|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
1-367 |
0e+00 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 548.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 1 MIDPLALTQRLIACPSVTPADAGAMAVIAEALEGLGFAVHRFAAGGppdgpIENLFAIRGESGPHFAFAGHSDVVPPG-- 78
Cdd:PRK13009 1 MSDVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDFGD-----VKNLWARRGTEGPHLCFAGHTDVVPPGdl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 79 SGWTGDPFVPEIRGELLYGRGAVDMKGA----IAAFIAAIARIEQDRGTVSLIITGDEEGPATHGTVALIDWMNERGIRP 154
Cdd:PRK13009 76 EAWTSPPFEPTIRDGMLYGRGAADMKGSlaafVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVLEWLKARGEKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 155 DLCLVGEPTSTHRLGDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPVPELVRALAALDALHLDDGNAWFQPSNLEITT 234
Cdd:PRK13009 156 DYCIVGEPTSTERLGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEGNEFFPPTSLQITN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 235 VDVGNSATNVIPAKASARVNIRFNDEHKGAELVERVSRTVLAHAPHAEIKAVISGESFITPPGDFSALVSSAITKVTGLV 314
Cdd:PRK13009 236 IDAGTGATNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDYTLEWTLSGEPFLTPPGKLVDAVVAAIEAVTGIT 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1819653059 315 PELSTTGGTSDARFLSRIC-PVVEFGLCNATMHKLDEAVAVPDLYALADIYEEI 367
Cdd:PRK13009 316 PELSTSGGTSDARFIADYGaQVVEFGPVNATIHKVNECVSVADLEKLTRIYERI 369
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
5-367 |
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: 531.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSVTPADAGAMAVIAEALEGLGFAVHRFaaggpPDGPIENLFAIRGESGPHFAFAGHSDVVPPG--SGWT 82
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERL-----EFGGVKNLWARRGTGGPHLCFAGHTDVVPPGdlEGWS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 83 GDPFVPEIRGELLYGRGAVDMKGA----IAAFIAAIARIEQDRGTVSLIITGDEEGPATHGTVALIDWMNERGIRPDLCL 158
Cdd:cd03891 76 SDPFSPTIKDGMLYGRGAADMKGGiaafVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKIDYCI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 159 VGEPTSTHRLGDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPVPELVRALAALDALHLDDGNAWFQPSNLEITTVDVG 238
Cdd:cd03891 156 VGEPTSEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLDEGNEFFPPSSLQITNIDVG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 239 NSATNVIPAKASARVNIRFNDEHKGAELVERVSRTVLAHAPHAEIKAVISGESFITPPGDFSALVSSAITKVTGLVPELS 318
Cdd:cd03891 236 NGATNVIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELS 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1819653059 319 TTGGTSDARFLSRI-CPVVEFGLCNATMHKLDEAVAVPDLYALADIYEEI 367
Cdd:cd03891 316 TSGGTSDARFIASYgCPVVEFGLVNATIHKVNERVSVADLEKLTDIYERI 365
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
5-368 |
7.37e-130 |
|
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: 376.75 E-value: 7.37e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSVTPADAGAMAVIAEALEGLGFAVHRFAAGGppdgpIENLFAIRGESGPHFAFAGHSDVVPPG--SGWT 82
Cdd:TIGR01246 2 TELAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGD-----TKNLWATRGTGEPVLAFAGHTDVVPAGpeEQWS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 83 GDPFVPEIRGELLYGRGAVDMKGA----IAAFIAAIARIEQDRGTVSLIITGDEEGPATHGTVALIDWMNERGIRPDLCL 158
Cdd:TIGR01246 77 SPPFEPVERDGKLYGRGAADMKGSlaafIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVETLMARDELIDYCI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 159 VGEPTSTHRLGDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPVPELVRALAALDALHLDDGNAWFQPSNLEITTVDVG 238
Cdd:TIGR01246 157 VGEPSSVKKLGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAIKWDEGNEFFPPTSLQITNIHAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 239 NSATNVIPAKASARVNIRFNDEHKGAELVERVSRTVLAHAPHAEIKAVISGESFITPPGDFSALVSSAITKVTGLVPELS 318
Cdd:TIGR01246 237 TGANNVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELS 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1819653059 319 TTGGTSDARFLSRI-CPVVEFGLCNATMHKLDEAVAVPDLYALADIYEEIV 368
Cdd:TIGR01246 317 TGGGTSDGRFIALMgAEVVEFGPVNATIHKVNECVSIEDLEKLSDVYQDLL 367
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
3-369 |
6.00e-93 |
|
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: 283.31 E-value: 6.00e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 3 DPLALTQRLIACPSVTPADAGAMAVIAEALEGLGFAVHRFaaggPPDGPIENLFAIR--GESGPHFAFAGHSDVVPPG-- 78
Cdd:COG0624 13 EALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERL----EVPPGRPNLVARRpgDGGGPTLLLYGHLDVVPPGdl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 79 SGWTGDPFVPEIRGELLYGRGAVDMKGAI----AAFIAAIARIEQDRGTVSLIITGDEEGPAtHGTVALIDWMNErGIRP 154
Cdd:COG0624 89 ELWTSDPFEPTIEDGRLYGRGAADMKGGLaamlAALRALLAAGLRLPGNVTLLFTGDEEVGS-PGARALVEELAE-GLKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 155 DLCLVGEPTSThrlgDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPVPELVRALAA-LDALHLDDGNAWFQPSNLEIT 233
Cdd:COG0624 167 DAAIVGEPTGV----PTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAAlRDLEFDGRADPLFGRTTLNVT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 234 TVDvGNSATNVIPAKASARVNIRFNDEHKGAELVERVSRTVLAHAPHAEIK---AVISGESFITPP-GDFSALVSSAITK 309
Cdd:COG0624 243 GIE-GGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEvevLGDGRPPFETPPdSPLVAAARAAIRE 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819653059 310 VTGLVPELSTTGGTSDARFLSRI--CPVVEFGLCN-ATMHKLDEAVAVPDLYALADIYEEIVR 369
Cdd:COG0624 322 VTGKEPVLSGVGGGTDARFFAEAlgIPTVVFGPGDgAGAHAPDEYVELDDLEKGARVLARLLE 384
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
6-368 |
5.19e-63 |
|
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: 205.61 E-value: 5.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 6 ALTQRLIACPSVTPADAGAMAVIAEALEGLGFAVHRFAAGGPPdgpieNLFA-IRGESGPHFAFAGHSDVVPPG--SGWT 82
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRG-----NLVAtVGGGDGPVLLLNGHIDTVPPGdgDKWS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 83 GDPFVPEIRGELLYGRGAVDMKGA----IAAFIAAIARIEQDRGTVSLIITGDEEGPAThGTVALIDwmNERGIRPDLCL 158
Cdd:cd08659 76 FPPFSGRIRDGRLYGRGACDMKGGlaamVAALIELKEAGALLGGRVALLATVDEEVGSD-GARALLE--AGYADRLDALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 159 VGEPTsthrlGDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPVPELVRALAALDALHLDDG-NAWFQPSNLEITTVDv 237
Cdd:cd08659 153 VGEPT-----GLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPaHPLLGPPTLNVGVIN- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 238 GNSATNVIPAKASARVNIRFNDEHKGAELVERVSRTVLAHAPHAEIKAVISGES--FITPPGDFSALVSSAITKVTGLvP 315
Cdd:cd08659 227 GGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPpfFTDPDHPLVQALQAAARALGGD-P 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1819653059 316 ELSTTGGTSDARFLSRI--CPVVEFGLCN-ATMHKLDEAVAVPDLYALADIYEEIV 368
Cdd:cd08659 306 VVRPFTGTTDASYFAKDlgFPVVVYGPGDlALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
67-369 |
8.28e-54 |
|
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: 180.24 E-value: 8.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 67 AFAGHSDVVPPGSGWtGDPFVPEIRGeLLYGRGAVDMKGAIAAFIAAIARIEQ---DRGTVSLIITGDEEGPaTHGTVAL 143
Cdd:pfam01546 1 LLRGHMDVVPDEETW-GWPFKSTEDG-KLYGRGHDDMKGGLLAALEALRALKEeglKKGTVKLLFQPDEEGG-MGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 144 IDWMNERGIRPDLCL---VGEPTS-THRLGDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPVPELVRALAALDALHLD 219
Cdd:pfam01546 78 IEDGLLEREKVDAVFglhIGEPTLlEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 220 DGNAwFQPSNLEITTVDVGNSATNVIPAKASARVNIRFNDEHKGAELVERVSRTVLAHAPH----AEIKAVISGESFITP 295
Cdd:pfam01546 158 NVDP-LDPAVVTVGNITGIPGGVNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAygvkVEVEYVEGGAPPLVN 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819653059 296 PGDFSALVSSAITKVTGLVPELSTTG--GTSDARFLSRICP--VVEFGLCNATMHKLDEAVAVPDLYALADIYEEIVR 369
Cdd:pfam01546 237 DSPLVAALREAAKELFGLKVELIVSGsmGGTDAAFFLLGVPptVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLLL 314
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
1-369 |
5.96e-45 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 159.00 E-value: 5.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 1 MIDPLALTQRLIACPSVTPA--DAGAMA-VIAEALEGLGFA--VHRFAAGGPPDGPIE--NLFAIRGESGPHFAFAGHSD 73
Cdd:PRK08651 5 MFDIVEFLKDLIKIPTVNPPgeNYEEIAeFLRDTLEELGFSteIIEVPNEYVKKHDGPrpNLIARRGSGNPHLHFNGHYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 74 VVPPGSGW-TGDPFVPEIRGELLYGRGAVDMKGA-IAAFIAAIARIEQDRGTVSLIITGDEEGPAThGTVALIDwmnERG 151
Cdd:PRK08651 85 VVPPGEGWsVNVPFEPKVKDGKVYGRGASDMKGGiAALLAAFERLDPAGDGNIELAIVPDEETGGT-GTGYLVE---EGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 152 IRPDLCLVGEPTSThrlgDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPVPELVRALAALDALHLDDGNAWFQPS--- 228
Cdd:PRK08651 161 VTPDYVIVGEPSGL----DNICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYEYDDerg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 229 -----NLEITTVDVGNsATNVIPAKASARVNIRFNDEHKGAELVERVSRTVLAHAP----HAEIKAVISGESFITPPG-D 298
Cdd:PRK08651 237 akptvTLGGPTVEGGT-KTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPelgiEVEFEITPFSEAFVTDPDsE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819653059 299 FSALVSSAITKVTGLVPELSTTGGTSDARFLSRI-CPVVEFG---LCNAtmHKLDEAVAVPDLYALADIYEEIVR 369
Cdd:PRK08651 316 LVKALREAIREVLGVEPKKTISLGGTDARFFGAKgIPTVVYGpgeLELA--HAPDEYVEVKDVEKAAKVYEEVLK 388
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-368 |
2.30e-39 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 143.30 E-value: 2.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSVTPADAG---AMAVIAEALEGLGFAVHRFaaggPPDGPIENLFAI--RGESGPHFAFAGHSDVVP--P 77
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDNtsaIAAYIKLLLEDLGYPVELH----EPPEEIYGVVSNivGGRKGKRLLFNGHYDVVPagD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 78 GSGWTGDPFVPEIRGELLYGRGAVDMKG----AIAAFIAAIARIEQDRGTVSLIITGDEEGPATHGTvaliDWMNERG-I 152
Cdd:cd08011 77 GEGWTVDPYSGKIKDGKLYGRGSSDMKGgiaaSIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGT----KYLLEKVrI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 153 RPDLCLVGEPTSThrlgDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPVPELVRalaaldaLHLDDGNawfqpsnlEI 232
Cdd:cd08011 153 KPNDVLIGEPSGS----DNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMK-------LIERLYE--------LE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 233 TTVDVGN----SATNVIPAKASARVNIRFNDEHKGAELVERVSRTVlahAPHAEIKAVISGESFITPPGDFSALVS---S 305
Cdd:cd08011 214 KTVNPGVikggVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHL---DSIEEVSFEIKSFYSPTVSNPDSEIVKkteE 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819653059 306 AITKVTGLVPELSTTGGTSDARFLSRI-CPVVEFGLCN-ATMHKLDEAVAVPDLYALADIYEEIV 368
Cdd:cd08011 291 AITEVLGIRPKEVISVGASDARFYRNAgIPAIVYGPGRlGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
5-363 |
1.09e-32 |
|
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: 125.59 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSVTP---ADAGAMAVIAEALEGLGFAVHRFA-AGGPPDGPIENLFAIRGESG-PHFAFAGHSDVVPPG- 78
Cdd:TIGR01910 1 VELLKDLISIPSVNPpggNEETIANYIKDLLREFGFSTDVIEiTDDRLKVLGKVVVKEPGNGNeKSLIFNGHYDVVPAGd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 79 -SGWTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQDRGTVSLII-----TGDEEGPAthGTVALIdwmnERGI 152
Cdd:TIGR01910 81 lELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIilqsvVDEESGEA--GTLYLL----QRGY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 153 R--PDLCLVGEPTSthrlGDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPV----------PELVRALAALDALHLDD 220
Cdd:TIGR01910 155 FkdADGVLIPEPSG----GDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAImklaklitelNELEEHIYARNSYGFIP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 221 GnawfqPSNLEITTVDVGNSAtNVIPAKASARVNIRF-----NDEHKG--AELVERVSRTVLAHAPHaEIKAVISGESFI 293
Cdd:TIGR01910 231 G-----PITFNPGVIKGGDWV-NSVPDYCEFSIDVRIipeenLDEVKQiiEDVVKALSKSDGWLYEN-EPVVKWSGPNET 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819653059 294 TPPGDFSALVSSAITKVTGLVPELSTTGGTSDARFLS-RICPVVEFGL-CNATMHKLDEAVAVPDLYALADI 363
Cdd:TIGR01910 304 PPDSRLVKALEAIIKKVRGIEPEVLVSTGGTDARFLRkAGIPSIVYGPgDLETAHQVNEYISIKNLVESTKV 375
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
6-369 |
3.93e-32 |
|
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: 123.86 E-value: 3.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 6 ALTQRLIACPSVTPADAGAM-AVIAEALEGLGFAVHRFAaggPPDGPIENLFA-IRGESGPHFAFAGHSDVVP-PGSGWT 82
Cdd:cd03894 1 ELLARLVAFDTVSRNSNLALiEYVADYLAALGVKSRRVP---VPEGGKANLLAtLGPGGEGGLLLSGHTDVVPvDGQKWS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 83 GDPFVPEIRGELLYGRGAVDMKGAIAA--FIAAIARIEQDRGTVSLIITGDEEgpATH-GTVALIDWMNERGIRPDLCLV 159
Cdd:cd03894 78 SDPFTLTERDGRLYGRGTCDMKGFLAAvlAAVPRLLAAKLRKPLHLAFSYDEE--VGClGVRHLIAALAARGGRPDAAIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 160 GEPTSthrlgdM-VKIGRRGSVNIWIENAGTQGHVAYPHLARNPVPELVRALAA----LDALHLDDGNAWFQP--SNLEI 232
Cdd:cd03894 156 GEPTS------LqPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKlrelADRLAPGLRDPPFDPpyPTLNV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 233 TTVDVGNsATNVIPAKASARVNIRFNDEHKGAELVERV---SRTVLAHAPHAeikavISGESFITPPGdFSALVSSAIT- 308
Cdd:cd03894 230 GLIHGGN-AVNIVPAECEFEFEFRPLPGEDPEAIDARLrdyAEALLEFPEAG-----IEVEPLFEVPG-LETDEDAPLVr 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819653059 309 ---KVTGLVPELSTTGGTSDARFLSRICPVVEFGLCN-ATMHKLDEAVAVPDLYALADIYEEIVR 369
Cdd:cd03894 303 laaALAGDNKVRTVAYGTEAGLFQRAGIPTVVCGPGSiAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
3-369 |
2.35e-26 |
|
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: 107.82 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 3 DPLALTQRLIACPSVTPADAGAMAVIAEALEGLGFAVHRFAAGgppdgpieNLFAIRGESGPHFAFAGHSDVVPpgsgwt 82
Cdd:cd05653 2 DAVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEAG--------NAVGGAGSGPPDVLLLGHIDTVP------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 83 gDPFVPEIRGELLYGRGAVDMKGA-IAAFIAAIARIEQDRGTVSLIITGDEEGpATHGTVALIdwmnERGIRPDLCLVGE 161
Cdd:cd05653 68 -GEIPVRVEGGVLYGRGAVDAKGPlAAMILAASALNEELGARVVVAGLVDEEG-SSKGARELV----RRGPRPDYIIIGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 162 PTSThrlgDMVKIGRRGSVNIWIENAGTQGHVAYPhlARNPVPELVRALAALDALHLDDGNAWFQPSNLEITTVDVGnSA 241
Cdd:cd05653 142 PSGW----DGITLGYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLIKKWLEVKKWAEGYNVGGRDFDSVVPTLIKGG-ES 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 242 TNVIPAKASARVNIRFNDEHKGAELVErvsrTVLAHAPHAEIKAVISGESFITPPGdfSALVSS---AITKvTGLVPELS 318
Cdd:cd05653 215 SNGLPQRAEATIDLRLPPRLSPEEAIA----LATALLPTCELEFIDDTEPVKVSKN--NPLARAfrrAIRK-QGGKPRLK 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1819653059 319 TTGGTSDARFLSRI--CPVVEFGLCNATM-HKLDEAVAVPDLYALADIYEEIVR 369
Cdd:cd05653 288 RKTGTSDMNVLAPLwtVPIVAYGPGDSTLdHTPNEHIELAEIERAAAVLKGALE 341
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
11-363 |
3.07e-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: 105.87 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 11 LIACPSVTPADA------GAMAVIAEALEGLGFAVHR-FAAGGPPdgpieNLFAIRGESG--PHFAFAGHSDVVPPG--S 79
Cdd:cd03893 7 LVAIPSVSAQPDrreelrRAAEWLADLLRRLGFTVEIvDTSNGAP-----VVFAEFPGAPgaPTVLLYGHYDVQPAGdeD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 80 GWTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQDRGT----VSLIITGDEEGpathGTVALIDWMNER--GIR 153
Cdd:cd03893 82 GWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDlpvnVKFIIEGEEES----GSPSLDQLVEAHrdLLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 154 PDLCLVGEPTSTHRLGDMVKIGRRGSVNIWIE------------------NAGT------------QGHVAYPHLARNP- 202
Cdd:cd03893 158 ADAIVISDSTWVGQEQPTLTYGLRGNANFDVEvkgldhdlhsglyggvvpDPMTalaqllaslrdeTGRILVPGLYDAVr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 203 ------------VPELVRALAALDALHLDdgNAWFQPSnLEITTVD---VGNSATNVIPAKASARVNIRFNDEHKGAELV 267
Cdd:cd03893 238 elpeeefrldagVLEEVEIIGGTTGSVAE--RLWTRPA-LTVLGIDggfPGEGSKTVIPPRARAKISIRLVPGQDPEEAS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 268 ERVSRTVLAHAP---HAEIKAVISGESFITPPGDFSAL-VSSAITKVTGLVPELSTTGGT-SDARFLSRI--CPVVEFGL 340
Cdd:cd03893 315 RLLEAHLEKHAPsgaKVTVSYVEGGMPWRSDPSDPAYQaAKDALRTAYGVEPPLTREGGSiPFISVLQEFpqAPVLLIGV 394
|
410 420
....*....|....*....|....*
gi 1819653059 341 CNAT--MHKLDEAVAVPDLYALADI 363
Cdd:cd03893 395 GDPDdnAHSPNESLRLGNYKEGTQA 419
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
1-164 |
5.27e-25 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 104.50 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 1 MIDPLALTQRLIACPSVTPADAGAM-AVIAEALEGLGFAVHRFAAggpPDGPIENLFA-IRGESGPHFAFAGHSDVVP-P 77
Cdd:PRK07522 3 SMSSLDILERLVAFDTVSRDSNLALiEWVRDYLAAHGVESELIPD---PEGDKANLFAtIGPADRGGIVLSGHTDVVPvD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 78 GSGWTGDPFVPEIRGELLYGRGAVDMKG--AIAAFIAAIARIEQDRGTVSLIITGDEE-GPAthGTVALIDWMNERGIRP 154
Cdd:PRK07522 80 GQAWTSDPFRLTERDGRLYGRGTCDMKGfiAAALAAVPELAAAPLRRPLHLAFSYDEEvGCL--GVPSMIARLPERGVKP 157
|
170
....*....|
gi 1819653059 155 DLCLVGEPTS 164
Cdd:PRK07522 158 AGCIVGEPTS 167
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
54-369 |
9.60e-21 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 92.25 E-value: 9.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 54 NLFAIRGESGPHFAFAGHSDVVPPG--SGWTGDPFVPEIRGELLYGRGAVDMK-GAIAAFIAAIARIEQD---RGTVSLI 127
Cdd:PRK08588 50 NLVAEIGSGSPVLALSGHMDVVAAGdvDKWTYDPFELTEKDGKLYGRGATDMKsGLAALVIAMIELKEQGqllNGTIRLL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 128 ITGDEEgPATHGTVALIdwmnERGIRPDL--CLVGEPTsthrlGDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPVPE 205
Cdd:PRK08588 130 ATAGEE-VGELGAKQLT----EKGYADDLdaLIIGEPS-----GHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 206 LVRALAALdalhlddgNAWFQ--PSNLEI-------TTVDVGNSATNVIPAKASARVNIRFNDEHKGAELVERVSRTV-- 274
Cdd:PRK08588 200 LLEFYNEQ--------KEYFDsiKKHNPYlgglthvVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIIne 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 275 LAHAPHAEIKA-VISGES--FITPPGDFSALVSSAITKVTGLVPELSTTGGTSDA-RFLSRI--CPVVEFGL-CNATMHK 347
Cdd:PRK08588 272 VNQNGAAQLSLdIYSNHRpvASDKDSKLVQLAKDVAKSYVGQDIPLSAIPGATDAsSFLKKKpdFPVIIFGPgNNLTAHQ 351
|
330 340
....*....|....*....|..
gi 1819653059 348 LDEAVAVPDLYALADIYEEIVR 369
Cdd:PRK08588 352 VDEYVEKDMYLKFIDIYKEIII 373
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
63-364 |
1.62e-20 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 91.38 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 63 GPHFAFAGHSDVVPpgsGWtgdpFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQDRGTVSLIITGDEEGPAThGTVA 142
Cdd:PRK00466 60 EGDILLASHVDTVP---GY----IEPKIEGEVIYGRGAVDAKGPLISMIIAAWLLNEKGIKVMVSGLADEESTSI-GAKE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 143 LIdwmnERGIRPDLCLVGEPTSThrlgDMVKIGRRGSVNIWIENAGTQGHVAYPhlARNPVPELVRALAaldalhlddgN 222
Cdd:PRK00466 132 LV----SKGFNFKHIIVGEPSNG----TDIVVEYRGSIQLDIMCEGTPEHSSSA--KSNLIVDISKKII----------E 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 223 AWFQPSNLE-----ITTVDVGNSAtNVIPAKASARVNIRFNDEHKGAELVERVSRTVlahaPHAEIKAVISgesfiTPPG 297
Cdd:PRK00466 192 VYKQPENYDkpsivPTIIRAGESY-NVTPAKLYLHFDVRYAINNKRDDLISEIKDKF----QECGLKIVDE-----TPPV 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819653059 298 DFSalVSSAITKV-------TGLVPELSTTGGTSDARFLSRICP-VVEFGLCNATM-HKLDEAVAVPDLYALADIY 364
Cdd:PRK00466 262 KVS--INNPVVKAlmrallkQNIKPRLVRKAGTSDMNILQKITTsIATYGPGNSMLeHTNQEKITLDEIYIAVKTY 335
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
10-368 |
2.93e-19 |
|
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: 87.95 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 10 RLIACPSVT-PADAGAMAVIAEALEGLGFAVHRFAagGPPDGPIENLFAIRGESGPH-FAFAGHSDVVP-PGSGWTGDPF 86
Cdd:TIGR01892 5 KLVAFDSTSfRPNVDLIDWAQAYLEALGFSVEVQP--FPDGAEKSNLVAVIGPSGAGgLALSGHTDVVPyDDAAWTRDPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 87 VPEIRGELLYGRGAVDMKG--AIAAFIAAIARIEQDRGTVSLIITGDEEGPAThGTVALIDWMnerGIRPDLCLVGEPTs 164
Cdd:TIGR01892 83 RLTEKDGRLYGRGTCDMKGflACALAAAPDLAAEQLKKPLHLALTADEEVGCT-GAPKMIEAG---AGRPRHAIIGEPT- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 165 thrlgDMVKI-GRRGSVNIWIENAGTQGHVAYPHLARNPV----PELVRALAALDALHLDDGNAWFQP--SNLEITTVDv 237
Cdd:TIGR01892 158 -----RLIPVrAHKGYASAEVTVRGRSGHSSYPDSGVNAIfragRFLQRLVHLADTLLREDLDEGFTPpyTTLNIGVIQ- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 238 GNSATNVIPAKASARVNIRF---NDEHKGAELVERVSRTVLAHAPHAEIK-AVISGESFITPPGDfsALVSSAITKVTGL 313
Cdd:TIGR01892 232 GGKAVNIIPGACEFVFEWRPipgMDPEELLQLLETIAQALVRDEPGFEVQiEVVSTDPGVNTEPD--AELVAFLEELSGN 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1819653059 314 VPELSTTGgtSDARFLSRI-CPVVEFGLCNATM-HKLDEAVAVPDLYALADIYEEIV 368
Cdd:TIGR01892 310 APEVVSYG--TEAPQFQELgAEAVVCGPGDIRQaHQPDEYVEIEDLVRCRAVLARLV 364
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
3-368 |
4.66e-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. 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: 86.98 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 3 DPLALTQRLIACPSVTPADAGAMAVIAEALEGLGFAVHRFAaggppdgpiENLFAIRG---ESGPHFAFAGHSDVVPPGS 79
Cdd:cd05651 1 EAIELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRKG---------NNVWAENGhfdEGKPTLLLNSHHDTVKPNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 80 GWTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIA--RIEQDRG-TVSLIITGDEEGPATHGTVALIDWMNERgirpDL 156
Cdd:cd05651 72 GWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLhlYSEGPLNyNLIYAASAEEEISGKNGIESLLPHLPPL----DL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 157 CLVGEPTSTHrlgdmVKIGRRGSVNIWIENAGTQGHVAYPHlARNPVPELVRALaaldalhlddgnAWFQ---------- 226
Cdd:cd05651 148 AIVGEPTEMQ-----PAIAEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDI------------QWLRdfrfdkvspl 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 227 --PSNLEITTVDVGnSATNVIPAKASARVNIRFNDEHKGAELVErvsrtVLAHAPHAEIKAvisgESFitppgdfsALVS 304
Cdd:cd05651 210 lgPVKMTVTQINAG-TQHNVVPDSCTFVVDIRTTEAYTNEEIFE-----IIRGNLKSEIKP----RSF--------RLNS 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819653059 305 SAI---------TKVTGLVPELSTTggTSDARFLSriCPVVEFGLCNATM-HKLDEAVAVPDLYALADIYEEIV 368
Cdd:cd05651 272 SAIppdhpivqaAIAAGRTPFGSPT--LSDQALMP--FPSVKIGPGDSSRsHTADEFIELSEIEEGIDIYIELL 341
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
5-369 |
7.24e-19 |
|
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: 87.41 E-value: 7.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSVTPADAG-----AMAVIAEALEGLGFAVHRFAAGGPP-DGpieNLFA-IRGE--SGPHFAFAGHSDVV 75
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTgsetrAAEVLAARLAEAGIQTEIFVVESHPgRA---NLVArIGGTdpSAGPLLLLGHIDVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 76 PP-GSGWTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQD----RGTVSLIITGDEEGPATHGtvalIDWMNER 150
Cdd:cd05675 78 PAdASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREgfkpKRDLVFAFVADEEAGGENG----AKWLVDN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 151 giRPDL------CL--VGEPTST-HRLGDMVKI--GRRGSVNIWIENAGTQGHVAYPH--------------LARNPVP- 204
Cdd:cd05675 154 --HPELfdgatfALneGGGGSLPvGKGRRLYPIqvAEKGIAWMKLTVRGRAGHGSRPTddnaitrlaealrrLGAHNFPv 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 205 -------------ELVRALAALDALHLDDGN----AWFQPSN------LEIT---TVDVGNSATNVIPAKASARVNIRFN 258
Cdd:cd05675 232 rltdetayfaqmaELAGGEGGALMLTAVPVLdpalAKLGPSApllnamLRNTaspTMLDAGYATNVLPGRATAEVDCRIL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 259 DEHKGAELVERVSRtvLAHAPHAEIKAVISGESFITPPGdfSALVsSAITKVTG-------LVPELSTtgGTSDARFLSR 331
Cdd:cd05675 312 PGQSEEEVLDTLDK--LLGDPDVSVEAVHLEPATESPLD--SPLV-DAMEAAVQavdpgapVVPYMSP--GGTDAKYFRR 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1819653059 332 IcPVVEFGLCNATM----------HKLDEAVAVPDLYALADIYEEIVR 369
Cdd:cd05675 385 L-GIPGYGFAPLFLppeldytglfHGVDERVPVESLYFGVRFLDRLVK 431
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
5-350 |
7.57e-19 |
|
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: 86.88 E-value: 7.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRL--IACPSVTPADAGAMA-VIAEALEGLGFAVHRFAAGGPPDgpieNLFA-IRGESGPHFAFAGHSDVV-PPGS 79
Cdd:cd03885 2 LDLLERLvnIESGTYDKEGVDRVAeLLAEELEALGFTVERRPLGEFGD----HLIAtFKGTGGKRVLLIGHMDTVfPEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 80 GWTgDPFvpEIRGELLYGRGAVDMKGAIAAFIAAIARIEQ----DRGTVSLIITGDEEgPATHGTVALIDwmnERGIRPD 155
Cdd:cd03885 78 LAF-RPF--TVDGDRAYGPGVADMKGGLVVILHALKALKAaggrDYLPITVLLNSDEE-IGSPGSRELIE---EEAKGAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 156 LCLVGEPTsthRLGDMVKIGRRGSVNIWIENAGTQGHV-AYPHLARNPVPELVRALaaldalhlddgNAWFQPSNLEI-T 233
Cdd:cd03885 151 YVLVFEPA---RADGNLVTARKGIGRFRLTVKGRAAHAgNAPEKGRSAIYELAHQV-----------LALHALTDPEKgT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 234 TVDV----GNSATNVIPAKASARVNIRFNDEHKGAELVERVsRTVLAHAPHAEIKAVISGEsFITPP----GDFSALV-- 303
Cdd:cd03885 217 TVNVgvisGGTRVNVVPDHAEAQVDVRFATAEEADRVEEAL-RAIVATTLVPGTSVELTGG-LNRPPmeetPASRRLLar 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1819653059 304 SSAITKVTGLVPELSTTGGTSDARFLSRI-CPVVE-FGLCNATMHKLDE 350
Cdd:cd03885 295 AQEIAAELGLTLDWEATGGGSDANFTAALgVPTLDgLGPVGGGAHTEDE 343
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-357 |
1.88e-18 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 85.82 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 6 ALTQRLIACPSVTPADAGAMAVIAEALEGLGFAVHRF-----AAGGPPD-GPIE-------NLFAI---RGESGPHFAFA 69
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDRWeidveKLKHHPGfSPVAvdyagapNVVGThrpRGETGRSLILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 70 GHSDVVPPGSG--WTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIE----QDRGTVSL-IITGDEEGPAthGTVA 142
Cdd:cd03895 81 GHIDVVPEGPVelWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRaaglQPAADVHFqSVVEEECTGN--GALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 143 LIdwmnERGIRPDLCLVGEPTsthrlGDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPVpELVRALAALDALHLDDGN 222
Cdd:cd03895 159 AL----MRGYRADAALIPEPT-----ELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAI-EKAMHLIQALQELEREWN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 223 A------WF----QPSNLEITTVDVGNSATNViPAKASARVNIRFNDEHKGAELVERVSRTVLAHAPHAE------IKAV 286
Cdd:cd03895 229 ArkkshpHFsdhpHPINFNIGKIEGGDWPSSV-PAWCVLDCRIGIYPGESPEEARREIEECVADAAATDPwlsnhpPEVE 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819653059 287 ISGESF----ITPPGDFSALVSSAITKVTGLVPELSTTGGTSDARFLSRI--CPVVEFGLCNATMHKLDEAVAVPDL 357
Cdd:cd03895 308 WNGFQAegyvLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYgdIPALCYGPGSRDAHGFDESVDLESL 384
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
1-180 |
7.23e-18 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 83.85 E-value: 7.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 1 MIDPLALTQRLIACPSVTPADAGAMAVIAEALEGLGFAVHRFAAGgppdgpieNLFAIRGESGPHFAFAGHSDVVPpgsg 80
Cdd:PRK04443 5 ALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREAWVDEAG--------NARGPAGDGPPLVLLLGHIDTVP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 81 wtGDpfVP-EIRGELLYGRGAVDMKGAIAAFIAAIARIEQDRGT-VSLIITGDEEGPATHGTVALIDWMnergiRPDLCL 158
Cdd:PRK04443 73 --GD--IPvRVEDGVLWGRGSVDAKGPLAAFAAAAARLEALVRArVSFVGAVEEEAPSSGGARLVADRE-----RPDAVI 143
|
170 180
....*....|....*....|..
gi 1819653059 159 VGEPTSThrlgDMVKIGRRGSV 180
Cdd:PRK04443 144 IGEPSGW----DGITLGYKGRL 161
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
3-203 |
6.58e-17 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 81.52 E-value: 6.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 3 DPLALTQRLIACPSVTPADAGAMAVIAEALEGLGF-AVHRfaaggppDgPIENLFAIRGeSGPH-FAFAGHSDVVPPG-- 78
Cdd:PRK13004 16 DMTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFdKVEI-------D-PMGNVLGYIG-HGKKlIAFDAHIDTVGIGdi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 79 SGWTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQ----DRGTvsLIITG-----DEEGpathgtVALIDWMNE 149
Cdd:PRK13004 87 KNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDlgldDEYT--LYVTGtvqeeDCDG------LCWRYIIEE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1819653059 150 RGIRPDLCLVGEPTSthrlgDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPV 203
Cdd:PRK13004 159 DKIKPDFVVITEPTD-----LNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAI 207
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
5-352 |
1.24e-16 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 80.82 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSVTPADAGAMAVIAEALEGLGFAVHRFA------AGGPPDGPIE-------NLFAI---RGESGPHFAF 68
Cdd:PRK06837 23 VAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDRWSidpddlKSHPGAGPVEidysgapNVVGTyrpAGKTGRSLIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 69 AGHSDVVPPG--SGWTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIE----QDRGTVSLIITGDEEgpaTHGTVA 142
Cdd:PRK06837 103 QGHIDVVPEGplDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRaaglAPAARVHFQSVIEEE---STGNGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 143 LIDWMneRGIRPDLCLVGEPTsthrlGDMVKIGRRGSvnIW--IENAGTQGHVAYPHLARNPVPE---LVRALAALDAL- 216
Cdd:PRK06837 180 LSTLQ--RGYRADACLIPEPT-----GEKLVRAQVGV--IWfrLRVRGAPVHVREAGTGANAIDAayhLIQALRELEAEw 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 217 -HLDDGNAWFQ----PSNLEITTVDVGNSATNViPAKASARVNIRF-----NDEHKgAELVERVSRTVLAHA------PH 280
Cdd:PRK06837 251 nARKASDPHFEdvphPINFNVGIIKGGDWASSV-PAWCDLDCRIAIypgvtAADAQ-AEIEACLAAAARDDRflsnnpPE 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819653059 281 AEIKAVISGESFITPPGDFSALVSSAITKVTGLVPELSTTGGTSDARFLS---RIcPVVEFGLCNATMHKLDEAV 352
Cdd:PRK06837 329 VVWSGFLAEGYVLEPGSEAEAALARAHAAVFGGPLRSFVTTAYTDTRFYGlyyGI-PALCYGPSGEGIHGFDERV 402
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
3-203 |
1.40e-16 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 80.57 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 3 DPLALTQRLIACPSVTP---ADAGAMAVIAEALEGLGFAVHRFAAGGPPDG----PIENLFAIR--GESGPHFAFAGHSD 73
Cdd:PRK13013 15 DLVALTQDLIRIPTLNPpgrAYREICEFLAARLAPRGFEVELIRAEGAPGDsetyPRWNLVARRqgARDGDCVHFNSHHD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 74 VVPPGSGWTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQD----RGTVSLIITGDEEGpATHGTVAlidWMNE 149
Cdd:PRK13013 95 VVEVGHGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVypdfAGSIEISGTADEES-GGFGGVA---YLAE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819653059 150 RG----IRPDLCLVGEPTSTHRlgdmVKIGRRGsvnIW---IENAGTQGHVAYPHLARNPV 203
Cdd:PRK13013 171 QGrfspDRVQHVIIPEPLNKDR----ICLGHRG---VWwaeVETRGRIAHGSMPFLGDSAI 224
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
55-374 |
6.18e-16 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 78.83 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 55 LFAIRG--ESGPHFAFAGHSDVVP--PGS--GWTGDPFVPEIRGELLYGRGAVDMKGAIAA----FIAAIARIEQDRGTV 124
Cdd:PRK08262 101 LYTWKGsdPSLKPIVLMAHQDVVPvaPGTegDWTHPPFSGVIADGYVWGRGALDDKGSLVAileaAEALLAQGFQPRRTI 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 125 SLIITGDEEgPATHGTVALIDWMNERGIRPDLCL-------------VGEPTSthrlgdMVKIGRRGSVNIWIENAGTQG 191
Cdd:PRK08262 181 YLAFGHDEE-VGGLGARAIAELLKERGVRLAFVLdeggaitegvlpgVKKPVA------LIGVAEKGYATLELTARATGG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 192 HVAYP--------------HLARNPVPELVRALAA----------LDALHLDDGNAW-FQPSNLEI------------TT 234
Cdd:PRK08262 254 HSSMPprqtaigrlaraltRLEDNPLPMRLRGPVAemfdtlapemSFAQRVVLANLWlFEPLLLRVlakspetaamlrTT 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 235 VDV----GNSATNVIPAKASARVNIRFNDEHKGAELVERVSRTVlaHAPHAEIKAV--ISGESFITPPGDFS-ALVSSAI 307
Cdd:PRK08262 334 TAPtmlkGSPKDNVLPQRATATVNFRILPGDSVESVLAHVRRAV--ADDRVEIEVLggNSEPSPVSSTDSAAyKLLAATI 411
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819653059 308 TKV---TGLVPELsTTGGTsDARFLS-------RICPVVEFGLCNATMHKLDEAVAVPDLYALADIYEEIVRVALAR 374
Cdd:PRK08262 412 REVfpdVVVAPYL-VVGAT-DSRHYSgisdnvyRFSPLRLSPEDLARFHGTNERISVANYARMIRFYYRLIENAAGL 486
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
174-282 |
2.55e-15 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 71.22 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 174 IGRRGSVNIWIENAGTQGHVAYPHLARNPVPELVRALAALDALHLDDGNAWfQPSNLEITTVDVGNsATNVIPAKASARV 253
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGFDF-PRTTLNITGIEGGT-ATNVIPAEAEAKF 78
|
90 100
....*....|....*....|....*....
gi 1819653059 254 NIRFNDEHKGAELVERVSRTVLAHAPHAE 282
Cdd:pfam07687 79 DIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-286 |
2.58e-15 |
|
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: 76.16 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSVTPADAGAMAVIAEALEGLGFAVHRFAAggpPDGPIENLFAIRGES-GPHFAFAGHSDVVPPgsgwtg 83
Cdd:cd05652 2 LSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKQPV---ENKDRFNVYAYPGSSrQPRVLLTSHIDTVPP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 84 dpFVP---EIRGELLYGRGAVDMKGAIAA----FIAAIARIEQDRGTVSLI-ITGDEEGpaTHGTVALIDWMNERgirPD 155
Cdd:cd05652 73 --FIPysiSDGGDTIYGRGSVDAKGSVAAqiiaVEELLAEGEVPEGDLGLLfVVGEETG--GDGMKAFNDLGLNT---WD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 156 LCLVGEPTSthrlGDMVKiGRRGSVNIWIENAGTQGHVAYPHLARNPVPELVRaLAALDALHLDDGNAWFQPSNLEITTV 235
Cdd:cd05652 146 AVIFGEPTE----LKLAS-GHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVE-ALVKLIDADLPSSELLGPTTLNIGRI 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1819653059 236 DvGNSATNVIPAKASARVNIRF-NDEHKGAELVERVSRTVLAHAPHAEIKAV 286
Cdd:cd05652 220 S-GGVAANVVPAAAEASVAIRLaAGPPEVKDIVKEAVAGILTDTEDIEVTFT 270
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
1-201 |
1.15e-14 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 74.50 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 1 MIDplaLTQRLIACPSVTPADAG----AMA-VIAEALEGLGFA-VHRFAAGGP--PDGPIENLFA-IRGESGPH-FAFAG 70
Cdd:PRK13983 7 MIE---LLSELIAIPAVNPDFGGegekEKAeYLESLLKEYGFDeVERYDAPDPrvIEGVRPNIVAkIPGGDGKRtLWIIS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 71 HSDVVPPG--SGWTGDPFVPEIRGELLYGRGAVD-MKGAIAAFIAAIARIEQD---RGTVSLIITGDEEGPATHGtvalI 144
Cdd:PRK13983 84 HMDVVPPGdlSLWETDPFKPVVKDGKIYGRGSEDnGQGIVSSLLALKALMDLGirpKYNLGLAFVSDEETGSKYG----I 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819653059 145 DWM--NERGI--RPDLCLV---GEPTsthrlGDMVKIGRRGSVNIWIENAGTQGHVAYPHLARN 201
Cdd:PRK13983 160 QYLlkKHPELfkKDDLILVpdaGNPD-----GSFIEIAEKSILWLKFTVKGKQCHASTPENGIN 218
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-367 |
1.43e-14 |
|
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: 74.42 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 7 LTQRLIACPSVTPADAG-AMAVIAEALEG----LGFA-VHRFAAGGPPDGPIENL-FAIRGESGPHFAFAGHSDVVPPG- 78
Cdd:cd05650 6 LERDLIRIPAVNPESGGeGEKEKADYLEKklreYGFYtLERYDAPDERGIIRPNIvAKIPGGNDKTLWIISHLDTVPPGd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 79 -SGWTGDPFVPEIRGELLYGRGAVD-----MKGAIAAFIAAIARIEQDRGtVSLIITGDEEGPATHGTVALIdwmNERGI 152
Cdd:cd05650 86 lSLWETDPWEPVVKDGKIYGRGVEDnqqgiVSSLLALKAIIKNGITPKYN-FGLLFVADEEDGSEYGIQYLL---NKFDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 153 --RPDLCLV---GEPTsthrlGDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNP----------VPELVRALAALDALH 217
Cdd:cd05650 162 fkKDDLIIVpdfGTED-----GEFIEIAEKSILWIKVNVKGKQCHASTPENGINAfvaasnfaleLDELLHEKFDEKDDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 218 LDDGNAWFQPSNLEITTVDVgnsatNVIPAKASARVNIRFNDEHKGAELVERVSRtvLAHAPHAEIKAVISGESFI---- 293
Cdd:cd05650 237 FNPPYSTFEPTKKEANVPNV-----NTIPGYDVFYFDCRVLPTYKLDEVLKFVNK--IISDFENSYGAGITYEIVQkeqa 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819653059 294 ---TPP-GDFSALVSSAITKVTGLVPELSTTGGTSDARFL-SRICPVVEFGLCNATMHKLDEAVAVPDLYALADIYEEI 367
Cdd:cd05650 310 ppaTPEdSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLrKKGYPAVVWSTLDETAHQPNEYIRISHIVKDAKVFAEM 388
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
5-366 |
2.42e-14 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 73.82 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSVTPADAGAMAV---IAEALEG-------LGFAVHRF--AAGgppdgpienlFAIRGESGPHFAFAGHS 72
Cdd:cd03888 11 LEDLKELVAIPSVRDEATEGAPFgegPRKALDKfldlakrLGFKTKNIdnYAG----------YAEYGEGEEVLGILGHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 73 DVVPPGSGWTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIE----QDRGTVSLIITGDEEG-------------- 134
Cdd:cd03888 81 DVVPAGEGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKdlglPLKKKIRLIFGTDEETgwkciehyfeheey 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 135 -----------PATHGtvalidwmnERGI-RPDLCLVGEPTSTHRLG--------DMV------------------KIGR 176
Cdd:cd03888 161 pdfgftpdaefPVING---------EKGIvTVDLTFKIDDDKGYRLIsikggeatNMVpdkaeavipgkdkeelalSAAT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 177 RGSVNIWIEN-------AGTQGHVAYPHLARNPVPELVRALAALDALHLDDGNA------WFQPSNLE-----ITTVDVG 238
Cdd:cd03888 232 DLKGNIEIDDggveltvTGKSAHASAPEKGVNAITLLAKFLAELNKDGNDKDFIkflaknLHEDYNGKklginFEDEVMG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 239 NSATNV-----IPAKASARVNIRFNDEHKGAELVERVSRTVlahaphAEIKAVISGESFITP---PGDfSALVSS---AI 307
Cdd:cd03888 312 ELTLNPgiitlDDGKLELGLNVRYPVGTSAEDIIKQIEEAL------EKYGVEVEGHKHQKPlyvPKD-SPLVKTllkVY 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819653059 308 TKVTGLVPELSTTGGTSDARFLSRIcpvVEFGLC----NATMHKLDEAVAVPDLYALADIYEE 366
Cdd:cd03888 385 EEQTGKEGEPVAIGGGTYARELPNG---VAFGPEfpgqKDTMHQANEFIPIDDLIKALAIYAE 444
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-203 |
3.32e-14 |
|
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: 73.22 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSVTPADAGAMAVIAEALEGLGF-AVHRfaaggppdGPIENLFAIRGESGPHFAFAGHSDVVPPG--SGW 81
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGFdEVEI--------DPMGNVIGYIGGGKKKILFDGHIDTVGIGniDNW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 82 TGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQDR-----GTVSLIITGDEE---GpathgtVALIDWMNERGIR 153
Cdd:cd05649 73 KFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGlrdfaYTILVAGTVQEEdcdG------VCWQYISKADKIK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1819653059 154 PDLCLVGEPTsthrlgDM-VKIGRRGSVNIWIENAGTQGHVAYPHLARNPV 203
Cdd:cd05649 147 PDFVVSGEPT------DGnIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAV 191
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
3-369 |
1.95e-13 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349935 [Multi-domain] Cd Length: 379 Bit Score: 70.97 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 3 DPLALTQRLI----ACPSVTPADAGAMAVIAEA----LEGLGFAVHRFAagGPPDGPiENLFAIRGESG-PHFAFAGHSD 73
Cdd:cd08013 2 DPVSLTQTLVrinsSNPSLSATGGAGEAEIATYvaawLAHRGIEAHRIE--GTPGRP-SVVGVVRGTGGgKSLMLNGHID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 74 VVPPgSGWTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQD--RGTVSLIITGDEEGpATHGTVALIdwmnERG 151
Cdd:cd08013 79 TVTL-DGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAglRGDVILAAVADEED-ASLGTQEVL----AAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 152 IRPDLCLVGEPTSThrlgdMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPVPE----LVRALAALDALHLDDGNAWFQP 227
Cdd:cd08013 153 WRADAAIVTEPTNL-----QIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKagyfLVALEEYQQELPERPVDPLLGR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 228 SNLEITTVDvGNSATNVIPAKASARVNIRF----NDEHKGAEL---VERVSRTVLAHApHAEIKAVISGESFITPPGD-F 299
Cdd:cd08013 228 ASVHASLIK-GGEEPSSYPARCTLTIERRTipgeTDESVLAELtaiLGELAQTVPNFS-YREPRITLSRPPFEVPKEHpF 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1819653059 300 SALVSSAITKVTGLVPELSTTGGTSDARFLSRI-CPVVEFGLCNATMHKLDEAVAVPDLYALADIYEEIVR 369
Cdd:cd08013 306 VQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAgIPSVVFGPSGAGLHAKEEWVDVESIRQLREVLSAVVR 376
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
3-357 |
2.14e-13 |
|
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: 70.66 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 3 DPLALTQRLIACPSVTPA--DAGAMAVIAEALEGLGFAVHRFAAggpPDG--------PIENLFAIR--GESGPHFAFAG 70
Cdd:cd02697 4 EEVRFLQKLVRVPTDTPPgnNAPHAERTAALLQGFGFEAERHPV---PEAevraygmeSITNLIVRRryGDGGRTVALNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 71 HSDVVPPGSGWTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQ----DRGTVSLIITGDEEgpatHGTVALIDW 146
Cdd:cd02697 81 HGDVVPPGDGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESlgapLRGAVELHFTYDEE----FGGELGPGW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 147 MNERGI-RPDLCLVG----EPTSTHrlgdmvkigrRGSVNIWIENAGTQGHVAYPHLARNPVPELVRALAALDALHLDDG 221
Cdd:cd02697 157 LLRQGLtKPDLLIAAgfsyEVVTAH----------NGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNAQYR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 222 NAWFQPSNLEITTVDV----GNSATNVIPAKASARVNIRFNDEHKGAEL---VERVSRTVLAHAP--HAEIKAVISGESF 292
Cdd:cd02697 227 QVSSQVEGITHPYLNVgrieGGTNTNVVPGKVTFKLDRRMIPEENPVEVeaeIRRVIADAAASMPgiSVDIRRLLLANSM 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819653059 293 iTPPGDFSALVSSAITKVTGLVPELSTTGGT---SDARFLSRI-CPVVEFG-----LCNATMHKLDEAVAVPDL 357
Cdd:cd02697 307 -RPLPGNAPLVEAIQTHGEAVFGEPVPAMGTplyTDVRLYAEAgIPGVIYGagprtVLESHAKRADERLQLEDL 379
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
9-164 |
3.41e-13 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 70.24 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 9 QRLIACPSVTPADA----GAMAVI---AEALEGLGFAVHRFAAGGPPDGpiENLFAIRGeSGPH-FAFAGHSDVVPPGSG 80
Cdd:PRK05111 12 RALIATPSISATDPaldqSNRAVIdllAGWFEDLGFNVEIQPVPGTRGK--FNLLASLG-SGEGgLLLAGHTDTVPFDEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 81 -WTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQDRGTVSLII--TGDEEgPATHGTVALIDwmnERGIRPDLC 157
Cdd:PRK05111 89 rWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYIlaTADEE-TSMAGARAFAE---ATAIRPDCA 164
|
....*..
gi 1819653059 158 LVGEPTS 164
Cdd:PRK05111 165 IIGEPTS 171
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
1-339 |
5.69e-13 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 69.02 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 1 MIDPLALTQRLIACPSVTPADAGAMAVIAEALEGLGFAVHRfaaggPPDGPIENLFAirgESGPHFAFAGHSDVVPPGSG 80
Cdd:PRK08652 1 TERAKELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHI-----ESDGEVINIVV---NSKAELFVEVHYDTVPVRAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 81 wtgdpfvPEIRGELLYGRGAVDMKGAIAA--FIAAIARIEQDRGTVSLIITGDEEgpatHGTVALIDWMNERgiRPDLCL 158
Cdd:PRK08652 73 -------FFVDGVYVYGTGACDAKGGVAAilLALEELGKEFEDLNVGIAFVSDEE----EGGRGSALFAERY--RPKMAI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 159 VGEPTSTHrlgdmVKIGRRGSVNIWIENAGTQGHVAYPHLARNPVPELVRALAALDALHLDDGNAWFQPSNLEITTvdvG 238
Cdd:PRK08652 140 VLEPTDLK-----VAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPHIGIQEII---G 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 239 NSATNVIPAKASARVNIRFNDEHKgaelVERVSRTVLAHAPHAEIKAVISGE--SFITPP-GDFSALVSSAItKVTGLVP 315
Cdd:PRK08652 212 GSPEYSIPALCRLRLDARIPPEVE----VEDVLDEIDPILDEYTVKYEYTEIwdGFELDEdEEIVQLLEKAM-KEVGLEP 286
|
330 340
....*....|....*....|....*
gi 1819653059 316 ELSTTGGTSDA-RFLSRICPVVEFG 339
Cdd:PRK08652 287 EFTVMRSWTDAiNFRYNGTKTVVWG 311
|
|
| PRK06915 |
PRK06915 |
peptidase; |
6-163 |
1.09e-12 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 68.95 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 6 ALTQRLIACPSVTPADAGAMAVIAEALEGLGFAV------------HR-FA------AGGPpdgpieNLFAI---RGEsG 63
Cdd:PRK06915 21 KLLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLdiwepsfkklkdHPyFVsprtsfSDSP------NIVATlkgSGG-G 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 64 PHFAFAGHSDVVPPG--SGWTGDPFVPEIRGELLYGRGAVDMKGaiaafiaaiarieqdrGTVSLIIT------------ 129
Cdd:PRK06915 94 KSMILNGHIDVVPEGdvNQWDHHPYSGEVIGGRIYGRGTTDMKG----------------GNVALLLAmealiesgielk 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1819653059 130 GD-------EEGPATHGTVALIdwmnERGIRPDLCLVGEPT 163
Cdd:PRK06915 158 GDvifqsviEEESGGAGTLAAI----LRGYKADGAIIPEPT 194
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
4-363 |
1.20e-12 |
|
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: 68.24 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 4 PLALTQRLIACPSVTPADAGAMAVIAEALEGLG-FAVHRFAaggppdgpiENLFAiRGESGP--HFAFAGHSDVVP-PGS 79
Cdd:cd05647 1 PIELTAALVDIPSVSGNEKPIADEIEAALRTLPhLEVIRDG---------NTVVA-RTERGLasRVILAGHLDTVPvAGN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 80 gwtgdpfVPEIRGE--LLYGRGAVDMKGAIAAFIAAIARIEQDRGTVSL--IITGDEEGPA-----THGTVALIDWmner 150
Cdd:cd05647 71 -------LPSRVEEdgVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLtlIFYDCEEVAAelnglGRLAEEHPEW---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 151 gIRPDLCLVGEPTsthrlGDMVKIGRRGSVNIWIENAGTQGHVAYPHLARNPV----PELVRALAALDALHLDDGNAWFQ 226
Cdd:cd05647 140 -LAADFAVLGEPT-----DGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIhklaPILARLAAYEPRTVNIDGLTYRE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 227 psNLEITTVDvGNSATNVIPAKASARVNIRFNDEHKGAELVERVsRTVLAhapHAEIKAVISGESFITPPGDFSALVSSA 306
Cdd:cd05647 214 --GLNAVFIS-GGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHV-REVFE---GLGYEIEVTDLSPGALPGLDHPVARDL 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1819653059 307 ITKVTGLVpeLSTTGGTSDARFLSRICPVVEFGLCNATM-HKLDEAVAVPDLYALADI 363
Cdd:cd05647 287 IEAVGGKV--RAKYGWTDVARFSALGIPAVNFGPGDPLLaHKRDEQVPVEQITACAAI 342
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
11-358 |
1.95e-11 |
|
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: 65.02 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 11 LIACPSVT--PADAGAMAVIAE----ALEGLGFA-VHRFAAGGPPdgpieNLFA--IRGESGPHFAFAGHSDVVP--PGS 79
Cdd:cd05680 7 LLRIPSVSadPAHKGDVRRAAEwladKLTEAGFEhTEVLPTGGHP-----LVYAewLGAPGAPTVLVYGHYDVQPpdPLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 80 GWTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQDRGT----VSLIITGDEEgpatHGTVALIDWMNERG--IR 153
Cdd:cd05680 82 LWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGAlpvnVKFLIEGEEE----IGSPSLPAFLEENAerLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 154 PDLCLVGEpTSTHRLGD-MVKIGRRG--SVNIWIENAGT----------------------------QGHVAYPHL---- 198
Cdd:cd05680 158 ADVVLVSD-TSMWSPDTpTITYGLRGlaYLEISVTGPNRdlhsgsyggavpnpanalarllaslhdeDGRVAIPGFyddv 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 199 -----------ARNPVPElvRALAALDALHLDDGNA--------WFQPSnLEITTVD---VGNSATNVIPAKASARVNIR 256
Cdd:cd05680 237 rpltdaereawAALPFDE--AAFKASLGVPALGGEAgyttlerlWARPT-LDVNGIWggyQGEGSKTVIPSKAHAKISMR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 257 F---NDEHKGAELVERVSRTVLAHAPHAEIKAVISGESFITPPGDFSAL-VSSAITKVTGLVPELSTTGGT--SDARFLS 330
Cdd:cd05680 314 LvpgQDPDAIADLLEAHLRAHAPPGVTLSVKPLHGGRPYLVPTDHPALQaAERALEEAFGKPPVFVREGGSipIVALFEK 393
|
410 420 430
....*....|....*....|....*....|.
gi 1819653059 331 RI-CPVV--EFGLCNATMHKLDEAVAVPDLY 358
Cdd:cd05680 394 VLgIPTVlmGFGLPDDAIHAPNEKFRLECFH 424
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
70-105 |
6.52e-11 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 63.32 E-value: 6.52e-11
10 20 30
....*....|....*....|....*....|....*.
gi 1819653059 70 GHSDVVPPGSGWTGDPFVPEIRGELLYGRGAVDMKG 105
Cdd:PRK07318 86 GHLDVVPAGDGWDTDPYEPVIKDGKIYARGTSDDKG 121
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
54-175 |
8.34e-11 |
|
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: 60.91 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 54 NLFAIRG--ESGPHFAFAGHSDVVPPGSGWTGDPFVPE--IRGELLYGRGAVDMKGAIAAFIAAIARIEQDR----GTVS 125
Cdd:cd18669 1 NVIARYGggGGGKRVLLGAHIDVVPAGEGDPRDPPFFVdtVEEGRLYGRGALDDKGGVAAALEALKLLKENGfklkGTVV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1819653059 126 LIITGDEEGPATHGTVALIDWMNERGIRPDLCLVGEPTSTHRLGDMVKIG 175
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTP 130
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
52-369 |
2.13e-10 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 61.71 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 52 IEN--LFAIRGESG---PHFAFAGHSDVVPPGSG-WTGDPFVPEIRGELLYGRGAVDMKG--AIAAFIAAIARIEQDRGT 123
Cdd:PRK08554 47 IEKdgYYAVYGEIGegkPKLLFMAHFDVVPVNPEeWNTEPFKLTVKGDKAYGRGSADDKGnvASVMLALKELSKEPLNGK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 124 VSLIITGDEEgpaTHGTVALidWMNER----GIRPDLCLVGEPTSthrlgdMVKIGRR-----GSVNIWIENAGTQG--- 191
Cdd:PRK08554 127 VIFAFTGDEE---IGGAMAM--HIAEKlreeGKLPKYMINADGIG------MKPIIRRrkgfgVTIRVPSEKVKVKGklr 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 192 --------------HVAY--PHLARNPVPELVRALAALDALHLDDGNAWFQ----PSNLEITTVDVGNSATNV------- 244
Cdd:PRK08554 196 eqtfeirtpvvetrHAAYflPGVDTHPLIAASHFLRESNVLAVSLEGKFLKgnvvPGEVTLTYLEPGEGEEVEvdlgltr 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 245 ----------IPAKA--------SARVNI-RFNDEHKGAEL-----------VERVSRTVLAHA-PHAEIKAVISGES-- 291
Cdd:PRK08554 276 llkaivplvrAPIKAekysdygvSITPNVySFAEGKHVLKLdiramsyskedIERTLKEVLEFNlPEAEVEIRTNEKAgy 355
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819653059 292 FITPPGDFSALVSSAITKVTGLVPELSTTGGTSDARFLS-RICPVVEFGLCNATMHKLDEAVAVPDLYALADIYEEIVR 369
Cdd:PRK08554 356 LFTPPDEEIVKVALRVLKELGEDAEPVEGPGASDSRYFTpYGVKAIDFGPKGGNIHGPNEYVEIDSLKKMPEVYKRIAL 434
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
5-158 |
5.62e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 60.40 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSVtpADAGAMAVIAEALEGlgfavhRFAAGGPPDGPIE---------NLFAIRGESGPHFA--FAGHSD 73
Cdd:PRK09133 40 RDLYKELIEINTT--ASTGSTTPAAEAMAA------RLKAAGFADADIEvtgpyprkgNLVARLRGTDPKKPilLLAHMD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 74 VV-PPGSGWTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQD----RGTVSLIITGDEEGPATHGTVALIDwmN 148
Cdd:PRK09133 112 VVeAKREDWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREgfkpKRDIILALTGDEEGTPMNGVAWLAE--N 189
|
170
....*....|.
gi 1819653059 149 ERG-IRPDLCL 158
Cdd:PRK09133 190 HRDlIDAEFAL 200
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
70-105 |
8.14e-10 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 60.08 E-value: 8.14e-10
10 20 30
....*....|....*....|....*....|....*.
gi 1819653059 70 GHSDVVPPGSGWTGDPFVPEIRGELLYGRGAVDMKG 105
Cdd:TIGR01887 74 GHLDVVPAGDGWTSPPFEPTIKDGRIYGRGTLDDKG 109
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
1-196 |
1.90e-09 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 58.67 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 1 MIDPLALT----QRLIACPSVTP----ADAGAMAVIAEALEGLGFAVHRFAAGGPpdgpieNLFAIRGEsgPHFAFAGHS 72
Cdd:PRK08737 1 MTDLLESTldhlQALVSFDTRNPpraiTTGGIFDYLRAQLPGFQVEVIDHGAGAV------SLYAVRGT--PKYLFNVHL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 73 DVVPPGSGWTGDPFVPEIRGELLYGRGAVDMKGAIaafIAAIARIEQDRGTVSLIITGDEEGPATHGTVALIdwmnERGI 152
Cdd:PRK08737 73 DTVPDSPHWSADPHVMRRTDDRVIGLGVCDIKGAA---AALLAAANAGDGDAAFLFSSDEEANDPRCVAAFL----ARGI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1819653059 153 RPDLCLVGEPTsthrLGDMVkIGRRGSVNIWIENAGTQGHVAYP 196
Cdd:PRK08737 146 PYEAVLVAEPT----MSEAV-LAHRGISSVLMRFAGRAGHASGK 184
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
5-105 |
3.44e-09 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 58.13 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSVTPA---DAGAMAVIAEALEGLGFAVHRFAAggPPDGPieNLFAI-RGESGPHFA---FAGHSDV--V 75
Cdd:PRK08596 16 LELLKTLVRFETPAPParnTNEAQEFIAEFLRKLGFSVDKWDV--YPNDP--NVVGVkKGTESDAYKsliINGHMDVaeV 91
|
90 100 110
....*....|....*....|....*....|
gi 1819653059 76 PPGSGWTGDPFVPEIRGELLYGRGAVDMKG 105
Cdd:PRK08596 92 SADEAWETNPFEPTIKDGWLYGRGAADMKG 121
|
|
| dipeptidase |
TIGR01886 |
dipeptidase PepV; This model represents a small clade of dipeptidase enzymes which are members ... |
70-105 |
5.17e-09 |
|
dipeptidase PepV; This model represents a small clade of dipeptidase enzymes which are members of the larger M25 subfamily of metalloproteases. Two characterized enzymes are included in the seed. One, from Lactococcus lactis has been shown to act on a wide range of dipeptides, but not larger peptides. The enzyme from Lactobacillus delbrueckii was originally characterized as a Xaa-His dipeptidase, specifically a carnosinase (beta-Ala-His) by complementation of an E. coli mutant. Further study, including the crystallization of the enzyme, has shown it to also be a non-specific dipeptidase. This group also includes enzymes from Streptococcus and Enterococcus. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 130941 [Multi-domain] Cd Length: 466 Bit Score: 57.59 E-value: 5.17e-09
10 20 30
....*....|....*....|....*....|....*.
gi 1819653059 70 GHSDVVPPGSGWTGDPFVPEIRGELLYGRGAVDMKG 105
Cdd:TIGR01886 85 GHMDVVPAGEGWTRDPFEPEIDEGRIYARGASDDKG 120
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
54-174 |
1.61e-08 |
|
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 53.97 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 54 NLFAIRGES--GPHFAFAGHSDVVPPGSGWTGDPFVPE--IRGELLYGRGAVDMKGAIAAFIAAIARIEQDR----GTVS 125
Cdd:cd03873 1 NLIARLGGGegGKSVALGAHLDVVPAGEGDNRDPPFAEdtEEEGRLYGRGALDDKGGVAAALEALKRLKENGfkpkGTIV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1819653059 126 LIITGDEEGPATHGTVALIDWMNERGIRPDLCLVGEPTSTHRLGDMVKI 174
Cdd:cd03873 81 VAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDATAGPILQKGVVI 129
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
10-105 |
4.01e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 54.91 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 10 RLIACPSV--TPADA----GAMAVIAEALEGLGFA-VHRFAAGG----------PPDGPIENLFAirgesgphfafagHS 72
Cdd:PRK07907 26 ELVRIPSVaaDPFRReevaRSAEWVADLLREAGFDdVRVVSADGapavigtrpaPPGAPTVLLYA-------------HH 92
|
90 100 110
....*....|....*....|....*....|....*
gi 1819653059 73 DVVPPG--SGWTGDPFVPEIRGELLYGRGAVDMKG 105
Cdd:PRK07907 93 DVQPPGdpDAWDSPPFELTERDGRLYGRGAADDKG 127
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
5-105 |
1.10e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 53.54 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSV-TPADAGAM--AVIAEALE-------GLGFAVHRFaaggpPDGPIEnlFAIRGESGPHFAFAGHSDV 74
Cdd:PRK07205 14 VAAIKTLVSYPSVlNEGENGTPfgQAIQDVLEatldlcqGLGFKTYLD-----PKGYYG--YAEIGQGEELLAILCHLDV 86
|
90 100 110
....*....|....*....|....*....|...
gi 1819653059 75 VPPG--SGWTGDPFVPEIRGELLYGRGAVDMKG 105
Cdd:PRK07205 87 VPEGdlSDWQTPPFEAVEKDGCLFGRGTQDDKG 119
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
5-364 |
4.04e-07 |
|
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: 51.33 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSVTPADAGAMAVIAEALEGLGF-AVHRfaaggppDGPIENLFAIRGE-SGPHFAFAGHSDVVPPGsgwt 82
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGLgDVER-------DGRGNVVGRLRGTgGGPALLFSAHLDTVFPG---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 83 GDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIarieQDRGTVSLIITGDEEGPATHGTVALIDwmnERGIRPDLCLVGEP 162
Cdd:cd03896 70 DTPATVRHEGGRIYGPGIGDNKGSLACLLAMA----RAMKEAGAALKGDVVFAANVGEEGLGD---LRGARYLLSAHGAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 163 TSTHRLGD----MVKIGRRGSVNIWIENAGTQGHVAYPHLARNPVPELVRALAALdalhlddgNAWFQPS----NLEITT 234
Cdd:cd03896 143 LDYFVVAEgtdgVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEAL--------YEWAAPYvpktTFAAIR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 235 VDVGNSAtNVIPAKASARVNIRFNDEHKGAELVE----RVSRTVLAHAP-HAEIKAVISGESFITPPGD--FSALVSSAI 307
Cdd:cd03896 215 GGGGTSV-NRIANLCSMYLDIRSNPDAELADVQReveaVVSKLAAKHLRvKARVKPVGDRPGGEAQGTEplVNAAVAAHR 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1819653059 308 TKVTGLVPELSTTggtsDAR-FLSRICPVVEFGLCN-ATMHKLDEAVAVPDLYALADIY 364
Cdd:cd03896 294 EVGGDPRPGSSST----DANpANSLGIPAVTYGLGRgGNAHRGDEYVLKDDMLKGAKAY 348
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
70-105 |
6.27e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 51.01 E-value: 6.27e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1819653059 70 GHSDVVPP-GSGWTGDPFVPEIRGELLYGRGAVDMKG 105
Cdd:PRK07906 72 GHLDVVPAeAADWSVHPFSGEIRDGYVWGRGAVDMKD 108
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
10-133 |
8.00e-07 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 50.80 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 10 RLIACPSVTPADAG----AMAViAEALEGLGFAVHRFAAGGppdGPIenLFA-IRGESGPHFAFAGHSDVVP--PGSGWT 82
Cdd:cd05681 7 DLLKIPSVSAQGRGipetADFL-KEFLRRLGAEVEIFETDG---NPI--VYAeFNSGDAKTLLFYNHYDVQPaePLELWT 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1819653059 83 GDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQDRG----TVSLIITGDEE 133
Cdd:cd05681 81 SDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGelpvNIKFLVEGEEE 135
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
68-317 |
1.80e-06 |
|
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: 49.56 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 68 FAGHSDVVP----PGSGWTGDPFVPEIRGELLYGRGAVDMK----GAIAAFIAAIARIEQDRGTVSLIITGDEEGPATHG 139
Cdd:cd05674 74 LMAHQDVVPvnpeTEDQWTHPPFSGHYDGGYIWGRGALDDKnsliGILEAVELLLKRGFKPRRTIILAFGHDEEVGGERG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 140 TVALIDWMNER-GIRPDLCLVGE------PTSTHRLGDMVKIGRRGSVNIWIENAGTQGHVAYPH--------------L 198
Cdd:cd05674 154 AGAIAELLLERyGVDGLAAILDEggavleGVFLGVPFALPGVAEKGYMDVEITVHTPGGHSSVPPkhtgigilseavaaL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 199 ARNP---------------------VPELVRA--------LAALDALHLDDGNAWFQPSNLEITT---VDVGNS--ATNV 244
Cdd:cd05674 234 EANPfppkltpgnpyygmlqclaehSPLPPRSlksnlwlaSPLLKALLASELLSTSPLTRALLRTtqaVDIINGgvKINA 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819653059 245 IPAKASARVNIRFNDEHKGAELVERVSRTVLAHAPHAEIKAVISGESFITPPGDFSALVS------SAITKVTGLVPEL 317
Cdd:cd05674 314 LPETATATVNHRIAPGSSVEEVLEHVKNLIADIAVKYGLGLSAFGGDVIYSTNGTKLLTSllspepSPVSSTSSPVWQL 392
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
26-369 |
3.29e-06 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 48.86 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 26 AVIAEALEGLGFAVHRFAAggpPDGPIENLFA-IRGESGPHFAFAGHSDVV-PPGSGWTgDPFvpEIRGELLYGRGAVDM 103
Cdd:PRK06133 64 ALLAERLKALGAKVERAPT---PPSAGDMVVAtFKGTGKRRIMLIAHMDTVyLPGMLAK-QPF--RIDGDRAYGPGIADD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 104 KGAIAAFIAAIARIEQ----DRGTVSLIITGDEEgPATHGTVALIdwmNERGIRPDLCLVGEPTsthRLGDMVKIGRRGS 179
Cdd:PRK06133 138 KGGVAVILHALKILQQlgfkDYGTLTVLFNPDEE-TGSPGSRELI---AELAAQHDVVFSCEPG---RAKDALTLATSGI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 180 VNIWIENAGTQGHV-AYPHLARNPVPEL----VRALAALDALHLDDGNaWfqpsnleitTVDVGNSATNVIPAKASARVN 254
Cdd:PRK06133 211 ATALLEVKGKASHAgAAPELGRNALYELahqlLQLRDLGDPAKGTTLN-W---------TVAKAGTNRNVIPASASAQAD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 255 IRFNDEhKGAELVE----RVSRTVLAHAPHAEIKAVISGESFI-TPPGDFSALVSSAITKVTG--LVPELSTTGGTSDAR 327
Cdd:PRK06133 281 VRYLDP-AEFDRLEadlqEKVKNKLVPDTEVTLRFERGRPPLEaNAASRALAEHAQGIYGELGrrLEPIDMGTGGGTDAA 359
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1819653059 328 FLSRI--CPVVE-FGLCNATMHKLDEAV----AVPDLYALADIYEEIVR 369
Cdd:PRK06133 360 FAAGSgkAAVLEgFGLVGFGAHSNDEYIelnsIVPRLYLLTRMIMELSR 408
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
28-105 |
5.84e-06 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 47.88 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 28 IAEALEGLGFAVHRFAAGGPPDGPIenLFAIRGESG--PHFAFAGHSDVVPPGSG-WTG--DPFVPEIRGELLYGRGAVD 102
Cdd:cd05679 37 MRPRFERLGFTVHIHDNPVAGRAPF--LIAERIEDPslPTLLIYGHGDVVPGYEGrWRDgrDPWTVTVWGERWYGRGTAD 114
|
...
gi 1819653059 103 MKG 105
Cdd:cd05679 115 NKG 117
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
68-367 |
8.12e-06 |
|
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: 47.34 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 68 FAGHSDVVPPG--SGWTGDPFVPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQDR---GTVSLIITGDEEGpATHGTVA 142
Cdd:cd05677 76 FYGHYDVIPAGetDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQEGeldNDVVFLIEGEEES-GSPGFKE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 143 LIDWMNERGIRPDLCLVgepTSTHRLGDMV---KIGRRGSVN----IWIENA--------------------------GT 189
Cdd:cd05677 155 VLRKNKELIGDIDWILL---SNSYWLDDNIpclNYGLRGVIHativVSSDKPdlhsgvdggvlreptadlikllsklqDP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 190 QGHVAYPHLaRNPVPELV------------RALAALDALHLDDGNAWFQPSnLEITTVDV-GNSATNVIPAKASARVNIR 256
Cdd:cd05677 232 DGRILIPHF-YDPVKPLTeaerarftaiaeTALIHEDTTVDSLIAKWRKPS-LTVHTVKVsGPGNTTVIPKSASASVSIR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 257 FNDEHKGAELVERVSRTVLA-----HAP-HAEIKAVISGESFI-TPPGDFSALVSSAITKVTGLVPELSTTGGT-SDARF 328
Cdd:cd05677 310 LVPDQDLDVIKQDLTDYIQScfaelKSQnHLDIEVLNEAEPWLgDPDNPAYQILREAVTAAWGVEPLYIREGGSiPTIRF 389
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1819653059 329 LSRI--CPVVEF--GLCNATMHKLDEAVAVPDLYALADIYEEI 367
Cdd:cd05677 390 LEKEfnAPAVQLpcGQSSDNAHLDNERLRIKNLYKMREILSRV 432
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
11-105 |
1.35e-05 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 46.82 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 11 LIACPSVT--PADAG----AMAVIAEALEGLGFAVHRFAAGGPP------DGPienlfairGESGPHFAFAGHSDVVP-- 76
Cdd:PRK09104 26 LLRIPSIStdPAYAAdcrkAADWLVADLASLGFEASVRDTPGHPmvvahhEGP--------TGDAPHVLFYGHYDVQPvd 97
|
90 100 110
....*....|....*....|....*....|....
gi 1819653059 77 PGSGWTGDPFVPEIR-----GELLYGRGAVDMKG 105
Cdd:PRK09104 98 PLDLWESPPFEPRIKetpdgRKVIVARGASDDKG 131
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
24-105 |
1.45e-05 |
|
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: 46.83 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 24 AMAVIAEALEGLGFAVHRFAAGG--PPDGPIENL----FAIRGE--SGPHFAFAGHSDVVPPGS--GWTGDPFV-PEIRG 92
Cdd:cd05676 38 MMEWAAERLEKLGFKVELVDIGTqtLPDGEELPLppvlLGRLGSdpSKKTVLIYGHLDVQPAKLedGWDTDPFElTEKDG 117
|
90
....*....|...
gi 1819653059 93 eLLYGRGAVDMKG 105
Cdd:cd05676 118 -KLYGRGSTDDKG 129
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
24-133 |
1.73e-05 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 46.66 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 24 AMAVIAEALEGLGFA-VHRFAAGGPPDGPIENLFAirgESGPHFAFAGHSDVVP--PGSGWTGDPFVPEIRGELLYGRGA 100
Cdd:PRK08201 42 AAEWLAGALEKAGLEhVEIMETAGHPIVYADWLHA---PGKPTVLIYGHYDVQPvdPLNLWETPPFEPTIRDGKLYARGA 118
|
90 100 110
....*....|....*....|....*....|....*..
gi 1819653059 101 VDMKGAIAAFIAAIARIEQDRGT----VSLIITGDEE 133
Cdd:PRK08201 119 SDDKGQVFMHLKAVEALLKVEGTlpvnVKFCIEGEEE 155
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
231-369 |
1.97e-05 |
|
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: 46.29 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 231 EITTVDVG----NSATNVIPAK----ASARVNIRFNDEHKGAELVERVSRTVLAHAPHAEIKAVISGESFITPPGDFSAL 302
Cdd:cd05683 220 EETTANIGkfqgGTATNIVTDEvnieAEARSLDEEKLDAQVKHMKETFETTAKEKGAHAEVEVETSYPGFKINEDEEVVK 299
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819653059 303 VSSAITKVTGLVPELSTTGGTSDARFLSRI-CPVVEFGLCNATMHKLDEAVAVPDLYALADIYEEIVR 369
Cdd:cd05683 300 LAKRAANNLGLEINTTYSGGGSDANIINGLgIPTVNLGIGYENIHTTNERIPIEDLYDTAVLVVEIIK 367
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
188-322 |
2.00e-05 |
|
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: 46.12 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 188 GTQGHVAYPHLARNPVpelvralAALDALHLDDGNAWFQPS---NLEITTVDVGNSATNVIPAKASARVNIRFNDEHKGA 264
Cdd:cd08018 176 GKQAHGARPHLGINAI-------EAASAIVNAVNAIHLDPNipwSVKMTKLQAGGEATNIIPDKAKFALDLRAQSNEAME 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819653059 265 ELVERVSRTVLAHAPHAEIKAVISGESFI---TPPGDFSALVSSAITKVTG---LVPELSTTGG 322
Cdd:cd08018 249 ELKEKVEHAIEAAAALYGASIEITEKGGMpaaEYDEEAVELMEEAITEVLGeekLAGPCVTPGG 312
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
68-301 |
4.19e-05 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 45.34 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 68 FAGHSDVV-PPGSgwtgdPF--VPEIRGELLYGRGAVDMKGAIAAFIAAIARIEQ----DRGTVSLIITGDEEgPATHGT 140
Cdd:PRK07338 97 LTGHMDTVfPADH-----PFqtLSWLDDGTLNGPGVADMKGGIVVMLAALLAFERsplaDKLGYDVLINPDEE-IGSPAS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 141 VALIDWMNERGirpDLCLVGEPTSTHrlGDMVKiGRRGSVNIWIENAGTQGHVAY-PHLARNPVPELVRALAALDALHLD 219
Cdd:PRK07338 171 APLLAELARGK---HAALTYEPALPD--GTLAG-ARKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAELALALHALNGQ 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 220 DGNAWFQPSNLEittvdvGNSATNVIPAKASARVNIRFNDEHKGAELVERVSRTVLAHAPHAEIKAVISGeSFITPPGDF 299
Cdd:PRK07338 245 RDGVTVNVAKID------GGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHGVSLHLHG-GFGRPPKPI 317
|
..
gi 1819653059 300 SA 301
Cdd:PRK07338 318 DA 319
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
5-105 |
5.85e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 44.91 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 5 LALTQRLIACPSV--TPADAGAMA-----VIAEALEGLGFAVHRFA---AGGPPdgpieNLFAIRGESG--PHFAFAGHS 72
Cdd:PRK07079 20 FADLARRVAYRTEsqNPDRAPALRayltdEIAPALAALGFTCRIVDnpvAGGGP-----FLIAERIEDDalPTVLIYGHG 94
|
90 100 110
....*....|....*....|....*....|....*.
gi 1819653059 73 DVVPPGSG-WTG--DPFVPEIRGELLYGRGAVDMKG 105
Cdd:PRK07079 95 DVVRGYDEqWREglSPWTLTEEGDRWYGRGTADNKG 130
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
71-208 |
1.36e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 43.59 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 71 HSDVVP--PGSGWTGDPFVPEIRGELLYGRGAVDMKGA-IAAFIAAIARIEQDRGTVS--LIITGDEEgpatHGTVALID 145
Cdd:PRK06446 70 HYDVQPvdPLSEWKRDPFSATIENGRIYARGASDNKGTlMARLFAIKHLIDKHKLNVNvkFLYEGEEE----IGSPNLED 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819653059 146 WM--NERGIRPDLCLVGEPTSTHRLGDMVKIGRRG--SVNIWIENAGTQGHVAYPHLARNPVPELVR 208
Cdd:PRK06446 146 FIekNKNKLKADSVIMEGAGLDPKGRPQIVLGVKGllYVELVLRTGTKDLHSSNAPIVRNPAWDLVK 212
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
276-364 |
2.81e-04 |
|
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: 41.64 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 276 AHAPHAEIKAVISGES--------FITPPGDFSALVSSAITKVTGLVPELSTTGGTSDARFL-SRICPVVEFGL-CNATM 345
Cdd:cd03873 102 LLAEDLKVDAAFVIDAtagpilqkGVVIRNPLVDALRKAAREVGGKPQRASVIGGGTDGRLFaELGIPGVTLGPpGDKGA 181
|
90
....*....|....*....
gi 1819653059 346 HKLDEAVAVPDLYALADIY 364
Cdd:cd03873 182 HSPNEFLNLDDLEKATKVY 200
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
188-332 |
3.08e-04 |
|
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: 42.33 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 188 GTQGHVAYPHLARNPVPELVRALAALDALHLDDGNAwFQPSNLEITTVDVGNsATNVIPAKASARVNIRFNDEHKGAELV 267
Cdd:TIGR01891 179 GKGAHAARPHLGRDALDAAAQLVVALQQIVSRNVDP-SRPAVVSVGIIEAGG-APNVIPDKASMSGTVRSLDPEVRDQII 256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819653059 268 ERVSRTV----LAHAPHAEIKAVISGESFITPPGDfSALVSSAITKVTGLVPE----LSTTGGTSDARFLSRI 332
Cdd:TIGR01891 257 DRIERIVegaaAMYGAKVELNYDRGLPAVTNDPAL-TQILKEVARHVVGPENVaedpEVTMGSEDFAYYSQKV 328
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
68-102 |
7.23e-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: 41.55 E-value: 7.23e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1819653059 68 FAGHSDVVPPGSGWTGD--PFVPEIRGELLYGRGAVD 102
Cdd:cd05682 78 LYGHMDKQPPFTGWDEGlgPTKPVIRGDKLYGRGGAD 114
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
188-340 |
1.15e-03 |
|
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: 40.49 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 188 GTQGHVAYPHLARNPVP---ELVralaaldalhlddgNAW----------FQPSNLEITTVDVGnSATNVIPAKASARVN 254
Cdd:COG1473 192 GKGGHAAAPHLGIDPIVaaaQIV--------------TALqtivsrnvdpLDPAVVTVGIIHGG-TAPNVIPDEAELEGT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819653059 255 IRFNDEHKGAELVERVSRTV--LAHAPHAEIKAVISGEsfiTPP----GDFSALVSSAITKVTG---LVPELSTTGGTsD 325
Cdd:COG1473 257 VRTFDPEVRELLEERIERIAegIAAAYGATAEVEYLRG---YPPtvndPELTELAREAAREVLGeenVVDAEPSMGSE-D 332
|
170
....*....|....*
gi 1819653059 326 ARFLSRICPVVEFGL 340
Cdd:COG1473 333 FAYYLQKVPGAFFFL 347
|
|
| |
