|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
1-379 |
0e+00 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 754.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 1 MKQIP-FIQRYAQLIELPTISSLVAEEDLSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYGEGEGGLLLAGHT 79
Cdd:PRK05111 1 KMKLPsFIEMYRALIATPSISATDPALDQSNRAVIDLLAGWFEDLGFNVEIQPVPGTRGKFNLLASLGSGEGGLLLAGHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 80 DTVPFDEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSHIR 159
Cdd:PRK05111 81 DTVPFDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAEATAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 160 PDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLFQVTHPTMNF 239
Cdd:PRK05111 161 PDCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQERYHNPAFTVPYPTLNL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 240 GNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGIPGYECEHSAQIVQVVEKLL 319
Cdd:PRK05111 241 GHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSERWPGRITVAPLHPPIPGYECPADHQLVRVVEKLL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493292681 320 GEKCDAVNYCTEAPFIQQL-CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLIYHFC 379
Cdd:PRK05111 321 GHKAEVVNYCTEAPFIQQLgCPTLVLGPGSIEQAHQPDEYLELSFIKPTRELLRQLIHHFC 381
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
10-375 |
4.18e-164 |
|
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: 463.99 E-value: 4.18e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 10 YAQLIELPTISSLvaeedlSNRRLIELLATWLADFGFKTEILAVEGsRNKYNLLATYG-EGEGGLLLAGHTDTVPFDEGK 88
Cdd:cd03894 3 LARLVAFDTVSRN------SNLALIEYVADYLAALGVKSRRVPVPE-GGKANLLATLGpGGEGGLLLSGHTDVVPVDGQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 89 WRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSH---IRPDCAII 165
Cdd:cd03894 76 WSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALAargGRPDAAIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 166 GEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLFQVTHPTMNFGNIHGG 245
Cdd:cd03894 156 GEPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPFDPPYPTLNVGLIHGG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 246 DAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGiPGYECEHSAQIVQVVEKLLGE-KCD 324
Cdd:cd03894 236 NAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPEAGIEVEPLFEV-PGLETDEDAPLVRLAAALAGDnKVR 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 493292681 325 AVNYCTEAPFIQQL-CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:cd03894 315 TVAYGTEAGLFQRAgIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLI 366
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
10-375 |
3.64e-153 |
|
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: 436.17 E-value: 3.64e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 10 YAQLIELPTISSLvaeedlSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYG-EGEGGLLLAGHTDTVPFDEGK 88
Cdd:TIGR01892 3 LTKLVAFDSTSFR------PNVDLIDWAQAYLEALGFSVEVQPFPDGAEKSNLVAVIGpSGAGGLALSGHTDVVPYDDAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 89 WRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSHIRPDCAIIGEP 168
Cdd:TIGR01892 77 WTRDPFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIEAGAGRPRHAIIGEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 169 TSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLFQVTHPTMNFGNIHGGDAI 248
Cdd:TIGR01892 157 TRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDLDEGFTPPYTTLNIGVIQGGKAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 249 NRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQY-GDLIEIRhLHDGIPGYECEHSAQIVQVVEKLLGEKCDAVN 327
Cdd:TIGR01892 237 NIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRDEpGFEVQIE-VVSTDPGVNTEPDAELVAFLEELSGNAPEVVS 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 493292681 328 YCTEAPFIQQL-CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:TIGR01892 316 YGTEAPQFQELgAEAVVCGPGDIRQAHQPDEYVEIEDLVRCRAVLARLV 364
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
6-380 |
8.90e-108 |
|
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: 321.45 E-value: 8.90e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 6 FIQRYAQLIELPTISslvaeedLSNRRLIELLATWLADFGFKTEILAVEGSRnkYNLLATY--GEGEGGLLLAGHTDTVP 83
Cdd:COG0624 14 ALELLRELVRIPSVS-------GEEAAAAELLAELLEALGFEVERLEVPPGR--PNLVARRpgDGGGPTLLLYGHLDVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 84 FDEG-KWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLT--QIKKPIRILATADEETTMLGARTFAQH--SHI 158
Cdd:COG0624 85 PGDLeLWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAglRLPGNVTLLFTGDEEVGSPGARALVEElaEGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 159 RPDCAIIGEPTS-LKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREkyhNPLFQvtHPTM 237
Cdd:COG0624 165 KADAAIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRA---DPLFG--RTTL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 238 NFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPmlEQYGDLIEIRHLHDGIPGYECEHSAQIVQVVEK 317
Cdd:COG0624 240 NVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAA--AAPGVEVEVEVLGDGRPPFETPPDSPLVAAARA 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493292681 318 LLGE------KCDAVNYCTEAPFIQQL--CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLIYHFCG 380
Cdd:COG0624 318 AIREvtgkepVLSGVGGGTDARFFAEAlgIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
11-361 |
4.18e-95 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 289.01 E-value: 4.18e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 11 AQLIELPTISslvaeeDLSNRRLIELLATWLADFGFKTEILAVEgSRNKYNLLATYG-EGEGGLLLAGHTDTVPFDEGKW 89
Cdd:PRK07522 11 ERLVAFDTVS------RDSNLALIEWVRDYLAAHGVESELIPDP-EGDKANLFATIGpADRGGIVLSGHTDVVPVDGQAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 90 RFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSH---IRPDCAIIG 166
Cdd:PRK07522 84 TSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPSMIARLPergVKPAGCIVG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 167 EPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYH-NPLFQVTHPTMNFGNIHGG 245
Cdd:PRK07522 164 EPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLAAPGPfDALFDPPYSTLQTGTIQGG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 246 DAINRICACCELQFDMRPLPNMAVQDLYA----MVNEHLKPMLEQYGDLIEIR-HLHDGIPGYECEHSAQIVQVVEKLLG 320
Cdd:PRK07522 244 TALNIVPAECEFDFEFRNLPGDDPEAILAriraYAEAELLPEMRAVHPEAAIEfEPLSAYPGLDTAEDAAAARLVRALTG 323
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 493292681 321 -EKCDAVNYCTEAPFIQQL-CPTLVLGPGSIEQAHQPDEFLEM 361
Cdd:PRK07522 324 dNDLRKVAYGTEAGLFQRAgIPTVVCGPGSIEQAHKPDEFVEL 366
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
12-375 |
1.18e-81 |
|
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: 253.76 E-value: 1.18e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 12 QLIELPTISSlvAEEDLSnrrliELLATWLADFGFKTEilaVEGSRNKYNLLATYGEGEG-GLLLAGHTDTVPF-DEGKW 89
Cdd:cd08659 5 DLVQIPSVNP--PEAEVA-----EYLAELLAKRGYGIE---STIVEGRGNLVATVGGGDGpVLLLNGHIDTVPPgDGDKW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 90 RFNPFQLTEKAGKLYGLGTADMK-GFFAFVVEVVSQLDLTQIKK-PIRILATADEETTMLGARTFAQHSHI-RPDCAIIG 166
Cdd:cd08659 75 SFPPFSGRIRDGRLYGRGACDMKgGLAAMVAALIELKEAGALLGgRVALLATVDEEVGSDGARALLEAGYAdRLDALIVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 167 EPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMhqsIGYLMKMRDELREKYHNPLFqvTHPTMNFGNIHGGD 246
Cdd:cd08659 155 EPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYAL---ADFLAELRTLFEELPAHPLL--GPPTLNVGVINGGT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 247 AINRICACCELQFDMRPLPNMAVQDLYAMVNEHlkpmLEQYGDLIEIRHLHDGIPGYECEHSAQIVQVVEKLLGEKCDA- 325
Cdd:cd08659 230 QVNSIPDEATLRVDIRLVPGETNEGVIARLEAI----LEEHEAKLTVEVSLDGDPPFFTDPDHPLVQALQAAARALGGDp 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 493292681 326 ----VNYCTEAPFIQQL--CPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:cd08659 306 vvrpFTGTTDASYFAKDlgFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
74-377 |
4.35e-62 |
|
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: 201.81 E-value: 4.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 74 LLAGHTDTVPfDEGKWRFnPFQLTEKaGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKK-PIRILATADEETTMLGARTF 152
Cdd:pfam01546 1 LLRGHMDVVP-DEETWGW-PFKSTED-GKLYGRGHDDMKGGLLAALEALRALKEEGLKKgTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 153 AQ---HSHIRPDCAI---IGEPTSL------KPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDE 220
Cdd:pfam01546 78 IEdglLEREKVDAVFglhIGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 221 LREKYHNPLFQVThptmNFGNIHGGdaINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGI 300
Cdd:pfam01546 158 NVDPLDPAVVTVG----NITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEYVEGGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 301 PgYECEHS---AQIVQVVEKLLGEKCD----AVNYCTEAPFIQQ-LCPTLV-LGPGSiEQAHQPDEFLEMKYIEPTKELL 371
Cdd:pfam01546 232 P-PLVNDSplvAALREAAKELFGLKVElivsGSMGGTDAAFFLLgVPPTVVfFGPGS-GLAHSPNEYVDLDDLEKGAKVL 309
|
....*.
gi 493292681 372 TKLIYH 377
Cdd:pfam01546 310 ARLLLK 315
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
12-375 |
5.37e-60 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 198.68 E-value: 5.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 12 QLIELPTisslVAEEDLSNRRLIELLATWLADFGFKTEILAVEGS------RNKYNLLATYGEGEGGLLLAGHTDTVPFD 85
Cdd:PRK08651 14 DLIKIPT----VNPPGENYEEIAEFLRDTLEELGFSTEIIEVPNEyvkkhdGPRPNLIARRGSGNPHLHFNGHYDVVPPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 86 EGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDlTQIKKPIRILATADEETTMLGARTFAQHSHIRPDCAII 165
Cdd:PRK08651 90 EGWSVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLD-PAGDGNIELAIVPDEETGGTGTGYLVEEGKVTPDYVIV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 166 GEPTSLKPI-RAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLFQVTHPTMNFGN--I 242
Cdd:PRK08651 169 GEPSGLDNIcIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYEYDDERGAKPTVTLGGptV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 243 HGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLhDGIPGYECEHSAQIVQVVEKLLGEK 322
Cdd:PRK08651 249 EGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFEIT-PFSEAFVTDPDSELVKALREAIREV 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 323 --CDAVNYC----TEA-PFIQQLCPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:PRK08651 328 lgVEPKKTIslggTDArFFGAKGIPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVL 387
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
7-373 |
4.54e-54 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 182.78 E-value: 4.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 7 IQRYAQLIELPTISSlvAEEDLSNrrlieLLATWLADFGFKTEILAVEGSRNkyNLLATYGEGEGGLLLAGHTDTV-PFD 85
Cdd:PRK08588 5 IQILADIVKINSVND--NEIEVAN-----YLQDLFAKHGIESKIVKVNDGRA--NLVAEIGSGSPVLALSGHMDVVaAGD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 86 EGKWRFNPFQLTEKAGKLYGLGTADMK-GFFAFVV---EVVSQLDLTQIKkpIRILATADEETTMLGARTFAQH---SHI 158
Cdd:PRK08588 76 VDKWTYDPFELTEKDGKLYGRGATDMKsGLAALVIamiELKEQGQLLNGT--IRLLATAGEEVGELGAKQLTEKgyaDDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 159 rpDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIElmhqsigYLMKMRDELREKY-----HNPLFQVT 233
Cdd:PRK08588 154 --DALIIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAID-------PLLEFYNEQKEYFdsikkHNPYLGGL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 234 hpTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGIPGYECEHS--AQI 311
Cdd:PRK08588 225 --THVVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNQNGAAQLSLDIYSNHRPVASDKDSklVQL 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493292681 312 VQ-VVEKLLGEKCD--AVNYCTEA----------PFIqqlcptlVLGPGSIEQAHQPDEFLE----MKYIEPTKELLTK 373
Cdd:PRK08588 303 AKdVAKSYVGQDIPlsAIPGATDAssflkkkpdfPVI-------IFGPGNNLTAHQVDEYVEkdmyLKFIDIYKEIIIQ 374
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
41-375 |
1.30e-47 |
|
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: 165.25 E-value: 1.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 41 LADFGFKTEIlaVEGSRNKYNLLATYGEGEGG--LLLAGHTDTVPFDEGK-WRFNPFQLTEKAGKLYGLGTADMKGFFAF 117
Cdd:cd08011 31 LEDLGYPVEL--HEPPEEIYGVVSNIVGGRKGkrLLFNGHYDVVPAGDGEgWTVDPYSGKIKDGKLYGRGSSDMKGGIAA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 118 VVEVVSQL--DLTQIKKPIRILATADEETT-MLGARTFAQHSHIRPDCAIIGEPTSLKPIR-AHKGHIGESVRITGRSGH 193
Cdd:cd08011 109 SIIAVARLadAKAPWDLPVVLTFVPDEETGgRAGTKYLLEKVRIKPNDVLIGEPSGSDNIRiGEKGLVWVIIEITGKPAH 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 194 SSDPAKGINAIELmhqsigyLMKMRDELREkyhnplfqvTHPTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLY 273
Cdd:cd08011 189 GSLPHRGESAVKA-------AMKLIERLYE---------LEKTVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 274 AMVNEHLKPMLEQYGdliEIRHLHDgipGYECEHSAQIVQVVE----KLLGEKcdAVNYCTEAP-----FIQQLCPTLVL 344
Cdd:cd08011 253 SRIIDHLDSIEEVSF---EIKSFYS---PTVSNPDSEIVKKTEeaitEVLGIR--PKEVISVGAsdarfYRNAGIPAIVY 324
|
330 340 350
....*....|....*....|....*....|.
gi 493292681 345 GPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:cd08011 325 GPGRLGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
7-368 |
7.04e-46 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 161.41 E-value: 7.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 7 IQRYAQLIELPTISS-LVAEEDLSNrrlieLLATWLADFGFKTEILAVEGSR-NKYNLLATYGEGEGG---LLLAGHTDT 81
Cdd:TIGR01910 1 VELLKDLISIPSVNPpGGNEETIAN-----YIKDLLREFGFSTDVIEITDDRlKVLGKVVVKEPGNGNeksLIFNGHYDV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 82 VPF-DEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKP--IRILATADEETTMLGARTFAQHS-H 157
Cdd:TIGR01910 76 VPAgDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNgnIILQSVVDEESGEAGTLYLLQRGyF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 158 IRPDCAIIGEPTSLKPI-RAHKGHIGESVRITGRSGHSSDPAKGINAIE-LMHqsigYLMKMRDELREKY--HNPLFQVT 233
Cdd:TIGR01910 156 KDADGVLIPEPSGGDNIvIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMkLAK----LITELNELEEHIYarNSYGFIPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 234 HPTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDlyamVNEHLKPMLEQYGDLIEIRHLHD-----GIPGYECEHS 308
Cdd:TIGR01910 232 PITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDE----VKQIIEDVVKALSKSDGWLYENEpvvkwSGPNETPPDS 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493292681 309 AQIVQ---VVEKLLGE--KCDAVNYCTEAPF-IQQLCPTLVLGPGSIEQAHQPDEFLEMK-YIEPTK 368
Cdd:TIGR01910 308 RLVKAleaIIKKVRGIepEVLVSTGGTDARFlRKAGIPSIVYGPGDLETAHQVNEYISIKnLVESTK 374
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-359 |
4.23e-37 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 137.02 E-value: 4.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 6 FIQRYAQLIELPTISSlvAEEDLSnrrliELLATWLADFGFKTEILAVEGSrNKYNLLATYGEGEG-GLLLAGHTDTVPf 84
Cdd:cd05652 1 LLSLHKSLVEIPSISG--NEAAVG-----DFLAEYLESLGFTVEKQPVENK-DRFNVYAYPGSSRQpRVLLTSHIDTVP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 85 degkwRFNPFQLTEKAGKLYGLGTADMKGFFAfvVEVVSQLDLTQIKK----PIRILATADEETTMLGARTFAQHSHIRP 160
Cdd:cd05652 72 -----PFIPYSISDGGDTIYGRGSVDAKGSVA--AQIIAVEELLAEGEvpegDLGLLFVVGEETGGDGMKAFNDLGLNTW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 161 DCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNplfqvthPTMNFG 240
Cdd:cd05652 145 DAVIFGEPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPSSELLGP-------TTLNIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 241 NIHGGDAINRICACCE--LQFDMRPLPNMAVQDLYAMVNEHLKPmleqyGDLIEIRHLHDGIPGY-ECEhsaqivqvVEk 317
Cdd:cd05652 218 RISGGVAANVVPAAAEasVAIRLAAGPPEVKDIVKEAVAGILTD-----TEDIEVTFTSGYGPVDlDCD--------VD- 283
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 493292681 318 llGEKCDAVNYCTEAPFIQQLCPTLVLGPGSIEQAHQPDEFL 359
Cdd:cd05652 284 --GFETDVVAYGTDIPYLKGDHKRYLYGPGSILVAHGPDEAI 323
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
45-365 |
6.25e-37 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 137.25 E-value: 6.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 45 GFKTEIlaVEGSRNKYNLLATYGEGEggLLLAGHTDTVPfDEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQ 124
Cdd:PRK08737 42 GFQVEV--IDHGAGAVSLYAVRGTPK--YLFNVHLDTVP-DSPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 125 LDltqikKPIRILATADEET-TMLGARTFAQHSHiRPDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDP-AKGIN 202
Cdd:PRK08737 117 GD-----GDAAFLFSSDEEAnDPRCVAAFLARGI-PYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKqDPSAS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 203 AIelmHQSIGYLMKMRDELREKYHNPLFQVTHPTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKP 282
Cdd:PRK08737 191 AL---HQAMRWGGQALDHVESLAHARFGGLTGLRFNIGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFAGFAEP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 283 MLEQYGDLIEIRHLHDGIPGYECEHSAQIVQVVEKLLGEKCDAVNYCTEAP-FIQQLCPTLVLGPGSIEQAHQPDEFLEM 361
Cdd:PRK08737 268 AAATFEETFRGPSLPSGDIARAEERRLAARDVADALDLPIGNAVDFWTEASlFSAAGYTALVYGPGDIAQAHTADEFVTL 347
|
....
gi 493292681 362 KYIE 365
Cdd:PRK08737 348 DQLQ 351
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
12-378 |
1.48e-34 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 130.26 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 12 QLIELPTISslvAEEDlsnrRLIELLATWLADFGFKTEIlavEGSRNKYNLLAtygEGEGGLLLAGHTDTVPFdegkwRF 91
Cdd:PRK08652 10 QLVKIPSPS---GQED----EIALHIMEFLESLGYDVHI---ESDGEVINIVV---NSKAELFVEVHYDTVPV-----RA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 92 NPFqltEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEETTMLGARTFAqhSHIRPDCAIIGEPTSL 171
Cdd:PRK08652 72 EFF---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSDEEEGGRGSALFA--ERYRPKMAIVLEPTDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 172 KPIRAHKGHIGESVRITGRSGHSSDPAKGINAIElmhQSIGYLMKMRDELREKyhNPLFQvthPTMNFGNIHGGDAINRI 251
Cdd:PRK08652 147 KVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIE---KAFEMLEKLKELLKAL--GKYFD---PHIGIQEIIGGSPEYSI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 252 CACCELQFDMRPLPNMAVQDlyamVNEHLKPMLEQYGDLIEIRHLHDgipGYECEHSAQIVQVVEKLLGEK--------- 322
Cdd:PRK08652 219 PALCRLRLDARIPPEVEVED----VLDEIDPILDEYTVKYEYTEIWD---GFELDEDEEIVQLLEKAMKEVglepeftvm 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 493292681 323 ---CDAVNycteapFIQQLCPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLIYHF 378
Cdd:PRK08652 292 rswTDAIN------FRYNGTKTVVWGPGELDLCHTKFERIDVREVEKAKEFLKALNEIL 344
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
57-380 |
2.89e-34 |
|
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: 130.51 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 57 RNKYNLLATY-GEGEGG--LLLAGHTDTVPFDEGK-WRFNPFQLTEKAGKLYGLGTADMKG-----FFAFvvEVVSQLDL 127
Cdd:cd03895 58 AGAPNVVGTHrPRGETGrsLILNGHIDVVPEGPVElWTRPPFEATIVDGWMYGRGAGDMKAglaanLFAL--DALRAAGL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 128 tQIKKPIRILATADEETTMLGARTFAQHSHiRPDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELM 207
Cdd:cd03895 136 -QPAADVHFQSVVEEECTGNGALAALMRGY-RADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 208 HQSIGYLMKMRDELREKYH-NPLF-QVTHP-TMNFGNIHGGDAINRICACCElqFDMRP--LPNMAVQDLYAMVNEHLK- 281
Cdd:cd03895 214 MHLIQALQELEREWNARKKsHPHFsDHPHPiNFNIGKIEGGDWPSSVPAWCV--LDCRIgiYPGESPEEARREIEECVAd 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 282 ------------PMLEQYGDLIEirhlhdgipGYECEHSAQIVQVV----EKLLGEKCD--AVNYCTEAPFIQQL--CPT 341
Cdd:cd03895 292 aaatdpwlsnhpPEVEWNGFQAE---------GYVLEPGSDAEQVLaaahQAVFGTPPVqsAMTATTDGRFFVLYgdIPA 362
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 493292681 342 LVLGPGSiEQAHQPDEFLEMKYI-EPTKELLTkLIYHFCG 380
Cdd:cd03895 363 LCYGPGS-RDAHGFDESVDLESLrKITKTIAL-FIAEWCG 400
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
21-379 |
3.63e-34 |
|
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: 129.90 E-value: 3.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 21 SLVAEEDLSNRRLIELLATWLADFGFKTEILavEGSRNKYNLLATYgEGEGG---LLLAGHTDTVPFDegKWRFNPFQLT 97
Cdd:cd08013 19 SLSATGGAGEAEIATYVAAWLAHRGIEAHRI--EGTPGRPSVVGVV-RGTGGgksLMLNGHIDTVTLD--GYDGDPLSGE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 98 EKAGKLYGLGTADMKGFFAfvVEVVSQLDLTqiKKPIR---ILA-TADEETTMLGARTFAQHShIRPDCAIIGEPTSLKP 173
Cdd:cd08013 94 IADGRVYGRGTLDMKGGLA--ACMAALADAK--EAGLRgdvILAaVADEEDASLGTQEVLAAG-WRADAAIVTEPTNLQI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 174 IRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLfqVTHPTMNFGNIHGGDAINRICA 253
Cdd:cd08013 169 IHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALEEYQQELPERPVDPL--LGRASVHASLIKGGEEPSSYPA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 254 CCELQFDMRPLP----NMAVQDLYAMVNEhLKPMLEQYGDLIEIRHLHDgiPGYECEHSAQIVQVV----EKLLGEKC-- 323
Cdd:cd08013 247 RCTLTIERRTIPgetdESVLAELTAILGE-LAQTVPNFSYREPRITLSR--PPFEVPKEHPFVQLVaahaAKVLGEAPqi 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 493292681 324 DAVNYCTEAPFIQQL-CPTLVLGPgSIEQAHQPDEFLEMKYIEPTKELLTKLIYHFC 379
Cdd:cd08013 324 RSETFWTDAALLAEAgIPSVVFGP-SGAGLHAKEEWVDVESIRQLREVLSAVVREFC 379
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
32-375 |
8.85e-34 |
|
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: 128.48 E-value: 8.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 32 RLIELLATWLADFGFKTEILAVEGSRNkyNLLATY-GEGEGGLLLAGHTDTVpFDEGKWRFNPFqlTEKAGKLYGLGTAD 110
Cdd:cd03885 23 RVAELLAEELEALGFTVERRPLGEFGD--HLIATFkGTGGKRVLLIGHMDTV-FPEGTLAFRPF--TVDGDRAYGPGVAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 111 MKGFFAFVVEVVSQLDLTQIKK--PIRILATADEETTMLGARTFAQHSHIRPDCAIIGEPTSL--KPIRAHKGHIGESVR 186
Cdd:cd03885 98 MKGGLVVILHALKALKAAGGRDylPITVLLNSDEEIGSPGSRELIEEEAKGADYVLVFEPARAdgNLVTARKGIGRFRLT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 187 ITGRSGHSS-DPAKGINAI-ELMHQSIGyLMKMRDELRekyhnplfqvtHPTMNFGNIHGGDAINRICACCELQFDMRpL 264
Cdd:cd03885 178 VKGRAAHAGnAPEKGRSAIyELAHQVLA-LHALTDPEK-----------GTTVNVGVISGGTRVNVVPDHAEAQVDVR-F 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 265 PNMA-----VQDLYAMVNEHLKPMLEqygdlIEIRHLHDGIPGYECEHSAQIVQVVEKL---LGEKCD--AVNYCTEAPF 334
Cdd:cd03885 245 ATAEeadrvEEALRAIVATTLVPGTS-----VELTGGLNRPPMEETPASRRLLARAQEIaaeLGLTLDweATGGGSDANF 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 493292681 335 IQQL-CPTL-VLGP-GsiEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:cd03885 320 TAALgVPTLdGLGPvG--GGAHTEDEYLELDSLVPRIKLLARLL 361
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
34-357 |
1.78e-32 |
|
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: 124.92 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 34 IELLATWLADFGFKTEILAVEGSRNkynLLATYGEGEGGLLLAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGLGTADMK 112
Cdd:cd03891 21 QDLIAERLKALGFTCERLEFGGVKN---LWARRGTGGPHLCFAGHTDVVPPgDLEGWSSDPFSPTIKDGMLYGRGAADMK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 113 G----FFAFVVEVVSQLDltQIKKPIRILATADEETTML-GART---FAQHSHIRPDCAIIGEPTSLKpirahkgHIGES 184
Cdd:cd03891 98 GgiaaFVAAAERFVAKHP--NHKGSISFLITSDEEGPAIdGTKKvleWLKARGEKIDYCIVGEPTSEK-------KLGDT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 185 VRI------------TGRSGHSSDPAKGINAIELMHQSIGYLMKMR-DElrekyHNPLFQVThpTMNFGNIHGG-DAINR 250
Cdd:cd03891 169 IKIgrrgslngkltiKGKQGHVAYPHLADNPIHLLAPILAELTATVlDE-----GNEFFPPS--SLQITNIDVGnGATNV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 251 ICACCELQFDMRPLPNMAVQDLYAMVNEHLKpmleQYGDLIEIRHLHDG-----IPGyecEHSAQIVQVVEKLLGekcda 325
Cdd:cd03891 242 IPGELKAKFNIRFNDEHTGESLKARIEAILD----KHGLDYDLEWKLSGepfltKPG---KLVDAVSAAIKEVTG----- 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 493292681 326 vnYCTE---------APFIQQL-CPTLVLGPGSiEQAHQPDE 357
Cdd:cd03891 310 --ITPElstsggtsdARFIASYgCPVVEFGLVN-ATIHKVNE 348
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-375 |
4.83e-29 |
|
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: 115.10 E-value: 4.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 13 LIELPTISSlvaEEDlsnrRLIELLATWLADFGFKTEilavegsRNKYNLLA---TYGEGEGGLLLAGHTDTVPFDEGkW 89
Cdd:cd05651 9 LIATPSFSR---EEH----KTADLIENYLEQKGIPFK-------RKGNNVWAengHFDEGKPTLLLNSHHDTVKPNAG-W 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 90 RFNPFQLTEKAGKLYGLGTADMKGffafvvEVVSQL-------DLTQIKKPIRILATADEETT-MLGARTFAqhSHIRP- 160
Cdd:cd05651 74 TKDPFEPVEKGGKLYGLGSNDAGA------SVVSLLatflhlySEGPLNYNLIYAASAEEEISgKNGIESLL--PHLPPl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 161 DCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPaKGINAIelmHQSIGYLMKMRDELREKYHNPLfqvTHPTMNFG 240
Cdd:cd05651 146 DLAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAARN-EGDNAI---YKALDDIQWLRDFRFDKVSPLL---GPVKMTVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 241 NIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDlieiRHLHDGIPgyeCEHSaqivqVVEKLLG 320
Cdd:cd05651 219 QINAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLKSEIKPRSF----RLNSSAIP---PDHP-----IVQAAIA 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 493292681 321 EKCDAVNYCTEAPFIQQLCPTLVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:cd05651 287 AGRTPFGSPTLSDQALMPFPSVKIGPGDSSRSHTADEFIELSEIEEGIDIYIELL 341
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
10-321 |
1.83e-28 |
|
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: 115.15 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 10 YAQLIELPTISSLvaEEDLSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYGEG---EGGLLLAGHTDTVPFDE 86
Cdd:cd05675 4 LQELIRIDTTNSG--DGTGSETRAAEVLAARLAEAGIQTEIFVVESHPGRANLVARIGGTdpsAGPLLLLGHIDVVPADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 87 GKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQI--KKPIRILATADEET-TMLGARTFAQHshiRPDC- 162
Cdd:cd05675 82 SDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFkpKRDLVFAFVADEEAgGENGAKWLVDN---HPELf 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 163 -----AI---------IGEPTSLKPIR-AHKGHIGESVRITGRSGHSSDPAKGiNAI----------------------- 204
Cdd:cd05675 159 dgatfALneggggslpVGKGRRLYPIQvAEKGIAWMKLTVRGRAGHGSRPTDD-NAItrlaealrrlgahnfpvrltdet 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 205 ---------------ELMHQSIGYLMKMRDELREKyhNPLFQ-VTHPTMNFGNIHGGDAINRICACCELQFDMRPLPNMA 268
Cdd:cd05675 238 ayfaqmaelaggeggALMLTAVPVLDPALAKLGPS--APLLNaMLRNTASPTMLDAGYATNVLPGRATAEVDCRILPGQS 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 493292681 269 VQdlyaMVNEHLKPMLEQYGdlIEIRHLHDgIPGYECEHSAQIVQVVEKLLGE 321
Cdd:cd05675 316 EE----EVLDTLDKLLGDPD--VSVEAVHL-EPATESPLDSPLVDAMEAAVQA 361
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
175-287 |
2.44e-28 |
|
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: 106.66 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 175 RAHKGHIGESVRITGRSGHSSDPAKGINAIELMhqsigylMKMRDELREKYHNPLFQVTHPTMNFGNIHGGDAINRICAC 254
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLL-------ARLLAELPAEYGDIGFDFPRTTLNITGIEGGTATNVIPAE 73
|
90 100 110
....*....|....*....|....*....|...
gi 493292681 255 CELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQY 287
Cdd:pfam07687 74 AEAKFDIRLLPGEDLEELLEEIEAILEKELPEG 106
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
34-377 |
5.44e-28 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 112.87 E-value: 5.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 34 IELLATWLADFGFKTEILAVEGSRNkynLLATYGEGEGGLLLAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGLGTADMK 112
Cdd:PRK13009 25 QDLLAERLEALGFTCERMDFGDVKN---LWARRGTEGPHLCFAGHTDVVPPgDLEAWTSPPFEPTIRDGMLYGRGAADMK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 113 GFFA-FVVEVVSQL-DLTQIKKPIRILATADEE------TT-MLgaRTFAQHsHIRPDCAIIGEPTSLKpirahkgHIGE 183
Cdd:PRK13009 102 GSLAaFVVAAERFVaAHPDHKGSIAFLITSDEEgpaingTVkVL--EWLKAR-GEKIDYCIVGEPTSTE-------RLGD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 184 SVRI------------TGRSGHSSDPAKGINAIELMHQSIGYLMKMR-DElrekyHNPLFQVThpTMNFGNIHGG-DAIN 249
Cdd:PRK13009 172 VIKNgrrgsltgkltvKGVQGHVAYPHLADNPIHLAAPALAELAATEwDE-----GNEFFPPT--SLQITNIDAGtGATN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 250 RICACCELQFDMRPLPNMAVQDLYAMVNEhlkpMLEQYGDLIEIRHLHDGIP-----GyecEHSAQIVQVVEKLLGEKcd 324
Cdd:PRK13009 245 VIPGELEAQFNFRFSTEHTAESLKARVEA----ILDKHGLDYTLEWTLSGEPfltppG---KLVDAVVAAIEAVTGIT-- 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493292681 325 avnycTE---------APFIQQLCPTLV-LGP--GSIeqaHQPDEFLEMKYIEPtkelLTKlIYH 377
Cdd:PRK13009 316 -----PElstsggtsdARFIADYGAQVVeFGPvnATI---HKVNECVSVADLEK----LTR-IYE 367
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
12-360 |
6.51e-28 |
|
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: 112.90 E-value: 6.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 12 QLIELPTISslvAEEdlsnRRLIELLATWLADFGFKTEILAVEGsrnkyNLLATYGEGEGGLLLAGHTDTVPF-DEGKWR 90
Cdd:cd05649 6 DLIQIPSES---GEE----KGVVERIEEEMEKLGFDEVEIDPMG-----NVIGYIGGGKKKILFDGHIDTVGIgNIDNWK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 91 FNPFQLTEKAGKLYGLGTADMKGFFAFVV---EVVSQLDLTQIKKPIRILATADEET-TMLGARTFAQHSHIRPDCAIIG 166
Cdd:cd05649 74 FDPYEGYETDGKIYGRGTSDQKGGLASMVyaaKIMKDLGLRDFAYTILVAGTVQEEDcDGVCWQYISKADKIKPDFVVSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 167 EPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIelmhqsigylMKMRDELRE-KYHNPLFQvTHPTMNFGNIHGG 245
Cdd:cd05649 154 EPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAV----------YKMADIIQDiRQLNPNFP-EAPFLGRGTLTVT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 246 DAINR---ICAC---CELQFDMRplpnMAVQDLYAMVNEHLK--PMLEQYGDLIEIRHLHDGIPGY-------EC----- 305
Cdd:cd05649 223 DIFSTspsRCAVpdsCRISIDRR----LTVGETWEGCLEEIRalPAVKKYGDDVAVSMYNYDRPSYtgevyesERyfptw 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493292681 306 ------EHSAQIVQVVEKLLGEK--CDAVNYCTEAPFIQ--QLCPTLVLGPGSIEQAHQPDEFLE 360
Cdd:cd05649 299 llpedhELVKALLEAYKALFGARplIDKWTFSTNGVSIMgrAGIPCIGFGPGAENQAHAPNEYTW 363
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
61-373 |
2.40e-25 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 105.79 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 61 NLLATYGEGEGGLLLAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQL-DLTqIKKPIRILA 138
Cdd:PRK13004 60 NVLGYIGHGKKLIAFDAHIDTVGIgDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIkDLG-LDDEYTLYV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 139 TA---DEETTMLGARTFAQHSHIRPDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLM 215
Cdd:PRK13004 139 TGtvqEEDCDGLCWRYIIEEDKIKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 216 KMRDELREkyhnplfqvtHPTMNFGNIHGGDAINR---ICAC---CELQFDMRPL----PNMAVQDLYAMVN-EHLKPML 284
Cdd:PRK13004 219 ELNPNLKE----------DPFLGKGTLTVSDIFSTspsRCAVpdsCAISIDRRLTvgetWESVLAEIRALPAvKKANAKV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 285 EQY--------GDLIEIRHLhdgIPGYECEHSAQIVQVVEK----LLGE--KCDAVNYCTEAPFIQQL--CPTLVLGPGS 348
Cdd:PRK13004 289 SMYnydrpsytGLVYPTECY---FPTWLYPEDHEFVKAAVEaykgLFGKapEVDKWTFSTNGVSIAGRagIPTIGFGPGK 365
|
330 340
....*....|....*....|....*
gi 493292681 349 IEQAHQPDEflemkYIEptKELLTK 373
Cdd:PRK13004 366 EPLAHAPNE-----YTW--KEQLVK 383
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
13-272 |
1.37e-23 |
|
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: 100.12 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 13 LIELPTISSLVAEEdlsnRRLIELLATWLADFGFKTEILAVEgsrnkyNLLATYGEGEGGLLLAGHTDTVPfdeGkwrFN 92
Cdd:cd05653 7 LLDLLSIYSPSGEE----ARAAKFLEEIMKELGLEAWVDEAG------NAVGGAGSGPPDVLLLGHIDTVP---G---EI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 93 PFQLTEkaGKLYGLGTADMKGFFAFVVEVVSQLDLtqiKKPIR--ILATADEETTMLGARtFAQHSHIRPDCAIIGEPTS 170
Cdd:cd05653 71 PVRVEG--GVLYGRGAVDAKGPLAAMILAASALNE---ELGARvvVAGLVDEEGSSKGAR-ELVRRGPRPDYIIIGEPSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 171 LKPIR-AHKGHIGESVRITGRSGHSSDPakGINAIELMHQSIgYLMKMRDELREKYHNPLFQVThPTMnfgnIHGGDAIN 249
Cdd:cd05653 145 WDGITlGYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLIKKW-LEVKKWAEGYNVGGRDFDSVV-PTL----IKGGESSN 216
|
250 260
....*....|....*....|....
gi 493292681 250 RICACCELQFDMR-PLPNMAVQDL 272
Cdd:cd05653 217 GLPQRAEATIDLRlPPRLSPEEAI 240
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
7-375 |
2.90e-23 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 99.35 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 7 IQRYAQLIELPTISSlvAEEDLSNrrlieLLATWLADFGFKTEIlavegsRNKYNLL----ATYGEGEGGLLLAGHTDTV 82
Cdd:COG2195 6 LERFLEYVKIPTPSD--HEEALAD-----YLVEELKELGLEVEE------DEAGNVIatlpATPGYNVPTIGLQAHMDTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 83 PFDEGKwrfnPFQLTEKAGKLYGLGT----ADMKGFFAFVVEVVSQLDLTQIK-KPIRILATADEETTMLGARTFaQHSH 157
Cdd:COG2195 73 PQFPGD----GIKPQIDGGLITADGTttlgADDKAGVAAILAALEYLKEPEIPhGPIEVLFTPDEEIGLRGAKAL-DVSK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 158 IRPDCAII--GEPtslkpirahkghIGE-----------SVRITGRSGHSSD-PAKGINAIELMHQSIgYLMKmRDELRE 223
Cdd:COG2195 148 LGADFAYTldGGE------------EGEleyecagaadaKITIKGKGGHSGDaKEKMINAIKLAARFL-AALP-LGRIPE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 224 KYhnplfqvthpTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYG-DLIEIRHlHDGIPG 302
Cdd:COG2195 214 ET----------EGNEGFIHGGSATNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGvGVVEVEI-EDQYPN 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 303 YECEHSAQIVQVVEKL---LGEKCD--AVNYCTEAPFI--QQLcPTLVLGPGsIEQAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:COG2195 283 WKPEPDSPIVDLAKEAyeeLGIEPKikPIRGGLDGGILsfKGL-PTPNLGPG-GHNFHSPDERVSIESMEKAWELLVEIL 360
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
60-314 |
1.01e-22 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 98.92 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 60 YNLLATY-GEGEGG--LLLAGHTDTVPfdEG---KWRFNPFQLTEKAGKLYGLGTADMKGFFA---FVVEVVSQLDLtQI 130
Cdd:PRK06837 84 PNVVGTYrPAGKTGrsLILQGHIDVVP--EGpldLWSRPPFDPVIVDGWMYGRGAADMKAGLAamlFALDALRAAGL-AP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 131 KKPIRILATADEETTMLGARTFAQHSHiRPDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQS 210
Cdd:PRK06837 161 AARVHFQSVIEEESTGNGALSTLQRGY-RADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHL 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 211 IGYLMKMRDEL-REKYHNPLF-QVTHP-TMNFGNIHGGDAINRICACCElqFDMRP--LPNMAVQDLYA----------- 274
Cdd:PRK06837 240 IQALRELEAEWnARKASDPHFeDVPHPiNFNVGIIKGGDWASSVPAWCD--LDCRIaiYPGVTAADAQAeieaclaaaar 317
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 493292681 275 ---MVNEHLkPMLEQYGDLIEirhlhdgipGYECEHSAQIVQV 314
Cdd:PRK06837 318 ddrFLSNNP-PEVVWSGFLAE---------GYVLEPGSEAEAA 350
|
|
| PRK06915 |
PRK06915 |
peptidase; |
61-380 |
4.88e-21 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 93.99 E-value: 4.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 61 NLLATY-GEGEG-GLLLAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGLGTADMKG---FFAFVVEVVSQLDLtQIKKPI 134
Cdd:PRK06915 82 NIVATLkGSGGGkSMILNGHIDVVPEgDVNQWDHHPYSGEVIGGRIYGRGTTDMKGgnvALLLAMEALIESGI-ELKGDV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 135 RILATADEETTmlGARTFAqhSHIR---PDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIE-LMH-- 208
Cdd:PRK06915 161 IFQSVIEEESG--GAGTLA--AILRgykADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEkSMFvi 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 209 QSIGYLMKMRDelrEKYHNPLFQ-VTHPT-MNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDlyamVNEHLKPMLEQ 286
Cdd:PRK06915 237 DHLRKLEEKRN---DRITDPLYKgIPIPIpINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEA----AKEEFENWIAE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 287 YGDLIE--IRHLHD-------GIPG-YECEHS--AQIVQVVEKLLGEK--CDAVNYCTEAPFIQQL--CPTLVLGPGSIE 350
Cdd:PRK06915 310 LNDVDEwfVEHPVEvewfgarWVPGeLEENHPlmTTLEHNFVEIEGNKpiIEASPWGTDGGLLTQIagVPTIVFGPGETK 389
|
330 340 350
....*....|....*....|....*....|
gi 493292681 351 QAHQPDEFLEMKYIEPTKELLTKLIYHFCG 380
Cdd:PRK06915 390 VAHYPNEYIEVDKMIAAAKIIALTLLDWCE 419
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
35-358 |
2.57e-20 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 91.45 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 35 ELLATWLADFGFKT-EILAVEGSRNKY----NLLATY--GEGEGGLLLAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGL 106
Cdd:PRK13983 34 EYLESLLKEYGFDEvERYDAPDPRVIEgvrpNIVAKIpgGDGKRTLWIISHMDVVPPgDLSLWETDPFKPVVKDGKIYGR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 107 GTAD-MKGFFA--FVVEVVSQLDLTQiKKPIRILATADEETtmlGAR-----TFAQHSHI-RPDCAII----GEPTSLKP 173
Cdd:PRK13983 114 GSEDnGQGIVSslLALKALMDLGIRP-KYNLGLAFVSDEET---GSKygiqyLLKKHPELfKKDDLILvpdaGNPDGSFI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 174 IRAHKGHIGESVRITGRSGHSSDPAKGINA-IELMHqsigYLMKMRDELREKYH--NPLFQVTH----PTMNFGNIhggD 246
Cdd:PRK13983 190 EIAEKSILWLKFTVKGKQCHASTPENGINAhRAAAD----FALELDEALHEKFNakDPLFDPPYstfePTKKEANV---D 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 247 AINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGIPGYECEHSAQIVQ----VVEKLLGEk 322
Cdd:PRK13983 263 NINTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIADEFEEEYGVKIEVEIVQREQAPPPTPPDSEIVKklkrAIKEVRGI- 341
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 493292681 323 cdAVNYC-----TEAPFIQQL-CPTLVLGPGsIEQAHQPDEF 358
Cdd:PRK13983 342 --EPKVGgigggTVAAFLRKKgYPAVVWSTL-DETAHQPNEY 380
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
14-370 |
2.80e-20 |
|
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: 91.00 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 14 IELPTIsslvAEEDLSnrrliELLATWLADFGF-KTEILAVegsrnkYNLLATY-GEGEG-GLLLAGHTDTVpFDEGkwr 90
Cdd:cd03896 10 IPAPTF----REGARA-----DLVAEWMADLGLgDVERDGR------GNVVGRLrGTGGGpALLFSAHLDTV-FPGD--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 91 fNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQI--KKPIRILATADEE--TTMLGARTFAQHSHIRPDCAIIG 166
Cdd:cd03896 71 -TPATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAalKGDVVFAANVGEEglGDLRGARYLLSAHGARLDYFVVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 167 EPTSLKPiraHKGHIGESV-RIT--GRSGHSSDPAKGINAIELMHQSIGYLmkmrdelrEKYHNPlfQVTHPTMNFGNIH 243
Cdd:cd03896 150 EGTDGVP---HTGAVGSKRfRITtvGPGGHSYGAFGSPSAIVAMAKLVEAL--------YEWAAP--YVPKTTFAAIRGG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 244 GGDAINRICACCELQFDMRPLPNMA----VQDLYAMVNE------HLKPMLEQYGDLieirhlhdgiPGYECEHSAQIVQ 313
Cdd:cd03896 217 GGTSVNRIANLCSMYLDIRSNPDAEladvQREVEAVVSKlaakhlRVKARVKPVGDR----------PGGEAQGTEPLVN 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493292681 314 VV-----EKLLGEKCDAvnYCTEA-PFIQQLCPTLVLGPGSIEQAHQPDEflemkYIEPTKEL 370
Cdd:cd03896 287 AAvaahrEVGGDPRPGS--SSTDAnPANSLGIPAVTYGLGRGGNAHRGDE-----YVLKDDML 342
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
11-358 |
8.14e-20 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 90.20 E-value: 8.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 11 AQLIELPTISSlvaeEDLSNRRLIELLATWLADFGFKTEILAVEGSRN------KYNLLATY-GEGEGGLL-LAGHTDTV 82
Cdd:PRK13013 21 QDLIRIPTLNP----PGRAYREICEFLAARLAPRGFEVELIRAEGAPGdsetypRWNLVARRqGARDGDCVhFNSHHDVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 83 PFDEGkWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKP--IRILATADEETTMLGARTF-AQH---S 156
Cdd:PRK13013 97 EVGHG-WTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAgsIEISGTADEESGGFGGVAYlAEQgrfS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 157 HIRPDCAIIGEPTSLKPI-RAHKGHIGESVRITGRSGHSSDPAKGINAIELMHqsiGYLMKMRDELRekyhnPLFQVT-- 233
Cdd:PRK13013 176 PDRVQHVIIPEPLNKDRIcLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMG---AVLAEIEERLF-----PLLATRrt 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 234 ----------HPTMNFGNIHGG--------DAINRICAC--CELQFDMRPLpnmaVQDLYAMVNEHLKPMLEQY-----G 288
Cdd:PRK13013 248 ampvvpegarQSTLNINSIHGGepeqdpdyTGLPAPCVAdrCRIVIDRRFL----IEEDLDEVKAEITALLERLkrarpG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 289 DLIEIRHLHDGIPGYeCEHSAQIVQVV----EKLLGEKCDAVnyctEAP---------FIQQLCPTLVLGPGSIEQAHQP 355
Cdd:PRK13013 324 FAYEIRDLFEVLPTM-TDRDAPVVRSVaaaiERVLGRQADYV----VSPgtydqkhidRIGKLKNCIAYGPGILDLAHQP 398
|
...
gi 493292681 356 DEF 358
Cdd:PRK13013 399 DEW 401
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
31-375 |
6.62e-19 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 87.38 E-value: 6.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 31 RRLIELLATWLADFGFKTEILAVEGSRNKyNLLATY-GEGEGGLLLAGHTDTVpFDEGKWRFNPFQltEKAGKLYGLGTA 109
Cdd:PRK06133 60 KQVAALLAERLKALGAKVERAPTPPSAGD-MVVATFkGTGKRRIMLIAHMDTV-YLPGMLAKQPFR--IDGDRAYGPGIA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 110 DMKGFFAFV---VEVVSQLDLTQIKKpIRILATADEETTMLGARTF-----AQHshirpDCAIIGEPTSLKP--IRAHKG 179
Cdd:PRK06133 136 DDKGGVAVIlhaLKILQQLGFKDYGT-LTVLFNPDEETGSPGSRELiaelaAQH-----DVVFSCEPGRAKDalTLATSG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 180 HIGESVRITGRSGHS-SDPAKGINA-IELMHQsigyLMKMRDELREkyhnplfqVTHPTMNFGNIHGGDAINRICACCEL 257
Cdd:PRK06133 210 IATALLEVKGKASHAgAAPELGRNAlYELAHQ----LLQLRDLGDP--------AKGTTLNWTVAKAGTNRNVIPASASA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 258 QFDMRPLPNMAV----QDLYAMVNEHLKPMLEqygdlIEIRhLHDGIPGYE--------CEHSAQI-------VQVVEKL 318
Cdd:PRK06133 278 QADVRYLDPAEFdrleADLQEKVKNKLVPDTE-----VTLR-FERGRPPLEanaasralAEHAQGIygelgrrLEPIDMG 351
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 493292681 319 LGEKCDA--VNYCTEAPFIQQLCptlVLGPGsieqAHQPDEFLEMKYIEPTKELLTKLI 375
Cdd:PRK06133 352 TGGGTDAafAAGSGKAAVLEGFG---LVGFG----AHSNDEYIELNSIVPRLYLLTRMI 403
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
35-364 |
2.85e-18 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 85.59 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 35 ELLATWLADFGFKT-EILAVEGSRNKY--NLLATYGEGEGGLL-LAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGLGTA 109
Cdd:cd05650 30 DYLEKKLREYGFYTlERYDAPDERGIIrpNIVAKIPGGNDKTLwIISHLDTVPPgDLSLWETDPWEPVVKDGKIYGRGVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 110 D-MKGFFA--FVVEVVSQLDLTQiKKPIRILATADEET-TMLGARTFAQHSHI-RPDCAII----GEPTSLKPIRAHKGH 180
Cdd:cd05650 110 DnQQGIVSslLALKAIIKNGITP-KYNFGLLFVADEEDgSEYGIQYLLNKFDLfKKDDLIIvpdfGTEDGEFIEIAEKSI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 181 IGESVRITGRSGHSSDPAKGINAielMHQSIGYLMKMRDELREKYH--NPLFQVTH----PTMNFGNIhggDAINRICAC 254
Cdd:cd05650 189 LWIKVNVKGKQCHASTPENGINA---FVAASNFALELDELLHEKFDekDDLFNPPYstfePTKKEANV---PNVNTIPGY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 255 CELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGIPGYECEHSAQIV----QVVEKLLG--EKCDAVNY 328
Cdd:cd05650 263 DVFYFDCRVLPTYKLDEVLKFVNKIISDFENSYGAGITYEIVQKEQAPPATPEDSEIVvrlsKAIKKVRGreAKLIGIGG 342
|
330 340 350
....*....|....*....|....*....|....*..
gi 493292681 329 CTEAPFIQQL-CPTLVLGPGsIEQAHQPDEFLEMKYI 364
Cdd:cd05650 343 GTVAAFLRKKgYPAVVWSTL-DETAHQPNEYIRISHI 378
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
10-204 |
5.04e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 82.36 E-value: 5.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 10 YAQLIELPTISSLVaeedlSNRRLIELLATWLADFGFKTEILAVEGSR-NKYNLLATY-GEGEGG-LLLAGHTDTVPFDE 86
Cdd:PRK09133 43 YKELIEINTTASTG-----STTPAAEAMAARLKAAGFADADIEVTGPYpRKGNLVARLrGTDPKKpILLLAHMDVVEAKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 87 GKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDlTQIKKPIR--ILA-TADEE-TTMLGARTFAQH--SHIRP 160
Cdd:PRK09133 118 EDWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLK-REGFKPKRdiILAlTGDEEgTPMNGVAWLAENhrDLIDA 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493292681 161 DCAI----------IGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGiNAI 204
Cdd:PRK09133 197 EFALneggggtldeDGKPVLLTVQAGEKTYADFRLEVTNPGGHSSRPTKD-NAI 249
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
13-207 |
2.56e-16 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 79.23 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 13 LIELPTISSLVAEEdlsnRRLIELLATWLADFGFKTEILAVEgsrnkyNLLATYGEGEGGLLLAGHTDTVPFDEgkwrfn 92
Cdd:PRK04443 12 LKGLVEIPSPSGEE----AAAAEFLVEFMESHGREAWVDEAG------NARGPAGDGPPLVLLLGHIDTVPGDI------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 93 PFQLteKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATaDEETTMLGARTFAQHSHiRPDCAIIGEPTSLK 172
Cdd:PRK04443 76 PVRV--EDGVLWGRGSVDAKGPLAAFAAAAARLEALVRARVSFVGAV-EEEAPSSGGARLVADRE-RPDAVIIGEPSGWD 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 493292681 173 PIR-AHKGHIGESVRITGRSGHSSDPakGINAIELM 207
Cdd:PRK04443 152 GITlGYKGRLLVTYVATSESFHSAGP--EPNAAEDA 185
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
61-170 |
5.04e-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: 75.93 E-value: 5.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 61 NLLATYGEGEGG--LLLAGHTDTVPFDEGKWRFNPFQ-LTEKAGKLYGLGTADMKGFFAFVVEVVSQL--DLTQIKKPIR 135
Cdd:cd18669 1 NVIARYGGGGGGkrVLLGAHIDVVPAGEGDPRDPPFFvDTVEEGRLYGRGALDDKGGVAAALEALKLLkeNGFKLKGTVV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 493292681 136 ILATADEETTMlGARTFAQHS-----HIRPDCAIIGEPTS 170
Cdd:cd18669 81 VAFTPDEEVGS-GAGKGLLSKdaleeDLKVDYLFVGDATP 119
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
20-281 |
5.73e-16 |
|
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: 78.65 E-value: 5.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 20 SSLVAEEDLSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATY-GEGEGGLL--LAGHTDTVPFDEGKWRFNPFQL 96
Cdd:cd08012 25 PQLVPKEDNAGRHVLEALTPYSTENGGPLVIDHVSYVKGRGNIIVEYpGTVDGKTVsfVGSHMDVVTANPETWEFDPFSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 97 TEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILAT--ADEE-TTMLGARTFAQHSHirpdcaiiGEPTSLK- 172
Cdd:cd08012 105 SIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVVAVfiANEEnSEIPGVGVDALVKS--------GLLDNLKs 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 173 ------------PIRAHKGHIGESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKM--------RDELREKYHNPlfQV 232
Cdd:cd08012 177 gplywvdsadsqPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVMEALAEIQKRfyidfpphPKEEVYGFATP--ST 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 493292681 233 THPTMnFGNIHGGdaINRICACCELQFDMRPLPNMAVQDLYAMVNEHLK 281
Cdd:cd08012 255 MKPTQ-WSYPGGS--INQIPGECTICGDCRLTPFYDVKEVREKLEEYVD 300
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
35-265 |
6.72e-16 |
|
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: 78.37 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 35 ELLATWLADFGFKTEILAVE-------GSRNKYNLLA--TYGEGEGGLLLAGHTDTVPFDEGkWRFNPFQLTEKAGKLYG 105
Cdd:cd02697 29 ERTAALLQGFGFEAERHPVPeaevrayGMESITNLIVrrRYGDGGRTVALNAHGDVVPPGDG-WTRDPYGAVVEDGVMYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 106 LGTADMKGFFA---FVVEVVSQLDLTqIKKPIRILATADEETT-MLGARTFAQHSHIRPDCAIIGEpTSLKPIRAHKGHI 181
Cdd:cd02697 108 RAAAVSKSDFAsftFAVRALESLGAP-LRGAVELHFTYDEEFGgELGPGWLLRQGLTKPDLLIAAG-FSYEVVTAHNGCL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 182 GESVRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDELREKyHNPLFQVTHPTMNFGNIHGGDAINRICACCELQFDM 261
Cdd:cd02697 186 QMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNAQYRQV-SSQVEGITHPYLNVGRIEGGTNTNVVPGKVTFKLDR 264
|
....
gi 493292681 262 RPLP 265
Cdd:cd02697 265 RMIP 268
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
61-169 |
1.28e-15 |
|
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: 74.77 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 61 NLLATYGEGEGG--LLLAGHTDTVPFDEGKWRFNPFQ-LTEKAGKLYGLGTADMKGFFAFVVEVVSQL--DLTQIKKPIR 135
Cdd:cd03873 1 NLIARLGGGEGGksVALGAHLDVVPAGEGDNRDPPFAeDTEEEGRLYGRGALDDKGGVAAALEALKRLkeNGFKPKGTIV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 493292681 136 ILATADEETTMlGARTFAQHS-----HIRPDCAIIGEPT 169
Cdd:cd03873 81 VAFTADEEVGS-GGGKGLLSKfllaeDLKVDAAFVIDAT 118
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
7-239 |
1.29e-15 |
|
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: 78.07 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 7 IQRYAQLIELPTISSLVAEEDLSNRRLIEL--LATWLA-DFGFKTEILAVEgSRNKYNLLATYgegEGG------LLLAG 77
Cdd:cd05674 1 IERLSGAVQIPTVSFDDMPPIDEDERWDAFykFHDYLEkTFPLVHKTLKVE-VVNEYGLLYTW---EGSdpslkpLLLMA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 78 HTDTVP---FDEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLdLTQIKKPIR--ILATA-DEETT-MLGAR 150
Cdd:cd05674 77 HQDVVPvnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELL-LKRGFKPRRtiILAFGhDEEVGgERGAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 151 TFAQHSHIR--PDCA--------------IIGEPTSLkPIRAHKGHIGESVRITGRSGHSSDPAKginaielmHQSIGYL 214
Cdd:cd05674 156 AIAELLLERygVDGLaaildeggavlegvFLGVPFAL-PGVAEKGYMDVEITVHTPGGHSSVPPK--------HTGIGIL 226
|
250 260
....*....|....*....|....*
gi 493292681 215 MKMRDELREKYHNPLFQVTHPTMNF 239
Cdd:cd05674 227 SEAVAALEANPFPPKLTPGNPYYGM 251
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
57-372 |
2.42e-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: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 57 RNKYNLLATYGEG-EGGLLLAGHTDTVPFDE---GKWrfnpfqltEKAGKLYGLGTADMKG-------FFAFVVEVVSQL 125
Cdd:cd05647 39 RDGNTVVARTERGlASRVILAGHLDTVPVAGnlpSRV--------EEDGVLYGCGATDMKAgdavqlkLAATLAAATLKH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 126 DLTQI---KKPIrilatADEETTMlgARTFAQH-SHIRPDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGI 201
Cdd:cd05647 111 DLTLIfydCEEV-----AAELNGL--GRLAEEHpEWLAADFAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 202 NAIelmHQSIGYLMKMrDELREKYHNPLFQVTHPTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVqdlyAMVNEHLK 281
Cdd:cd05647 184 NAI---HKLAPILARL-AAYEPRTVNIDGLTYREGLNAVFISGGVAGNVIPDEARVNLNYRFAPDKSL----AEAIAHVR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 282 PMLEQYGDLIEIRhlhDGIPGYECEHSAQIVQVVEKLLGEKCDAVNYCTE-APFIQQLCPTLVLGPGSIEQAHQPDEFLE 360
Cdd:cd05647 256 EVFEGLGYEIEVT---DLSPGALPGLDHPVARDLIEAVGGKVRAKYGWTDvARFSALGIPAVNFGPGDPLLAHKRDEQVP 332
|
330
....*....|..
gi 493292681 361 MKYIEPTKELLT 372
Cdd:cd05647 333 VEQITACAAILR 344
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
35-195 |
2.63e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 76.81 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 35 ELLATWLADFGFKTEIlaVEGSRNKYNLLATYgEGE----GGLLLAGHTDTVPFDEGKWRFNPFQLTEKAGKLYGLGTAD 110
Cdd:PRK07906 29 EYVAEKLAEVGLEPTY--LESAPGRANVVARL-PGAdpsrPALLVHGHLDVVPAEAADWSVHPFSGEIRDGYVWGRGAVD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 111 MKGFFAFVVEVVSQLDLTQIKKP--IRILATADEETTM-LGARTFAQHshiRPD----C--AI---------IGEPTSLK 172
Cdd:PRK07906 106 MKDMDAMMLAVVRHLARTGRRPPrdLVFAFVADEEAGGtYGAHWLVDN---HPElfegVteAIsevggfsltVPGRDRLY 182
|
170 180
....*....|....*....|....
gi 493292681 173 PIR-AHKGHIGESVRITGRSGHSS 195
Cdd:PRK07906 183 LIEtAEKGLAWMRLTARGRAGHGS 206
|
|
| dapE-gram_pos |
TIGR01900 |
succinyl-diaminopimelate desuccinylase; This model represents a clade of ... |
74-365 |
7.06e-15 |
|
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: 75.01 E-value: 7.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 74 LLAGHTDTVPFDE---GKWRfnpfqltekAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRILATADEE----TTM 146
Cdd:TIGR01900 61 ILAGHLDTVPIADnlpSRVE---------GGRLYGRGAVDMKGGLAVMLALAATLDRTEPRHDLTLVFYEREEgpaeENG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 147 LGaRTFAQHSH-IRPDCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGINAIelmHQSIGYLMKMRD-ELREK 224
Cdd:TIGR01900 132 LG-RLLREHPEwLAGDLAVLLEPTDGKIEAGCQGTLRATVTFHGRRAHSARSWMGENAI---HKAAPILARLAAyEPREV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 225 YHNPL--FQVTHPTMnfgnIHGGDAINRICACCELQFDMRPLPNMAVqdlyAMVNEHLKPMLEQYGDLIEIRhlhDGIPG 302
Cdd:TIGR01900 208 TVDGLtyREGLNAVR----IEGGVAGNVIPDECEVNVNYRFAPDRSL----EQARAHVRELFEGDGAEVEVT---DLSPG 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493292681 303 YECEHSAQIVQVVEKLLGEKCDAVNYCTE-APFIQQLCPTLVLGPGSIEQAHQPDEFLEMKYIE 365
Cdd:TIGR01900 277 ARPGLDNPLAAELVAAVGGEVRAKYGWTDvARFSALGIPAVNFGPGDPALAHQDDEHVPVAQLT 340
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
42-207 |
1.28e-14 |
|
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: 74.97 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 42 ADFGFKTEILavegsrNKYNLLATYGEGEGGLLLAGHTDTVPFDEGkWRFNPFQLTEKAGKLYGLGTADMKG-----FFA 116
Cdd:cd03888 49 KRLGFKTKNI------DNYAGYAEYGEGEEVLGILGHLDVVPAGEG-WTTDPFKPVIKDGKLYGRGTIDDKGptiaaLYA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 117 fvVEVVSQLDLtQIKKPIRILATADEETTMLGARTFAQHSHIrPDCA---------IIGE-------------PTSLKPI 174
Cdd:cd03888 122 --LKILKDLGL-PLKKKIRLIFGTDEETGWKCIEHYFEHEEY-PDFGftpdaefpvINGEkgivtvdltfkidDDKGYRL 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493292681 175 ---------------------RAHKGHIGES-----------------VRITGRSGHSSDPAKGINAIELM 207
Cdd:cd03888 198 isikggeatnmvpdkaeavipGKDKEELALSaatdlkgnieiddggveLTVTGKSAHASAPEKGVNAITLL 268
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
29-266 |
1.98e-14 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 73.66 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 29 SNRRLIELLATWLADFGFKTEILAvegSRNKYNLlatygeGEGGLLLAGHTDTVPfdegkWRFNPFQLTEkagKLYGLGT 108
Cdd:PRK00466 28 NETNATKFFEKISNELNLKLEILP---DSNSFIL------GEGDILLASHVDTVP-----GYIEPKIEGE---VIYGRGA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 109 ADMKGFFAFVVEVVSQLDLTQIKkpIRILATADEETTMLGARTFAQhSHIRPDCAIIGEPT-SLKPIRAHKGHIGESVRI 187
Cdd:PRK00466 91 VDAKGPLISMIIAAWLLNEKGIK--VMVSGLADEESTSIGAKELVS-KGFNFKHIIVGEPSnGTDIVVEYRGSIQLDIMC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 188 TGRSGHSSDPAKGInAIELMHQSIGYLmkmrdELREKYHNPLFQVTHptmnfgnIHGGDAINRICACCELQFDMR-PLPN 266
Cdd:PRK00466 168 EGTPEHSSSAKSNL-IVDISKKIIEVY-----KQPENYDKPSIVPTI-------IRAGESYNVTPAKLYLHFDVRyAINN 234
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
8-377 |
6.27e-13 |
|
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: 69.66 E-value: 6.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 8 QRYAQLIELPTISSlVAEEDLSNRRLIELLATWLADFGFKTEIlaVEGSRNKYNLLATYGEGEGG--LLLAGHTDTVP-F 84
Cdd:cd03893 2 QTLAELVAIPSVSA-QPDRREELRRAAEWLADLLRRLGFTVEI--VDTSNGAPVVFAEFPGAPGAptVLLYGHYDVQPaG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 85 DEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQL--DLTQIKKPIRILATADEET--TMLGARTFAQHSHIRP 160
Cdd:cd03893 79 DEDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALmqQGGDLPVNVKFIIEGEEESgsPSLDQLVEAHRDLLAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 161 DCAIIGEPTSLKPIR-----AHKGHIGESVRITGRSG--HSS-------DP-AKGINAIELMHQSIGYLM---------- 215
Cdd:cd03893 159 DAIVISDSTWVGQEQptltyGLRGNANFDVEVKGLDHdlHSGlyggvvpDPmTALAQLLASLRDETGRILvpglydavre 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 216 -------KMRDEL-------REKYHNPLFQVTHPTMNFGNIHGG----DAINRICACCELQFDMRPLPNMAVQDLYAMVN 277
Cdd:cd03893 239 lpeeefrLDAGVLeeveiigGTTGSVAERLWTRPALTVLGIDGGfpgeGSKTVIPPRARAKISIRLVPGQDPEEASRLLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 278 EHLK---PmleqYGDLIEIRHLHDGIPgYECEHSAQIVQVVEKLLGEKCDA-VNYCTEA---PFIQQL-----CPTLVLG 345
Cdd:cd03893 319 AHLEkhaP----SGAKVTVSYVEGGMP-WRSDPSDPAYQAAKDALRTAYGVePPLTREGgsiPFISVLqefpqAPVLLIG 393
|
410 420 430
....*....|....*....|....*....|...
gi 493292681 346 PGSIE-QAHQPDEFLEMKYIEPTKELLTKLIYH 377
Cdd:cd03893 394 VGDPDdNAHSPNESLRLGNYKEGTQAEAALLYS 426
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
41-187 |
7.14e-13 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 69.42 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 41 LADFGFKTEILAVEGSrnkYNLLATYGEGEGGLLLAGHTDTVPFDEGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVE 120
Cdd:PRK08554 37 LESWGIESELIEKDGY---YAVYGEIGEGKPKLLFMAHFDVVPVNPEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVML 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493292681 121 VVSQLDLTQIKKPIRILATADEETTMLGARTFAQHSH---IRPDCAIIGEPTSLKPI-RAHKGhIGESVRI 187
Cdd:PRK08554 114 ALKELSKEPLNGKVIFAFTGDEEIGGAMAMHIAEKLReegKLPKYMINADGIGMKPIiRRRKG-FGVTIRV 183
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
73-379 |
9.33e-13 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 68.91 E-value: 9.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 73 LLLAGHTDTVPFDEGK-WRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRIL--ATADEETTMLGA 149
Cdd:PRK08596 80 LIINGHMDVAEVSADEaWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIfqSVIGEEVGEAGT 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 150 RTFAQHSHiRPDCAIIGEPTSLkpirahkgHI-GESVRITG--------------RSG--HSSDPAKGINAIELMHQSIG 212
Cdd:PRK08596 160 LQCCERGY-DADFAVVVDTSDL--------HMqGQGGVITGwitvkspqtfhdgtRRQmiHAGGGLFGASAIEKMMKIIQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 213 YLmkmrDELREKY----HNPLFQVTHPTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHL-------- 280
Cdd:PRK08596 231 SL----QELERHWavmkSYPGFPPGTNTINPAVIEGGRHAAFIADECRLWITVHFYPNETYEQVIKEIEEYIgkvaaadp 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 281 -------------KPMLEQYGDL---IEIRHLHDGIPGYECEHsaqivqvvEKLLGEK--CDAVNYCTEAPFIQQL-CPT 341
Cdd:PRK08596 307 wlrenppqfkwggESMIEDRGEIfpsLEIDSEHPAVKTLSSAH--------ESVLSKNaiLDMSTTVTDGGWFAEFgIPA 378
|
330 340 350
....*....|....*....|....*....|....*...
gi 493292681 342 LVLGPGSIEQAHQPDEFLEMKYIEPTKELLTKLIYHFC 379
Cdd:PRK08596 379 VIYGPGTLEEAHSVNEKVEIEQLIEYTKVITAFIYEWC 416
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
73-263 |
1.18e-12 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 68.45 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 73 LLLAGHTDTVpFDEGkwrfNPFQLTE--KAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPI--RILATADEETTMLG 148
Cdd:PRK07338 95 VLLTGHMDTV-FPAD----HPFQTLSwlDDGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLgyDVLINPDEEIGSPA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 149 ART----FAQHSHirpdCAIIGEPT----SLKPIRAHKGHIgeSVRITGRSGHSS-DPAKGINAIEL---MHQSIGYLMK 216
Cdd:PRK07338 170 SAPllaeLARGKH----AALTYEPAlpdgTLAGARKGSGNF--TIVVTGRAAHAGrAFDEGRNAIVAaaeLALALHALNG 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493292681 217 MRDELrekyhnplfqvthpTMNFGNIHGGDAINRICACCELQFDMRP 263
Cdd:PRK07338 244 QRDGV--------------TVNVAKIDGGGPLNVVPDNAVLRFNIRP 276
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
6-113 |
2.55e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 68.02 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 6 FIQRYAQLIELPTISSLVAEEDLSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYGEGEG--GLLLAGHTDTVP 83
Cdd:PRK07079 19 FFADLARRVAYRTESQNPDRAPALRAYLTDEIAPALAALGFTCRIVDNPVAGGGPFLIAERIEDDAlpTVLIYGHGDVVR 98
|
90 100 110
....*....|....*....|....*....|..
gi 493292681 84 FDEGKWR--FNPFQLTEKAGKLYGLGTADMKG 113
Cdd:PRK07079 99 GYDEQWRegLSPWTLTEEGDRWYGRGTADNKG 130
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
61-375 |
3.59e-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: 67.09 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 61 NLLATY-GEGEGG--LLLAGHTDTVpfDEGKWRFNPfqlTEKAGKLYGLGT----ADMKGFFAFVVEVVSQLDLTQIK-K 132
Cdd:cd05683 55 NLICTLkADKEEVpkILFTSHMDTV--TPGINVKPP---QIADGYIYSDGTtilgADDKAGIAAILEAIRVIKEKNIPhG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 133 PIRILATADEETTMLGART-----------FAQHSHIRPDCAIIGEPTSLKPirahkghigeSVRITGRSGHSS-DPAKG 200
Cdd:cd05683 130 QIQFVITVGEESGLVGAKAldpelidadygYALDSEGDVGTIIVGAPTQDKI----------NAKIYGKTAHAGtSPEKG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 201 INAIELMHQSIgylMKMrdelrekyhnPLFQVTH-PTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEH 279
Cdd:cd05683 200 ISAINIAAKAI---SNM----------KLGRIDEeTTANIGKFQGGTATNIVTDEVNIEAEARSLDEEKLDAQVKHMKET 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 280 LKPMLEQYGDLIEIRhLHDGIPGYECEHSAQIVQVVEKLLGE-----KCDAVNYCTEAPFIQQL-CPTLVLGPGsIEQAH 353
Cdd:cd05683 267 FETTAKEKGAHAEVE-VETSYPGFKINEDEEVVKLAKRAANNlgleiNTTYSGGGSDANIINGLgIPTVNLGIG-YENIH 344
|
330 340
....*....|....*....|..
gi 493292681 354 QPDEFLEMKYIEPTKELLTKLI 375
Cdd:cd05683 345 TTNERIPIEDLYDTAVLVVEII 366
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
6-113 |
8.81e-12 |
|
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: 66.09 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 6 FIQRYAQLIELPTISSlvaeeDLSNR----RLIELLATWLADFGFKTEIlaVEGSRNKYN----------LLATYGE--G 69
Cdd:cd05676 12 FIERLREAVAIQSVSA-----DPEKRpeliRMMEWAAERLEKLGFKVEL--VDIGTQTLPdgeelplppvLLGRLGSdpS 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 493292681 70 EGGLLLAGHTDTVPFD-EGKWRFNPFQLTEKAGKLYGLGTADMKG 113
Cdd:cd05676 85 KKTVLIYGHLDVQPAKlEDGWDTDPFELTEKDGKLYGRGSTDDKG 129
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
73-287 |
2.08e-11 |
|
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: 64.60 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 73 LLLAGHTDTVPFDEGKWRFNPFQLTEKA-GKLYGLGTADMKGFFAFVVEVVSQLDLT--QIKKPIRILATADEET-TMLG 148
Cdd:cd05646 67 ILLNSHTDVVPVFEEKWTHDPFSAHKDEdGNIYARGAQDMKCVGIQYLEAIRRLKASgfKPKRTIHLSFVPDEEIgGHDG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 149 ARTFAQHSHIR---PDCAI---IGEPTSlkpirAHKGHIGE------SVRITGRSGHSSDPAKGiNAIELMHQSIGYLMK 216
Cdd:cd05646 147 MEKFVKTEEFKklnVGFALdegLASPTE-----EYRVFYGErspwwvVITAPGTPGHGSKLLEN-TAGEKLRKVIESIME 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493292681 217 MRDELREKYHN----PLFQVThpTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQY 287
Cdd:cd05646 221 FRESQKQRLKSnpnlTLGDVT--TVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGRGV 293
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
43-144 |
3.45e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 61.25 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 43 DFGFKTEIlavegSRNKYNLLATYGEGEGGLLLAGHTDTVPF-DEGKWRFNPFQLTEKAGKLYGLGTADMKG-FFAFVVE 120
Cdd:PRK07205 53 GLGFKTYL-----DPKGYYGYAEIGQGEELLAILCHLDVVPEgDLSDWQTPPFEAVEKDGCLFGRGTQDDKGpSMAALYA 127
|
90 100
....*....|....*....|....*
gi 493292681 121 VVSQLDL-TQIKKPIRILATADEET 144
Cdd:PRK07205 128 VKALLDAgVQFNKRIRFIFGTDEET 152
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
13-136 |
6.46e-09 |
|
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: 57.35 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 13 LIELPTISslvaeedLSNRRLIE---LLATWLADFGFKTEILavEGSRNKYnLLATYGEG-EGGLLLAGHTDTVPFDE-G 87
Cdd:cd05681 8 LLKIPSVS-------AQGRGIPEtadFLKEFLRRLGAEVEIF--ETDGNPI-VYAEFNSGdAKTLLFYNHYDVQPAEPlE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 493292681 88 KWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRI 136
Cdd:cd05681 78 LWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNI 126
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
4-285 |
9.26e-09 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 56.72 E-value: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 4 IPFIQRYAQLIELPTISSLVAEEDlsnrrlIELLATWLadfGFKTEILAVegsrnkynllatygegegglLLAGHTDTVP 83
Cdd:TIGR01880 34 VDFLIKQADELGLARKTIEFVPGK------PVVVLTWP---GSNPELPSI--------------------LLNSHTDVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 84 FDEGKWRFNPFQ-LTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLT--QIKKPIRILATADEET-TMLGARTFAQHSHIR 159
Cdd:TIGR01880 85 VFREHWTHPPFSaFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASgfKFKRTIHISFVPDEEIgGHDGMEKFAKTDEFK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 160 P-------DCAIIGEPTSLKPIRAHKGHIGESVRITGRSGHSSDPAKGiNAIELMHQSIGYLMKMRDE----LREKYHNP 228
Cdd:TIGR01880 165 AlnlgfalDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKLMEN-TAMEKLEKSVESIRRFRESqfqlLQSNPDLA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 493292681 229 LFQVThpTMNFGNIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLE 285
Cdd:TIGR01880 244 IGDVT--SVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAGE 298
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
68-256 |
2.07e-08 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 55.56 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 68 EGEGGLLLAGHTDTV-PFdeGKWRFNPFQltEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKK--PIRILATADEET 144
Cdd:PRK07473 73 QGEPGILIAGHMDTVhPV--GTLEKLPWR--REGNKCYGPGILDMKGGNYLALEAIRQLARAGITTplPITVLFTPDEEV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 145 TMLGARTFAQHSHIRPDCAIIGEPTslkpiRAHKGHI-GE------SVRITGRSGHS-SDPAKGINAIELMHQSIGYLMK 216
Cdd:PRK07473 149 GTPSTRDLIEAEAARNKYVLVPEPG-----RPDNGVVtGRyaiarfNLEATGRPSHAgATLSEGRSAIREMARQILAIDA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493292681 217 MRDElrekyhnplfqvtHPTMNFGNIHGGDAINRICACCE 256
Cdd:PRK07473 224 MTTE-------------DCTFSVGIVHGGQWVNCVATTCT 250
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
45-144 |
6.36e-08 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 54.08 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 45 GFKTEilAVEGsrnkYNLLATYGEGEGGLLLAGHTDTVPFDEGkWRFNPFQLTEKAGKLYGLGTADMKG-----FFAfvV 119
Cdd:PRK07318 60 GFKTK--NVDN----YAGHIEYGEGEEVLGILGHLDVVPAGDG-WDTDPYEPVIKDGKIYARGTSDDKGptmaaYYA--L 130
|
90 100
....*....|....*....|....*
gi 493292681 120 EVVSQLDLTqIKKPIRILATADEET 144
Cdd:PRK07318 131 KIIKELGLP-LSKKVRFIVGTDEES 154
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
2-113 |
4.67e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 51.44 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 2 KQIPFIQR-YAQLIELPTISSLVAEEDlSNRRLIELLATWLADFGF-KTEILAVEGSRNkynLLATYgEGEGG---LLLA 76
Cdd:PRK07907 15 ELLPRVRAdLEELVRIPSVAADPFRRE-EVARSAEWVADLLREAGFdDVRVVSADGAPA---VIGTR-PAPPGaptVLLY 89
|
90 100 110
....*....|....*....|....*....|....*...
gi 493292681 77 GHTDTVP-FDEGKWRFNPFQLTEKAGKLYGLGTADMKG 113
Cdd:PRK07907 90 AHHDVQPpGDPDAWDSPPFELTERDGRLYGRGAADDKG 127
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
31-113 |
2.67e-06 |
|
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: 49.03 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 31 RRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYGEGEGG--LLLAGHTDTVPFDEGKWR--FNPFQLTEKAGKLYGL 106
Cdd:cd05679 31 AYLDQEMRPRFERLGFTVHIHDNPVAGRAPFLIAERIEDPSLptLLIYGHGDVVPGYEGRWRdgRDPWTVTVWGERWYGR 110
|
....*..
gi 493292681 107 GTADMKG 113
Cdd:cd05679 111 GTADNKG 117
|
|
| M20_Acy1L2-like |
cd09849 |
M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
155-370 |
2.02e-05 |
|
M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli , to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins 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 the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349947 [Multi-domain] Cd Length: 389 Bit Score: 46.32 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 155 HSHIRPDCAIIGEPTSlkpirahKGHIGESVRITGRSGHS-SDPAKGINAIELMHQSIGYLMKMRDELREKYHNPLfqvt 233
Cdd:cd09849 171 HALDLGEDKALINPES-------NGFIGKKVKFTGKESHAgSAPFSGINALNAATLAINNVNAQRETFKESDKVRF---- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 234 HPTMnfgnIHGGDAINRICACCELQFDMRPLPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHlhdgIPGYE--CEHSAQI 311
Cdd:cd09849 240 HPII----TKGGDIVNVVPADVRVESYVRARSIDYMKEANSKVNRALRASAMAVGAEVEIKE----LPGYLpiLQDRDLD 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 312 VQVVEKL--LGEKCD-----AVNYCTEAPFIQQLCPTLVLGPGSIEQAHQPDEFL----EMKYIEPTKEL 370
Cdd:cd09849 312 NFLKENLqdLGLIERiidggDFTGSFDFGDLSHLMPTLHPMFGGVEGALHTRDFKivdpEFAYILPAKAL 381
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
7-143 |
2.05e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 46.29 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 7 IQRYAQLIELPTISSlvaeedlsNRRLIELLATWLADF----GFKTEILAVEGsrNKYnllaTYGEGEGG----LLLAGH 78
Cdd:PRK06446 5 LYTLIEFLKKPSISA--------TGEGIEETANYLKDTmeklGIKANIERTKG--HPV----VYGEINVGakktLLIYNH 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493292681 79 TDTVPFDE-GKWRFNPFQLTEKAGKLYGLGTADMKG-FFAFVVEVVSQLDLTQIKKPIRILATADEE 143
Cdd:PRK06446 71 YDVQPVDPlSEWKRDPFSATIENGRIYARGASDNKGtLMARLFAIKHLIDKHKLNVNVKFLYEGEEE 137
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
7-122 |
3.25e-05 |
|
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: 349929 [Multi-domain] Cd Length: 437 Bit Score: 45.76 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 7 IQRYAQLIELPTISSLVA-EEDLsnRRLIELLATWLADFGF-KTEILAVEGsrnkynLLATYGEGEGG-----LLLAGHT 79
Cdd:cd05680 1 LEELFELLRIPSVSADPAhKGDV--RRAAEWLADKLTEAGFeHTEVLPTGG------HPLVYAEWLGApgaptVLVYGHY 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 493292681 80 DTVPFD-EGKWRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVV 122
Cdd:cd05680 73 DVQPPDpLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAV 116
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
58-227 |
4.33e-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: 45.41 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 58 NKYNLLATY-GEGEG--GLLLAGHTDTVPFDE-GKWR---FNPFQLTE-----------------KAGK-LYGLGTADMK 112
Cdd:cd05654 56 GRRNVTALVkGKKPSkrTIILISHFDTVGIEDyGELKdiaFDPDELTKafseyveeldeevredlLSGEwLFGRGTMDMK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 113 GFFAFVVEVVSQL-DLTQIKKPIRILATADEETT---MLGART----FAQHSHIRPDCAIIGEPTSLK----PIRA-HKG 179
Cdd:cd05654 136 SGLAVHLALLEQAsEDEDFDGNLLLMAVPDEEVNsrgMRAAVPalleLKKKHDLEYKLAINSEPIFPQydgdQTRYiYTG 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493292681 180 HIGE---SVRITGRSGHSSDPAKGINAiELMHQSIGYLMKMRDELREKYHN 227
Cdd:cd05654 216 SIGKilpGFLCYGKETHVGEPFAGINA-NLMASEITARLELNADLCEKVEG 265
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
11-113 |
8.05e-05 |
|
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex.
Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 44.26 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 11 AQLIELPTISSLVAEED-LSNRRLIELLATWLADFGFKTEILAVEGSRNKYNLLATYG-----EGEGGLLLAGHTDTVPF 84
Cdd:cd05677 6 SEFIAFQTVSQSPTTENaEDSRRCAIFLRQLFKKLGATNCLLLPSGPGTNPIVLATFSgnssdAKRKRILFYGHYDVIPA 85
|
90 100 110
....*....|....*....|....*....|
gi 493292681 85 DE-GKWRFNPFQLTEKAGKLYGLGTADMKG 113
Cdd:cd05677 86 GEtDGWDTDPFTLTCENGYLYGRGVSDNKG 115
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
185-333 |
8.91e-05 |
|
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: 44.13 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 185 VRITGRSGHSSDPAKGINAIELMHQSIGYLMKMRDelREkyhnplFQVTHP-TMNFGNIHGGDAINRICACCELQFDMRP 263
Cdd:cd03886 176 ITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVVS--RE------LDPLEPaVVTVGKFHAGTAFNVIPDTAVLEGTIRT 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 264 LPNMAVQDLYAMVNEHLKPMLEQYGDLIEIRHLHDGIPGY-ECEHSAQIVQVVEKLLGEKC-----------DAVNYCTE 331
Cdd:cd03886 248 FDPEVREALEARIKRLAEGIAAAYGATVELEYGYGYPAVInDPELTELVREAAKELLGEEAvvepepvmgseDFAYYLEK 327
|
..
gi 493292681 332 AP 333
Cdd:cd03886 328 VP 329
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
78-155 |
2.11e-04 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 43.03 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 78 HTDTVPFDEGKW-----RFNPFQLTEKAGKLYGLGTADMKGFFA---FVVEVV--SQLDLtqiKKPIRILATADEETTML 147
Cdd:PRK06156 117 HADVVPANPELWvldgtRLDPFKVTLVGDRLYGRGTEDDKGAIVtalYAMKAIkdSGLPL---ARRIELLVYTTEETDGD 193
|
....*...
gi 493292681 148 GARTFAQH 155
Cdd:PRK06156 194 PLKYYLER 201
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
12-136 |
6.08e-04 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 41.65 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493292681 12 QLIELPTISSLvAEEDLSNRRLIELLATWLADFGF-KTEILAVEGSRNKYnllATYGEGEGG--LLLAGHTDTVPFDEGK 88
Cdd:PRK08201 22 EFLRIPSISAL-SEHKEDVRKAAEWLAGALEKAGLeHVEIMETAGHPIVY---ADWLHAPGKptVLIYGHYDVQPVDPLN 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 493292681 89 -WRFNPFQLTEKAGKLYGLGTADMKGFFAFVVEVVSQLDLTQIKKPIRI 136
Cdd:PRK08201 98 lWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNV 146
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