|
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: 760.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 2 SCPVIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAWRGR-GETLAFAGHTDVVPSGDADRWIN 80
Cdd:PRK13009 1 MSDVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDFGDVKNLWARRGTeGPHLCFAGHTDVVPPGDLEAWTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNGTVKVVEALMARNERLDYCLV 160
Cdd:PRK13009 81 PPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVLEWLKARGEKIDYCIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 161 GEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNEFFPPTSMQIANVQSGT 240
Cdd:PRK13009 161 GEPTSTERLGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEGNEFFPPTSLQITNIDAGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 241 GSNNVIPGDMFVQFNFRFSTELTDEMIKARVVALLEKYELRYSVDWWLSGQPFLTSRGKLVDAVVNAIEHYNEIKPQLLT 320
Cdd:PRK13009 241 GATNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDYTLEWTLSGEPFLTPPGKLVDAVVAAIEAVTGITPELST 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 490205977 321 NGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQLVA 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: 683.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAWRG-RGETLAFAGHTDVVPSGDADRWINPPFE 84
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFGGVKNLWARRGtGGPHLCFAGHTDVVPPGDLEGWSSDPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNGTVKVVEALMARNERLDYCLVGEPS 164
Cdd:cd03891 81 PTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKIDYCIVGEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 165 STEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNEFFPPTSMQIANVQSGTGSNN 244
Cdd:cd03891 161 SEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLDEGNEFFPPSSLQITNIDVGNGATN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 245 VIPGDMFVQFNFRFSTELTDEMIKARVVALLEKYELRYSVDWWLSGQPFLTSRGKLVDAVVNAIEHYNEIKPQLLTNGGT 324
Cdd:cd03891 241 VIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELSTSGGT 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 490205977 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: 614.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 5 VIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAWRGRGE-TLAFAGHTDVVPSGDADRWINPPF 83
Cdd:TIGR01246 1 VTELAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGDTKNLWATRGTGEpVLAFAGHTDVVPAGPEEQWSSPPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 84 EPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNGTVKVVEALMARNERLDYCLVGEP 163
Cdd:TIGR01246 81 EPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVETLMARDELIDYCIVGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 164 SSTEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNEFFPPTSMQIANVQSGTGSN 243
Cdd:TIGR01246 161 SSVKKLGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAIKWDEGNEFFPPTSLQITNIHAGTGAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 244 NVIPGDMFVQFNFRFSTELTDEMIKARVVALLEKYELRYSVDWWLSGQPFLTSRGKLVDAVVNAIEHYNEIKPQLLTNGG 323
Cdd:TIGR01246 241 NVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELSTGGG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 490205977 324 TSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQL 373
Cdd:TIGR01246 321 TSDGRFIALMGAEVVEFGPVNATIHKVNECVSIEDLEKLSDVYQDLLENL 370
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
5-375 |
3.01e-122 |
|
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 358.04 E-value: 3.01e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 5 VIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDF-GDTQNFWAWR---GRGETLAFAGHTDVVPSGDADRWIN 80
Cdd:COG0624 14 ALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVpPGRPNLVARRpgdGGGPTLLLYGHLDVVPPGDLELWTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAkNGTVKVVEALmARNERLDYCLV 160
Cdd:COG0624 94 DPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGS-PGARALVEEL-AEGLKADAAIV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 161 GEPSSTevvgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWD-KGNEFFPPTSMQIANVQSG 239
Cdd:COG0624 172 GEPTGV----PTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDgRADPLFGRTTLNVTGIEGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 240 TGSnNVIPGDMFVQFNFRFSTELTDEMIKARVVALLEK--YELRYSVDWWL-SGQPFLTS-RGKLVDAVVNAIEHYNEIK 315
Cdd:COG0624 248 TAV-NVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAaaPGVEVEVEVLGdGRPPFETPpDSPLVAAARAAIREVTGKE 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490205977 316 PQLLTNGGTSDGRFIAR-MGAQVVELGPVN-ATIHKINECVNAADLQLLARMYQRIMEQLVA 375
Cdd:COG0624 327 PVLSGVGGGTDARFFAEaLGIPTVVFGPGDgAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
7-369 |
1.57e-110 |
|
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like; Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.
Pssm-ID: 349944 [Multi-domain] Cd Length: 361 Bit Score: 327.33 E-value: 1.57e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 7 ELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAWRG--RGETLAFAGHTDVVPSGDADRWINPPFE 84
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVATVGggDGPVLLLNGHIDTVPPGDGDKWSFPPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASaKNGTVKVVEALMArnERLDYCLVGEPS 164
Cdd:cd08659 81 GRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVG-SDGARALLEAGYA--DRLDALIVGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 165 stevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKG-NEFFPPTSMQIANVQSGTGSn 243
Cdd:cd08659 158 -----GLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPaHPLLGPPTLNVGVINGGTQV- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 244 NVIPGDMFVQFNFRFSTELTDEMIKARVVALLEKYELRYSVDWWLSGQP--FLTSRGKLVDAVVNAIEHYNeIKPQLLTN 321
Cdd:cd08659 232 NSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPpfFTDPDHPLVQALQAAARALG-GDPVVRPF 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 490205977 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 |
4.33e-84 |
|
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 258.05 E-value: 4.33e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 62 AFAGHTDVVPSGDADRWinpPFEPTIrDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNhKGRLAFLITSDEEaSAKNGT 141
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEE-GGMGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 142 VKVVEALMARNERLDYCL---VGEPSSTE-VVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNI 217
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFglhIGEPTLLEgGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 218 EWDKGNEFFPP--TSMQIANVQSGTgsnNVIPGDMFVQFNFRFSTELTDEMIKARVVALLEK----YELRYSVDWWLSGQ 291
Cdd:pfam01546 155 VSRNVDPLDPAvvTVGNITGIPGGV---NVIPGEAELKGDIRLLPGEDLEELEERIREILEAiaaaYGVKVEVEYVEGGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 292 PFLTSRGKLVDAVVNAIEHYNEIKPQLLTNG--GTSDGRFIA-RMGAQVVELGPVNATIHKINECVNAADLQLLARMYQR 368
Cdd:pfam01546 232 PPLVNDSPLVAALREAAKELFGLKVELIVSGsmGGTDAAFFLlGVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLAR 311
|
....
gi 490205977 369 IMEQ 372
Cdd:pfam01546 312 LLLK 315
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
31-371 |
8.83e-52 |
|
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: 176.24 E-value: 8.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 31 ERLRAIGFTVEPMDFGDTQ--NFWAWRG--RGETLAFAGHTDVVPSgDADRWINPPFEPTIRDGMLFGRGAADMKGSLAA 106
Cdd:cd03894 26 DYLAALGVKSRRVPVPEGGkaNLLATLGpgGEGGLLLSGHTDVVPV-DGQKWSSDPFTLTERDGRLYGRGTCDMKGFLAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 107 MVVAAERFVAQypNHKGRLAFLITSDEEASAKnGTVKVVEALMARNERLDYCLVGEPSSTEVVgdvvkNGRRGSLTCNLT 186
Cdd:cd03894 105 VLAAVPRLLAA--KLRKPLHLAFSYDEEVGCL-GVRHLIAALAARGGRPDAAIVGEPTSLQPV-----VAHKGIASYRIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 187 IHGVQGHVAYPHLADNPVHRAAPMLAELVNI--EWDKGNE---FFPPTS-MQIANVQSGTGSnNVIPGDMFVQFNFRF-- 258
Cdd:cd03894 177 VRGRAAHSSLPPLGVNAIEAAARLIGKLRELadRLAPGLRdppFDPPYPtLNVGLIHGGNAV-NIVPAECEFEFEFRPlp 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 259 --STELTDEMIKARVVALLEKYELRYSVDWWLSGQPFLTSRGklvDAVVNAIEHYNEIKPQLLTNGGTsDGRFIARMGAQ 336
Cdd:cd03894 256 geDPEAIDARLRDYAEALLEFPEAGIEVEPLFEVPGLETDED---APLVRLAAALAGDNKVRTVAYGT-EAGLFQRAGIP 331
|
330 340 350
....*....|....*....|....*....|....*.
gi 490205977 337 VVELGPVN-ATIHKINECVNAADLQLLARMYQRIME 371
Cdd:cd03894 332 TVVCGPGSiAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
6-352 |
1.21e-51 |
|
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: 176.44 E-value: 1.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 6 IELAQQLIRRPSLSP---DDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAWR--------GRGETLAFAGHTDVVPSGD 74
Cdd:TIGR01910 1 VELLKDLISIPSVNPpggNEETIANYIKDLLREFGFSTDVIEITDDRLKVLGKvvvkepgnGNEKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 75 ADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEaSAKNGTVKVVEALMARNEr 154
Cdd:TIGR01910 81 LELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEE-SGEAGTLYLLQRGYFKDA- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 155 lDYCLVGEPSStevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIE--WDKGNE--FFP-PT 229
Cdd:TIGR01910 159 -DGVLIPEPSG----GDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEehIYARNSygFIPgPI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 230 SMQIANVQSGTGSnNVIPGDMFVQFNFRFSTELTDEMIKARVVALLEK--------YELRYSVDWwlSGQPFLTSRGKLV 301
Cdd:TIGR01910 234 TFNPGVIKGGDWV-NSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKAlsksdgwlYENEPVVKW--SGPNETPPDSRLV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 490205977 302 DAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGAQVVELGP-VNATIHKINE 352
Cdd:TIGR01910 311 KALEAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPgDLETAHQVNE 362
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
5-375 |
4.31e-48 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 167.47 E-value: 4.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 5 VIELAQQLIRRPSLSP---DDAGCQALMIERLRAIGFTVEPMDFGDT---------QNFWAWRGRGET-LAFAGHTDVVP 71
Cdd:PRK08651 8 IVEFLKDLIKIPTVNPpgeNYEEIAEFLRDTLEELGFSTEIIEVPNEyvkkhdgprPNLIARRGSGNPhLHFNGHYDVVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 72 SGDADRwINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVaqyPNHKGRLAFLITSDEEaSAKNGTVKVVEALMAr 151
Cdd:PRK08651 88 PGEGWS-VNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLD---PAGDGNIELAIVPDEE-TGGTGTGYLVEEGKV- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 152 neRLDYCLVGEPSSTEVVGdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWD-KGNEFFPPTS 230
Cdd:PRK08651 162 --TPDYVIVGEPSGLDNIC----IGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTiKSKYEYDDER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 231 MQIANVQ------SGTGSNNVIPGDMFVQFNFRFSTELTDEMIKARVVALLE----KYELRYSVDWWLSGQPFLTSRG-K 299
Cdd:PRK08651 236 GAKPTVTlggptvEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDevapELGIEVEFEITPFSEAFVTDPDsE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490205977 300 LVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGAQVVELGP-VNATIHKINECVNAADLQLLARMYQRIMEQLVA 375
Cdd:PRK08651 316 LVKALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPgELELAHAPDEYVEVKDVEKAAKVYEEVLKRLAK 392
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-370 |
7.59e-40 |
|
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: 144.45 E-value: 7.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 6 IELAQQLIRRPSLSPDDAG---CQALMIERLRAIGFTVE-----PMDFGDTQNFWAWRGrGETLAFAGHTDVVPSGDADR 77
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDNtsaIAAYIKLLLEDLGYPVElheppEEIYGVVSNIVGGRK-GKRLLFNGHYDVVPAGDGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 78 WINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNGTVKVVEALMARNerlDY 157
Cdd:cd08011 80 WTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYLLEKVRIKP---ND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 158 CLVGEPSSTevvgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEwdkgneffppTSMQIANVQ 237
Cdd:cd08011 157 VLIGEPSGS----DNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELE----------KTVNPGVIK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 238 SGTgSNNVIPGDMFVQFNFRFSTELTDEMIKARVVALLEKYE-LRYSVDWWLSGqPFLTSRGKLVDAVVNAIEHYNEIKP 316
Cdd:cd08011 223 GGV-KVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSIEeVSFEIKSFYSP-TVSNPDSEIVKKTEEAITEVLGIRP 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 490205977 317 QLLTNGGTSDGRFIARMGAQVVELGPVN-ATIHKINECVNAADLQLLARMYQRIM 370
Cdd:cd08011 301 KEVISVGASDARFYRNAGIPAIVYGPGRlGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
61-372 |
2.12e-37 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 138.48 E-value: 2.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 61 LAFAGHTDVVPSGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEaSAKNG 140
Cdd:PRK08588 62 LALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEE-VGELG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 141 TVKVVEALMARNerLDYCLVGEPSstevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNpvhrAAPMLAELVNIEwd 220
Cdd:PRK08588 141 AKQLTEKGYADD--LDALIIGEPS-----GHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVN----AIDPLLEFYNEQ-- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 221 kgNEFFpPTSMQIANVQSGT--------GSN--NVIPGDMFVQFNFRFSTELTDEMIKARVVALLEKYE----LRYSVDW 286
Cdd:PRK08588 208 --KEYF-DSIKKHNPYLGGLthvvtiinGGEqvNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNqngaAQLSLDI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 287 WLSGQPFLTSR-GKLVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGA--QVVELGP-VNATIHKINECVNAADLQLL 362
Cdd:PRK08588 285 YSNHRPVASDKdSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKPdfPVIIFGPgNNLTAHQVDEYVEKDMYLKF 364
|
330
....*....|
gi 490205977 363 ARMYQRIMEQ 372
Cdd:PRK08588 365 IDIYKEIIIQ 374
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
5-364 |
6.94e-35 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 132.96 E-value: 6.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 5 VIELAQQLIRRPSLSPDDAG---CQALMIERLRAIGFTVE-------PmdfGDTQNFWAW--------RGRGETLAFAGH 66
Cdd:PRK13013 16 LVALTQDLIRIPTLNPPGRAyreICEFLAARLAPRGFEVEliraegaP---GDSETYPRWnlvarrqgARDGDCVHFNSH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 67 TDVVPSGDAdrWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNGTVKVVE 146
Cdd:PRK13013 93 HDVVEVGHG--WTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGGVAYLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 147 ALMARNERLDYCLVGEPSSTevvgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAElvnIEwdkgNEFF 226
Cdd:PRK13013 171 QGRFSPDRVQHVIIPEPLNK----DRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAE---IE----ERLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 227 P-----PTSMQIA--NVQSGTGSNNVIPGDMFVQ-------------------FNFRFSTELTDEMIKARVVALLEK--- 277
Cdd:PRK13013 240 PllatrRTAMPVVpeGARQSTLNINSIHGGEPEQdpdytglpapcvadrcrivIDRRFLIEEDLDEVKAEITALLERlkr 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 278 ------YELRysvDWWlSGQPFLTSRGK-LVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGA--QVVELGP-VNATI 347
Cdd:PRK13013 320 arpgfaYEIR---DLF-EVLPTMTDRDApVVRSVAAAIERVLGRQADYVVSPGTYDQKHIDRIGKlkNCIAYGPgILDLA 395
|
410
....*....|....*..
gi 490205977 348 HKINECVNAADLQLLAR 364
Cdd:PRK13013 396 HQPDEWVGIADMVDSAK 412
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-247 |
1.34e-33 |
|
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: 127.43 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 5 VIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDfgdtQNFWAWRGRGE----TLAFAGHTDVVPSGDAdrWIN 80
Cdd:cd05651 2 AIELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRKG----NNVWAENGHFDegkpTLLLNSHHDTVKPNAG--WTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQyPNHKGRLAFLITSDEEASAKNGtvkvVEALMARNERLDYCLV 160
Cdd:cd05651 76 DPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSE-GPLNYNLIYAASAEEEISGKNG----IESLLPHLPPLDLAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 161 GEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHlADNPVHRAAPMLAELVNIEWDKGNEFFPPTSMQIANVQSGT 240
Cdd:cd05651 151 GEPTEMQPA-----IAEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDIQWLRDFRFDKVSPLLGPVKMTVTQINAGT 224
|
....*..
gi 490205977 241 gSNNVIP 247
Cdd:cd05651 225 -QHNVVP 230
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
65-257 |
2.05e-33 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 128.00 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 65 GHTDVVPSgDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ---YPNHkgrLAFliTSDEEAsaknGT 141
Cdd:PRK07522 71 GHTDVVPV-DGQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAplrRPLH---LAF--SYDEEV----GC 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 142 VKV---VEALMARNERLDYCLVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNI- 217
Cdd:PRK07522 141 LGVpsmIARLPERGVKPAGCIVGEPTSMRPV-----VGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLa 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490205977 218 EWDKGNEFF-----PP-TSMQIANVQSGTgSNNVIPGDMFVQFNFR 257
Cdd:PRK07522 216 DRLAAPGPFdalfdPPySTLQTGTIQGGT-ALNIVPAECEFDFEFR 260
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
5-373 |
1.30e-32 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 124.77 E-value: 1.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 5 VIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGdtqNFWAWRGRGE-TLAFAGHTDVVPSgdadrwinpPF 83
Cdd:cd05653 3 AVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEAG---NAVGGAGSGPpDVLLLGHIDTVPG---------EI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 84 EPTIRDGMLFGRGAADMKGSLAAMVVAAerfVAQYPNHKGRLAFLITSDEEASAKnGTvkvvEALMARNERLDYCLVGEP 163
Cdd:cd05653 71 PVRVEGGVLYGRGAVDAKGPLAAMILAA---SALNEELGARVVVAGLVDEEGSSK-GA----RELVRRGPRPDYIIIGEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 164 SSTEvvGDVVknGRRGSLTCNLTIHGVQGHVAyphladNPVHRAAPMLAE-LVNI-EWDKGNE--FFPPTSMQIANVQSG 239
Cdd:cd05653 143 SGWD--GITL--GYRGSLLVKIRCEGRSGHSS------SPERNAAEDLIKkWLEVkKWAEGYNvgGRDFDSVVPTLIKGG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 240 TgSNNVIPGDMFVQFNFRFSTELTDEMIKARVVALLEKYELRYSVDwwlsGQPFLTS-RGKLVDAVVNAIEHYNeIKPQL 318
Cdd:cd05653 213 E-SSNGLPQRAEATIDLRLPPRLSPEEAIALATALLPTCELEFIDD----TEPVKVSkNNPLARAFRRAIRKQG-GKPRL 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 490205977 319 LTNGGTSDGRFIA-RMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRIMEQL 373
Cdd:cd05653 287 KRKTGTSDMNVLApLWTVPIVAYGPGDSTLdHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
5-375 |
2.42e-32 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 125.44 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 5 VIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFT-VEPMDFGdtqNFWAWRGRGETL-AFAGHTDVVPSGDADRWINPP 82
Cdd:PRK13004 17 MTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFDkVEIDPMG---NVLGYIGHGKKLiAFDAHIDTVGIGDIKNWDFDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 83 FEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEasakngtvkVVEALMAR------NERLD 156
Cdd:PRK13004 94 FEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEE---------DCDGLCWRyiieedKIKPD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 157 YCLVGEPSSTEvvgdvVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAEL----VNIEWDkgnEFFPPTSMQ 232
Cdd:PRK13004 165 FVVITEPTDLN-----IYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELeelnPNLKED---PFLGKGTLT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 233 IANVQSGTGSNNVIPGDMFVQFNFRFSTELTDEMIKARVVAL--LEKYE-----LRYSVDWWlSGQPFLTSR-------- 297
Cdd:PRK13004 237 VSDIFSTSPSRCAVPDSCAISIDRRLTVGETWESVLAEIRALpaVKKANakvsmYNYDRPSY-TGLVYPTECyfptwlyp 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 298 --GKLVDAVVNAIEHYNEIKPQL-----LTNGGTSDGRFiarmGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRI 369
Cdd:PRK13004 316 edHEFVKAAVEAYKGLFGKAPEVdkwtfSTNGVSIAGRA----GIPTIGFGPGKEPLaHAPNEYTWKEQLVKAAAMYAAI 391
|
....*.
gi 490205977 370 MEQLVA 375
Cdd:PRK13004 392 PKSLLK 397
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
5-365 |
1.06e-31 |
|
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.
Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 122.70 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 5 VIELAQQLIRRPSLSPDDAGCQA---LMIERLRAIGFTVE---PMDFGDTQNF-WAWRGRGETLaFAGHTDVV-PSGDAD 76
Cdd:cd03885 1 MLDLLERLVNIESGTYDKEGVDRvaeLLAEELEALGFTVErrpLGEFGDHLIAtFKGTGGKRVL-LIGHMDTVfPEGTLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 77 RWinpPFepTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKnGTVKVVEALmARNErlD 156
Cdd:cd03885 80 FR---PF--TVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSP-GSRELIEEE-AKGA--D 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 157 YCLVGEPSSTevvGDVVKNGRRGSLTCNLTIHGVQGHV-AYPHLADNPVHRAAPMLAELVNIewdkgNEFFPPTSMQIAN 235
Cdd:cd03885 151 YVLVFEPARA---DGNLVTARKGIGRFRLTVKGRAAHAgNAPEKGRSAIYELAHQVLALHAL-----TDPEKGTTVNVGV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 236 VQSGTGSnNVIPGDMFVQFNFRFST----ELTDEMIKARV-VALLEKYELRYSVDwwLSGQPFLTSRG--KLVDAVVNAi 308
Cdd:cd03885 223 ISGGTRV-NVVPDHAEAQVDVRFATaeeaDRVEEALRAIVaTTLVPGTSVELTGG--LNRPPMEETPAsrRLLARAQEI- 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490205977 309 ehYNEIKPQLLT--NGGTSDGRFIARMGAQVVE-LGPVNATIHKINECVNAADL----QLLARM 365
Cdd:cd03885 299 --AAELGLTLDWeaTGGGSDANFTAALGVPTLDgLGPVGGGAHTEDEYLELDSLvpriKLLARL 360
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-279 |
1.94e-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 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: 121.61 E-value: 1.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 5 VIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVE--PMDFGDTQNFWAWRG--RGETLAFAGHTDVVPsgdadrwin 80
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEkqPVENKDRFNVYAYPGssRQPRVLLTSHIDTVP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 81 P--PFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEasakNGTVKVVEALMARNERLDYC 158
Cdd:cd05652 72 PfiPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEE----TGGDGMKAFNDLGLNTWDAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 159 LVGEPssTEvvGDVVKnGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKgNEFFPPTSMQIANVQS 238
Cdd:cd05652 148 IFGEP--TE--LKLAS-GHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPS-SELLGPTTLNIGRISG 221
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 490205977 239 GTGSnNVIPGDMFVQFNFRFSTELTD--EMIKARVVALLEKYE 279
Cdd:cd05652 222 GVAA-NVVPAAAEASVAIRLAAGPPEvkDIVKEAVAGILTDTE 263
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-370 |
2.59e-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: 119.49 E-value: 2.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 5 VIELAQQLIRRPSLSPDDAG------CQALMiERLRAIGF-TVEPMDFGDTQNFW-------AWRGRGETLAFAGHTDVV 70
Cdd:cd05650 3 IIELERDLIRIPAVNPESGGegekekADYLE-KKLREYGFyTLERYDAPDERGIIrpnivakIPGGNDKTLWIISHLDTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 71 PSGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ--YPNHKGRLAFLitSDEEASAKNGTVKVVEAL 148
Cdd:cd05650 82 PPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNgiTPKYNFGLLFV--ADEEDGSEYGIQYLLNKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 149 -MARNErlDYCLVgePSSTEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNE--- 224
Cdd:cd05650 160 dLFKKD--DLIIV--PDFGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFALELDELLHEKFDEkdd 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 225 -FFPPTSMQIANVQSGTGSN-NVIPGDMFVQFNFRF--STELTD--EMIKARVVALLEKY--ELRYSVDWWLSGQPFLTS 296
Cdd:cd05650 236 lFNPPYSTFEPTKKEANVPNvNTIPGYDVFYFDCRVlpTYKLDEvlKFVNKIISDFENSYgaGITYEIVQKEQAPPATPE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490205977 297 RGKLVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIM 370
Cdd:cd05650 316 DSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYIRISHIVKDAKVFAEML 389
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-364 |
3.82e-29 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 116.64 E-value: 3.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 7 ELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVE-----PMDFGDTQNFW--------------AWRGRGET---LAFA 64
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDrweidVEKLKHHPGFSpvavdyagapnvvgTHRPRGETgrsLILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 65 GHTDVVPSGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEaSAKNGTVkv 144
Cdd:cd03895 81 GHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEE-CTGNGAL-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 145 veALMARNERLDYCLVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAEL--VNIEW--- 219
Cdd:cd03895 158 --AALMRGYRADAALIPEPTELKLV-----RAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALqeLEREWnar 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 220 ---DKGNEFFP-PTSMQIANVQSGTGSNNVIPG---DMFVQFNFRFSTELTDEMIKARVVALLekyelrySVDWWLSGQP 292
Cdd:cd03895 231 kksHPHFSDHPhPINFNIGKIEGGDWPSSVPAWcvlDCRIGIYPGESPEEARREIEECVADAA-------ATDPWLSNHP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 293 F-------------LTSRGKLVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGA-QVVELGPVNATIHKINECVNAAD 358
Cdd:cd03895 304 PevewngfqaegyvLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGDiPALCYGPGSRDAHGFDESVDLES 383
|
....*.
gi 490205977 359 LQLLAR 364
Cdd:cd03895 384 LRKITK 389
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
5-368 |
1.23e-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: 114.08 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 5 VIELAQQLIRRPSLSpDDAGCQALMIER-LRAIGfTVEPMDFGDTQNFWAWRGRGETLAFAGHTDVVPSGDadrwiNPPf 83
Cdd:cd05647 1 PIELTAALVDIPSVS-GNEKPIADEIEAaLRTLP-HLEVIRDGNTVVARTERGLASRVILAGHLDTVPVAG-----NLP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 84 ePTIR-DGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKgrLAFLITSDEE-ASAKNGTVKVVEALmarNERL--DYCL 159
Cdd:cd05647 73 -SRVEeDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHD--LTLIFYDCEEvAAELNGLGRLAEEH---PEWLaaDFAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 160 VGEPSSTEVVGdvvknGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAEL-------VNIEwdkGNEFFPPTSmq 232
Cdd:cd05647 147 LGEPTDGTIEG-----GCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLaayeprtVNID---GLTYREGLN-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 233 iANVQSGTGSNNVIPGDMFVQFNFRFSTELTDEMIKARVVALLEKYELRYSVDwWLSG-------QPFLTSrgkLVDAVv 305
Cdd:cd05647 217 -AVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEIEVT-DLSPgalpgldHPVARD---LIEAV- 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490205977 306 naiehYNEIKPQLltnGGTSDGRFiARMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQR 368
Cdd:cd05647 291 -----GGKVRAKY---GWTDVARF-SALGIPAVNFGPGDPLLaHKRDEQVPVEQITACAAILRR 345
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
5-370 |
6.88e-27 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 110.32 E-value: 6.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 5 VIELAQQLIRRPSLSPDDAG------CQALMiERLRAIGFT-VEPMDFGDTQNFWAWR--------GRGE--TLAFAGHT 67
Cdd:PRK13983 7 MIELLSELIAIPAVNPDFGGegekekAEYLE-SLLKEYGFDeVERYDAPDPRVIEGVRpnivakipGGDGkrTLWIISHM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 68 DVVPSGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNGtvkvVEA 147
Cdd:PRK13983 86 DVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYG----IQY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 148 LMARNERL----DYCLV---GEPSstevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNpVHRAAPMLA----ELVN 216
Cdd:PRK13983 162 LLKKHPELfkkdDLILVpdaGNPD-----GSFIEIAEKSILWLKFTVKGKQCHASTPENGIN-AHRAAADFAleldEALH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 217 IEWDKGNEFF-PPTS-----MQIANVQsgtgSNNVIPGDMFVQFNFR-FSTELTDEMIKArVVALLEKYELR------YS 283
Cdd:PRK13983 236 EKFNAKDPLFdPPYStfeptKKEANVD----NINTIPGRDVFYFDCRvLPDYDLDEVLKD-IKEIADEFEEEygvkieVE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 284 VDWWLSGQPFLTSRGKLVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLA 363
Cdd:PRK13983 311 IVQREQAPPPTPPDSEIVKKLKRAIKEVRGIEPKVGGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYAKISNLIEDA 390
|
....*..
gi 490205977 364 RMYQRIM 370
Cdd:PRK13983 391 KVFALLL 397
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
6-221 |
8.23e-27 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 110.48 E-value: 8.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVE--PMDFGDTQNF-----WAW------------RGRGET---LAF 63
Cdd:PRK06837 23 VAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDrwSIDPDDLKSHpgagpVEIdysgapnvvgtyRPAGKTgrsLIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 64 AGHTDVVPSGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVA--AERFVAQYPnhKGRLaFLITSDEEASAKNGt 141
Cdd:PRK06837 103 QGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFAldALRAAGLAP--AARV-HFQSVIEEESTGNG- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 142 vkvveALMA--RNERLDYCLVGEPSSTEVVGDVVkngrrGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAEL--VNI 217
Cdd:PRK06837 179 -----ALSTlqRGYRADACLIPEPTGEKLVRAQV-----GVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALreLEA 248
|
....
gi 490205977 218 EWDK 221
Cdd:PRK06837 249 EWNA 252
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
56-373 |
6.94e-26 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 106.41 E-value: 6.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 56 GRGETLaFAGHTDVVPSGdadrwinppFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFvaqypNHKG-RLAFLITSDEE 134
Cdd:PRK00466 59 GEGDIL-LASHVDTVPGY---------IEPKIEGEVIYGRGAVDAKGPLISMIIAAWLL-----NEKGiKVMVSGLADEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 135 asaknGTVKVVEALMARNERLDYCLVGEPSSTEvvgDVVKnGRRGSLTCNLTIHGVQGHvayphlADNPVHRAAPMLAEL 214
Cdd:PRK00466 124 -----STSIGAKELVSKGFNFKHIIVGEPSNGT---DIVV-EYRGSIQLDIMCEGTPEH------SSSAKSNLIVDISKK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 215 VnIEWDKGNEFFPPTSMQIANVQSGTgSNNVIPGDMFVQFNFRFSTELTDEMIKARVVALLEKYELRySVDwwlSGQPFL 294
Cdd:PRK00466 189 I-IEVYKQPENYDKPSIVPTIIRAGE-SYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQECGLK-IVD---ETPPVK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 295 TS-RGKLVDAVVNAIEHYNeIKPQLLTNGGTSDGRFIARMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRIMEQ 372
Cdd:PRK00466 263 VSiNNPVVKALMRALLKQN-IKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLeHTNQEKITLDEIYIAVKTYMLAIEE 341
|
.
gi 490205977 373 L 373
Cdd:PRK00466 342 L 342
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
175-282 |
8.48e-26 |
|
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: 99.73 E-value: 8.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 175 NGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNeFFPPTSMQIANVQSGTgSNNVIPGDMFVQF 254
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGF-DFPRTTLNITGIEGGT-ATNVIPAEAEAKF 78
|
90 100
....*....|....*....|....*...
gi 490205977 255 NFRFSTELTDEMIKARVVALLEKYELRY 282
Cdd:pfam07687 79 DIRLLPGEDLEELLEEIEAILEKELPEG 106
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
8-368 |
1.07e-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: 104.36 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 8 LAQQLIRRPSLSPDDAGCQA-----LMIERLRAIGFTVEPMDFGDTQnfwawrGRGETLA-------------FAGHTDV 69
Cdd:cd05675 3 LLQELIRIDTTNSGDGTGSEtraaeVLAARLAEAGIQTEIFVVESHP------GRANLVAriggtdpsagpllLLGHIDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 70 VPSgDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNGTVKVVEALM 149
Cdd:cd05675 77 VPA-DASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDNHP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 150 ARNERLDYCL--VGEPSSTEVVGDV---VKNGRRGSLTCNLTIHGVQGHVAYPHlADNPVHRAAPMLAELVNIEW----D 220
Cdd:cd05675 156 ELFDGATFALneGGGGSLPVGKGRRlypIQVAEKGIAWMKLTVRGRAGHGSRPT-DDNAITRLAEALRRLGAHNFpvrlT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 221 KGNEFF------------------PPTSMQIANVQSGTG--------------------SNNVIPGDMFVQFNFRFSTEL 262
Cdd:cd05675 235 DETAYFaqmaelaggeggalmltaVPVLDPALAKLGPSApllnamlrntasptmldagyATNVLPGRATAEVDCRILPGQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 263 TDEMIKARVVALLEKYELRYSvdwWLSGQPFLTS--RGKLVDAVVNAIEHYN---EIKPQLLTngGTSDGRFIARMGAQV 337
Cdd:cd05675 315 SEEEVLDTLDKLLGDPDVSVE---AVHLEPATESplDSPLVDAMEAAVQAVDpgaPVVPYMSP--GGTDAKYFRRLGIPG 389
|
410 420 430
....*....|....*....|....*....|....*....
gi 490205977 338 VELGPVNAT--------IHKINECVNAADLQLLARMYQR 368
Cdd:cd05675 390 YGFAPLFLPpeldytglFHGVDERVPVESLYFGVRFLDR 428
|
|
| PRK06915 |
PRK06915 |
peptidase; |
6-193 |
1.86e-24 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 103.62 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTV---EP---------------MDFGDTQNFWA-WRGRGE--TLAFA 64
Cdd:PRK06915 20 VKLLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLdiwEPsfkklkdhpyfvsprTSFSDSPNIVAtLKGSGGgkSMILN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 65 GHTDVVPSGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEaSAKNGTVKV 144
Cdd:PRK06915 100 GHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEE-SGGAGTLAA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490205977 145 VEalmaRNERLDYCLVGEPSSTEVvgdVVKngRRGSLTCNLTIHGVQGH 193
Cdd:PRK06915 179 IL----RGYKADGAIIPEPTNMKF---FPK--QQGSMWFRLHVKGKAAH 218
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-278 |
2.58e-24 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 102.50 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGF---TVEPMDfgdtqNFWAWRGRGET-LAFAGHTDVVPSGDADRWINP 81
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGFdevEIDPMG-----NVIGYIGGGKKkILFDGHIDTVGIGNIDNWKFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 82 PFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFV-AQYPNHKGRLAFLITSDEEasakngtvkVVEALMAR------NER 154
Cdd:cd05649 76 PYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKdLGLRDFAYTILVAGTVQEE---------DCDGVCWQyiskadKIK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 155 LDYCLVGEPSSTEvvgdvVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKG-NEFFPPTSMQI 233
Cdd:cd05649 147 PDFVVSGEPTDGN-----IYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFPeAPFLGRGTLTV 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490205977 234 ANVQSGTGSNNVIPGDMFVQFNFRFSTELTDEMIKA--RVVALLEKY 278
Cdd:cd05649 222 TDIFSTSPSRCAVPDSCRISIDRRLTVGETWEGCLEeiRALPAVKKY 268
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
54-373 |
1.16e-23 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 101.94 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 54 WRGRGETLA---FAGHTDVVP--SGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ--YPNHKGRLA 126
Cdd:PRK08262 104 WKGSDPSLKpivLMAHQDVVPvaPGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQgfQPRRTIYLA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 127 FliTSDEEASAKnGTVKVVEALMARNERLDyCLVGEpsSTEVVGDVVKN----------GRRGSLTCNLTIHGVQGHVAY 196
Cdd:PRK08262 184 F--GHDEEVGGL-GARAIAELLKERGVRLA-FVLDE--GGAITEGVLPGvkkpvaligvAEKGYATLELTARATGGHSSM 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 197 P--------------HLADNP------------VHRAAP--------MLAELVNIEWDKGNEFF--PPTSmqiANVQSGT 240
Cdd:PRK08262 258 PprqtaigrlaraltRLEDNPlpmrlrgpvaemFDTLAPemsfaqrvVLANLWLFEPLLLRVLAksPETA---AMLRTTT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 241 ------GSN--NVIPGDMFVQFNFRFSTELTDEMIKARVVALLEKYELRYSVDWWLSGQPFLTSRGKLVDAVVNA-IEHY 311
Cdd:PRK08262 335 aptmlkGSPkdNVLPQRATATVNFRILPGDSVESVLAHVRRAVADDRVEIEVLGGNSEPSPVSSTDSAAYKLLAAtIREV 414
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490205977 312 NE---IKPQLLTnGGTsDGRFIARMGAQVVELGPVNAT------IHKINECVNAADLQLLARMYQRIMEQL 373
Cdd:PRK08262 415 FPdvvVAPYLVV-GAT-DSRHYSGISDNVYRFSPLRLSpedlarFHGTNERISVANYARMIRFYYRLIENA 483
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
33-359 |
3.83e-23 |
|
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation.
Pssm-ID: 349888 [Multi-domain] Cd Length: 426 Bit Score: 99.71 E-value: 3.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 33 LRAIGFTVEPMDFGDTQNF-WAWRGRGE---TLAFAGHTDVVPSGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMV 108
Cdd:cd03893 34 LRRLGFTVEIVDTSNGAPVvFAEFPGAPgapTVLLYGHYDVQPAGDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 109 VAAERFVAQYPNHKGRLAFLITSDEEAsaknGTVKVVEALMARNERL--DYCLVGEPSSTEVVGDVVKNGRRGSLTCNLT 186
Cdd:cd03893 114 AALRALMQQGGDLPVNVKFIIEGEEES----GSPSLDQLVEAHRDLLaaDAIVISDSTWVGQEQPTLTYGLRGNANFDVE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 187 IHGVQGHV---AYPHLADNPVHRAAPMLAELVNiewDKGN----------------------------EFFPPTSMQIA- 234
Cdd:cd03893 190 VKGLDHDLhsgLYGGVVPDPMTALAQLLASLRD---ETGRilvpglydavrelpeeefrldagvleevEIIGGTTGSVAe 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 235 --------NV------QSGTGSNNVIPGDMFVQFNFRFSTELTDEMIKARVVALLEK---YELRYSVDWWLSGQPFLTS- 296
Cdd:cd03893 267 rlwtrpalTVlgidggFPGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLEAHLEKhapSGAKVTVSYVEGGMPWRSDp 346
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490205977 297 RGKLVDAVVNAIEHYNEIKPQLLTNGGT--SDGRFIARMGAQVVELGPVNAT--IHKINECVNAADL 359
Cdd:cd03893 347 SDPAYQAAKDALRTAYGVEPPLTREGGSipFISVLQEFPQAPVLLIGVGDPDdnAHSPNESLRLGNY 413
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
55-176 |
7.48e-23 |
|
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 94.81 E-value: 7.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 55 RGRGETLAFAGHTDVVPSGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEE 134
Cdd:cd18669 9 GGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 490205977 135 ASAKNGTVKVVEALMARNERLDYCLVGEPSSTEVVGDVVKNG 176
Cdd:cd18669 89 VGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTP 130
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
6-284 |
9.85e-23 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 97.52 E-value: 9.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAwRGRGEtLAFAGHTDVVPsgdadrwinPPFEP 85
Cdd:PRK08652 5 KELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIESDGEVINIVV-NSKAE-LFVEVHYDTVP---------VRAEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 86 TIRDGMLFGRGAADMKGSLAAMVVAAERFvaQYPNHKGRLAFLITSDEEASAKNgtvkvvEALMARNERLDYCLVGEPSS 165
Cdd:PRK08652 74 FVDGVYVYGTGACDAKGGVAAILLALEEL--GKEFEDLNVGIAFVSDEEEGGRG------SALFAERYRPKMAIVLEPTD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 166 TEVvgdvvKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNEFFPPTSMQIAnvqSGTGSNNV 245
Cdd:PRK08652 146 LKV-----AIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPHIGIQEI---IGGSPEYS 217
|
250 260 270
....*....|....*....|....*....|....*....
gi 490205977 246 IPGDMFVQFNFRFSTELTDEMIKARVVALLEKYELRYSV 284
Cdd:PRK08652 218 IPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEY 256
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
5-366 |
1.22e-22 |
|
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: 98.47 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 5 VIELAQQLIRRPS-LSPDDAGC-------QAL--MIERLRAIGFTVEPMDfgdtqNFWA---WRGRGETLAFAGHTDVVP 71
Cdd:cd03888 10 ILEDLKELVAIPSvRDEATEGApfgegprKALdkFLDLAKRLGFKTKNID-----NYAGyaeYGEGEEVLGILGHLDVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 72 SGDAdrWINPPFEPTIRDGMLFGRGAADMKG----SLAAMVVAAE---------RFV----------------------- 115
Cdd:cd03888 85 AGEG--WTTDPFKPVIKDGKLYGRGTIDDKGptiaALYALKILKDlglplkkkiRLIfgtdeetgwkciehyfeheeypd 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 116 ------AQYP---NHKGRLAFLITSDEeasaKNGTVKVVEAL---MARNERLDYC-LVGEPSSTEVVGDVVKNGRRGSLT 182
Cdd:cd03888 163 fgftpdAEFPvinGEKGIVTVDLTFKI----DDDKGYRLISIkggEATNMVPDKAeAVIPGKDKEELALSAATDLKGNIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 183 CN-----LTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKG-----NEFFPPTS------MQIANVQSG-----TG 241
Cdd:cd03888 239 IDdggveLTVTGKSAHASAPEKGVNAITLLAKFLAELNKDGNDKDfikflAKNLHEDYngkklgINFEDEVMGeltlnPG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 242 SNNVIPGDMFVQFNFRFSTELTDEMIKARVVALLEKYELRYSVDwwLSGQPFLTSR-GKLVDAVVNAIEHYNEIKPQLLT 320
Cdd:cd03888 319 IITLDDGKLELGLNVRYPVGTSAEDIIKQIEEALEKYGVEVEGH--KHQKPLYVPKdSPLVKTLLKVYEEQTGKEGEPVA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 490205977 321 NGGTSDGRFIARMgaqvVELGP----VNATIHKINECVNAADLQLLARMY 366
Cdd:cd03888 397 IGGGTYARELPNG----VAFGPefpgQKDTMHQANEFIPIDDLIKALAIY 442
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
10-257 |
3.47e-21 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 93.73 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 10 QQLIRRPSLSPDDAGCQALMIERLRAI--GFTVEPMDFGD-TQNFWAWRGRGETLaFAGHTDVVPsgDADRWINPPFEPT 86
Cdd:PRK08737 13 QALVSFDTRNPPRAITTGGIFDYLRAQlpGFQVEVIDHGAgAVSLYAVRGTPKYL-FNVHLDTVP--DSPHWSADPHVMR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 87 IRDGMLFGRGAADMKGSLAAMVVAAERFVAQYpnhkgrlAFLITSDEEAsaknGTVKVVEALMARNERLDYCLVGEPSST 166
Cdd:PRK08737 90 RTDDRVIGLGVCDIKGAAAALLAAANAGDGDA-------AFLFSSDEEA----NDPRCVAAFLARGIPYEAVLVAEPTMS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 167 EVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPH-LADNPVHRAAPMLAELVNIEWDKGNEFFPPTS---MQIANVQSGTGS 242
Cdd:PRK08737 159 EAV-----LAHRGISSVLMRFAGRAGHASGKQdPSASALHQAMRWGGQALDHVESLAHARFGGLTglrFNIGRVEGGIKA 233
|
250
....*....|....*
gi 490205977 243 NNVIPGdMFVQFNFR 257
Cdd:PRK08737 234 NMIAPA-AELRFGFR 247
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
6-358 |
6.17e-21 |
|
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: 93.56 E-value: 6.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 6 IELAQQLIRRPSLSPDDAG---CQALMIERLRAIGFTVE-------PMDFGDTQNfwawrGRGETLAFAGHTDVVPSGDA 75
Cdd:cd05681 2 LEDLRDLLKIPSVSAQGRGipeTADFLKEFLRRLGAEVEifetdgnPIVYAEFNS-----GDAKTLLFYNHYDVQPAEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 76 DRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNgtvkvVEALMARNERL 155
Cdd:cd05681 77 ELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPN-----LEKFVAEHADL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 156 ---DYCL-----VGEPSSTEVVGdvvknGRRGSLTCNLTIHG--VQGHVAYPHLADNPVHRAAPMLAELVN--------- 216
Cdd:cd05681 152 lkaDGCIwegggKNPKGRPQISL-----GVKGIVYVELRVKTadFDLHSSYGAIVENPAWRLVQALNSLRDedgrvlipg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 217 ----IEWDKGNE-----------------------------------FFPPTsMQIANVQSG---TGSNNVIPGDMFVQF 254
Cdd:cd05681 227 fyddVRPLSEAEralidtydfdpeelrktyglkrplqvegkdplralFTEPT-CNINGIYSGytgEGSKTILPSEAFAKL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 255 NFRfsteLTDEMIKARVVALLEKY---------ELRYSvdwwLSGQPFLTSRG-KLVDAVVN-AIEHYNEiKPQLLTNGG 323
Cdd:cd05681 306 DFR----LVPDQDPAKILSLLRKHldkngfddiEIHDL----LGEKPFRTDPDaPFVQAVIEsAKEVYGQ-DPIVLPNSA 376
|
410 420 430
....*....|....*....|....*....|....*....
gi 490205977 324 TSD--GRFIARMGAQVVELGPVNA--TIHKINECVNAAD 358
Cdd:cd05681 377 GTGpmYPFYDALEVPVVAIGVGNAgsNAHAPNENIRIAD 415
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
1-197 |
5.85e-20 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 89.63 E-value: 5.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 1 MSCPVIELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGdtqNFWAWRG-RGETLAFAGHTDVVPsGDAdrwi 79
Cdd:PRK04443 4 SALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREAWVDEAG---NARGPAGdGPPLVLLLGHIDTVP-GDI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 80 npPFEptIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPnhkGRLAFLITSDEEASAKNGTvkvveALMARNERLDYCL 159
Cdd:PRK04443 76 --PVR--VEDGVLWGRGSVDAKGPLAAFAAAAARLEALVR---ARVSFVGAVEEEAPSSGGA-----RLVADRERPDAVI 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 490205977 160 VGEPSSTevvgDVVKNGRRGSLTCNLTIHGVQGHVAYP 197
Cdd:PRK04443 144 IGEPSGW----DGITLGYKGRLLVTYVATSESFHSAGP 177
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
12-215 |
7.24e-20 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 90.45 E-value: 7.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 12 LIRRPSLS------PDDAGCQALMIERLRAIGF-TVE-------PMDFGDtqnfWAWRGRGETLAFAGHTDVVPSGDADR 77
Cdd:cd05680 7 LLRIPSVSadpahkGDVRRAAEWLADKLTEAGFeHTEvlptgghPLVYAE----WLGAPGAPTVLVYGHYDVQPPDPLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 78 WINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNgtvkvVEALMARN-ERL- 155
Cdd:cd05680 83 WTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIGSPS-----LPAFLEENaERLa 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490205977 156 -DYCLVGEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQ-----GHvaYPHLADNPVHRAAPMLAELV 215
Cdd:cd05680 158 aDVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNrdlhsGS--YGGAVPNPANALARLLASLH 221
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
6-170 |
4.20e-19 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 88.17 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 6 IELAQQLIRRPSLSP---DDAGCQALMIERLRAIGFTVEPMDFGDTQNFWAWRGRGE------TLAFAGHTDVVPSGDAD 76
Cdd:PRK08596 16 LELLKTLVRFETPAPparNTNEAQEFIAEFLRKLGFSVDKWDVYPNDPNVVGVKKGTesdaykSLIINGHMDVAEVSADE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 77 RWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEAsAKNGTVKVVEalmaRNERLD 156
Cdd:PRK08596 96 AWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEV-GEAGTLQCCE----RGYDAD 170
|
170
....*....|....
gi 490205977 157 YCLVGEPSSTEVVG 170
Cdd:PRK08596 171 FAVVVDTSDLHMQG 184
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
56-372 |
4.21e-19 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349935 [Multi-domain] Cd Length: 379 Bit Score: 87.53 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 56 GRGETLAFAGHTDVVPSgdaDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPnhKGRLAFLITSDEEa 135
Cdd:cd08013 66 GGGKSLMLNGHIDTVTL---DGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGL--RGDVILAAVADEE- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 136 SAKNGTvkvvEALMARNERLDYCLVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAEL- 214
Cdd:cd08013 140 DASLGT----QEVLAAGWRADAAIVTEPTNLQII-----HAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALe 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 215 ---VNIEWDKGNEFFPPTSMQIANVQSGTGSNNViPGDMFVQFNFRFSTELTDEMIKARVVALLEK---------YELRY 282
Cdd:cd08013 211 eyqQELPERPVDPLLGRASVHASLIKGGEEPSSY-PARCTLTIERRTIPGETDESVLAELTAILGElaqtvpnfsYREPR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 283 SVdwwLSGQPFLTSRGK-LVDAVVNAIEHYNEIKPQLLTNGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQL 361
Cdd:cd08013 290 IT---LSRPPFEVPKEHpFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGAGLHAKEEWVDVESIRQ 366
|
330
....*....|.
gi 490205977 362 LARMYQRIMEQ 372
Cdd:cd08013 367 LREVLSAVVRE 377
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
4-342 |
7.49e-19 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 86.80 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 4 PVIELAQQLIRRPSLS---PD-DAGCQALmIERL----RAIGFTVEPM---DFGDTQNFWAWRGRGET-LAFAGHTDVVP 71
Cdd:PRK05111 6 SFIEMYRALIATPSISatdPAlDQSNRAV-IDLLagwfEDLGFNVEIQpvpGTRGKFNLLASLGSGEGgLLLAGHTDTVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 72 SgDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKgrLAFLITSDEEaSAKNGTVKVVEalmAR 151
Cdd:PRK05111 85 F-DEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKP--LYILATADEE-TSMAGARAFAE---AT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 152 NERLDYCLVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPV---HRAAPMLAELVNiEWDKG--NEFF 226
Cdd:PRK05111 158 AIRPDCAIIGEPTSLKPV-----RAHKGHMSEAIRITGQSGHSSDPALGVNAIelmHDVIGELLQLRD-ELQERyhNPAF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 227 P---PTsMQIANVQSGTGSNNvIPGDMFVQFNFR----FSTELTDEMIKARVVALLEKYELRYSVDWWLSG-QPFLTSRg 298
Cdd:PRK05111 232 TvpyPT-LNLGHIHGGDAPNR-ICGCCELHFDIRplpgMTLEDLRGLLREALAPVSERWPGRITVAPLHPPiPGYECPA- 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 490205977 299 klvDA-VVNAIEHYNEIKPQLLtNGGTsDGRFIARMGAQVVELGP 342
Cdd:PRK05111 309 ---DHqLVRVVEKLLGHKAEVV-NYCT-EAPFIQQLGCPTLVLGP 348
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
58-175 |
7.99e-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: 83.63 E-value: 7.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 58 GETLAFAGHTDVVPSGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASA 137
Cdd:cd03873 12 GKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGS 91
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 490205977 138 KNGTVKVVEALMARNERLDYCLVGEPS--STEVVGDVVKN 175
Cdd:cd03873 92 GGGKGLLSKFLLAEDLKVDAAFVIDATagPILQKGVVIRN 131
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
54-229 |
1.62e-17 |
|
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: 83.46 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 54 WRGRGETLA---FAGHTDVVP--SGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQypNHKGR---- 124
Cdd:cd05674 62 WEGSDPSLKpllLMAHQDVVPvnPETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKR--GFKPRrtii 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 125 LAFliTSDEEASAKNGTVKVVEALMAR-NERLDYCLVGEPS---STEVVGD---VVKNGRRGSLTCNLTIHGVQGHVAYP 197
Cdd:cd05674 140 LAF--GHDEEVGGERGAGAIAELLLERyGVDGLAAILDEGGavlEGVFLGVpfaLPGVAEKGYMDVEITVHTPGGHSSVP 217
|
170 180 190
....*....|....*....|....*....|...
gi 490205977 198 hladnPVHRAAPMLAELV-NIEwdkgNEFFPPT 229
Cdd:cd05674 218 -----PKHTGIGILSEAVaALE----ANPFPPK 241
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
4-373 |
1.73e-16 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 80.22 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 4 PVIELAQQLIRRPSL--SPDDAGCQALMIERLRAIGFTVEPMDF--GDTQNFWAWRGRGETLA---FAGHTDVVPSGDaD 76
Cdd:TIGR01880 10 IAVTRFREYLRINTVqpNPDYAACVDFLIKQADELGLARKTIEFvpGKPVVVLTWPGSNPELPsilLNSHTDVVPVFR-E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 77 RWINPPFEPTI-RDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNGTVKVVEALMARNERL 155
Cdd:TIGR01880 89 HWTHPPFSAFKdEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEKFAKTDEFKALNL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 156 DYCL-VGEPSSTEVVgdVVKNGRRGSLTCNLTIHGVQGHVA--YPHLADNPVHRAAPMLAELVNIEWD--KGNEFFPP-- 228
Cdd:TIGR01880 169 GFALdEGLASPDDVY--RVFYAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRRFRESQFQllQSNPDLAIgd 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 229 -TSMQIANVQSGTGSnNVIPGDMFVQFNFRFSTELTDEMIKARVV----ALLEKYELRYSVDWwlsGQPFLTSrgklVD- 302
Cdd:TIGR01880 247 vTSVNLTKLKGGVQS-NVIPSEAEAGFDIRLAPSVDFEEMENRLDewcaDAGEGVTYEFSQHS---GKPLVTP----HDd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 303 ------AVVNAIEHYN-EIKPQLLTngGTSDGRFIARMGAQVVELGPVNAT---IHKINECVNAADLQLLARMYQRIMEQ 372
Cdd:TIGR01880 319 snpwwvAFKDAVKEMGcTFKPEILP--GSTDSRYIRAAGVPALGFSPMNNTpvlLHDHNEFLNEAVFLRGIEIYQTLISA 396
|
.
gi 490205977 373 L 373
Cdd:TIGR01880 397 L 397
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
65-219 |
3.08e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 79.51 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 65 GHTDVVPSgDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVA--QYPNHKGRLAFLitSDEEASAKNGTV 142
Cdd:PRK07906 72 GHLDVVPA-EAADWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARtgRRPPRDLVFAFV--ADEEAGGTYGAH 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 143 KVVEalmARNERLDYClvgepssTEVVGDV---------------VKNGRRGSLTCNLTIHGVQGHVAYPHlADNPVHRA 207
Cdd:PRK07906 149 WLVD---NHPELFEGV-------TEAISEVggfsltvpgrdrlylIETAEKGLAWMRLTARGRAGHGSMVN-DDNAVTRL 217
|
170
....*....|..
gi 490205977 208 APMLAELVNIEW 219
Cdd:PRK07906 218 AEAVARIGRHRW 229
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
29-134 |
8.58e-16 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 78.19 E-value: 8.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 29 MIERLRAIGFTVEpmDFGDTQNFWAWrGRG-ETLAFAGHTDVVPSGDAdrWINPPFEPTIRDGMLFGRGAADMKG----S 103
Cdd:TIGR01887 40 FLEIAKRDGFTTE--NVDNYAGYIEY-GQGeEVLGILGHLDVVPAGDG--WTSPPFEPTIKDGRIYGRGTLDDKGptiaA 114
|
90 100 110
....*....|....*....|....*....|.
gi 490205977 104 LAAMVVAAErfvAQYPNHKgRLAFLITSDEE 134
Cdd:TIGR01887 115 YYAMKILKE---LGLKLKK-KIRFIFGTDEE 141
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
56-374 |
2.79e-15 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 76.74 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 56 GRGETLaFAGHTDVVPSGdADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQypNHKGRLAFLITSDEEA 135
Cdd:PRK08554 62 GKPKLL-FMAHFDVVPVN-PEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKE--PLNGKVIFAFTGDEEI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 136 SAKNGtVKVVEALMARNERLDYCLVGEPSSTEVV-------GDVVK--------NGRRGSLTCNLTIHGVQG-HVAY--- 196
Cdd:PRK08554 138 GGAMA-MHIAEKLREEGKLPKYMINADGIGMKPIirrrkgfGVTIRvpsekvkvKGKLREQTFEIRTPVVETrHAAYflp 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 197 -----PHLADNPVHRAAPMLAELVNIEWDKGNEFfpPTSMQIANVQSGTGSN------------NVIP------------ 247
Cdd:PRK08554 217 gvdthPLIAASHFLRESNVLAVSLEGKFLKGNVV--PGEVTLTYLEPGEGEEvevdlgltrllkAIVPlvrapikaekys 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 248 ---------------GDMFVQFNFR---FSTELTDEMIKARVVALLEKYELRYSVDwWLSGQPFLTSRGKLVDAVVNAIE 309
Cdd:PRK08554 295 dygvsitpnvysfaeGKHVLKLDIRamsYSKEDIERTLKEVLEFNLPEAEVEIRTN-EKAGYLFTPPDEEIVKVALRVLK 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490205977 310 HYNEiKPQLLTNGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQLV 374
Cdd:PRK08554 374 ELGE-DAEPVEGPGASDSRYFTPYGVKAIDFGPKGGNIHGPNEYVEIDSLKKMPEVYKRIALRLL 437
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
6-134 |
4.30e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 76.27 E-value: 4.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 6 IELAQQLIRRPS-LSPDDAGC---QAL------MIERLRAIGFTVepmdFGDTQNFW--AWRGRG-ETLAFAGHTDVVPS 72
Cdd:PRK07205 14 VAAIKTLVSYPSvLNEGENGTpfgQAIqdvleaTLDLCQGLGFKT----YLDPKGYYgyAEIGQGeELLAILCHLDVVPE 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490205977 73 GDADRWINPPFEPTIRDGMLFGRGAADMKG-SLAAMvVAAERFVAQYPNHKGRLAFLITSDEE 134
Cdd:PRK07205 90 GDLSDWQTPPFEAVEKDGCLFGRGTQDDKGpSMAAL-YAVKALLDAGVQFNKRIRFIFGTDEE 151
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
27-208 |
6.36e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 75.81 E-value: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 27 ALMIERLRAIGF-----TVEPmDFGDTQNFWA-WRGRGET--LAFAGHTDVVpsgDADR--WINPPFEPTIRDGMLFGRG 96
Cdd:PRK09133 63 EAMAARLKAAGFadadiEVTG-PYPRKGNLVArLRGTDPKkpILLLAHMDVV---EAKRedWTRDPFKLVEENGYFYGRG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 97 AADMKgSLAAMVVAA------ERFVaqyPNHKGRLAFliTSDEEASAKNGTVKVVE-------ALMARNE----RLDYcl 159
Cdd:PRK09133 139 TSDDK-ADAAIWVATlirlkrEGFK---PKRDIILAL--TGDEEGTPMNGVAWLAEnhrdlidAEFALNEggggTLDE-- 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490205977 160 VGEPSSTEVVGdvvknGRRGSLTCNLTIHGVQGHVAYPhLADNPVHRAA 208
Cdd:PRK09133 211 DGKPVLLTVQA-----GEKTYADFRLEVTNPGGHSSRP-TKDNAIYRLA 253
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
11-113 |
5.08e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 73.02 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 11 QLIRRPSLSPD-------DAGCQALmIERLRAIGF-TVEPMDFGDTQNFWAWR----GRGETLAFAgHTDVVPSGDADRW 78
Cdd:PRK07907 26 ELVRIPSVAADpfrreevARSAEWV-ADLLREAGFdDVRVVSADGAPAVIGTRpappGAPTVLLYA-HHDVQPPGDPDAW 103
|
90 100 110
....*....|....*....|....*....|....*
gi 490205977 79 INPPFEPTIRDGMLFGRGAADMKGSLaAMVVAAER 113
Cdd:PRK07907 104 DSPPFELTERDGRLYGRGAADDKGGI-AMHLAALR 137
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
57-160 |
9.93e-14 |
|
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex.
Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 71.99 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 57 RGETLAFAGHTDVVPSGDADRWINPPFEPTIRDGMLFGRGAADMKG-SLAAMVVAAERFVAQYPNHKgrLAFLITSDEEA 135
Cdd:cd05677 70 KRKRILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGpLLAAIYAVAELFQEGELDND--VVFLIEGEEES 147
|
90 100
....*....|....*....|....*
gi 490205977 136 SAKnGTVKVVEALMARNERLDYCLV 160
Cdd:cd05677 148 GSP-GFKEVLRKNKELIGDIDWILL 171
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
63-373 |
1.79e-13 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 71.15 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 63 FAGHTDVVPSGDAdrwinpPFE--PTIRDGMLFGRGAADMKGSLAAMVVAAERFvAQYPnHKGRLAF--LITSDEE---- 134
Cdd:PRK07338 97 LTGHMDTVFPADH------PFQtlSWLDDGTLNGPGVADMKGGIVVMLAALLAF-ERSP-LADKLGYdvLINPDEEigsp 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 135 ASAkngtvkVVEALMARneRLDYCLVGEPSSTEvvGDVVKNgRRGSLTCNLTIHGVQGHVAY-PHLADNPVHRAAPMLAE 213
Cdd:PRK07338 169 ASA------PLLAELAR--GKHAALTYEPALPD--GTLAGA-RKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAELALA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 214 LvniewDKGNEFFPPTSMQIANVQSGtGSNNVIPGDMFVQFNFRFSTELTDEMIKARVVALLEKYELRYSVDWWLSGQ-- 291
Cdd:PRK07338 238 L-----HALNGQRDGVTVNVAKIDGG-GPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHGVSLHLHGGfg 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 292 ----PFLTSRGKLVDAVVNAIEHYN-EIKPQllTNGGTSDGRFIARMGAQVVE-LGPVNATIHKINECVNAADLQLLARM 365
Cdd:PRK07338 312 rppkPIDAAQQRLFEAVQACGAALGlTIDWK--DSGGVCDGNNLAAAGLPVVDtLGVRGGNIHSEDEFVILDSLVERAQL 389
|
....*...
gi 490205977 366 YQRIMEQL 373
Cdd:PRK07338 390 SALILMRL 397
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
56-106 |
1.35e-12 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 68.71 E-value: 1.35e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 490205977 56 GRG-ETLAFAGHTDVVPSGDAdrWINPPFEPTIRDGMLFGRGAADMKG-SLAA 106
Cdd:PRK07318 76 GEGeEVLGILGHLDVVPAGDG--WDTDPYEPVIKDGKIYARGTSDDKGpTMAA 126
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
58-214 |
9.92e-12 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 65.92 E-value: 9.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 58 GETLAFAGHTDVVPSGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQypnhKGRL----AFLITSDE 133
Cdd:PRK08201 79 KPTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKV----EGTLpvnvKFCIEGEE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 134 EASAKNgtvkVVEALMARNERL--DYCLVGEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQGHV---AYPHLADNPVHRAA 208
Cdd:PRK08201 155 EIGSPN----LDSFVEEEKDKLaaDVVLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLhsgLYGGAVPNALHALV 230
|
....*.
gi 490205977 209 PMLAEL 214
Cdd:PRK08201 231 QLLASL 236
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
10-276 |
1.77e-11 |
|
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.
Pssm-ID: 349869 [Multi-domain] Cd Length: 394 Bit Score: 64.88 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 10 QQLIRRPSLSP--DDAGCQALMIERLRAIGFTVE--PMDFGDTQNF-------WAWRGR----GETLAFAGHTDVVPSGD 74
Cdd:cd02697 10 QKLVRVPTDTPpgNNAPHAERTAALLQGFGFEAErhPVPEAEVRAYgmesitnLIVRRRygdgGRTVALNAHGDVVPPGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 75 AdrWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNGTVKVVEALMARNer 154
Cdd:cd02697 90 G--WTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGELGPGWLLRQGLTKP-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 155 lDYcLVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELvnieWDKGNEFFPPTS---- 230
Cdd:cd02697 166 -DL-LIAAGFSYEVV-----TAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNAL----YALNAQYRQVSSqveg 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 490205977 231 -----MQIANVQSGTGSnNVIPGDMFVQFNFRFSTELTDEMIKARVVALLE 276
Cdd:cd02697 235 ithpyLNVGRIEGGTNT-NVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIA 284
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
29-114 |
5.79e-11 |
|
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: 63.78 E-value: 5.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 29 MIERLRAIGFTVEPMDFGDTQNfwawrGRGE-------------------TLAFAGHTDVVPSGDADRWINPPFEPTIRD 89
Cdd:cd05676 42 AAERLEKLGFKVELVDIGTQTL-----PDGEelplppvllgrlgsdpskkTVLIYGHLDVQPAKLEDGWDTDPFELTEKD 116
|
90 100
....*....|....*....|....*
gi 490205977 90 GMLFGRGAADMKGSLAAMVVAAERF 114
Cdd:cd05676 117 GKLYGRGSTDDKGPVLGWLNAIEAY 141
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
11-371 |
6.18e-11 |
|
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: 63.24 E-value: 6.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 11 QLIRRPSLSPDDAGCQALMIERLRAIGFTVEPMDFGDTQNFWA------WRGRGE---TLAFAGHTDVVPSGDadrwINP 81
Cdd:cd05683 11 ELVQIDSETLHEKEISKVLKKKFENLGLSVIEDDAGKTTGGGAgnlictLKADKEevpKILFTSHMDTVTPGI----NVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 82 PfePTIRDGMLFGRG----AADMKGSLAAMVVAAERFVAQYPNHkGRLAFLITSDEEASakngtvkVVEALMARNERLD- 156
Cdd:cd05683 87 P--PQIADGYIYSDGttilGADDKAGIAAILEAIRVIKEKNIPH-GQIQFVITVGEESG-------LVGAKALDPELIDa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 157 ---YCLVGEpsstevvGDVvkngrrGSLTC--------NLTIHGVQGHVA-YPHLADNPVHRAAPMLAelvNIEWDKGNE 224
Cdd:cd05683 157 dygYALDSE-------GDV------GTIIVgaptqdkiNAKIYGKTAHAGtSPEKGISAINIAAKAIS---NMKLGRIDE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 225 FfppTSMQIANVQSGTGSNnVIPGDMFVQFNFRfstELTDEMIKARVVALLEKYEL-------RYSVDWWLSGQPF-LTS 296
Cdd:cd05683 221 E---TTANIGKFQGGTATN-IVTDEVNIEAEAR---SLDEEKLDAQVKHMKETFETtakekgaHAEVEVETSYPGFkINE 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490205977 297 RGKLVDAVVNAIEHYnEIKPQLLTNGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIME 371
Cdd:cd05683 294 DEEVVKLAKRAANNL-GLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAVLVVEIIK 367
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
6-308 |
2.44e-10 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 61.34 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGF-TVEPMDFGDTQNFWAWRGRGETLAFAGHTDVVPSGDAdrwinpPFE 84
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGLgDVERDGRGNVVGRLRGTGGGPALLFSAHLDTVFPGDT------PAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNGTVKvvEALMARNERLDYCLVGEPS 164
Cdd:cd03896 75 VRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEGLGDLRGAR--YLLSAHGARLDYFVVAEGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 165 stevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDkgneFFPPTSMQIANVQSGTgSNN 244
Cdd:cd03896 153 -----DGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAP----YVPKTTFAAIRGGGGT-SVN 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490205977 245 VIPGDMFVQFNFRF--STELTDemIKARVVALLEKYELRYS-----VDWWLSGQPFLTSR-GKLVDAVVNAI 308
Cdd:cd03896 223 RIANLCSMYLDIRSnpDAELAD--VQREVEAVVSKLAAKHLrvkarVKPVGDRPGGEAQGtEPLVNAAVAAH 292
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
56-352 |
2.59e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 61.69 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 56 GRGETLAFAGHTDVVPSGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYpnhKGRLA--FLITSDE 133
Cdd:PRK06446 60 GAKKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKH---KLNVNvkFLYEGEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 134 EASAKNgtvkvVEALMARNERL---DYCLV-GEPSSTEVVGDVVKnGRRGSLTCNLTIHGVQG--HVAYPHLADNPVHRA 207
Cdd:PRK06446 137 EIGSPN-----LEDFIEKNKNKlkaDSVIMeGAGLDPKGRPQIVL-GVKGLLYVELVLRTGTKdlHSSNAPIVRNPAWDL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 208 APMLAELVN-------------IEW---------------------------DKGNE--------FFPPTSmQIANVQS- 238
Cdd:PRK06446 211 VKLLSTLVDgegrvlipgfyddVRElteeerellkkydidveelrkalgfkeLKYSDrekiaealLTEPTC-NIDGFYSg 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 239 --GTGSNNVIPGDMFVQFNFRFSTELTDEMIKARVVALLEKYELRYSVDWWLSGQPFLTS-RGKLVDAVVNAIEHYNEIK 315
Cdd:PRK06446 290 ytGKGSKTIVPSRAFAKLDFRLVPNQDPYKIFELLKKHLQKVGFNGEIIVHGFEYPVRTSvNSKVVKAMIESAKRVYGTE 369
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 490205977 316 PQLLTNG-GTSD-GRFIARMG----AQVVELGPVNATIHKINE 352
Cdd:PRK06446 370 PVVIPNSaGTQPmGLFVYKLGirdiVSAIGVGGYYSNAHAPNE 412
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
11-160 |
3.53e-10 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 61.07 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 11 QLIRRPSLSPDDA---GCQA---LMIERLRAIGFTVE-------PMDFGDTQnfwAWRGRGETLAFAGHTDVVPSGDADR 77
Cdd:PRK09104 25 ALLRIPSISTDPAyaaDCRKaadWLVADLASLGFEASvrdtpghPMVVAHHE---GPTGDAPHVLFYGHYDVQPVDPLDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 78 WINPPFEPTIRDG-----MLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNgtvkVVEALMARN 152
Cdd:PRK09104 102 WESPPFEPRIKETpdgrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEESGSPS----LVPFLEANA 177
|
170
....*....|
gi 490205977 153 ERL--DYCLV 160
Cdd:PRK09104 178 EELkaDVALV 187
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
4-372 |
2.27e-09 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 58.49 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 4 PVIELAQQLIRRPSLSPDDAGCQ---ALMIERLRAIGFTVEPMD----FGDtqNFWA-WRGRGE-TLAFAGHTDVV--PS 72
Cdd:PRK06133 38 AYLDTLKELVSIESGSGDAEGLKqvaALLAERLKALGAKVERAPtppsAGD--MVVAtFKGTGKrRIMLIAHMDTVylPG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 73 GDADRwinpPFEptIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKnGTVKVVEALMARN 152
Cdd:PRK06133 116 MLAKQ----PFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGSP-GSRELIAELAAQH 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 153 erlDYCLVGEPSSTEvvgDVVKNGRRGSLTCNLTIHGVQGHV-AYPHLADNPVHRAAPMLAELVniewDKGNeffPPTSM 231
Cdd:PRK06133 189 ---DVVFSCEPGRAK---DALTLATSGIATALLEVKGKASHAgAAPELGRNALYELAHQLLQLR----DLGD---PAKGT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 232 QIANVQSGTGSN-NVIPGDMFVQFNFRFS-TELTDEMIKA--RVVA--LLEKYELRYSVDwwlSGQPFL--TSRGKLVDA 303
Cdd:PRK06133 256 TLNWTVAKAGTNrNVIPASASAQADVRYLdPAEFDRLEADlqEKVKnkLVPDTEVTLRFE---RGRPPLeaNAASRALAE 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490205977 304 VVNAIehYNEI----KPQLLTNGGTSDGRFIARMG-AQVVE-LGPVNATIHKINECVN----AADLQLLARMyqrIMEQ 372
Cdd:PRK06133 333 HAQGI--YGELgrrlEPIDMGTGGGTDAAFAAGSGkAAVLEgFGLVGFGAHSNDEYIElnsiVPRLYLLTRM---IMEL 406
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
44-322 |
3.78e-09 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 57.94 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 44 DFGDTQNFWA-WRGRGE---TLAFAGHTDVV--------------PSGDADRWINPPFEPTIRDGM-----LFGRGAADM 100
Cdd:COG4187 61 DPLGRKNVTAlVKGKGEskkTVILISHFDVVdvedygslkplafdPEELTEALKEIKLPEDVRKDLesgewLFGRGTMDM 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 101 KGSLAAMVVAAERFvAQYPNHKGRLAFLITSDEEA-SAknGTVKVVEAL--MARNERLDY--CLVGEPSSTEVVGDvvkN 175
Cdd:COG4187 141 KAGLALHLALLEEA-SENEEFPGNLLLLAVPDEEVnSA--GMRAAVPLLaeLKEKYGLEYklAINSEPSFPKYPGD---E 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 176 GRR---GS----LTCNLtIHGVQGHVAYPHLADNPVHraapMLAELVN-IEW-----DK-GNEFF-PPTSMQIA------ 234
Cdd:COG4187 215 TRYiytGSigklMPGFY-CYGKETHVGEPFSGLNANL----LASELTReLELnpdfcEEvGGEVTpPPVSLKQKdlkeey 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 235 NVQsgtgsnnvIPGDMFVQFN-FRFST---ELTDEMIKARVVAL---LEKYELRYSVDWWLSGQPFLTSRGK-------- 299
Cdd:COG4187 290 SVQ--------TPHRAVAYFNvLTLERspkEILEKLKKIAEEAAekiLEHYKEQYEKYCKLTGEPFVPLPWKvkvltyee 361
|
330 340
....*....|....*....|....*...
gi 490205977 300 LVDAVVNA-----IEHYNEIKPQLLTNG 322
Cdd:COG4187 362 LYEEAVKKygedfVEAIEEIAEKLNNGE 389
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
56-278 |
1.52e-08 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 55.93 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 56 GRGETLAFAG-HTDVVPSgDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEE 134
Cdd:cd08012 75 VDGKTVSFVGsHMDVVTA-NPETWEFDPFSLSIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVVAVFIANEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 135 ASAKNGTvkVVEALMARNErLDYCLVGEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAEl 214
Cdd:cd08012 154 NSEIPGV--GVDALVKSGL-LDNLKSGPLYWVDSADSQPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVMEALAE- 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490205977 215 vnIEWDKGNEFFP-----------PTSMQIANVQSGTGSNNVIPGDMFVQFNFRfsteLTDEMIKARVVALLEKY 278
Cdd:cd08012 230 --IQKRFYIDFPPhpkeevygfatPSTMKPTQWSYPGGSINQIPGECTICGDCR----LTPFYDVKEVREKLEEY 298
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
105-286 |
6.80e-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: 53.76 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 105 AAMVVAAERFVAQYPNHKGRLAFLITSDEEASAknGTVKVVEALMARNERLDYCLvGEPSSTEV-VGDVVknGRRGSLTC 183
Cdd:cd03886 95 AMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPG--GAKAMIEEGVLENPGVDAAF-GLHVWPGLpVGTVG--VRSGALMA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 184 -----NLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIewdKGNEFFPPTS--MQIANVQSGTGsNNVIPGDMFVQFNF 256
Cdd:cd03886 170 sadefEITVKGKGGHGASPHLGVDPIVAAAQIVLALQTV---VSRELDPLEPavVTVGKFHAGTA-FNVIPDTAVLEGTI 245
|
170 180 190
....*....|....*....|....*....|....
gi 490205977 257 RFSTELTDEMIKARVVALLEK----YELRYSVDW 286
Cdd:cd03886 246 RTFDPEVREALEARIKRLAEGiaaaYGATVELEY 279
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
4-373 |
8.31e-08 |
|
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: 53.43 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 4 PVIELAQQLIRRPSL--SPDDAGCQALMIERLRAIGFTVEPMDFgDTQNFWA---WRGRGETLA---FAGHTDVVPSGDa 75
Cdd:cd05646 3 PAVTRFREYLRINTVhpNPDYDACVEFLKRQADELGLPVRVIEV-VPGKPVVvltWEGSNPELPsilLNSHTDVVPVFE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 76 DRWINPPFEPTI-RDGMLFGRGAADMKGSLAAMVVAAERFVAQypNHKGRLAFLIT--SDEEASAKNGTVKVVEALMARN 152
Cdd:cd05646 81 EKWTHDPFSAHKdEDGNIYARGAQDMKCVGIQYLEAIRRLKAS--GFKPKRTIHLSfvPDEEIGGHDGMEKFVKTEEFKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 153 ERLDYCL-VGEPSSTEVVgdVVKNGRRGSLTCNLTIHGVQGHVA--YPHLADNPVHRAAPMLAELVNIEWD--KGNEFFP 227
Cdd:cd05646 159 LNVGFALdEGLASPTEEY--RVFYGERSPWWVVITAPGTPGHGSklLENTAGEKLRKVIESIMEFRESQKQrlKSNPNLT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 228 P---TSMQIANVQSGTgSNNVIPGDMFVQFNFRFsTELTD-----EMIKARVVALLEKYELRY----------SVD---- 285
Cdd:cd05646 237 LgdvTTVNLTMLKGGV-QMNVVPSEAEAGFDLRI-PPTVDleefeKQIDEWCAEAGRGVTYEFeqkspekdptSLDdsnp 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 286 WWlsgqpfltsrgklvDAVVNAIEHYN-EIKPQLLTngGTSDGRFIARMGAQVVELGPVNAT---IHKINECVNAADLQL 361
Cdd:cd05646 315 WW--------------AAFKKAVKEMGlKLKPEIFP--AATDSRYIRALGIPALGFSPMNNTpilLHDHNEFLNEDVFLR 378
|
410
....*....|..
gi 490205977 362 LARMYQRIMEQL 373
Cdd:cd05646 379 GIEIYEKIIPAL 390
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
6-310 |
1.61e-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: 52.73 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 6 IELAQQLIRRPSLSPDDAGCQALMIERLRAIGFTVEPmDFGDTQNFWAWRGRG---ETLAFAGHTDVVPSGDADRWinpP 82
Cdd:TIGR01891 2 TDIRRHLHEHPELSFEEFKTSSLIAEALESLGIEVRR-GVGGATGVVATIGGGkpgPVVALRADMDALPIQEQTDL---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 83 FEPTIrDGMLFGRGaadmKGSLAAMVVAAERFVAQYPNH-KGRLAFLITSDEEASAknGTVKVVEA-LMarnERLDYCLV 160
Cdd:TIGR01891 78 YKSTN-PGVMHACG----HDLHTAILLGTAKLLKKLADLlEGTVRLIFQPAEEGGG--GATKMIEDgVL---DDVDAILG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 161 GEPSSTEVVGDVVKngRRGSLT-----CNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNEFFPPTsMQIAN 235
Cdd:TIGR01891 148 LHPDPSIPAGTVGL--RPGTIMaaadkFEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQIVSRNVDPSRPAV-VSVGI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 236 VQSGTGSnNVIPGDMFVQFNFRFSTELTDEMIKARVVALLE--------KYELRysvdwWLSGQPFLTSRGKLVDAVVNA 307
Cdd:TIGR01891 225 IEAGGAP-NVIPDKASMSGTVRSLDPEVRDQIIDRIERIVEgaaamygaKVELN-----YDRGLPAVTNDPALTQILKEV 298
|
...
gi 490205977 308 IEH 310
Cdd:TIGR01891 299 ARH 301
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
105-271 |
1.59e-06 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349914 [Multi-domain] Cd Length: 399 Bit Score: 49.65 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 105 AAMVVAAERFVAQYPNHKGRLAFLITSDEE--ASAKngtVKVVEALMARNERLDYCL----VGEPSSTevVGdvVKNGRR 178
Cdd:cd05664 105 AALLGAARLLVEAKDAWSGTLIAVFQPAEEtgGGAQ---AMVDDGLYDKIPKPDVVLaqhvMPGPAGT--VG--TRPGRF 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 179 GSLTCNL--TIHGVQGHVAYPHLADNPVHRAAPMLAELVNIewdKGNEFFP--PTSMQIANVQSGTgSNNVIPGDMFVQF 254
Cdd:cd05664 178 LSAADSLdiTIFGRGGHGSMPHLTIDPVVMAASIVTRLQTI---VSREVDPqeFAVVTVGSIQAGS-AENIIPDEAELKL 253
|
170
....*....|....*..
gi 490205977 255 NFRFSTELTDEMIKARV 271
Cdd:cd05664 254 NVRTFDPEVREKVLNAI 270
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
36-232 |
7.56e-06 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 47.72 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 36 IGFTVEPMDFGDTQNFWAWRGRGE---TLAFAGHTDVVPSGDADRWINPPFEPTI-----------------RDGM---- 91
Cdd:cd05654 46 VWQLLPPDDLGRRNVTALVKGKKPskrTIILISHFDTVGIEDYGELKDIAFDPDEltkafseyveeldeevrEDLLsgew 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 92 LFGRGAADMKGSLAAMVVAAERFvAQYPNHKGRLAFLITSDEEaSAKNGTVKVVEAL--MARNERLDY--CLVGEPSSTE 167
Cdd:cd05654 126 LFGRGTMDMKSGLAVHLALLEQA-SEDEDFDGNLLLMAVPDEE-VNSRGMRAAVPALleLKKKHDLEYklAINSEPIFPQ 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490205977 168 VVGDVVK---NGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAEL-VNI---EWDKGNEFFPPTSMQ 232
Cdd:cd05654 204 YDGDQTRyiyTGSIGKILPGFLCYGKETHVGEPFAGINANLMASEITARLeLNAdlcEKVEGEITPPPVCLK 275
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
180-272 |
1.06e-05 |
|
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349939 [Multi-domain] Cd Length: 365 Bit Score: 46.89 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 180 SLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNeffpPTSMQIANVQSGTGSNNVIPGDMFVQFNFRFS 259
Cdd:cd08018 167 STFLEGTIKGKQAHGARPHLGINAIEAASAIVNAVNAIHLDPNI----PWSVKMTKLQAGGEATNIIPDKAKFALDLRAQ 242
|
90
....*....|...
gi 490205977 260 TELTDEMIKARVV 272
Cdd:cd08018 243 SNEAMEELKEKVE 255
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
79-214 |
1.08e-05 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 47.09 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 79 INPPFEPTIRdgmLFGRGAADMKGSLAAMVVAAERFVAQYPNHKGRLAFLITSDEEASAKNgtvkVVEALMARNERL--D 156
Cdd:cd05678 106 IFSNLDPEWR---VFARAAADDKGPIMMMLAALDALKAGGIAPKFNVKIILDSEEEKGSPS----LPKAVKEYKELLaaD 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490205977 157 YCLVGEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQ-----GHvaYPHLADNPVHRAAPMLAEL 214
Cdd:cd05678 179 ALIIMDGPAHATNKPTLTFGCRGIATATLTTYGAKvpqhsGH--YGNYAPNPAFRLSSLLASM 239
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
29-136 |
1.24e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 46.83 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 29 MIERLRAIGFTVEPMDfgdtqNFWAWRG------RGE-----TLAFAGHTDVVPsGDADRWINP--PFEPTIRDGMLFGR 95
Cdd:PRK07079 50 IAPALAALGFTCRIVD-----NPVAGGGpfliaeRIEddalpTVLIYGHGDVVR-GYDEQWREGlsPWTLTEEGDRWYGR 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 490205977 96 GAADMKG----SLAAM-VVAAERfvaqypnhKGRLAF----LITSDEEAS 136
Cdd:PRK07079 124 GTADNKGqhtiNLAALeQVLAAR--------GGRLGFnvklLIEMGEEIG 165
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
177-311 |
1.14e-04 |
|
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 43.95 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 177 RRGSLTCN-----LTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIewdkGNEFFPPTSMQ---IANVQSGTgSNNVIPG 248
Cdd:COG1473 175 RPGPIMAAadsfeITIKGKGGHAAAPHLGIDPIVAAAQIVTALQTI----VSRNVDPLDPAvvtVGIIHGGT-APNVIPD 249
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490205977 249 DMFVQFNFRFSTELTDEMIKARVVALLEK----YELRYSVDwWLSGQPFLTSRGKLVDAVVNAIEHY 311
Cdd:COG1473 250 EAELEGTVRTFDPEVRELLEERIERIAEGiaaaYGATAEVE-YLRGYPPTVNDPELTELAREAAREV 315
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
184-282 |
3.05e-04 |
|
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349920 [Multi-domain] Cd Length: 367 Bit Score: 42.25 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 184 NLTIHGVQGHVAYPHLADNPVHRAAPMLAELVNIEWDKGNeffPPTS--MQIANVQSGTgSNNVIPGDMFVQFNFRFSTE 261
Cdd:cd05670 176 HIDFIGKSGHAAYPHNANDMVVAAANFVTQLQTIVSRNVD---PIDGavVTIGKIHAGT-ARNVIAGTAHLEGTIRTLTQ 251
|
90 100
....*....|....*....|.
gi 490205977 262 LTDEMIKARVVALLEKYELRY 282
Cdd:cd05670 252 EMMELVKQRVRDIAEGIELAF 272
|
|
| M20_Acy1L2_AbgB |
cd05673 |
M20 Peptidase Aminoacylase 1-like protein 2 aminobenzoyl-glutamate utilization protein B ... |
27-285 |
2.90e-03 |
|
M20 Peptidase Aminoacylase 1-like protein 2 aminobenzoyl-glutamate utilization protein B subfamily; Peptidase M20 family, ACY1L2 aminobenzoyl-glutamate utilization protein B (AbgB) subfamily. This group contains mostly bacterial amidohydrolases, including gene products of abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate is a natural end product of folate catabolism, and its utilization is initiated by the abg region gene product, AbgT, by enabling uptake of its into the cell in a concentration-dependent, saturable manner. It is subsequently cleaved by AbgA and AbgB (sometimes referred to as AbgAB).
Pssm-ID: 349922 [Multi-domain] Cd Length: 437 Bit Score: 39.59 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 27 ALMIERLRAIGFTVEPMDFGDTQNFWAWRGRGE-TLAFAGHTDVVP--SGDADrwiNPPFEPTIRDGM-------LFGrg 96
Cdd:cd05673 30 ALLKEALEEEGFTVERGVAGIPTAFVASYGSGGpVIAILGEYDALPglSQEAG---VAERKPVEPGANghgcghnLLG-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 97 aadmKGSLAAmVVAAERFVAQYpNHKGRLAFLITSDEE-ASAKngtvkvveALMARN---ERLDYCLVGEPSSTEVVGdv 172
Cdd:cd05673 105 ----TGSLGA-AIAVKDYMEEN-NLAGTVRFYGCPAEEgGSGK--------TFMVRDgvfDDVDAAISWHPASFNGVW-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 173 vkngrRGSLTCNL----TIHGVQGHVAY-PHLAdnpvhRAAPMLAELVNIEWDKGNEFFPP-TSMQIANVQSGTGSNNVI 246
Cdd:cd05673 169 -----STSSLANIsvkfKFKGISAHAAAaPHLG-----RSALDAVELMNVGVNYLREHMIPeARVHYAITNGGGAAPNVV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 490205977 247 PGDMFVQFNFRFST-----ELTDEMIK-ARVVALLEKYELRYSVD 285
Cdd:cd05673 239 PAFAEVWYYIRAPKmeaaeELYDRVDKiAKGAAMMTETEVEYEFI 283
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
9-107 |
5.48e-03 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 38.63 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490205977 9 AQQLIRRPSLSpddAGCQALMIERLRAIGFTVEPMDfgdtqNFWAWRG------RGE-----TLAFAGHTDVVPSGDAdR 77
Cdd:cd05679 20 SQEPARKPELR---AYLDQEMRPRFERLGFTVHIHD-----NPVAGRApfliaeRIEdpslpTLLIYGHGDVVPGYEG-R 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 490205977 78 WIN--PPFEPTIRDGMLFGRGAADMKG----SLAAM 107
Cdd:cd05679 91 WRDgrDPWTVTVWGERWYGRGTADNKGqhsiNMAAL 126
|
|
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