|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
2-375 |
0e+00 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 759.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 2 SCPVIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAWRGH-GETLAFAGHTDVVPAGDADRWIN 80
Cdd:PRK13009 1 MSDVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDFGDVKNLWARRGTeGPHLCFAGHTDVVPPGDLEAWTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKNGTVKVVETLMARNERLDYCLV 160
Cdd:PRK13009 81 PPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVLEWLKARGEKIDYCIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 161 GEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNEFFPPTSMQIANVQSGT 240
Cdd:PRK13009 161 GEPTSTERLGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEGNEFFPPTSLQITNIDAGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 241 GSNNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEKYQLRYSVEWWLSGQPFLTGRGKLVDAVVNAIEHYNEIKPQLLT 320
Cdd:PRK13009 241 GATNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDYTLEWTLSGEPFLTPPGKLVDAVVAAIEAVTGITPELST 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489003140 321 NGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRVMEQLVA 375
Cdd:PRK13009 321 SGGTSDARFIADYGAQVVEFGPVNATIHKVNECVSVADLEKLTRIYERILERLLA 375
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
6-370 |
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: 680.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAWRGH-GETLAFAGHTDVVPAGDADRWINPPFE 84
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFGGVKNLWARRGTgGPHLCFAGHTDVVPPGDLEGWSSDPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKNGTVKVVETLMARNERLDYCLVGEPS 164
Cdd:cd03891 81 PTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKIDYCIVGEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 165 STEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNEFFPPTSMQIANVQSGTGSNN 244
Cdd:cd03891 161 SEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLDEGNEFFPPSSLQITNIDVGNGATN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 245 VIPGDMFVQFNFRFSTELTDEMIKSRVIALLEKYQLRYSVEWWLSGQPFLTGRGKLVDAVVNAIEHYNEIKPQLLTNGGT 324
Cdd:cd03891 241 VIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELSTSGGT 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489003140 325 SDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRVM 370
Cdd:cd03891 321 SDARFIASYGCPVVEFGLVNATIHKVNERVSVADLEKLTDIYERIL 366
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
5-373 |
0e+00 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 617.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 5 VIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAWRGHGE-TLAFAGHTDVVPAGDADRWINPPF 83
Cdd:TIGR01246 1 VTELAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGDTKNLWATRGTGEpVLAFAGHTDVVPAGPEEQWSSPPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 84 EPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKNGTVKVVETLMARNERLDYCLVGEP 163
Cdd:TIGR01246 81 EPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVETLMARDELIDYCIVGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 164 SSTEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNEFFPPTSMQIANVQSGTGSN 243
Cdd:TIGR01246 161 SSVKKLGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAIKWDEGNEFFPPTSLQITNIHAGTGAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 244 NVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEKYQLRYSVEWWLSGQPFLTGRGKLVDAVVNAIEHYNEIKPQLLTNGG 323
Cdd:TIGR01246 241 NVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELSTGGG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489003140 324 TSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRVMEQL 373
Cdd:TIGR01246 321 TSDGRFIALMGAEVVEFGPVNATIHKVNECVSIEDLEKLSDVYQDLLENL 370
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
5-375 |
7.60e-122 |
|
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 357.27 E-value: 7.60e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 5 VIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDF-GDTQNFWAWR---GHGETLAFAGHTDVVPAGDADRWIN 80
Cdd:COG0624 14 ALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVpPGRPNLVARRpgdGGGPTLLLYGHLDVVPPGDLELWTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAkNGTVKVVETLmARNERLDYCLV 160
Cdd:COG0624 94 DPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGS-PGARALVEEL-AEGLKADAAIV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 161 GEPSSTevvgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWD-KGNEFFPPTSMQIANVQSG 239
Cdd:COG0624 172 GEPTGV----PTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDgRADPLFGRTTLNVTGIEGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 240 TGSnNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEK--YQLRYSVEWWL-SGQPFLTG-RGKLVDAVVNAIEHYNEIK 315
Cdd:COG0624 248 TAV-NVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAaaPGVEVEVEVLGdGRPPFETPpDSPLVAAARAAIREVTGKE 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489003140 316 PQLLTNGGTSDGRFIAR-MGAQVVELGPVN-ATIHKINECVNAADLQLLARMYQRVMEQLVA 375
Cdd:COG0624 327 PVLSGVGGGTDARFFAEaLGIPTVVFGPGDgAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
7-369 |
1.94e-110 |
|
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: 327.33 E-value: 1.94e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 7 ELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAWRGHGE--TLAFAGHTDVVPAGDADRWINPPFE 84
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVATVGGGDgpVLLLNGHIDTVPPGDGDKWSFPPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASaKNGTVKVVETLMArnERLDYCLVGEPS 164
Cdd:cd08659 81 GRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVG-SDGARALLEAGYA--DRLDALIVGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 165 stevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKG-NEFFPPTSMQIANVQSGTGSn 243
Cdd:cd08659 158 -----GLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPaHPLLGPPTLNVGVINGGTQV- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 244 NVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEKYQLRYSVEWWLSGQP--FLTGRGKLVDAVVNAIEHYNeIKPQLLTN 321
Cdd:cd08659 232 NSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPpfFTDPDHPLVQALQAAARALG-GDPVVRPF 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 489003140 322 GGTSDGRFIARM-GAQVVELGP-VNATIHKINECVNAADLQLLARMYQRV 369
Cdd:cd08659 311 TGTTDASYFAKDlGFPVVVYGPgDLALAHQPDEYVSLEDLLRAAEIYKEI 360
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
62-372 |
5.58e-83 |
|
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: 255.35 E-value: 5.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 62 AFAGHTDVVPAGDADRWinpPFEPTIrDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNhRGRLAFLITSDEEaSAKNGT 141
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEE-GGMGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 142 VKVVETLMARNERLDYCL---VGEPSSTE-VVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNI 217
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFglhIGEPTLLEgGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 218 EWDKGNEFFPP--TSMQIANVQSGTgsnNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEK----YQLRYSVEWWLSGQ 291
Cdd:pfam01546 155 VSRNVDPLDPAvvTVGNITGIPGGV---NVIPGEAELKGDIRLLPGEDLEELEERIREILEAiaaaYGVKVEVEYVEGGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 292 PFLTGRGKLVDAVVNAIEHYNEIKPQLLTNG--GTSDGRFIA-RMGAQVVELGPVNATIHKINECVNAADLQLLARMYQR 368
Cdd:pfam01546 232 PPLVNDSPLVAALREAAKELFGLKVELIVSGsmGGTDAAFFLlGVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLAR 311
|
....
gi 489003140 369 VMEQ 372
Cdd:pfam01546 312 LLLK 315
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
31-371 |
8.48e-51 |
|
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349889 [Multi-domain] Cd Length: 367 Bit Score: 173.93 E-value: 8.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 31 ERLRAIGFTVEPMDFGDTQ--NFWAWRG--HGETLAFAGHTDVVPAgDADRWINPPFEPTIRDGMLFGRGAADMKGSLAA 106
Cdd:cd03894 26 DYLAALGVKSRRVPVPEGGkaNLLATLGpgGEGGLLLSGHTDVVPV-DGQKWSSDPFTLTERDGRLYGRGTCDMKGFLAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 107 MVVAAERFVAQypNHRGRLAFLITSDEEASAKnGTVKVVETLMARNERLDYCLVGEPSSTEVVgdvvkNGRRGSLTCNLT 186
Cdd:cd03894 105 VLAAVPRLLAA--KLRKPLHLAFSYDEEVGCL-GVRHLIAALAARGGRPDAAIVGEPTSLQPV-----VAHKGIASYRIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 187 IHGVQGHVAYPHLADNPVHRAAPMLAELVNI--EWDKGNE---FFPPTS-MQIANVQSGTGSnNVIPGDMFVQFNFRF-- 258
Cdd:cd03894 177 VRGRAAHSSLPPLGVNAIEAAARLIGKLRELadRLAPGLRdppFDPPYPtLNVGLIHGGNAV-NIVPAECEFEFEFRPlp 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 259 --STELTDEMIKSRVIALLEKYQLRYSVEWWLSGQPFLTgrgKLVDAVVNAIEHYNEIKPQLLTNGGTsDGRFIARMGAQ 336
Cdd:cd03894 256 geDPEAIDARLRDYAEALLEFPEAGIEVEPLFEVPGLET---DEDAPLVRLAAALAGDNKVRTVAYGT-EAGLFQRAGIP 331
|
330 340 350
....*....|....*....|....*....|....*.
gi 489003140 337 VVELGPVN-ATIHKINECVNAADLQLLARMYQRVME 371
Cdd:cd03894 332 TVVCGPGSiAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
5-375 |
2.53e-50 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 173.25 E-value: 2.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 5 VIELAQQLIRRPSLSP---DDAGCQALMIERLRAIGFTVEPMDFGDT---------QNFWAWRGHGET-LAFAGHTDVVP 71
Cdd:PRK08651 8 IVEFLKDLIKIPTVNPpgeNYEEIAEFLRDTLEELGFSTEIIEVPNEyvkkhdgprPNLIARRGSGNPhLHFNGHYDVVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 72 AGDADRwINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVaqyPNHRGRLAFLITSDEEaSAKNGTVKVVETLMAr 151
Cdd:PRK08651 88 PGEGWS-VNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLD---PAGDGNIELAIVPDEE-TGGTGTGYLVEEGKV- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 152 neRLDYCLVGEPSSTEVVGdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWD-KGNEFFPPTS 230
Cdd:PRK08651 162 --TPDYVIVGEPSGLDNIC----IGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTiKSKYEYDDER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 231 MQIANVQ------SGTGSNNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLE----KYQLRYSVEWWLSGQPFLTGRG-K 299
Cdd:PRK08651 236 GAKPTVTlggptvEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDevapELGIEVEFEITPFSEAFVTDPDsE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489003140 300 LVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGAQVVELGP-VNATIHKINECVNAADLQLLARMYQRVMEQLVA 375
Cdd:PRK08651 316 LVKALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPgELELAHAPDEYVEVKDVEKAAKVYEEVLKRLAK 392
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
6-352 |
2.56e-50 |
|
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: 172.97 E-value: 2.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 6 IELAQQLIRRPSLSP---DDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAWR--------GHGETLAFAGHTDVVPAGD 74
Cdd:TIGR01910 1 VELLKDLISIPSVNPpggNEETIANYIKDLLREFGFSTDVIEITDDRLKVLGKvvvkepgnGNEKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 75 ADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEaSAKNGTVKVVETLMARNEr 154
Cdd:TIGR01910 81 LELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEE-SGEAGTLYLLQRGYFKDA- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 155 lDYCLVGEPSStevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIE--WDKGNE--FFP-PT 229
Cdd:TIGR01910 159 -DGVLIPEPSG----GDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEehIYARNSygFIPgPI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 230 SMQIANVQSGTGSnNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEK--------YQLRYSVEWwlSGQPFLTGRGKLV 301
Cdd:TIGR01910 234 TFNPGVIKGGDWV-NSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKAlsksdgwlYENEPVVKW--SGPNETPPDSRLV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489003140 302 DAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGAQVVELGP-VNATIHKINE 352
Cdd:TIGR01910 311 KALEAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPgDLETAHQVNE 362
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-370 |
4.91e-41 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349933 [Multi-domain] Cd Length: 355 Bit Score: 147.92 E-value: 4.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 6 IELAQQLIRRPSLSPDDAG---CQALMIERLRAIGFTVE-----PMDFGDTQNFWAWRGhGETLAFAGHTDVVPAGDADR 77
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDNtsaIAAYIKLLLEDLGYPVElheppEEIYGVVSNIVGGRK-GKRLLFNGHYDVVPAGDGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 78 WINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKNGTVKVVETLMARNerlDY 157
Cdd:cd08011 80 WTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYLLEKVRIKP---ND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 158 CLVGEPSSTevvgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEwdkgneffppTSMQIANVQ 237
Cdd:cd08011 157 VLIGEPSGS----DNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELE----------KTVNPGVIK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 238 SGTgSNNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEKY-QLRYSVEWWLSGqPFLTGRGKLVDAVVNAIEHYNEIKP 316
Cdd:cd08011 223 GGV-KVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSIeEVSFEIKSFYSP-TVSNPDSEIVKKTEEAITEVLGIRP 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 489003140 317 QLLTNGGTSDGRFIARMGAQVVELGPVN-ATIHKINECVNAADLQLLARMYQRVM 370
Cdd:cd08011 301 KEVISVGASDARFYRNAGIPAIVYGPGRlGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
56-372 |
6.88e-37 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 137.32 E-value: 6.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 56 GHGE-TLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ-YPNHrGRLAFLITSDE 133
Cdd:PRK08588 56 GSGSpVLALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQgQLLN-GTIRLLATAGE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 134 EasakngtvkvVETLMARN-------ERLDYCLVGEPSstevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNpvhr 206
Cdd:PRK08588 135 E----------VGELGAKQltekgyaDDLDALIIGEPS-----GHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVN---- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 207 AAPMLAELVNIEwdkgNEFFpPTSMQIANVQSGT--------GSN--NVIPGDMFVQFNFRFSTELTDEMIKSRVIALLE 276
Cdd:PRK08588 196 AIDPLLEFYNEQ----KEYF-DSIKKHNPYLGGLthvvtiinGGEqvNSVPDEAELEFNIRTIPEYDNDQVISLLQEIIN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 277 KY------QLrySVEWWLSGQPFLT-GRGKLVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGA--QVVELGP-VNAT 346
Cdd:PRK08588 271 EVnqngaaQL--SLDIYSNHRPVASdKDSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKPdfPVIIFGPgNNLT 348
|
330 340
....*....|....*....|....*.
gi 489003140 347 IHKINECVNAADLQLLARMYQRVMEQ 372
Cdd:PRK08588 349 AHQVDEYVEKDMYLKFIDIYKEIIIQ 374
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-247 |
6.38e-34 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 128.20 E-value: 6.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 5 VIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDfgdtQNFWAWRGHGE----TLAFAGHTDVVPAGDAdrWIN 80
Cdd:cd05651 2 AIELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRKG----NNVWAENGHFDegkpTLLLNSHHDTVKPNAG--WTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQyPNHRGRLAFLITSDEEASAKNGtvkvVETLMARNERLDYCLV 160
Cdd:cd05651 76 DPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSE-GPLNYNLIYAASAEEEISGKNG----IESLLPHLPPLDLAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 161 GEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHlADNPVHRAAPMLAELVNIEWDKGNEFFPPTSMQIANVQSGT 240
Cdd:cd05651 151 GEPTEMQPA-----IAEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDIQWLRDFRFDKVSPLLGPVKMTVTQINAGT 224
|
....*..
gi 489003140 241 gSNNVIP 247
Cdd:cd05651 225 -QHNVVP 230
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
65-257 |
1.13e-33 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 128.77 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 65 GHTDVVPAgDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ---YPNHrgrLAFliTSDEEAsaknGT 141
Cdd:PRK07522 71 GHTDVVPV-DGQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAplrRPLH---LAF--SYDEEV----GC 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 142 VKV---VETLMARNERLDYCLVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNI- 217
Cdd:PRK07522 141 LGVpsmIARLPERGVKPAGCIVGEPTSMRPV-----VGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLa 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489003140 218 -----EWDKGNEFFPP-TSMQIANVQSGTgSNNVIPGDMFVQFNFR 257
Cdd:PRK07522 216 drlaaPGPFDALFDPPySTLQTGTIQGGT-ALNIVPAECEFDFEFR 260
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
5-375 |
1.37e-33 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 129.11 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 5 VIELAQQLIRRPSLSPDDAG---CQALMIERLRAIGFTVE-------PmdfGDTQNFWAW--------RGHGETLAFAGH 66
Cdd:PRK13013 16 LVALTQDLIRIPTLNPPGRAyreICEFLAARLAPRGFEVEliraegaP---GDSETYPRWnlvarrqgARDGDCVHFNSH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 67 TDVVPAGDAdrWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKNGTVKVVE 146
Cdd:PRK13013 93 HDVVEVGHG--WTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGGVAYLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 147 TLMARNERLDYCLVGEPSSTevvgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAElvnIEwdkgNEFF 226
Cdd:PRK13013 171 QGRFSPDRVQHVIIPEPLNK----DRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAE---IE----ERLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 227 P-----PTSMQIA--NVQSGTGSNNVIPGDMFVQ-------------------FNFRFSTELTDEMIKSRVIALLEKYQ- 279
Cdd:PRK13013 240 PllatrRTAMPVVpeGARQSTLNINSIHGGEPEQdpdytglpapcvadrcrivIDRRFLIEEDLDEVKAEITALLERLKr 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 280 ----LRYSVEWWLSGQPFLTGRGK-LVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGA--QVVELGP-VNATIHKIN 351
Cdd:PRK13013 320 arpgFAYEIRDLFEVLPTMTDRDApVVRSVAAAIERVLGRQADYVVSPGTYDQKHIDRIGKlkNCIAYGPgILDLAHQPD 399
|
410 420
....*....|....*....|....
gi 489003140 352 ECVNAADLQLLARMYQRVMEQLVA 375
Cdd:PRK13013 400 EWVGIADMVDSAKVMALVLADLLA 423
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
5-214 |
1.49e-33 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 128.52 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 5 VIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFT-VEPMDFGdtqNFWAWRGHGETL-AFAGHTDVVPAGDADRWINPP 82
Cdd:PRK13004 17 MTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFDkVEIDPMG---NVLGYIGHGKKLiAFDAHIDTVGIGDIKNWDFDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 83 FEPTIRDGMLFGRGAADMKGSLAAMVVAAErfvaqypnhrgrlaflITSDEEASAKnGTVKVVETLM------------- 149
Cdd:PRK13004 94 FEGEEDDGRIYGRGTSDQKGGMASMVYAAK----------------IIKDLGLDDE-YTLYVTGTVQeedcdglcwryii 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489003140 150 -ARNERLDYCLVGEPSSTEvvgdvVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAEL 214
Cdd:PRK13004 157 eEDKIKPDFVVITEPTDLN-----IYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNEL 217
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
5-373 |
3.40e-32 |
|
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: 123.62 E-value: 3.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 5 VIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGdtqNFWAWRGHGE-TLAFAGHTDVVPAgdadrwinpPF 83
Cdd:cd05653 3 AVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEAG---NAVGGAGSGPpDVLLLGHIDTVPG---------EI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 84 EPTIRDGMLFGRGAADMKGSLAAMVVAAerfVAQYPNHRGRLAFLITSDEEASAKnGTvkvvETLMARNERLDYCLVGEP 163
Cdd:cd05653 71 PVRVEGGVLYGRGAVDAKGPLAAMILAA---SALNEELGARVVVAGLVDEEGSSK-GA----RELVRRGPRPDYIIIGEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 164 SSTEvvGDVVknGRRGSLTCNLTIHGVQGHVAyphladNPVHRAAPMLAE-LVNI-EWDKGNE--FFPPTSMQIANVQSG 239
Cdd:cd05653 143 SGWD--GITL--GYRGSLLVKIRCEGRSGHSS------SPERNAAEDLIKkWLEVkKWAEGYNvgGRDFDSVVPTLIKGG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 240 TgSNNVIPGDMFVQFNFRFSTELTDEmiksRVIALLEKYQLRYSVEWWLSGQPFLTG-RGKLVDAVVNAIEHYNeIKPQL 318
Cdd:cd05653 213 E-SSNGLPQRAEATIDLRLPPRLSPE----EAIALATALLPTCELEFIDDTEPVKVSkNNPLARAFRRAIRKQG-GKPRL 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489003140 319 LTNGGTSDGRFIA-RMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRVMEQL 373
Cdd:cd05653 287 KRKTGTSDMNVLApLWTVPIVAYGPGDSTLdHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
5-365 |
8.59e-31 |
|
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: 120.39 E-value: 8.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 5 VIELAQQLIRRPSLSPDDAGCQA---LMIERLRAIGFTVE---PMDFGDTQnFWAWRGHGET-LAFAGHTDVV-PAGDAD 76
Cdd:cd03885 1 MLDLLERLVNIESGTYDKEGVDRvaeLLAEELEALGFTVErrpLGEFGDHL-IATFKGTGGKrVLLIGHMDTVfPEGTLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 77 RWinpPFepTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKnGTVKVVETLmARNErlD 156
Cdd:cd03885 80 FR---PF--TVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSP-GSRELIEEE-AKGA--D 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 157 YCLVGEPSSTevvGDVVKNGRRGSLTCNLTIHGVQGHV-AYPHLADNPVHRAAPMLAELVNIewdkgNEFFPPTSMQIAN 235
Cdd:cd03885 151 YVLVFEPARA---DGNLVTARKGIGRFRLTVKGRAAHAgNAPEKGRSAIYELAHQVLALHAL-----TDPEKGTTVNVGV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 236 VQSGTGSnNVIPGDMFVQFNFRFSTELTDEMIKSRVIALL-EKYQLRYSVEwwLSGQ----PFLTGRG--KLVDAVVNAi 308
Cdd:cd03885 223 ISGGTRV-NVVPDHAEAQVDVRFATAEEADRVEEALRAIVaTTLVPGTSVE--LTGGlnrpPMEETPAsrRLLARAQEI- 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489003140 309 ehYNEIKPQLLT--NGGTSDGRFIARMGAQVVE-LGPVNATIHKINECVNAADL----QLLARM 365
Cdd:cd03885 299 --AAELGLTLDWeaTGGGSDANFTAALGVPTLDgLGPVGGGAHTEDEYLELDSLvpriKLLARL 360
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-271 |
5.30e-30 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 117.76 E-value: 5.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 5 VIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVE--PMDFGDTQNFWAWRGHGET--LAFAGHTDVVPagdadrwin 80
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEkqPVENKDRFNVYAYPGSSRQprVLLTSHIDTVP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 81 P--PFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKnGTVKVVEtlmARNERLDYC 158
Cdd:cd05652 72 PfiPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGD-GMKAFND---LGLNTWDAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 159 LVGEPssTEvvGDVVKnGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKgNEFFPPTSMQIANVQS 238
Cdd:cd05652 148 IFGEP--TE--LKLAS-GHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPS-SELLGPTTLNIGRISG 221
|
250 260 270
....*....|....*....|....*....|....*
gi 489003140 239 GTGSnNVIPGDMFVQFNFRFSTELTD--EMIKSRV 271
Cdd:cd05652 222 GVAA-NVVPAAAEASVAIRLAAGPPEvkDIVKEAV 255
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-364 |
3.00e-29 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 116.64 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 7 ELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVE-----PMDFGDTQNFW--------------AWRGHGET---LAFA 64
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDrweidVEKLKHHPGFSpvavdyagapnvvgTHRPRGETgrsLILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 65 GHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEaSAKNGTvkv 144
Cdd:cd03895 81 GHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEE-CTGNGA--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 145 VETLMaRNERLDYCLVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAEL--VNIEW--- 219
Cdd:cd03895 157 LAALM-RGYRADAALIPEPTELKLV-----RAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALqeLEREWnar 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 220 ---DKGNEFFP-PTSMQIANVQSGTGSNNVIPG---DMFVQFNFRFSTELTDEMIKSRVIALLEKY----QLRYSVEWW- 287
Cdd:cd03895 231 kksHPHFSDHPhPINFNIGKIEGGDWPSSVPAWcvlDCRIGIYPGESPEEARREIEECVADAAATDpwlsNHPPEVEWNg 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489003140 288 LSGQPF-LTGRGKLVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGA-QVVELGPVNATIHKINECVNAADLQLLAR 364
Cdd:cd03895 311 FQAEGYvLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGDiPALCYGPGSRDAHGFDESVDLESLRKITK 389
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-370 |
3.25e-29 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 116.40 E-value: 3.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 5 VIELAQQLIRRPSLSPDDAG------CQALMiERLRAIGF-TVEPMDFGDTQNFW-------AWRGHGETLAFAGHTDVV 70
Cdd:cd05650 3 IIELERDLIRIPAVNPESGGegekekADYLE-KKLREYGFyTLERYDAPDERGIIrpnivakIPGGNDKTLWIISHLDTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 71 PAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ--YPNHRGRLAFLitSDEEASAKNGTVKVVETL 148
Cdd:cd05650 82 PPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNgiTPKYNFGLLFV--ADEEDGSEYGIQYLLNKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 149 -MARNErlDYCLVgePSSTEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNE--- 224
Cdd:cd05650 160 dLFKKD--DLIIV--PDFGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFALELDELLHEKFDEkdd 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 225 -FFPPTSMQIANVQSGTGSN-NVIPGDMFVQFNFRF--STELTD--EMIKSRVIALLEKYQLRYSVEWWLSGQ--PFLTG 296
Cdd:cd05650 236 lFNPPYSTFEPTKKEANVPNvNTIPGYDVFYFDCRVlpTYKLDEvlKFVNKIISDFENSYGAGITYEIVQKEQapPATPE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489003140 297 RGKLVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRVM 370
Cdd:cd05650 316 DSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYIRISHIVKDAKVFAEML 389
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
5-370 |
1.57e-26 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 108.30 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 5 VIELAQQLIRRPSLSpDDAGCQALMIER-LRAIGfTVEPMDFGDTQNFWAWRGHGETLAFAGHTDVVPAGDadrwiNPPf 83
Cdd:cd05647 1 PIELTAALVDIPSVS-GNEKPIADEIEAaLRTLP-HLEVIRDGNTVVARTERGLASRVILAGHLDTVPVAG-----NLP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 84 ePTIR-DGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRgrLAFLITSDEE-ASAKNGTVKVVEtlmARNERL--DYCL 159
Cdd:cd05647 73 -SRVEeDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHD--LTLIFYDCEEvAAELNGLGRLAE---EHPEWLaaDFAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 160 VGEPSSTEVVGdvvknGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAEL-------VNIEwdkGNEFFPPTSmq 232
Cdd:cd05647 147 LGEPTDGTIEG-----GCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLaayeprtVNID---GLTYREGLN-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 233 iANVQSGTGSNNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEKYQLRYSVEwWLSG-------QPFLTGrgkLVDAVv 305
Cdd:cd05647 217 -AVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEIEVT-DLSPgalpgldHPVARD---LIEAV- 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489003140 306 naiehYNEIKPQLltnGGTSDGRFiARMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRVM 370
Cdd:cd05647 291 -----GGKVRAKY---GWTDVARF-SALGIPAVNFGPGDPLLaHKRDEQVPVEQITACAAILRRWL 347
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
6-221 |
1.88e-26 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 109.32 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVE--PMDFGDTQNF-----WAW------------RGHGET---LAF 63
Cdd:PRK06837 23 VAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDrwSIDPDDLKSHpgagpVEIdysgapnvvgtyRPAGKTgrsLIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 64 AGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVA--AERFVAQYPNHRgrlAFLITSDEEASAKNGT 141
Cdd:PRK06837 103 QGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFAldALRAAGLAPAAR---VHFQSVIEEESTGNGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 142 VKvveTLMaRNERLDYCLVGEPSSTEVVGDVVkngrrGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAEL--VNIEW 219
Cdd:PRK06837 180 LS---TLQ-RGYRADACLIPEPTGEKLVRAQV-----GVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALreLEAEW 250
|
..
gi 489003140 220 DK 221
Cdd:PRK06837 251 NA 252
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
56-373 |
1.30e-25 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 105.64 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 56 GHGETLaFAGHTDVVPAGdadrwinppFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFvaqypNHRG-RLAFLITSDEE 134
Cdd:PRK00466 59 GEGDIL-LASHVDTVPGY---------IEPKIEGEVIYGRGAVDAKGPLISMIIAAWLL-----NEKGiKVMVSGLADEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 135 asaknGTVKVVETLMARNERLDYCLVGEPSSTEvvgDVVKnGRRGSLTCNLTIHGVQGHvayphlADNPVHRAAPMLAEL 214
Cdd:PRK00466 124 -----STSIGAKELVSKGFNFKHIIVGEPSNGT---DIVV-EYRGSIQLDIMCEGTPEH------SSSAKSNLIVDISKK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 215 VnIEWDKGNEFFPPTSMQIANVQSGTgSNNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEKYQLRySVEwwlSGQPFL 294
Cdd:PRK00466 189 I-IEVYKQPENYDKPSIVPTIIRAGE-SYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQECGLK-IVD---ETPPVK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 295 TG-RGKLVDAVVNAIEHYNeIKPQLLTNGGTSDGRFIARMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRVMEQ 372
Cdd:PRK00466 263 VSiNNPVVKALMRALLKQN-IKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLeHTNQEKITLDEIYIAVKTYMLAIEE 341
|
.
gi 489003140 373 L 373
Cdd:PRK00466 342 L 342
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
5-370 |
1.36e-25 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 106.47 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 5 VIELAQQLIRRPSLSPDDAG------CQALMiERLRAIGFT-VEPMDFGDTQNFWAWR---------GHGE-TLAFAGHT 67
Cdd:PRK13983 7 MIELLSELIAIPAVNPDFGGegekekAEYLE-SLLKEYGFDeVERYDAPDPRVIEGVRpnivakipgGDGKrTLWIISHM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 68 DVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ--YPNHRGRLAFLitSDEEASAKNGtvkvV 145
Cdd:PRK13983 86 DVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLgiRPKYNLGLAFV--SDEETGSKYG----I 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 146 ETLMARNERL----DYCLV---GEPSstevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNpVHRAAPMLA----EL 214
Cdd:PRK13983 160 QYLLKKHPELfkkdDLILVpdaGNPD-----GSFIEIAEKSILWLKFTVKGKQCHASTPENGIN-AHRAAADFAleldEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 215 VNIEWDKGNEFF-PPTS-----MQIANVQsgtgSNNVIPGDMFVQFNFRF--STELTD--EMIKSRVIALLEKYQLRYSV 284
Cdd:PRK13983 234 LHEKFNAKDPLFdPPYStfeptKKEANVD----NINTIPGRDVFYFDCRVlpDYDLDEvlKDIKEIADEFEEEYGVKIEV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 285 EWWLSGQ--PFLTGRGKLVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLL 362
Cdd:PRK13983 310 EIVQREQapPPTPPDSEIVKKLKRAIKEVRGIEPKVGGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYAKISNLIED 389
|
....*...
gi 489003140 363 ARMYQRVM 370
Cdd:PRK13983 390 AKVFALLL 397
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
175-282 |
2.10e-25 |
|
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: 98.96 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 175 NGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNeFFPPTSMQIANVQSGTgSNNVIPGDMFVQF 254
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGF-DFPRTTLNITGIEGGT-ATNVIPAEAEAKF 78
|
90 100
....*....|....*....|....*...
gi 489003140 255 NFRFSTELTDEMIKSRVIALLEKYQLRY 282
Cdd:pfam07687 79 DIRLLPGEDLEELLEEIEAILEKELPEG 106
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
8-369 |
3.49e-25 |
|
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: 105.90 E-value: 3.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 8 LAQQLIRRPSLSPDDAGCQA-----LMIERLRAIGFTVEPMDF----GDTQNFWAWRGHGET---LAFAGHTDVVPAgDA 75
Cdd:cd05675 3 LLQELIRIDTTNSGDGTGSEtraaeVLAARLAEAGIQTEIFVVeshpGRANLVARIGGTDPSagpLLLLGHIDVVPA-DA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 76 DRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKNGTVKVVETLMARNERL 155
Cdd:cd05675 82 SDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDNHPELFDGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 156 DYCL--VGEPSSTEVVGDV---VKNGRRGSLTCNLTIHGVQGHVAYPHlADNPVHRAAPMLAELVNIEW----DKGNEFF 226
Cdd:cd05675 162 TFALneGGGGSLPVGKGRRlypIQVAEKGIAWMKLTVRGRAGHGSRPT-DDNAITRLAEALRRLGAHNFpvrlTDETAYF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 227 ------------------PPTSMQIANVQSGTG--------------------SNNVIPGDMFVQFNFRFSTELTDEMIK 268
Cdd:cd05675 241 aqmaelaggeggalmltaVPVLDPALAKLGPSApllnamlrntasptmldagyATNVLPGRATAEVDCRILPGQSEEEVL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 269 SRVIALLEKYqlRYSVEW-WLSGQPFLTGRGKLVDAVVNAIEHYN---EIKPQLLTngGTSDGRFIARMGAQVVELGPVN 344
Cdd:cd05675 321 DTLDKLLGDP--DVSVEAvHLEPATESPLDSPLVDAMEAAVQAVDpgaPVVPYMSP--GGTDAKYFRRLGIPGYGFAPLF 396
|
410 420 430
....*....|....*....|....*....|...
gi 489003140 345 AT--------IHKINECVNAADLQLLARMYQRV 369
Cdd:cd05675 397 LPpeldytglFHGVDERVPVESLYFGVRFLDRL 429
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-366 |
6.03e-25 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 104.43 E-value: 6.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGF---TVEPMDfgdtqNFWAWRGHGET-LAFAGHTDVVPAGDADRWINP 81
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGFdevEIDPMG-----NVIGYIGGGKKkILFDGHIDTVGIGNIDNWKFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 82 PFEPTIRDGMLFGRGAADMKGSLAAMVVAaerfvAQYPNHRGRLAFlitSDEEASAknGTV--KVVETLMAR------NE 153
Cdd:cd05649 76 PYEGYETDGKIYGRGTSDQKGGLASMVYA-----AKIMKDLGLRDF---AYTILVA--GTVqeEDCDGVCWQyiskadKI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 154 RLDYCLVGEPSSTEvvgdvVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKG-NEFFPPTSMQ 232
Cdd:cd05649 146 KPDFVVSGEPTDGN-----IYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFPeAPFLGRGTLT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 233 IANVQSGTGSNNVIPGDMFVQFNFRFSTELTDEMI--KSRVIALLEKYQLRYSVEWWLSGQPFLTG-------------- 296
Cdd:cd05649 221 VTDIFSTSPSRCAVPDSCRISIDRRLTVGETWEGCleEIRALPAVKKYGDDVAVSMYNYDRPSYTGevyeseryfptwll 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489003140 297 --RGKLVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIA-RMGAQVVELGP-VNATIHKINECVNAADLQLLARMY 366
Cdd:cd05649 301 peDHELVKALLEAYKALFGARPLIDKWTFSTNGVSIMgRAGIPCIGFGPgAENQAHAPNEYTWKEDLVRCAAGY 374
|
|
| PRK06915 |
PRK06915 |
peptidase; |
6-193 |
5.31e-24 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 102.46 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTV---EP---------------MDFGDTQNF---WAWRGHGETLAFA 64
Cdd:PRK06915 20 VKLLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLdiwEPsfkklkdhpyfvsprTSFSDSPNIvatLKGSGGGKSMILN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 65 GHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEaSAKNGTVKV 144
Cdd:PRK06915 100 GHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEE-SGGAGTLAA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489003140 145 VEtlmaRNERLDYCLVGEPSSTEVvgdVVKngRRGSLTCNLTIHGVQGH 193
Cdd:PRK06915 179 IL----RGYKADGAIIPEPTNMKF---FPK--QQGSMWFRLHVKGKAAH 218
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
50-176 |
9.34e-24 |
|
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: 97.12 E-value: 9.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 50 NFWAWRGHGE---TLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLA 126
Cdd:cd18669 1 NVIARYGGGGggkRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489003140 127 FLITSDEEASAKNGTVKVVETLMARNERLDYCLVGEPSSTEVVGDVVKNG 176
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTP 130
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
33-359 |
1.35e-23 |
|
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: 101.25 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 33 LRAIGFTVEPMDFGDTQNF-WAWRGHGE---TLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMV 108
Cdd:cd03893 34 LRRLGFTVEIVDTSNGAPVvFAEFPGAPgapTVLLYGHYDVQPAGDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 109 VAaerfVAQYPNHRGRLA----FLITSDEEAsaknGTVKVVETLMARNERL--DYCLVGEPSSTEVVGDVVKNGRRGSLT 182
Cdd:cd03893 114 AA----LRALMQQGGDLPvnvkFIIEGEEES----GSPSLDQLVEAHRDLLaaDAIVISDSTWVGQEQPTLTYGLRGNAN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 183 CNLTIHGVQGHV---AYPHLADNPVHRAAPMLAELVNiewDKGN----------------------------EFFPPTSM 231
Cdd:cd03893 186 FDVEVKGLDHDLhsgLYGGVVPDPMTALAQLLASLRD---ETGRilvpglydavrelpeeefrldagvleevEIIGGTTG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 232 QIA---------NV------QSGTGSNNVIPGDMfvqfNFRFSTELTDEMIKSRVIALLEK-------YQLRYSVEWWLS 289
Cdd:cd03893 263 SVAerlwtrpalTVlgidggFPGEGSKTVIPPRA----RAKISIRLVPGQDPEEASRLLEAhlekhapSGAKVTVSYVEG 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489003140 290 GQPFLTG-RGKLVDAVVNAIEHYNEIKPQLLTNGGT--SDGRFIARMGAQVVELGPVNAT--IHKINECVNAADL 359
Cdd:cd03893 339 GMPWRSDpSDPAYQAAKDALRTAYGVEPPLTREGGSipFISVLQEFPQAPVLLIGVGDPDdnAHSPNESLRLGNY 413
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
6-287 |
1.07e-22 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 97.52 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAwRGHGEtLAFAGHTDVVPagdadrwinPPFEP 85
Cdd:PRK08652 5 KELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIESDGEVINIVV-NSKAE-LFVEVHYDTVP---------VRAEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 86 TIRDGMLFGRGAADMKGSLAAMVVAAERFvaQYPNHRGRLAFLITSDEEASAKnGTVKVVETLMARnerldYCLVGEPSS 165
Cdd:PRK08652 74 FVDGVYVYGTGACDAKGGVAAILLALEEL--GKEFEDLNVGIAFVSDEEEGGR-GSALFAERYRPK-----MAIVLEPTD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 166 TEVvgdvvKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNEFFPPTSMQIAnvqSGTGSNNV 245
Cdd:PRK08652 146 LKV-----AIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPHIGIQEI---IGGSPEYS 217
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489003140 246 IPGDMFVQFNFRFSTELTDEMIKSRVIALLEKYQLRYS-VEWW 287
Cdd:PRK08652 218 IPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEyTEIW 260
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
54-373 |
2.45e-22 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 98.09 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 54 WRGHGETLA---FAGHTDVVPA--GDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ--YPNHRGRLA 126
Cdd:PRK08262 104 WKGSDPSLKpivLMAHQDVVPVapGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQgfQPRRTIYLA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 127 FliTSDEEASAKnGTVKVVETLMARNERLDyCLVGEpsSTEVVGDVVKN----------GRRGSLTCNLTIHGVQGHVAY 196
Cdd:PRK08262 184 F--GHDEEVGGL-GARAIAELLKERGVRLA-FVLDE--GGAITEGVLPGvkkpvaligvAEKGYATLELTARATGGHSSM 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 197 P--------------HLADNP------------VHRAAP--------MLAELVNIEWDKGNEFF--PPTSmqiANVQSGT 240
Cdd:PRK08262 258 PprqtaigrlaraltRLEDNPlpmrlrgpvaemFDTLAPemsfaqrvVLANLWLFEPLLLRVLAksPETA---AMLRTTT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 241 ------GSN--NVIPGDMFVQFNFRF----STELTDEMIKsRVIAllekyQLRYSVEW-----------WLSGQPFltgr 297
Cdd:PRK08262 335 aptmlkGSPkdNVLPQRATATVNFRIlpgdSVESVLAHVR-RAVA-----DDRVEIEVlggnsepspvsSTDSAAY---- 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 298 gKLVDAVVNAIEHYNEIKPQLLTnGGTsDGRFIARMGAQVVELGPVNAT------IHKINECVNAADLQLLARMYQRVME 371
Cdd:PRK08262 405 -KLLAATIREVFPDVVVAPYLVV-GAT-DSRHYSGISDNVYRFSPLRLSpedlarFHGTNERISVANYARMIRFYYRLIE 481
|
..
gi 489003140 372 QL 373
Cdd:PRK08262 482 NA 483
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
5-366 |
2.77e-21 |
|
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: 94.62 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 5 VIELAQQLIRRPS-LSPDDAGC-------QAL--MIERLRAIGFTVEPMDfgdtqNFWA---WRGHGETLAFAGHTDVVP 71
Cdd:cd03888 10 ILEDLKELVAIPSvRDEATEGApfgegprKALdkFLDLAKRLGFKTKNID-----NYAGyaeYGEGEEVLGILGHLDVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 72 AGDAdrWINPPFEPTIRDGMLFGRGAADMKG----SLAAMVVAAE---------RFV----------------------- 115
Cdd:cd03888 85 AGEG--WTTDPFKPVIKDGKLYGRGTIDDKGptiaALYALKILKDlglplkkkiRLIfgtdeetgwkciehyfeheeypd 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 116 ------AQYP---NHRGRLAFLITSDEeasaKNGTVKVVETL---MARNERLDYC-LVGEPSSTEVVGDVVKNGRRGSLT 182
Cdd:cd03888 163 fgftpdAEFPvinGEKGIVTVDLTFKI----DDDKGYRLISIkggEATNMVPDKAeAVIPGKDKEELALSAATDLKGNIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 183 CN-----LTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKG-----NEFFPPTS------MQIANVQSG-----TG 241
Cdd:cd03888 239 IDdggveLTVTGKSAHASAPEKGVNAITLLAKFLAELNKDGNDKDfikflAKNLHEDYngkklgINFEDEVMGeltlnPG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 242 SNNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEKYQLRYSVEwwLSGQPFLTGR-GKLVDAVVNAIEHYNEIKPQLLT 320
Cdd:cd03888 319 IITLDDGKLELGLNVRYPVGTSAEDIIKQIEEALEKYGVEVEGH--KHQKPLYVPKdSPLVKTLLKVYEEQTGKEGEPVA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 489003140 321 NGGTSDGRFIARMgaqvVELGP----VNATIHKINECVNAADLQLLARMY 366
Cdd:cd03888 397 IGGGTYARELPNG----VAFGPefpgQKDTMHQANEFIPIDDLIKALAIY 442
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
1-197 |
5.01e-21 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 92.71 E-value: 5.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 1 MSCPVIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGdtqNFWAWRGHG-ETLAFAGHTDVVPaGDAdrwi 79
Cdd:PRK04443 4 SALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREAWVDEAG---NARGPAGDGpPLVLLLGHIDTVP-GDI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 80 npPFEptIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYpnhRGRLAFLITSDEEASAKNGTVKVVETlmarnERLDYCL 159
Cdd:PRK04443 76 --PVR--VEDGVLWGRGSVDAKGPLAAFAAAAARLEALV---RARVSFVGAVEEEAPSSGGARLVADR-----ERPDAVI 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 489003140 160 VGEPSSTevvgDVVKNGRRGSLTCNLTIHGVQGHVAYP 197
Cdd:PRK04443 144 IGEPSGW----DGITLGYKGRLLVTYVATSESFHSAGP 177
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
10-257 |
1.64e-20 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 91.42 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 10 QQLIRRPSLSPDDAGCQALMIERLRAI--GFTVEPMDFGD-TQNFWAWRGHGETLaFAGHTDVVPagDADRWINPPFEPT 86
Cdd:PRK08737 13 QALVSFDTRNPPRAITTGGIFDYLRAQlpGFQVEVIDHGAgAVSLYAVRGTPKYL-FNVHLDTVP--DSPHWSADPHVMR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 87 IRDGMLFGRGAADMKGSLAAMVVAAERFVAQYpnhrgrlAFLITSDEEAsaknGTVKVVETLMARNERLDYCLVGEPSST 166
Cdd:PRK08737 90 RTDDRVIGLGVCDIKGAAAALLAAANAGDGDA-------AFLFSSDEEA----NDPRCVAAFLARGIPYEAVLVAEPTMS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 167 EVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPH-LADNPVHRAAPMLAELVNIEWDKGNEFFPPTS---MQIANVQSGTGS 242
Cdd:PRK08737 159 EAV-----LAHRGISSVLMRFAGRAGHASGKQdPSASALHQAMRWGGQALDHVESLAHARFGGLTglrFNIGRVEGGIKA 233
|
250
....*....|....*
gi 489003140 243 NNVIPGdMFVQFNFR 257
Cdd:PRK08737 234 NMIAPA-AELRFGFR 247
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
12-215 |
4.61e-20 |
|
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: 90.83 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 12 LIRRPSLS------PDDAGCQALMIERLRAIGF-TVE-------PMDFGDtqnfWAWRGHGETLAFAGHTDVVPAGDADR 77
Cdd:cd05680 7 LLRIPSVSadpahkGDVRRAAEWLADKLTEAGFeHTEvlptgghPLVYAE----WLGAPGAPTVLVYGHYDVQPPDPLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 78 WINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQypnhRGRLA----FLITSDEEASAKNgtvkvVETLMARN- 152
Cdd:cd05680 83 WTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAV----EGALPvnvkFLIEGEEEIGSPS-----LPAFLEENa 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 153 ERL--DYCLVGEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQ-----GHvaYPHLADNPVHRAAPMLAELV 215
Cdd:cd05680 154 ERLaaDVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNrdlhsGS--YGGAVPNPANALARLLASLH 221
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
6-277 |
1.87e-19 |
|
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: 89.32 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 6 IELAQQLIRRPSLSPDDAG---CQALMIERLRAIGFTVE-------PMDFGDTQNfwawrGHGETLAFAGHTDVVPAGDA 75
Cdd:cd05681 2 LEDLRDLLKIPSVSAQGRGipeTADFLKEFLRRLGAEVEifetdgnPIVYAEFNS-----GDAKTLLFYNHYDVQPAEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 76 DRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKNgtvkvVETLMARNERL 155
Cdd:cd05681 77 ELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPN-----LEKFVAEHADL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 156 ---DYCL-----VGEPSSTEVVGdvvknGRRGSLTCNLTIHG--VQGHVAYPHLADNPVHRAAPMLAELVN--------- 216
Cdd:cd05681 152 lkaDGCIwegggKNPKGRPQISL-----GVKGIVYVELRVKTadFDLHSSYGAIVENPAWRLVQALNSLRDedgrvlipg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 217 ----IEWDKGNE-----------------------------------FFPPTsMQIANVQSG---TGSNNVIPGDMFVQF 254
Cdd:cd05681 227 fyddVRPLSEAEralidtydfdpeelrktyglkrplqvegkdplralFTEPT-CNINGIYSGytgEGSKTILPSEAFAKL 305
|
330 340
....*....|....*....|...
gi 489003140 255 NFRFSTELTDEMIKSRVIALLEK 277
Cdd:cd05681 306 DFRLVPDQDPAKILSLLRKHLDK 328
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
58-175 |
1.98e-19 |
|
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: 85.17 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 58 GETLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASA 137
Cdd:cd03873 12 GKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGS 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489003140 138 KNGTVKVVETLMARNERLDYCLVGEPS--STEVVGDVVKN 175
Cdd:cd03873 92 GGGKGLLSKFLLAEDLKVDAAFVIDATagPILQKGVVIRN 131
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
6-170 |
2.78e-19 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 88.56 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 6 IELAQQLIRRPSLSP---DDAGCQALMIERLRAIGFTVEPMDF--GDTQNFWAWRGHGET----LAFAGHTDVVPAGDAD 76
Cdd:PRK08596 16 LELLKTLVRFETPAPparNTNEAQEFIAEFLRKLGFSVDKWDVypNDPNVVGVKKGTESDayksLIINGHMDVAEVSADE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 77 RWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEAsAKNGTVKVVEtlmaRNERLD 156
Cdd:PRK08596 96 AWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEV-GEAGTLQCCE----RGYDAD 170
|
170
....*....|....
gi 489003140 157 YCLVGEPSSTEVVG 170
Cdd:PRK08596 171 FAVVVDTSDLHMQG 184
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
56-372 |
5.09e-19 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 87.53 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 56 GHGETLAFAGHTDVVpagDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPnhRGRLAFLITSDEEa 135
Cdd:cd08013 66 GGGKSLMLNGHIDTV---TLDGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGL--RGDVILAAVADEE- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 136 SAKNGTvkvvETLMARNERLDYCLVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAEL- 214
Cdd:cd08013 140 DASLGT----QEVLAAGWRADAAIVTEPTNLQII-----HAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALe 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 215 ---VNIEWDKGNEFFPPTSMQIANVQSGTGSNNViPGDMFVQFNFRFSTELTDEMIKSRVIALLE---------KYQLRY 282
Cdd:cd08013 211 eyqQELPERPVDPLLGRASVHASLIKGGEEPSSY-PARCTLTIERRTIPGETDESVLAELTAILGelaqtvpnfSYREPR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 283 SVewwLSGQPF-LTGRGKLVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQL 361
Cdd:cd08013 290 IT---LSRPPFeVPKEHPFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGAGLHAKEEWVDVESIRQ 366
|
330
....*....|.
gi 489003140 362 LARMYQRVMEQ 372
Cdd:cd08013 367 LREVLSAVVRE 377
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
4-165 |
1.57e-18 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 86.03 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 4 PVIELAQQLIRRPSLS---PD-DAGCQALmIERL----RAIGFTVEPM---DFGDTQNFWAWRGHGET-LAFAGHTDVVP 71
Cdd:PRK05111 6 SFIEMYRALIATPSISatdPAlDQSNRAV-IDLLagwfEDLGFNVEIQpvpGTRGKFNLLASLGSGEGgLLLAGHTDTVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 72 AgDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHrgRLAFLITSDEEaSAKNGTVKVVEtlmAR 151
Cdd:PRK05111 85 F-DEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKK--PLYILATADEE-TSMAGARAFAE---AT 157
|
170
....*....|....
gi 489003140 152 NERLDYCLVGEPSS 165
Cdd:PRK05111 158 AIRPDCAIIGEPTS 171
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
54-229 |
7.97e-18 |
|
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: 84.61 E-value: 7.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 54 WRGHGETLA---FAGHTDVVPA--GDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ--YPNHRGRLA 126
Cdd:cd05674 62 WEGSDPSLKpllLMAHQDVVPVnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRgfKPRRTIILA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 127 FliTSDEEASAKNGTVKVVETLMAR-NERLDYCLVGEPS---STEVVGD---VVKNGRRGSLTCNLTIHGVQGHVAYPhl 199
Cdd:cd05674 142 F--GHDEEVGGERGAGAIAELLLERyGVDGLAAILDEGGavlEGVFLGVpfaLPGVAEKGYMDVEITVHTPGGHSSVP-- 217
|
170 180 190
....*....|....*....|....*....|.
gi 489003140 200 adnPVHRAAPMLAELV-NIEwdkgNEFFPPT 229
Cdd:cd05674 218 ---PKHTGIGILSEAVaALE----ANPFPPK 241
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
65-219 |
1.38e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 83.75 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 65 GHTDVVPAgDADRWINPPFEPTIRDGMLFGRGAADMKGsLAAMVVAAERFVAQypnhRGR-------LAFLitSDEEASA 137
Cdd:PRK07906 72 GHLDVVPA-EAADWSVHPFSGEIRDGYVWGRGAVDMKD-MDAMMLAVVRHLAR----TGRrpprdlvFAFV--ADEEAGG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 138 KNGTVKVVETlmaRNERLDYClvgepssTEVVGDV---------------VKNGRRGSLTCNLTIHGVQGHVAYPHlADN 202
Cdd:PRK07906 144 TYGAHWLVDN---HPELFEGV-------TEAISEVggfsltvpgrdrlylIETAEKGLAWMRLTARGRAGHGSMVN-DDN 212
|
170
....*....|....*..
gi 489003140 203 PVHRAAPMLAELVNIEW 219
Cdd:PRK07906 213 AVTRLAEAVARIGRHRW 229
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
4-373 |
1.14e-16 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 80.61 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 4 PVIELAQQLIRRPSL--SPDDAGCQALMIERLRAIGFTVEPMDF--GDTQNFWAWRGHGETLA---FAGHTDVVPAGDaD 76
Cdd:TIGR01880 10 IAVTRFREYLRINTVqpNPDYAACVDFLIKQADELGLARKTIEFvpGKPVVVLTWPGSNPELPsilLNSHTDVVPVFR-E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 77 RWINPPFEPTI-RDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKNGTVKVVETLMARNERL 155
Cdd:TIGR01880 89 HWTHPPFSAFKdEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEKFAKTDEFKALNL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 156 DYCL-VGEPSSTEVVgdVVKNGRRGSLTCNLTIHGVQGHVA--YPHLADNPVHRAAPMLAELVNIEWD--KGNEFFPP-- 228
Cdd:TIGR01880 169 GFALdEGLASPDDVY--RVFYAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRRFRESQFQllQSNPDLAIgd 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 229 -TSMQIANVQSGTGSnNVIPGDMFVQFNFRFSTELTDEMIKSRViallekyqlrysVEWW-------------LSGQPFL 294
Cdd:TIGR01880 247 vTSVNLTKLKGGVQS-NVIPSEAEAGFDIRLAPSVDFEEMENRL------------DEWCadagegvtyefsqHSGKPLV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 295 T---GRGKLVDAVVNAIEHYN-EIKPQLLTngGTSDGRFIARMGAQVVELGPVNAT---IHKINECVNAADLQLLARMYQ 367
Cdd:TIGR01880 314 TphdDSNPWWVAFKDAVKEMGcTFKPEILP--GSTDSRYIRAAGVPALGFSPMNNTpvlLHDHNEFLNEAVFLRGIEIYQ 391
|
....*.
gi 489003140 368 RVMEQL 373
Cdd:TIGR01880 392 TLISAL 397
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
29-134 |
1.05e-15 |
|
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: 78.19 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 29 MIERLRAIGFTVEpmDFGDTQNFWAWRGHGETLAFAGHTDVVPAGDAdrWINPPFEPTIRDGMLFGRGAADMKG----SL 104
Cdd:TIGR01887 40 FLEIAKRDGFTTE--NVDNYAGYIEYGQGEEVLGILGHLDVVPAGDG--WTSPPFEPTIKDGRIYGRGTLDDKGptiaAY 115
|
90 100 110
....*....|....*....|....*....|
gi 489003140 105 AAMVVAAERFVAqyPNHRGRlaFLITSDEE 134
Cdd:TIGR01887 116 YAMKILKELGLK--LKKKIR--FIFGTDEE 141
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
6-134 |
3.30e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 76.66 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 6 IELAQQLIRRPS-LSPDDAGC---QAL------MIERLRAIGFTVepmdFGDTQNFW--AWRGHG-ETLAFAGHTDVVPA 72
Cdd:PRK07205 14 VAAIKTLVSYPSvLNEGENGTpfgQAIqdvleaTLDLCQGLGFKT----YLDPKGYYgyAEIGQGeELLAILCHLDVVPE 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489003140 73 GDADRWINPPFEPTIRDGMLFGRGAADMKG-SLAAMvVAAERFVAQYPNHRGRLAFLITSDEE 134
Cdd:PRK07205 90 GDLSDWQTPPFEAVEKDGCLFGRGTQDDKGpSMAAL-YAVKALLDAGVQFNKRIRFIFGTDEE 151
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
27-208 |
3.96e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 76.58 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 27 ALMIERLRAIGF-----TVEPmDFGDTQNFWA-WRGHGET--LAFAGHTDVVPAGDADrWINPPFEPTIRDGMLFGRGAA 98
Cdd:PRK09133 63 EAMAARLKAAGFadadiEVTG-PYPRKGNLVArLRGTDPKkpILLLAHMDVVEAKRED-WTRDPFKLVEENGYFYGRGTS 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 99 DMKgSLAAMVVAA------ERFVaqyPNHRGRLAFliTSDEEASAKNGTVKVVETL-------MARNE----RLDYclVG 161
Cdd:PRK09133 141 DDK-ADAAIWVATlirlkrEGFK---PKRDIILAL--TGDEEGTPMNGVAWLAENHrdlidaeFALNEggggTLDE--DG 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489003140 162 EPSSTEVVGdvvknGRRGSLTCNLTIHGVQGHVAYPhLADNPVHRAA 208
Cdd:PRK09133 213 KPVLLTVQA-----GEKTYADFRLEVTNPGGHSSRP-TKDNAIYRLA 253
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
11-113 |
3.66e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 73.40 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 11 QLIRRPSLSPD-------DAGCQALmIERLRAIGF-TVEPMDFGDTQNFWAWR----GHGETLAFAgHTDVVPAGDADRW 78
Cdd:PRK07907 26 ELVRIPSVAADpfrreevARSAEWV-ADLLREAGFdDVRVVSADGAPAVIGTRpappGAPTVLLYA-HHDVQPPGDPDAW 103
|
90 100 110
....*....|....*....|....*....|....*
gi 489003140 79 INPPFEPTIRDGMLFGRGAADMKGSLaAMVVAAER 113
Cdd:PRK07907 104 DSPPFELTERDGRLYGRGAADDKGGI-AMHLAALR 137
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
61-374 |
4.36e-14 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 73.27 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 61 LAFAGHTDVVPAGdADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQypNHRGRLAFLITSDEEASAKNG 140
Cdd:PRK08554 66 LLFMAHFDVVPVN-PEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKE--PLNGKVIFAFTGDEEIGGAMA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 141 tVKVVETLMARNERLDYCLVGEPSSTEVV-------GDVVK--------NGRRGSLTCNLTIHGVQG-HVAY-------- 196
Cdd:PRK08554 143 -MHIAEKLREEGKLPKYMINADGIGMKPIirrrkgfGVTIRvpsekvkvKGKLREQTFEIRTPVVETrHAAYflpgvdth 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 197 PHLADNPVHRAAPMLAELVNIEWDKGNEFfpPTSMQIANVQSGTGSN------------NVIP----------------- 247
Cdd:PRK08554 222 PLIAASHFLRESNVLAVSLEGKFLKGNVV--PGEVTLTYLEPGEGEEvevdlgltrllkAIVPlvrapikaekysdygvs 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 248 ----------GDMFVQFNFRFSTELTDEMikSRVIALLEKYQLRySVEWWL-----SGQPFLTGRGKLVDAVVNAIEHYN 312
Cdd:PRK08554 300 itpnvysfaeGKHVLKLDIRAMSYSKEDI--ERTLKEVLEFNLP-EAEVEIrtnekAGYLFTPPDEEIVKVALRVLKELG 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489003140 313 EiKPQLLTNGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRVMEQLV 374
Cdd:PRK08554 377 E-DAEPVEGPGASDSRYFTPYGVKAIDFGPKGGNIHGPNEYVEIDSLKKMPEVYKRIALRLL 437
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
58-160 |
7.70e-14 |
|
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: 72.38 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 58 GETLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKG-SLAAMVVAAERFVAQYPNHrgRLAFLITSDEEAS 136
Cdd:cd05677 71 RKRILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGpLLAAIYAVAELFQEGELDN--DVVFLIEGEEESG 148
|
90 100
....*....|....*....|....
gi 489003140 137 AKnGTVKVVETLMARNERLDYCLV 160
Cdd:cd05677 149 SP-GFKEVLRKNKELIGDIDWILL 171
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
59-106 |
1.79e-13 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 71.41 E-value: 1.79e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489003140 59 ETLAFAGHTDVVPAGDAdrWINPPFEPTIRDGMLFGRGAADMKG-SLAA 106
Cdd:PRK07318 80 EVLGILGHLDVVPAGDG--WDTDPYEPVIKDGKIYARGTSDDKGpTMAA 126
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
10-214 |
4.04e-13 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 70.16 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 10 QQLIRRPSLSP------DDAGCQALMIERLRAIGFT-VEPMDFGDTQNFWAWRGHGE---TLAFAGHTDVVPAGDADRWI 79
Cdd:PRK08201 21 KEFLRIPSISAlsehkeDVRKAAEWLAGALEKAGLEhVEIMETAGHPIVYADWLHAPgkpTVLIYGHYDVQPVDPLNLWE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 80 NPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQypnhRGRL----AFLITSDEEASAKNgtvkvVETLMARN-ER 154
Cdd:PRK08201 101 TPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKV----EGTLpvnvKFCIEGEEEIGSPN-----LDSFVEEEkDK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489003140 155 L--DYCLVGEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQGHV---AYPHLADNPVHRAAPMLAEL 214
Cdd:PRK08201 172 LaaDVVLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLhsgLYGGAVPNALHALVQLLASL 236
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
63-352 |
4.30e-12 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 66.91 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 63 FAGHTDVV-PAGDadrwinpPFE--PTIRDGMLFGRGAADMKGSLAAMVVAAERFvAQYPnHRGRLAF--LITSDEE--- 134
Cdd:PRK07338 97 LTGHMDTVfPADH-------PFQtlSWLDDGTLNGPGVADMKGGIVVMLAALLAF-ERSP-LADKLGYdvLINPDEEigs 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 135 -ASAkngtvKVVETLMARNerlDYCLVGEPSSTEvvGDVVKNgRRGSLTCNLTIHGVQGHVAY-PHLADNPVHRAAPMLA 212
Cdd:PRK07338 168 pASA-----PLLAELARGK---HAALTYEPALPD--GTLAGA-RKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAELAL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 213 ELvniewDKGNEFFPPTSMQIANVQSGtGSNNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEKYQLRYSVEWWLSGQ- 291
Cdd:PRK07338 237 AL-----HALNGQRDGVTVNVAKIDGG-GPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHGVSLHLHGGf 310
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489003140 292 -----PFLTGRGKLVDAVVNAIEHYN-EIKPQllTNGGTSDGRFIARMGAQVVE-LGPVNATIHKINE 352
Cdd:PRK07338 311 grppkPIDAAQQRLFEAVQACGAALGlTIDWK--DSGGVCDGNNLAAAGLPVVDtLGVRGGNIHSEDE 376
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
29-114 |
4.36e-12 |
|
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.
Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 67.24 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 29 MIERLRAIGFTVEPMDFGDTQNFWAWRGH------GE--------TLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFG 94
Cdd:cd05676 42 AAERLEKLGFKVELVDIGTQTLPDGEELPlppvllGRlgsdpskkTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYG 121
|
90 100
....*....|....*....|
gi 489003140 95 RGAADMKGSLAAMVVAAERF 114
Cdd:cd05676 122 RGSTDDKGPVLGWLNAIEAY 141
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
10-374 |
1.01e-11 |
|
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: 65.65 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 10 QQLIRRPSLSP--DDAGCQALMIERLRAIGFTVE--PMDFGDTQ--------NFWAWRGHGE---TLAFAGHTDVVPAGD 74
Cdd:cd02697 10 QKLVRVPTDTPpgNNAPHAERTAALLQGFGFEAErhPVPEAEVRaygmesitNLIVRRRYGDggrTVALNAHGDVVPPGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 75 AdrWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKNGTVKVVETLMARNer 154
Cdd:cd02697 90 G--WTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGELGPGWLLRQGLTKP-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 155 lDYcLVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELvnieWDKGNEFFPPTS---- 230
Cdd:cd02697 166 -DL-LIAAGFSYEVV-----TAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNAL----YALNAQYRQVSSqveg 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 231 -----MQIANVQSGTGSnNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEKYQ-----LRYSVEWWLSGQPF--LTGRG 298
Cdd:cd02697 235 ithpyLNVGRIEGGTNT-NVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAasmpgISVDIRRLLLANSMrpLPGNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 299 KLVDAVVNaieHYNEIKPQLLTNGGT---SDGRFIARMGAQVVELGPVNATI-----HKINECVNAADLQLLARMYQRVM 370
Cdd:cd02697 314 PLVEAIQT---HGEAVFGEPVPAMGTplyTDVRLYAEAGIPGVIYGAGPRTVleshaKRADERLQLEDLRRATKVIARSL 390
|
....
gi 489003140 371 EQLV 374
Cdd:cd02697 391 RDLL 394
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
56-352 |
1.89e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 62.08 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 56 GHGETLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGrLAFLITSDEEA 135
Cdd:PRK06446 60 GAKKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKHKLNVN-VKFLYEGEEEI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 136 SAKNgtvkvVETLMARNERL---DYCLV-GEPSSTEVVGDVVKnGRRGSLTCNLTIHGVQG--HVAYPHLADNPVHRAAP 209
Cdd:PRK06446 139 GSPN-----LEDFIEKNKNKlkaDSVIMeGAGLDPKGRPQIVL-GVKGLLYVELVLRTGTKdlHSSNAPIVRNPAWDLVK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 210 MLAELVN-------------IEW---------------------------DKGNE--------FFPPTSmQIANVQS--- 238
Cdd:PRK06446 213 LLSTLVDgegrvlipgfyddVRElteeerellkkydidveelrkalgfkeLKYSDrekiaealLTEPTC-NIDGFYSgyt 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 239 GTGSNNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLEKYQLRYSVEWWLSGQPFLTG-RGKLVDAVVNAIEHYNEIKPQ 317
Cdd:PRK06446 292 GKGSKTIVPSRAFAKLDFRLVPNQDPYKIFELLKKHLQKVGFNGEIIVHGFEYPVRTSvNSKVVKAMIESAKRVYGTEPV 371
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 489003140 318 LLTNG-GTSD-GRFIARMG----AQVVELGPVNATIHKINE 352
Cdd:PRK06446 372 VIPNSaGTQPmGLFVYKLGirdiVSAIGVGGYYSNAHAPNE 412
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
11-365 |
2.10e-10 |
|
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: 61.70 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 11 QLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWA------WRG---HGETLAFAGHTDVVPAGDadrwINP 81
Cdd:cd05683 11 ELVQIDSETLHEKEISKVLKKKFENLGLSVIEDDAGKTTGGGAgnlictLKAdkeEVPKILFTSHMDTVTPGI----NVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 82 PfePTIRDGMLFGRG----AADMKGSLAAMVVAAERFVAQYPNHrGRLAFLITSDEEAS---AKNgtvkvvetlmARNER 154
Cdd:cd05683 87 P--PQIADGYIYSDGttilGADDKAGIAAILEAIRVIKEKNIPH-GQIQFVITVGEESGlvgAKA----------LDPEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 155 LD----YCLVGEpsstevvGDVvkngrrGSLTC--------NLTIHGVQGHVA-YPHLADNPVHRAAPMLAelvNIEWDK 221
Cdd:cd05683 154 IDadygYALDSE-------GDV------GTIIVgaptqdkiNAKIYGKTAHAGtSPEKGISAINIAAKAIS---NMKLGR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 222 GNEFfppTSMQIANVQSGTGSNnVIPGDMFVQFNFRfstELTDEMIKSRV-------IALLEKYQLRYSVEWWLSGQPF- 293
Cdd:cd05683 218 IDEE---TTANIGKFQGGTATN-IVTDEVNIEAEAR---SLDEEKLDAQVkhmketfETTAKEKGAHAEVEVETSYPGFk 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489003140 294 LTGRGKLVDAVVNAIEHYnEIKPQLLTNGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARM 365
Cdd:cd05683 291 INEDEEVVKLAKRAANNL-GLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAVL 361
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
6-308 |
2.19e-10 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 61.34 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGF-TVEPMDFGDTQNFWAWRGHGETLAFAGHTDVVPAGDAdrwinpPFE 84
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGLgDVERDGRGNVVGRLRGTGGGPALLFSAHLDTVFPGDT------PAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKNGTVKVVetLMARNERLDYCLVGEPS 164
Cdd:cd03896 75 VRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEGLGDLRGARYL--LSAHGARLDYFVVAEGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 165 stevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDkgneFFPPTSMQIANVQSGTgSNN 244
Cdd:cd03896 153 -----DGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAP----YVPKTTFAAIRGGGGT-SVN 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489003140 245 VIPGDMFVQFNFRF--STELTDemIKSRVIALLEKYQLRYS-----VEWWLSGQPFLT-GRGKLVDAVVNAI 308
Cdd:cd03896 223 RIANLCSMYLDIRSnpDAELAD--VQREVEAVVSKLAAKHLrvkarVKPVGDRPGGEAqGTEPLVNAAVAAH 292
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
11-160 |
2.38e-10 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 61.84 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 11 QLIRRPSLSPDDA---GCQA---LMIERLRAIGFTVE-------PMDFGDTQnfwAWRGHGETLAFAGHTDVVPAGDADR 77
Cdd:PRK09104 25 ALLRIPSISTDPAyaaDCRKaadWLVADLASLGFEASvrdtpghPMVVAHHE---GPTGDAPHVLFYGHYDVQPVDPLDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 78 WINPPFEPTIRDG-----MLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKNgtvkVVETLMARN 152
Cdd:PRK09104 102 WESPPFEPRIKETpdgrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEESGSPS----LVPFLEANA 177
|
170
....*....|
gi 489003140 153 ERL--DYCLV 160
Cdd:PRK09104 178 EELkaDVALV 187
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
4-369 |
2.58e-09 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 58.49 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 4 PVIELAQQLIRRPSLSPDDAGCQ---ALMIERLRAIGFTVEPMD----FGDtqNFWA-WRGHGE-TLAFAGHTDVV-PAG 73
Cdd:PRK06133 38 AYLDTLKELVSIESGSGDAEGLKqvaALLAERLKALGAKVERAPtppsAGD--MVVAtFKGTGKrRIMLIAHMDTVyLPG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 74 DADRwinPPFEptIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKnGTVKVVETLMARNe 153
Cdd:PRK06133 116 MLAK---QPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGSP-GSRELIAELAAQH- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 154 rlDYCLVGEPSSTEvvgDVVKNGRRGSLTCNLTIHGVQGHV-AYPHLADNPVHRAAPMLAELVniewDKGNeffPPTSMQ 232
Cdd:PRK06133 189 --DVVFSCEPGRAK---DALTLATSGIATALLEVKGKASHAgAAPELGRNALYELAHQLLQLR----DLGD---PAKGTT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 233 IANVQSGTGSN-NVIPGDMFVQFNFRFS-TELTD-------EMIKSRVIALLEkYQLRYSVewwlsGQPFL--TGRGKLV 301
Cdd:PRK06133 257 LNWTVAKAGTNrNVIPASASAQADVRYLdPAEFDrleadlqEKVKNKLVPDTE-VTLRFER-----GRPPLeaNAASRAL 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489003140 302 DAVVNAIehYNEI----KPQLLTNGGTSDGRFIARMG-AQVVE-LGPVNATIHKINECVN----AADLQLLARMYQRV 369
Cdd:PRK06133 331 AEHAQGI--YGELgrrlEPIDMGTGGGTDAAFAAGSGkAAVLEgFGLVGFGAHSNDEYIElnsiVPRLYLLTRMIMEL 406
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
4-357 |
7.31e-09 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 56.90 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 4 PVIELAQQLIRRPSL--SPDDAGCQALMIERLRAIGFTVEPMDFgDTQNFWA---WRGHGETLA---FAGHTDVVPAGDa 75
Cdd:cd05646 3 PAVTRFREYLRINTVhpNPDYDACVEFLKRQADELGLPVRVIEV-VPGKPVVvltWEGSNPELPsilLNSHTDVVPVFE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 76 DRWINPPFEPTI-RDGMLFGRGAADMKGSLAAMVVAAERFVAQypNHRGRLAFLIT--SDEEASAKNGTVKVVETLMARN 152
Cdd:cd05646 81 EKWTHDPFSAHKdEDGNIYARGAQDMKCVGIQYLEAIRRLKAS--GFKPKRTIHLSfvPDEEIGGHDGMEKFVKTEEFKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 153 ERLDYCL-VGEPSSTEVVgdVVKNGRRGSLTCNLTIHGVQGHVA--YPHLADNPVHRAAPMLAELVNIEWD--KGNEFFP 227
Cdd:cd05646 159 LNVGFALdEGLASPTEEY--RVFYGERSPWWVVITAPGTPGHGSklLENTAGEKLRKVIESIMEFRESQKQrlKSNPNLT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 228 P---TSMQIANVQSGTgSNNVIPGDMFVQFNFRFsTELTD-----EMIKSRVIALLEKYQLRYSVEWWLSGQPFLTGRGK 299
Cdd:cd05646 237 LgdvTTVNLTMLKGGV-QMNVVPSEAEAGFDLRI-PPTVDleefeKQIDEWCAEAGRGVTYEFEQKSPEKDPTSLDDSNP 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489003140 300 LVDAVVNAIEHYN-EIKPQLLTngGTSDGRFIARMGAQVVELGPVNAT---IHKINECVNAA 357
Cdd:cd05646 315 WWAAFKKAVKEMGlKLKPEIFP--AATDSRYIRALGIPALGFSPMNNTpilLHDHNEFLNED 374
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
44-322 |
1.21e-08 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 56.40 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 44 DFGDTQNFWA-WRGHGE---TLAFAGHTDVVPAGDADRWINPPFEP-----TIRDGML--------------FGRGAADM 100
Cdd:COG4187 61 DPLGRKNVTAlVKGKGEskkTVILISHFDVVDVEDYGSLKPLAFDPeelteALKEIKLpedvrkdlesgewlFGRGTMDM 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 101 KGSLAAMVVAAERFvAQYPNHRGRLAFLITSDEEA-SAknGTVKVVETL--MARNERLDY--CLVGEPSSTEVVGDvvkN 175
Cdd:COG4187 141 KAGLALHLALLEEA-SENEEFPGNLLLLAVPDEEVnSA--GMRAAVPLLaeLKEKYGLEYklAINSEPSFPKYPGD---E 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 176 GRR---GS----LTCNLtIHGVQGHVAYPHLADNPVHraapMLAELVN-IEW-----DK-GNEFF-PPTSMQIA------ 234
Cdd:COG4187 215 TRYiytGSigklMPGFY-CYGKETHVGEPFSGLNANL----LASELTReLELnpdfcEEvGGEVTpPPVSLKQKdlkeey 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 235 NVQsgtgsnnvIPGDMFVQFN-FRFST---ELTDEMIKSRVIAL---LEKYQLRYSVEWWLSGQPFLTGRGK-------- 299
Cdd:COG4187 290 SVQ--------TPHRAVAYFNvLTLERspkEILEKLKKIAEEAAekiLEHYKEQYEKYCKLTGEPFVPLPWKvkvltyee 361
|
330 340
....*....|....*....|....*...
gi 489003140 300 LVDAVVNA-----IEHYNEIKPQLLTNG 322
Cdd:COG4187 362 LYEEAVKKygedfVEAIEEIAEKLNNGE 389
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
56-249 |
6.21e-08 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 54.00 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 56 GHGETLAFAG-HTDVVPAgDADRWINPPFEPTIRDGMLFGRGAADMKGSLaAMVVAAERFVAQY--PNHRGRLAFLITSd 132
Cdd:cd08012 75 VDGKTVSFVGsHMDVVTA-NPETWEFDPFSLSIDGDKLYGRGTTDCLGHV-ALVTELFRQLATEkpALKRTVVAVFIAN- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 133 EEASAKNGTvkVVETLMARNErLDYCLVGEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLA 212
Cdd:cd08012 152 EENSEIPGV--GVDALVKSGL-LDNLKSGPLYWVDSADSQPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVMEALA 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489003140 213 ElvnIEWDKGNEFFP-----------PTSMQIANVQSGTGSNNVIPGD 249
Cdd:cd08012 229 E---IQKRFYIDFPPhpkeevygfatPSTMKPTQWSYPGGSINQIPGE 273
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
105-286 |
3.62e-07 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 51.45 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 105 AAMVVAAERFVAQYPNHRGRLAFLITSDEEASAknGTVKVVETLMARNERLDYCLvGEPSSTEV-VGDVVknGRRGSLTC 183
Cdd:cd03886 95 AMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPG--GAKAMIEEGVLENPGVDAAF-GLHVWPGLpVGTVG--VRSGALMA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 184 -----NLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIewdKGNEFFPPTS--MQIANVQSGTGsNNVIPGDMFVQFNF 256
Cdd:cd03886 170 sadefEITVKGKGGHGASPHLGVDPIVAAAQIVLALQTV---VSRELDPLEPavVTVGKFHAGTA-FNVIPDTAVLEGTI 245
|
170 180 190
....*....|....*....|....*....|....
gi 489003140 257 R-FSTELTD---EMIKSRVIALLEKYQLRYSVEW 286
Cdd:cd03886 246 RtFDPEVREaleARIKRLAEGIAAAYGATVELEY 279
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
105-271 |
2.78e-06 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349914 [Multi-domain] Cd Length: 399 Bit Score: 48.87 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 105 AAMVVAAERFVAQYPNHRGRLAFLITSDEEASAknGTVKVVET-LMARNERLDYCL----VGEPSSTevVGdvVKNGRRG 179
Cdd:cd05664 105 AALLGAARLLVEAKDAWSGTLIAVFQPAEETGG--GAQAMVDDgLYDKIPKPDVVLaqhvMPGPAGT--VG--TRPGRFL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 180 SLTCNL--TIHGVQGHVAYPHLADNPVHRAAPMLAELVNIewdKGNEFFP--PTSMQIANVQSGTgSNNVIPGDMFVQFN 255
Cdd:cd05664 179 SAADSLdiTIFGRGGHGSMPHLTIDPVVMAASIVTRLQTI---VSREVDPqeFAVVTVGSIQAGS-AENIIPDEAELKLN 254
|
170
....*....|....*.
gi 489003140 256 FRFSTELTDEMIKSRV 271
Cdd:cd05664 255 VRTFDPEVREKVLNAI 270
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
180-286 |
7.42e-06 |
|
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: 47.28 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 180 SLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNeffpPTSMQIANVQSGTGSNNVIPGDMFVQFNFRFS 259
Cdd:cd08018 167 STFLEGTIKGKQAHGARPHLGINAIEAASAIVNAVNAIHLDPNI----PWSVKMTKLQAGGEATNIIPDKAKFALDLRAQ 242
|
90 100 110
....*....|....*....|....*....|.
gi 489003140 260 TELTDEMIKSRVIALLEK----YQLRYSVEW 286
Cdd:cd08018 243 SNEAMEELKEKVEHAIEAaaalYGASIEITE 273
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
36-232 |
8.33e-06 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 47.72 E-value: 8.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 36 IGFTVEPMDFGDTQNFWAWRGHGE---TLAFAGHTDVVPAGDADRWINPPFEPTI-----------------RDGM---- 91
Cdd:cd05654 46 VWQLLPPDDLGRRNVTALVKGKKPskrTIILISHFDTVGIEDYGELKDIAFDPDEltkafseyveeldeevrEDLLsgew 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 92 LFGRGAADMKGSLAAMVVAAERFVAqyPNHR-GRLAFLITSDEEaSAKNGTVKVVETL--MARNERLDY--CLVGEPSST 166
Cdd:cd05654 126 LFGRGTMDMKSGLAVHLALLEQASE--DEDFdGNLLLMAVPDEE-VNSRGMRAAVPALleLKKKHDLEYklAINSEPIFP 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489003140 167 EVVGDVVK---NGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAEL-VNI---EWDKGNEFFPPTSMQ 232
Cdd:cd05654 203 QYDGDQTRyiyTGSIGKILPGFLCYGKETHVGEPFAGINANLMASEITARLeLNAdlcEKVEGEITPPPVCLK 275
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
79-214 |
2.59e-05 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 45.94 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 79 INPPFEPTIRdgmLFGRGAADMKGSLAAMVVAAERFVAQYPNHRGRLAFLITSDEEASAKNgtvkVVETLMARNERL--D 156
Cdd:cd05678 106 IFSNLDPEWR---VFARAAADDKGPIMMMLAALDALKAGGIAPKFNVKIILDSEEEKGSPS----LPKAVKEYKELLaaD 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489003140 157 YCLVGEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQ-----GHvaYPHLADNPVHRAAPMLAEL 214
Cdd:cd05678 179 ALIIMDGPAHATNKPTLTFGCRGIATATLTTYGAKvpqhsGH--YGNYAPNPAFRLSSLLASM 239
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
65-136 |
2.83e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 45.68 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 65 GHTDVVPaGDADRWINP--PFEPTIRDGMLFGRGAADMKG----SLAAM-VVAAERfvaqypnhRGRLAF----LITSDE 133
Cdd:PRK07079 92 GHGDVVR-GYDEQWREGlsPWTLTEEGDRWYGRGTADNKGqhtiNLAALeQVLAAR--------GGRLGFnvklLIEMGE 162
|
...
gi 489003140 134 EAS 136
Cdd:PRK07079 163 EIG 165
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
6-310 |
2.88e-05 |
|
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: 45.80 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAWRGH--GETLAFAGHTDVVPAGDADRWinpPF 83
Cdd:TIGR01891 2 TDIRRHLHEHPELSFEEFKTSSLIAEALESLGIEVRRGVGGATGVVATIGGGkpGPVVALRADMDALPIQEQTDL---PY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 84 EPTIrDGMLFGRGaadmKGSLAAMVVAAERFVAQYPNH-RGRLAFLITSDEEASAknGTVKVVET-LMarnERLDYCLVG 161
Cdd:TIGR01891 79 KSTN-PGVMHACG----HDLHTAILLGTAKLLKKLADLlEGTVRLIFQPAEEGGG--GATKMIEDgVL---DDVDAILGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 162 EPSSTEVVGDVVKngRRGSLT-----CNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNEFFPPTsMQIANV 236
Cdd:TIGR01891 149 HPDPSIPAGTVGL--RPGTIMaaadkFEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQIVSRNVDPSRPAV-VSVGII 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 237 QSGTGSnNVIPGDMFVQFNFRFSTELTDEMIKSRVIALLE--------KYQLRysvewWLSGQPFLTGRGKLVDAVVNAI 308
Cdd:TIGR01891 226 EAGGAP-NVIPDKASMSGTVRSLDPEVRDQIIDRIERIVEgaaamygaKVELN-----YDRGLPAVTNDPALTQILKEVA 299
|
..
gi 489003140 309 EH 310
Cdd:TIGR01891 300 RH 301
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
184-285 |
2.64e-04 |
|
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349920 [Multi-domain] Cd Length: 367 Bit Score: 42.64 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 184 NLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNeffPPTS--MQIANVQSGTgSNNVIPGDMFVQFNFRFSTE 261
Cdd:cd05670 176 HIDFIGKSGHAAYPHNANDMVVAAANFVTQLQTIVSRNVD---PIDGavVTIGKIHAGT-ARNVIAGTAHLEGTIRTLTQ 251
|
90 100
....*....|....*....|....
gi 489003140 262 LTDEMIKSRVIALLEKYQLRYSVE 285
Cdd:cd05670 252 EMMELVKQRVRDIAEGIELAFDCE 275
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
177-311 |
7.06e-04 |
|
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: 41.26 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 177 RRGSLTCN-----LTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIewdkGNEFFPPTSMQ---IANVQSGTgSNNVIPG 248
Cdd:COG1473 175 RPGPIMAAadsfeITIKGKGGHAAAPHLGIDPIVAAAQIVTALQTI----VSRNVDPLDPAvvtVGIIHGGT-APNVIPD 249
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489003140 249 DMFVQFNFRFSTELTDEMIKSRVIALLEK----YQLRYSVEwWLSGQPFLTGRGKLVDAVVNAIEHY 311
Cdd:COG1473 250 EAELEGTVRTFDPEVRELLEERIERIAEGiaaaYGATAEVE-YLRGYPPTVNDPELTELAREAAREV 315
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
9-216 |
2.20e-03 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 39.79 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 9 AQQLIRRPSLSpddAGCQALMIERLRAIGFTVEPMD--FGDTQNFWAWRGHGE----TLAFAGHTDVVPAGDAdRWIN-- 80
Cdd:cd05679 20 SQEPARKPELR---AYLDQEMRPRFERLGFTVHIHDnpVAGRAPFLIAERIEDpslpTLLIYGHGDVVPGYEG-RWRDgr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 81 PPFEPTIRDGMLFGRGAADMKGSlAAMVVAAERFVAQypNHRGRLAFLITSDEEASAKNGTVKVVETLMARNERLDYCLV 160
Cdd:cd05679 96 DPWTVTVWGERWYGRGTADNKGQ-HSINMAALRQVLE--ARGGKLGFNVKFLIEMGEEMGSPGLRAFCFSHREALKADLF 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489003140 161 GEPSSTEVVGD--VVKNGRRGSLTCNLTIHGVQG--HVA-YPHLADNPVHRAAPMLAELVN 216
Cdd:cd05679 173 IASDGPRLAADrpTMFLGSRGGLNFELRVNLREGghHSGnWGGLLANPGIILANAIASLVD 233
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
58-134 |
9.14e-03 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 38.08 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489003140 58 GETLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAAD----MKGSLAAMVVAAERfvaQYPnhRGRLAFLITSDE 133
Cdd:cd05682 73 DDTVLLYGHMDKQPPFTGWDEGLGPTKPVIRGDKLYGRGGADdgyaIFASLTAIKALQEQ---GIP--HPRCVVLIEACE 147
|
.
gi 489003140 134 E 134
Cdd:cd05682 148 E 148
|
|
| |
