|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
10-384 |
0e+00 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 715.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 10 SPTLKLAFELLRRASVTPDDEGCQDLMIERLTALGFHIEQLPFGDVKNFWAVRGHHGPVLAFAGHTDVVPSGPHTNWEFP 89
Cdd:PRK13009 2 SDVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDFGDVKNLWARRGTEGPHLCFAGHTDVVPPGDLEAWTSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 90 PFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEGPAIDGTRAVVEHLRERNDRLDYCIV 169
Cdd:PRK13009 82 PFEPTIRD-GMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVLEWLKARGEKIDYCIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 170 GEPSSTARLGDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALVNEHWDAGNDFFPATSFQISNLRAGT 249
Cdd:PRK13009 161 GEPTSTERLGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEGNEFFPPTSLQITNIDAGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 250 GATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEYHIDWTLNGEPFLTSEGELVEAAIRGVEAVTGERPALST 329
Cdd:PRK13009 241 GATNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDYTLEWTLSGEPFLTPPGKLVDAVVAAIEAVTGITPELST 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1011478961 330 SGGTSDGRFIATLGTQVVELGPLNDTIHKVNERVRASDLDALSRIYEATLQALLT 384
Cdd:PRK13009 321 SGGTSDARFIADYGAQVVEFGPVNATIHKVNECVSVADLEKLTRIYERILERLLA 375
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
13-379 |
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: 649.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 13 LKLAFELLRRASVTPDDEGCQDLMIERLTALGFHIEQLPFGDVKNFWAVRGHHGPVLAFAGHTDVVPSGPHTNWEFPPFE 92
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFGGVKNLWARRGTGGPHLCFAGHTDVVPPGDLEGWSSDPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 93 PCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEGPAIDGTRAVVEHLRERNDRLDYCIVGEP 172
Cdd:cd03891 81 PTIKD-GMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKIDYCIVGEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 173 SSTARLGDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALVNEHWDAGNDFFPATSFQISNLRAGTGAT 252
Cdd:cd03891 160 TSEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLDEGNEFFPPSSLQITNIDVGNGAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 253 NVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEYHIDWTLNGEPFLTSEGELVEAAIRGVEAVTGERPALSTSGG 332
Cdd:cd03891 240 NVIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELSTSGG 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1011478961 333 TSDGRFIATLGTQVVELGPLNDTIHKVNERVRASDLDALSRIYEATL 379
Cdd:cd03891 320 TSDARFIASYGCPVVEFGLVNATIHKVNERVSVADLEKLTDIYERIL 366
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
13-382 |
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: 583.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 13 LKLAFELLRRASVTPDDEGCQDLMIERLTALGFHIEQLPFGDVKNFWAVRGHHGPVLAFAGHTDVVPSGPHTNWEFPPFE 92
Cdd:TIGR01246 2 TELAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGDTKNLWATRGTGEPVLAFAGHTDVVPAGPEEQWSSPPFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 93 PCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEGPAIDGTRAVVEHLRERNDRLDYCIVGEP 172
Cdd:TIGR01246 82 PVERD-GKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVETLMARDELIDYCIVGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 173 SSTARLGDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALVNEHWDAGNDFFPATSFQISNLRAGTGAT 252
Cdd:TIGR01246 161 SSVKKLGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAIKWDEGNEFFPPTSLQITNIHAGTGAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 253 NVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEYHIDWTLNGEPFLTSEGELVEAAIRGVEAVTGERPALSTSGG 332
Cdd:TIGR01246 241 NVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELSTGGG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1011478961 333 TSDGRFIATLGTQVVELGPLNDTIHKVNERVRASDLDALSRIYEATLQAL 382
Cdd:TIGR01246 321 TSDGRFIALMGAEVVEFGPVNATIHKVNECVSIEDLEKLSDVYQDLLENL 370
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
7-383 |
1.01e-121 |
|
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 357.27 E-value: 1.01e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 7 ASLSPTLKLAFELLRRASVTPDDEGCQDLMIERLTALGFHIEQLPFGDVK-NFWAVRGHH--GPVLAFAGHTDVVPSGPH 83
Cdd:COG0624 9 AHLDEALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPPGRpNLVARRPGDggGPTLLLYGHLDVVPPGDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 84 TNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEGPAiDGTRAVVEHLRERnDR 163
Cdd:COG0624 89 ELWTSDPFEPTIED-GRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGS-PGARALVEELAEG-LK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 164 LDYCIVGEPSSTarlgDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALVNEHWDAG-NDFFPATSFQI 242
Cdd:COG0624 166 ADAAIVGEPTGV----PTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRaDPLFGRTTLNV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 243 SNLRAGTgATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEYHIDWTL---NGEPFLTSE-GELVEAAIRGVE 318
Cdd:COG0624 242 TGIEGGT-AVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEVEVlgdGRPPFETPPdSPLVAAARAAIR 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011478961 319 AVTGERPALSTSGGTSDGRFIAT-LGTQVVELGPLN-DTIHKVNERVRASDLDALSRIYEATLQALL 383
Cdd:COG0624 321 EVTGKEPVLSGVGGGTDARFFAEaLGIPTVVFGPGDgAGAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
14-379 |
1.63e-101 |
|
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: 304.99 E-value: 1.63e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 14 KLAFELLRRASVTPDDEGCQDLMIERLTALGFHIEQLPFGDVKNFWAVRGH-HGPVLAFAGHTDVVPSGPHTNWEFPPFE 92
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVATVGGgDGPVLLLNGHIDTVPPGDGDKWSFPPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 93 PCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEGPAiDGTRAVVEHLRErnDRLDYCIVGEP 172
Cdd:cd08659 81 GRIRD-GRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGS-DGARALLEAGYA--DRLDALIVGEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 173 SstarlGDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALVNEHWDAG-NDFFPATSFQISNLRAGTgA 251
Cdd:cd08659 157 T-----GLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPaHPLLGPPTLNVGVINGGT-Q 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 252 TNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEYHIDWTLNGEP--FLTSEGELVEAAIRGVEAVTGeRPALST 329
Cdd:cd08659 231 VNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPpfFTDPDHPLVQALQAAARALGG-DPVVRP 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1011478961 330 SGGTSDGRFIA-TLGTQVVELGPLND-TIHKVNERVRASDLDALSRIYEATL 379
Cdd:cd08659 310 FTGTTDASYFAkDLGFPVVVYGPGDLaLAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
70-381 |
8.35e-80 |
|
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: 247.65 E-value: 8.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 70 AFAGHTDVVPSGPHTNWefpPFEPCIDdqGMLCGRGAADMKGSLAAMLTAVERFVARYPDhDGRIAFLITSDEEGPaIDG 149
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTED--GKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGG-MGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 150 TRAVVEHLRERNDRLDYCI---VGEPSS-TARLGDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALVN 225
Cdd:pfam01546 74 ARALIEDGLLEREKVDAVFglhIGEPTLlEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 226 EHWDAGNDFFPATsFQISNLRAGTGATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQ----HGLEYHIDWTLNGEP 301
Cdd:pfam01546 154 IVSRNVDPLDPAV-VTVGNITGIPGGVNVIPGEAELKGDIRLLPGEDLEELEERIREILEAiaaaYGVKVEVEYVEGGAP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 302 FLTSEGELVEAAIRGVEAVTGERPALSTSG--GTSDGRFIAT-LGTQVVELGPLNDTIHKVNERVRASDLDALSRIYEAT 378
Cdd:pfam01546 233 PLVNDSPLVAALREAAKELFGLKVELIVSGsmGGTDAAFFLLgVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLARL 312
|
...
gi 1011478961 379 LQA 381
Cdd:pfam01546 313 LLK 315
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
18-386 |
2.00e-61 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 202.91 E-value: 2.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 18 ELLRRASVTP---DDEGCQDLMIERLTALGFHIEQLPFGDVK---------NFWAVRGHHGPVLAFAGHTDVVPsgPHTN 85
Cdd:PRK08651 14 DLIKIPTVNPpgeNYEEIAEFLRDTLEELGFSTEIIEVPNEYvkkhdgprpNLIARRGSGNPHLHFNGHYDVVP--PGEG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 86 W-EFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVaryPDHDGRIAFLITSDEEgpaIDGTRAvvEHLRERND-R 163
Cdd:PRK08651 92 WsVNVPFEPKVKD-GKVYGRGASDMKGGIAALLAAFERLD---PAGDGNIELAIVPDEE---TGGTGT--GYLVEEGKvT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 164 LDYCIVGEPSSTarlgDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALVNEHWDAGNDF---FPATSF 240
Cdd:PRK08651 163 PDYVIVGEPSGL----DNICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYeydDERGAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 241 QISNLRA----GTGATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEYHIDWTLN----GEPFLTS-EGELVE 311
Cdd:PRK08651 239 PTVTLGGptveGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFEitpfSEAFVTDpDSELVK 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011478961 312 AAIRGVEAVTGERPALSTSGGTSDGRFIATLGTQVVELGPLN-DTIHKVNERVRASDLDALSRIYEATLQALLTTN 386
Cdd:PRK08651 319 ALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGElELAHAPDEYVEVKDVEKAAKVYEEVLKRLAKGS 394
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-379 |
1.51e-51 |
|
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: 176.04 E-value: 1.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 13 LKLAFELLRRASVTP---DDEGCQDLMIERLTALGFHIEQLPFGDVKNFW---AVRGHHGPVLAFAGHTDVVPSGPHTNW 86
Cdd:cd08011 1 VKLLQELVQIPSPNPpgdNTSAIAAYIKLLLEDLGYPVELHEPPEEIYGVvsnIVGGRKGKRLLFNGHYDVVPAGDGEGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 87 EFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEGPAIDGTRAVVEHLRERNdrlDY 166
Cdd:cd08011 81 TVDPYSGKIKD-GKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYLLEKVRIKP---ND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 167 CIVGEPSSTarlgDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALVNEHwdagndffpaTSFQISNLR 246
Cdd:cd08011 157 VLIGEPSGS----DNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELE----------KTVNPGVIK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 247 AGTgATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQhGLEYHIDWTLNGEPFLTS-EGELVEAAIRGVEAVTGERP 325
Cdd:cd08011 223 GGV-KVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDS-IEEVSFEIKSFYSPTVSNpDSEIVKKTEEAITEVLGIRP 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1011478961 326 ALSTSGGTSDGRFIATLGTQVVELGPLN-DTIHKVNERVRASDLDALSRIYEATL 379
Cdd:cd08011 301 KEVISVGASDARFYRNAGIPAIVYGPGRlGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
38-380 |
1.93e-50 |
|
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349889 [Multi-domain] Cd Length: 367 Bit Score: 173.16 E-value: 1.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 38 ERLTALGFHIEQLPFGDVK--NFWAVRG-HHGPVLAFAGHTDVVP-SGPHtnWEFPPFEPCIDDqGMLCGRGAADMKGSL 113
Cdd:cd03894 26 DYLAALGVKSRRVPVPEGGkaNLLATLGpGGEGGLLLSGHTDVVPvDGQK--WSSDPFTLTERD-GRLYGRGTCDMKGFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 114 AAMLTAVERFVARYPDHDgrIAFLITSDEE-GPAidGTRAVVEHLRERNDRLDYCIVGEPSSTarlgDVIkNGRRGSLGG 192
Cdd:cd03894 103 AAVLAAVPRLLAAKLRKP--LHLAFSYDEEvGCL--GVRHLIAALAARGGRPDAAIVGEPTSL----QPV-VAHKGIASY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 193 VLHIKGIQGHVAYPHLARNPIHQAMPAL-------DALVNEHWDAGNDfFPATSFQISNLRAGTgATNVIPGEVEVVFNF 265
Cdd:cd03894 174 RIRVRGRAAHSSLPPLGVNAIEAAARLIgklrelaDRLAPGLRDPPFD-PPYPTLNVGLIHGGN-AVNIVPAECEFEFEF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 266 RY----STEVTHDELRSRTEAILDQHGLEYHIDWTLNGEPFLTSEGelvEAAIRGVEAVTGERPALSTSGGTsDGRFIAT 341
Cdd:cd03894 252 RPlpgeDPEAIDARLRDYAEALLEFPEAGIEVEPLFEVPGLETDED---APLVRLAAALAGDNKVRTVAYGT-EAGLFQR 327
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1011478961 342 LGTQVVELGPLN-DTIHKVNERVRASDLDALSRIYEATLQ 380
Cdd:cd03894 328 AGIPTVVCGPGSiAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
13-368 |
4.67e-49 |
|
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: 169.89 E-value: 4.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 13 LKLAFELLRRASVTP---DDEGCQDLMIERLTALGFHIEQLPFGD------VKNFWAVRGH-HGPVLAFAGHTDVVPSGP 82
Cdd:TIGR01910 1 VELLKDLISIPSVNPpggNEETIANYIKDLLREFGFSTDVIEITDdrlkvlGKVVVKEPGNgNEKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 83 HTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEE-GPAidGTRAVVEhlRERN 161
Cdd:TIGR01910 81 LELWKTDPFKPVEKD-GKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEEsGEA--GTLYLLQ--RGYF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 162 DRLDYCIVGEPSStarlGDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALVN--EHWDAGND--FFP- 236
Cdd:TIGR01910 156 KDADGVLIPEPSG----GDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNEleEHIYARNSygFIPg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 237 ATSFQISNLRAGTGAtNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQhgLEYHIDWTLNGEP--------FLTSEGE 308
Cdd:TIGR01910 232 PITFNPGVIKGGDWV-NSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKA--LSKSDGWLYENEPvvkwsgpnETPPDSR 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011478961 309 LVEAAIRGVEAVTGERPALSTSGGTSDGRFIATLGTQVVELGP-LNDTIHKVNERVRASDL 368
Cdd:TIGR01910 309 LVKALEAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPgDLETAHQVNEYISIKNL 369
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
73-383 |
9.19e-37 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 137.24 E-value: 9.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 73 GHTDVVP-SGPhtNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVA---RYPDHdgrIAFliTSDEEGPAId 148
Cdd:PRK07522 71 GHTDVVPvDGQ--AWTSDPFRLTERD-GRLYGRGTCDMKGFIAAALAAVPELAAaplRRPLH---LAF--SYDEEVGCL- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 149 GTRAVVEHLRERNDRLDYCIVGEPSStarLGDVIknGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALV---- 224
Cdd:PRK07522 142 GVPSMIARLPERGVKPAGCIVGEPTS---MRPVV--GHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRdlad 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 225 ----NEHWDAGNDfFPATSFQISNLRAGTgATNVIPGEVEVVFNFRY----STEVTHDELRSRTEAILD----QHGLEYH 292
Cdd:PRK07522 217 rlaaPGPFDALFD-PPYSTLQTGTIQGGT-ALNIVPAECEFDFEFRNlpgdDPEAILARIRAYAEAELLpemrAVHPEAA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 293 IDWT-LNGEPFLTSEGElvEAAIRGVEAVTGERPALSTSGGTSDGRFiATLGTQVVELGPLN-DTIHKVNERVRASDLDA 370
Cdd:PRK07522 295 IEFEpLSAYPGLDTAED--AAAARLVRALTGDNDLRKVAYGTEAGLF-QRAGIPTVVCGPGSiEQAHKPDEFVELAQLAA 371
|
330
....*....|...
gi 1011478961 371 LsriyEATLQALL 383
Cdd:PRK07522 372 C----EAFLRRLL 380
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
63-383 |
3.00e-33 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 127.69 E-value: 3.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 63 GHHGPVLAFAGHTDVVPSGPHTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTA-VERFVARYPDHdGRIAFLITSD 141
Cdd:PRK08588 56 GSGSPVLALSGHMDVVAAGDVDKWTYDPFELTEKD-GKLYGRGATDMKSGLAALVIAmIELKEQGQLLN-GTIRLLATAG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 142 EEgpaIDGTRAvvEHLRERN--DRLDYCIVGEPSstarlGDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNpihqampA 219
Cdd:PRK08588 134 EE---VGELGA--KQLTEKGyaDDLDALIIGEPS-----GHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVN-------A 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 220 LDALV------NEHWD---AGNDFFPATSFQISNLRAGTgATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLE 290
Cdd:PRK08588 197 IDPLLefyneqKEYFDsikKHNPYLGGLTHVVTIINGGE-QVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNQN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 291 YH----IDWTLNGEPFLTS-EGELVEAAIRGVEAVTGERPALSTSGGTSDGRFIATLGT--QVVELGP-LNDTIHKVNER 362
Cdd:PRK08588 276 GAaqlsLDIYSNHRPVASDkDSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKPdfPVIIFGPgNNLTAHQVDEY 355
|
330 340
....*....|....*....|.
gi 1011478961 363 VRASDLDALSRIYEATLQALL 383
Cdd:PRK08588 356 VEKDMYLKFIDIYKEIIIQYL 376
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
34-368 |
7.27e-32 |
|
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.
Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 123.47 E-value: 7.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 34 DLMIERLTALGFHIEQLPFGDVKN--FWAVRGHHGPVLAFAGHTDVVpsgphtnweFP----PFEPCIDDQGMLCGRGAA 107
Cdd:cd03885 26 ELLAEELEALGFTVERRPLGEFGDhlIATFKGTGGKRVLLIGHMDTV---------FPegtlAFRPFTVDGDRAYGPGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 108 DMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEgPAIDGTRavvEHLRERNDRLDYCIVGEPsstARLGDVIKNGRR 187
Cdd:cd03885 97 DMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEE-IGSPGSR---ELIEEEAKGADYVLVFEP---ARADGNLVTARK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 188 GSLGGVLHIKGIQGHV-AYPHLARNPI----HQAMpALDALvnehwdagNDFFPATSFQISNLRAGTGaTNVIPGEVEVV 262
Cdd:cd03885 170 GIGRFRLTVKGRAAHAgNAPEKGRSAIyelaHQVL-ALHAL--------TDPEKGTTVNVGVISGGTR-VNVVPDHAEAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 263 FNFRYSTEVTHDELRSRTEAILDQH---GLEYHIDWTLNGEPFLTSEG-----ELVEAAIRGV-EAVTGERpalstSGGT 333
Cdd:cd03885 240 VDVRFATAEEADRVEEALRAIVATTlvpGTSVELTGGLNRPPMEETPAsrrllARAQEIAAELgLTLDWEA-----TGGG 314
|
330 340 350
....*....|....*....|....*....|....*.
gi 1011478961 334 SDGRFIATLGTQVVE-LGPLNDTIHKVNERVRASDL 368
Cdd:cd03885 315 SDANFTAALGVPTLDgLGPVGGGAHTEDEYLELDSL 350
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
14-382 |
9.71e-31 |
|
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: 120.15 E-value: 9.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 14 KLAFELLRRASVTPDDEGCQDLMIERLTALGFHIEQLpfgDVKNFWAVRGHHGPVLAFAGHTDVVPSgphtnwefpPFEP 93
Cdd:cd05653 5 ELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVD---EAGNAVGGAGSGPPDVLLLGHIDTVPG---------EIPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 94 CIDDqGMLCGRGAADMKGSLAAMLTAverFVARYPDHDGRIAFLITSDEEGPAIdGTRavveHLRERNDRLDYCIVGEPS 173
Cdd:cd05653 73 RVEG-GVLYGRGAVDAKGPLAAMILA---ASALNEELGARVVVAGLVDEEGSSK-GAR----ELVRRGPRPDYIIIGEPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 174 STARlgdvIKNGRRGSLGGVLHIKGIQGHVAYPhlARNPIHQAMP---ALDALVNEHWDAGNDFFPATsfqiSNLRAGTG 250
Cdd:cd05653 144 GWDG----ITLGYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLIKkwlEVKKWAEGYNVGGRDFDSVV----PTLIKGGE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 251 ATNVIPGEVEVVFNFRYSTEVTHDELRsrteAILDQHGLEYHIDWTLNGEPFLTS-EGELVEAAIRGVEAvTGERPALST 329
Cdd:cd05653 214 SSNGLPQRAEATIDLRLPPRLSPEEAI----ALATALLPTCELEFIDDTEPVKVSkNNPLARAFRRAIRK-QGGKPRLKR 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1011478961 330 SGGTSDGRFIA-TLGTQVVELGPLNDTI-HKVNERVRASDLDALSRIYEATLQAL 382
Cdd:cd05653 289 KTGTSDMNVLApLWTVPIVAYGPGDSTLdHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
14-383 |
1.64e-29 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 117.73 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 14 KLAFELLRRASVTPDDEGCQDLMIERLTALGF-HIEQLPFGdvkNFWAVRGHHGPVLAFAGHTDVVPSGPHTNWEFPPFE 92
Cdd:PRK13004 19 RFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFdKVEIDPMG---NVLGYIGHGKKLIAFDAHIDTVGIGDIKNWDFDPFE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 93 PCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEgpAIDGT--RAVVEhlrERNDRLDYCIVG 170
Cdd:PRK13004 96 GEEDD-GRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEE--DCDGLcwRYIIE---EDKIKPDFVVIT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 171 EPSStarLGdvIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDAL--VNEHWDAgNDFFPATSFQISNLRAG 248
Cdd:PRK13004 170 EPTD---LN--IYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELeeLNPNLKE-DPFLGKGTLTVSDIFST 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 249 TGATNVIPGEVEVVFNFRysteVTHDELRsrtEAILDQ------------------------HGLEYHID-----WTLNg 299
Cdd:PRK13004 244 SPSRCAVPDSCAISIDRR----LTVGETW---ESVLAEiralpavkkanakvsmynydrpsyTGLVYPTEcyfptWLYP- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 300 epfltSEGELVEAAIRGVEAVTGERP-----ALSTSGGTSDGRF-IATLGtqvveLGP-LNDTIHKVNERVRASDLDALS 372
Cdd:PRK13004 316 -----EDHEFVKAAVEAYKGLFGKAPevdkwTFSTNGVSIAGRAgIPTIG-----FGPgKEPLAHAPNEYTWKEQLVKAA 385
|
410
....*....|.
gi 1011478961 373 RIYEATLQALL 383
Cdd:PRK13004 386 AMYAAIPKSLL 396
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
184-292 |
5.43e-28 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 105.89 E-value: 5.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 184 NGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALVNEHWDAGNdFFPATSFQISNLRAGTgATNVIPGEVEVVF 263
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGF-DFPRTTLNITGIEGGT-ATNVIPAEAEAKF 78
|
90 100
....*....|....*....|....*....
gi 1011478961 264 NFRYSTEVTHDELRSRTEAILDQHGLEYH 292
Cdd:pfam07687 79 DIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
18-374 |
1.15e-27 |
|
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: 112.79 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 18 ELLRRASVTPDDEGCQDLMIERLTALGF----------HIEQLP-FGDV----KNFWAVRGHHGPV------LAFAGHTD 76
Cdd:cd03895 5 DLVRFPSLRGEEAAAQDLVAAALRSRGYtvdrweidveKLKHHPgFSPVavdyAGAPNVVGTHRPRgetgrsLILNGHID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 77 VVPSGPHTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEGPAiDGTRAVVeh 156
Cdd:cd03895 85 VVPEGPVELWTRPPFEATIVD-GWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTG-NGALAAL-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 157 lrERNDRLDYCIVGEPSstarlGDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDAL--VNEHWDAGNDF 234
Cdd:cd03895 161 --MRGYRADAALIPEPT-----ELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALqeLEREWNARKKS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 235 FPATS-------FQISNLRAGTGATNVIPgevEVVFNFRYS--TEVTHDELRSRTEAILDQhgLEYHIDW--------TL 297
Cdd:cd03895 234 HPHFSdhphpinFNIGKIEGGDWPSSVPA---WCVLDCRIGiyPGESPEEARREIEECVAD--AAATDPWlsnhppevEW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 298 NG---EPFLTSEGELVEAAI-RGVEAVTGERPALSTSGGTSDGRFIATLG-TQVVELGPLNDTIHKVNERVrasDLDALS 372
Cdd:cd03895 309 NGfqaEGYVLEPGSDAEQVLaAAHQAVFGTPPVQSAMTATTDGRFFVLYGdIPALCYGPGSRDAHGFDESV---DLESLR 385
|
..
gi 1011478961 373 RI 374
Cdd:cd03895 386 KI 387
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
47-379 |
1.56e-26 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and 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: 109.47 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 47 IEQLPFGDVKNFWAVrghhgpvlafaGHTDVVPSGPHTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVAR 126
Cdd:cd05650 61 VAKIPGGNDKTLWII-----------SHLDTVPPGDLSLWETDPWEPVVKD-GKIYGRGVEDNQQGIVSSLLALKAIIKN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 127 --YPDHDGRIAFLitSDEEgpaiDGTRAVVEHLRERNDRL---DYCIVgePSSTARLGDVIKNGRRGSLGGVLHIKGIQG 201
Cdd:cd05650 129 giTPKYNFGLLFV--ADEE----DGSEYGIQYLLNKFDLFkkdDLIIV--PDFGTEDGEFIEIAEKSILWIKVNVKGKQC 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 202 HVAYPHLARNPIHQA---MPALDALVNEHWDAGNDFF--PATSFQISNLRAGTGATNVIPGEVEVVFNFRYSTEVTHDEL 276
Cdd:cd05650 201 HASTPENGINAFVAAsnfALELDELLHEKFDEKDDLFnpPYSTFEPTKKEANVPNVNTIPGYDVFYFDCRVLPTYKLDEV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 277 RSRTEAILD------QHGLEYHIDWTLNGEPFLTSEGELVEAAIRGVEAVTGERPALSTSGGTSDGRFIATLGTQVVELG 350
Cdd:cd05650 281 LKFVNKIISdfensyGAGITYEIVQKEQAPPATPEDSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWS 360
|
330 340
....*....|....*....|....*....
gi 1011478961 351 PLNDTIHKVNERVRASDLDALSRIYEATL 379
Cdd:cd05650 361 TLDETAHQPNEYIRISHIVKDAKVFAEML 389
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-301 |
7.88e-26 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 106.59 E-value: 7.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 13 LKLAFELLRRASVTPDDEGCQDLMIERLTALGFHIEQ--LPFGDVKNFWAVRG-HHGPVLAFAGHTDVVPsgPHTnwefp 89
Cdd:cd05652 2 LSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKqpVENKDRFNVYAYPGsSRQPRVLLTSHIDTVP--PFI----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 90 PFEPCIDDQgMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEgpaIDGtravvEHLRERND----RLD 165
Cdd:cd05652 75 PYSISDGGD-TIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEE---TGG-----DGMKAFNDlglnTWD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 166 YCIVGEPSSTArLGdvikNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALVNEHWdAGNDFFPATSFQISNL 245
Cdd:cd05652 146 AVIFGEPTELK-LA----SGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADL-PSSELLGPTTLNIGRI 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1011478961 246 RAGTgATNVIPGEVEVVFNFR--YSTEVTHDELRSRTEAILDQHGLEyHIDWTLNGEP 301
Cdd:cd05652 220 SGGV-AANVVPAAAEASVAIRlaAGPPEVKDIVKEAVAGILTDTEDI-EVTFTSGYGP 275
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
12-370 |
1.52e-24 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 103.77 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 12 TLKLAFELLRRASVTPDDEGcqDLMIERLTALGFHIEQLPFGDVKNFWAV--RGHHG---------------PVLAFAGH 74
Cdd:PRK13983 7 MIELLSELIAIPAVNPDFGG--EGEKEKAEYLESLLKEYGFDEVERYDAPdpRVIEGvrpnivakipggdgkRTLWIISH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 75 TDVVPSGPHTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVAR--YPDHDGRIAFLitSDEEgpaiDGTRA 152
Cdd:PRK13983 85 MDVVPPGDLSLWETDPFKPVVKD-GKIYGRGSEDNGQGIVSSLLALKALMDLgiRPKYNLGLAFV--SDEE----TGSKY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 153 VVEHLRERNDRL----DYCIVgePSSTARLGDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMP---ALDALVN 225
Cdd:PRK13983 158 GIQYLLKKHPELfkkdDLILV--PDAGNPDGSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRAAADfalELDEALH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 226 EHWDAGNDFF--PATSFQISNLRAGTGATNVIPGEVEVVFNFR----YSTEVTHDELRSRTEAILDQHG--LEYHIDWTL 297
Cdd:PRK13983 236 EKFNAKDPLFdpPYSTFEPTKKEANVDNINTIPGRDVFYFDCRvlpdYDLDEVLKDIKEIADEFEEEYGvkIEVEIVQRE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1011478961 298 NGEPFLTSEGELVEAAIRGVEAVTGERPALSTSGGTSDGRFIATLGTQVVELGPLNDTIHKVNERVRASDL--DA 370
Cdd:PRK13983 316 QAPPPTPPDSEIVKKLKRAIKEVRGIEPKVGGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYAKISNLieDA 390
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
15-385 |
4.85e-24 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 102.92 E-value: 4.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 15 LAFELLRRASVTPDDEG---CQDLMIERLTALGFHIEQL-----PfGDVKNF--WAVRGHH-----GPVLAFAGHTDVVP 79
Cdd:PRK13013 19 LTQDLIRIPTLNPPGRAyreICEFLAARLAPRGFEVELIraegaP-GDSETYprWNLVARRqgardGDCVHFNSHHDVVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 80 SGphTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEGPAIDGTRAVVEHLRE 159
Cdd:PRK13013 98 VG--HGWTRDPFGGEVKD-GRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGGVAYLAEQGRF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 160 RNDRLDYCIVGEPSSTARlgdvIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALVNEhwdagndFFPA-- 237
Cdd:PRK13013 175 SPDRVQHVIIPEPLNKDR----ICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEIEER-------LFPLla 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 238 ---------------TSFQISNLRAG--------TG-ATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILD-----QHG 288
Cdd:PRK13013 244 trrtampvvpegarqSTLNINSIHGGepeqdpdyTGlPAPCVADRCRIVIDRRFLIEEDLDEVKAEITALLErlkraRPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 289 LEYHIDWTLNGEPFLTS-EGELVEAAIRGVEAVTGERPALSTSGGTSDGRFIATLGT--QVVELGP-LNDTIHKVNERVR 364
Cdd:PRK13013 324 FAYEIRDLFEVLPTMTDrDAPVVRSVAAAIERVLGRQADYVVSPGTYDQKHIDRIGKlkNCIAYGPgILDLAHQPDEWVG 403
|
410 420
....*....|....*....|.
gi 1011478961 365 ASDLDALSRIYEATLQALLTT 385
Cdd:PRK13013 404 IADMVDSAKVMALVLADLLAG 424
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
15-374 |
9.44e-23 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 98.92 E-value: 9.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 15 LAF--ELLRRASVTPDDEGCQDLMIERLTALGFH----------IEQLP--------FGDVKNFWAV---RGHHGPVLAF 71
Cdd:PRK06837 23 VAFtqDLVRFPSTRGAEAPCQDFLARAFRERGYEvdrwsidpddLKSHPgagpveidYSGAPNVVGTyrpAGKTGRSLIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 72 AGHTDVVPSGPHTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEGpaiDGTR 151
Cdd:PRK06837 103 QGHIDVVPEGPLDLWSRPPFDPVIVD-GWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEES---TGNG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 152 AVVEHLreRNDRLDYCIVGEPsstarLGDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDAL--VNEHWD 229
Cdd:PRK06837 179 ALSTLQ--RGYRADACLIPEP-----TGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALreLEAEWN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 230 A---GNDFFPA----TSFQISNLRAGTGATNViPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEY--------HID 294
Cdd:PRK06837 252 ArkaSDPHFEDvphpINFNVGIIKGGDWASSV-PAWCDLDCRIAIYPGVTAADAQAEIEACLAAAARDDrflsnnppEVV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 295 WT-LNGEPFLTSEGELVEAAI-RGVEAVTGERPALSTSGGTSDGRFIAT-LGTQVVELGPLNDTIHKVNERVrasDLDAL 371
Cdd:PRK06837 331 WSgFLAEGYVLEPGSEAEAALaRAHAAVFGGPLRSFVTTAYTDTRFYGLyYGIPALCYGPSGEGIHGFDERV---DLESV 407
|
...
gi 1011478961 372 SRI 374
Cdd:PRK06837 408 RKV 410
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
16-375 |
3.55e-22 |
|
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: 96.22 E-value: 3.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 16 AFELLRRASVTP----DDEGCQDLMIERLTALGFHIEQLPfgdvKNFWAVRGHHG---PVLAFAGHTDVVPsgPHTNWEF 88
Cdd:cd05651 2 AIELLKSLIATPsfsrEEHKTADLIENYLEQKGIPFKRKG----NNVWAENGHFDegkPTLLLNSHHDTVK--PNAGWTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 89 PPFEPcIDDQGMLCGRGAADMKGSLAAMLTAVERFvARYPDHDGRIAFLITSDEEGPAIDGTRAVVEHLRErndrLDYCI 168
Cdd:cd05651 76 DPFEP-VEKGGKLYGLGSNDAGASVVSLLATFLHL-YSEGPLNYNLIYAASAEEEISGKNGIESLLPHLPP----LDLAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 169 VGEPSS----TARLGDVIKNgrrgslggvLHIKGIQGHVAYPHlARNPIHQAMPALDALVNEHWDAGNDFFPATSFQISN 244
Cdd:cd05651 150 VGEPTEmqpaIAEKGLLVLD---------CTARGKAGHAARNE-GDNAIYKALDDIQWLRDFRFDKVSPLLGPVKMTVTQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 245 LRAGTgATNVIPGEVEVVFNFR----YSTEVTHDELRSRTEAILDQHGLEYHidwtlngEPFLTSEGELVEAAIRgveav 320
Cdd:cd05651 220 INAGT-QHNVVPDSCTFVVDIRtteaYTNEEIFEIIRGNLKSEIKPRSFRLN-------SSAIPPDHPIVQAAIA----- 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1011478961 321 TGERPALSTSggTSDGrfiATLGTQVVELGPlNDTI--HKVNERVRASDLDALSRIY 375
Cdd:cd05651 287 AGRTPFGSPT--LSDQ---ALMPFPSVKIGP-GDSSrsHTADEFIELSEIEEGIDIY 337
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
70-379 |
8.98e-22 |
|
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: 95.20 E-value: 8.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 70 AFAGHTDVVPSGPHtnwefppFEPCIDDQGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDgrIAFLITSDEEGPA-ID 148
Cdd:cd05647 57 ILAGHLDTVPVAGN-------LPSRVEEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHD--LTLIFYDCEEVAAeLN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 149 GTRAVVEHLRERNDrLDYCIVGEPSSTArlgdvIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALvnehw 228
Cdd:cd05647 128 GLGRLAEEHPEWLA-ADFAVLGEPTDGT-----IEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARL----- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 229 dagNDFFPATsFQISNLR----------AGTGATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEYHI-DWTL 297
Cdd:cd05647 197 ---AAYEPRT-VNIDGLTyreglnavfiSGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEIEVtDLSP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 298 NGEPFLTSE--GELVEAAIRGVEAvtgerpalsTSGGTSDGRFiATLGTQVVELGPLNDTI-HKVNERVRASDLDALSRI 374
Cdd:cd05647 273 GALPGLDHPvaRDLIEAVGGKVRA---------KYGWTDVARF-SALGIPAVNFGPGDPLLaHKRDEQVPVEQITACAAI 342
|
....*
gi 1011478961 375 YEATL 379
Cdd:cd05647 343 LRRWL 347
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
40-380 |
2.29e-21 |
|
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: 95.09 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 40 LTALGFHIEQLPFGDVKNF-WAVRGHHG--PVLAFAGHTDVVPSGPHTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAM 116
Cdd:cd03893 34 LRRLGFTVEIVDTSNGAPVvFAEFPGAPgaPTVLLYGHYDVQPAGDEDGWDSDPFELTERD-GRLYGRGAADDKGPILAH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 117 LTAVERFVARYPDHDGRIAFLITSDEE--GPAIDgtrAVVEHLRERNDrLDYCIVGEPSSTARLGDVIKNGRRGSLGGVL 194
Cdd:cd03893 113 LAALRALMQQGGDLPVNVKFIIEGEEEsgSPSLD---QLVEAHRDLLA-ADAIVISDSTWVGQEQPTLTYGLRGNANFDV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 195 HIKGI------------------------------QGHVAYPHLAR--NPIHQAMPALDALVNEHWD-AGND-------- 233
Cdd:cd03893 189 EVKGLdhdlhsglyggvvpdpmtalaqllaslrdeTGRILVPGLYDavRELPEEEFRLDAGVLEEVEiIGGTtgsvaerl 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 234 -FFPATSFQ-ISNLRAGTGATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQH---GLEYHIDWTLNGEPFLTS-EG 307
Cdd:cd03893 269 wTRPALTVLgIDGGFPGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLEAHLEKHapsGAKVTVSYVEGGMPWRSDpSD 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011478961 308 ELVEAAIRGVEAVTGERPALSTSGGT--SDGRFIATLGTQVVELGPLN--DTIHKVNERVRASDLDALSRIYEATLQ 380
Cdd:cd03893 349 PAYQAAKDALRTAYGVEPPLTREGGSipFISVLQEFPQAPVLLIGVGDpdDNAHSPNESLRLGNYKEGTQAEAALLY 425
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
16-369 |
2.49e-21 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 93.87 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 16 AFELLRRA----SVTPDDEGCQDLMIERLTALGF--HIEqlpfgDVKNFWAVRGHHGPVLAFAGHTDVVPSgphtnwEFP 89
Cdd:PRK04443 8 ARELLKGLveipSPSGEEAAAAEFLVEFMESHGReaWVD-----EAGNARGPAGDGPPLVLLLGHIDTVPG------DIP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 90 PFepcIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPdhdGRIAFLITSDEEGPAIDGTRAVVEHLRErndrlDYCIV 169
Cdd:PRK04443 77 VR---VED-GVLWGRGSVDAKGPLAAFAAAAARLEALVR---ARVSFVGAVEEEAPSSGGARLVADRERP-----DAVII 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 170 GEPSSTARlgdvIKNGRRGSLGGVLHIKGIQGHVAypHLARNPIHQAMPALDALVN--EHWDAGNDFFPATSFQISNLRA 247
Cdd:PRK04443 145 GEPSGWDG----ITLGYKGRLLVTYVATSESFHSA--GPEPNAAEDAIEWWLAVEAwfEANDGRERVFDQVTPKLVDFDS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 248 GTGATNVipgEVEVVFNFRYSTEVTHDELRsrteAILDQHGLEYHIDWTLNGEPFLTS-EGELVEAAIRGVEAVTGErPA 326
Cdd:PRK04443 219 SSDGLTV---EAEMTVGLRLPPGLSPEEAR----EILDALLPTGTVTFTGAVPAYMVSkRTPLARAFRVAIREAGGT-PR 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1011478961 327 LSTSGGTSDGRFIA-TLGTQVVELGPLNDTI-HKVNERVRASDLD 369
Cdd:PRK04443 291 LKRKTGTSDMNVVApAWGCPMVAYGPGDSDLdHTPDEHLPLAEYL 335
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
18-375 |
3.50e-21 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 93.67 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 18 ELLRRASVTPDDEGCQDLMIERLTALGF--HIEQLpfGDVKNFWAvrgHHGPVLAFAGHTDVVPsgPHTnwefPPFEpci 95
Cdd:PRK08652 10 QLVKIPSPSGQEDEIALHIMEFLESLGYdvHIESD--GEVINIVV---NSKAELFVEVHYDTVP--VRA----EFFV--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 96 dDQGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLitSDEEGPAIdGTRAVVEHLRERndrldYCIVGEPSST 175
Cdd:PRK08652 76 -DGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFV--SDEEEGGR-GSALFAERYRPK-----MAIVLEPTDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 176 ArlgdvIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALvNEHWDAGNDFF-PATSFQIsnLRAGTgATNV 254
Cdd:PRK08652 147 K-----VAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKL-KELLKALGKYFdPHIGIQE--IIGGS-PEYS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 255 IPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEYHIDWTLNGepFLTSE----GELVEAAIR--GVEAVTGERPALs 328
Cdd:PRK08652 218 IPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEYTEIWDG--FELDEdeeiVQLLEKAMKevGLEPEFTVMRSW- 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1011478961 329 tsggTSDGRFIATlGTQVVELGPLN-DTIHKVNERVRASD-------LDALSRIY 375
Cdd:PRK08652 295 ----TDAINFRYN-GTKTVVWGPGElDLCHTKFERIDVREvekakefLKALNEIL 344
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
18-382 |
1.32e-20 |
|
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: 92.48 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 18 ELLRRASVTPDDEGCQDLMIERLTALgfhIEQLPFGDVK-----NFWAVRGHHGPVLAFAGHTDVVPSGPHTNWEFPPFE 92
Cdd:cd05649 2 RFLRDLIQIPSESGEEKGVVERIEEE---MEKLGFDEVEidpmgNVIGYIGGGKKKILFDGHIDTVGIGNIDNWKFDPYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 93 PCIDDqGMLCGRGAADMKGSLAAMLTAVERFV-ARYPDHDGRIAFLITSDEEgpAIDGT--RAVVEhlrERNDRLDYCIV 169
Cdd:cd05649 79 GYETD-GKIYGRGTSDQKGGLASMVYAAKIMKdLGLRDFAYTILVAGTVQEE--DCDGVcwQYISK---ADKIKPDFVVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 170 GEPSstaRLGdvIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDAL--VNEHWDAgNDFFPATSFQISNLRA 247
Cdd:cd05649 153 GEPT---DGN--IYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIrqLNPNFPE-APFLGRGTLTVTDIFS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 248 GTGATNVIPGEVEVVFNFRYST----EVTHDELR------------SRTEAILDQH---GLEYHID-----WTLNgepfl 303
Cdd:cd05649 227 TSPSRCAVPDSCRISIDRRLTVgetwEGCLEEIRalpavkkygddvAVSMYNYDRPsytGEVYESEryfptWLLP----- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 304 tSEGELVEAAIRGVEAVTGERPAL-----STSGGTSDGRFiatlGTQVVELGPLNDTI-HKVNERVRASDLDALSRIYEA 377
Cdd:cd05649 302 -EDHELVKALLEAYKALFGARPLIdkwtfSTNGVSIMGRA----GIPCIGFGPGAENQaHAPNEYTWKEDLVRCAAGYAA 376
|
....*
gi 1011478961 378 TLQAL 382
Cdd:cd05649 377 IPTSY 381
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
67-375 |
1.04e-19 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 90.39 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 67 PVLaFAGHTDVVPSGPHT--NWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVAR--YPDHDgrIAFLITSDE 142
Cdd:PRK08262 113 PIV-LMAHQDVVPVAPGTegDWTHPPFSGVIAD-GYVWGRGALDDKGSLVAILEAAEALLAQgfQPRRT--IYLAFGHDE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 143 EgPAIDGTRAVVEHLRERNDRLDyCIVGE---------PSSTARLGdVIKNGRRGSLGGVLHIKGIQGHVAYP------- 206
Cdd:PRK08262 189 E-VGGLGARAIAELLKERGVRLA-FVLDEggaitegvlPGVKKPVA-LIGVAEKGYATLELTARATGGHSSMPprqtaig 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 207 HLARnpihqampALDALVNEHW-----DAGNDFF----PATSF---------------------QISNLRA--------- 247
Cdd:PRK08262 266 RLAR--------ALTRLEDNPLpmrlrGPVAEMFdtlaPEMSFaqrvvlanlwlfeplllrvlaKSPETAAmlrtttapt 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 248 ---GTGATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEyhIDWT-LNGEPFLTSEG-----ELVEAAIRGVE 318
Cdd:PRK08262 338 mlkGSPKDNVLPQRATATVNFRILPGDSVESVLAHVRRAVADDRVE--IEVLgGNSEPSPVSSTdsaayKLLAATIREVF 415
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011478961 319 AVTGERPALSTSGgtSDGRFIATLGTQVVELGPLN------DTIHKVNERVRASDLDALSRIY 375
Cdd:PRK08262 416 PDVVVAPYLVVGA--TDSRHYSGISDNVYRFSPLRlspedlARFHGTNERISVANYARMIRFY 476
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
57-185 |
1.16e-19 |
|
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: 85.95 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 57 NFWAVRGH--HGPVLAFAGHTDVVPSGPHTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRI 134
Cdd:cd18669 1 NVIARYGGggGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEE-GRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1011478961 135 AFLITSDEEGPAIDGTRAVVEHLRERNDRLDYCIVGEPSSTARLGDVIKNG 185
Cdd:cd18669 80 VVAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTP 130
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
68-375 |
2.39e-19 |
|
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: 89.23 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 68 VLAFAGHTDVVPSGPhtNWEFPPFEPCIDDqGMLCGRGAADMKG-SLAAM--LTAVE----------RF----------- 123
Cdd:cd03888 73 VLGILGHLDVVPAGE--GWTTDPFKPVIKD-GKLYGRGTIDDKGpTIAALyaLKILKdlglplkkkiRLifgtdeetgwk 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 124 -VARYPDHDGRIAFLITSDEEGPAIDGTRAVVE---HLRERND---RLDYCIVGE------PSSTARL------------ 178
Cdd:cd03888 150 cIEHYFEHEEYPDFGFTPDAEFPVINGEKGIVTvdlTFKIDDDkgyRLISIKGGEatnmvpDKAEAVIpgkdkeelalsa 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 179 -GDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPI---------HQAMPALDALV---NEHW---DAGNDFFPATSFQI 242
Cdd:cd03888 230 aTDLKGNIEIDDGGVELTVTGKSAHASAPEKGVNAItllakflaeLNKDGNDKDFIkflAKNLhedYNGKKLGINFEDEV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 243 S-NLRAGTGATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEYHIDwtLNGEPFLTS-EGELVEAAIRGVEAV 320
Cdd:cd03888 310 MgELTLNPGIITLDDGKLELGLNVRYPVGTSAEDIIKQIEEALEKYGVEVEGH--KHQKPLYVPkDSPLVKTLLKVYEEQ 387
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1011478961 321 TGERPALSTSGGTSDGRFIAtlgtQVVELGPL----NDTIHKVNERVRASDLDALSRIY 375
Cdd:cd03888 388 TGKEGEPVAIGGGTYARELP----NGVAFGPEfpgqKDTMHQANEFIPIDDLIKALAIY 442
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
13-367 |
1.06e-18 |
|
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: 87.01 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 13 LKLAFELLRRASVTPDDEG---CQDLMIERLTALGFHIEQLPfgdVKNFWAVRGHHG----PVLAFAGHTDVVPSGPHTN 85
Cdd:cd05681 2 LEDLRDLLKIPSVSAQGRGipeTADFLKEFLRRLGAEVEIFE---TDGNPIVYAEFNsgdaKTLLFYNHYDVQPAEPLEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 86 WEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEgpaiDGTRAVVEHLRERNDRL- 164
Cdd:cd05681 79 WTSDPFELTIRN-GKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEE----VGSPNLEKFVAEHADLLk 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 165 -DYCI--VGEPSSTARLgdVIKNGRRGSLGGVLHIKGIQG--HVAYPHLARNPIHQAMPALDALVNE------------- 226
Cdd:cd05681 154 aDGCIweGGGKNPKGRP--QISLGVKGIVYVELRVKTADFdlHSSYGAIVENPAWRLVQALNSLRDEdgrvlipgfyddv 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 227 ------------------------------HWDAGNDFFPATSFQ----ISNLRAG---TGATNVIPGEVEVVFNFRYST 269
Cdd:cd05681 232 rplseaeralidtydfdpeelrktyglkrpLQVEGKDPLRALFTEptcnINGIYSGytgEGSKTILPSEAFAKLDFRLVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 270 EVTHDELRSRTEAILDQHGL-EYHIDWTLNGEPFLTSEG-ELVEAAIRGVEAVTGERPA-LSTSGGTSD-GRFIATLGTQ 345
Cdd:cd05681 312 DQDPAKILSLLRKHLDKNGFdDIEIHDLLGEKPFRTDPDaPFVQAVIESAKEVYGQDPIvLPNSAGTGPmYPFYDALEVP 391
|
410 420
....*....|....*....|....
gi 1011478961 346 VVE--LGPLNDTIHKVNERVRASD 367
Cdd:cd05681 392 VVAigVGNAGSNAHAPNENIRIAD 415
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
66-382 |
1.10e-18 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 86.38 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 66 GPVLAFAGHTDVVPSGphtnwefppFEPCIDDQgMLCGRGAADMKGSLAAMLTAverfvARYPDHDG-RIAFLITSDEEG 144
Cdd:PRK00466 60 EGDILLASHVDTVPGY---------IEPKIEGE-VIYGRGAVDAKGPLISMIIA-----AWLLNEKGiKVMVSGLADEES 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 145 PAIdGTRAVVehlrERNDRLDYCIVGEPSSTarLGDVIknGRRGSLGGVLHIKGIQGHVAYPhlARNPIHQAMPALDALV 224
Cdd:PRK00466 125 TSI-GAKELV----SKGFNFKHIIVGEPSNG--TDIVV--EYRGSIQLDIMCEGTPEHSSSA--KSNLIVDISKKIIEVY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 225 NEhwdagNDFFPATSFQISNLRAGTgATNVIPGEVEVVFNFRYSTEVTHDELRSRteaILDQ-HGLEYHIDWTLngEPFL 303
Cdd:PRK00466 194 KQ-----PENYDKPSIVPTIIRAGE-SYNVTPAKLYLHFDVRYAINNKRDDLISE---IKDKfQECGLKIVDET--PPVK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 304 TS-EGELVEAAIRGVEAvTGERPALSTSGGTSDGRFIATLGTQVVELGPLNDTI-HKVNERVRASDLDALSRIYEATLQA 381
Cdd:PRK00466 263 VSiNNPVVKALMRALLK-QNIKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLeHTNQEKITLDEIYIAVKTYMLAIEE 341
|
.
gi 1011478961 382 L 382
Cdd:PRK00466 342 L 342
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
67-367 |
1.69e-18 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 86.93 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 67 PVLaFAGHTDVVPSGPHT--NWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVAR--YPDHDGRIAFliTSDE 142
Cdd:cd05674 71 PLL-LMAHQDVVPVNPETedQWTHPPFSGHYDG-GYIWGRGALDDKNSLIGILEAVELLLKRgfKPRRTIILAF--GHDE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 143 EGPAIDGTRAVVEHLRER--NDRLdYCIVGEPSSTARLGD------VIKNGRRGSLGGVLHIKGIQGHVAYPH------- 207
Cdd:cd05674 147 EVGGERGAGAIAELLLERygVDGL-AAILDEGGAVLEGVFlgvpfaLPGVAEKGYMDVEITVHTPGGHSSVPPkhtgigi 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 208 -------LARNP--------------------------------IHQAMPALDALVNEHWDAGNDFFPA---TSFQISNL 245
Cdd:cd05674 226 lseavaaLEANPfppkltpgnpyygmlqclaehsplpprslksnLWLASPLLKALLASELLSTSPLTRAllrTTQAVDII 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 246 RAGTgATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEYHIDWTLNGEPFLTSEG------------------ 307
Cdd:cd05674 306 NGGV-KINALPETATATVNHRIAPGSSVEEVLEHVKNLIADIAVKYGLGLSAFGGDVIYSTNgtklltsllspepspvss 384
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011478961 308 ------ELVEAAIRGVEAVTGER----PALSTsGGTsDGRFIATLGTQVVELGP------LNDTIHKVNERVRASD 367
Cdd:cd05674 385 tsspvwQLLAGTIRQVFEQFGEDlvvaPGIMT-GNT-DTRHYWNLTKNIYRFTPirlnpeDLGRIHGVNERISIDD 458
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
17-369 |
3.47e-18 |
|
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: 85.82 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 17 FELLRRASV------TPDDEGCQDLMIERLTALGF-HIEQLPFGdvkNFWAVRGHH-----GPVLAFAGHTDVVPSGPHT 84
Cdd:cd05680 5 FELLRIPSVsadpahKGDVRRAAEWLADKLTEAGFeHTEVLPTG---GHPLVYAEWlgapgAPTVLVYGHYDVQPPDPLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 85 NWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEE--GPAIDgtrAVVEHLRERND 162
Cdd:cd05680 82 LWTSPPFEPVVRD-GRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEigSPSLP---AFLEENAERLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 163 rLDYCIVGEPSSTARLGDVIKNGRRGSLGGVLHIKGI-----QGHvaYPHLARNPIHQAMPALDALVNEHW--------- 228
Cdd:cd05680 158 -ADVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPnrdlhSGS--YGGAVPNPANALARLLASLHDEDGrvaipgfyd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 229 ------DAGNDFFPATSFQISNLRA-----------------------------------GTGATNVIPGEVEVVFNFRY 267
Cdd:cd05680 235 dvrpltDAEREAWAALPFDEAAFKAslgvpalggeagyttlerlwarptldvngiwggyqGEGSKTVIPSKAHAKISMRL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 268 STEVTHDELRSRTEAILDQH---GLEYHIDWTLNGEPFLTSEGE-LVEAAIRGVEAVTGERPALSTSGGTSD--GRFIAT 341
Cdd:cd05680 315 VPGQDPDAIADLLEAHLRAHappGVTLSVKPLHGGRPYLVPTDHpALQAAERALEEAFGKPPVFVREGGSIPivALFEKV 394
|
410 420 430
....*....|....*....|....*....|
gi 1011478961 342 LGTQVVELG-PLND-TIHKVNERVRASDLD 369
Cdd:cd05680 395 LGIPTVLMGfGLPDdAIHAPNEKFRLECFH 424
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
13-380 |
4.02e-18 |
|
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: 85.49 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 13 LKLAFELLRRASVTPDDEGCQ-----DLMIERLTALGFHIEQLPFGDV---KNFWAVRGHHGP---VLAFAGHTDVVPSG 81
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTGSetraaEVLAARLAEAGIQTEIFVVESHpgrANLVARIGGTDPsagPLLLLGHIDVVPAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 82 PhTNWEFPPFEPCIDDqGMLCGRGAADMKGsLAAMLTAVERFVAR---YPDHDGRIAFliTSDEEGPAIDGTRAVVEHLR 158
Cdd:cd05675 81 A-SDWSVDPFSGEIKD-GYVYGRGAVDMKN-MAAMMLAVLRHYKRegfKPKRDLVFAF--VADEEAGGENGAKWLVDNHP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 159 ERNDRLDYCIvGE------PSSTARLGDVIKNGRRGSLGGVLHIKGIQGHVAYPH-----------LAR----------N 211
Cdd:cd05675 156 ELFDGATFAL-NEggggslPVGKGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRPTddnaitrlaeaLRRlgahnfpvrlT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 212 PIHQ-----------------------AMPALDAL--VNEHWDAgndfFPATSFQISNLRAGTgATNVIPGEVEVVFNFR 266
Cdd:cd05675 235 DETAyfaqmaelaggeggalmltavpvLDPALAKLgpSAPLLNA----MLRNTASPTMLDAGY-ATNVLPGRATAEVDCR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 267 YSTEVTHDELRSRTEAILdqhgLEYHIDWT-LNGEPFLTSE--GELVEAAIRGVEAVTGERPALST-SGGTSDGRFIATL 342
Cdd:cd05675 310 ILPGQSEEEVLDTLDKLL----GDPDVSVEaVHLEPATESPldSPLVDAMEAAVQAVDPGAPVVPYmSPGGTDAKYFRRL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1011478961 343 GTQVVELGPL--------NDTIHKVNERVRASDLDALSRIYEATLQ 380
Cdd:cd05675 386 GIPGYGFAPLflppeldyTGLFHGVDERVPVESLYFGVRFLDRLVK 431
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
34-351 |
2.15e-17 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 82.95 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 34 DLMIERLTALGFHIE--QLPFGDVK-NFWAVRGHhGPV-LAFAGHTDVVPSGPHtNWEFPPFEPCIDDqGMLCGRGAADM 109
Cdd:PRK05111 36 DLLAGWFEDLGFNVEiqPVPGTRGKfNLLASLGS-GEGgLLLAGHTDTVPFDEG-RWTRDPFTLTEHD-GKLYGLGTADM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 110 KGSLAAMLTAVERFVARYPDHDGRIafLITSDEEgPAIDGTRAVVEHLRERndrLDYCIVGEPSStarLGDVikNGRRGS 189
Cdd:PRK05111 113 KGFFAFILEALRDIDLTKLKKPLYI--LATADEE-TSMAGARAFAEATAIR---PDCAIIGEPTS---LKPV--RAHKGH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 190 LGGVLHIKGIQGHVAYPHLARNPI---HQAMPAL----DALVNEHWDAGndffpatsFQIS----NLRA--GTGATNVIP 256
Cdd:PRK05111 182 MSEAIRITGQSGHSSDPALGVNAIelmHDVIGELlqlrDELQERYHNPA--------FTVPyptlNLGHihGGDAPNRIC 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 257 GEVEVVFNFR----YSTEVTHDELRSRTEAILDQHGLEYHIDWTLNG-EPFLTS-EGELVeaaiRGVEAVTGERPAlSTS 330
Cdd:PRK05111 254 GCCELHFDIRplpgMTLEDLRGLLREALAPVSERWPGRITVAPLHPPiPGYECPaDHQLV----RVVEKLLGHKAE-VVN 328
|
330 340
....*....|....*....|.
gi 1011478961 331 GGTsDGRFIATLGTQVVELGP 351
Cdd:PRK05111 329 YCT-EAPFIQQLGCPTLVLGP 348
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
66-184 |
1.02e-16 |
|
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: 77.85 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 66 GPVLAFAGHTDVVPSGPHTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEGP 145
Cdd:cd03873 12 GKSVALGAHLDVVPAGEGDNRDPPFAEDTEEE-GRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVG 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1011478961 146 AIDGTRAVVEHLRERNDRLDYCIVGEPS--STARLGDVIKN 184
Cdd:cd03873 91 SGGGKGLLSKFLLAEDLKVDAAFVIDATagPILQKGVVIRN 131
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
58-383 |
4.61e-16 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 79.43 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 58 FWAVRGHHG---PVLAFAGHTDVVPSGPHtNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARypDHDGRI 134
Cdd:PRK08554 52 YYAVYGEIGegkPKLLFMAHFDVVPVNPE-EWNTEPFKLTVKG-DKAYGRGSADDKGNVASVMLALKELSKE--PLNGKV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 135 AFLITSDEEgpaIDGTRA--VVEHLRERNDRLDYCIVGEPSSTArlgDVIKngRRGSLGGVLHIKG----IQGHVAYPHL 208
Cdd:PRK08554 128 IFAFTGDEE---IGGAMAmhIAEKLREEGKLPKYMINADGIGMK---PIIR--RRKGFGVTIRVPSekvkVKGKLREQTF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 209 A-RNPI----HQA--MPALDA--LVnehwdAGNDFFPATSFQISNLRAGTGATNVIPGEV-----------EVVFNFR-- 266
Cdd:PRK08554 200 EiRTPVvetrHAAyfLPGVDThpLI-----AASHFLRESNVLAVSLEGKFLKGNVVPGEVtltylepgegeEVEVDLGlt 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 267 ------------------------------YSTEVTHDELR------SRTEAILDQ---HGLEYHI---DWTLN-----G 299
Cdd:PRK08554 275 rllkaivplvrapikaekysdygvsitpnvYSFAEGKHVLKldiramSYSKEDIERtlkEVLEFNLpeaEVEIRtnekaG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 300 EPFLTSEGELVEAAIRGVEAVtGERPALSTSGGTSDGRFIATLGTQVVELGPLNDTIHKVNERVRASDLDALSRIYEATL 379
Cdd:PRK08554 355 YLFTPPDEEIVKVALRVLKEL-GEDAEPVEGPGASDSRYFTPYGVKAIDFGPKGGNIHGPNEYVEIDSLKKMPEVYKRIA 433
|
....
gi 1011478961 380 QALL 383
Cdd:PRK08554 434 LRLL 437
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
18-382 |
6.09e-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: 78.68 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 18 ELLRRASVTPDDE--GCQDLMIERLTALGFHIEQLPFGDVKNF----WAVRGHHGPVLAFAGHTDVVPSGPHtNWEFPPF 91
Cdd:TIGR01880 17 EYLRINTVQPNPDyaACVDFLIKQADELGLARKTIEFVPGKPVvvltWPGSNPELPSILLNSHTDVVPVFRE-HWTHPPF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 92 EPCIDDQGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEGPAIDGTRAVVEHLRERNDRLDYCI-VG 170
Cdd:TIGR01880 96 SAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEKFAKTDEFKALNLGFALdEG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 171 EPSSTarlgDVIK--NGRRGSLGGVLHIKGIQGHVA--YPHLARNPIHQAMPALDALVNEHWD---AGNDFF--PATSFQ 241
Cdd:TIGR01880 176 LASPD----DVYRvfYAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRRFRESQFQllqSNPDLAigDVTSVN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 242 ISNLRAGTgATNVIPGEVEVVFNFRYSTEVTHDELRSRteaiLDQ------HGLEYHIDwTLNGEPFLTSEGE------L 309
Cdd:TIGR01880 252 LTKLKGGV-QSNVIPSEAEAGFDIRLAPSVDFEEMENR----LDEwcadagEGVTYEFS-QHSGKPLVTPHDDsnpwwvA 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011478961 310 VEAAIRgvEAVTGERPALSTsgGTSDGRFIATLGTQVVELGPLNDT---IHKVNERVRASDLDALSRIYEATLQAL 382
Cdd:TIGR01880 326 FKDAVK--EMGCTFKPEILP--GSTDSRYIRAAGVPALGFSPMNNTpvlLHDHNEFLNEAVFLRGIEIYQTLISAL 397
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
44-266 |
1.70e-15 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 77.16 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 44 GFHIEQLPFGD-VKNFWAVRGHhgPVLAFAGHTDVVPSGPHtnWEFPPFEPCIDDQGMLcGRGAADMKGSLAAMLTAVEr 122
Cdd:PRK08737 42 GFQVEVIDHGAgAVSLYAVRGT--PKYLFNVHLDTVPDSPH--WSADPHVMRRTDDRVI-GLGVCDIKGAAAALLAAAN- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 123 fvarypDHDGRIAFLITSDEEGpaiDGTRAVVEHLrERNDRLDYCIVGEPS-STARLgdviknGRRGSLGGVLHIKGIQG 201
Cdd:PRK08737 116 ------AGDGDAAFLFSSDEEA---NDPRCVAAFL-ARGIPYEAVLVAEPTmSEAVL------AHRGISSVLMRFAGRAG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011478961 202 HVAYPH-LARNPIHQAMPALDALVNEHWDAGNDFFPATS---FQISNLRAGTGAtNVIPGEVEVVFNFR 266
Cdd:PRK08737 180 HASGKQdPSASALHQAMRWGGQALDHVESLAHARFGGLTglrFNIGRVEGGIKA-NMIAPAAELRFGFR 247
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
38-350 |
1.72e-15 |
|
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: 77.00 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 38 ERLTALGFHIEqLPFGDVKNFWAVRGHH--GPVLAFAGHTDVVPSGPHTNWefpPFEPCIDDQGMLCGRGAadmkgsLAA 115
Cdd:TIGR01891 27 EALESLGIEVR-RGVGGATGVVATIGGGkpGPVVALRADMDALPIQEQTDL---PYKSTNPGVMHACGHDL------HTA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 116 MLTAVERFVARYPDH-DGRIAFLITSDEEGPAidGTRAVVEHlrERNDRLDYCIVGEPSSTARLGdVIKNGRRGSLGGV- 193
Cdd:TIGR01891 97 ILLGTAKLLKKLADLlEGTVRLIFQPAEEGGG--GATKMIED--GVLDDVDAILGLHPDPSIPAG-TVGLRPGTIMAAAd 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 194 ---LHIKGIQGHVAYPHLARNPI---HQAMPALDALVNEHWDAgNDFFPATSFQISnlraGTGATNVIPGEVEVVFNFRY 267
Cdd:TIGR01891 172 kfeVTIHGKGAHAARPHLGRDALdaaAQLVVALQQIVSRNVDP-SRPAVVSVGIIE----AGGAPNVIPDKASMSGTVRS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 268 STEVTHDELRSRTEAILDQ----HGLEYHIDWTlNGEPFLTSEGELVEAAIRGVEAVTGERPA----LSTSGGTSDGRF- 338
Cdd:TIGR01891 247 LDPEVRDQIIDRIERIVEGaaamYGAKVELNYD-RGLPAVTNDPALTQILKEVARHVVGPENVaedpEVTMGSEDFAYYs 325
|
330
....*....|....*...
gi 1011478961 339 ------IATLGTQVVELG 350
Cdd:TIGR01891 326 qkvpgaFFFLGIGNEGTG 343
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
71-374 |
4.14e-15 |
|
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex.
Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 76.23 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 71 FAGHTDVVPSGPHTNWEFPPFEPCIDDqGMLCGRGAADMKG-SLAAMLTAVERFVARYPDHDgrIAFLITSDEE-GPAid 148
Cdd:cd05677 76 FYGHYDVIPAGETDGWDTDPFTLTCEN-GYLYGRGVSDNKGpLLAAIYAVAELFQEGELDND--VVFLIEGEEEsGSP-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 149 GTRAVVEHLRERNDRLDYCIVgepSSTARLGD---VIKNGRRGSL------------------GGVLH------------ 195
Cdd:cd05677 151 GFKEVLRKNKELIGDIDWILL---SNSYWLDDnipCLNYGLRGVIhativvssdkpdlhsgvdGGVLReptadlikllsk 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 196 IKGIQGHVAYPHLARN--PIHQAMPAL------DALVNEHWDA----GNDFFPA---TSFQISnlraGTGATNVIPGEVE 260
Cdd:cd05677 228 LQDPDGRILIPHFYDPvkPLTEAERARftaiaeTALIHEDTTVdsliAKWRKPSltvHTVKVS----GPGNTTVIPKSAS 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 261 VVFNFRY----STEVTHDELRSRTEAILDQHGLEYHIDWTLNG--EPFLTS-EGELVEAAIRGVEAVTGERPALSTSGGT 333
Cdd:cd05677 304 ASVSIRLvpdqDLDVIKQDLTDYIQSCFAELKSQNHLDIEVLNeaEPWLGDpDNPAYQILREAVTAAWGVEPLYIREGGS 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1011478961 334 SDG-RFIA-TLGTQVVEL--GPLNDTIHKVNERVRASDLDALSRI 374
Cdd:cd05677 384 IPTiRFLEkEFNAPAVQLpcGQSSDNAHLDNERLRIKNLYKMREI 428
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
18-376 |
6.23e-14 |
|
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: 72.48 E-value: 6.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 18 ELLRRASVTPDDEGCQDLMIERLTALGFHIEQLPFGDVKNF--------WAVRGHHGPVLAFAGHTDVVPSGPHTnwefp 89
Cdd:cd05683 11 ELVQIDSETLHEKEISKVLKKKFENLGLSVIEDDAGKTTGGgagnlictLKADKEEVPKILFTSHMDTVTPGINV----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 90 pfEPCIDDQGMLCGRG----AADMKGSLAAMLTAVERFVARYPDHdGRIAFLITSDEEGPAIdGTRAVvehlreRNDRLD 165
Cdd:cd05683 86 --KPPQIADGYIYSDGttilGADDKAGIAAILEAIRVIKEKNIPH-GQIQFVITVGEESGLV-GAKAL------DPELID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 166 ----YCI-----VGEPSSTARLGDVIKngrrgslggvLHIKGIQGHVA-YPHLARNPIhqaMPALDALVNEHWDAGNDFf 235
Cdd:cd05683 156 adygYALdsegdVGTIIVGAPTQDKIN----------AKIYGKTAHAGtSPEKGISAI---NIAAKAISNMKLGRIDEE- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 236 paTSFQISNLRAGTgATNVIPGEVEVVFNFR------YSTEVTHdeLRSRTEAILDQHGLEYHIDWTLNGEPFLTSEGE- 308
Cdd:cd05683 222 --TTANIGKFQGGT-ATNIVTDEVNIEAEARsldeekLDAQVKH--MKETFETTAKEKGAHAEVEVETSYPGFKINEDEe 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011478961 309 LVEAAIRGVEAVtGERPALSTSGGTSDGRFIATLGTQVVELGPLNDTIHKVNERVRASDL-DALSRIYE 376
Cdd:cd05683 297 VVKLAKRAANNL-GLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLyDTAVLVVE 364
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
13-179 |
8.48e-14 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 72.38 E-value: 8.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 13 LKLAFELLRRASVTP---DDEGCQDLMIERLTALGFHI--EQLPFGDvKNFWAVRGHHGP----VLAFAGHTDVVPSGPH 83
Cdd:PRK08596 16 LELLKTLVRFETPAPparNTNEAQEFIAEFLRKLGFSVdkWDVYPND-PNVVGVKKGTESdaykSLIINGHMDVAEVSAD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 84 TNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFL-ITSDEEGPAidGTRAVVehlrERND 162
Cdd:PRK08596 95 EAWETNPFEPTIKD-GWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQsVIGEEVGEA--GTLQCC----ERGY 167
|
170
....*....|....*..
gi 1011478961 163 RLDYCIVGEPSSTARLG 179
Cdd:PRK08596 168 DADFAVVVDTSDLHMQG 184
|
|
| PRK06915 |
PRK06915 |
peptidase; |
16-202 |
9.41e-14 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 72.03 E-value: 9.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 16 AFELLRR----ASVTPDDEGCQDLMIERLTALG------------------FHIEQLPFGDVKNFWAV-RGH-HGPVLAF 71
Cdd:PRK06915 19 AVKLLKRliqeKSVSGDESGAQAIVIEKLRELGldldiwepsfkklkdhpyFVSPRTSFSDSPNIVATlKGSgGGKSMIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 72 AGHTDVVPSGPHTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEE-GPAidGT 150
Cdd:PRK06915 99 NGHIDVVPEGDVNQWDHHPYSGEVIG-GRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEEsGGA--GT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1011478961 151 RAVVehlrERNDRLDYCIVGEPSSTArlgdvIKNGRRGSLGGVLHIKGIQGH 202
Cdd:PRK06915 176 LAAI----LRGYKADGAIIPEPTNMK-----FFPKQQGSMWFRLHVKGKAAH 218
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
114-323 |
2.37e-12 |
|
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: 67.83 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 114 AAMLTAVERFVARYPDHDGRIAFLITSDEEGPAidGTRAVVEH-LRERNDrLDYCI-----VGEPSSTArlgdVIKNGRR 187
Cdd:COG1473 107 AMLLGAAKALAELRDELKGTVRLIFQPAEEGGG--GAKAMIEDgLLDRPD-VDAIFglhvwPGLPVGTI----GVRPGPI 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 188 --GSLGGVLHIKGIQGHVAYPHLARNPIH---QAMPALDALVNEHWDagndffPATSFQIS--NLRAGTgATNVIPGEVE 260
Cdd:COG1473 180 maAADSFEITIKGKGGHAAAPHLGIDPIVaaaQIVTALQTIVSRNVD------PLDPAVVTvgIIHGGT-APNVIPDEAE 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011478961 261 VVFNFRYSTEVTHDELRSRTEAILDQ----HGLEYHIDWTlNGEPFLTSEGELVEAAIRGVEAVTGE 323
Cdd:COG1473 253 LEGTVRTFDPEVRELLEERIERIAEGiaaaYGATAEVEYL-RGYPPTVNDPELTELAREAAREVLGE 318
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
73-343 |
2.74e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 67.57 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 73 GHTDVVPSGPhTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVA--RYPDHDGRIAFLitSDEEGPAIDGT 150
Cdd:PRK07906 72 GHLDVVPAEA-ADWSVHPFSGEIRD-GYVWGRGAVDMKDMDAMMLAVVRHLARtgRRPPRDLVFAFV--ADEEAGGTYGA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 151 RAVVEHLRERNDRLDYCI--VGEPSSTARLGD---VIKNGRRGSLGGVLHIKGIQGHVAYPH-----------LARNPIH 214
Cdd:PRK07906 148 HWLVDNHPELFEGVTEAIseVGGFSLTVPGRDrlyLIETAEKGLAWMRLTARGRAGHGSMVNddnavtrlaeaVARIGRH 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 215 Q----AMPALDALVNEHWDA-GNDFFP----ATSFQISNLRAGTGAT----------------NVIPGEVEVVFNFRY-- 267
Cdd:PRK07906 228 RwplvLTPTVRAFLDGVAELtGLEFDPddpdALLAKLGPAARMVGATlrntanptmlkagykvNVIPGTAEAVVDGRFlp 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 268 ----STEVTHDEL---RSRTEAILDQHGLEYhidwtlngePFltsEGELVEAAIRGVEAvtgERPALST-----SGGTsD 335
Cdd:PRK07906 308 greeEFLATVDELlgpDVEREWVHRDPALET---------PF---DGPLVDAMNAALLA---EDPGARVvpymlSGGT-D 371
|
....*...
gi 1011478961 336 GRFIATLG 343
Cdd:PRK07906 372 AKAFSRLG 379
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
66-381 |
4.06e-12 |
|
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: 67.12 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 66 GPVLAFAGHTDVVPSgphTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERfvARYPDHDGRIAFLITSDEEGP 145
Cdd:cd08013 68 GKSLMLNGHIDTVTL---DGYDGDPLSGEIAD-GRVYGRGTLDMKGGLAACMAALAD--AKEAGLRGDVILAAVADEEDA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 146 AIdGTRAVVehlrERNDRLDYCIVGEPSSTArlgdvIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQA---MPALDA 222
Cdd:cd08013 142 SL-GTQEVL----AAGWRADAAIVTEPTNLQ-----IIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAgyfLVALEE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 223 LVNE-HWDAGNDFFPATSFQISNLRAGTgATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILD---QHGLEYHIDW--- 295
Cdd:cd08013 212 YQQElPERPVDPLLGRASVHASLIKGGE-EPSSYPARCTLTIERRTIPGETDESVLAELTAILGelaQTVPNFSYREpri 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 296 TLNGEPF-LTSEGELVEAAIRGVEAVTGERPALSTSGGTSDGRFIATLGTQVVELGPLNDTIHKVNERVRASDLDALSRI 374
Cdd:cd08013 291 TLSRPPFeVPKEHPFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGAGLHAKEEWVDVESIRQLREV 370
|
....*..
gi 1011478961 375 YEATLQA 381
Cdd:cd08013 371 LSAVVRE 377
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
13-330 |
6.95e-12 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 65.97 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 13 LKLAFELLRRASVTPDDEGCQDLMIERLTALGFH-IEQLPFGDVKNFWAVRGHhGPVLAFAGHTDVVPSGpHTNWEfppf 91
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGLGdVERDGRGNVVGRLRGTGG-GPALLFSAHLDTVFPG-DTPAT---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 92 epCIDDQGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEGPAID-GTRAVVEHLRernDRLDYCIVG 170
Cdd:cd03896 75 --VRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEGLGDLrGARYLLSAHG---ARLDYFVVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 171 EPSstarlGDVIKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHqampALDALVNEHWDAGNDFFPATSFQISNLRAGTG 250
Cdd:cd03896 150 EGT-----DGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIV----AMAKLVEALYEWAAPYVPKTTFAAIRGGGGTS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 251 AtNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEyHIDWTLNGEPFLTSEGELV----------EAAIRgvEAV 320
Cdd:cd03896 221 V-NRIANLCSMYLDIRSNPDAELADVQREVEAVVSKLAAK-HLRVKARVKPVGDRPGGEAqgteplvnaaVAAHR--EVG 296
|
330
....*....|
gi 1011478961 321 TGERPALSTS 330
Cdd:cd03896 297 GDPRPGSSST 306
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
26-143 |
2.30e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 65.10 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 26 TPDDEGCQDLMIERLT---ALGFHIEQLPFGDVKnfWAVRGHHGPVLAFAGHTDVVPSGPHTNWEFPPFEPCIDDqGMLC 102
Cdd:PRK07205 34 TPFGQAIQDVLEATLDlcqGLGFKTYLDPKGYYG--YAEIGQGEELLAILCHLDVVPEGDLSDWQTPPFEAVEKD-GCLF 110
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1011478961 103 GRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEE 143
Cdd:PRK07205 111 GRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGTDEE 151
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
17-214 |
3.96e-11 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 64.15 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 17 FELLRRASVTPD---DEGCQ---DLMIERLTALGFHIEQLPFGDVKnfwAVRGHH------GPVLAFAGHTDVVPSGPHT 84
Cdd:PRK09104 24 FALLRIPSISTDpayAADCRkaaDWLVADLASLGFEASVRDTPGHP---MVVAHHegptgdAPHVLFYGHYDVQPVDPLD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 85 NWEFPPFEPCIDDQG----MLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEgpaiDGTRAVVEHLRER 160
Cdd:PRK09104 101 LWESPPFEPRIKETPdgrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEE----SGSPSLVPFLEAN 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011478961 161 NDRL--DYCIV--------GEPSSTARLgdvikngrRGSLGGVLHIKGI-----QGHvaYPHLARNPIH 214
Cdd:PRK09104 177 AEELkaDVALVcdtgmwdrETPAITTSL--------RGLVGEEVTITAAdrdlhSGL--FGGAAANPIR 235
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
1-376 |
4.41e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 64.25 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 1 MPITEPASLSPTLKLAFELLRRA----------SVTPddegCQDLMIERLTALGFHIEQL----PFGDVKNFwaVRGHHG 66
Cdd:PRK09133 24 AAAAAPAAPTADQQAARDLYKELieinttastgSTTP----AAEAMAARLKAAGFADADIevtgPYPRKGNL--VARLRG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 67 -----PVLaFAGHTDVVPSGPHTnWEFPPFEPCIDDqGMLCGRGAADMKgSLAAMLTAV------ERFVaryPDHDGRIA 135
Cdd:PRK09133 98 tdpkkPIL-LLAHMDVVEAKRED-WTRDPFKLVEEN-GYFYGRGTSDDK-ADAAIWVATlirlkrEGFK---PKRDIILA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 136 FliTSDEEGPAIDGTRAVVEHLRERNDrLDYCIvgepsSTARLGDVIKNGRRGSL---GG-------VLHIKGIQGHVAY 205
Cdd:PRK09133 171 L--TGDEEGTPMNGVAWLAENHRDLID-AEFAL-----NEGGGGTLDEDGKPVLLtvqAGektyadfRLEVTNPGGHSSR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 206 PhLARNPIHQAMPALDALVN-----EHWDAGNDFFPATSFQ---------------------ISNLRA------------ 247
Cdd:PRK09133 243 P-TKDNAIYRLAAALSRLAAyrfpvMLNDVTRAYFKQSAAIetgplaaamrafaanpadeaaIALLSAdpsynamlrttc 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 248 ------GTGATNVIPGEVEVVFNFRYSTEVTHDELRSRTEAILDQHGLEYhidwTLNGEPFLTSEGELVEAAIRGVEAVT 321
Cdd:PRK09133 322 vatmleGGHAENALPQRATANVNCRIFPGDTIEAVRATLKQVVADPAIKI----TRIGDPSPSPASPLRPDIMKAVEKLT 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1011478961 322 GER-------PALSTsgGTSDGRF-----IATLGTQVVELGPLNDTIHKVNERVR-ASDLDALSRIYE 376
Cdd:PRK09133 398 AAMwpgvpviPSMST--GATDGRYlraagIPTYGVSGLFGDPDDTFAHGLNERIPvASFYEGRDFLYE 463
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
63-383 |
4.59e-11 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 63.83 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 63 GHHGPVLA------------FAGHTDVVPSGPHtnwefpPFEPCID-DQGMLCGRGAADMKGSLAAMLTAVERFvARYPD 129
Cdd:PRK07338 77 QAHGPALHvsvrpeaprqvlLTGHMDTVFPADH------PFQTLSWlDDGTLNGPGVADMKGGIVVMLAALLAF-ERSPL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 130 HDgRIAF--LITSDEEGPAIdGTRAVVEHLRERND-RLDYcivgEPsstARLGDVIKNGRRGSlgGVLHIKgIQGHVAY- 205
Cdd:PRK07338 150 AD-KLGYdvLINPDEEIGSP-ASAPLLAELARGKHaALTY----EP---ALPDGTLAGARKGS--GNFTIV-VTGRAAHa 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 206 ---PHLARNPIHQAMPALDALvnehwDAGNDFFPATSFQISNLrAGTGATNVIPGEVEVVFNFRYSTE----VTHDELRS 278
Cdd:PRK07338 218 graFDEGRNAIVAAAELALAL-----HALNGQRDGVTVNVAKI-DGGGPLNVVPDNAVLRFNIRPPTPedaaWAEAELKK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 279 RTEAILDQHGLEYHI--DWTLNGEPFLTSEGELVEaAIRGVEAVTGERPALSTSGGTSDGRFIATLGTQVVE-LGPLNDT 355
Cdd:PRK07338 292 LIAQVNQRHGVSLHLhgGFGRPPKPIDAAQQRLFE-AVQACGAALGLTIDWKDSGGVCDGNNLAAAGLPVVDtLGVRGGN 370
|
330 340
....*....|....*....|....*...
gi 1011478961 356 IHKVNERVRasdLDALSRiyEATLQALL 383
Cdd:PRK07338 371 IHSEDEFVI---LDSLVE--RAQLSALI 393
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
74-382 |
8.59e-11 |
|
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: 63.06 E-value: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 74 HTDVVPSGPhTNWEFPPFEPCIDDQGMLCGRGAADMKGSLAAMLTAVERFVARypdhdGR-----IAFLITSDEEGPAID 148
Cdd:cd05646 72 HTDVVPVFE-EKWTHDPFSAHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKAS-----GFkpkrtIHLSFVPDEEIGGHD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 149 GTRAVVEHLRERNDRLDYCI---VGEPSSTARLgdviKNGRRGSLGGVLHIKGIQGHVA--YPHLARNPIHQAMPALDAL 223
Cdd:cd05646 146 GMEKFVKTEEFKKLNVGFALdegLASPTEEYRV----FYGERSPWWVVITAPGTPGHGSklLENTAGEKLRKVIESIMEF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 224 VNEHWD---AGNDFFPA--TSFQISNLRAGTgATNVIPGEVEVVFNFRYSTEVTHDELRSR-----TEAILD------QH 287
Cdd:cd05646 222 RESQKQrlkSNPNLTLGdvTTVNLTMLKGGV-QMNVVPSEAEAGFDLRIPPTVDLEEFEKQidewcAEAGRGvtyefeQK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 288 GLEYHIDWTLNGEPFLTSEGELVEAAirGVEAVTGERPAlstsggTSDGRFIATLGTQVVELGPLNDT---IHKVNERVR 364
Cdd:cd05646 301 SPEKDPTSLDDSNPWWAAFKKAVKEM--GLKLKPEIFPA------ATDSRYIRALGIPALGFSPMNNTpilLHDHNEFLN 372
|
330
....*....|....*...
gi 1011478961 365 ASDLDALSRIYEATLQAL 382
Cdd:cd05646 373 EDVFLRGIEIYEKIIPAL 390
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
59-224 |
2.18e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 61.85 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 59 WAVRGHHGP------VLAFAgHTDVVPSGPHTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHdg 132
Cdd:PRK07907 71 PAVIGTRPAppgaptVLLYA-HHDVQPPGDPDAWDSPPFELTERD-GRLYGRGAADDKGGIAMHLAALRALGGDLPVG-- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 133 rIAFLITSDEEGpaidGTRAVVEHLRERNDRL--DYCI--------VGEPSSTARLgdvikngrRGSLGGVLHIKGIQGh 202
Cdd:PRK07907 147 -VTVFVEGEEEM----GSPSLERLLAEHPDLLaaDVIViadsgnwsVGVPALTTSL--------RGNADVVVTVRTLEH- 212
|
170 180
....*....|....*....|....*
gi 1011478961 203 vayphlarnPIHQAM---PALDALV 224
Cdd:PRK07907 213 ---------AVHSGQfggAAPDALT 228
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
18-227 |
5.01e-10 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 60.91 E-value: 5.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 18 ELLRRASVTPDDEGCQDL------MIERLTALGF-HIEQLPFGDVKNFWAVRGHH--GPVLAFAGHTDVVPSGPHTNWEF 88
Cdd:PRK08201 22 EFLRIPSISALSEHKEDVrkaaewLAGALEKAGLeHVEIMETAGHPIVYADWLHApgKPTVLIYGHYDVQPVDPLNLWET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 89 PPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEgpaiDGTRAVVEHLRERNDRL--DY 166
Cdd:PRK08201 102 PPFEPTIRD-GKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEE----IGSPNLDSFVEEEKDKLaaDV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011478961 167 CIVGEPSSTARLGDVIKNGRRGSLGGVLHIKGIQGHV---AYPHLARNPIHQAMPALDALVNEH 227
Cdd:PRK08201 177 VLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLhsgLYGGAVPNALHALVQLLASLHDEH 240
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
101-212 |
5.08e-09 |
|
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: 57.74 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 101 LCGRGAADMKGSLAAMLTAVERFvARYPDHDGRIAFLITSDEEGPAiDGTRAVVEHLRE--RNDRLDY--CIVGEPSSTA 176
Cdd:cd05654 126 LFGRGTMDMKSGLAVHLALLEQA-SEDEDFDGNLLLMAVPDEEVNS-RGMRAAVPALLElkKKHDLEYklAINSEPIFPQ 203
|
90 100 110
....*....|....*....|....*....|....*....
gi 1011478961 177 RLGDVIKNGRRGSLGGVL---HIKGIQGHVAYPHLARNP 212
Cdd:cd05654 204 YDGDQTRYIYTGSIGKILpgfLCYGKETHVGEPFAGINA 242
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
34-168 |
7.65e-09 |
|
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: 57.23 E-value: 7.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 34 DLMIERLTALGFHIEQLPFGDVKNFWAVRGHHGPVLaFA--------------GHTDVVPSGPHTNWEFPPFEpCIDDQG 99
Cdd:cd05676 40 EWAAERLEKLGFKVELVDIGTQTLPDGEELPLPPVL-LGrlgsdpskktvliyGHLDVQPAKLEDGWDTDPFE-LTEKDG 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011478961 100 MLCGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEgpaiDGTRAVVEHLRERNDRL----DY-CI 168
Cdd:cd05676 118 KLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEGMEE----SGSEGLDELIEARKDTFfsdvDYvCI 187
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
64-285 |
1.37e-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: 56.31 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 64 HHGPVLAFAG-HTDVVPSGPHTnWEFPPFEPCID-DQgmLCGRGAADMKGSLAaMLTAVERFVArypdhdgriaflitsd 141
Cdd:cd08012 75 VDGKTVSFVGsHMDVVTANPET-WEFDPFSLSIDgDK--LYGRGTTDCLGHVA-LVTELFRQLA---------------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 142 EEGPAIDGTRAVVEHLRERNDRLDYCIVGEPSSTARLgDVIKNGRR------------GSLGGV---LHIKGIQGHVAYP 206
Cdd:cd08012 135 TEKPALKRTVVAVFIANEENSEIPGVGVDALVKSGLL-DNLKSGPLywvdsadsqpciGTGGMVtwkLTATGKLFHSGLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 207 HLARNPIHQAMPALDALVNEHWdagNDFFP-----ATSFQISNLRAGT------GATNVIPGEVEVVFNFRYSTEVTHDE 275
Cdd:cd08012 214 HKAINALELVMEALAEIQKRFY---IDFPPhpkeeVYGFATPSTMKPTqwsypgGSINQIPGECTICGDCRLTPFYDVKE 290
|
250
....*....|
gi 1011478961 276 LRSRTEAILD 285
Cdd:cd08012 291 VREKLEEYVD 300
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
195-332 |
1.40e-08 |
|
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: 56.14 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 195 HIKGIQGHVAYPHLARNPIHQAMPALDALVNEHWDAGNdffpATSFQISNLRAGTGATNVIPGEVEVVFNFRYSTEVTHD 274
Cdd:cd08018 173 TIKGKQAHGARPHLGINAIEAASAIVNAVNAIHLDPNI----PWSVKMTKLQAGGEATNIIPDKAKFALDLRAQSNEAME 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011478961 275 ELRSRTEAILDQHGLEYH--IDWTLNGE-PFLTSEGELVEAAIRGVEAVTGE---RPALSTSGG 332
Cdd:cd08018 249 ELKEKVEHAIEAAAALYGasIEITEKGGmPAAEYDEEAVELMEEAITEVLGEeklAGPCVTPGG 312
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
34-383 |
4.65e-08 |
|
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: 54.48 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 34 DLMIERLTALGFHIEQ--LPFGDVKNF-------WAVRGHHGP---VLAFAGHTDVVPsgPHTNWEFPPFEPCIDDqGML 101
Cdd:cd02697 29 ERTAALLQGFGFEAERhpVPEAEVRAYgmesitnLIVRRRYGDggrTVALNAHGDVVP--PGDGWTRDPYGAVVED-GVM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 102 CGRGAADMKGSLAAMLTAVERFVARYPDHDGRIAFLITSDEEGPAIDGTRAVvehLRERNDRLDYCIvgepssTARLGDV 181
Cdd:cd02697 106 YGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGELGPGWL---LRQGLTKPDLLI------AAGFSYE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 182 IKNGRRGSLGGVLHIKGIQGHVAYPHLARNPIHQAMPALDALVnehwdAGNDFFPATSFQISNLRA---------GTGAT 252
Cdd:cd02697 177 VVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALY-----ALNAQYRQVSSQVEGITHpylnvgrieGGTNT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 253 NVIPGEVEVVFNFRY-----STEVTHDELRSRTEAILDQHGLEYHIDWTLNGEPF--LTSEGELVEAAIRGVEAVTGER- 324
Cdd:cd02697 252 NVVPGKVTFKLDRRMipeenPVEVEAEIRRVIADAAASMPGISVDIRRLLLANSMrpLPGNAPLVEAIQTHGEAVFGEPv 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011478961 325 PALSTSGGTsDGRFIATLGTQVVELGP-----LNDTIHKVNERVRASDLDALSRIYEATLQALL 383
Cdd:cd02697 332 PAMGTPLYT-DVRLYAEAGIPGVIYGAgprtvLESHAKRADERLQLEDLRRATKVIARSLRDLL 394
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
114-327 |
5.53e-08 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 54.14 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 114 AAMLTAVERFVARYPDHDGRIAFLITSDEEGPAidGTRAVVEHLRERNDRLDYcIVGEPSSTArlgdvIKNGRRGSLGGV 193
Cdd:cd03886 95 AMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPG--GAKAMIEEGVLENPGVDA-AFGLHVWPG-----LPVGTVGVRSGA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 194 LH---------IKGIQGHVAYPHLARNPIH---QAMPALDALVNEHWDagndffPATSFQIS--NLRAGTgATNVIPGEV 259
Cdd:cd03886 167 LMasadefeitVKGKGGHGASPHLGVDPIVaaaQIVLALQTVVSRELD------PLEPAVVTvgKFHAGT-AFNVIPDTA 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011478961 260 EVVFNFRYST----EVTHDELRSRTEAILDQHGLEYHIDWtLNGEPFLTSEGELVEAAIRGVEAVTGERPAL 327
Cdd:cd03886 240 VLEGTIRTFDpevrEALEARIKRLAEGIAAAYGATVELEY-GYGYPAVINDPELTELVREAAKELLGEEAVV 310
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
103-203 |
1.35e-07 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 53.32 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 103 GRGAADMKGSLAAMLTAVERFvARYPDHDGRIAFLITSDEEGPAIdGTRAVVEHLRERNDR--LDY--CIVGEPSSTARL 178
Cdd:COG4187 134 GRGTMDMKAGLALHLALLEEA-SENEEFPGNLLLLAVPDEEVNSA-GMRAAVPLLAELKEKygLEYklAINSEPSFPKYP 211
|
90 100 110
....*....|....*....|....*....|.
gi 1011478961 179 GDvikNGRR---GSLGGVL---HIKGIQGHV 203
Cdd:COG4187 212 GD---ETRYiytGSIGKLMpgfYCYGKETHV 239
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
74-367 |
2.85e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 52.06 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 74 HTDVVPSGPHTNWEFPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHDGrIAFLITSDEEGPAIDgtrav 153
Cdd:PRK06446 70 HYDVQPVDPLSEWKRDPFSATIEN-GRIYARGASDNKGTLMARLFAIKHLIDKHKLNVN-VKFLYEGEEEIGSPN----- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 154 VEHLRERNDRL---DYCIVGEPSSTARLGDVIKNGRRGSLGGVLHIKGIQG--HVAYPHLARNPIHQAMPALDALV---- 224
Cdd:PRK06446 143 LEDFIEKNKNKlkaDSVIMEGAGLDPKGRPQIVLGVKGLLYVELVLRTGTKdlHSSNAPIVRNPAWDLVKLLSTLVdgeg 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 225 -------------------------------------------NEHWDAGNDFFPATSFQISNLRA---GTGATNVIPGE 258
Cdd:PRK06446 223 rvlipgfyddvrelteeerellkkydidveelrkalgfkelkySDREKIAEALLTEPTCNIDGFYSgytGKGSKTIVPSR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 259 VEVVFNFRYSTEVTHDELRSRTEAILDQ---------HGLEYhidwtlngePFLTS-EGELVEAAIRGVEAVTGERP-AL 327
Cdd:PRK06446 303 AFAKLDFRLVPNQDPYKIFELLKKHLQKvgfngeiivHGFEY---------PVRTSvNSKVVKAMIESAKRVYGTEPvVI 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1011478961 328 STSGGTSD-GRFIATLG-TQVVE---LGPLNDTIHKVNERVRASD 367
Cdd:PRK06446 374 PNSAGTQPmGLFVYKLGiRDIVSaigVGGYYSNAHAPNENIRIDD 418
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
35-322 |
6.06e-06 |
|
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1L2 family contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.
Pssm-ID: 349945 [Multi-domain] Cd Length: 366 Bit Score: 48.01 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 35 LMIERLTALGFHIEQLPfGDVKNFWAV--RGHHGPVLAFAGHTDVVPSGPHTNWefpPFEPCIDDQGMLCGRgaadmKGS 112
Cdd:cd08660 24 KIRRWLEEEQIEILDVP-QLKTGVIAEikGGEDGPVIAIRADIDALPIQEQTNL---PFASKVDGT*HACGH-----DFH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 113 LAAMLTAVERFVARYPDHDGRIAFLITSDEEGPAidGTRAVVEhlRERNDRLDYCIVGEPSSTARLGDV-IKNGRRGSLG 191
Cdd:cd08660 95 TTSIIGTA*LLNQRRAELKGTVVFIFQPAEEGAA--GARKVLE--AGVLNGVSAIFGIHNKPDLPVGTIgVKEGPL*ASV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 192 GVLH--IKGIQGHVAYPHLARNPIHQA---MPALDALVNEHWDAGNDffpaTSFQISNLRAGTgATNVIPGEVEVVFNFR 266
Cdd:cd08660 171 DVFEivIKGKGGHASIPNNSIDPIAAAgqiISGLQSVVSRNISSLQN----AVVSITRVQGGT-AWNVIPDQAE*EGTVR 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 267 YSTEVTHDEL----RSRTEAILDQHGLEYHIDWTLNGEPFLTSEGELVEAAIRGVEAVTG 322
Cdd:cd08660 246 AFTKEARQAVpeh*RRVAEGIAAGYGCQAEFKWFPNGPSEVQNDGTLLNAFSKAAARLGY 305
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
20-342 |
4.95e-05 |
|
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.
Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 45.21 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 20 LRRASVTPDDEGCQDLMIERLTALGFHIEQLPFGDVKNFWAVRGHHGPVLAFAGHTDVVPSGphtnwefppfepciddqg 99
Cdd:cd03884 19 VTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVGNLFGRLEGTDPDAPPVLTGSHLDTVPNG------------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 100 mlcGR--GAAdmkGSLAAmLTAVER-----FVARYPdhdgrIAFLITSDEEG----PAIDGTRAVV-----EHLRERNDR 163
Cdd:cd03884 81 ---GRydGIL---GVLAG-LEALRAlkeagIRPRRP-----IEVVAFTNEEGsrfpPSMLGSRAFAgtldlEELLSLRDA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 164 LDYCIVGEPSSTARLGDVIKNGR-RGSLGGV--LHI----------------KGIQGHVAY--------------PHLAR 210
Cdd:cd03884 149 DGVSLAEALKAIGYDGDRPASARrPGDIKAYveLHIeqgpvleeeglpigvvTGIAGQRWLevtvtgeaghagttPMALR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 211 npiHQAMPALDALVNEHWDAGNDFFPATSFQISNLRAGTGATNVIPGEVEVVFNFRY----STEVTHDELRSRTEAILDQ 286
Cdd:cd03884 229 ---RDALLAAAELILAVEEIALEHGDDLVATVGRIEVKPNAVNVIPGEVEFTLDLRHpddaVLDAMVERIRAEAEAIAAE 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1011478961 287 HGLEYHIDWTLNGEPFLTSEgELVEAAIRGVEAVtGERPALSTSGGTSDGRFIATL 342
Cdd:cd03884 306 RGVEVEVERLWDSPPVPFDP-ELVAALEAAAEAL-GLSYRRMPSGAGHDAMFMARI 359
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
102-283 |
6.36e-05 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349914 [Multi-domain] Cd Length: 399 Bit Score: 44.64 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 102 CGRgaaDMKgsLAAMLTAVERFVARYPDHDGRIAFLITSDEEGpaIDGTRAVVEH-LRERNDRLDYC----IVGEPSSTA 176
Cdd:cd05664 98 CGH---DMH--VAALLGAARLLVEAKDAWSGTLIAVFQPAEET--GGGAQAMVDDgLYDKIPKPDVVlaqhVMPGPAGTV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 177 rlgdVIKNGRRGSLGGVL--HIKGIQGHVAYPHLARNPIHQAMPA---LDALVNEHWDAgNDFFPATsfqISNLRAGTgA 251
Cdd:cd05664 171 ----GTRPGRFLSAADSLdiTIFGRGGHGSMPHLTIDPVVMAASIvtrLQTIVSREVDP-QEFAVVT---VGSIQAGS-A 241
|
170 180 190
....*....|....*....|....*....|..
gi 1011478961 252 TNVIPGEVEVVFNFRYSTEVTHDELRSRTEAI 283
Cdd:cd05664 242 ENIIPDEAELKLNVRTFDPEVREKVLNAIKRI 273
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
196-320 |
8.46e-05 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 44.19 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 196 IKGIQGHVAYPHLARNPI---HQAMPALDALVNEHWDAgndFFPA----TSFQisnlraGTGATNVIPGEVEVVFNFRYS 268
Cdd:cd08021 188 IKGKGGHGSMPHETVDPIviaAQIVTALQTIVSRRVDP---LDPAvvtiGTFQ------GGTSFNVIPDTVELKGTVRTF 258
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1011478961 269 TEVTHDELRSRTEAIL----DQHGLEYHIDWtLNGEPFLTSEGELVEAAIRGVEAV 320
Cdd:cd08021 259 DEEVREQVPKRIERIVkgicEAYGASYELEY-QPGYPVVYNDPEVTELVKKAAKEV 313
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
194-323 |
2.03e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349916 [Multi-domain] Cd Length: 373 Bit Score: 42.90 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 194 LHIKGIQGHVAYPHLARNPI---HQAMPALDALVNEHWDAGNdffPA----TSFQisnlrAGTgATNVIPGEVEVVFNFR 266
Cdd:cd05666 177 ITIRGKGGHAAMPHLGVDPIvaaAQLVQALQTIVSRNVDPLD---AAvvsvTQIH-----AGD-AYNVIPDTAELRGTVR 247
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011478961 267 YSTEVTHDELRSRTEAILDQ----HGLEYHIDWTlNGEPFLTSEGELVEAAIRGVEAVTGE 323
Cdd:cd05666 248 AFDPEVRDLIEERIREIADGiaaaYGATAEVDYR-RGYPVTVNDAEETAFAAEVAREVVGA 307
|
|
| PRK12890 |
PRK12890 |
allantoate amidohydrolase; Reviewed |
22-382 |
5.68e-04 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 237248 [Multi-domain] Cd Length: 414 Bit Score: 41.81 E-value: 5.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 22 RASVTPDDEGCQDLMIERLTALGFHIEQLPFGDVKNFWAVRGHHGPVLAFAGHTDVVPSGphtnwefppfepciddqgml 101
Cdd:PRK12890 30 RLALSDEERAARALLAAWMRAAGLEVRRDAAGNLFGRLPGRDPDLPPLMTGSHLDTVPNG-------------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 102 cgrGAAD-MKGSLAAMLtAVERFVA--RYPDHDgrIAFLITSDEEGP----------AIDGTRAVVEHLRERND------ 162
Cdd:PRK12890 90 ---GRYDgILGVLAGLE-VVAALREagIRPPHP--LEVIAFTNEEGVrfgpsmigsrALAGTLDVEAVLATRDDdgttla 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 163 ----RLDYCIVGEPSSTARLGDV-------IKNG----RRG-SLGGVLHIKGI-------QGHVAypHLARNPIHQAMPA 219
Cdd:PRK12890 164 ealrRIGGDPDALPGALRPPGAVaaflelhIEQGpvleAEGlPIGVVTAIQGIrrqavtvEGEAN--HAGTTPMDLRRDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 220 LDAL------VNEHWDAGNDFFPATsfqISNLRAGTGATNVIPGEVEVVFNFRYSTEVTHDE----LRSRTEAILDQHGL 289
Cdd:PRK12890 242 LVAAaelvtaMERRARALLHDLVAT---VGRLDVEPNAINVVPGRVVFTLDLRSPDDAVLEAaeaaLLAELEAIAAARGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 290 EYHIDWTLNGEPfLTSEGELVEAAIRGVEAVtGERPALSTSGGTSDGRFIATLGTQVVELGPLNDTI-HKVNERVRASDL 368
Cdd:PRK12890 319 RIELERLSRSEP-VPCDPALVDAVEAAAARL-GYPSRRMPSGAGHDAAAIARIGPSAMIFVPCRGGIsHNPEEAMDPEDL 396
|
410
....*....|....
gi 1011478961 369 DALSRIYEATLQAL 382
Cdd:PRK12890 397 AAGARVLLDAVLRL 410
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
20-332 |
4.81e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 38.98 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 20 LRRASVTPDDEGCQDLMIERLTALGFHIEQLPFGDVKNFWAVRGHHGPVLAFAGHTDVVPSGphtnwefppfepciddqg 99
Cdd:PRK09290 27 VTRLALSPEDLQARDLFAEWMEAAGLTVRVDAVGNLFGRLEGRDPDAPAVLTGSHLDTVPNG------------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 100 mlcGR--GAAdmkGSLAAmLTAVERFVARY--PDHDgrIAFLITSDEEG----PAIDGTRAVV-----EHLRERNDRlDY 166
Cdd:PRK09290 89 ---GRfdGPL---GVLAG-LEAVRTLNERGirPRRP--IEVVAFTNEEGsrfgPAMLGSRVFTgaltpEDALALRDA-DG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 167 CIVGEpsSTARLG---DVIKNGRR--GSLGGV--LHIK----------------GIQGHVAY--------------P-HL 208
Cdd:PRK09290 159 VSFAE--ALAAIGydgDEAVGAARarRDIKAFveLHIEqgpvleaeglpigvvtGIVGQRRYrvtftgeanhagttPmAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 209 ARNPIH---QAMPALDALVNEHWDagndffpatsfqisNLRAGTG-------ATNVIPGEVEVVFNFR-YSTEV---THD 274
Cdd:PRK09290 237 RRDALLaaaEIILAVERIAAAHGP--------------DLVATVGrlevkpnSVNVIPGEVTFTLDIRhPDDAVldaLVA 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1011478961 275 ELRSRTEAILDQHGLEYHIDWTLNGEPFLTSEGeLVEAAIRGVEAVTGERPALSTSGG 332
Cdd:PRK09290 303 ELRAAAEAIAARRGVEVEIELISRRPPVPFDPG-LVAALEEAAERLGLSYRRLPSGAG 359
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
63-197 |
5.65e-03 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 38.47 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 63 GHHGPVLAFAGHTDVVPsgPHTNWE--FPPFEPCIDDqGMLCGRGAADMKGSLAAMLTAVERFVARYPDHdGRIAFLITS 140
Cdd:cd05682 70 EQDDDTVLLYGHMDKQP--PFTGWDegLGPTKPVIRG-DKLYGRGGADDGYAIFASLTAIKALQEQGIPH-PRCVVLIEA 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1011478961 141 DEEGPAIDgTRAVVEHLRERNDRLDY--CIVGEPSSTARLGdvIKNGRRGSLGGVLHIK 197
Cdd:cd05682 146 CEESGSAD-LPFYLDKLKERIGNVDLvvCLDSGCGNYEQLW--LTTSLRGVLGGDLTVQ 201
|
|
| M20_IAA_Hyd |
cd08017 |
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ... |
196-321 |
9.26e-03 |
|
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349938 [Multi-domain] Cd Length: 376 Bit Score: 37.68 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 196 IKGIQGHVAYPHLARNPI---HQAMPALDALVNEHWDagndffPATSFQISNLRAGTG-ATNVIPGEVEVVFNFRYSTEV 271
Cdd:cd08017 175 IRGKGGHAAMPHHTVDPVvaaSSAVLALQQLVSRETD------PLDSQVVSVTRFNGGhAFNVIPDSVTFGGTLRALTTE 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011478961 272 THDELRSR-TEAILDQ---HGLEYHIDWTLNGEPF---------LTSEGELVEAAIRGVEAVT 321
Cdd:cd08017 249 GFYRLRQRiEEVIEGQaavHRCNATVDFSEDERPPypptvnderMYEHAKKVAADLLGPENVK 311
|
|
| M20_ACY1L2-like |
cd05672 |
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 ... |
204-330 |
9.79e-03 |
|
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. This subfamily includes Staphylococcus aureus antibiotic resistance factor HmrA that has been shown to participate in methicillin resistance mechanisms in vivo in the presence of beta-lactams. Aminoacylase 1 (ACY1) proteins 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 the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349921 [Multi-domain] Cd Length: 360 Bit Score: 37.93 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011478961 204 AYPHLARNpihqampALDALVnehwdagndffpaTSFQ-ISNLR---------------AGTgATNVIPGEVEVVFNFRY 267
Cdd:cd05672 174 AAPWEGIN-------ALDAAV-------------LAYNaISALRqqlkptwrihgiiteGGK-APNIIPDYAEARFYVRA 232
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011478961 268 STEVTHDELRSRTEAILD----QHGLEYHIDWTLNG-EPFLTSE--GELVEAAIR--GVEAVTGERPALSTS 330
Cdd:cd05672 233 PTRKELEELRERVIACFEgaalATGCTVEIEEDEPPyADLRPNKtlAEIYAENMEalGEEVIDDPEGVGTGS 304
|
|
| |
