|
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: 762.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 2 SCPVIELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDFADTQNFWAWRG-QGETLAFAGHTDVVPPGDADRWIN 80
Cdd:PRK13009 1 MSDVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDFGDVKNLWARRGtEGPHLCFAGHTDVVPPGDLEAWTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNGTVKVVEALMARNERLDYCLV 160
Cdd:PRK13009 81 PPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVLEWLKARGEKIDYCIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 161 GEPSSIEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATSMQIANIQAGT 240
Cdd:PRK13009 161 GEPTSTERLGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEGNEFFPPTSLQITNIDAGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 241 GSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTVDWWLSGQPFLTARGKLVDAVVNAVEHYNEIKPQLLT 320
Cdd:PRK13009 241 GATNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDYTLEWTLSGEPFLTPPGKLVDAVVAAIEAVTGITPELST 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1476918594 321 TGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQLVA 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: 684.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 6 IELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDFADTQNFWAWRGQ-GETLAFAGHTDVVPPGDADRWINPPFE 84
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFGGVKNLWARRGTgGPHLCFAGHTDVVPPGDLEGWSSDPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNGTVKVVEALMARNERLDYCLVGEPS 164
Cdd:cd03891 81 PTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKIDYCIVGEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 165 SIEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATSMQIANIQAGTGSNN 244
Cdd:cd03891 161 SEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLDEGNEFFPPSSLQITNIDVGNGATN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 245 VIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTVDWWLSGQPFLTARGKLVDAVVNAVEHYNEIKPQLLTTGGT 324
Cdd:cd03891 241 VIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELSTSGGT 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1476918594 325 SDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIM 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: 614.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 5 VIELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDFADTQNFWAWRGQGE-TLAFAGHTDVVPPGDADRWINPPF 83
Cdd:TIGR01246 1 VTELAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGDTKNLWATRGTGEpVLAFAGHTDVVPAGPEEQWSSPPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 84 EPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNGTVKVVEALMARNERLDYCLVGEP 163
Cdd:TIGR01246 81 EPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVETLMARDELIDYCIVGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 164 SSIEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATSMQIANIQAGTGSN 243
Cdd:TIGR01246 161 SSVKKLGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAIKWDEGNEFFPPTSLQITNIHAGTGAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 244 NVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTVDWWLSGQPFLTARGKLVDAVVNAVEHYNEIKPQLLTTGG 323
Cdd:TIGR01246 241 NVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELSTGGG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1476918594 324 TSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQL 373
Cdd:TIGR01246 321 TSDGRFIALMGAEVVEFGPVNATIHKVNECVSIEDLEKLSDVYQDLLENL 370
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
5-375 |
1.07e-125 |
|
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: 366.90 E-value: 1.07e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 5 VIELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDFADTQ-NFWAWR---GQGETLAFAGHTDVVPPGDADRWIN 80
Cdd:COG0624 14 ALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPPGRpNLVARRpgdGGGPTLLLYGHLDVVPPGDLELWTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAhNGTVKVVEALmARNERLDYCLV 160
Cdd:COG0624 94 DPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGS-PGARALVEEL-AEGLKADAAIV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 161 GEPSSIevvgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWD-QGNEFFPATSMQIANIQAG 239
Cdd:COG0624 172 GEPTGV----PTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDgRADPLFGRTTLNVTGIEGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 240 TGSnNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQ--LRYTVDWWL-SGQPFLT-ARGKLVDAVVNAVEHYNEIK 315
Cdd:COG0624 248 TAV-NVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAApgVEVEVEVLGdGRPPFETpPDSPLVAAARAAIREVTGKE 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1476918594 316 PQLLTTGGTSDGRFIAR-MGAQVVELGPVN-ATIHKINECVNAADLQLLARMYQRIMEQLVA 375
Cdd:COG0624 327 PVLSGVGGGTDARFFAEaLGIPTVVFGPGDgAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
7-369 |
1.37e-112 |
|
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: 332.73 E-value: 1.37e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 7 ELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDFADTQNFWAWRGQGE--TLAFAGHTDVVPPGDADRWINPPFE 84
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVATVGGGDgpVLLLNGHIDTVPPGDGDKWSFPPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAhNGTVKVVEALMArnERLDYCLVGEPS 164
Cdd:cd08659 81 GRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGS-DGARALLEAGYA--DRLDALIVGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 165 sievvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWD-QGNEFFPATSMQIANIQAGTGSn 243
Cdd:cd08659 158 -----GLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEElPAHPLLGPPTLNVGVINGGTQV- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 244 NVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTVDWWLSGQP--FLTARGKLVDAVVNAVEHYNeIKPQLLTT 321
Cdd:cd08659 232 NSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPpfFTDPDHPLVQALQAAARALG-GDPVVRPF 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1476918594 322 GGTSDGRFIARM-GAQVVELGP-VNATIHKINECVNAADLQLLARMYQRI 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 |
1.14e-85 |
|
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: 262.28 E-value: 1.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 62 AFAGHTDVVPPGDADRWinpPFEPTIrDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHtGRLAFLITSDEEaSAHNGT 141
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLKK-GTVKLLFQPDEE-GGMGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 142 VKVVEALMARNERLDYCL---VGEPSS-IEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAI 217
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFglhIGEPTLlEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 218 EWDQGNEFFPA--TSMQIANIQAGTgsnNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEK----HQLRYTVDWWLSGQ 291
Cdd:pfam01546 155 VSRNVDPLDPAvvTVGNITGIPGGV---NVIPGEAELKGDIRLLPGEDLEELEERIREILEAiaaaYGVKVEVEYVEGGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 292 PFLTARGKLVDAVVNAVEHYNEIKPQLLTTG--GTSDGRFIA-RMGAQVVELGPVNATIHKINECVNAADLQLLARMYQR 368
Cdd:pfam01546 232 PPLVNDSPLVAALREAAKELFGLKVELIVSGsmGGTDAAFFLlGVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLAR 311
|
....
gi 1476918594 369 IMEQ 372
Cdd:pfam01546 312 LLLK 315
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
7-371 |
6.91e-54 |
|
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: 182.02 E-value: 6.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 7 ELTQQLIRRPSLSPD-DAGCQALLIERLQAIGFTVERMDFADTQ--NFWAWRGQG--ETLAFAGHTDVVPPgDADRWINP 81
Cdd:cd03894 1 ELLARLVAFDTVSRNsNLALIEYVADYLAALGVKSRRVPVPEGGkaNLLATLGPGgeGGLLLSGHTDVVPV-DGQKWSSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 82 PFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTgrLAFLITSDEEASaHNGTVKVVEALMARNERLDYCLVG 161
Cdd:cd03894 80 PFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKP--LHLAFSYDEEVG-CLGVRHLIAALAARGGRPDAAIVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 162 EPSSIEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELV--AIEWDQG--NEFF--PATSMQIAN 235
Cdd:cd03894 157 EPTSLQPV-----VAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRelADRLAPGlrDPPFdpPYPTLNVGL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 236 IQAGTGSnNVIPGELFVQFNFRF----STELTDEMIKAQVLALLEKHQLRYTVDWWLSGQPFLTARGklvDAVVNAVEHY 311
Cdd:cd03894 232 IHGGNAV-NIVPAECEFEFEFRPlpgeDPEAIDARLRDYAEALLEFPEAGIEVEPLFEVPGLETDED---APLVRLAAAL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1476918594 312 NEIKPQLLTTGGTsDGRFIARMGAQVVELGPVN-ATIHKINECVNAADLQLLARMYQRIME 371
Cdd:cd03894 308 AGDNKVRTVAYGT-EAGLFQRAGIPTVVCGPGSiAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
6-352 |
1.06e-52 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 179.13 E-value: 1.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 6 IELTQQLIRRPSLSP---DDAGCQALLIERLQAIGFTVERMDFADTQNFWAWR--------GQGETLAFAGHTDVVPPGD 74
Cdd:TIGR01910 1 VELLKDLISIPSVNPpggNEETIANYIKDLLREFGFSTDVIEITDDRLKVLGKvvvkepgnGNEKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 75 ADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEaSAHNGTVKVVEALMARNEr 154
Cdd:TIGR01910 81 LELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEE-SGEAGTLYLLQRGYFKDA- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 155 lDYCLVGEPSSievvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNEL--VAIEWDQGNEFFPATSMQ 232
Cdd:TIGR01910 159 -DGVLIPEPSG----GDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELneLEEHIYARNSYGFIPGPI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 233 IANIQAGTGSNNV--IPGELFVQFNFRFSTELTDEMIKAQVLAL---LEKHQ---LRYTVDWWLSGQPFLTARGKLVDAV 304
Cdd:TIGR01910 234 TFNPGVIKGGDWVnsVPDYCEFSIDVRIIPEENLDEVKQIIEDVvkaLSKSDgwlYENEPVVKWSGPNETPPDSRLVKAL 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1476918594 305 VNAVEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGP-VNATIHKINE 352
Cdd:TIGR01910 314 EAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPgDLETAHQVNE 362
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
5-375 |
7.37e-48 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 166.70 E-value: 7.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 5 VIELTQQLIRRPSLSP---DDAGCQALLIERLQAIGFTVERMDFADT---------QNFWAWRGQGET-LAFAGHTDVVP 71
Cdd:PRK08651 8 IVEFLKDLIKIPTVNPpgeNYEEIAEFLRDTLEELGFSTEIIEVPNEyvkkhdgprPNLIARRGSGNPhLHFNGHYDVVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 72 PGDADRwINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFvaqHPNHTGRLAFLITSDEEaSAHNGTVKVVEALMAr 151
Cdd:PRK08651 88 PGEGWS-VNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERL---DPAGDGNIELAIVPDEE-TGGTGTGYLVEEGKV- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 152 neRLDYCLVGEPSSIEVVGdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELV-AIEWDQGNEFFPATS 230
Cdd:PRK08651 162 --TPDYVIVGEPSGLDNIC----IGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKsSLSTIKSKYEYDDER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 231 MQIANIQAGT------GSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLE----KHQLRYTVDWWLSGQPFLTARG-K 299
Cdd:PRK08651 236 GAKPTVTLGGptveggTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDevapELGIEVEFEITPFSEAFVTDPDsE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1476918594 300 LVDAVVNAVEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGP-VNATIHKINECVNAADLQLLARMYQRIMEQLVA 375
Cdd:PRK08651 316 LVKALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPgELELAHAPDEYVEVKDVEKAAKVYEEVLKRLAK 392
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
56-372 |
2.28e-39 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 143.87 E-value: 2.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 56 GQGE-TLAFAGHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ-HPNHtGRLAFLITSDE 133
Cdd:PRK08588 56 GSGSpVLALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQgQLLN-GTIRLLATAGE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 134 EaSAHNGTVKVVEALMARNerLDYCLVGEPSsievvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNE 213
Cdd:PRK08588 135 E-VGELGAKQLTEKGYADD--LDALIIGEPS-----GHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 214 LvaiewdqgNEFFpATSMQIANIQAGT--------GSN--NVIPGELFVQFNFRFSTELTDEMIKAQVLALLEK------ 277
Cdd:PRK08588 207 Q--------KEYF-DSIKKHNPYLGGLthvvtiinGGEqvNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEvnqnga 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 278 HQLRYTVDwwLSGQPFLTAR-GKLVDAVVNAVEHYNEIKPQLLTTGGTSDGRFIARMGA--QVVELGP-VNATIHKINEC 353
Cdd:PRK08588 278 AQLSLDIY--SNHRPVASDKdSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKPdfPVIIFGPgNNLTAHQVDEY 355
|
330
....*....|....*....
gi 1476918594 354 VNAADLQLLARMYQRIMEQ 372
Cdd:PRK08588 356 VEKDMYLKFIDIYKEIIIQ 374
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-370 |
1.98e-38 |
|
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: 140.99 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 6 IELTQQLIRRPSLSPDDAG---CQALLIERLQAIGFTVERMDFADTQNFW-----AWRGqGETLAFAGHTDVVPPGDADR 77
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDNtsaIAAYIKLLLEDLGYPVELHEPPEEIYGVvsnivGGRK-GKRLLFNGHYDVVPAGDGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 78 WINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNGTVKVVEALMARNerlDY 157
Cdd:cd08011 80 WTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYLLEKVRIKP---ND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 158 CLVGEPSSievvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEwdqgneffpaTSMQIANIQ 237
Cdd:cd08011 157 VLIGEPSG----SDNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELE----------KTVNPGVIK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 238 AGTgSNNVIPGELFVQFNFRFSTEL-TDEmikaqVLALLEKH-----QLRYTVDWWLSGqPFLTARGKLVDAVVNAVEHY 311
Cdd:cd08011 223 GGV-KVNLVPDYCEFSVDIRLPPGIsTDE-----VLSRIIDHldsieEVSFEIKSFYSP-TVSNPDSEIVKKTEEAITEV 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 312 NEIKPQLLTTGGTSDGRFIARMGAQVVELGPVN-ATIHKINECVNAADLQLLARMYQRIM 370
Cdd:cd08011 296 LGIRPKEVISVGASDARFYRNAGIPAIVYGPGRlGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-282 |
5.52e-36 |
|
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: 133.97 E-value: 5.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 5 VIELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDfadtQNFWAWRGQGE----TLAFAGHTDVVPPGDAdrWIN 80
Cdd:cd05651 2 AIELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRKG----NNVWAENGHFDegkpTLLLNSHHDTVKPNAG--WTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPnHTGRLAFLITSDEEASAHNGtvkvVEALMARNERLDYCLV 160
Cdd:cd05651 76 DPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGP-LNYNLIYAASAEEEISGKNG----IESLLPHLPPLDLAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 161 GEPSSIEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHlADNPVHRAAPFLNELVAIEWDQGNEFFPATSMQIANIQAGT 240
Cdd:cd05651 151 GEPTEMQPA-----IAEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDIQWLRDFRFDKVSPLLGPVKMTVTQINAGT 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1476918594 241 gSNNVIPGE----LFVQFNFRFSTELTDEMIKAQVLALLEKHQLRY 282
Cdd:cd05651 225 -QHNVVPDSctfvVDIRTTEAYTNEEIFEIIRGNLKSEIKPRSFRL 269
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
28-365 |
2.05e-35 |
|
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: 132.71 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 28 LLIERLQAIGFTVERMDFADTQN--FWAWRGQGET-LAFAGHTDVV-PPGDADRWinpPFepTIRDGMLFGRGAADMKGS 103
Cdd:cd03885 27 LLAEELEALGFTVERRPLGEFGDhlIATFKGTGGKrVLLIGHMDTVfPEGTLAFR---PF--TVDGDRAYGPGVADMKGG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 104 LAAMVVAAERFVAQHPNHTGRLAFLITSDEE-ASAHNGTVKVVEALMArnerlDYCLVGEPSSievVGDVVKNGRRGSLT 182
Cdd:cd03885 102 LVVILHALKALKAAGGRDYLPITVLLNSDEEiGSPGSRELIEEEAKGA-----DYVLVFEPAR---ADGNLVTARKGIGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 183 CNLTIHGVQGHV-AYPHLADNPVHRAAPFLNELVAIewdqgNEFFPATSMQIANIQAGTGSnNVIPGELFVQFNFRFSTE 261
Cdd:cd03885 174 FRLTVKGRAAHAgNAPEKGRSAIYELAHQVLALHAL-----TDPEKGTTVNVGVISGGTRV-NVVPDHAEAQVDVRFATA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 262 LTDEMIKAQVLALLEKHQLRYTVdwwlsgqpfLTARGKLV-------DAVVNAVEHYNEIKPQL-LT-----TGGTSDGR 328
Cdd:cd03885 248 EEADRVEEALRAIVATTLVPGTS---------VELTGGLNrppmeetPASRRLLARAQEIAAELgLTldweaTGGGSDAN 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1476918594 329 FIARMGAQVVE-LGPVNATIHKINECVNAADL----QLLARM 365
Cdd:cd03885 319 FTAALGVPTLDgLGPVGGGAHTEDEYLELDSLvpriKLLARL 360
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
65-375 |
3.91e-35 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 132.62 E-value: 3.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 65 GHTDVVPPgDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ---HPNHtgrLAFliTSDEEAsahnGT 141
Cdd:PRK07522 71 GHTDVVPV-DGQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAplrRPLH---LAF--SYDEEV----GC 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 142 VKV---VEALMARNERLDYCLVGEPSSIEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAI- 217
Cdd:PRK07522 141 LGVpsmIARLPERGVKPAGCIVGEPTSMRPV-----VGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLa 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 218 ----EWDQGNEFF--PATSMQIANIQAGTgSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLrytvdwwlsgq 291
Cdd:PRK07522 216 drlaAPGPFDALFdpPYSTLQTGTIQGGT-ALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAELL----------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 292 PFLTARGKLVDAVVNAVEHYneikPQLLT-------------TG---------GTSDGRFiARMGAQVVELGPVN-ATIH 348
Cdd:PRK07522 284 PEMRAVHPEAAIEFEPLSAY----PGLDTaedaaaarlvralTGdndlrkvayGTEAGLF-QRAGIPTVVCGPGSiEQAH 358
|
330 340
....*....|....*....|....*..
gi 1476918594 349 KINECVNAADLQLLARMYQRIMEQLVA 375
Cdd:PRK07522 359 KPDEFVELAQLAACEAFLRRLLASLAA 385
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-279 |
5.37e-35 |
|
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: 131.24 E-value: 5.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 5 VIELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVER--MDFADTQNFWAWRGQGET--LAFAGHTDVVPPgdadrWIn 80
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKqpVENKDRFNVYAYPGSSRQprVLLTSHIDTVPP-----FI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 81 pPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASaHNGTVKVVEALmarNERLDYCLV 160
Cdd:cd05652 75 -PYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETG-GDGMKAFNDLG---LNTWDAVIF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 161 GEPSSIEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQgNEFFPATSMQIANIQAGT 240
Cdd:cd05652 150 GEPTELKLA-----SGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPS-SELLGPTTLNIGRISGGV 223
|
250 260 270
....*....|....*....|....*....|....*....
gi 1476918594 241 GSnNVIPGELFVQFNFRFSTEltDEMIKAQVLALLEKHQ 279
Cdd:cd05652 224 AA-NVVPAAAEASVAIRLAAG--PPEVKDIVKEAVAGIL 259
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
5-364 |
1.58e-34 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 131.81 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 5 VIELTQQLIRRPSLSPDDAG---CQALLIERLQAIGFTVERMDF----ADTQNFWAW--------RGQGETLAFAGHTDV 69
Cdd:PRK13013 16 LVALTQDLIRIPTLNPPGRAyreICEFLAARLAPRGFEVELIRAegapGDSETYPRWnlvarrqgARDGDCVHFNSHHDV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 70 VPPGDAdrWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNGTVKVVEALM 149
Cdd:PRK13013 96 VEVGHG--WTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGGVAYLAEQGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 150 ARNERLDYCLVGEPSSIevvgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNElvaIEwdqgNEFFPA- 228
Cdd:PRK13013 174 FSPDRVQHVIIPEPLNK----DRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAE---IE----ERLFPLl 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 229 ----TSMQIA---------NIQAGTGSNNV------------IPGELFVQFNFRFSTELTDEMIKAQVLALLEK-----H 278
Cdd:PRK13013 243 atrrTAMPVVpegarqstlNINSIHGGEPEqdpdytglpapcVADRCRIVIDRRFLIEEDLDEVKAEITALLERlkrarP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 279 QLRYTVDWWLSGQPFLTARGK-LVDAVVNAVEHYNEIKPQLLTTGGTSDGRFIARMGA--QVVELGP-VNATIHKINECV 354
Cdd:PRK13013 323 GFAYEIRDLFEVLPTMTDRDApVVRSVAAAIERVLGRQADYVVSPGTYDQKHIDRIGKlkNCIAYGPgILDLAHQPDEWV 402
|
410
....*....|
gi 1476918594 355 NAADLQLLAR 364
Cdd:PRK13013 403 GIADMVDSAK 412
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
5-375 |
3.54e-33 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 127.36 E-value: 3.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 5 VIELTQQLIRRPSLSPDDAGCQALLIERLQAIGFT-VERMDFAdtqNFWAWRGQGETL-AFAGHTDVVPPGDADRWINPP 82
Cdd:PRK13004 17 MTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFDkVEIDPMG---NVLGYIGHGKKLiAFDAHIDTVGIGDIKNWDFDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 83 FEPTIRDGMLFGRGAADMKGSLAAMVVAAERFvaQHPNHTGRLAFLITsdeeasahnGTV--KVVEALMAR------NER 154
Cdd:PRK13004 94 FEGEEDDGRIYGRGTSDQKGGMASMVYAAKII--KDLGLDDEYTLYVT---------GTVqeEDCDGLCWRyiieedKIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 155 LDYCLVGEPSSIEvvgdvVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGN-EFFPATSMQI 233
Cdd:PRK13004 163 PDFVVITEPTDLN-----IYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNLKEdPFLGKGTLTV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 234 ANIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTVDWW------LSGQPFLTAR---------- 297
Cdd:PRK13004 238 SDIFSTSPSRCAVPDSCAISIDRRLTVGETWESVLAEIRALPAVKKANAKVSMYnydrpsYTGLVYPTECyfptwlyped 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 298 GKLVDAVVNAVEHYNEIKPQL----LTTGGTSdgrfIA-RMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRIME 371
Cdd:PRK13004 318 HEFVKAAVEAYKGLFGKAPEVdkwtFSTNGVS----IAgRAGIPTIGFGPGKEPLaHAPNEYTWKEQLVKAAAMYAAIPK 393
|
....
gi 1476918594 372 QLVA 375
Cdd:PRK13004 394 SLLK 397
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
5-373 |
5.91e-33 |
|
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: 125.93 E-value: 5.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 5 VIELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERmdfADTQNFWAWRGQGE-TLAFAGHTDVVPpGDadrwinppF 83
Cdd:cd05653 3 AVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWV---DEAGNAVGGAGSGPpDVLLLGHIDTVP-GE--------I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 84 EPTIRDGMLFGRGAADMKGSLAAMVVAAerfVAQHPNHTGRLAFLITSDEEASAhngtvKVVEALMARNERLDYCLVGEP 163
Cdd:cd05653 71 PVRVEGGVLYGRGAVDAKGPLAAMILAA---SALNEELGARVVVAGLVDEEGSS-----KGARELVRRGPRPDYIIIGEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 164 SSievvGDVVKNGRRGSLTCNLTIHGVQGHVAYPhlADNPVHRAAPFLNELVaiEWDQGNE--FFPATSMQIANIQAGTg 241
Cdd:cd05653 143 SG----WDGITLGYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLIKKWLEVK--KWAEGYNvgGRDFDSVVPTLIKGGE- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 242 SNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTVDwwlsGQPFLTA-RGKLVDAVVNAVEHYNeIKPQLLT 320
Cdd:cd05653 214 SSNGLPQRAEATIDLRLPPRLSPEEAIALATALLPTCELEFIDD----TEPVKVSkNNPLARAFRRAIRKQG-GKPRLKR 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1476918594 321 TGGTSDGRFIA-RMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRIMEQL 373
Cdd:cd05653 289 KTGTSDMNVLApLWTVPIVAYGPGDSTLdHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-364 |
2.38e-31 |
|
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: 122.42 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 7 ELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVER--MDFADTQN---FW--AW---------------RGQGETLAFA 64
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDRweIDVEKLKHhpgFSpvAVdyagapnvvgthrprGETGRSLILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 65 GHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEaSAHNGTVkv 144
Cdd:cd03895 81 GHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEE-CTGNGAL-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 145 veALMARNERLDYCLVGEPSSIEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIE--WDQG 222
Cdd:cd03895 158 --AALMRGYRADAALIPEPTELKLV-----RAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEreWNAR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 223 NEFFPATS-------MQIANIQAGTGSNNViPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRytvDWWLSGQPF-- 293
Cdd:cd03895 231 KKSHPHFSdhphpinFNIGKIEGGDWPSSV-PAWCVLDCRIGIYPGESPEEARREIEECVADAAAT---DPWLSNHPPev 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 294 -----------LTARGKLVDAVVNAVEHYNEIKPQLLTTGGTSDGRFIARMGA-QVVELGPVNATIHKINECVNAADLQL 361
Cdd:cd03895 307 ewngfqaegyvLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGDiPALCYGPGSRDAHGFDESVDLESLRK 386
|
...
gi 1476918594 362 LAR 364
Cdd:cd03895 387 ITK 389
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-370 |
4.84e-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 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: 118.71 E-value: 4.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 5 VIELTQQLIRRPSLSPDDAG------CQALLiERLQAIGF-TVERMDFADTQNFW-------AWRGQGETLAFAGHTDVV 70
Cdd:cd05650 3 IIELERDLIRIPAVNPESGGegekekADYLE-KKLREYGFyTLERYDAPDERGIIrpnivakIPGGNDKTLWIISHLDTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 71 PPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQH--PNHTGRLAFLitSDEEASAHNGTVKVVEAL 148
Cdd:cd05650 82 PPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGitPKYNFGLLFV--ADEEDGSEYGIQYLLNKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 149 -MARNErlDYCLVgePSSIEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPF---LNELVAIEWDQGNE 224
Cdd:cd05650 160 dLFKKD--DLIIV--PDFGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFaleLDELLHEKFDEKDD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 225 FF--PATSMQIANIQAGTGSNNVIPGELFVQFNFR-FSTELTDEMIKA--QVLALLEKH---QLRYTVDWWLSGQPFLTA 296
Cdd:cd05650 236 LFnpPYSTFEPTKKEANVPNVNTIPGYDVFYFDCRvLPTYKLDEVLKFvnKIISDFENSygaGITYEIVQKEQAPPATPE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1476918594 297 RGKLVDAVVNAVEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIM 370
Cdd:cd05650 316 DSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYIRISHIVKDAKVFAEML 389
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
175-283 |
7.19e-29 |
|
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: 108.20 E-value: 7.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 175 NGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNeFFPATSMQIANIQAGTgSNNVIPGELFVQF 254
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGF-DFPRTTLNITGIEGGT-ATNVIPAEAEAKF 78
|
90 100
....*....|....*....|....*....
gi 1476918594 255 NFRFSTELTDEMIKAQVLALLEKHQLRYT 283
Cdd:pfam07687 79 DIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
6-359 |
1.32e-28 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 115.48 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 6 IELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVER--MDFADTQNF-----WAW---------------RGQGETLAF 63
Cdd:PRK06837 23 VAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDRwsIDPDDLKSHpgagpVEIdysgapnvvgtyrpaGKTGRSLIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 64 AGHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVA--AERFVAQHPnhTGRLaFLITSDEEASAHNGt 141
Cdd:PRK06837 103 QGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFAldALRAAGLAP--AARV-HFQSVIEEESTGNG- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 142 vkvveALMA--RNERLDYCLVGEPSSIEVVGDVVkngrrGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNEL--VAI 217
Cdd:PRK06837 179 -----ALSTlqRGYRADACLIPEPTGEKLVRAQV-----GVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALreLEA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 218 EWDQ---GNEFFPA----TSMQIANIQAGTGSNNViPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRytvDWWLSG 290
Cdd:PRK06837 249 EWNArkaSDPHFEDvphpINFNVGIIKGGDWASSV-PAWCDLDCRIAIYPGVTAADAQAEIEACLAAAARD---DRFLSN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 291 QP-------F------LTARGKLVDAVVNAVEHYNEIKPQLLTTGGTSDGRFIA---RMGAQVveLGPVNATIHKINECV 354
Cdd:PRK06837 325 NPpevvwsgFlaegyvLEPGSEAEAALARAHAAVFGGPLRSFVTTAYTDTRFYGlyyGIPALC--YGPSGEGIHGFDERV 402
|
....*
gi 1476918594 355 NAADL 359
Cdd:PRK06837 403 DLESV 407
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
5-368 |
4.64e-28 |
|
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: 112.54 E-value: 4.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 5 VIELTQQLIRRPSLSPD-----DAGCQALlieRLQAIgFTVERmdFADTQNFWAWRGQGETLAFAGHTDVVPPGDadrwi 79
Cdd:cd05647 1 PIELTAALVDIPSVSGNekpiaDEIEAAL---RTLPH-LEVIR--DGNTVVARTERGLASRVILAGHLDTVPVAG----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 80 NPPfePTIR-DGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTgrLAFLITSDEE-ASAHNGTVKVVEALmarNERL-- 155
Cdd:cd05647 70 NLP--SRVEeDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHD--LTLIFYDCEEvAAELNGLGRLAEEH---PEWLaa 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 156 DYCLVGEPSSIEVVGdvvknGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEwdqgneffPATsmqiAN 235
Cdd:cd05647 143 DFAVLGEPTDGTIEG-----GCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLAAYE--------PRT----VN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 236 IQ-------------AGTGSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTV-DWWLSGQPFLTArgKLV 301
Cdd:cd05647 206 IDgltyreglnavfiSGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEIEVtDLSPGALPGLDH--PVA 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1476918594 302 DAVVNAVEhyNEIKPQLlttGGTSDGRFiARMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQR 368
Cdd:cd05647 284 RDLIEAVG--GKVRAKY---GWTDVARF-SALGIPAVNFGPGDPLLaHKRDEQVPVEQITACAAILRR 345
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
5-370 |
6.05e-27 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 110.32 E-value: 6.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 5 VIELTQQLIRRPSLSPDDAG------CQALLiERLQAIGFT-VERMDFADTQNFWAWR--------GQGE--TLAFAGHT 67
Cdd:PRK13983 7 MIELLSELIAIPAVNPDFGGegekekAEYLE-SLLKEYGFDeVERYDAPDPRVIEGVRpnivakipGGDGkrTLWIISHM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 68 DVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQH--PNHTGRLAFLitSDEEASAHNGtvkvV 145
Cdd:PRK13983 86 DVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGirPKYNLGLAFV--SDEETGSKYG----I 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 146 EALMARNERL----DYCLV---GEP--SSIEVvgdvvknGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNEL-- 214
Cdd:PRK13983 160 QYLLKKHPELfkkdDLILVpdaGNPdgSFIEI-------AEKSILWLKFTVKGKQCHASTPENGINAHRAAADFALELde 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 215 -VAIEWDQGNEFF--PATSMQIANIQAGTGSNNVIPGElfVQFNF------RFSTELTDEMIKAQVLALLEKHQLRYTVD 285
Cdd:PRK13983 233 aLHEKFNAKDPLFdpPYSTFEPTKKEANVDNINTIPGR--DVFYFdcrvlpDYDLDEVLKDIKEIADEFEEEYGVKIEVE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 286 WWLSGQ--PFLTARGKLVDAVVNAVEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLA 363
Cdd:PRK13983 311 IVQREQapPPTPPDSEIVKKLKRAIKEVRGIEPKVGGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYAKISNLIEDA 390
|
....*..
gi 1476918594 364 RMYQRIM 370
Cdd:PRK13983 391 KVFALLL 397
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
5-366 |
1.04e-26 |
|
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: 110.41 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 5 VIELTQQLIRRPSLSPDDA-------GCQALLIERLQ---AIGFTVERMD-FADTQNFwawrGQG-ETLAFAGHTDVVPP 72
Cdd:cd03888 10 ILEDLKELVAIPSVRDEATegapfgeGPRKALDKFLDlakRLGFKTKNIDnYAGYAEY----GEGeEVLGILGHLDVVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 73 GDAdrWINPPFEPTIRDGMLFGRGAADMKG-SLAAMVvaAERFVAQH---PNHTGRlaFLITSDEEAS--------AHNG 140
Cdd:cd03888 86 GEG--WTTDPFKPVIKDGKLYGRGTIDDKGpTIAALY--ALKILKDLglpLKKKIR--LIFGTDEETGwkciehyfEHEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 141 TVK----------VVEA------LMAR-------NERLDYCLVGE-----PSSIEVVGDVVKNGRRGSLTCN-------- 184
Cdd:cd03888 160 YPDfgftpdaefpVINGekgivtVDLTfkidddkGYRLISIKGGEatnmvPDKAEAVIPGKDKEELALSAATdlkgniei 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 185 ------LTIHGVQGHVAYPHLADNPVHRAAPFLNELvaiewDQGNEFFPATSMQIANI-QAGTGSN-------------- 243
Cdd:cd03888 240 ddggveLTVTGKSAHASAPEKGVNAITLLAKFLAEL-----NKDGNDKDFIKFLAKNLhEDYNGKKlginfedevmgelt 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 244 ------NVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTVDwwLSGQPFLTAR-GKLVDAVVNAVEHYNEIKP 316
Cdd:cd03888 315 lnpgiiTLDDGKLELGLNVRYPVGTSAEDIIKQIEEALEKYGVEVEGH--KHQKPLYVPKdSPLVKTLLKVYEEQTGKEG 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1476918594 317 QLLTTGGTSDGRFIARMgaqvVELGP----VNATIHKINECVNAADLQLLARMY 366
Cdd:cd03888 393 EPVAIGGGTYARELPNG----VAFGPefpgQKDTMHQANEFIPIDDLIKALAIY 442
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
10-359 |
1.46e-25 |
|
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation.
Pssm-ID: 349888 [Multi-domain] Cd Length: 426 Bit Score: 106.64 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 10 QQLIRRPSLSPDDAGCQAL------LIERLQAIGFTVERMDFADTQNF-WAWRGQGE---TLAFAGHTDVVPPGDADRWI 79
Cdd:cd03893 5 AELVAIPSVSAQPDRREELrraaewLADLLRRLGFTVEIVDTSNGAPVvFAEFPGAPgapTVLLYGHYDVQPAGDEDGWD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 80 NPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEAsahnGTVKVVEALMARNERL--DY 157
Cdd:cd03893 85 SDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEES----GSPSLDQLVEAHRDLLaaDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 158 CLVGEPSSIEVVGDVVKNGRRGSLTCNLTI----HGV--------------------------QGHVAYPHLADNP---- 203
Cdd:cd03893 161 IVISDSTWVGQEQPTLTYGLRGNANFDVEVkgldHDLhsglyggvvpdpmtalaqllaslrdeTGRILVPGLYDAVrelp 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 204 --VHRAAPFLNELVAIEWDQGNEF------FPATSMQ-IANIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKAQVLAL 274
Cdd:cd03893 241 eeEFRLDAGVLEEVEIIGGTTGSVaerlwtRPALTVLgIDGGFPGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLEAH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 275 LEKH---QLRYTVDWWLSGQPFLT-ARGKLVDAVVNAVEHYNEIKPQLLTTGGT--SDGRFIARMGAQVVELGPVNAT-- 346
Cdd:cd03893 321 LEKHapsGAKVTVSYVEGGMPWRSdPSDPAYQAAKDALRTAYGVEPPLTREGGSipFISVLQEFPQAPVLLIGVGDPDdn 400
|
410
....*....|...
gi 1476918594 347 IHKINECVNAADL 359
Cdd:cd03893 401 AHSPNESLRLGNY 413
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-274 |
4.90e-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: 104.81 E-value: 4.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 6 IELTQQLIRRPSLSPDDAGCQALLIERLQAIGF---TVERMDfadtqNFWAWRGQGET-LAFAGHTDVVPPGDADRWINP 81
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGFdevEIDPMG-----NVIGYIGGGKKkILFDGHIDTVGIGNIDNWKFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 82 PFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFvaqhpNHTGRLAFlitSDEEASAhnGTV--KVVEALMAR------NE 153
Cdd:cd05649 76 PYEGYETDGKIYGRGTSDQKGGLASMVYAAKIM-----KDLGLRDF---AYTILVA--GTVqeEDCDGVCWQyiskadKI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 154 RLDYCLVGEPSSIEvvgdvVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQG-NEFFPATSMQ 232
Cdd:cd05649 146 KPDFVVSGEPTDGN-----IYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFPeAPFLGRGTLT 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1476918594 233 IANIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKAQVLAL 274
Cdd:cd05649 221 VTDIFSTSPSRCAVPDSCRISIDRRLTVGETWEGCLEEIRAL 262
|
|
| PRK06915 |
PRK06915 |
peptidase; |
6-193 |
5.17e-25 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 105.16 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 6 IELTQQLIRRPSLSPDDAGCQALLIERLQAIG------------------FTVERMDFADTQNFWA-WRGQGE--TLAFA 64
Cdd:PRK06915 20 VKLLKRLIQEKSVSGDESGAQAIVIEKLRELGldldiwepsfkklkdhpyFVSPRTSFSDSPNIVAtLKGSGGgkSMILN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 65 GHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEaSAHNGTVKV 144
Cdd:PRK06915 100 GHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEE-SGGAGTLAA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1476918594 145 VEalmaRNERLDYCLVGEPSSIEVvgdVVKngRRGSLTCNLTIHGVQGH 193
Cdd:PRK06915 179 IL----RGYKADGAIIPEPTNMKF---FPK--QQGSMWFRLHVKGKAAH 218
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
8-368 |
3.19e-24 |
|
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.
Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 103.21 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 8 LTQQLIRRPSLSPDDAGCQA-----LLIERLQAIGFTVE---------------RMDFADTQNfwawrgqgETLAFAGHT 67
Cdd:cd05675 3 LLQELIRIDTTNSGDGTGSEtraaeVLAARLAEAGIQTEifvveshpgranlvaRIGGTDPSA--------GPLLLLGHI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 68 DVVPpGDADRWINPPFEPTIRDGMLFGRGAADMKGsLAAMVVAAERFVAQH---PNHTGRLAFliTSDEEASAHNGTVKV 144
Cdd:cd05675 75 DVVP-ADASDWSVDPFSGEIKDGYVYGRGAVDMKN-MAAMMLAVLRHYKREgfkPKRDLVFAF--VADEEAGGENGAKWL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 145 VEALMARNERLDYCLV-GEPSSIEVVGD----VVKNGRRGSLTCNLTIHGVQGHVAYPHlADNPVHRAAPFLNELVAIEW 219
Cdd:cd05675 151 VDNHPELFDGATFALNeGGGGSLPVGKGrrlyPIQVAEKGIAWMKLTVRGRAGHGSRPT-DDNAITRLAEALRRLGAHNF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 220 --------------------DQGNEFFPATSMQIANIQAGTGSN----------------------NVIPGELFVQFNFR 257
Cdd:cd05675 230 pvrltdetayfaqmaelaggEGGALMLTAVPVLDPALAKLGPSApllnamlrntasptmldagyatNVLPGRATAEVDCR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 258 FSTELTDEMIKAQVLALLEKhqlrYTVDW-WLSGQPFL--TARGKLVDAVVNAVEHYN---EIKPQLLTtgGTSDGRFIA 331
Cdd:cd05675 310 ILPGQSEEEVLDTLDKLLGD----PDVSVeAVHLEPATesPLDSPLVDAMEAAVQAVDpgaPVVPYMSP--GGTDAKYFR 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1476918594 332 RMGAQVVELGPVNAT--------IHKINECVNAADLQLLARMYQR 368
Cdd:cd05675 384 RLGIPGYGFAPLFLPpeldytglFHGVDERVPVESLYFGVRFLDR 428
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
55-176 |
8.70e-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: 8.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 55 RGQGETLAFAGHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEE 134
Cdd:cd18669 9 GGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1476918594 135 ASAHNGTVKVVEALMARNERLDYCLVGEPSSIEVVGDVVKNG 176
Cdd:cd18669 89 VGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTP 130
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
54-373 |
7.04e-23 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 99.63 E-value: 7.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 54 WRGQGETLA---FAGHTDVVP--PGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ--HPNHTGRLA 126
Cdd:PRK08262 104 WKGSDPSLKpivLMAHQDVVPvaPGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQgfQPRRTIYLA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 127 FliTSDEEASAHnGTVKVVEALMARNERLDyCLVGEpsSIEVVGDVVKN----------GRRGSLTCNLTIHGVQGHVAY 196
Cdd:PRK08262 184 F--GHDEEVGGL-GARAIAELLKERGVRLA-FVLDE--GGAITEGVLPGvkkpvaligvAEKGYATLELTARATGGHSSM 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 197 P--------------HLADNP------------VHRAAP---FLNELV-AIEWDqgneFFPATSMQIANIQAG------- 239
Cdd:PRK08262 258 PprqtaigrlaraltRLEDNPlpmrlrgpvaemFDTLAPemsFAQRVVlANLWL----FEPLLLRVLAKSPETaamlrtt 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 240 ------TGSN--NVIPGELFVQFNFRFSTELTDEMIKAQVLALLekHQLRYTVDW-----------WLSGQPFltargKL 300
Cdd:PRK08262 334 taptmlKGSPkdNVLPQRATATVNFRILPGDSVESVLAHVRRAV--ADDRVEIEVlggnsepspvsSTDSAAY-----KL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 301 VDAVVnavehyNEIKPQL-----LTTGGTsDGRFIARMGAQVVELGPVNAT------IHKINECVNAADLQLLARMYQRI 369
Cdd:PRK08262 407 LAATI------REVFPDVvvapyLVVGAT-DSRHYSGISDNVYRFSPLRLSpedlarFHGTNERISVANYARMIRFYYRL 479
|
....
gi 1476918594 370 MEQL 373
Cdd:PRK08262 480 IENA 483
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
56-373 |
1.64e-22 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 97.16 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 56 GQGETLaFAGHTDVVPPGdadrwinppFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFvaqhpNHTG-RLAFLITSDEE 134
Cdd:PRK00466 59 GEGDIL-LASHVDTVPGY---------IEPKIEGEVIYGRGAVDAKGPLISMIIAAWLL-----NEKGiKVMVSGLADEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 135 asahnGTVKVVEALMARNERLDYCLVGEPSSievvGDVVKNGRRGSLTCNLTIHGVQGHVAYPhlADNPVHRAAPFLnel 214
Cdd:PRK00466 124 -----STSIGAKELVSKGFNFKHIIVGEPSN----GTDIVVEYRGSIQLDIMCEGTPEHSSSA--KSNLIVDISKKI--- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 215 vaIEWDQGNEFFPATSMQIANIQAGTgSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRyTVDwwlSGQPFL 294
Cdd:PRK00466 190 --IEVYKQPENYDKPSIVPTIIRAGE-SYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQECGLK-IVD---ETPPVK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 295 TA-RGKLVDAVVNAVEHYNeIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRIMEQ 372
Cdd:PRK00466 263 VSiNNPVVKALMRALLKQN-IKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLeHTNQEKITLDEIYIAVKTYMLAIEE 341
|
.
gi 1476918594 373 L 373
Cdd:PRK00466 342 L 342
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-372 |
1.66e-21 |
|
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: 94.47 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 5 VIELTQQLIR----RPSLSPDDAGCQALLIERLQAI----GFTVERMDFADTQ----NFWAWRGQGETLAFAGHTDVVP- 71
Cdd:cd08013 3 PVSLTQTLVRinssNPSLSATGGAGEAEIATYVAAWlahrGIEAHRIEGTPGRpsvvGVVRGTGGGKSLMLNGHIDTVTl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 72 ---PGDadrwinpPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNhtGRLAFLITSDEEaSAHNGTvkvvEAL 148
Cdd:cd08013 83 dgyDGD-------PLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGLR--GDVILAAVADEE-DASLGT----QEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 149 MARNERLDYCLVGEPSSIEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVA----IEWDQGNE 224
Cdd:cd08013 149 LAAGWRADAAIVTEPTNLQII-----HAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALEEyqqeLPERPVDP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 225 FFPATSMQIANIQAGTGSNNViPGELFVQFNFRFSTELTDEMIKAQVLALLEK-----HQLRYTV-DWWLSGQPFLTARG 298
Cdd:cd08013 224 LLGRASVHASLIKGGEEPSSY-PARCTLTIERRTIPGETDESVLAELTAILGElaqtvPNFSYREpRITLSRPPFEVPKE 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1476918594 299 K-LVDAVVNAVEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQ 372
Cdd:cd08013 303 HpFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGAGLHAKEEWVDVESIRQLREVLSAVVRE 377
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
32-370 |
3.09e-21 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 93.73 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 32 RLQAIGFTVERMDFAD-TQNFWAWRGQGETLaFAGHTDVVPpgDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVA 110
Cdd:PRK08737 37 RAQLPGFQVEVIDHGAgAVSLYAVRGTPKYL-FNVHLDTVP--DSPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 111 AERfvaqhpnHTGRLAFLITSDEEAsahnGTVKVVEALMARNERLDYCLVGEPSSIEVVgdvvkNGRRGSLTCNLTIHGV 190
Cdd:PRK08737 114 ANA-------GDGDAAFLFSSDEEA----NDPRCVAAFLARGIPYEAVLVAEPTMSEAV-----LAHRGISSVLMRFAGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 191 QGHVAYPH-LADNPVHRAAPFLNElvAIEWDQG---NEFFPATSMQ--IANIQAGTGSNNVIPgELFVQFNFRFSTELTD 264
Cdd:PRK08737 178 AGHASGKQdPSASALHQAMRWGGQ--ALDHVESlahARFGGLTGLRfnIGRVEGGIKANMIAP-AAELRFGFRPLPSMDV 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 265 EMIKAQVLALLEKHQLRYTVDWWLSGQP---FLTARGKLVDA----------VVNAVEHYNEikPQLLTTGGTSdgrfia 331
Cdd:PRK08737 255 DGLLATFAGFAEPAAATFEETFRGPSLPsgdIARAEERRLAArdvadaldlpIGNAVDFWTE--ASLFSAAGYT------ 326
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1476918594 332 rmgaqVVELGPVN-ATIHKINECVNAADLQLLARMYQRIM 370
Cdd:PRK08737 327 -----ALVYGPGDiAQAHTADEFVTLDQLQRYAESVHRII 361
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
12-215 |
1.08e-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: 92.76 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 12 LIRRPSLS------PDDAGCQALLIERLQAIGF-TVERMD-------FADtqnfWAWRGQGETLAFAGHTDVVPPGDADR 77
Cdd:cd05680 7 LLRIPSVSadpahkGDVRRAAEWLADKLTEAGFeHTEVLPtgghplvYAE----WLGAPGAPTVLVYGHYDVQPPDPLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 78 WINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNgtvkvVEALMARN-ERL- 155
Cdd:cd05680 83 WTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIGSPS-----LPAFLEENaERLa 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1476918594 156 -DYCLVGEPSSIEVVGDVVKNGRRGSLTCNLTIHGV-----QGHvaYPHLADNPVHRAAPFLNELV 215
Cdd:cd05680 158 aDVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPnrdlhSGS--YGGAVPNPANALARLLASLH 221
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
54-216 |
1.03e-19 |
|
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: 90.39 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 54 WRGQGETLA---FAGHTDVVP--PGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQH--PNHTGRLA 126
Cdd:cd05674 62 WEGSDPSLKpllLMAHQDVVPvnPETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGfkPRRTIILA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 127 FliTSDEEASAHNGTVKVVEALMAR-NERLDYCLVGEPSSI---EVVGD---VVKNGRRGSLTCNLTIHGVQGHVAYPhl 199
Cdd:cd05674 142 F--GHDEEVGGERGAGAIAELLLERyGVDGLAAILDEGGAVlegVFLGVpfaLPGVAEKGYMDVEITVHTPGGHSSVP-- 217
|
170
....*....|....*..
gi 1476918594 200 adnPVHRAAPFLNELVA 216
Cdd:cd05674 218 ---PKHTGIGILSEAVA 231
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
4-342 |
1.38e-19 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 89.11 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 4 PVIELTQQLIRRPSLSPDDAgcqAL------LIERLQ----AIGFTVERMDFADT---QNFWAWRGQGET-LAFAGHTDV 69
Cdd:PRK05111 6 SFIEMYRALIATPSISATDP---ALdqsnraVIDLLAgwfeDLGFNVEIQPVPGTrgkFNLLASLGSGEGgLLLAGHTDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 70 VPpGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVA---QHPnhtgrLAFLITSDEEaSAHNGTVKVVE 146
Cdd:PRK05111 83 VP-FDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLtklKKP-----LYILATADEE-TSMAGARAFAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 147 almARNERLDYCLVGEPSSIEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPV---HRAapfLNELVAI--EWDQ 221
Cdd:PRK05111 156 ---ATAIRPDCAIIGEPTSLKPV-----RAHKGHMSEAIRITGQSGHSSDPALGVNAIelmHDV---IGELLQLrdELQE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 222 G--NEFF--PATSMQIANIQAGTGSNNvIPGELFVQFNFR----FSTELTDEMIKAQVLALLEKHQLRYTVDWWLSG-QP 292
Cdd:PRK05111 225 RyhNPAFtvPYPTLNLGHIHGGDAPNR-ICGCCELHFDIRplpgMTLEDLRGLLREALAPVSERWPGRITVAPLHPPiPG 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1476918594 293 FLTARGKlvdAVVNAVEHYNEIKPQLLTTGgtSDGRFIARMGAQVVELGP 342
Cdd:PRK05111 304 YECPADH---QLVRVVEKLLGHKAEVVNYC--TEAPFIQQLGCPTLVLGP 348
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
4-373 |
1.43e-19 |
|
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: 89.47 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 4 PVIELTQQLIRRPSL--SPDDAGCQALLIERLQAIGFTVERMDFADTQNF--WAWRGQGETLA---FAGHTDVVPPGDaD 76
Cdd:TIGR01880 10 IAVTRFREYLRINTVqpNPDYAACVDFLIKQADELGLARKTIEFVPGKPVvvLTWPGSNPELPsilLNSHTDVVPVFR-E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 77 RWINPPFEPTI-RDGMLFGRGAADMKGSLAAMVVAAERFVAQ--HPNHTGRLAFLitSDEEASAHNGTVKVVEALMARNE 153
Cdd:TIGR01880 89 HWTHPPFSAFKdEDGNIYARGAQDMKCVGVQYLEAVRNLKASgfKFKRTIHISFV--PDEEIGGHDGMEKFAKTDEFKAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 154 RLDYCL-VGEPSSIEVVgdVVKNGRRGSLTCNLTIHGVQGHVA--YPHLADNPVHRAAPFLNELVAIEWD--QGNEFFP- 227
Cdd:TIGR01880 167 NLGFALdEGLASPDDVY--RVFYAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRRFRESQFQllQSNPDLAi 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 228 --ATSMQIANIQAGTGSnNVIPGELFVQFNFRFSTELTDEMIKAQVlallekhqlrytVDWW-------------LSGQP 292
Cdd:TIGR01880 245 gdVTSVNLTKLKGGVQS-NVIPSEAEAGFDIRLAPSVDFEEMENRL------------DEWCadagegvtyefsqHSGKP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 293 FLTArgklVD-------AVVNAVEHYN-EIKPQLLTtgGTSDGRFIARMGAQVVELGPVNAT---IHKINECVNAADLQL 361
Cdd:TIGR01880 312 LVTP----HDdsnpwwvAFKDAVKEMGcTFKPEILP--GSTDSRYIRAAGVPALGFSPMNNTpvlLHDHNEFLNEAVFLR 385
|
410
....*....|..
gi 1476918594 362 LARMYQRIMEQL 373
Cdd:TIGR01880 386 GIEIYQTLISAL 397
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
12-358 |
1.53e-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: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 12 LIRRPSLSPDDAG---CQALLIERLQAIGFTVER-------MDFADTQNfwawrGQGETLAFAGHTDVVPPGDADRWINP 81
Cdd:cd05681 8 LLKIPSVSAQGRGipeTADFLKEFLRRLGAEVEIfetdgnpIVYAEFNS-----GDAKTLLFYNHYDVQPAEPLELWTSD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 82 PFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNgtvkvVEALMARNERL---DYC 158
Cdd:cd05681 83 PFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPN-----LEKFVAEHADLlkaDGC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 159 L-----VGEPSSIEVVGdvvknGRRGSLTCNLTIHG--VQGHVAYPHLADNPVHRAAPFLNELVA-------------IE 218
Cdd:cd05681 158 IwegggKNPKGRPQISL-----GVKGIVYVELRVKTadFDLHSSYGAIVENPAWRLVQALNSLRDedgrvlipgfyddVR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 219 WDQGNE----------------------------------FFPATSMQIANIQAG---TGSNNVIPGELFVQFNFRfste 261
Cdd:cd05681 233 PLSEAEralidtydfdpeelrktyglkrplqvegkdplraLFTEPTCNINGIYSGytgEGSKTILPSEAFAKLDFR---- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 262 LTDEMIKAQVLALLEKH---------QLRYTvdwwLSGQPFltaRGKLVDAVVNAV-----EHYNEiKPQLL-TTGGTSD 326
Cdd:cd05681 309 LVPDQDPAKILSLLRKHldkngfddiEIHDL----LGEKPF---RTDPDAPFVQAViesakEVYGQ-DPIVLpNSAGTGP 380
|
410 420 430
....*....|....*....|....*....|....*
gi 1476918594 327 -GRFIARMGAQVVELGPVNA--TIHKINECVNAAD 358
Cdd:cd05681 381 mYPFYDALEVPVVAIGVGNAgsNAHAPNENIRIAD 415
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
6-284 |
1.54e-19 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 88.66 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 6 IELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDFADTQNFWAwrGQGETLAFAGHTDVVPPGDadrwinppfEP 85
Cdd:PRK08652 5 KELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIESDGEVINIVV--NSKAELFVEVHYDTVPVRA---------EF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 86 TIRDGMLFGRGAADMKGSLAAMVVAAER--FVAQHPNHTgrLAFLitSDEEASAHNgtvkvvEALMARNERLDYCLVGEP 163
Cdd:PRK08652 74 FVDGVYVYGTGACDAKGGVAAILLALEElgKEFEDLNVG--IAFV--SDEEEGGRG------SALFAERYRPKMAIVLEP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 164 SSIEvvgdvVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATSMQIAniqAGTGSN 243
Cdd:PRK08652 144 TDLK-----VAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPHIGIQEI---IGGSPE 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1476918594 244 NVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTV 284
Cdd:PRK08652 216 YSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEY 256
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
55-175 |
2.44e-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: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 55 RGQGETLAFAGHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEE 134
Cdd:cd03873 9 GEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1476918594 135 ASAHNGTVKVVEALMARNERLDYCLVGEPS--SIEVVGDVVKN 175
Cdd:cd03873 89 VGSGGGKGLLSKFLLAEDLKVDAAFVIDATagPILQKGVVIRN 131
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
65-334 |
5.62e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 87.60 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 65 GHTDVVPpGDADRWINPPFEPTIRDGMLFGRGAADMKGsLAAMVVAaerfVAQHPNHTGR-------LAFLitSDEEASA 137
Cdd:PRK07906 72 GHLDVVP-AEAADWSVHPFSGEIRDGYVWGRGAVDMKD-MDAMMLA----VVRHLARTGRrpprdlvFAFV--ADEEAGG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 138 HNGTVKVVEalmARNERLDYCL--VGEPS--SIEVVGD----VVKNGRRGSLTCNLTIHGVQGHVAYPHlADNPVHRAA- 208
Cdd:PRK07906 144 TYGAHWLVD---NHPELFEGVTeaISEVGgfSLTVPGRdrlyLIETAEKGLAWMRLTARGRAGHGSMVN-DDNAVTRLAe 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 209 ----------P---------FLN---ELVAIEWDQGNeffPATSM----QIANIQAGTGSN-------------NVIPGE 249
Cdd:PRK07906 220 avarigrhrwPlvltptvraFLDgvaELTGLEFDPDD---PDALLaklgPAARMVGATLRNtanptmlkagykvNVIPGT 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 250 LFVQFNFRFSTELTDEMIkAQVLALLEKHqlrytVDW-WLSGQPFLTA--RGKLVDAVVNAVEHYN---EIKPQLLtTGG 323
Cdd:PRK07906 297 AEAVVDGRFLPGREEEFL-ATVDELLGPD-----VEReWVHRDPALETpfDGPLVDAMNAALLAEDpgaRVVPYML-SGG 369
|
330
....*....|.
gi 1476918594 324 TsDGRFIARMG 334
Cdd:PRK07906 370 T-DAKAFSRLG 379
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
1-197 |
7.33e-19 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 86.55 E-value: 7.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 1 MSCPVIELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVeRMDFADtqNFWAWRGQG-ETLAFAGHTDVVPpGDAdrwi 79
Cdd:PRK04443 4 SALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREA-WVDEAG--NARGPAGDGpPLVLLLGHIDTVP-GDI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 80 npPFEptIRDGMLFGRGAADMKGSLAAMVVAAERfvAQHPNHTgRLAFLITSDEEASAHNGTvkvveALMARNERLDYCL 159
Cdd:PRK04443 76 --PVR--VEDGVLWGRGSVDAKGPLAAFAAAAAR--LEALVRA-RVSFVGAVEEEAPSSGGA-----RLVADRERPDAVI 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 1476918594 160 VGEPSSIevvgDVVKNGRRGSLTCNLTIHGVQGHVAYP 197
Cdd:PRK04443 144 IGEPSGW----DGITLGYKGRLLVTYVATSESFHSAGP 177
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
6-170 |
9.87e-19 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 87.02 E-value: 9.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 6 IELTQQLIRRPSLSP---DDAGCQALLIERLQAIGFTVERMDFADTQNFWAWRGQGE------TLAFAGHTDVVPPGDAD 76
Cdd:PRK08596 16 LELLKTLVRFETPAPparNTNEAQEFIAEFLRKLGFSVDKWDVYPNDPNVVGVKKGTesdaykSLIINGHMDVAEVSADE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 77 RWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEAsAHNGTVKVVEalmaRNERLD 156
Cdd:PRK08596 96 AWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEV-GEAGTLQCCE----RGYDAD 170
|
170
....*....|....
gi 1476918594 157 YCLVGEPSSIEVVG 170
Cdd:PRK08596 171 FAVVVDTSDLHMQG 184
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
63-373 |
1.05e-15 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 77.70 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 63 FAGHTDVVPPGDAdrwinpPFE--PTIRDGMLFGRGAADMKGSLAAMVVAAERFvAQHPnHTGRLAF--LITSDEE---- 134
Cdd:PRK07338 97 LTGHMDTVFPADH------PFQtlSWLDDGTLNGPGVADMKGGIVVMLAALLAF-ERSP-LADKLGYdvLINPDEEigsp 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 135 ASAhngtvkVVEALMARneRLDYCLVGEPSSIEvvGDVVKNgRRGSLTCNLTIHGVQGHVAY-PHLADNPVHRAAPFLNE 213
Cdd:PRK07338 169 ASA------PLLAELAR--GKHAALTYEPALPD--GTLAGA-RKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAELALA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 214 LVAIewdqgNEFFPATSMQIANIQAGtGSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKHQLRYTVDWWLSGQ-- 291
Cdd:PRK07338 238 LHAL-----NGQRDGVTVNVAKIDGG-GPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHGVSLHLHGGfg 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 292 ----PFLTARGKLVDAVVNAVEHYN-EIKPQllTTGGTSDGRFIARMGAQVVE-LGPVNATIHKINECVNAADLQLLARM 365
Cdd:PRK07338 312 rppkPIDAAQQRLFEAVQACGAALGlTIDWK--DSGGVCDGNNLAAAGLPVVDtLGVRGGNIHSEDEFVILDSLVERAQL 389
|
....*...
gi 1476918594 366 YQRIMEQL 373
Cdd:PRK07338 390 SALILMRL 397
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
11-371 |
1.16e-15 |
|
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: 77.49 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 11 QLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDFADTQNFWA------WRGQGE---TLAFAGHTDVVPPGDadrwINP 81
Cdd:cd05683 11 ELVQIDSETLHEKEISKVLKKKFENLGLSVIEDDAGKTTGGGAgnlictLKADKEevpKILFTSHMDTVTPGI----NVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 82 PfePTIRDGMLFGRG----AADMKGSLAAmVVAAERFVAQHPNHTGRLAFLITSDEEASahngtvkVVEALMARNERLD- 156
Cdd:cd05683 87 P--PQIADGYIYSDGttilGADDKAGIAA-ILEAIRVIKEKNIPHGQIQFVITVGEESG-------LVGAKALDPELIDa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 157 ---YCL--VGEPSSIeVVG----DVVkngrrgsltcNLTIHGVQGHVA-YPHLADNPVHRAAPFLNELvaiEWDQGNEFf 226
Cdd:cd05683 157 dygYALdsEGDVGTI-IVGaptqDKI----------NAKIYGKTAHAGtSPEKGISAINIAAKAISNM---KLGRIDEE- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 227 paTSMQIANIQAGTGSNnVIPGELFVQFNFRfstELTDEMIKAQVLALLE-------KHQLRYTVDWWLSGQPF-LTARG 298
Cdd:cd05683 222 --TTANIGKFQGGTATN-IVTDEVNIEAEAR---SLDEEKLDAQVKHMKEtfettakEKGAHAEVEVETSYPGFkINEDE 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1476918594 299 KLVDAVVNAVEHYnEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIME 371
Cdd:cd05683 296 EVVKLAKRAANNL-GLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAVLVVEIIK 367
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
36-134 |
2.39e-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: 77.03 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 36 IGFTVErmDFADTQNFWAWrGQG-ETLAFAGHTDVVPPGDAdrWINPPFEPTIRDGMLFGRGAADMKG----SLAAMVVA 110
Cdd:TIGR01887 47 DGFTTE--NVDNYAGYIEY-GQGeEVLGILGHLDVVPAGDG--WTSPPFEPTIKDGRIYGRGTLDDKGptiaAYYAMKIL 121
|
90 100
....*....|....*....|....
gi 1476918594 111 AERFVAqhPNHTGRlaFLITSDEE 134
Cdd:TIGR01887 122 KELGLK--LKKKIR--FIFGTDEE 141
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
6-134 |
3.39e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 76.66 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 6 IELTQQLIRRPS-LSPDDAGC------QALLIERL---QAIGFTVermdFADTQNFW--AWRGQG-ETLAFAGHTDVVPP 72
Cdd:PRK07205 14 VAAIKTLVSYPSvLNEGENGTpfgqaiQDVLEATLdlcQGLGFKT----YLDPKGYYgyAEIGQGeELLAILCHLDVVPE 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1476918594 73 GDADRWINPPFEPTIRDGMLFGRGAADMKG-SLAAMvVAAERFVAQHPNHTGRLAFLITSDEE 134
Cdd:PRK07205 90 GDLSDWQTPPFEAVEKDGCLFGRGTQDDKGpSMAAL-YAVKALLDAGVQFNKRIRFIFGTDEE 151
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
32-216 |
3.93e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 76.58 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 32 RLQAIGFT---VERMD-FADTQNFWA-WRGQGET--LAFAGHTDVVppgDADR--WINPPFEPTIRDGMLFGRGAADMKg 102
Cdd:PRK09133 68 RLKAAGFAdadIEVTGpYPRKGNLVArLRGTDPKkpILLLAHMDVV---EAKRedWTRDPFKLVEENGYFYGRGTSDDK- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 103 SLAAMVVAA------ERFVaqhPNHTGRLAFliTSDEEASAHNGtvkvVEALMARNERL---DYCL-VGEPSSIEVVGDV 172
Cdd:PRK09133 144 ADAAIWVATlirlkrEGFK---PKRDIILAL--TGDEEGTPMNG----VAWLAENHRDLidaEFALnEGGGGTLDEDGKP 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1476918594 173 VKNGRRGS----LTCNLTIHGVQGHVAYPhLADNPVHRAAPFLNELVA 216
Cdd:PRK09133 215 VLLTVQAGektyADFRLEVTNPGGHSSRP-TKDNAIYRLAAALSRLAA 261
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
10-276 |
7.76e-15 |
|
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.
Pssm-ID: 349869 [Multi-domain] Cd Length: 394 Bit Score: 75.28 E-value: 7.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 10 QQLIRRPSLSP--DDAGCQALLIERLQAIGFTVERMDFADTQ----------NFWAWRGQGE---TLAFAGHTDVVPPGD 74
Cdd:cd02697 10 QKLVRVPTDTPpgNNAPHAERTAALLQGFGFEAERHPVPEAEvraygmesitNLIVRRRYGDggrTVALNAHGDVVPPGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 75 AdrWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNGTVKVVEALMARNer 154
Cdd:cd02697 90 G--WTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGELGPGWLLRQGLTKP-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 155 lDYcLVGEPSSIEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELvaieWDQGNEFFPATS---- 230
Cdd:cd02697 166 -DL-LIAAGFSYEVV-----TAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNAL----YALNAQYRQVSSqveg 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1476918594 231 -----MQIANIQAGTGSnNVIPGELFVQFNFRFSTELTDEMIKAQVLALLE 276
Cdd:cd02697 235 ithpyLNVGRIEGGTNT-NVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIA 284
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
61-374 |
4.16e-14 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 73.27 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 61 LAFAGHTDVVPPGdADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNhtGRLAFLITSDEEASAHNG 140
Cdd:PRK08554 66 LLFMAHFDVVPVN-PEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLN--GKVIFAFTGDEEIGGAMA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 141 tVKVVEALMARNERLDYCLVGEPSSIEVV-------GDVVK--------NGRRGSLTCNLTIHGVQG-HVAY--PHLADN 202
Cdd:PRK08554 143 -MHIAEKLREEGKLPKYMINADGIGMKPIirrrkgfGVTIRvpsekvkvKGKLREQTFEIRTPVVETrHAAYflPGVDTH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 203 PVHRAAPFLNE--LVAI----EWDQGNeFFPAtSMQIANIQAGTGSN------------NVIP----------------- 247
Cdd:PRK08554 222 PLIAASHFLREsnVLAVslegKFLKGN-VVPG-EVTLTYLEPGEGEEvevdlgltrllkAIVPlvrapikaekysdygvs 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 248 ----------GELFVQFNFR---FSTELTDEMIKAQVLALLEKHQLRYTVDwWLSGQPFLTARGKLVDAVVNAVEHYNEi 314
Cdd:PRK08554 300 itpnvysfaeGKHVLKLDIRamsYSKEDIERTLKEVLEFNLPEAEVEIRTN-EKAGYLFTPPDEEIVKVALRVLKELGE- 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 315 KPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQLV 374
Cdd:PRK08554 378 DAEPVEGPGASDSRYFTPYGVKAIDFGPKGGNIHGPNEYVEIDSLKKMPEVYKRIALRLL 437
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
66-113 |
4.99e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 73.02 E-value: 4.99e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1476918594 66 HTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLaAMVVAAER 113
Cdd:PRK07907 91 HHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGI-AMHLAALR 137
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
6-106 |
9.23e-14 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 72.18 E-value: 9.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 6 IELTQQLIRRPS---LSPDDAG-------CQAL-----LIERLqaiGFTVERMD-FADTQNFwawrGQG-ETLAFAGHTD 68
Cdd:PRK07318 17 IEDLQELLRINSvrdDSKAKEGapfgpgpVKALekfleIAERD---GFKTKNVDnYAGHIEY----GEGeEVLGILGHLD 89
|
90 100 110
....*....|....*....|....*....|....*....
gi 1476918594 69 VVPPGDAdrWINPPFEPTIRDGMLFGRGAADMKG-SLAA 106
Cdd:PRK07318 90 VVPAGDG--WDTDPYEPVIKDGKIYARGTSDDKGpTMAA 126
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
58-160 |
1.19e-12 |
|
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: 68.91 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 58 GETLAFAGHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKG-SLAAMVVAAERFVAQHPNHTgrLAFLITSDEEaS 136
Cdd:cd05677 71 RKRILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGpLLAAIYAVAELFQEGELDND--VVFLIEGEEE-S 147
|
90 100
....*....|....*....|....
gi 1476918594 137 AHNGTVKVVEALMARNERLDYCLV 160
Cdd:cd05677 148 GSPGFKEVLRKNKELIGDIDWILL 171
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
4-372 |
3.93e-12 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 66.96 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 4 PVIELTQQLIRRPSLSPDDAGCQ---ALLIERLQAIGFTVERMDFADT--QNFWA-WRGQGE-TLAFAGHTDVV-PPGDA 75
Cdd:PRK06133 38 AYLDTLKELVSIESGSGDAEGLKqvaALLAERLKALGAKVERAPTPPSagDMVVAtFKGTGKrRIMLIAHMDTVyLPGML 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 76 DRwinPPFEptIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAhNGTVKVVEALMARNerl 155
Cdd:PRK06133 118 AK---QPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGS-PGSRELIAELAAQH--- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 156 DYCLVGEPSSievVGDVVKNGRRGSLTCNLTIHGVQGHV-AYPHLADNPVHRAAPFLNELVaiewDQGNEfFPATSMQIA 234
Cdd:PRK06133 189 DVVFSCEPGR---AKDALTLATSGIATALLEVKGKASHAgAAPELGRNALYELAHQLLQLR----DLGDP-AKGTTLNWT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 235 NIQAGTgSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEKH-------QLRYTVdwwlsGQPFLTARGKLVDAVVNA 307
Cdd:PRK06133 261 VAKAGT-NRNVIPASASAQADVRYLDPAEFDRLEADLQEKVKNKlvpdtevTLRFER-----GRPPLEANAASRALAEHA 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1476918594 308 VEHYNEI----KPQLLTTGGTSDGRFIARMG-AQVVE-LGPVNATIHKINECVN----AADLQLLARMyqrIMEQ 372
Cdd:PRK06133 335 QGIYGELgrrlEPIDMGTGGGTDAAFAAGSGkAAVLEgFGLVGFGAHSNDEYIElnsiVPRLYLLTRM---IMEL 406
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
6-341 |
5.31e-12 |
|
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: 66.35 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 6 IELTQQLIRRPSLSPDDAGCQALLIERLQAIGF-TVERMDFADTQNFWAWRGQGETLAFAGHTDVVPPGDAdrwinpPFE 84
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGLgDVERDGRGNVVGRLRGTGGGPALLFSAHLDTVFPGDT------PAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNGTVKvvEALMARNERLDYCLVGEPS 164
Cdd:cd03896 75 VRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEGLGDLRGAR--YLLSAHGARLDYFVVAEGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 165 sievvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDqgneFFPATSMQIANIQAGTgSNN 244
Cdd:cd03896 153 -----DGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAP----YVPKTTFAAIRGGGGT-SVN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 245 VIPGELFVQFNFRF--STELTDemIKAQVLALLEKHQLRYT-----VDWWLSGQPFLTARGKLVdaVVNAVEHYNEIKPQ 317
Cdd:cd03896 223 RIANLCSMYLDIRSnpDAELAD--VQREVEAVVSKLAAKHLrvkarVKPVGDRPGGEAQGTEPL--VNAAVAAHREVGGD 298
|
330 340
....*....|....*....|....
gi 1476918594 318 LLTTGGTSDGRFIARMGAQVVELG 341
Cdd:cd03896 299 PRPGSSSTDANPANSLGIPAVTYG 322
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
10-214 |
8.59e-12 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 66.31 E-value: 8.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 10 QQLIRRPSLSP------DDAGCQALLIERLQAIGFT-VERMD-------FADtqnfWAWRGQGETLAFAGHTDVVPPGDA 75
Cdd:PRK08201 21 KEFLRIPSISAlsehkeDVRKAAEWLAGALEKAGLEhVEIMEtaghpivYAD----WLHAPGKPTVLIYGHYDVQPVDPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 76 DRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQhpnhTGRL----AFLITSDEEASAHNgtvkVVEALMAR 151
Cdd:PRK08201 97 NLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKV----EGTLpvnvKFCIEGEEEIGSPN----LDSFVEEE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1476918594 152 NERL--DYCLVGEPSSIEVVGDVVKNGRRGSLTCNLTIHGVQGHV---AYPHLADNPVHRAAPFLNEL 214
Cdd:PRK08201 169 KDKLaaDVVLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLhsgLYGGAVPNALHALVQLLASL 236
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
11-160 |
1.99e-10 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 61.84 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 11 QLIRRPSLSPDDA---GCQA---LLIERLQAIGFTVER-------MDFADTQnfwAWRGQGETLAFAGHTDVVPPGDADR 77
Cdd:PRK09104 25 ALLRIPSISTDPAyaaDCRKaadWLVADLASLGFEASVrdtpghpMVVAHHE---GPTGDAPHVLFYGHYDVQPVDPLDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 78 WINPPFEPTIRDG-----MLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEasahNGTVKVVEALMARN 152
Cdd:PRK09104 102 WESPPFEPRIKETpdgrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEE----SGSPSLVPFLEANA 177
|
170
....*....|
gi 1476918594 153 ERL--DYCLV 160
Cdd:PRK09104 178 EELkaDVALV 187
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
31-118 |
5.18e-10 |
|
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: 60.69 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 31 ERLQAIGFTVERMDFADTQNfwawrGQGE-------------------TLAFAGHTDVVPPGDADRWINPPFEPTIRDGM 91
Cdd:cd05676 44 ERLEKLGFKVELVDIGTQTL-----PDGEelplppvllgrlgsdpskkTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGK 118
|
90 100
....*....|....*....|....*..
gi 1476918594 92 LFGRGAADMKGSLAAMVVAAERFVAQH 118
Cdd:cd05676 119 LYGRGSTDDKGPVLGWLNAIEAYQKLG 145
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
4-373 |
7.29e-10 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 59.98 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 4 PVIELTQQLIRRPSL--SPDDAGCQALLIERLQAIGFTVERMDFAdTQNFWA---WRGQGETLA---FAGHTDVVPPGDa 75
Cdd:cd05646 3 PAVTRFREYLRINTVhpNPDYDACVEFLKRQADELGLPVRVIEVV-PGKPVVvltWEGSNPELPsilLNSHTDVVPVFE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 76 DRWINPPFEPTI-RDGMLFGRGAADMKGSLAAMVVAAERFVAQ--HPNHTGRLAFLitSDEEASAHNGTVKVVEALMARN 152
Cdd:cd05646 81 EKWTHDPFSAHKdEDGNIYARGAQDMKCVGIQYLEAIRRLKASgfKPKRTIHLSFV--PDEEIGGHDGMEKFVKTEEFKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 153 ERLDYCL-VGEPSSIEVVgdVVKNGRRGSLTCNLTIHGVQGHVA--YPHLADNPVHRAAPFLNELVAIEWD--QGNEFFP 227
Cdd:cd05646 159 LNVGFALdEGLASPTEEY--RVFYGERSPWWVVITAPGTPGHGSklLENTAGEKLRKVIESIMEFRESQKQrlKSNPNLT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 228 ---ATSMQIANIQAGTgSNNVIPGELFVQFNFRFSTELTDEMIKAQV------------LALLEKHQLRY--TVD----W 286
Cdd:cd05646 237 lgdVTTVNLTMLKGGV-QMNVVPSEAEAGFDLRIPPTVDLEEFEKQIdewcaeagrgvtYEFEQKSPEKDptSLDdsnpW 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 287 WlsgqpfltargklvDAVVNAVEHYN-EIKPQLLTtgGTSDGRFIARMGAQVVELGPVNAT---IHKINECVNAADLQLL 362
Cdd:cd05646 316 W--------------AAFKKAVKEMGlKLKPEIFP--AATDSRYIRALGIPALGFSPMNNTpilLHDHNEFLNEDVFLRG 379
|
410
....*....|.
gi 1476918594 363 ARMYQRIMEQL 373
Cdd:cd05646 380 IEIYEKIIPAL 390
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
56-220 |
3.43e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 58.23 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 56 GQGETLAFAGHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGrLAFLITSDEEA 135
Cdd:PRK06446 60 GAKKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKHKLNVN-VKFLYEGEEEI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 136 SAHNgtvkvVEALMARNERL---DYCLVgEPSSIEVVG-DVVKNGRRGSLTCNLTIHGVQG--HVAYPHLADNPVHRAAP 209
Cdd:PRK06446 139 GSPN-----LEDFIEKNKNKlkaDSVIM-EGAGLDPKGrPQIVLGVKGLLYVELVLRTGTKdlHSSNAPIVRNPAWDLVK 212
|
170
....*....|.
gi 1476918594 210 FLNELVAIEWD 220
Cdd:PRK06446 213 LLSTLVDGEGR 223
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
105-271 |
3.89e-08 |
|
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: 54.65 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 105 AAMVVAAERFVAQHPNHTGRLAFLITSDEEASAhnGTVKVVE-ALMARNERLDYCL----VGEPSSieVVGdvVKNGRRG 179
Cdd:cd05664 105 AALLGAARLLVEAKDAWSGTLIAVFQPAEETGG--GAQAMVDdGLYDKIPKPDVVLaqhvMPGPAG--TVG--TRPGRFL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 180 SLTCNL--TIHGVQGHVAYPHLADNPVHRAAPFLNELVAIewdQGNEFFPATS--MQIANIQAGTgSNNVIPGELFVQFN 255
Cdd:cd05664 179 SAADSLdiTIFGRGGHGSMPHLTIDPVVMAASIVTRLQTI---VSREVDPQEFavVTVGSIQAGS-AENIIPDEAELKLN 254
|
170
....*....|....*.
gi 1476918594 256 FRFSTELTDEMIKAQV 271
Cdd:cd05664 255 VRTFDPEVREKVLNAI 270
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
105-311 |
4.55e-08 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 54.53 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 105 AAMVVAAERFVAQHPNHTGRLAFLITSDEEASAhnGTVKVVEALMARNERLDYCLVGEPSSIEVVGDVVknGRRGSLTC- 183
Cdd:cd03886 95 AMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPG--GAKAMIEEGVLENPGVDAAFGLHVWPGLPVGTVG--VRSGALMAs 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 184 ----NLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATsMQIANIQAGTGsNNVIPGELFVQFNFRFS 259
Cdd:cd03886 171 adefEITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVVSRELDPLEPAV-VTVGKFHAGTA-FNVIPDTAVLEGTIRTF 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1476918594 260 TELTDEMIKAQVLALLEK--HQLRYTVDW-WLSGQPFLTARGKLVDAVVNAVEHY 311
Cdd:cd03886 249 DPEVREALEARIKRLAEGiaAAYGATVELeYGYGYPAVINDPELTELVREAAKEL 303
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
27-310 |
2.47e-07 |
|
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: 51.96 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 27 ALLIERLQAIGFTVERmDFADTQNFWAWRGQG---ETLAFAGHTDVVPPGDADRWinpPFEPTIrDGMLFGRGaadmKGS 103
Cdd:TIGR01891 23 SLIAEALESLGIEVRR-GVGGATGVVATIGGGkpgPVVALRADMDALPIQEQTDL---PYKSTN-PGVMHACG----HDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 104 LAAMVVAAERFVAQHPNH-TGRLAFLITSDEEAsaHNGTVKVVEA-LMarnERLDYCLVGEPSSIEVVGDVVKngRRGSL 181
Cdd:TIGR01891 94 HTAILLGTAKLLKKLADLlEGTVRLIFQPAEEG--GGGATKMIEDgVL---DDVDAILGLHPDPSIPAGTVGL--RPGTI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 182 T-----CNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATsMQIANIQAGTGSnNVIPGELFVQFNF 256
Cdd:TIGR01891 167 MaaadkFEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQIVSRNVDPSRPAV-VSVGIIEAGGAP-NVIPDKASMSGTV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1476918594 257 RFSTELTDEMIKAQVLALLEK----HQLRYTVDwWLSGQPFLTARGKLVDAVVNAVEH 310
Cdd:TIGR01891 245 RSLDPEVRDQIIDRIERIVEGaaamYGAKVELN-YDRGLPAVTNDPALTQILKEVARH 301
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
56-249 |
3.67e-07 |
|
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: 51.69 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 56 GQGETLAFAG-HTDVVPpGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEE 134
Cdd:cd08012 75 VDGKTVSFVGsHMDVVT-ANPETWEFDPFSLSIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVVAVFIANEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 135 ASAHNGTvkVVEALMARNErLDYCLVGEPSSIEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNEL 214
Cdd:cd08012 154 NSEIPGV--GVDALVKSGL-LDNLKSGPLYWVDSADSQPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVMEALAEI 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1476918594 215 VAIEWDQgnefFPA------------TSMQIANIQAGTGSNNVIPGE 249
Cdd:cd08012 231 QKRFYID----FPPhpkeevygfatpSTMKPTQWSYPGGSINQIPGE 273
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
44-164 |
6.09e-07 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 51.39 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 44 DFADTQNFWA-WRGQGE---TLAFAGHTDVV--------------PPGDADRWINPPFEPTIRDGM-----LFGRGAADM 100
Cdd:COG4187 61 DPLGRKNVTAlVKGKGEskkTVILISHFDVVdvedygslkplafdPEELTEALKEIKLPEDVRKDLesgewLFGRGTMDM 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1476918594 101 KGSLAAMVVAAERFvAQHPNHTGRLAFLITSDEEASaHNGTVKVVEAL--MARNERLDY--CLVGEPS 164
Cdd:COG4187 141 KAGLALHLALLEEA-SENEEFPGNLLLLAVPDEEVN-SAGMRAAVPLLaeLKEKYGLEYklAINSEPS 206
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
180-268 |
1.69e-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: 49.59 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 180 SLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNeffpATSMQIANIQAGTGSNNVIPGELFVQFNFRFS 259
Cdd:cd08018 167 STFLEGTIKGKQAHGARPHLGINAIEAASAIVNAVNAIHLDPNI----PWSVKMTKLQAGGEATNIIPDKAKFALDLRAQ 242
|
90
....*....|
gi 1476918594 260 T-ELTDEMIK 268
Cdd:cd08018 243 SnEAMEELKE 252
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
32-136 |
6.34e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 47.99 E-value: 6.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 32 RLQAIGFTVERMDFADTQN---FWAWRGQGE---TLAFAGHTDVVPpGDADRWINP--PFEPTIRDGMLFGRGAADMKG- 102
Cdd:PRK07079 53 ALAALGFTCRIVDNPVAGGgpfLIAERIEDDalpTVLIYGHGDVVR-GYDEQWREGlsPWTLTEEGDRWYGRGTADNKGq 131
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1476918594 103 ---SLAAM-VVAAERfvaqhpnhTGRLAF----LITSDEEAS 136
Cdd:PRK07079 132 htiNLAALeQVLAAR--------GGRLGFnvklLIEMGEEIG 165
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
92-214 |
2.02e-05 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 46.57 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 92 LFGRGAADMKGSLAAMVVAAERFvAQHPNHTGRLAFLITSDEEaSAHNGTVKVVEAL--MARNERLDY--CLVGEPSSIE 167
Cdd:cd05654 126 LFGRGTMDMKSGLAVHLALLEQA-SEDEDFDGNLLLMAVPDEE-VNSRGMRAAVPALleLKKKHDLEYklAINSEPIFPQ 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1476918594 168 VVGDVVK---NGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNEL 214
Cdd:cd05654 204 YDGDQTRyiyTGSIGKILPGFLCYGKETHVGEPFAGINANLMASEITARL 253
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
184-276 |
2.76e-05 |
|
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349920 [Multi-domain] Cd Length: 367 Bit Score: 45.72 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 184 NLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATsMQIANIQAGTgSNNVIPGELFVQFNFRFSTELT 263
Cdd:cd05670 176 HIDFIGKSGHAAYPHNANDMVVAAANFVTQLQTIVSRNVDPIDGAV-VTIGKIHAGT-ARNVIAGTAHLEGTIRTLTQEM 253
|
90
....*....|...
gi 1476918594 264 DEMIKAQVLALLE 276
Cdd:cd05670 254 MELVKQRVRDIAE 266
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
177-286 |
4.64e-05 |
|
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: 45.11 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 177 RRGSLTCN-----LTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATsMQIANIQAGTgSNNVIPGELF 251
Cdd:COG1473 175 RPGPIMAAadsfeITIKGKGGHAAAPHLGIDPIVAAAQIVTALQTIVSRNVDPLDPAV-VTVGIIHGGT-APNVIPDEAE 252
|
90 100 110
....*....|....*....|....*....|....*....
gi 1476918594 252 VQFNFRFSTELTDEMIKAQVLALLEK----HQLRYTVDW 286
Cdd:COG1473 253 LEGTVRTFDPEVRELLEERIERIAEGiaaaYGATAEVEY 291
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
58-138 |
1.88e-04 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 43.09 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 58 GETLAFAGHTDVVPPGDADRWINPPFEPTIRDGMLFGRGAAD----MKGSLAAmVVAAERFVAQHPnhtgRLAFLITSDE 133
Cdd:cd05682 73 DDTVLLYGHMDKQPPFTGWDEGLGPTKPVIRGDKLYGRGGADdgyaIFASLTA-IKALQEQGIPHP----RCVVLIEACE 147
|
....*.
gi 1476918594 134 EA-SAH 138
Cdd:cd05682 148 ESgSAD 153
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
13-333 |
3.69e-04 |
|
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.
Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 42.13 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 13 IRRPSLSPDDAGCQALLIERLQAIGFTVERMDFAdtqNFWAWR----GQGETLAFAGHTDVVPpgDADRWinppfeptir 88
Cdd:cd03884 19 VTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVG---NLFGRLegtdPDAPPVLTGSHLDTVP--NGGRY---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 89 DGMLfgrgaadmkGSLAAMVVAAErfVAQH---PNHTgrLAFLITSDEEAS------------AHNGTVKVVEALMARN- 152
Cdd:cd03884 84 DGIL---------GVLAGLEALRA--LKEAgirPRRP--IEVVAFTNEEGSrfppsmlgsrafAGTLDLEELLSLRDADg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 153 -------ERLDYCLVGEPSS-------------IE-------------VVGDVVkngrrGSLTCNLTIHGVQGH---VAY 196
Cdd:cd03884 151 vslaealKAIGYDGDRPASArrpgdikayvelhIEqgpvleeeglpigVVTGIA-----GQRWLEVTVTGEAGHagtTPM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 197 PHLADnPVHRAAPFLnelVAIEwDQGNEFFPATSMQIANIQAGTGSNNVIPGELFVQFNFR-FSTELTDEM---IKAQVL 272
Cdd:cd03884 226 ALRRD-ALLAAAELI---LAVE-EIALEHGDDLVATVGRIEVKPNAVNVIPGEVEFTLDLRhPDDAVLDAMverIRAEAE 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1476918594 273 ALLEKHQLRYTVDWWLSGQPFLTArGKLVDAVVNAVEHyNEIKPQLLTTGGTSDGRFIARM 333
Cdd:cd03884 301 AIAAERGVEVEVERLWDSPPVPFD-PELVAALEAAAEA-LGLSYRRMPSGAGHDAMFMARI 359
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
79-211 |
6.24e-04 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 41.70 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 79 INPPFEPTIRdgmLFGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEAsahnGTVKVVEALMARNERL--D 156
Cdd:cd05678 106 IFSNLDPEWR---VFARAAADDKGPIMMMLAALDALKAGGIAPKFNVKIILDSEEEK----GSPSLPKAVKEYKELLaaD 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 157 YCLVGEPSSIEVVGDVVKNGRRGSLTCNLTIHGVQ-----GHvaYPHLADNPVHRAAPFL 211
Cdd:cd05678 179 ALIIMDGPAHATNKPTLTFGCRGIATATLTTYGAKvpqhsGH--YGNYAPNPAFRLSSLL 236
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
6-309 |
1.12e-03 |
|
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1L2 family contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.
Pssm-ID: 349945 [Multi-domain] Cd Length: 366 Bit Score: 40.69 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 6 IELTQQLIRRPSLSPDDAGCQALLIERLQAIGFTVERMDFADTqNFWAWRGQGET---LAFAGHTDVVPPGDADRWinpP 82
Cdd:cd08660 2 INIRRDIHEHPELGFEEVETSKKIRRWLEEEQIEILDVPQLKT-GVIAEIKGGEDgpvIAIRADIDALPIQEQTNL---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 83 FEPTIRdgmlfGRGAADMKGSLAAMVVAAERFVAQHPNHTGRLAFLITSDEEASAHNGTvKVVEALMARNerLDYCLVGE 162
Cdd:cd08660 78 FASKVD-----GT*HACGHDFHTTSIIGTA*LLNQRRAELKGTVVFIFQPAEEGAAGAR-KVLEAGVLNG--VSAIFGIH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 163 PSSIEVVGDVvkNGRRGSLTC-----NLTIHGVQGHVAYPHLADNPVHRAAP---FLNELVAIEWDQGNEffpaTSMQIA 234
Cdd:cd08660 150 NKPDLPVGTI--GVKEGPL*AsvdvfEIVIKGKGGHASIPNNSIDPIAAAGQiisGLQSVVSRNISSLQN----AVVSIT 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1476918594 235 NIQAGTgSNNVIPGELFVQFNFRFSTELTDEMIKAQVLALLEK----HQLRYTVDWWLSGQPFLTARGKLVDAVVNAVE 309
Cdd:cd08660 224 RVQGGT-AWNVIPDQAE*EGTVRAFTKEARQAVPEH*RRVAEGiaagYGCQAEFKWFPNGPSEVQNDGTLLNAFSKAAA 301
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
185-309 |
2.15e-03 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 39.95 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 185 LTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATSMqIANIQAGTgSNNVIPGELFVQFNFRFSTELTD 264
Cdd:cd08021 186 ITIKGKGGHGSMPHETVDPIVIAAQIVTALQTIVSRRVDPLDPAVVT-IGTFQGGT-SFNVIPDTVELKGTVRTFDEEVR 263
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1476918594 265 EMIKAQVLALL----EKHQLRYTVDwWLSGQPFLTARGKLVDAVVNAVE 309
Cdd:cd08021 264 EQVPKRIERIVkgicEAYGASYELE-YQPGYPVVYNDPEVTELVKKAAK 311
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
186-269 |
2.82e-03 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 39.24 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476918594 186 TIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDQGNEFFPATsMQIANIQAGTgSNNVIPGELFVQFNFR-FSTELTD 264
Cdd:cd08019 174 EVKGKGGHGSMPHQGIDAVLAAASIVMNLQSIVSREIDPLEPVV-VTVGKLNSGT-RFNVIADEAKIEGTLRtFNPETRE 251
|
....*
gi 1476918594 265 EMIKA 269
Cdd:cd08019 252 KTPEI 256
|
|
| |
