|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
17-377 |
0e+00 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 742.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 17 PSVTPIDHTCQTIMADRLAKVGFHIEPMRFGDVDNLWARRGTEGPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYG 96
Cdd:PRK13009 15 PSVTPDDAGCQDLLAERLEALGFTCERMDFGDVKNLWARRGTEGPHLCFAGHTDVVPPGDLEAWTSPPFEPTIRDGMLYG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 97 RGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEGPAVNGTVKVIETLEKRNEKITWCLVGEPSSTHKLGDIVK 176
Cdd:PRK13009 95 RGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVLEWLKARGEKIDYCIVGEPTSTERLGDVIK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 177 NGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDNGNEYFPATSFQISNIHAGTGATNVIPGALEVTF 256
Cdd:PRK13009 175 NGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEGNEFFPPTSLQITNIDAGTGATNVIPGELEAQF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 257 NFRYSTEVTAEQLKQRVHEILDKHGLQYEIVWNLSGLPFLTPVGELVNAAQTAILNVTGTETELSTSGGTSDGRFIAPTG 336
Cdd:PRK13009 255 NFRFSTEHTAESLKARVEAILDKHGLDYTLEWTLSGEPFLTPPGKLVDAVVAAIEAVTGITPELSTSGGTSDARFIADYG 334
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446939317 337 AQVLELGVLNATIHQINEHVDVHDLDPLTDIYEQILENLLA 377
Cdd:PRK13009 335 AQVVEFGPVNATIHKVNECVSVADLEKLTRIYERILERLLA 375
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
17-372 |
0e+00 |
|
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: 670.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 17 PSVTPIDHTCQTIMADRLAKVGFHIEPMRFGDVDNLWARRGTEGPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYG 96
Cdd:cd03891 11 PSVTPDDAGAQDLIAERLKALGFTCERLEFGGVKNLWARRGTGGPHLCFAGHTDVVPPGDLEGWSSDPFSPTIKDGMLYG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 97 RGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEGPAVNGTVKVIETLEKRNEKITWCLVGEPSSTHKLGDIVK 176
Cdd:cd03891 91 RGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKIDYCIVGEPTSEKKLGDTIK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 177 NGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDNGNEYFPATSFQISNIHAGTGATNVIPGALEVTF 256
Cdd:cd03891 171 IGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLDEGNEFFPPSSLQITNIDVGNGATNVIPGELKAKF 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 257 NFRYSTEVTAEQLKQRVHEILDKHGLQYEIVWNLSGLPFLTPVGELVNAAQTAILNVTGTETELSTSGGTSDGRFIAPTG 336
Cdd:cd03891 251 NIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELSTSGGTSDARFIASYG 330
|
330 340 350
....*....|....*....|....*....|....*.
gi 446939317 337 AQVLELGVLNATIHQINEHVDVHDLDPLTDIYEQIL 372
Cdd:cd03891 331 CPVVEFGLVNATIHKVNERVSVADLEKLTDIYERIL 366
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
17-375 |
0e+00 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 593.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 17 PSVTPIDHTCQTIMADRLAKVGFHIEPMRFGDVDNLWARRGTEGPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYG 96
Cdd:TIGR01246 12 PSVTPNDAGCQDIIAERLEKLGFEIEWMHFGDTKNLWATRGTGEPVLAFAGHTDVVPAGPEEQWSSPPFEPVERDGKLYG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 97 RGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEGPAVNGTVKVIETLEKRNEKITWCLVGEPSSTHKLGDIVK 176
Cdd:TIGR01246 92 RGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVETLMARDELIDYCIVGEPSSVKKLGDVIK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 177 NGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDNGNEYFPATSFQISNIHAGTGATNVIPGALEVTF 256
Cdd:TIGR01246 172 NGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAIKWDEGNEFFPPTSLQITNIHAGTGANNVIPGELYVQF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 257 NFRYSTEVTAEQLKQRVHEILDKHGLQYEIVWNLSGLPFLTPVGELVNAAQTAILNVTGTETELSTSGGTSDGRFIAPTG 336
Cdd:TIGR01246 252 NLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELSTGGGTSDGRFIALMG 331
|
330 340 350
....*....|....*....|....*....|....*....
gi 446939317 337 AQVLELGVLNATIHQINEHVDVHDLDPLTDIYEQILENL 375
Cdd:TIGR01246 332 AEVVEFGPVNATIHKVNECVSIEDLEKLSDVYQDLLENL 370
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
17-377 |
9.03e-122 |
|
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: 357.27 E-value: 9.03e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 17 PSVTPIDHTCQTIMADRLAKVGFHIEPMRF-GDVDNLWARR-GTEG-PVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGK 93
Cdd:COG0624 25 PSVSGEEAAAAELLAELLEALGFEVERLEVpPGRPNLVARRpGDGGgPTLLLYGHLDVVPPGDLELWTSDPFEPTIEDGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 94 LYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEGPAvNGTVKVIETLeKRNEKITWCLVGEPSSThklgD 173
Cdd:COG0624 105 LYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGS-PGARALVEEL-AEGLKADAAIVGEPTGV----P 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 174 IVKNGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDNG-NEYFPATSFQISNIHAGTgATNVIPGAL 252
Cdd:COG0624 179 TIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRaDPLFGRTTLNVTGIEGGT-AVNVIPDEA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 253 EVTFNFRYSTEVTAEQLKQRVHEILDKHGLQYEIVW---NLSGLPFLTPV-GELVNAAQTAILNVTGTETELSTSGGTSD 328
Cdd:COG0624 258 EAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEVevlGDGRPPFETPPdSPLVAAARAAIREVTGKEPVLSGVGGGTD 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446939317 329 GRFIA-PTGAQVLELGVLN-ATIHQINEHVDVHDLDPLTDIYEQILENLLA 377
Cdd:COG0624 338 ARFFAeALGIPTVVFGPGDgAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
17-372 |
7.23e-107 |
|
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: 318.09 E-value: 7.23e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 17 PSVTPIDHTCQTIMADRLAKVGFHIEPMRFGDVDNLWARRGTE-GPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLY 95
Cdd:cd08659 10 PSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVATVGGGdGPVLLLNGHIDTVPPGDGDKWSFPPFSGRIRDGRLY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 96 GRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEGpAVNGTVKVIETLekRNEKITWCLVGEPSsthklGDIV 175
Cdd:cd08659 90 GRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEV-GSDGARALLEAG--YADRLDALIVGEPT-----GLDV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 176 KNGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWD-NGNEYFPATSFQISNIHAGTgATNVIPGALEV 254
Cdd:cd08659 162 VYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEElPAHPLLGPPTLNVGVINGGT-QVNSIPDEATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 255 TFNFRYSTEVTAEQLKQRVHEILDKHGLQYEIVWNLSGLP--FLTPVGELVNAAQTAILNVTGTEtELSTSGGTSDGRFI 332
Cdd:cd08659 241 RVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPpfFTDPDHPLVQALQAAARALGGDP-VVRPFTGTTDASYF 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446939317 333 APT-GAQVLELGVLN-ATIHQINEHVDVHDLDPLTDIYEQIL 372
Cdd:cd08659 320 AKDlGFPVVVYGPGDlALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
64-374 |
4.33e-84 |
|
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: 258.43 E-value: 4.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 64 CFAGHTDVVPTGRLDAWnsdPFAPEIrDGKLYGRGSADMKTALAAMVVASERFVAKHPNhKGSIAFLITSDEEGPaVNGT 143
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGG-MGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 144 VKVIETLEKRNEKITWCL---VGEPSS-THKLGDIVKNGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQT 219
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFglhIGEPTLlEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 220 VWDNGNEYFPATsFQISNIHAGTGATNVIPGALEVTFNFRYSTEVTAEQLKQRVHEILDK----HGLQYEIVWNLSGLPF 295
Cdd:pfam01546 155 VSRNVDPLDPAV-VTVGNITGIPGGVNVIPGEAELKGDIRLLPGEDLEELEERIREILEAiaaaYGVKVEVEYVEGGAPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 296 LTPVGELVNAAQTAILNVTGTETELSTSG--GTSDGRFIAP-TGAQVLELGVLNATIHQINEHVDVHDLDPLTDIYEQIL 372
Cdd:pfam01546 234 LVNDSPLVAALREAAKELFGLKVELIVSGsmGGTDAAFFLLgVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLL 313
|
..
gi 446939317 373 EN 374
Cdd:pfam01546 314 LK 315
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
17-367 |
2.29e-52 |
|
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: 178.36 E-value: 2.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 17 PSVTPI---DHTCQTIMADRLAKVGFHIEPMRFGDVDNLWARR------GT-EGPVFCFAGHTDVVPTGRLDAWNSDPFA 86
Cdd:TIGR01910 11 PSVNPPggnEETIANYIKDLLREFGFSTDVIEITDDRLKVLGKvvvkepGNgNEKSLIFNGHYDVVPAGDLELWKTDPFK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 87 PEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEgpavNGTVKVIETLEKRNEKIT-WCLVGEP 165
Cdd:TIGR01910 91 PVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEE----SGEAGTLYLLQRGYFKDAdGVLIPEP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 166 SSthklGDIVKNGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTV--WDNGNEYFP---ATSFQISNIHA 240
Cdd:TIGR01910 167 SG----GDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEehIYARNSYGFipgPITFNPGVIKG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 241 GTGAtNVIPGALEVTFNFRYSTEVTAEQLKQRVHEILDKHGLQ------YEIVWNLSGLPFLTPVGELVNAAQTAILNVT 314
Cdd:TIGR01910 243 GDWV-NSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSdgwlyeNEPVVKWSGPNETPPDSRLVKALEAIIKKVR 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446939317 315 GTETELSTSGGTSDGRFIAPTGAQVLELGV-LNATIHQINEHVDVHDLDPLTDI 367
Cdd:TIGR01910 322 GIEPEVLVSTGGTDARFLRKAGIPSIVYGPgDLETAHQVNEYISIKNLVESTKV 375
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
31-373 |
1.23e-50 |
|
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: 173.55 E-value: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 31 ADRLAKVGFHIEPMRFGDVD--NLWARRGTEG-PVFCFAGHTDVVPT-GrlDAWNSDPFAPEIRDGKLYGRGSADMKTAL 106
Cdd:cd03894 25 ADYLAALGVKSRRVPVPEGGkaNLLATLGPGGeGGLLLSGHTDVVPVdG--QKWSSDPFTLTERDGRLYGRGTCDMKGFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 107 AAMVVASERFVAKHPnhKGSIAFLITSDEEgpaVN--GTVKVIETLEKRNEKITWCLVGEPSSThklgdIVKNGRRGSLN 184
Cdd:cd03894 103 AAVLAAVPRLLAAKL--RKPLHLAFSYDEE---VGclGVRHLIAALAARGGRPDAAIVGEPTSL-----QPVVAHKGIAS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 185 AVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTV--WDNG--NEYF--PATSFQISNIHAGTgATNVIPGALEVTFNF 258
Cdd:cd03894 173 YRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELAdrLAPGlrDPPFdpPYPTLNVGLIHGGN-AVNIVPAECEFEFEF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 259 RYSTEVTAEQLKQRVHEILDKHGLQY----EIVWNLSGLPFLTPV-GELVNAAQTAilnvTGTETELSTSGGTsDGRFIA 333
Cdd:cd03894 252 RPLPGEDPEAIDARLRDYAEALLEFPeagiEVEPLFEVPGLETDEdAPLVRLAAAL----AGDNKVRTVAYGT-EAGLFQ 326
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446939317 334 PTGAQVLELGVLN-ATIHQINEHVDVHDLDPLTDIYEQILE 373
Cdd:cd03894 327 RAGIPTVVCGPGSiAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
30-377 |
2.91e-50 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 173.25 E-value: 2.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 30 MADRLAKVGFHIEPMRFGDV---------DNLWARRGTEGPVFCFAGHTDVVPTGrlDAWNS-DPFAPEIRDGKLYGRGS 99
Cdd:PRK08651 35 LRDTLEELGFSTEIIEVPNEyvkkhdgprPNLIARRGSGNPHLHFNGHYDVVPPG--EGWSVnVPFEPKVKDGKVYGRGA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 100 ADMKTALAAMVVASERFvakHPNHKGSIAFLITSDEEgpaVNGTvKVIETLEKRNEKITWCLVGEPSSThklgDIVKNGR 179
Cdd:PRK08651 113 SDMKGGIAALLAAFERL---DPAGDGNIELAIVPDEE---TGGT-GTGYLVEEGKVTPDYVIVGEPSGL----DNICIGH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 180 RGSLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDNGNEY---FPATSFQISNIHA----GTGATNVIPGAL 252
Cdd:PRK08651 182 RGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYeydDERGAKPTVTLGGptveGGTKTNIVPGYC 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 253 EVTFNFRYSTEVTAEQLKQRVHEILDK------HGLQYEIVwNLSGlPFLT-PVGELVNAAQTAILNVTGTETELSTSGG 325
Cdd:PRK08651 262 AFSIDRRLIPEETAEEVRDELEALLDEvapelgIEVEFEIT-PFSE-AFVTdPDSELVKALREAIREVLGVEPKKTISLG 339
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 446939317 326 TSDGRFIAPTGAQVL-----ELGVlnatIHQINEHVDVHDLDPLTDIYEQILENLLA 377
Cdd:PRK08651 340 GTDARFFGAKGIPTVvygpgELEL----AHAPDEYVEVKDVEKAAKVYEEVLKRLAK 392
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
39-369 |
1.78e-41 |
|
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: 149.07 E-value: 1.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 39 FHIEPMRFGDVDNLWARRGteGPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVA 118
Cdd:cd08011 41 HEPPEEIYGVVSNIVGGRK--GKRLLFNGHYDVVPAGDGEGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 119 KHPNHKGSIAFLITSDEEGPAVNGTVKVietLEKRNEKITWCLVGEPSSThklgDIVKNGRRGSLNAVLKVQGKQGHVAY 198
Cdd:cd08011 119 AKAPWDLPVVLTFVPDEETGGRAGTKYL---LEKVRIKPNDVLIGEPSGS----DNIRIGEKGLVWVIIEITGKPAHGSL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 199 PHLARNPIHEASPALAELcqtvwdnGNEYfpaTSFQISNIHAGTgATNVIPGALEVTFNFRYSTEVTAEQLKQRVHEILD 278
Cdd:cd08011 192 PHRGESAVKAAMKLIERL-------YELE---KTVNPGVIKGGV-KVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 279 K-HGLQYEIVWNLSGlPFLTPVGELVNAAQTAILNVTGTETELSTSGGTSDGRFIAPTG--AQVLELGVLNaTIHQINEH 355
Cdd:cd08011 261 SiEEVSFEIKSFYSP-TVSNPDSEIVKKTEEAITEVLGIRPKEVISVGASDARFYRNAGipAIVYGPGRLG-QMHAPNEY 338
|
330
....*....|....
gi 446939317 356 VDVHDLDPLTDIYE 369
Cdd:cd08011 339 VEIDELIKVIKVHA 352
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
51-377 |
1.90e-39 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 144.26 E-value: 1.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 51 NLWARRGTEGPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVAS-ERFVAKHPNHkGSIAF 129
Cdd:PRK08588 50 NLVAEIGSGSPVLALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMiELKEQGQLLN-GTIRL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 130 LITSDEE----GPAV---NGTVKVIETLekrnekitwcLVGEPSS-----THKlgdivkngrrGSLNAVLKVQGKQGHVA 197
Cdd:PRK08588 129 LATAGEEvgelGAKQlteKGYADDLDAL----------IIGEPSGhgivyAHK----------GSMDYKVTSTGKAAHSS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 198 YPHLARNPI-------HEASPALAELCQTvwdngNEYFPATSFQISNIHAGTgATNVIPGALEVTFNFRYSTEVTAEQLK 270
Cdd:PRK08588 189 MPELGVNAIdpllefyNEQKEYFDSIKKH-----NPYLGGLTHVVTIINGGE-QVNSVPDEAELEFNIRTIPEYDNDQVI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 271 QRVHEILDK------HGLQYEIVWNLSglPFLT-PVGELVNAAQTAILNVTGTETELSTSGGTSDG-RFI-APTGAQVLE 341
Cdd:PRK08588 263 SLLQEIINEvnqngaAQLSLDIYSNHR--PVASdKDSKLVQLAKDVAKSYVGQDIPLSAIPGATDAsSFLkKKPDFPVII 340
|
330 340 350
....*....|....*....|....*....|....*..
gi 446939317 342 LGV-LNATIHQINEHVDVHDLDPLTDIYEQILENLLA 377
Cdd:PRK08588 341 FGPgNNLTAHQVDEYVEKDMYLKFIDIYKEIIIQYLK 377
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
31-275 |
1.45e-36 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 136.47 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 31 ADRLAKVGfhIEPMRF----GDVDNLWARRG-TEGPVFCFAGHTDVVP-TGRldAWNSDPFAPEIRDGKLYGRGSADMKT 104
Cdd:PRK07522 32 RDYLAAHG--VESELIpdpeGDKANLFATIGpADRGGIVLSGHTDVVPvDGQ--AWTSDPFRLTERDGRLYGRGTCDMKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 105 ALAAMVVASERFVA---KHPNHkgsIAFliTSDEEGpavnGTVKV---IETLEKRNEKITWCLVGEPSSthkLGDIVknG 178
Cdd:PRK07522 108 FIAAALAAVPELAAaplRRPLH---LAF--SYDEEV----GCLGVpsmIARLPERGVKPAGCIVGEPTS---MRPVV--G 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 179 RRGSLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQ-----TVWDNGNEYF--PATSFQISNIHAGTgATNVIPGA 251
Cdd:PRK07522 174 HKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDladrlAAPGPFDALFdpPYSTLQTGTIQGGT-ALNIVPAE 252
|
250 260
....*....|....*....|....
gi 446939317 252 LEVTFNFRYSTEVTAEQLKQRVHE 275
Cdd:PRK07522 253 CEFDFEFRNLPGDDPEAILARIRA 276
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
24-377 |
2.79e-35 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 134.12 E-value: 2.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 24 HTCQTIMADRLAKVGFHIEPMRF----GDVD-----NLWARR--GTEGPVFCFAGHTDVVPTGrlDAWNSDPFAPEIRDG 92
Cdd:PRK13013 37 REICEFLAARLAPRGFEVELIRAegapGDSEtyprwNLVARRqgARDGDCVHFNSHHDVVEVG--HGWTRDPFGGEVKDG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 93 KLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEGPAVNGTVKVIETLEKRNEKITWCLVGEPssTHKlg 172
Cdd:PRK13013 115 RIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGGVAYLAEQGRFSPDRVQHVIIPEP--LNK-- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 173 DIVKNGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELcqtvwdnGNEYFPA-----------------TSFQI 235
Cdd:PRK13013 191 DRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEI-------EERLFPLlatrrtampvvpegarqSTLNI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 236 SNIHAG--------TG-ATNVIPGALEVTFNFRYSTEVTAEQLKQRVHEILDK-----HGLQYEIVWNLSGLPFLTPVGE 301
Cdd:PRK13013 264 NSIHGGepeqdpdyTGlPAPCVADRCRIVIDRRFLIEEDLDEVKAEITALLERlkrarPGFAYEIRDLFEVLPTMTDRDA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 302 -LVNAAQTAILNVTGTETELSTSGGTSDGRFIA---------PTGAQVLELGvlnatiHQINEHVDVHDLDPLTDIYEQI 371
Cdd:PRK13013 344 pVVRSVAAAIERVLGRQADYVVSPGTYDQKHIDrigklknciAYGPGILDLA------HQPDEWVGIADMVDSAKVMALV 417
|
....*.
gi 446939317 372 LENLLA 377
Cdd:PRK13013 418 LADLLA 423
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
28-371 |
3.20e-32 |
|
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: 124.55 E-value: 3.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 28 TIMADRLAKVGFHIEPMRFGDVD---NLWARRGTEGPV-FCFAGHTDVVPTGRlDAWNSDPFAPEIRDGKLYGRGSADMK 103
Cdd:TIGR01892 22 DWAQAYLEALGFSVEVQPFPDGAeksNLVAVIGPSGAGgLALSGHTDVVPYDD-AAWTRDPFRLTEKDGRLYGRGTCDMK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 104 TALAAMVVASERFVAKhpNHKGSIAFLITSDEEgPAVNGTVKVIETLEKRNEKItwcLVGEPSSThklgdIVKNGRRGSL 183
Cdd:TIGR01892 101 GFLACALAAAPDLAAE--QLKKPLHLALTADEE-VGCTGAPKMIEAGAGRPRHA---IIGEPTRL-----IPVRAHKGYA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 184 NAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDNGNEYF------PATSFQISNIHAGTgATNVIPGALEVTFN 257
Cdd:TIGR01892 170 SAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDLdegftpPYTTLNIGVIQGGK-AVNIIPGACEFVFE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 258 FRYSTEVTAEQLKQRVHEI---LDKHGLQYEIVWNL-SGLPFLT--PVGELVNAAQTAilnvTGTETElSTSGGTSDGRF 331
Cdd:TIGR01892 249 WRPIPGMDPEELLQLLETIaqaLVRDEPGFEVQIEVvSTDPGVNtePDAELVAFLEEL----SGNAPE-VVSYGTEAPQF 323
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 446939317 332 I-APTGAQVLELGVLNATiHQINEHVDVHDLDPLTDIYEQI 371
Cdd:TIGR01892 324 QeLGAEAVVCGPGDIRQA-HQPDEYVEIEDLVRCRAVLARL 363
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
29-358 |
5.92e-32 |
|
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: 123.47 E-value: 5.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 29 IMADRLAKVGFHIEPMRFGDV-DNLWAR-RGTEGPVFCFAGHTDVV-PTGRLDAWnsdPFapEIRDGKLYGRGSADMKTA 105
Cdd:cd03885 27 LLAEELEALGFTVERRPLGEFgDHLIATfKGTGGKRVLLIGHMDTVfPEGTLAFR---PF--TVDGDRAYGPGVADMKGG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 106 LAAMVVASERFVAKHPNHKGSIAFLITSDEEgPAVNGTVKVIETlEKRNEKItwCLVGEPSSThklGDIVKNGRRGSLNA 185
Cdd:cd03885 102 LVVILHALKALKAAGGRDYLPITVLLNSDEE-IGSPGSRELIEE-EAKGADY--VLVFEPARA---DGNLVTARKGIGRF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 186 VLKVQGKQGHV-AYPHLARNPIHEASP---ALAELcqtvwdngNEYFPATSFQISNIHAGTGaTNVIPGALEVTFNFRYS 261
Cdd:cd03885 175 RLTVKGRAAHAgNAPEKGRSAIYELAHqvlALHAL--------TDPEKGTTVNVGVISGGTR-VNVVPDHAEAQVDVRFA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 262 TEVTAEQLKQRVHEILDKH---GLQYEIVWNLSGLPFL-TPVGE-LVNAAQTAILNVTGTETELSTsGGTSDGRFIAPTG 336
Cdd:cd03885 246 TAEEADRVEEALRAIVATTlvpGTSVELTGGLNRPPMEeTPASRrLLARAQEIAAELGLTLDWEAT-GGGSDANFTAALG 324
|
330 340
....*....|....*....|...
gi 446939317 337 AQVLE-LGVLNATIHQINEHVDV 358
Cdd:cd03885 325 VPTLDgLGPVGGGAHTEDEYLEL 347
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
177-285 |
1.15e-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: 107.43 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 177 NGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDNGNeYFPATSFQISNIHAGTgATNVIPGALEVTF 256
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGF-DFPRTTLNITGIEGGT-ATNVIPAEAEAKF 78
|
90 100
....*....|....*....|....*....
gi 446939317 257 NFRYSTEVTAEQLKQRVHEILDKHGLQYE 285
Cdd:pfam07687 79 DIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
17-361 |
1.51e-26 |
|
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: 109.32 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 17 PSVTPIDHTCQTIMADRLAKVG-----FHIEPMR------FGDVDNLWAR----------RGTEGPVFCFAGHTDVVPTG 75
Cdd:cd03895 10 PSLRGEEAAAQDLVAAALRSRGytvdrWEIDVEKlkhhpgFSPVAVDYAGapnvvgthrpRGETGRSLILNGHIDVVPEG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 76 RLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEGPAvNGTVKVIEtlekRNE 155
Cdd:cd03895 90 PVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTG-NGALAALM----RGY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 156 KITWCLVGEPSStHKLgdIVKNGrrGSLNAVLKVQGKQGHVAYPHLARNPIHEASP---ALAELcQTVWDNGNEYFPATS 232
Cdd:cd03895 165 RADAALIPEPTE-LKL--VRAQV--GVIWFRVKVRGTPAHVAEASEGVNAIEKAMHliqALQEL-EREWNARKKSHPHFS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 233 -------FQISNIHAGTGATNVipgALEVTFNFRY------STEVTAEQLKQRVHEILDKH----GLQYEIVWN-LSGLP 294
Cdd:cd03895 239 dhphpinFNIGKIEGGDWPSSV---PAWCVLDCRIgiypgeSPEEARREIEECVADAAATDpwlsNHPPEVEWNgFQAEG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446939317 295 F-LTPVGELVNAAQTAILNVTGTETELSTSGGTSDGRFIAPTGA-QVLELGVLNATIHQINEHVDVHDL 361
Cdd:cd03895 316 YvLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGDiPALCYGPGSRDAHGFDESVDLESL 384
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
40-372 |
2.01e-26 |
|
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: 107.91 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 40 HIEPMRFGDvdNLWAR--RGTEGPVFcFAGHTDVVPTgrldawnSDPFAPEIR-DGKLYGRGSADMKTALAAMVVASERF 116
Cdd:cd05647 34 HLEVIRDGN--TVVARteRGLASRVI-LAGHLDTVPV-------AGNLPSRVEeDGVLYGCGATDMKAGDAVQLKLAATL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 117 VAKHPNHkgSIAFLITSDEEGPA-VNGTVKVIEtleKRNEKIT--WCLVGEPSsthklGDIVKNGRRGSLNAVLKVQGKQ 193
Cdd:cd05647 104 AAATLKH--DLTLIFYDCEEVAAeLNGLGRLAE---EHPEWLAadFAVLGEPT-----DGTIEGGCQGTLRFKVTTHGVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 194 GHVAYPHLARNPIHEASPALAELcqtvwdngNEYFPAT-------------SFQISnihaGTGATNVIPGALEVTFNFRY 260
Cdd:cd05647 174 AHSARSWLGENAIHKLAPILARL--------AAYEPRTvnidgltyreglnAVFIS----GGVAGNVIPDEARVNLNYRF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 261 STEVTAEQLKQRVHEILDKHGLQYEIVwNLSG--LPFL-TPVG-ELVNAAQtailnvtgtETELSTSGGTSDGRFIApTG 336
Cdd:cd05647 242 APDKSLAEAIAHVREVFEGLGYEIEVT-DLSPgaLPGLdHPVArDLIEAVG---------GKVRAKYGWTDVARFSA-LG 310
|
330 340 350
....*....|....*....|....*....|....*..
gi 446939317 337 AQVLELGVLNATI-HQINEHVDVHDLDPLTDIYEQIL 372
Cdd:cd05647 311 IPAVNFGPGDPLLaHKRDEQVPVEQITACAAILRRWL 347
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
67-374 |
9.11e-26 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 107.24 E-value: 9.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 67 GHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEgpavNGTVKV 146
Cdd:PRK13983 83 SHMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEE----TGSKYG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 147 IETLEKRNEKIT----WCLVgePSSTHKLGDIVKNGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASP---ALAELCQT 219
Cdd:PRK13983 159 IQYLLKKHPELFkkddLILV--PDAGNPDGSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRAAADfalELDEALHE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 220 VWDNGNEYF--PATSFQISNIHAGTGATNVIPGalEVTFNF------RYSTEVTAEQLKQRVHEILDKHG--LQYEIVWN 289
Cdd:PRK13983 237 KFNAKDPLFdpPYSTFEPTKKEANVDNINTIPG--RDVFYFdcrvlpDYDLDEVLKDIKEIADEFEEEYGvkIEVEIVQR 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 290 LSGLPFLTPVGELVNAAQTAILNVTGTETELSTSGGTSDGRFIAPTGAQVLELGVLNATIHQINEHVDVHDLDPLTDIYE 369
Cdd:PRK13983 315 EQAPPPTPPDSEIVKKLKRAIKEVRGIEPKVGGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYAKISNLIEDAKVFA 394
|
....*
gi 446939317 370 QILEN 374
Cdd:PRK13983 395 LLLLE 399
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
31-377 |
2.13e-25 |
|
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: 106.26 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 31 ADRLAKVGFHIEPMRFGDVDN-LWARRGTEG--PVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTALA 107
Cdd:cd03893 31 ADLLRRLGFTVEIVDTSNGAPvVFAEFPGAPgaPTVLLYGHYDVQPAGDEDGWDSDPFELTERDGRLYGRGAADDKGPIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 108 AMVVASERFVAKHPNHKGSIAFLITSDEEgpavNGTVKVIETLEKRNE--KITWCLVGEPSSTHKLGDIVKNGRRGSLNA 185
Cdd:cd03893 111 AHLAALRALMQQGGDLPVNVKFIIEGEEE----SGSPSLDQLVEAHRDllAADAIVISDSTWVGQEQPTLTYGLRGNANF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 186 VLKVQGKQGHVaypH--LARNPIHEASPALAELCQTVWDNGNE------YF-----PATSFQIS---------------- 236
Cdd:cd03893 187 DVEVKGLDHDL---HsgLYGGVVPDPMTALAQLLASLRDETGRilvpglYDavrelPEEEFRLDagvleeveiiggttgs 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 237 -----------NIHA------GTGATNVIPGALEVTFNFRYSTEVTAEQLKQRVHEILDKH---GLQYEIVWNLSGLPFL 296
Cdd:cd03893 264 vaerlwtrpalTVLGidggfpGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLEAHLEKHapsGAKVTVSYVEGGMPWR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 297 TPV-GELVNAAQTAILNVTGTETELSTSGGT--SDGRFIAPTGAQVLELGVLNAT--IHQINEHVDVHDLDPLTdiyeQI 371
Cdd:cd03893 344 SDPsDPAYQAAKDALRTAYGVEPPLTREGGSipFISVLQEFPQAPVLLIGVGDPDdnAHSPNESLRLGNYKEGT----QA 419
|
....*.
gi 446939317 372 LENLLA 377
Cdd:cd03893 420 EAALLY 425
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
57-372 |
2.39e-25 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 105.62 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 57 GTEGPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEE 136
Cdd:cd05650 66 GGNDKTLWIISHLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 137 GPAVNGtvkVIETLEKRNEKITWCLVGEPSSTHKLGDIVKNGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASP---AL 213
Cdd:cd05650 146 DGSEYG---IQYLLNKFDLFKKDDLIIVPDFGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNfalEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 214 AELCQTVWDNGNEYF--PATSFQISNIHAGTGATNVIPGALEVTFNFR----YSTEVTAEQLKQRVHEI--LDKHGLQYE 285
Cdd:cd05650 223 DELLHEKFDEKDDLFnpPYSTFEPTKKEANVPNVNTIPGYDVFYFDCRvlptYKLDEVLKFVNKIISDFenSYGAGITYE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 286 IVWNLSGLPFLTPVGELVNAAQTAILNVTGTETELSTSGGTSDGRFIAPTGAQVLELGVLNATIHQINEHVDVHDLDPLT 365
Cdd:cd05650 303 IVQKEQAPPATPEDSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYIRISHIVKDA 382
|
....*..
gi 446939317 366 DIYEQIL 372
Cdd:cd05650 383 KVFAEML 389
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
67-368 |
1.14e-24 |
|
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: 104.63 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 67 GHTDVVPTGrlDAWNSDPFAPEIRDGKLYGRGSADMK----TALAAMvvaseRFVAKH---PNHKgsIAFLITSDEEG-- 137
Cdd:cd03888 78 GHLDVVPAG--EGWTTDPFKPVIKDGKLYGRGTIDDKgptiAALYAL-----KILKDLglpLKKK--IRLIFGTDEETgw 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 138 -----------------------PAVNG-----TVKVI------------------------ETLEKRNEKITWCLVGEP 165
Cdd:cd03888 149 kciehyfeheeypdfgftpdaefPVINGekgivTVDLTfkidddkgyrlisikggeatnmvpDKAEAVIPGKDKEELALS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 166 SSTHKLGDI-VKNGrrgslNAVLKVQGKQGHVAYPHLARNPIheasPALAELCQTVWDNGNEYfPATSFQISNIHAGT-- 242
Cdd:cd03888 229 AATDLKGNIeIDDG-----GVELTVTGKSAHASAPEKGVNAI----TLLAKFLAELNKDGNDK-DFIKFLAKNLHEDYng 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 243 -------------------GATNVIPGALEVTFNFRYSTEVTAEQLKQRVHEILDKHGLQYEIVWNLSglPFLTPV-GEL 302
Cdd:cd03888 299 kklginfedevmgeltlnpGIITLDDGKLELGLNVRYPVGTSAEDIIKQIEEALEKYGVEVEGHKHQK--PLYVPKdSPL 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446939317 303 VNAAQTAILNVTGTETELSTSGGTSDGRFIaPTGAQV--LELGVlNATIHQINEHVDVHDLDPLTDIY 368
Cdd:cd03888 377 VKTLLKVYEEQTGKEGEPVAIGGGTYAREL-PNGVAFgpEFPGQ-KDTMHQANEFIPIDDLIKALAIY 442
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
17-372 |
1.41e-24 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 102.77 E-value: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 17 PSVTPIDHTCQTIMADRLAKVGFHIEpmRFGDvdNLWARRG---TEGPVFCFAGHTDVVPTGRldAWNSDPFAPEIRDGK 93
Cdd:cd05651 13 PSFSREEHKTADLIENYLEQKGIPFK--RKGN--NVWAENGhfdEGKPTLLLNSHHDTVKPNA--GWTKDPFEPVEKGGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 94 LYGRGSADMKTALAAMVVASERFVAKHPnHKGSIAFLITSDEEGPAVNGtvkvIETLEKRNEKITWCLVGEPSSTHklgd 173
Cdd:cd05651 87 LYGLGSNDAGASVVSLLATFLHLYSEGP-LNYNLIYAASAEEEISGKNG----IESLLPHLPPLDLAIVGEPTEMQ---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 174 iVKNGRRGSLNAVLKVQGKQGHVAYPHlARNPIHEASPALAELCQTVWDNGNEYFPATSFQISNIHAGTgATNVIPGALE 253
Cdd:cd05651 158 -PAIAEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDIQWLRDFRFDKVSPLLGPVKMTVTQINAGT-QHNVVPDSCT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 254 VTFNFR----YSTEVTAEQLKQRVHEILDKHGLQYeivwNLSGLPFLTPvgeLVNAAQTAILNVTGTETelstsggTSDG 329
Cdd:cd05651 235 FVVDIRtteaYTNEEIFEIIRGNLKSEIKPRSFRL----NSSAIPPDHP---IVQAAIAAGRTPFGSPT-------LSDQ 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446939317 330 RFIaptGAQVLELGVLNAT-IHQINEHVDVHDLDPLTDIYEQIL 372
Cdd:cd05651 301 ALM---PFPSVKIGPGDSSrSHTADEFIELSEIEEGIDIYIELL 341
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
48-375 |
1.76e-24 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 102.43 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 48 DVDNLWARRGTEGPVFCFAGHTDVVPtGRLDawnsdpfaPEIRDGKLYGRGSADMKTALAAMVVAserFVAKHPNHKGSI 127
Cdd:cd05653 42 EAGNAVGGAGSGPPDVLLLGHIDTVP-GEIP--------VRVEGGVLYGRGAVDAKGPLAAMILA---ASALNEELGARV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 128 AFLITSDEEGPAvNGTVKVIEtlekRNEKITWCLVGEPSSThklgDIVKNGRRGSLNAVLKVQGKQGHVAYPhlARNPIH 207
Cdd:cd05653 110 VVAGLVDEEGSS-KGARELVR----RGPRPDYIIIGEPSGW----DGITLGYRGSLLVKIRCEGRSGHSSSP--ERNAAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 208 EASPALAELCQTVWDNGNEYFPATSFQISNIHAGTgATNVIPGALEVTFNFRYSTEVTAEQLKQRVHEILDkhGLQYEIV 287
Cdd:cd05653 179 DLIKKWLEVKKWAEGYNVGGRDFDSVVPTLIKGGE-SSNGLPQRAEATIDLRLPPRLSPEEAIALATALLP--TCELEFI 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 288 WNLSglPFLTPVGE-LVNAAQTAILNVTGTETeLSTSGGTSDGRFIAPT-GAQVLELGVLNATI-HQINEHVDVHDLDPL 364
Cdd:cd05653 256 DDTE--PVKVSKNNpLARAFRRAIRKQGGKPR-LKRKTGTSDMNVLAPLwTVPIVAYGPGDSTLdHTPNEHIELAEIERA 332
|
330
....*....|.
gi 446939317 365 TDIYEQILENL 375
Cdd:cd05653 333 AAVLKGALEEL 343
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
17-278 |
1.65e-23 |
|
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: 99.66 E-value: 1.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 17 PSVTPIDHTCQTIMADRLAKVGFHIE--PMRFGDVDNLWARRG-TEGPVFCFAGHTDVVPtgrldawnsdPFAP---EIR 90
Cdd:cd05652 12 PSISGNEAAVGDFLAEYLESLGFTVEkqPVENKDRFNVYAYPGsSRQPRVLLTSHIDTVP----------PFIPysiSDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 91 DGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEgpavNGTVKVIETLEKRNEKITWCLVGEPSSThK 170
Cdd:cd05652 82 GDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEE----TGGDGMKAFNDLGLNTWDAVIFGEPTEL-K 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 171 LGdivkNGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDnGNEYFPATSFQISNIHAGTgATNVIPG 250
Cdd:cd05652 157 LA----SGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLP-SSELLGPTTLNIGRISGGV-AANVVPA 230
|
250 260 270
....*....|....*....|....*....|
gi 446939317 251 ALEVTFNFR--YSTEVTAEQLKQRVHEILD 278
Cdd:cd05652 231 AAEASVAIRlaAGPPEVKDIVKEAVAGILT 260
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
51-178 |
3.00e-23 |
|
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: 95.96 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 51 NLWARRGTE--GPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIA 128
Cdd:cd18669 1 NVIARYGGGggGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446939317 129 FLITSDEEGPAVNGTVKVIETLEKRNEKITWCLVGEPSSTHKLGDIVKNG 178
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTP 130
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
30-378 |
1.95e-22 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 97.70 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 30 MADRLAKVGF---HIEPMrfgdvDNLWARRGTEGPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTAL 106
Cdd:PRK13004 41 IKEEMEKVGFdkvEIDPM-----GNVLGYIGHGKKLIAFDAHIDTVGIGDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 107 AAMVVASERFvaKHPNHKGSIAFLITS-----DEEGPAVNgtvkviETLEKRNEKITWCLVGEPSSthklGDIvKNGRRG 181
Cdd:PRK13004 116 ASMVYAAKII--KDLGLDDEYTLYVTGtvqeeDCDGLCWR------YIIEEDKIKPDFVVITEPTD----LNI-YRGQRG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 182 SLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDNGNEYF--PATsFQISNIHAGTGATNVIPGALEVTFNFR 259
Cdd:PRK13004 183 RMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNLKEDPFlgKGT-LTVSDIFSTSPSRCAVPDSCAISIDRR 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 260 ----YSTEVTAEQLKQ--RVHEILDK-----------HGLQYEI-----VWnlsglpfLTPVG-ELVNAAQTAILNVTGT 316
Cdd:PRK13004 262 ltvgETWESVLAEIRAlpAVKKANAKvsmynydrpsyTGLVYPTecyfpTW-------LYPEDhEFVKAAVEAYKGLFGK 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446939317 317 ETEL-----STSGGTSDGRFIAPT-----GAQVLElgvlnatiHQINEHVDVHDLDPLTDIYEQILENLLAQ 378
Cdd:PRK13004 335 APEVdkwtfSTNGVSIAGRAGIPTigfgpGKEPLA--------HAPNEYTWKEQLVKAAAMYAAIPKSLLKK 398
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
17-358 |
2.92e-22 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 97.38 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 17 PSVTPIDHTCQTIMADRLAKVG-----FHIEP-------------MRFGDVDNLWAR---RGTEGPVFCFAGHTDVVPTG 75
Cdd:PRK06837 33 PSTRGAEAPCQDFLARAFRERGyevdrWSIDPddlkshpgagpveIDYSGAPNVVGTyrpAGKTGRSLILQGHIDVVPEG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 76 RLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEGPAvNGTvkvIETLEkRNE 155
Cdd:PRK06837 113 PLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEESTG-NGA---LSTLQ-RGY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 156 KITWCLVGEPssthkLGDIVKNGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASP---ALAELcQTVWDN---GNEYFP 229
Cdd:PRK06837 188 RADACLIPEP-----TGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHliqALREL-EAEWNArkaSDPHFE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 230 A----TSFQISNIHAGTGATNVipgALEVTFNFRYST--EVTAEQLK----------QRVHEILDKHglQYEIVWN--LS 291
Cdd:PRK06837 262 DvphpINFNVGIIKGGDWASSV---PAWCDLDCRIAIypGVTAADAQaeieaclaaaARDDRFLSNN--PPEVVWSgfLA 336
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446939317 292 GLPFLTPVGELVNAAQTAILNVTGTETELSTSGGTSDGRFIA-PTGAQVLELGVLNATIHQINEHVDV 358
Cdd:PRK06837 337 EGYVLEPGSEAEAALARAHAAVFGGPLRSFVTTAYTDTRFYGlYYGIPALCYGPSGEGIHGFDERVDL 404
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
51-175 |
6.62e-22 |
|
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: 92.10 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 51 NLWARRGTE--GPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIA 128
Cdd:cd03873 1 NLIARLGGGegGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446939317 129 FLITSDEEGPAVNGTVKVIETLEKRNEKITWCLVGEPSSTHKLGDIV 175
Cdd:cd03873 81 VAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDATAGPILQKGV 127
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
18-372 |
2.11e-21 |
|
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: 95.12 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 18 SVTPIDHTCQTI-----MADRLAKVGFHIEPMRFGDV---DNLWARRGTEGP---VFCFAGHTDVVPTGRLDaWNSDPFA 86
Cdd:cd05675 12 TTNSGDGTGSETraaevLAARLAEAGIQTEIFVVESHpgrANLVARIGGTDPsagPLLLLGHIDVVPADASD-WSVDPFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 87 PEIRDGKLYGRGSADMKtALAAMVVASERFVAKH---PnhKGSIAFLITSDEEGPAVNGTVKVIETLEKRNEKITWCLVG 163
Cdd:cd05675 91 GEIKDGYVYGRGAVDMK-NMAAMMLAVLRHYKREgfkP--KRDLVFAFVADEEAGGENGAKWLVDNHPELFDGATFALNE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 164 EPSSTHKLGD-----IVKNGRRGSLNAVLKVQGKQGHVAYPHlARNPIHEASPALAELCQTVW----DNGNEYFPA---- 230
Cdd:cd05675 168 GGGGSLPVGKgrrlyPIQVAEKGIAWMKLTVRGRAGHGSRPT-DDNAITRLAEALRRLGAHNFpvrlTDETAYFAQmael 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 231 -----------------------------------TSFQISNIHAGTgATNVIPGALEVTFNFRYSTEVTAEQLKQRVHE 275
Cdd:cd05675 247 aggeggalmltavpvldpalaklgpsapllnamlrNTASPTMLDAGY-ATNVLPGRATAEVDCRILPGQSEEEVLDTLDK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 276 ILDKHGLQYEIVWNLSGLPflTPV-GELVNAAQTAILNV-TGTETELSTSGGTSDGRFIAPTGAQVLELGVLNAT----- 348
Cdd:cd05675 326 LLGDPDVSVEAVHLEPATE--SPLdSPLVDAMEAAVQAVdPGAPVVPYMSPGGTDAKYFRRLGIPGYGFAPLFLPpeldy 403
|
410 420
....*....|....*....|....*..
gi 446939317 349 ---IHQINEHVDVHDLDPLTDIYEQIL 372
Cdd:cd05675 404 tglFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
30-374 |
7.24e-21 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 92.96 E-value: 7.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 30 MADRLAKVGFHIE-------PMRFgdvdNLWARRGT-EGPVFcFAGHTDVVP--TGRldaWNSDPFAPEIRDGKLYGRGS 99
Cdd:PRK05111 38 LAGWFEDLGFNVEiqpvpgtRGKF----NLLASLGSgEGGLL-LAGHTDTVPfdEGR---WTRDPFTLTEHDGKLYGLGT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 100 ADMKTALAAMVVASERFVA---KHPnhkgsIAFLITSDEEgPAVNGTVKVIETLEKRNEkitWCLVGEPSS-----THKl 171
Cdd:PRK05111 110 ADMKGFFAFILEALRDIDLtklKKP-----LYILATADEE-TSMAGARAFAEATAIRPD---CAIIGEPTSlkpvrAHK- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 172 gdivkngrrGSLNAVLKVQGKQGHVAYPHLARNPI---HEASPALAELCQTVWDN-GNEYF--PATSFQISNIHAGTGAt 245
Cdd:PRK05111 180 ---------GHMSEAIRITGQSGHSSDPALGVNAIelmHDVIGELLQLRDELQERyHNPAFtvPYPTLNLGHIHGGDAP- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 246 NVIPGALEVTFNFR----YSTEVTAEQLKQRVHEILDKHGLQYEIVWNLSGLP-FLTPV-GELVNAAQtailNVTGTETE 319
Cdd:PRK05111 250 NRICGCCELHFDIRplpgMTLEDLRGLLREALAPVSERWPGRITVAPLHPPIPgYECPAdHQLVRVVE----KLLGHKAE 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 446939317 320 lSTSGGTsDGRFIAPTGAQVLELGvlNATI---HQINEHVDVHDLDPLTDIYEQILEN 374
Cdd:PRK05111 326 -VVNYCT-EAPFIQQLGCPTLVLG--PGSIeqaHQPDEYLELSFIKPTRELLRQLIHH 379
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
33-259 |
7.39e-19 |
|
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: 87.09 E-value: 7.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 33 RLAKVGF---HIEPMrfgdvDNLWARRGTEGPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAM 109
Cdd:cd05649 27 EMEKLGFdevEIDPM-----GNVIGYIGGGKKKILFDGHIDTVGIGNIDNWKFDPYEGYETDGKIYGRGTSDQKGGLASM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 110 VVASERFvaKH---PNHKGSIAFLITSDEE---GPAVNgtvkviETLEKRNEKITWCLVGEPSsthKLGdiVKNGRRGSL 183
Cdd:cd05649 102 VYAAKIM--KDlglRDFAYTILVAGTVQEEdcdGVCWQ------YISKADKIKPDFVVSGEPT---DGN--IYRGQRGRM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 184 NAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTvwdngNEYFPATSF------QISNIHAGTGATNVIPGALEVTFN 257
Cdd:cd05649 169 EIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQL-----NPNFPEAPFlgrgtlTVTDIFSTSPSRCAVPDSCRISID 243
|
..
gi 446939317 258 FR 259
Cdd:cd05649 244 RR 245
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
38-259 |
7.39e-19 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 86.79 E-value: 7.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 38 GFHIEPMRFGD-VDNLWARRGTegPVFCFAGHTDVVPTGrlDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERf 116
Cdd:PRK08737 42 GFQVEVIDHGAgAVSLYAVRGT--PKYLFNVHLDTVPDS--PHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANA- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 117 vakhpnHKGSIAFLITSDEEGpavnGTVKVIETLEKRNEKITWCLVGEPSSThklgdIVKNGRRGSLNAVLKVQGKQGHV 196
Cdd:PRK08737 117 ------GDGDAAFLFSSDEEA----NDPRCVAAFLARGIPYEAVLVAEPTMS-----EAVLAHRGISSVLMRFAGRAGHA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446939317 197 AYPH-LARNPIHEASPALAELCQTVWDNGNEYFPATS---FQISNIHAGTGAtNVIPGALEVTFNFR 259
Cdd:PRK08737 182 SGKQdPSASALHQAMRWGGQALDHVESLAHARFGGLTglrFNIGRVEGGIKA-NMIAPAAELRFGFR 247
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
17-376 |
9.09e-19 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 86.35 E-value: 9.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 17 PSVTPIDHTCQTIMADRLAKVGF--HIEPMrfGDVDNLWARRGTEgpVFcFAGHTDVVPTGRldawnsdpfAPEIRDGKL 94
Cdd:PRK08652 15 PSPSGQEDEIALHIMEFLESLGYdvHIESD--GEVINIVVNSKAE--LF-VEVHYDTVPVRA---------EFFVDGVYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 95 YGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLitSDEEGPAvNGTVKVIETLEKRnekitWCLVGEPSSTHklgdi 174
Cdd:PRK08652 81 YGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFV--SDEEEGG-RGSALFAERYRPK-----MAIVLEPTDLK----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 175 VKNGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDNGNEYFPATSFQISnihAGTGATNVIPGALEV 254
Cdd:PRK08652 148 VAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPHIGIQEI---IGGSPEYSIPALCRL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 255 TFNFRYSTEVTAEQLKQRVHEILDKHGLQYEIVWNLSGLpFLTPVGELVNAAQTAiLNVTGTETELSTSGGTSDGRFIAP 334
Cdd:PRK08652 225 RLDARIPPEVEVEDVLDEIDPILDEYTVKYEYTEIWDGF-ELDEDEEIVQLLEKA-MKEVGLEPEFTVMRSWTDAINFRY 302
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446939317 335 TGAQVLELGVLNATI-HQINEHVDVHDLDPLTDIYEQILENLL 376
Cdd:PRK08652 303 NGTKTVVWGPGELDLcHTKFERIDVREVEKAKEFLKALNEILL 345
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
66-375 |
9.93e-19 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 86.38 E-value: 9.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 66 AGHTDVVPtGRLDawnsdpfaPEIRDGKLYGRGSADMKTALAAMVVASERFvakhpNHKG-SIAFLITSDEEgpavnGTV 144
Cdd:PRK00466 66 ASHVDTVP-GYIE--------PKIEGEVIYGRGAVDAKGPLISMIIAAWLL-----NEKGiKVMVSGLADEE-----STS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 145 KVIETLEKRNEKITWCLVGEPSSThkLGDIVknGRRGSLNAVLKVQGKQGHVAYPhlARNPIHEASPALAELCQTvwdng 224
Cdd:PRK00466 127 IGAKELVSKGFNFKHIIVGEPSNG--TDIVV--EYRGSIQLDIMCEGTPEHSSSA--KSNLIVDISKKIIEVYKQ----- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 225 NEYFPATSFQISNIHAGTgATNVIPGALEVTFNFRYSTEVTAEQLKQRVHEILdkHGLQYEIVWNLSglPFLTPVGELVN 304
Cdd:PRK00466 196 PENYDKPSIVPTIIRAGE-SYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKF--QECGLKIVDETP--PVKVSINNPVV 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446939317 305 AAQTAILNVTGTETELSTSGGTSDGRFIAPTGAQVLELGVLNATI-HQINEHVDVHDLDPLTDIYEQILENL 375
Cdd:PRK00466 271 KALMRALLKQNIKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLeHTNQEKITLDEIYIAVKTYMLAIEEL 342
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
61-376 |
3.30e-17 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 82.51 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 61 PVFCFAGHTDVVPTGRlDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNhkGSIAFLITSDEEGPAV 140
Cdd:PRK08554 64 PKLLFMAHFDVVPVNP-EEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLN--GKVIFAFTGDEEIGGA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 141 NGtVKVIETLEKRNEKITWCLVGEPSsthklGDIVKNGRRGSLNAVLKVQGKQG---------------------HVAY- 198
Cdd:PRK08554 141 MA-MHIAEKLREEGKLPKYMINADGI-----GMKPIIRRRKGFGVTIRVPSEKVkvkgklreqtfeirtpvvetrHAAYf 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 199 -------PHLARNPIHEASPALAELCQTVWDNGNeYFPAtSFQISNIHAGTGA------------TNVIP---------- 249
Cdd:PRK08554 215 lpgvdthPLIAASHFLRESNVLAVSLEGKFLKGN-VVPG-EVTLTYLEPGEGEevevdlgltrllKAIVPlvrapikaek 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 250 -----------------GALEVTFNFR---YSTEVTAEQLKQRVHEILDKHGLQYEiVWNLSGLPFLTPVGELVNAAqTA 309
Cdd:PRK08554 293 ysdygvsitpnvysfaeGKHVLKLDIRamsYSKEDIERTLKEVLEFNLPEAEVEIR-TNEKAGYLFTPPDEEIVKVA-LR 370
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446939317 310 ILNVTGTETELSTSGGTSDGRFIAPTGAQVLELGVLNATIHQINEHVDVHDLDPLTDIYEQILENLL 376
Cdd:PRK08554 371 VLKELGEDAEPVEGPGASDSRYFTPYGVKAIDFGPKGGNIHGPNEYVEIDSLKKMPEVYKRIALRLL 437
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
65-377 |
3.64e-17 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 82.68 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 65 FAGHTDVVP--TGRLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEE--GPav 140
Cdd:PRK08262 116 LMAHQDVVPvaPGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEvgGL-- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 141 nGTVKVIETLEKRNEKItWCLVGE---------PSSTHKLGDI-VknGRRGSLNAVLKVQGKQGHVAYP----------- 199
Cdd:PRK08262 194 -GARAIAELLKERGVRL-AFVLDEggaitegvlPGVKKPVALIgV--AEKGYATLELTARATGGHSSMPprqtaigrlar 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 200 ---HLARNP----IH------------EASPALAELCQTVWDNG---NEYFPATSFQISNIHAGTGAT--------NVIP 249
Cdd:PRK08262 270 altRLEDNPlpmrLRgpvaemfdtlapEMSFAQRVVLANLWLFEpllLRVLAKSPETAAMLRTTTAPTmlkgspkdNVLP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 250 GALEVTFNFRYSTEVTAEQLKQRVHEILDkhGLQYEIVWnLSGLPFLTPVG-------ELVNAAQTAILNVTGTETELST 322
Cdd:PRK08262 350 QRATATVNFRILPGDSVESVLAHVRRAVA--DDRVEIEV-LGGNSEPSPVSstdsaayKLLAATIREVFPDVVVAPYLVV 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446939317 323 SGgtSDGRFIAPTGAQV-----LELGVLN-ATIHQINEHVDVHDLDPLTDIYEQILENLLA 377
Cdd:PRK08262 427 GA--TDSRHYSGISDNVyrfspLRLSPEDlARFHGTNERISVANYARMIRFYYRLIENAAG 485
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
17-375 |
7.96e-17 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 80.77 E-value: 7.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 17 PSVTPIDHTCQTIMADRLAKVGF--HIEpmrfgDVDNLWARRGTEGPVFCFAGHTDVVPtGRLdawnsdpfaP-EIRDGK 93
Cdd:PRK04443 19 PSPSGEEAAAAEFLVEFMESHGReaWVD-----EAGNARGPAGDGPPLVLLLGHIDTVP-GDI---------PvRVEDGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 94 LYGRGSADMKTALAAMVVASERFVAKHPnhkGSIAFLITSDEEGPAVNGTVKVIETlekrnEKITWCLVGEPSSThklgD 173
Cdd:PRK04443 84 LWGRGSVDAKGPLAAFAAAAARLEALVR---ARVSFVGAVEEEAPSSGGARLVADR-----ERPDAVIIGEPSGW----D 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 174 IVKNGRRGSLNAVLKVQGKQGHVAypHLARNPIHEASP---ALAELCQtVWDNGNEYFPATSFQISNIHAGTGATNVipg 250
Cdd:PRK04443 152 GITLGYKGRLLVTYVATSESFHSA--GPEPNAAEDAIEwwlAVEAWFE-ANDGRERVFDQVTPKLVDFDSSSDGLTV--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 251 ALEVTFNFRYSTEVTAEqlkqRVHEILDKHGLQYEIVWNLSGLPFLT-PVGELVNAAQTAILNVTGTETELSTSgGTSDG 329
Cdd:PRK04443 226 EAEMTVGLRLPPGLSPE----EAREILDALLPTGTVTFTGAVPAYMVsKRTPLARAFRVAIREAGGTPRLKRKT-GTSDM 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446939317 330 RFIAPT-GAQVLELGVLNATI-HQINEHVDVHDLDPLTDIYEQILENL 375
Cdd:PRK04443 301 NVVAPAwGCPMVAYGPGDSDLdHTPDEHLPLAEYLRAIAVLTDVLERL 348
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
61-375 |
9.23e-17 |
|
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: 80.99 E-value: 9.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 61 PVFCFAGHTDVVPTGRlDAWNSDPFAPEI-RDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEGPA 139
Cdd:TIGR01880 72 PSILLNSHTDVVPVFR-EHWTHPPFSAFKdEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 140 VNGTVKVIETLEKRNEKITWCL-VGEPSSTHKLGdiVKNGRRGSLNAVLKVQGKQGHVA--YPHLARNPIHEASPALAEL 216
Cdd:TIGR01880 151 HDGMEKFAKTDEFKALNLGFALdEGLASPDDVYR--VFYAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRRF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 217 CQTVWD---NGNE--YFPATSFQISNIHAGTgATNVIPGALEVTFNFRYSTEVTAEQLKQRVHEILDK--HGLQYEIVwN 289
Cdd:TIGR01880 229 RESQFQllqSNPDlaIGDVTSVNLTKLKGGV-QSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADagEGVTYEFS-Q 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 290 LSGLPFLTPVGElVNAAQTAILNVTGTETELSTS---GGTSDGRFIAPTGAQVLELGVLNAT---IHQINEHVDVHDLDP 363
Cdd:TIGR01880 307 HSGKPLVTPHDD-SNPWWVAFKDAVKEMGCTFKPeilPGSTDSRYIRAAGVPALGFSPMNNTpvlLHDHNEFLNEAVFLR 385
|
330
....*....|..
gi 446939317 364 LTDIYEQILENL 375
Cdd:TIGR01880 386 GIEIYQTLISAL 397
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
30-143 |
1.25e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 81.20 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 30 MADRLAKVGF-----HIEPmRFGDVDNLWAR-RGT--EGPVFcFAGHTDVVPTGRLDaWNSDPFAPEIRDGKLYGRGSAD 101
Cdd:PRK09133 65 MAARLKAAGFadadiEVTG-PYPRKGNLVARlRGTdpKKPIL-LLAHMDVVEAKRED-WTRDPFKLVEENGYFYGRGTSD 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446939317 102 MKtALAAMVVAS------ERFVAKHPnhkgsIAFLITSDEEGPAVNGT 143
Cdd:PRK09133 142 DK-ADAAIWVATlirlkrEGFKPKRD-----IILALTGDEEGTPMNGV 183
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
56-373 |
1.33e-16 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 80.21 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 56 RGTEG-PVFCFAGHTDVVPtgrLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPnhKGSIAFLITSD 134
Cdd:cd08013 63 RGTGGgKSLMLNGHIDTVT---LDGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGL--RGDVILAAVAD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 135 EEGPAVnGTVKVIetlekrneKITW----CLVGEPSSThklgdIVKNGRRGSLNAVLKVQGKQGHVAYPHLARNPIHEAS 210
Cdd:cd08013 138 EEDASL-GTQEVL--------AAGWradaAIVTEPTNL-----QIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 211 PALAELcqtvwdngNEYfpATSFQISNIHAGTGATNV----IPGALE---------VTFNFRYSTEVTAEQLKQRVHEIL 277
Cdd:cd08013 204 YFLVAL--------EEY--QQELPERPVDPLLGRASVhaslIKGGEEpssyparctLTIERRTIPGETDESVLAELTAIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 278 DK-----HGLQYE----IVWNLS-GLPFLTPVGELVnAAQTAilNVTGTETELSTSGGTSDGRFIAPTGAQVLELGVLNA 347
Cdd:cd08013 274 GElaqtvPNFSYRepriTLSRPPfEVPKEHPFVQLV-AAHAA--KVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGA 350
|
330 340
....*....|....*....|....*.
gi 446939317 348 TIHQINEHVDVHDLDPLTDIYEQILE 373
Cdd:cd08013 351 GLHAKEEWVDVESIRQLREVLSAVVR 376
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
65-292 |
1.73e-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: 77.68 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 65 FAGHTDVVPT--GRLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEGPAVNG 142
Cdd:cd05674 74 LMAHQDVVPVnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTIILAFGHDEEVGGERG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 143 TVKVIETLEKR--NEKITWCL-----VGEPSSTHKLGDIVKNGRRGSLNAVLKVQGKQGHVAYPH--------------L 201
Cdd:cd05674 154 AGAIAELLLERygVDGLAAILdeggaVLEGVFLGVPFALPGVAEKGYMDVEITVHTPGGHSSVPPkhtgigilseavaaL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 202 ARNP----IHEASPALAEL-CQ------------------------------TVWDNGNEYFPATSFQISNIHAGTgATN 246
Cdd:cd05674 234 EANPfppkLTPGNPYYGMLqCLaehsplpprslksnlwlaspllkallaselLSTSPLTRALLRTTQAVDIINGGV-KIN 312
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446939317 247 VIPGALEVTFNFRYSTEVTAEQLKQRVHEILDKHGLQYEIVWNLSG 292
Cdd:cd05674 313 ALPETATATVNHRIAPGSSVEEVLEHVKNLIADIAVKYGLGLSAFG 358
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
65-280 |
2.10e-15 |
|
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: 77.00 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 65 FAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMK-TALAAMVVASERFVAKHPNHkgSIAFLITSDEEgpavNGT 143
Cdd:cd05677 76 FYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKgPLLAAIYAVAELFQEGELDN--DVVFLIEGEEE----SGS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 144 VKVIETLEK---RNEKITWCLVgepSSTHKLGDIV---KNGRRGSLNAVLKV---------------------------- 189
Cdd:cd05677 150 PGFKEVLRKnkeLIGDIDWILL---SNSYWLDDNIpclNYGLRGVIHATIVVssdkpdlhsgvdggvlreptadliklls 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 190 --QGKQGHVAYPHLARN--PIHEASPA-LAELCQTVWDNGNEY---------FPATSFQISNIhAGTGATNVIPGALEVT 255
Cdd:cd05677 227 klQDPDGRILIPHFYDPvkPLTEAERArFTAIAETALIHEDTTvdsliakwrKPSLTVHTVKV-SGPGNTTVIPKSASAS 305
|
250 260
....*....|....*....|....*
gi 446939317 256 FNFRYSTEVTAEQLKQRVHEILDKH 280
Cdd:cd05677 306 VSIRLVPDQDLDVIKQDLTDYIQSC 330
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
30-360 |
7.30e-15 |
|
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: 75.45 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 30 MADRLAKVGFHIE-------PMRFGDVDNlwarrgTEGPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADM 102
Cdd:cd05681 28 LKEFLRRLGAEVEifetdgnPIVYAEFNS------GDAKTLLFYNHYDVQPAEPLELWTSDPFELTIRNGKLYARGVADD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 103 KTALAAMVVASERFVAKHPNHKGSIAFLITSDEE---------------------------------GPAVNGTVKVIET 149
Cdd:cd05681 102 KGELMARLAALRALLQHLGELPVNIKFLVEGEEEvgspnlekfvaehadllkadgciwegggknpkgRPQISLGVKGIVY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 150 LEKRnekitwcLVGEPSSTHK-LGDIVKNGRRGSLNAVLKVQGKQGHVAYPHLaRNPIHEASPALAELCQTVWDNGNEY- 227
Cdd:cd05681 182 VELR-------VKTADFDLHSsYGAIVENPAWRLVQALNSLRDEDGRVLIPGF-YDDVRPLSEAERALIDTYDFDPEELr 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 228 --------------------FPATSFQISNIHAG---TGATNVIPGALEVTFNFRYSTEVTAEQLKQRVHEILDKHGL-Q 283
Cdd:cd05681 254 ktyglkrplqvegkdplralFTEPTCNINGIYSGytgEGSKTILPSEAFAKLDFRLVPDQDPAKILSLLRKHLDKNGFdD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 284 YEIVWNLSGLPFLTPVG-ELVNAAQTAILNVTGTETE-LSTSGGTSD-GRFIAPTGAQVLELGVLNA--TIHQINEHVDV 358
Cdd:cd05681 334 IEIHDLLGEKPFRTDPDaPFVQAVIESAKEVYGQDPIvLPNSAGTGPmYPFYDALEVPVVAIGVGNAgsNAHAPNENIRI 413
|
..
gi 446939317 359 HD 360
Cdd:cd05681 414 AD 415
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
17-136 |
1.23e-14 |
|
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: 74.65 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 17 PSVTPI-DHT-----CQTIMADRLAKVGF-HIE-------PMRFGDvdnlwaRRGTEG-PVFCFAGHTDVVPTGRLDAWN 81
Cdd:cd05680 11 PSVSADpAHKgdvrrAAEWLADKLTEAGFeHTEvlptgghPLVYAE------WLGAPGaPTVLVYGHYDVQPPDPLELWT 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446939317 82 SDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEE 136
Cdd:cd05680 85 SPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEE 139
|
|
| PRK06915 |
PRK06915 |
peptidase; |
67-195 |
2.46e-14 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 73.96 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 67 GHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEE-GPAvnGTVK 145
Cdd:PRK06915 100 GHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEEsGGA--GTLA 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446939317 146 VIEtlekRNEKITWCLVGEPSSThKLgdIVKngRRGSLNAVLKVQGKQGH 195
Cdd:PRK06915 178 AIL----RGYKADGAIIPEPTNM-KF--FPK--QQGSMWFRLHVKGKAAH 218
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
89-356 |
4.78e-14 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 72.69 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 89 IRDGKLYGRGSADMKTALAAMVVASERFvAKHPnHKGSIAF--LITSDEEGPAVnGTVKVIETLEKRNekiTWCLVGEPS 166
Cdd:PRK07338 117 LDDGTLNGPGVADMKGGIVVMLAALLAF-ERSP-LADKLGYdvLINPDEEIGSP-ASAPLLAELARGK---HAALTYEPA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 167 STHklGDIVKNgRRGSLNAVLKVQGKQGHVAY-PHLARNPIHEASPALAELcqtvwDNGNEYFPATSFQISNIHAGtGAT 245
Cdd:PRK07338 191 LPD--GTLAGA-RKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAELALAL-----HALNGQRDGVTVNVAKIDGG-GPL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 246 NVIPGALEVTFNFRYSTEVTAEQLKQRVHEILDKHGLQYEIVWNLSGLpFLTPVgELVNAAQTAILNVT-------GTET 318
Cdd:PRK07338 262 NVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHGVSLHLHGG-FGRPP-KPIDAAQQRLFEAVqacgaalGLTI 339
|
250 260 270
....*....|....*....|....*....|....*....
gi 446939317 319 ELSTSGGTSDGRFIAPTGAQVLE-LGVLNATIHQINEHV 356
Cdd:PRK07338 340 DWKDSGGVCDGNNLAAAGLPVVDtLGVRGGNIHSEDEFV 378
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
30-103 |
1.50e-12 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 68.71 E-value: 1.50e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446939317 30 MADRLakvGFHIEpmrfgDVDNLWAR----RGTEgpVFCFAGHTDVVPTGrlDAWNSDPFAPEIRDGKLYGRGSADMK 103
Cdd:PRK07318 55 IAERD---GFKTK-----NVDNYAGHieygEGEE--VLGILGHLDVVPAG--DGWDTDPYEPVIKDGKIYARGTSDDK 120
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
29-156 |
2.67e-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: 67.63 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 29 IMADRLAKVGFHIE-------PMRFGDVDNL----WARRG--TEGPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLY 95
Cdd:cd05676 41 WAAERLEKLGFKVElvdigtqTLPDGEELPLppvlLGRLGsdPSKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLY 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446939317 96 GRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEEgpavNGTVKVIETLEKRNEK 156
Cdd:cd05676 121 GRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEGMEE----SGSEGLDELIEARKDT 177
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
57-373 |
3.20e-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: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 57 GTEGPVFCFAGHTDVVPTGRldawNSDPfaPEIRDGKLYGRGS----ADMKTALAAMVVASERFVAKHPNHkGSIAFLIT 132
Cdd:cd05683 64 KEEVPKILFTSHMDTVTPGI----NVKP--PQIADGYIYSDGTtilgADDKAGIAAILEAIRVIKEKNIPH-GQIQFVIT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 133 SDEEGPAVNGtvKVIETlEKRNEKITWCL--VGEPSSThklgdIVKNGRRGSLNAvlKVQGKQGHVA-YPHLARNPIHEA 209
Cdd:cd05683 137 VGEESGLVGA--KALDP-ELIDADYGYALdsEGDVGTI-----IVGAPTQDKINA--KIYGKTAHAGtSPEKGISAINIA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 210 SPALAELCQTVWDNgneyfpATSFQISNIHAGTgATNVIPGALEVTFNFRYSTEVTAEQLKQRVHEILDK----HGLQYE 285
Cdd:cd05683 207 AKAISNMKLGRIDE------ETTANIGKFQGGT-ATNIVTDEVNIEAEARSLDEEKLDAQVKHMKETFETtakeKGAHAE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 286 IVWNLSGLPFLTPVGE-LVNAAQTAILNVtGTETELSTSGGTSDGRFIAPTGAQVLELGVLNATIHQINEHVDVHDLDPL 364
Cdd:cd05683 280 VEVETSYPGFKINEDEeVVKLAKRAANNL-GLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDT 358
|
....*....
gi 446939317 365 TDIYEQILE 373
Cdd:cd05683 359 AVLVVEIIK 367
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
51-376 |
3.23e-12 |
|
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: 67.19 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 51 NLWARR--GTEGPVFCFAGHTDVVPTGrlDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIA 128
Cdd:cd02697 62 NLIVRRryGDGGRTVALNAHGDVVPPG--DGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 129 FLITSDEEGPAVNGTVKVI-ETLEKRNEKITWCLVGEPSSTHKlgdivkngrrGSLNAVLKVQGKQGHVAYPHLArnpiH 207
Cdd:cd02697 140 LHFTYDEEFGGELGPGWLLrQGLTKPDLLIAAGFSYEVVTAHN----------GCLQMEVTVHGKQAHAAIPDTG----V 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 208 EASPALAELCQTVWDNGNEYFPATS---------FQISNIHAGTGaTNVIPGALEVTFNFRYSTEVTAEQLKQRVHEILD 278
Cdd:cd02697 206 DALQGAVAILNALYALNAQYRQVSSqvegithpyLNVGRIEGGTN-TNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 279 KH-----GLQYEIVWNLSGLPFlTPVGE---LVNAAQTAILNVTGtetELSTSGGT---SDGRFIAPTGAQVLELG---- 343
Cdd:cd02697 285 DAaasmpGISVDIRRLLLANSM-RPLPGnapLVEAIQTHGEAVFG---EPVPAMGTplyTDVRLYAEAGIPGVIYGagpr 360
|
330 340 350
....*....|....*....|....*....|....
gi 446939317 344 -VLNATIHQINEHVDVHDLDPLTDIYEQILENLL 376
Cdd:cd02697 361 tVLESHAKRADERLQLEDLRRATKVIARSLRDLL 394
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
29-363 |
3.94e-12 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 66.96 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 29 IMADRLAKVGFHIE--PMRFGDVDNLWAR-RGTEGPVFCFAGHTDVV-PTGRLdawNSDPFapEIRDGKLYGRGSADMKT 104
Cdd:PRK06133 65 LLAERLKALGAKVEraPTPPSAGDMVVATfKGTGKRRIMLIAHMDTVyLPGML---AKQPF--RIDGDRAYGPGIADDKG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 105 ALAAMVVASErfVAKHPNHK--GSIAFLITSDEEGPAVnGTVKVIETLEKRNEKITWClvgEPSSThklGDIVKNGRRGS 182
Cdd:PRK06133 140 GVAVILHALK--ILQQLGFKdyGTLTVLFNPDEETGSP-GSRELIAELAAQHDVVFSC---EPGRA---KDALTLATSGI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 183 LNAVLKVQGKQGHV-AYPHLARNPIHEASPALAELcqtvWDNGNEYfPATSFQISNIHAGTgATNVIPGALEVTFNFRYS 261
Cdd:PRK06133 211 ATALLEVKGKASHAgAAPELGRNALYELAHQLLQL----RDLGDPA-KGTTLNWTVAKAGT-NRNVIPASASAQADVRYL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 262 TEVTAEQLKQRVHEILDKH-------GLQYEivwnlSGLPFL--TPVGE-LVNAAQTaILNVTGTETELST--SGGTSDG 329
Cdd:PRK06133 285 DPAEFDRLEADLQEKVKNKlvpdtevTLRFE-----RGRPPLeaNAASRaLAEHAQG-IYGELGRRLEPIDmgTGGGTDA 358
|
330 340 350
....*....|....*....|....*....|....*.
gi 446939317 330 RFIAPTG-AQVLE-LGVLNATIHQINEHVDVHDLDP 363
Cdd:PRK06133 359 AFAAGSGkAAVLEgFGLVGFGAHSNDEYIELNSIVP 394
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
68-216 |
1.90e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 65.16 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 68 HTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKgSIAFLITSDEEGPAVNgtvkvI 147
Cdd:PRK06446 70 HYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKHKLNV-NVKFLYEGEEEIGSPN-----L 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 148 ETLEKRNEKItwclvgePSSTHKLGDIVKNGRRGSLNAVLKVQG------------KQGHVAYPHLARNPIHEASPALAE 215
Cdd:PRK06446 144 EDFIEKNKNK-------LKADSVIMEGAGLDPKGRPQIVLGVKGllyvelvlrtgtKDLHSSNAPIVRNPAWDLVKLLST 216
|
.
gi 446939317 216 L 216
Cdd:PRK06446 217 L 217
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
27-172 |
2.00e-11 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 65.06 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 27 QTIMADRLAKVGFHI--EPMRFGDVDNLWARRGTEGPVF---CFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSAD 101
Cdd:PRK08596 39 QEFIAEFLRKLGFSVdkWDVYPNDPNVVGVKKGTESDAYkslIINGHMDVAEVSADEAWETNPFEPTIKDGWLYGRGAAD 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446939317 102 MKTALAAMVVASERFVAKHPNHKGSIAFL-ITSDEEGPAvnGTVKVIEtlekRNEKITWCLVGEPSSTHKLG 172
Cdd:PRK08596 119 MKGGLAGALFAIQLLHEAGIELPGDLIFQsVIGEEVGEA--GTLQCCE----RGYDADFAVVVDTSDLHMQG 184
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
68-190 |
2.74e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 64.54 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 68 HTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHkgsIAFLITSDEEGpavnGTVKVI 147
Cdd:PRK07907 91 HHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRALGGDLPVG---VTVFVEGEEEM----GSPSLE 163
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446939317 148 ETLEKRNEKIT-----------WClVGEPSSTHKLgdivkngrRGSLNAVLKVQ 190
Cdd:PRK07907 164 RLLAEHPDLLAadviviadsgnWS-VGVPALTTSL--------RGNADVVVTVR 208
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
188-325 |
6.56e-11 |
|
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349939 [Multi-domain] Cd Length: 365 Bit Score: 63.07 E-value: 6.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 188 KVQGKQGHVAYPHLARNPIHEASPALAELcQTVWDNGNEyfpATSFQISNIHAGTGATNVIPGALEVTFNFRYSTEVTAE 267
Cdd:cd08018 173 TIKGKQAHGARPHLGINAIEAASAIVNAV-NAIHLDPNI---PWSVKMTKLQAGGEATNIIPDKAKFALDLRAQSNEAME 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446939317 268 QLKQRVHEILDK----HGLQYEIVWnLSGLPFLTPVGELVNAAQTAILNVTGTET---ELSTSGG 325
Cdd:cd08018 249 ELKEKVEHAIEAaaalYGASIEITE-KGGMPAAEYDEEAVELMEEAITEVLGEEKlagPCVTPGG 312
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
179-318 |
6.83e-11 |
|
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 63.21 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 179 RRGSLNA-----VLKVQGKQGHVAYPHLARNPIHEASPALAELcQTVWDNGNEyfPATSFQIS--NIHAGTgATNVIPGA 251
Cdd:COG1473 175 RPGPIMAaadsfEITIKGKGGHAAAPHLGIDPIVAAAQIVTAL-QTIVSRNVD--PLDPAVVTvgIIHGGT-APNVIPDE 250
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446939317 252 LEVTFNFRYSTEVTAEQLKQRVHEILDK----HGLQYEIVWnLSGLPFLTPVGELVNAAQTAILNVTGTET 318
Cdd:COG1473 251 AELEGTVRTFDPEVRELLEERIERIAEGiaaaYGATAEVEY-LRGYPPTVNDPELTELAREAAREVLGEEN 320
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
53-136 |
7.17e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 63.17 E-value: 7.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 53 WARRGTEGPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSIAFLIT 132
Cdd:PRK07205 68 YAEIGQGEELLAILCHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFG 147
|
....
gi 446939317 133 SDEE 136
Cdd:PRK07205 148 TDEE 151
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
31-363 |
1.17e-10 |
|
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: 62.11 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 31 ADRLAKVGFHiEPMRFGDVDNLWARRGT-EGPVFCFAGHTDVVPTGrldawnSDPFAPEIRDGKLYGRGSADMKTALAAM 109
Cdd:cd03896 25 AEWMADLGLG-DVERDGRGNVVGRLRGTgGGPALLFSAHLDTVFPG------DTPATVRHEGGRIYGPGIGDNKGSLACL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 110 VVASERFVAKHPNHKGSIAFLITSDEEGPAVNGTVKVIetLEKRNEKITWCLVGEPSsthkLGDIVkNGRRGSLNAVLKV 189
Cdd:cd03896 98 LAMARAMKEAGAALKGDVVFAANVGEEGLGDLRGARYL--LSAHGARLDYFVVAEGT----DGVPH-TGAVGSKRFRITT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 190 QGKQGHVAYPHLARNPIHEASPALAELCQTVWDngneYFPATSFQISNIHAGTGAtNVIPGALEVTFNFRYSTEVTAEQL 269
Cdd:cd03896 171 VGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAP----YVPKTTFAAIRGGGGTSV-NRIANLCSMYLDIRSNPDAELADV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 270 KQRVHEILDKHGLQY-----EIVWNLSGLPFLT-PVGELVNAAQTAILNVTGTETELSTSggtSDGRFIAPTGAQVLELG 343
Cdd:cd03896 246 QREVEAVVSKLAAKHlrvkaRVKPVGDRPGGEAqGTEPLVNAAVAAHREVGGDPRPGSSS---TDANPANSLGIPAVTYG 322
|
330 340
....*....|....*....|.
gi 446939317 344 V-LNATIHQINEHVDVHDLDP 363
Cdd:cd03896 323 LgRGGNAHRGDEYVLKDDMLK 343
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
59-276 |
4.08e-10 |
|
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: 60.94 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 59 EGPVFCFAG-HTDVVPTGRlDAWNSDPFAPEIRDGKLYGRGSADMKTALAAMVVASERFVAKHPNHKGSI-AFLITSDEE 136
Cdd:cd08012 76 DGKTVSFVGsHMDVVTANP-ETWEFDPFSLSIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVvAVFIANEEN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 137 ----GPAVNGTVKVIETLEKRNEKITWCLVGEPSSTHKLGdivkngrrGSLNAVLKVQGKQGHVAYPHLARNPIHEASPA 212
Cdd:cd08012 155 seipGVGVDALVKSGLLDNLKSGPLYWVDSADSQPCIGTG--------GMVTWKLTATGKLFHSGLPHKAINALELVMEA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 213 LAELCQTVWDNgneyFPA------TSFQISNIHAGT------GATNVIPGALEVTFNFR----YSTEVTAEQLKQRVHEI 276
Cdd:cd08012 227 LAEIQKRFYID----FPPhpkeevYGFATPSTMKPTqwsypgGSINQIPGECTICGDCRltpfYDVKEVREKLEEYVDDI 302
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
68-275 |
7.04e-10 |
|
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: 59.98 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 68 HTDVVPTGRlDAWNSDPFAPEI-RDGKLYGRGSADMKT-------ALAAMVVASERFvakhpnhKGSIAFLITSDEEGPA 139
Cdd:cd05646 72 HTDVVPVFE-EKWTHDPFSAHKdEDGNIYARGAQDMKCvgiqyleAIRRLKASGFKP-------KRTIHLSFVPDEEIGG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 140 VNGTVKVIETLEKRNEKITWCL---VGEPSSTHKlgdiVKNGRRGSLNAVLKVQGKQGHVA--YPHLARNPIHEASPALA 214
Cdd:cd05646 144 HDGMEKFVKTEEFKKLNVGFALdegLASPTEEYR----VFYGERSPWWVVITAPGTPGHGSklLENTAGEKLRKVIESIM 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446939317 215 ELCQTVW----DNGN-EYFPATSFQISNIHAGTgATNVIPGALEVTFNFRYSTEVTAEQLKQRVHE 275
Cdd:cd05646 220 EFRESQKqrlkSNPNlTLGDVTTVNLTMLKGGV-QMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDE 284
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
31-331 |
8.41e-10 |
|
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273857 [Multi-domain] Cd Length: 363 Bit Score: 59.67 E-value: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 31 ADRLAKVGFHIEPmRFGDVDNLWARRGT--EGPVFCFAGHTDVVPTGRLDAWnsdPFAPEIrDGKLYGRGsadmKTALAA 108
Cdd:TIGR01891 26 AEALESLGIEVRR-GVGGATGVVATIGGgkPGPVVALRADMDALPIQEQTDL---PYKSTN-PGVMHACG----HDLHTA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 109 MVVASERFVAKHPNH-KGSIAFLITSDEEGPAvnGTVKVIET--LEKRNEKITWclvgEPSSTHKLGDIVKngRRGSLNA 185
Cdd:TIGR01891 97 ILLGTAKLLKKLADLlEGTVRLIFQPAEEGGG--GATKMIEDgvLDDVDAILGL----HPDPSIPAGTVGL--RPGTIMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 186 -----VLKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDNGNeyfPATSFQIS--NIHAGtGATNVIPGALEVTFNF 258
Cdd:TIGR01891 169 aadkfEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQIVSRNVD---PSRPAVVSvgIIEAG-GAPNVIPDKASMSGTV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 259 RYSTEVTAEQLKQRVHEILDK----HGLQYEIVWnLSGLPFLTP---VGELVNAAQTAILNVTGT-ETELSTSGGTSDGR 330
Cdd:TIGR01891 245 RSLDPEVRDQIIDRIERIVEGaaamYGAKVELNY-DRGLPAVTNdpaLTQILKEVARHVVGPENVaEDPEVTMGSEDFAY 323
|
.
gi 446939317 331 F 331
Cdd:TIGR01891 324 Y 324
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
67-136 |
1.06e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 59.48 E-value: 1.06e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446939317 67 GHTDVVPTGRLDaWNSDPFAPEIRDGKLYGRGSADMKTALaAMVVASERFVAKH---PNHKGSIAFLitSDEE 136
Cdd:PRK07906 72 GHLDVVPAEAAD-WSVHPFSGEIRDGYVWGRGAVDMKDMD-AMMLAVVRHLARTgrrPPRDLVFAFV--ADEE 140
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
30-136 |
1.30e-09 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 59.37 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 30 MADRLAKVGF-HIEPMRFGDVDNLWARR--GTEGPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRDGKLYGRGSADMKTAL 106
Cdd:PRK08201 46 LAGALEKAGLeHVEIMETAGHPIVYADWlhAPGKPTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQV 125
|
90 100 110
....*....|....*....|....*....|
gi 446939317 107 AAMVVASERFVAKHPNHKGSIAFLITSDEE 136
Cdd:PRK08201 126 FMHLKAVEALLKVEGTLPVNVKFCIEGEEE 155
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
107-317 |
1.56e-08 |
|
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: 55.68 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 107 AAMVVASERFVAKHPNH-KGSIAFLITSDEEGPAvnGTVKVIETLEKRNEKITWCLVGEPSSTHKLGDIVknGRRGSLNA 185
Cdd:cd03886 94 TAMLLGAAKLLAERRDPlKGTVRFIFQPAEEGPG--GAKAMIEEGVLENPGVDAAFGLHVWPGLPVGTVG--VRSGALMA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 186 -----VLKVQGKQGHVAYPHLARNPIHEASPALAELcQTVwdNGNEYFPATSFQIS--NIHAGTgATNVIPGALEVTFNF 258
Cdd:cd03886 170 sadefEITVKGKGGHGASPHLGVDPIVAAAQIVLAL-QTV--VSRELDPLEPAVVTvgKFHAGT-AFNVIPDTAVLEGTI 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446939317 259 RYSTEVTAEQLKQRVHEILDK----HGLQYEIVWnLSGLPFLTPVGELVNAAQTAILNVTGTE 317
Cdd:cd03886 246 RTFDPEVREALEARIKRLAEGiaaaYGATVELEY-GYGYPAVINDPELTELVREAAKELLGEE 307
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
67-307 |
2.01e-07 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 52.94 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 67 GHTDVVPT---GRL--DAWNSDPFAPEIRDGKL--------------YGRGSADMKTALAAMVVASERFvAKHPNHKGSI 127
Cdd:COG4187 86 SHFDVVDVedyGSLkpLAFDPEELTEALKEIKLpedvrkdlesgewlFGRGTMDMKAGLALHLALLEEA-SENEEFPGNL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 128 AFLITSDEEgpaVN-----GTVKVIETL-EKRNEKITWCLVGEPSSTHKLGDIVK---NGRRGSLNAVLKVQGKQGHVAY 198
Cdd:COG4187 165 LLLAVPDEE---VNsagmrAAVPLLAELkEKYGLEYKLAINSEPSFPKYPGDETRyiyTGSIGKLMPGFYCYGKETHVGE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 199 PHLARNPIHEAS---------PALAE------------LCQTvwDNGNEYfpatSFQISniHAGTGATNVIpgalevTFN 257
Cdd:COG4187 242 PFSGLNANLLASeltrelelnPDFCEevggevtpppvsLKQK--DLKEEY----SVQTP--HRAVAYFNVL------TLE 307
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446939317 258 fRYSTEVTaEQLKQRVHE----ILDKHGLQYEIVWNLSGLPFLTPVG--------ELVNAAQ 307
Cdd:COG4187 308 -RSPKEIL-EKLKKIAEEaaekILEHYKEQYEKYCKLTGEPFVPLPWkvkvltyeELYEEAV 367
|
|
| M20_IAA_Hyd |
cd08017 |
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ... |
188-299 |
2.26e-07 |
|
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349938 [Multi-domain] Cd Length: 376 Bit Score: 52.32 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 188 KVQGKQGHVAYPHLARNPIHEASPALAELCQTVwdnGNEYFPATS--FQISNIHAGTgATNVIPGALEVTFNFRYSTEVT 265
Cdd:cd08017 174 VIRGKGGHAAMPHHTVDPVVAASSAVLALQQLV---SRETDPLDSqvVSVTRFNGGH-AFNVIPDSVTFGGTLRALTTEG 249
|
90 100 110
....*....|....*....|....*....|....*...
gi 446939317 266 AEQLKQRVHEILDK----HGLQYEIVWNLSGLPFLTPV 299
Cdd:cd08017 250 FYRLRQRIEEVIEGqaavHRCNATVDFSEDERPPYPPT 287
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
188-317 |
3.01e-07 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 51.95 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 188 KVQGKQGHVAYPHLARNPIHEASPALAELcQTVWDNGNEYFPATSFQISNIHAGTgATNVIPGALEVTFNFRYSTEVTAE 267
Cdd:cd08019 174 EVKGKGGHGSMPHQGIDAVLAAASIVMNL-QSIVSREIDPLEPVVVTVGKLNSGT-RFNVIADEAKIEGTLRTFNPETRE 251
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446939317 268 QLKQRVHEILDKHGLQYEIVWNLSgLPFLTPV----GELVNAAQTAILNVTGTE 317
Cdd:cd08019 252 KTPEIIERIAKHTAASYGAEAELT-YGAATPPvindEKLSKIARQAAIKIFGED 304
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
187-289 |
3.22e-07 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 51.89 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 187 LKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDNGNeyfPATSFQIS--NIHAGTgATNVIPGALEVTFNFRYSTEV 264
Cdd:cd08021 186 ITIKGKGGHGSMPHETVDPIVIAAQIVTALQTIVSRRVD---PLDPAVVTigTFQGGT-SFNVIPDTVELKGTVRTFDEE 261
|
90 100
....*....|....*....|....*....
gi 446939317 265 TAEQLKQRVHEIL----DKHGLQYEIVWN 289
Cdd:cd08021 262 VREQVPKRIERIVkgicEAYGASYELEYQ 290
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
66-216 |
7.14e-07 |
|
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: 51.19 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 66 AGHTDVVPTGRLDAWNSDPFAPEI-----------------RDGK----LYGRGSADMKTALAAMVVASERFvAKHPNHK 124
Cdd:cd05654 77 ISHFDTVGIEDYGELKDIAFDPDEltkafseyveeldeevrEDLLsgewLFGRGTMDMKSGLAVHLALLEQA-SEDEDFD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 125 GSIAFLITSDEEGPAvNGTVKVIETLEKRNEK----ITWCLVGEPSSTHKLGDIVKNGRRGSLNAVLK---VQGKQGHVA 197
Cdd:cd05654 156 GNLLLMAVPDEEVNS-RGMRAAVPALLELKKKhdleYKLAINSEPIFPQYDGDQTRYIYTGSIGKILPgflCYGKETHVG 234
|
170
....*....|....*....
gi 446939317 198 YPHLARNPIHEASPALAEL 216
Cdd:cd05654 235 EPFAGINANLMASEITARL 253
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
30-136 |
4.66e-06 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 48.36 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 30 MADRLAKVGFHIE-------PMRFGDVDNlwarRGTEGPVFCFAGHTDVVPTGRLDAWNSDPFAPEIRD----GK-LYGR 97
Cdd:PRK09104 49 LVADLASLGFEASvrdtpghPMVVAHHEG----PTGDAPHVLFYGHYDVQPVDPLDLWESPPFEPRIKEtpdgRKvIVAR 124
|
90 100 110
....*....|....*....|....*....|....*....
gi 446939317 98 GSADMKTALAAMVVASERFVAKHPNHKGSIAFLITSDEE 136
Cdd:PRK09104 125 GASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEE 163
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
57-328 |
2.62e-05 |
|
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in 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 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. ACY1L2 family 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 E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.
Pssm-ID: 349945 [Multi-domain] Cd Length: 366 Bit Score: 45.69 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 57 GTEGPVFCFAGHTDVVPTGRLDAWnsdPFAPEIrDGKLYGRGsadmKTALAAMVVASERFVAKHPNH-KGSIAFLITSDE 135
Cdd:cd08660 53 GEDGPVIAIRADIDALPIQEQTNL---PFASKV-DGT*HACG----HDFHTTSIIGTA*LLNQRRAElKGTVVFIFQPAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 136 EGpAVNGTVKVIETLEKRNEKITWCLVGE--PSSTHKLGDIVKNGRRGSLNAVLKvqGKQGHVAYPHLARNPIHEASPAL 213
Cdd:cd08660 125 EG-AAGARKVLEAGVLNGVSAIFGIHNKPdlPVGTIGVKEGPL*ASVDVFEIVIK--GKGGHASIPNNSIDPIAAAGQII 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 214 AELCQTVWDNgNEYFPATSFQISNIHAGTgATNVIPGALEVTFNFRYSTEVTAEQLKQRVHEILDK----HGLQYEIVWN 289
Cdd:cd08660 202 SGLQSVVSRN-ISSLQNAVVSITRVQGGT-AWNVIPDQAE*EGTVRAFTKEARQAVPEH*RRVAEGiaagYGCQAEFKWF 279
|
250 260 270
....*....|....*....|....*....|....*....
gi 446939317 290 LSGLPFLTPVGELVNAAQTAILNVTGTETELSTSGGTSD 328
Cdd:cd08660 280 PNGPSEVQNDGTLLNAFSKAAARLGYATVHAEQSPGSED 318
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
174-276 |
3.28e-05 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349914 [Multi-domain] Cd Length: 399 Bit Score: 45.41 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 174 IVKNGRRGSLNAVLKVQ--GKQGHVAYPHLARNPIHEASPALAELcQTVWDNGNEYFPATSFQISNIHAGTgATNVIPGA 251
Cdd:cd05664 171 GTRPGRFLSAADSLDITifGRGGHGSMPHLTIDPVVMAASIVTRL-QTIVSREVDPQEFAVVTVGSIQAGS-AENIIPDE 248
|
90 100
....*....|....*....|....*
gi 446939317 252 LEVTFNFRYSTEVTAEQLKQRVHEI 276
Cdd:cd05664 249 AELKLNVRTFDPEVREKVLNAIKRI 273
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
187-278 |
3.31e-05 |
|
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349920 [Multi-domain] Cd Length: 367 Bit Score: 45.33 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 187 LKVQGKQGHVAYPHLARNPIHEASPALAELcQTVWDNGNEYFPATSFQISNIHAGTgATNVIPGALEVTFNFRYSTEVTA 266
Cdd:cd05670 177 IDFIGKSGHAAYPHNANDMVVAAANFVTQL-QTIVSRNVDPIDGAVVTIGKIHAGT-ARNVIAGTAHLEGTIRTLTQEMM 254
|
90
....*....|..
gi 446939317 267 EQLKQRVHEILD 278
Cdd:cd05670 255 ELVKQRVRDIAE 266
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
181-278 |
6.78e-05 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349916 [Multi-domain] Cd Length: 373 Bit Score: 44.44 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 181 GSLNAVLKVQGKQGHVAYPHLARNPIheasPALAELC---QT-VWDNGNeyfPATSFQIS--NIHAGTgATNVIPGALEV 254
Cdd:cd05666 171 SADTFEITIRGKGGHAAMPHLGVDPI----VAAAQLVqalQTiVSRNVD---PLDAAVVSvtQIHAGD-AYNVIPDTAEL 242
|
90 100
....*....|....*....|....
gi 446939317 255 TFNFRYSTEVTAEQLKQRVHEILD 278
Cdd:cd05666 243 RGTVRAFDPEVRDLIEERIREIAD 266
|
|
| PLN02693 |
PLN02693 |
IAA-amino acid hydrolase |
59-281 |
1.03e-04 |
|
IAA-amino acid hydrolase
Pssm-ID: 178296 [Multi-domain] Cd Length: 437 Bit Score: 44.27 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 59 EGPVFCFAGHTDVVPTGRLDAWNSDPFAPeirdGKLYGRGsadmKTALAAMVVASERFVAKHPNH-KGSIAFLITSDEEG 137
Cdd:PLN02693 101 EPPFVALRADMDALPIQEAVEWEHKSKIP----GKMHACG----HDGHVAMLLGAAKILQEHRHHlQGTVVLIFQPAEEG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 138 paVNGTVKVIETLEKRNEKITWCLVGEP-----SSTHKLGDIVKNGrrGSLNAVlkVQGKQGHVAYPHLARNPIHEASPA 212
Cdd:PLN02693 173 --LSGAKKMREEGALKNVEAIFGIHLSPrtpfgKAASRAGSFMAGA--GVFEAV--ITGKGGHAAIPQHTIDPVVAASSI 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446939317 213 LAELCQTVwdnGNEYFPATS--FQISNIHAGTgATNVIPGALEVTFNFRYSTEVTaeQLKQRVHEILDKHG 281
Cdd:PLN02693 247 VLSLQQLV---SRETDPLDSkvVTVSKVNGGN-AFNVIPDSITIGGTLRAFTGFT--QLQQRIKEIITKQA 311
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
187-336 |
1.26e-04 |
|
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.
Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 43.67 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 187 LKVQGKQGHV-AYPHLARnpiHEASPALAELCQTVWDNGNEYFPATSFQISNIHAGTGATNVIPGALEVTFNFRySTEVT 265
Cdd:cd03884 211 VTVTGEAGHAgTTPMALR---RDALLAAAELILAVEEIALEHGDDLVATVGRIEVKPNAVNVIPGEVEFTLDLR-HPDDA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 266 -----AEQLKQRVHEILDKHGLQYEI--VWNLSGLPFLTPVGELVNAAQTAIlnvtGTETELSTSGGTSDGRFIA---PT 335
Cdd:cd03884 287 vldamVERIRAEAEAIAAERGVEVEVerLWDSPPVPFDPELVAALEAAAEAL----GLSYRRMPSGAGHDAMFMAricPT 362
|
.
gi 446939317 336 G 336
Cdd:cd03884 363 A 363
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
65-190 |
2.50e-04 |
|
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 dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 42.71 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 65 FAGHTDVVPtgRLDAWNSD--PFAPEIRDGKLYGRGSAD----MKTALAAmVVASERFVAKHPnhkgSIAFLITSDEEgp 138
Cdd:cd05682 78 LYGHMDKQP--PFTGWDEGlgPTKPVIRGDKLYGRGGADdgyaIFASLTA-IKALQEQGIPHP----RCVVLIEACEE-- 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446939317 139 avNGTVKVIETLEKRNEKI-----TWCLVGEPSSTHKLGdiVKNGRRGSLNAVLKVQ 190
Cdd:cd05682 149 --SGSADLPFYLDKLKERIgnvdlVVCLDSGCGNYEQLW--LTTSLRGVLGGDLTVQ 201
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
186-324 |
5.31e-04 |
|
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349919 [Multi-domain] Cd Length: 371 Bit Score: 41.51 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 186 VLKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDNGNEYFPATsFQISNIHAGTgATNVIPGALEVTFNFRYSTEVT 265
Cdd:cd05669 176 EIEIAGKGAHAAKPENGVDPIVAASQIINALQTIVSRNISPLESAV-VSVTRIHAGN-TWNVIPDSAELEGTVRTFDAEV 253
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446939317 266 AEQLKQRVHEILD----KHGLQYEIVWnLSGLPFLTPVGELVN----AAQTAILNVtgTETELSTSG 324
Cdd:cd05669 254 RQLVKERFEQIVEgiaaAFGAKIEFKW-HSGPPAVINDEELTDlaseVAAQAGYEV--VHAEPSLGG 317
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
57-136 |
5.87e-04 |
|
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.
Pssm-ID: 349885 [Multi-domain] Cd Length: 474 Bit Score: 41.74 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 57 GTEG----PVFCFAGHTDVVPTGRLDA---WNSDPFAPEIRDGKLYGRGS---ADMKTALAAM--VVASERFvaKHPNhk 124
Cdd:cd03890 53 ATPGyenaPPVILQGHMDMVCEKNADSehdFEKDPIKLRIDGDWLKATGTtlgADNGIGVAYAlaILEDKDI--EHPP-- 128
|
90
....*....|..
gi 446939317 125 gsIAFLITSDEE 136
Cdd:cd03890 129 --LEVLFTVDEE 138
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
30-108 |
1.08e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 41.05 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 30 MADRLAKVGFHIEPmrfgdVDN--------LWARRgTEGP----VFCFaGHTDVVPtGRLDAWNS--DPFAPEIRDGKLY 95
Cdd:PRK07079 50 IAPALAALGFTCRI-----VDNpvagggpfLIAER-IEDDalptVLIY-GHGDVVR-GYDEQWREglSPWTLTEEGDRWY 121
|
90 100
....*....|....*....|
gi 446939317 96 GRGSADMK-------TALAA 108
Cdd:PRK07079 122 GRGTADNKgqhtinlAALEQ 141
|
|
| M20_Acy1-like |
cd05667 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
108-286 |
3.14e-03 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349917 [Multi-domain] Cd Length: 403 Bit Score: 39.33 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 108 AMVVASERFVAKHPNH-KGSIAFLITSDEEGPAVN---GTVKVIE--TLEK-RNEKITWCLVGEPSSTHKLGdiVKNGrr 180
Cdd:cd05667 114 AILLGAAEVLAANKDKiKGTVMFIFQPAEEGPPEGeegGAKLMLKegAFKDyKPEAIFGLHVGSGLPSGQLG--YRSG-- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 181 GSLNAV----LKVQGKQGHVAYPHLARNPIHEASPALAELCQTVWDNGNEYFPATSFQISNIHAGTgATNVIPGALEV-- 254
Cdd:cd05667 190 PIMASAdrfrITVKGKQTHGSRPWDGIDPIMASAQIIQGLQTIISRRIDLTKEPAVISIGKINGGT-RGNIIPEDAEMvg 268
|
170 180 190
....*....|....*....|....*....|....*
gi 446939317 255 ---TFNFRYSTEVTAEqLKQRVHEILDKHGLQYEI 286
Cdd:cd05667 269 tirTFDPEMREDIFAR-LKTIAEHIAKAYGATAEV 302
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
30-103 |
5.36e-03 |
|
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: 38.63 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 30 MADRLAKVGF----HIEPMrFGDVDNLWARRgTEGP----VFCFaGHTDVVPtGRLDAWNS--DPFAPEIRDGKLYGRGS 99
Cdd:cd05679 37 MRPRFERLGFtvhiHDNPV-AGRAPFLIAER-IEDPslptLLIY-GHGDVVP-GYEGRWRDgrDPWTVTVWGERWYGRGT 112
|
....
gi 446939317 100 ADMK 103
Cdd:cd05679 113 ADNK 116
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
187-286 |
8.62e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 37.83 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446939317 187 LKVQGKQGHV-AYPHLARnpiHEASPALAELCQTVWDNGNEYFP---ATsfqISNIHAGTGATNVIPGALEVTFNFR-YS 261
Cdd:PRK09290 220 VTFTGEANHAgTTPMALR---RDALLAAAEIILAVERIAAAHGPdlvAT---VGRLEVKPNSVNVIPGEVTFTLDIRhPD 293
|
90 100
....*....|....*....|....*...
gi 446939317 262 TEVTA---EQLKQRVHEILDKHGLQYEI 286
Cdd:PRK09290 294 DAVLDalvAELRAAAEAIAARRGVEVEI 321
|
|
| |
