRVTGHSGHSSNPALGVNAIEVMhevlfalMKLRDDLIKAYHHPGFDIPNPTLNLGHIHGGDSANRICGC 252
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLL-------ARLLAELPAEYGDIGFDFPRTTLNITGIEGGTATNVIPAE 73
|
90 100 110
....*....|....*....|....*....|....
gi 549778073 253 CELHYDVRPLPGISIDGLDNMLREALKEVEAKWP 286
Cdd:pfam07687 74 AEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
32-363 |
1.93e-26 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 108.31 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 32 EVIAKLATWFEDLGFETQVVEVEKGKHNLIakmgKGEGGLLLAGHTDTVPFDEGrwnydphaLTEANDRFYGLGTADMKG 111
Cdd:PRK08652 23 EIALHIMEFLESLGYDVHIESDGEVINIVV----NSKAELFVEVHYDTVPVRAE--------FFVDGVYVYGTGACDAKG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 112 FFAFILEAVKKTDWSQQTKPLYVLATCDEETTMLGARHFTEDapFKPDYCIIGEPTSLVPIRAHKGHVANAIRVTGHSGH 191
Cdd:PRK08652 91 GVAAILLALEELGKEFEDLNVGIAFVSDEEEGGRGSALFAER--YRPKMAIVLEPTDLKVAIAHYGNLEAYVEVKGKPSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 192 SSNPALGVNAIEVMHEVLFALMKLRDDLIKAYhhpgfdipNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGISIDGLD 271
Cdd:PRK08652 169 GACPESGVNAIEKAFEMLEKLKELLKALGKYF--------DPHIGIQEIIGGSPEYSIPALCRLRLDARIPPEVEVEDVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 272 NMLREALKEVEAKwpgrieiKPLHEPIPGYECDHEHPFIEGMERICEQPSETVNYC-----TEA-PFLQQLCPTLVLGPG 345
Cdd:PRK08652 241 DEIDPILDEYTVK-------YEYTEIWDGFELDEDEEIVQLLEKAMKEVGLEPEFTvmrswTDAiNFRYNGTKTVVWGPG 313
|
330
....*....|....*...
gi 549778073 346 SIDQAHQPdeflaFEFID 363
Cdd:PRK08652 314 ELDLCHTK-----FERID 326
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
27-355 |
4.48e-26 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 107.50 E-value: 4.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 27 DEGNSEVIAKLatwFEDLGFETQVVEVEKGKhNLIAKMGKGEGGLLLAGHTDTVPF-DEGRWNYDPHALTEANDRFYGLG 105
Cdd:TIGR01246 18 DAGCQDIIAER---LEKLGFEIEWMHFGDTK-NLWATRGTGEPVLAFAGHTDVVPAgPEEQWSSPPFEPVERDGKLYGRG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 106 TADMKGFFAFILEA----VKKTDWSQQTkpLYVLATCDEETTML-GARHFTE---DAPFKPDYCIIGEPTSLVPI----- 172
Cdd:TIGR01246 94 AADMKGSLAAFIVAaerfVKKNPDHKGS--ISLLITSDEEGTAIdGTKKVVEtlmARDELIDYCIVGEPSSVKKLgdvik 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 173 RAHKGHVANAIRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIKAYhhpgfdIPNPTLNLGHIHGG-DSANRICG 251
Cdd:TIGR01246 172 NGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAIKWDEGNEF------FPPTSLQITNIHAGtGANNVIPG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 252 CCELHYDVRPLPGISIDGLDNMLREALKEVEAKWpgRIEIKPLHEPIPGYECDHEHPFIEGMERICEQPSE--TVNYCTE 329
Cdd:TIGR01246 246 ELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDY--DLEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPElsTGGGTSD 323
|
330 340
....*....|....*....|....*..
gi 549778073 330 APFLQQLCPTLV-LGPGSiDQAHQPDE 355
Cdd:TIGR01246 324 GRFIALMGAEVVeFGPVN-ATIHKVNE 349
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
37-357 |
4.60e-26 |
|
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: 107.18 E-value: 4.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 37 LATWFEDLGFETqvVEVEkGKHNLIAKM-GKGEG-GLLLAGHTDTVpFDEGrwnyDPHALTEANDRFYGLGTADMKGFFA 114
Cdd:cd03896 24 VAEWMADLGLGD--VERD-GRGNVVGRLrGTGGGpALLFSAHLDTV-FPGD----TPATVRHEGGRIYGPGIGDNKGSLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 115 FILEAVK--KTDWSQQTKPLYVLATCDEE--TTMLGARHFTEDAPFKPDYCIIGEPTSLVPIRAHKGHVANAIRVTGHSG 190
Cdd:cd03896 96 CLLAMARamKEAGAALKGDVVFAANVGEEglGDLRGARYLLSAHGARLDYFVVAEGTDGVPHTGAVGSKRFRITTVGPGG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 191 HSSNPALGVNAIEVMHEVLFALMKLRDDLikayhhpgfdIPNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGISIDGL 270
Cdd:cd03896 176 HSYGAFGSPSAIVAMAKLVEALYEWAAPY----------VPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPDAELADV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 271 DNMLREALKEVEAKWPG-RIEIKPLHEPiPGYECDHEHPFIEGMERICEQPSETVNY---CTEA-PFLQQLCPTLVLGPG 345
Cdd:cd03896 246 QREVEAVVSKLAAKHLRvKARVKPVGDR-PGGEAQGTEPLVNAAVAAHREVGGDPRPgssSTDAnPANSLGIPAVTYGLG 324
|
330
....*....|..
gi 549778073 346 SIDQAHQPDEFL 357
Cdd:cd03896 325 RGGNAHRGDEYV 336
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
31-373 |
1.50e-25 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 105.81 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 31 SEVIAKLATWFEDLGFETQVVEVEkgkhNLIAKMGKGEGGLLLAGHTDTVPFD-----EGrwnydphalteanDRFYGLG 105
Cdd:PRK04443 26 AAAAEFLVEFMESHGREAWVDEAG----NARGPAGDGPPLVLLLGHIDTVPGDipvrvED-------------GVLWGRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 106 TADMKGFFAFILEAVKKTDWSQQTKPLYVLATcDEETTMLGARHFTEDApFKPDYCIIGEPTSLVPIR-AHKGHVANAIR 184
Cdd:PRK04443 89 SVDAKGPLAAFAAAAARLEALVRARVSFVGAV-EEEAPSSGGARLVADR-ERPDAVIIGEPSGWDGITlGYKGRLLVTYV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 185 VTGHSGHSSNPalGVNAIEVMHEVLFAlmklrddlIKAY------HHPGFDIPNPTLNLGHIHGGDSANRicgcCELHYD 258
Cdd:PRK04443 167 ATSESFHSAGP--EPNAAEDAIEWWLA--------VEAWfeandgRERVFDQVTPKLVDFDSSSDGLTVE----AEMTVG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 259 VRPLPGISIDGLDNMLREALKEVEAKWPGrieikplhePIPGYECDHEHPFI---------EGMERICEQPSETVNYCTE 329
Cdd:PRK04443 233 LRLPPGLSPEEAREILDALLPTGTVTFTG---------AVPAYMVSKRTPLArafrvaireAGGTPRLKRKTGTSDMNVV 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 549778073 330 APFLQqlCPTLVLGPGSIDQAHQPDEFLAFEFIDPTIKILDRAI 373
Cdd:PRK04443 304 APAWG--CPMVAYGPGDSDLDHTPDEHLPLAEYLRAIAVLTDVL 345
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
46-376 |
2.05e-25 |
|
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: 105.08 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 46 FETQVVEVEKGKHNLIAKMG---KGEGGLLLAGHTDTVPFDEGrWNYDPHALTEANDRFYGLGTADMKGFFAFILeAVKK 122
Cdd:cd05651 30 LEQKGIPFKRKGNNVWAENGhfdEGKPTLLLNSHHDTVKPNAG-WTKDPFEPVEKGGKLYGLGSNDAGASVVSLL-ATFL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 123 TDWSQQTKP--LYVLATCDEETT-MLGARHFTEDAPfKPDYCIIGEPTSLVPIRAHKGHVANAIRVTGHSGHSSNPAlGV 199
Cdd:cd05651 108 HLYSEGPLNynLIYAASAEEEISgKNGIESLLPHLP-PLDLAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAARNE-GD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 200 NAIevmHEVLFALMKLRDdlikaYHHPGFD--IPNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGISIDGLDNMLREA 277
Cdd:cd05651 186 NAI---YKALDDIQWLRD-----FRFDKVSplLGPVKMTVTQINAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 278 LKEveakwpgriEIKPLHEPIPGYECDHEHPFIEGMERICEQP--SETVNYCTEAPFlqqlcPTLVLGPGSIDQAHQPDE 355
Cdd:cd05651 258 LKS---------EIKPRSFRLNSSAIPPDHPIVQAAIAAGRTPfgSPTLSDQALMPF-----PSVKIGPGDSSRSHTADE 323
|
330 340
....*....|....*....|.
gi 549778073 356 FLafefidpTIKILDRAIHQY 376
Cdd:cd05651 324 FI-------ELSEIEEGIDIY 337
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
65-283 |
2.88e-24 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 103.16 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 65 GKGEGG--LLLAGHTDTVPfdEG---RWNYDPHALTEANDRFYGLGTADMKGFFA---FILEAVKKTDWsQQTKPLYVLA 136
Cdd:PRK06837 92 PAGKTGrsLILQGHIDVVP--EGpldLWSRPPFDPVIVDGWMYGRGAADMKAGLAamlFALDALRAAGL-APAARVHFQS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 137 TCDEETTMLGA-----RHFTEDApfkpdyCIIGEPTSLVPIRAHKGHVANAIRVTGHSGHSSNPALGVNAIEVMHEVLFA 211
Cdd:PRK06837 169 VIEEESTGNGAlstlqRGYRADA------CLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQA 242
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549778073 212 LMKLRDDL-IKAYHHPGF-DIPNP-TLNLGHIHGGDSANRICGCCELHYDVRPLPGISIDgldnmlrEALKEVEA 283
Cdd:PRK06837 243 LRELEAEWnARKASDPHFeDVPHPiNFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAA-------DAQAEIEA 310
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
37-297 |
2.96e-24 |
|
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: 102.20 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 37 LATWFEDLGFETQVVEVEkGKHNLIAKMGKGEGGLLLAGHTDTVPF-DEGRWNYDPHALTEANDRFYGLGTADMKG---- 111
Cdd:cd03891 24 IAERLKALGFTCERLEFG-GVKNLWARRGTGGPHLCFAGHTDVVPPgDLEGWSSDPFSPTIKDGMLYGRGAADMKGgiaa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 112 FFAFILEAVKKTDWSQQTkpLYVLATCDEETTmlgARHFT-------EDAPFKPDYCIIGEPTSlvpiRAHKGHV----- 179
Cdd:cd03891 103 FVAAAERFVAKHPNHKGS--ISFLITSDEEGP---AIDGTkkvlewlKARGEKIDYCIVGEPTS----EKKLGDTikigr 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 180 ---ANA-IRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDlikayhhPGFDIPNPT-LNLGHIHGGDSA-NRICGCC 253
Cdd:cd03891 174 rgsLNGkLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLD-------EGNEFFPPSsLQITNIDVGNGAtNVIPGEL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 549778073 254 ELHYDVRPLPGISIDGLDNMLREALKEVEAKWpgRIEIKPLHEP 297
Cdd:cd03891 247 KAKFNIRFNDEHTGESLKARIEAILDKHGLDY--DLEWKLSGEP 288
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
32-357 |
4.54e-24 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 101.67 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 32 EVIAKLATWFEDLGFETQVVEVekgkHNLIAK----MGKGEGGLLLAGHTDTVPFDEGRwNYDPHaltEANDRFYGLGT- 106
Cdd:COG2195 24 ALADYLVEELKELGLEVEEDEA----GNVIATlpatPGYNVPTIGLQAHMDTVPQFPGD-GIKPQ---IDGGLITADGTt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 107 ---ADMKGFFAFILEAVKkTDWSQQTK--PLYVLATCDEETTMLGARHFTEDApFKPDYCII---GEPTSLVpIRAhkgh 178
Cdd:COG2195 96 tlgADDKAGVAAILAALE-YLKEPEIPhgPIEVLFTPDEEIGLRGAKALDVSK-LGADFAYTldgGEEGELE-YEC---- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 179 vANA----IRVTGHSGHS-SNPALGVNAIEVMHEVLFALmklrddlikayhhPGFDIPNPT-LNLGHIHGGDSANRICGC 252
Cdd:COG2195 169 -AGAadakITIKGKGGHSgDAKEKMINAIKLAARFLAAL-------------PLGRIPEETeGNEGFIHGGSATNAIPRE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 253 CELHYDVRPLpgiSIDGLD---NMLREALKEVEAKWP-GRIEIKpLHEPIPGYECDHEHPFIEGMERICEQPSETVNYC- 327
Cdd:COG2195 235 AEAVYIIRDH---DREKLEarkAELEEAFEEENAKYGvGVVEVE-IEDQYPNWKPEPDSPIVDLAKEAYEELGIEPKIKp 310
|
330 340 350
....*....|....*....|....*....|....*.
gi 549778073 328 ----TEAPFL--QQLcPTLVLGPGsIDQAHQPDEFL 357
Cdd:COG2195 311 irggLDGGILsfKGL-PTPNLGPG-GHNFHSPDERV 344
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
29-298 |
6.19e-24 |
|
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: 102.44 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 29 GNSEVIAKLATWFEDLGFETQVVEVEK--GKHNLIAKMGKG---EGGLLLAGHTDTVPFDEGRWNYDPHALTEANDRFYG 103
Cdd:cd05675 21 SETRAAEVLAARLAEAGIQTEIFVVEShpGRANLVARIGGTdpsAGPLLLLGHIDVVPADASDWSVDPFSGEIKDGYVYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 104 LGTADMKGFFAFILEAVKktDWSQQ----TKPLYVLATCDEET-TMLGARHFTEDAP--FKP-DYCI---------IGEP 166
Cdd:cd05675 101 RGAVDMKNMAAMMLAVLR--HYKREgfkpKRDLVFAFVADEEAgGENGAKWLVDNHPelFDGaTFALneggggslpVGKG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 167 TSLVPIR-AHKGHVANAIRVTGHSGHSSNP----ALgVNAIEVMHEV--------------LFALM-KLRDDLIKAYHHP 226
Cdd:cd05675 179 RRLYPIQvAEKGIAWMKLTVRGRAGHGSRPtddnAI-TRLAEALRRLgahnfpvrltdetaYFAQMaELAGGEGGALMLT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 227 GFDIPNPTLN-LGH-----------------IHGGDSANRICGCCELHYDVRPLPGISIDGLDNMLREALK--EVEAKWP 286
Cdd:cd05675 258 AVPVLDPALAkLGPsapllnamlrntasptmLDAGYATNVLPGRATAEVDCRILPGQSEEEVLDTLDKLLGdpDVSVEAV 337
|
330
....*....|....
gi 549778073 287 GRIE--IKPLHEPI 298
Cdd:cd05675 338 HLEPatESPLDSPL 351
|
|
| PRK06915 |
PRK06915 |
peptidase; |
55-377 |
2.67e-20 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 91.68 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 55 KGKHNLIAKM-GKGEG-GLLLAGHTDTVPF-DEGRWNYDPHALTEANDRFYGLGTADMKG-----FFAfiLEAVKKTDWS 126
Cdd:PRK06915 78 SDSPNIVATLkGSGGGkSMILNGHIDVVPEgDVNQWDHHPYSGEVIGGRIYGRGTTDMKGgnvalLLA--MEALIESGIE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 127 QQTKpLYVLATCDEETTMLGA-----RHFTEDApfkpdyCIIGEPTSLVPIRAHKGHVANAIRVTGHSGHSSNPALGVNA 201
Cdd:PRK06915 156 LKGD-VIFQSVIEEESGGAGTlaailRGYKADG------AIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 202 IE-VMHEV--LFALMKLRDDLIKAYHHPGFDIPNPtLNLGHIHGGD----SANRI-----CGCCelhydvrplPGISIDG 269
Cdd:PRK06915 229 IEkSMFVIdhLRKLEEKRNDRITDPLYKGIPIPIP-INIGKIEGGSwpssVPDSVilegrCGIA---------PNETIEA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 270 LDNMLREALKE------------VEAKWPGRieikplhEPIPGyECDHEHPFI----EGMERICEQPS--ETVNYCTEAP 331
Cdd:PRK06915 299 AKEEFENWIAElndvdewfvehpVEVEWFGA-------RWVPG-ELEENHPLMttleHNFVEIEGNKPiiEASPWGTDGG 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 549778073 332 FLQQL--CPTLVLGPGSIDQAHQPDEFLAFEFIDPTIKILDRAIHQYC 377
Cdd:PRK06915 371 LLTQIagVPTIVFGPGETKVAHYPNEYIEVDKMIAAAKIIALTLLDWC 418
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
37-377 |
2.94e-20 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 91.64 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 37 LATWFEDLGFETQVVEVEKGKHNLIAKMgKGEG-----GLLLAGHTDTVPFDEGR-WNYDPHALTEANDRFYGLGTADMK 110
Cdd:PRK08596 42 IAEFLRKLGFSVDKWDVYPNDPNVVGVK-KGTEsdaykSLIINGHMDVAEVSADEaWETNPFEPTIKDGWLYGRGAADMK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 111 GFFAFILEAVKK-TDWSQQTK-PLYVLATCDEETTMLGARHFTEDAPfKPDYCIIGEpTSLVPIRAHKGHVANAIRV--- 185
Cdd:PRK08596 121 GGLAGALFAIQLlHEAGIELPgDLIFQSVIGEEVGEAGTLQCCERGY-DADFAVVVD-TSDLHMQGQGGVITGWITVksp 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 186 -TGHSG------HSSNPALGVNAIEVMHEVLFALMKLRDDLIKAYHHPGFDIPNPTLNLGHIHGGDSANRICGCCELHYD 258
Cdd:PRK08596 199 qTFHDGtrrqmiHAGGGLFGASAIEKMMKIIQSLQELERHWAVMKSYPGFPPGTNTINPAVIEGGRHAAFIADECRLWIT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 259 VRPLPGISIDGLDNMLREALKEVEA------------KWPGRIEIKPLHEPIPGYECDHEHPFIEGM----ERICEQP-- 320
Cdd:PRK08596 279 VHFYPNETYEQVIKEIEEYIGKVAAadpwlrenppqfKWGGESMIEDRGEIFPSLEIDSEHPAVKTLssahESVLSKNai 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549778073 321 ---SETVnycTEAPFLQQL-CPTLVLGPGSIDQAHQPDEFL-AFEFIDPTiKILDRAIHQYC 377
Cdd:PRK08596 359 ldmSTTV---TDGGWFAEFgIPAVIYGPGTLEEAHSVNEKVeIEQLIEYT-KVITAFIYEWC 416
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
27-297 |
1.11e-18 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 86.29 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 27 DEGNSEVIAKLatwFEDLGFETQVVEVEkGKHNLIAKmgKGEGGLLL--AGHTDTVPF-DEGRWNYDPHALTEANDRFYG 103
Cdd:PRK13009 21 DAGCQDLLAER---LEALGFTCERMDFG-DVKNLWAR--RGTEGPHLcfAGHTDVVPPgDLEAWTSPPFEPTIRDGMLYG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 104 LGTADMKG----FFAFILEAVKKTDWSQQTkpLYVLATCDEE------TT----MLGARHftedapFKPDYCIIGEPTS- 168
Cdd:PRK13009 95 RGAADMKGslaaFVVAAERFVAAHPDHKGS--IAFLITSDEEgpaingTVkvleWLKARG------EKIDYCIVGEPTSt 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 169 -----LVPI-RahKGHVANAIRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIKAYhhpgFdiPNPTLNLGHIHG 242
Cdd:PRK13009 167 erlgdVIKNgR--RGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEGNEF----F--PPTSLQITNIDA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 549778073 243 GDSA-NRICGCCELHYDVRPLPGISIDGLDNMLREALKEVEAKWpgRIEIKPLHEP 297
Cdd:PRK13009 239 GTGAtNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDY--TLEWTLSGEP 292
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
28-356 |
2.00e-18 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 86.06 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 28 EGNSEVIAKLATWFEDLGF-ETQVVEV--EKGKH----NLIAKM--GKGEGGLLLAGHTDTVPF-DEGRWNYDPHALTEA 97
Cdd:PRK13983 27 EGEKEKAEYLESLLKEYGFdEVERYDApdPRVIEgvrpNIVAKIpgGDGKRTLWIISHMDVVPPgDLSLWETDPFKPVVK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 98 NDRFYGLGTAD-MKGFFA--FILEAVKKtdwsQQTKPLYVLATC---DEET-TMLGARHF--TEDAPFKPDYCII----G 164
Cdd:PRK13983 107 DGKIYGRGSEDnGQGIVSslLALKALMD----LGIRPKYNLGLAfvsDEETgSKYGIQYLlkKHPELFKKDDLILvpdaG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 165 EPT-SLVPIrAHKGHVANAIRVTGHSGHSSNPALGVNAievmHEVLFAL-MKLRDDLIKAYH--HPGFDIPN----PTln 236
Cdd:PRK13983 183 NPDgSFIEI-AEKSILWLKFTVKGKQCHASTPENGINA----HRAAADFaLELDEALHEKFNakDPLFDPPYstfePT-- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 237 lghIHGG--DSANRICGCCELHYDVRPLPGISIDGLDNMLREALKEVEAKWPGRIEIKPLHEPIPGYECDHEHPFIEGME 314
Cdd:PRK13983 256 ---KKEAnvDNINTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIADEFEEEYGVKIEVEIVQREQAPPPTPPDSEIVKKLK 332
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 549778073 315 R-ICEQPSETVNYC-----TEAPFLQQL-CPTLVLGPGsIDQAHQPDEF 356
Cdd:PRK13983 333 RaIKEVRGIEPKVGgigggTVAAFLRKKgYPAVVWSTL-DETAHQPNEY 380
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
54-356 |
6.48e-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: 78.27 E-value: 6.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 54 EKGKH--NLIAKMGKGEGGLL-LAGHTDTVPF-DEGRWNYDPHALTEANDRFYGLGTAD-MKGFFA--FILEAVKKTDws 126
Cdd:cd05650 52 ERGIIrpNIVAKIPGGNDKTLwIISHLDTVPPgDLSLWETDPWEPVVKDGKIYGRGVEDnQQGIVSslLALKAIIKNG-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 127 qqTKPLY---VLATCDEET-TMLGARHFTEDAP-FKPDYCII----GEPTSLVPIRAHKGHVANAIRVTGHSGHSSNPAL 197
Cdd:cd05650 130 --ITPKYnfgLLFVADEEDgSEYGIQYLLNKFDlFKKDDLIIvpdfGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPEN 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 198 GVNAIEV-------MHEVLFALMKLRDDLikayhhpgFDIP----NPTLNLGHIhggDSANRICGCCELHYDVRPLPGIS 266
Cdd:cd05650 208 GINAFVAasnfaleLDELLHEKFDEKDDL--------FNPPystfEPTKKEANV---PNVNTIPGYDVFYFDCRVLPTYK 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 267 IDGLDNMLREALKEVEAKWPGRIEIKPLH-EPIPGYECDHEHPFIEGMERICEQPSETVNYC-----TEAPFLQQL-CPT 339
Cdd:cd05650 277 LDEVLKFVNKIISDFENSYGAGITYEIVQkEQAPPATPEDSEIVVRLSKAIKKVRGREAKLIgigggTVAAFLRKKgYPA 356
|
330
....*....|....*..
gi 549778073 340 LVLGPGsIDQAHQPDEF 356
Cdd:cd05650 357 VVWSTL-DETAHQPNEY 372
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
59-168 |
6.92e-16 |
|
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: 75.55 E-value: 6.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 59 NLIAKMGKGEGG--LLLAGHTDTVPFDEGRWNYDPHA-LTEANDRFYGLGTADMKGFFAFILEAVK--KTDWSQQTKPLY 133
Cdd:cd18669 1 NVIARYGGGGGGkrVLLGAHIDVVPAGEGDPRDPPFFvDTVEEGRLYGRGALDDKGGVAAALEALKllKENGFKLKGTVV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 549778073 134 VLATCDEETTMLGAR----HFTEDAPFKPDYCIIGEPTS 168
Cdd:cd18669 81 VAFTPDEEVGSGAGKgllsKDALEEDLKVDYLFVGDATP 119
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
59-300 |
1.19e-15 |
|
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.
Pssm-ID: 349869 [Multi-domain] Cd Length: 394 Bit Score: 77.59 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 59 NLIAKMGKGEGGLLLA--GHTDTVPFDEGrWNYDPHALTEANDRFYGLGTADMKGFFAFILEAVKKTDwsQQTKPLY--- 133
Cdd:cd02697 62 NLIVRRRYGDGGRTVAlnAHGDVVPPGDG-WTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALE--SLGAPLRgav 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 134 -VLATCDEETT-MLGARHFTEDAPFKPDYcIIGEPTSLVPIRAHKGHVANAIRVTGHSGHSSNPALGVNAIEVMHEVLFA 211
Cdd:cd02697 139 eLHFTYDEEFGgELGPGWLLRQGLTKPDL-LIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 212 LMKLRDDLIKAYHH-PGfdIPNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGISIDGLDNMLREALKEVEAKWPG-RI 289
Cdd:cd02697 218 LYALNAQYRQVSSQvEG--ITHPYLNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAASMPGiSV 295
|
250
....*....|....*.
gi 549778073 290 EIKPL-----HEPIPG 300
Cdd:cd02697 296 DIRRLllansMRPLPG 311
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
51-371 |
2.71e-15 |
|
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: 76.33 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 51 VEVEKGKHNLIAKMGKG-EGGLLLAGHTDTVPFDE---GRWnydphaltEANDRFYGLGTADMKGFFAFILEAVKKTDWS 126
Cdd:cd05647 35 LEVIRDGNTVVARTERGlASRVILAGHLDTVPVAGnlpSRV--------EEDGVLYGCGATDMKAGDAVQLKLAATLAAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 127 QQTKPL-YVLATCDEETTML-GARHFTEDAP--FKPDYCIIGEPTSLVPIRAHKGHVANAIRVTGHSGHSSNPALGVNAI 202
Cdd:cd05647 107 TLKHDLtLIFYDCEEVAAELnGLGRLAEEHPewLAADFAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 203 EVMHEVLFALMKLRDdliKAYHHPGFDIpNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGISIDGLDNMLREALKEVE 282
Cdd:cd05647 187 HKLAPILARLAAYEP---RTVNIDGLTY-REGLNAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 283 AKWpgriEIKPLH-EPIPGYECDHEHPFIegmERICEQPSETVNYCTEAPFLQQLCPTLVLGPGSIDQAHQPDEFLAFEF 361
Cdd:cd05647 263 YEI----EVTDLSpGALPGLDHPVARDLI---EAVGGKVRAKYGWTDVARFSALGIPAVNFGPGDPLLAHKRDEQVPVEQ 335
|
330
....*....|
gi 549778073 362 IDPTIKILDR 371
Cdd:cd05647 336 ITACAAILRR 345
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
37-356 |
2.86e-15 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 76.72 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 37 LATWFEDLGFETQVVEVEKG--------KHNLIAKM-GKGEGGLL-LAGHTDTVPFDEGrWNYDPHALTEANDRFYGLGT 106
Cdd:PRK13013 43 LAARLAPRGFEVELIRAEGApgdsetypRWNLVARRqGARDGDCVhFNSHHDVVEVGHG-WTRDPFGGEVKDGRIYGRGA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 107 ADMKGFFAFILEAVKKTdwsQQTKPLY-----VLATCDEETTML-GARHFTEDAPFKP---DYCIIGEPTSLVPI-RAHK 176
Cdd:PRK13013 122 CDMKGGLAASIIAAEAF---LAVYPDFagsieISGTADEESGGFgGVAYLAEQGRFSPdrvQHVIIPEPLNKDRIcLGHR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 177 GHVANAIRVTGHSGHSSNPALGVNAIEVMHEVLfalMKLRDDLIKAYHHPGFDIP-------NPTLNLGHIHGGDS---- 245
Cdd:PRK13013 199 GVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVL---AEIEERLFPLLATRRTAMPvvpegarQSTLNINSIHGGEPeqdp 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 246 ------ANRICGCCELHYDVRPLPGISIDGLDNMLREALKEVEAKWPG-RIEIKPLHEPIPGYeCDHEHPFI----EGME 314
Cdd:PRK13013 276 dytglpAPCVADRCRIVIDRRFLIEEDLDEVKAEITALLERLKRARPGfAYEIRDLFEVLPTM-TDRDAPVVrsvaAAIE 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 549778073 315 RICEQPSETVnyCTEAPFLQQ-------LCPTLVLGPGSIDQAHQPDEF 356
Cdd:PRK13013 355 RVLGRQADYV--VSPGTYDQKhidrigkLKNCIAYGPGILDLAHQPDEW 401
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
37-357 |
6.89e-15 |
|
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: 75.44 E-value: 6.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 37 LATWFEDLGFETQVVEVEKGKHNLIAKMGKGEGG--LLLAGHTDTVP-FDEGRWNYDPHALTEANDRFYGLGTADMKGFF 113
Cdd:cd03893 30 LADLLRRLGFTVEIVDTSNGAPVVFAEFPGAPGAptVLLYGHYDVQPaGDEDGWDSDPFELTERDGRLYGRGAADDKGPI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 114 AFILEAVKKtdWSQQTKPLYV----LATCDEETTMLGARHFTEDAP--FKPDYCII--------GEPTSLVPIRAhkghV 179
Cdd:cd03893 110 LAHLAALRA--LMQQGGDLPVnvkfIIEGEEESGSPSLDQLVEAHRdlLAADAIVIsdstwvgqEQPTLTYGLRG----N 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 180 ANA-IRVTG-----HSGHSSNPALgvnaiEVMHEVLFALMKLRDD----LIKAYHHPGFDIPN----------------- 232
Cdd:cd03893 184 ANFdVEVKGldhdlHSGLYGGVVP-----DPMTALAQLLASLRDEtgriLVPGLYDAVRELPEeefrldagvleeveiig 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 233 -------------PTLNL----GHIHGGDSANRICGCCELHYDVRPLPGISIDGLDNMLREALKEVeAKWPGRIEIKPLH 295
Cdd:cd03893 259 gttgsvaerlwtrPALTVlgidGGFPGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLEAHLEKH-APSGAKVTVSYVE 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549778073 296 EPIPgYECDHEHPFIEGMERICEQPSET-VNYCTE------APFLQQL--CPTLVLGPGSID-QAHQPDEFL 357
Cdd:cd03893 338 GGMP-WRSDPSDPAYQAAKDALRTAYGVePPLTREggsipfISVLQEFpqAPVLLIGVGDPDdNAHSPNESL 408
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
67-284 |
1.05e-14 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 74.43 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 67 GEGGLLLAGHTDTVP-FDEGRwnydphaltEANDRFYGLGTADMKG-FFAFILEAvkktdWSQQTKPL--YVLATCDEET 142
Cdd:PRK00466 59 GEGDILLASHVDTVPgYIEPK---------IEGEVIYGRGAVDAKGpLISMIIAA-----WLLNEKGIkvMVSGLADEES 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 143 TMLGARHFTEDApFKPDYCIIGEPTSLVPIRA-HKGHVANAIRVTGHSGHSSNPALGvnaievmhevlfALMKLRDDLIK 221
Cdd:PRK00466 125 TSIGAKELVSKG-FNFKHIIVGEPSNGTDIVVeYRGSIQLDIMCEGTPEHSSSAKSN------------LIVDISKKIIE 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549778073 222 AYHHP-GFDIPN--PTLnlghIHGGDSANRICGCCELHYDVRPLPGISIDGLDNMLREALKEVEAK 284
Cdd:PRK00466 192 VYKQPeNYDKPSivPTI----IRAGESYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQECGLK 253
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
28-284 |
1.73e-14 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 74.28 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 28 EGNSEVIAKLATWFEDLGFETQVVEV-EKGKHNLIAKM-GKGEGGLLLAGHTDTVpFDEGRWNYDPhaLTEANDRFYGLG 105
Cdd:PRK06133 57 EGLKQVAALLAERLKALGAKVERAPTpPSAGDMVVATFkGTGKRRIMLIAHMDTV-YLPGMLAKQP--FRIDGDRAYGPG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 106 TADMKGFFAFILEAV---KKTDWSQQTKpLYVLATCDEETTMLGARHFTEDAPFKPDYCIIGEPT----SLVpiRAHKGH 178
Cdd:PRK06133 134 IADDKGGVAVILHALkilQQLGFKDYGT-LTVLFNPDEETGSPGSRELIAELAAQHDVVFSCEPGrakdALT--LATSGI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 179 VANAIRVTGHSGHS-SNPALGVNA-IEVMHEVLfalmKLRDdlikayhhPGFDIPNPTLNLGHIHGGDSANRICGCCELH 256
Cdd:PRK06133 211 ATALLEVKGKASHAgAAPELGRNAlYELAHQLL----QLRD--------LGDPAKGTTLNWTVAKAGTNRNVIPASASAQ 278
|
250 260
....*....|....*....|....*...
gi 549778073 257 YDVRplpgISIDGLDNMLREALKEVEAK 284
Cdd:PRK06133 279 ADVR----YLDPAEFDRLEADLQEKVKN 302
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
59-167 |
3.65e-14 |
|
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: 70.53 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 59 NLIAKMGKGEGG--LLLAGHTDTVPFDEGRWNYDPHA-LTEANDRFYGLGTADMKGFFAFILEAVK--KTDWSQQTKPLY 133
Cdd:cd03873 1 NLIARLGGGEGGksVALGAHLDVVPAGEGDNRDPPFAeDTEEEGRLYGRGALDDKGGVAAALEALKrlKENGFKPKGTIV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 549778073 134 VLATCDEETTMlGARHFT-----EDAPFKPDYCIIGEPT 167
Cdd:cd03873 81 VAFTADEEVGS-GGGKGLlskflLAEDLKVDAAFVIDAT 118
|
|
| dapE-gram_pos |
TIGR01900 |
succinyl-diaminopimelate desuccinylase; This model represents a clade of ... |
52-355 |
4.70e-14 |
|
succinyl-diaminopimelate desuccinylase; This model represents a clade of succinyl-diaminopimelate desuccinylases from actinobacteria (high-GC gram positives), delta-proteobacteria and aquificales and is based on the characterization of the enzyme from Corynebacterium glutamicum. This enzyme is involved in the biosynthesis of lysine, and is related to the enzyme acetylornithine deacetylase and other amidases and peptidases found within pfam01546. Other sequences included in the seed of this model were assessed to confirm that 1) the related genes DapC (succinyl-diaminopimelate transaminase) and DapD (2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase) are also found in the genome, 2) each is found only once in those genomes, 3) the lysine biosynthesis pathway is complete and 4) the direct (TIGR03540 or TIGR03542) or acetylated (GenProp0787) aminotransferase pathways are absent in thes genomes. Additionally, a number of the seed members are observed adjacent to either DapC or DapD (often as a divergon with a putative promoter site between them. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273864 [Multi-domain] Cd Length: 351 Bit Score: 72.70 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 52 EVEKGKHNLIAKMGKGEGG-LLLAGHTDTVPFDE---GRWNydphalteaNDRFYGLGTADMKGFFAFILEAVKKTDWSQ 127
Cdd:TIGR01900 40 EVIRHGNSVVARTNLGRPSrVILAGHLDTVPIADnlpSRVE---------GGRLYGRGAVDMKGGLAVMLALAATLDRTE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 128 QTKPL-YVLATCDE---ETTMLGarHFTEDAP--FKPDYCIIGEPTSLVPIRAHKGHVANAIRVTGHSGHSSNPALGVNA 201
Cdd:TIGR01900 111 PRHDLtLVFYEREEgpaEENGLG--RLLREHPewLAGDLAVLLEPTDGKIEAGCQGTLRATVTFHGRRAHSARSWMGENA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 202 IEVMHEVLFAL--MKLRDDLIKAYHHpgFDIPNPTLnlghIHGGDSANRICGCCELHYDVRPLPGISIDGLDNMLREALK 279
Cdd:TIGR01900 189 IHKAAPILARLaaYEPREVTVDGLTY--REGLNAVR----IEGGVAGNVIPDECEVNVNYRFAPDRSLEQARAHVRELFE 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549778073 280 EVEAKWpgriEIKPLhepIPGYECDHEHPFIEGM-ERICEQPSETVNYCTEAPFLQQLCPTLVLGPGSIDQAHQPDE 355
Cdd:TIGR01900 263 GDGAEV----EVTDL---SPGARPGLDNPLAAELvAAVGGEVRAKYGWTDVARFSALGIPAVNFGPGDPALAHQDDE 332
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
30-223 |
6.44e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 69.64 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 30 NSEVIAKLATWFEDLGF---ETQVVEVEKGKHNLIAKM-GKGEGG-LLLAGHTDTVPFDEGRWNYDPHALTEANDRFYGL 104
Cdd:PRK09133 58 TTPAAEAMAARLKAAGFadaDIEVTGPYPRKGNLVARLrGTDPKKpILLLAHMDVVEAKREDWTRDPFKLVEENGYFYGR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 105 GTADMKgFFAFILEAV----KKTDWsQQTKPLYVLATCDEE-TTMLGARHFTEDAP--FKPDYCI----------IGEPT 167
Cdd:PRK09133 138 GTSDDK-ADAAIWVATlirlKREGF-KPKRDIILALTGDEEgTPMNGVAWLAENHRdlIDAEFALneggggtldeDGKPV 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 549778073 168 SLVPIRAHKGHVANAIRVTGHSGHSSNPAlGVNAIEVMHEVL-------FALMklRDDLIKAY 223
Cdd:PRK09133 216 LLTVQAGEKTYADFRLEVTNPGGHSSRPT-KDNAIYRLAAALsrlaayrFPVM--LNDVTRAY 275
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
42-373 |
8.51e-13 |
|
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: 69.20 E-value: 8.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 42 EDLGFETQVVEvekgKHNLIAKMGKGEGGLLLAGHTDTVPFDEGrWNYDPHALTEANDRFYGLGTADMKG-----FFAfi 116
Cdd:cd03888 49 KRLGFKTKNID----NYAGYAEYGEGEEVLGILGHLDVVPAGEG-WTTDPFKPVIKDGKLYGRGTIDDKGptiaaLYA-- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 117 LEAVKKTDWsQQTKPLYVLATCDEETTMLGARHFTEDAP-----FKPD--YCII-------------------------- 163
Cdd:cd03888 122 LKILKDLGL-PLKKKIRLIFGTDEETGWKCIEHYFEHEEypdfgFTPDaeFPVIngekgivtvdltfkidddkgyrlisi 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 164 --GEPTSLVP-------IRAHKGHVANA-----------------IRVTGHSGHSSNPALGVNAIEVMHEVL------FA 211
Cdd:cd03888 201 kgGEATNMVPdkaeaviPGKDKEELALSaatdlkgnieiddggveLTVTGKSAHASAPEKGVNAITLLAKFLaelnkdGN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 212 LMKLRDDLIKAYHHPGF----------DIPNP-TLNLGHIHGGDSANricgccELHYDVRPLPGISIDgldnMLREALKE 280
Cdd:cd03888 281 DKDFIKFLAKNLHEDYNgkklginfedEVMGElTLNPGIITLDDGKL------ELGLNVRYPVGTSAE----DIIKQIEE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 281 VEAKWPGRIEIKPLHEPIpgYeCDHEHPFIEGMERICEQ----PSETV-----NYCTEAPFLQQLCPTLvlgPGSIDQAH 351
Cdd:cd03888 351 ALEKYGVEVEGHKHQKPL--Y-VPKDSPLVKTLLKVYEEqtgkEGEPVaigggTYARELPNGVAFGPEF---PGQKDTMH 424
|
410 420
....*....|....*....|..
gi 549778073 352 QPDEFLAFEFIDPTIKILDRAI 373
Cdd:cd03888 425 QANEFIPIDDLIKALAIYAEAI 446
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
33-185 |
3.20e-12 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 67.49 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 33 VIAKLATWfedlGFETQVVEvEKGKHNLIAKMGKGEGGLLLAGHTDTVPFDEGRWNYDPHALTEANDRFYGLGTADMKGF 112
Cdd:PRK08554 33 IKDTLESW----GIESELIE-KDGYYAVYGEIGEGKPKLLFMAHFDVVPVNPEEWNTEPFKLTVKGDKAYGRGSADDKGN 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 549778073 113 FAFILEAVKKTDWSQQTKPLYVLATCDEETTMLGARHFTE---DAPFKPDYCIIGEPTSLVPI-RAHKGHVAnAIRV 185
Cdd:PRK08554 108 VASVMLALKELSKEPLNGKVIFAFTGDEEIGGAMAMHIAEklrEEGKLPKYMINADGIGMKPIiRRRKGFGV-TIRV 183
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
42-276 |
6.12e-12 |
|
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: 66.53 E-value: 6.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 42 EDLGFETQVVEVEKGKHNLIAKMgkgEG------GLLLAGHTDTVPFDEGRWNYDPH-ALTEANDRFYGLGTADMKGFFA 114
Cdd:cd05646 35 DELGLPVRVIEVVPGKPVVVLTW---EGsnpelpSILLNSHTDVVPVFEEKWTHDPFsAHKDEDGNIYARGAQDMKCVGI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 115 FILEAVK--KTDWSQQTKPLYVLATCDEET-TMLGARHFTEDAPFK---PDYCI---IGEPTSLVPI----RAhKGHVan 181
Cdd:cd05646 112 QYLEAIRrlKASGFKPKRTIHLSFVPDEEIgGHDGMEKFVKTEEFKklnVGFALdegLASPTEEYRVfygeRS-PWWV-- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 182 AIRVTGHSGHSSNpALGVNAIEVMHEVLFALMKLRD-DLIKAYHHPGFDIPN-PTLNLGHIHGGDSANRICGCCELHYDV 259
Cdd:cd05646 189 VITAPGTPGHGSK-LLENTAGEKLRKVIESIMEFREsQKQRLKSNPNLTLGDvTTVNLTMLKGGVQMNVVPSEAEAGFDL 267
|
250
....*....|....*..
gi 549778073 260 RPLPGISIDGLDNMLRE 276
Cdd:cd05646 268 RIPPTVDLEEFEKQIDE 284
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
33-155 |
6.42e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 66.41 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 33 VIAKLAtwfeDLGFETQVVEVEKGKHNLIAKMgKGE----GGLLLAGHTDTVPFDEGRWNYDPHALTEANDRFYGLGTAD 108
Cdd:PRK07906 31 VAEKLA----EVGLEPTYLESAPGRANVVARL-PGAdpsrPALLVHGHLDVVPAEAADWSVHPFSGEIRDGYVWGRGAVD 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 549778073 109 MKGFFAFILEAVKktDWSQQ-TKPL--YVLA-TCDEETTM-LGARHFTEDAP 155
Cdd:PRK07906 106 MKDMDAMMLAVVR--HLARTgRRPPrdLVFAfVADEEAGGtYGAHWLVDNHP 155
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
29-291 |
7.95e-12 |
|
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: 65.93 E-value: 7.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 29 GNSEVIAK-LATWFEDLGFEtqVVEVEKGKH------NLIAKM-GKGEGG--LLLAGHTDTVpfDEGRWNYDPhalTEAN 98
Cdd:cd05683 20 LHEKEISKvLKKKFENLGLS--VIEDDAGKTtgggagNLICTLkADKEEVpkILFTSHMDTV--TPGINVKPP---QIAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 99 DRFYGLGT----ADMKGFFAFILEAVKKTDWSQ-QTKPLYVLATCDEETTMLGARHFTEDApFKPDYCII----GEPTSL 169
Cdd:cd05683 93 GYIYSDGTtilgADDKAGIAAILEAIRVIKEKNiPHGQIQFVITVGEESGLVGAKALDPEL-IDADYGYAldseGDVGTI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 170 VpIRAHKGHVANAIrVTGHSGHSS-NPALGVNAIEVMHEVLFALMKLRDDLIKayhhpgfdipnpTLNLGHIHGGDSANR 248
Cdd:cd05683 172 I-VGAPTQDKINAK-IYGKTAHAGtSPEKGISAINIAAKAISNMKLGRIDEET------------TANIGKFQGGTATNI 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 549778073 249 ICGCCELHYDVRPLPGISIDGLDNMLREALKEVEAKWPGRIEI 291
Cdd:cd05683 238 VTDEVNIEAEARSLDEEKLDAQVKHMKETFETTAKEKGAHAEV 280
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
71-212 |
1.55e-11 |
|
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: 65.35 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 71 LLLAGHTDTVP---FDEGRWNYDPHALTEANDRFYGLGTADMKGFFAFILEAV----KKTDWSQQTkpLYVLATCDEETT 143
Cdd:cd05674 72 LLLMAHQDVVPvnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVelllKRGFKPRRT--IILAFGHDEEVG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 144 -MLGARH-----------------FTEDAPFKPDYcIIGEPTSLVPIrAHKGHVANAIRVTGHSGHSSNPALGvNAIEVM 205
Cdd:cd05674 150 gERGAGAiaelllerygvdglaaiLDEGGAVLEGV-FLGVPFALPGV-AEKGYMDVEITVHTPGGHSSVPPKH-TGIGIL 226
|
....*..
gi 549778073 206 HEVLFAL 212
Cdd:cd05674 227 SEAVAAL 233
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
71-283 |
2.15e-10 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 61.52 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 71 LLLAGHTDTV-----PFDEGRWNYDphalteanDRFYGLGTADMKGFFAFILEAVKKTDWSQQTKPL-Y-VLATCDEETT 143
Cdd:PRK07338 95 VLLTGHMDTVfpadhPFQTLSWLDD--------GTLNGPGVADMKGGIVVMLAALLAFERSPLADKLgYdVLINPDEEIG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 144 MLGARHFTEDAPFKPDYCIIGEPT----SLVPIRahKGHVANAIRVTGHSGHSS-NPALGVNAIEVMHEVLFALMKLRDD 218
Cdd:PRK07338 167 SPASAPLLAELARGKHAALTYEPAlpdgTLAGAR--KGSGNFTIVVTGRAAHAGrAFDEGRNAIVAAAELALALHALNGQ 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549778073 219 LikayhhpgfdiPNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGISIDGLDNMLREALKEVEA 283
Cdd:PRK07338 245 R-----------DGVTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQ 298
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
44-319 |
4.94e-10 |
|
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: 60.58 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 44 LGFETQVVEVEKGKHNLIAKMgKGEG----GLLLAGHTDTVPFDEGRWNYDPH-ALTEANDRFYGLGTADMKGFFAFILE 118
Cdd:TIGR01880 44 LGLARKTIEFVPGKPVVVLTW-PGSNpelpSILLNSHTDVVPVFREHWTHPPFsAFKDEDGNIYARGAQDMKCVGVQYLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 119 AVKKTDwSQQTKPL---YVLATCDEET-TMLGARHFTEDAPFKpDYCI-------IGEPTSLVPI-RAHKGHVANAIRVT 186
Cdd:TIGR01880 123 AVRNLK-ASGFKFKrtiHISFVPDEEIgGHDGMEKFAKTDEFK-ALNLgfaldegLASPDDVYRVfYAERVPWWVVVTAP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 187 GHSGHSSNpALGVNAIEVMHEVLFALMKLRD---DLIKAyhHPGFDIPN-PTLNLGHIHGGDSANRICGCCELHYDVRPL 262
Cdd:TIGR01880 201 GNPGHGSK-LMENTAMEKLEKSVESIRRFREsqfQLLQS--NPDLAIGDvTSVNLTKLKGGVQSNVIPSEAEAGFDIRLA 277
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 549778073 263 PGISIDGLDNMLREALK--------EVEAKWPgrieiKPLHEPIpgyecDHEHPFIEGMERICEQ 319
Cdd:TIGR01880 278 PSVDFEEMENRLDEWCAdagegvtyEFSQHSG-----KPLVTPH-----DDSNPWWVAFKDAVKE 332
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
71-299 |
5.24e-10 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 60.73 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 71 LLLAGHTDTVPFD---EGRWNYDPHALTEANDRFYGLGTADMKGFFAFILEAVK---KTDWsQQTKPLYVLATCDEETTM 144
Cdd:PRK08262 114 IVLMAHQDVVPVApgtEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEallAQGF-QPRRTIYLAFGHDEEVGG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 145 LGARH---------------------FTEDAPfkPdycIIGEPTSLVPIrAHKGHVANAIRVTGHSGHSSNPALGvNAIE 203
Cdd:PRK08262 193 LGARAiaellkergvrlafvldeggaITEGVL--P---GVKKPVALIGV-AEKGYATLELTARATGGHSSMPPRQ-TAIG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 204 VMHEVLFAL------MKLRDDLIKAYHHPGFDIP-----------------------NPTLN--------LGHIHGGDSA 246
Cdd:PRK08262 266 RLARALTRLednplpMRLRGPVAEMFDTLAPEMSfaqrvvlanlwlfeplllrvlakSPETAamlrtttaPTMLKGSPKD 345
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 549778073 247 NRICGCCELHYDVRPLPGISIDGLDNMLREALKEveakwpGRIEIKPLH---EPIP 299
Cdd:PRK08262 346 NVLPQRATATVNFRILPGDSVESVLAHVRRAVAD------DRVEIEVLGgnsEPSP 395
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
37-120 |
1.92e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 58.77 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 37 LATWFEDLGFETQVVE--VEKGKHNLIAKMGKGEG--GLLLAGHTDTVPFDEGRWN--YDPHALTEANDRFYGLGTADMK 110
Cdd:PRK07079 50 IAPALAALGFTCRIVDnpVAGGGPFLIAERIEDDAlpTVLIYGHGDVVRGYDEQWRegLSPWTLTEEGDRWYGRGTADNK 129
|
90
....*....|....*
gi 549778073 111 G-----FFAfiLEAV 120
Cdd:PRK07079 130 GqhtinLAA--LEQV 142
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
55-375 |
2.31e-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: 58.62 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 55 KGKHNLIAKM-GKGEGGLL--LAGHTDTVPFDEGRWNYDPHALTEANDRFYGLGTADMKGFFAFILEAVKKTdwsQQTKP 131
Cdd:cd08012 62 KGRGNIIVEYpGTVDGKTVsfVGSHMDVVTANPETWEFDPFSLSIDGDKLYGRGTTDCLGHVALVTELFRQL---ATEKP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 132 ------LYVLATCDEETTMLGARHFTEDAPFKPDYCIIGePTSLV------PIRAHKGHVANAIRVTGHSGHSSNPALGV 199
Cdd:cd08012 139 alkrtvVAVFIANEENSEIPGVGVDALVKSGLLDNLKSG-PLYWVdsadsqPCIGTGGMVTWKLTATGKLFHSGLPHKAI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 200 NAIEVMHEVLfALMKLRdDLIKAYHHP-----GFDIPN---PTLnlgHIHGGDSANRICGCCELHYDVRPLPGISIDGLD 271
Cdd:cd08012 218 NALELVMEAL-AEIQKR-FYIDFPPHPkeevyGFATPStmkPTQ---WSYPGGSINQIPGECTICGDCRLTPFYDVKEVR 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 272 NMLRE-------ALKEVEAKWP------------GRIEIKPLHEPIPGYECDHEHPfieGMERICEQPSETVNYCTeaPF 332
Cdd:cd08012 293 EKLEEyvddinaNIEELPTRGPvskyvlpaeglrGRVSLEFDEAAASGVACNLDSP---GFHALCKATSEVVGYVK--PY 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 549778073 333 lqQLCPTLVL--------------GPGSIDQAHQPDEFLAFEFIDPTIKILDRAIHQ 375
Cdd:cd08012 368 --AITGSLPLirelqdegfdvqitGYGLMATYHAKNEYCLLSDFQNGFKVLARTIAQ 422
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
41-123 |
5.01e-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.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 54.43 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 41 FEDLGFETQVVE--VEKGKHNLIAKmgKGEGG----LLLAGHTDTVPFDEGRWN--YDPHALTEANDRFYGLGTADMKGF 112
Cdd:cd05679 41 FERLGFTVHIHDnpVAGRAPFLIAE--RIEDPslptLLIYGHGDVVPGYEGRWRdgRDPWTVTVWGERWYGRGTADNKGQ 118
|
90
....*....|.
gi 549778073 113 FAFILEAVKKT 123
Cdd:cd05679 119 HSINMAALRQV 129
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
66-254 |
3.36e-07 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 51.71 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 66 KGEGGLLLAGHTDTV----PFDEGRWNYDphalteaNDRFYGLGTADMKGFFAFILEAVKKTDWSQQTKPL--YVLATCD 139
Cdd:PRK07473 73 QGEPGILIAGHMDTVhpvgTLEKLPWRRE-------GNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLpiTVLFTPD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 140 EETTMLGARHFTEDAPFKPDYCIIGEPTslvpiRAHKGHVAN--AI-----RVTGHSGHS-SNPALGVNAIEVMHEVLFA 211
Cdd:PRK07473 146 EEVGTPSTRDLIEAEAARNKYVLVPEPG-----RPDNGVVTGryAIarfnlEATGRPSHAgATLSEGRSAIREMARQILA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 549778073 212 LMKLRDDlikayhhpgfdipNPTLNLGHIHGGDSANRICGCCE 254
Cdd:PRK07473 221 IDAMTTE-------------DCTFSVGIVHGGQWVNCVATTCT 250
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
42-121 |
5.20e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 51.23 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 42 EDLGFETqvVEVEKGKHNLiAKMGKGEGGLLLAGHTDTVPF-DEGRWNYDPHALTEANDRFYGLGTADMKGFFAFILEAV 120
Cdd:PRK07205 52 QGLGFKT--YLDPKGYYGY-AEIGQGEELLAILCHLDVVPEgDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAV 128
|
.
gi 549778073 121 K 121
Cdd:PRK07205 129 K 129
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
28-217 |
5.39e-07 |
|
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: 51.19 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 28 EGNSEVIAKLATWFEDLGFEtqvVEVEKGKHNLIAKMGKGEGG---LLLAGHTDTVPFDE-GRWNYDPHALTEANDRFYG 103
Cdd:cd05681 19 RGIPETADFLKEFLRRLGAE---VEIFETDGNPIVYAEFNSGDaktLLFYNHYDVQPAEPlELWTSDPFELTIRNGKLYA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 104 LGTADMKGFFAFILEAVKKtdWSQQTKPLYV----LATCDEETTMLGARHFTEDAP--FKPDYCI-----IGEPTSLVPI 172
Cdd:cd05681 96 RGVADDKGELMARLAALRA--LLQHLGELPVnikfLVEGEEEVGSPNLEKFVAEHAdlLKADGCIwegggKNPKGRPQIS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 549778073 173 RAHKGHVANAIRVTGHSG--HSSNPALGVNAIevmHEVLFALMKLRD 217
Cdd:cd05681 174 LGVKGIVYVELRVKTADFdlHSSYGAIVENPA---WRLVQALNSLRD 217
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
183-299 |
1.06e-06 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 50.29 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 183 IRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIKAyHHPGfdipnpTLNLGHIHGGDSANRICGCCELHYDVRPL 262
Cdd:cd03886 176 ITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVVSRELDP-LEPA------VVTVGKFHAGTAFNVIPDTAVLEGTIRTF 248
|
90 100 110
....*....|....*....|....*....|....*..
gi 549778073 263 PGISIDGLDNMLREALKEVEAKWPGRIEIKPLHEPIP 299
Cdd:cd03886 249 DPEVREALEARIKRLAEGIAAAYGATVELEYGYGYPA 285
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
26-121 |
1.85e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 49.52 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 26 WDEGNSEVIAKLATW----FEDLGFETQVVEVEKGKHNLIAKMGKGEGG--LLLAGHTDTVP-FDEGRWNYDPHALTEAN 98
Cdd:PRK07907 35 ADPFRREEVARSAEWvadlLREAGFDDVRVVSADGAPAVIGTRPAPPGAptVLLYAHHDVQPpGDPDAWDSPPFELTERD 114
|
90 100
....*....|....*....|...
gi 549778073 99 DRFYGLGTADMKGFFAFILEAVK 121
Cdd:PRK07907 115 GRLYGRGAADDKGGIAMHLAALR 137
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
37-123 |
5.65e-06 |
|
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.
Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 47.98 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 37 LATWFEDLGFETQVVEVEKGKHN----------LIAKMGK--GEGGLLLAGHTDTVPFD-EGRWNYDPHALTEANDRFYG 103
Cdd:cd05676 42 AAERLEKLGFKVELVDIGTQTLPdgeelplppvLLGRLGSdpSKKTVLIYGHLDVQPAKlEDGWDTDPFELTEKDGKLYG 121
|
90 100
....*....|....*....|...
gi 549778073 104 LGTADMKG-FFAFI--LEAVKKT 123
Cdd:cd05676 122 RGSTDDKGpVLGWLnaIEAYQKL 144
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
54-219 |
5.48e-05 |
|
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: 45.03 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 54 EKGKHNLIAKMgKGEGG----LLLAGHTDTVPFDE-GRWN---YDPHALTEA------------------NDRFYGLGTA 107
Cdd:cd05654 54 DLGRRNVTALV-KGKKPskrtIILISHFDTVGIEDyGELKdiaFDPDELTKAfseyveeldeevredllsGEWLFGRGTM 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 108 DMKG----FFAFILEAVKKTDWSQQtkpLYVLATCDEETT---MLGARHFTEDAPFKPDYCIIGEPTSLVPIRAHKGHVA 180
Cdd:cd05654 133 DMKSglavHLALLEQASEDEDFDGN---LLLMAVPDEEVNsrgMRAAVPALLELKKKHDLEYKLAINSEPIFPQYDGDQT 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 549778073 181 NAIR------------VTGHSGHSSNPALGVNAIEVMHEVLfALMKLRDDL 219
Cdd:cd05654 210 RYIYtgsigkilpgflCYGKETHVGEPFAGINANLMASEIT-ARLELNADL 259
|
|
| Peptidase_M28 |
pfam04389 |
Peptidase family M28; |
59-157 |
4.64e-04 |
|
Peptidase family M28;
Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 40.73 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 59 NLIAKM--GKGEGGLLLAGHTDTVPFDEGrwnydphalteANDRfyGLGTAdmkgffaFILEAVKK-TDWSQQTKPLYVL 135
Cdd:pfam04389 1 NVIAKLpgKAPDEVVLLSAHYDSVGTGPG-----------ADDN--ASGVA-------ALLELARVlAAGQRPKRSVRFL 60
|
90 100
....*....|....*....|..
gi 549778073 136 ATCDEETTMLGARHFTEDAPFK 157
Cdd:pfam04389 61 FFDAEEAGLLGSHHFAKSHPPL 82
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
28-217 |
1.71e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 40.12 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 28 EGNSEVIAKLATWFEDLGFETQVVEvEKGKHNLIAKMGKG-EGGLLLAGHTDTVPFDE-GRWNYDPHALTEANDRFYGLG 105
Cdd:PRK06446 22 EGIEETANYLKDTMEKLGIKANIER-TKGHPVVYGEINVGaKKTLLIYNHYDVQPVDPlSEWKRDPFSATIENGRIYARG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 106 TADMKG-----FFAfILEAVKKTDWSQQTKPLYvlaTCDEETTMLGARHFTEDAPFKP--DYCII--------GEPTSLV 170
Cdd:PRK06446 101 ASDNKGtlmarLFA-IKHLIDKHKLNVNVKFLY---EGEEEIGSPNLEDFIEKNKNKLkaDSVIMegagldpkGRPQIVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 549778073 171 PIrahKGHVANAIRV-TGHSG-HSSNPALGVNAIevmHEVLFALMKLRD 217
Cdd:PRK06446 177 GV---KGLLYVELVLrTGTKDlHSSNAPIVRNPA---WDLVKLLSTLVD 219
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
183-292 |
2.39e-03 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of uncharacterized bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349936 [Multi-domain] Cd Length: 371 Bit Score: 39.56 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 183 IRVTGHSGHSSNPALGVNAIEVMHEVLFALMKLRDDLIKAYHhpgfdipnPT-LNLGHIHGGDSANRICGCCELHYDVRP 261
Cdd:cd08014 175 IRIQGEGGHGARPHLTVDLVWAAAQVVTDLPQAISRRIDPRS--------PVvLTWGSIEGGRAPNVIPDSVELSGTVRT 246
|
90 100 110
....*....|....*....|....*....|.
gi 549778073 262 LPGISIDGLDNMLREALKEVEAKWPGRIEIK 292
Cdd:cd08014 247 LDPDTWAQLPDLVEEIVAGICAPYGAKYELE 277
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
183-260 |
7.87e-03 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 38.02 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549778073 183 IRVTGHSGHSSNPALGVNAIEVMHEVLFALMKL---RDDLIKAyhhpgfdipnPTLNLGHIHGGDSANRICGCCELHYDV 259
Cdd:cd08021 186 ITIKGKGGHGSMPHETVDPIVIAAQIVTALQTIvsrRVDPLDP----------AVVTIGTFQGGTSFNVIPDTVELKGTV 255
|
.
gi 549778073 260 R 260
Cdd:cd08021 256 R 256
|
|
| |
