|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
1-379 |
0e+00 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 719.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 1 MSATLALTEQLIARASVTPDDQHCQQLMIERLAALGFECETIASHGVTNFWAVKrgtaGRAGKLLAFAGHTDVVPTGPLE 80
Cdd:PRK13009 1 MSDVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDFGDVKNLWARR----GTEGPHLCFAGHTDVVPPGDLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 81 QWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGPATDGTVKVVEALAARGERLD 160
Cdd:PRK13009 77 AWTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVLEWLKARGEKID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 161 YCIVGEPTSTATLGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDEGNEYFPPTTWQVSNL 240
Cdd:PRK13009 157 YCIVGEPTSTERLGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEGNEFFPPTSLQITNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 241 RAGTGATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLDYTLNWSVSGLPFLTPRGELSNALDAAIRAETGVSP 320
Cdd:PRK13009 237 DAGTGATNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDYTLEWTLSGEPFLTPPGKLVDAVVAAIEAVTGITP 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 490656189 321 ELSTTGGTSDGRFIARICPQVIEFGPPNASIHKIDEHIDVRFVDPLKNVYRRVLEQLIA 379
Cdd:PRK13009 317 ELSTSGGTSDARFIADYGAQVVEFGPVNATIHKVNECVSVADLEKLTRIYERILERLLA 375
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
5-374 |
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: 635.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 5 LALTEQLIARASVTPDDQHCQQLMIERLAALGFECETIASHGVTNFWAVKrgtaGRAGKLLAFAGHTDVVPTGPLEQWSS 84
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFGGVKNLWARR----GTGGPHLCFAGHTDVVPPGDLEGWSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 85 PPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGPATDGTVKVVEALAARGERLDYCIV 164
Cdd:cd03891 77 DPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKIDYCIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 165 GEPTSTATLGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDEGNEYFPPTTWQVSNLRAGT 244
Cdd:cd03891 157 GEPTSEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLDEGNEFFPPSSLQITNIDVGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 245 GATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLDYTLNWSVSGLPFLTPRGELSNALDAAIRAETGVSPELST 324
Cdd:cd03891 237 GATNVIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELST 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 490656189 325 TGGTSDGRFIARICPQVIEFGPPNASIHKIDEHIDVRFVDPLKNVYRRVL 374
Cdd:cd03891 317 SGGTSDARFIASYGCPVVEFGLVNATIHKVNERVSVADLEKLTDIYERIL 366
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
5-377 |
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: 534.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 5 LALTEQLIARASVTPDDQHCQQLMIERLAALGFECETIASHGVTNFWAvKRGTAGragKLLAFAGHTDVVPTGPLEQWSS 84
Cdd:TIGR01246 2 TELAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGDTKNLWA-TRGTGE---PVLAFAGHTDVVPAGPEEQWSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 85 PPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGPATDGTVKVVEALAARGERLDYCIV 164
Cdd:TIGR01246 78 PPFEPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVETLMARDELIDYCIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 165 GEPTSTATLGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDEGNEYFPPTTWQVSNLRAGT 244
Cdd:TIGR01246 158 GEPSSVKKLGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAIKWDEGNEFFPPTSLQITNIHAGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 245 GATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLDYTLNWSVSGLPFLTPRGELSNALDAAIRAETGVSPELST 324
Cdd:TIGR01246 238 GANNVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELST 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 490656189 325 TGGTSDGRFIARICPQVIEFGPPNASIHKIDEHIDVRFVDPLKNVYRRVLEQL 377
Cdd:TIGR01246 318 GGGTSDGRFIALMGAEVVEFGPVNATIHKVNECVSIEDLEKLSDVYQDLLENL 370
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
1-377 |
4.19e-116 |
|
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: 342.64 E-value: 4.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 1 MSATLALTEQLIARASVTPDDQHCQQLMIERLAALGFECETIASH-GVTNFWAVKRGTAGraGKLLAFAGHTDVVPTGPL 79
Cdd:COG0624 11 LDEALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPpGRPNLVARRPGDGG--GPTLLLYGHLDVVPPGDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 80 EQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGPAtDGTVKVVEALAArGERL 159
Cdd:COG0624 89 ELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGS-PGARALVEELAE-GLKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 160 DYCIVGEPTSTatlgDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWD-EGNEYFPPTTWQVS 238
Cdd:COG0624 167 DAAIVGEPTGV----PTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDgRADPLFGRTTLNVT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 239 NLRAGTgATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLDYTLNWSV---SGLPFLTP-RGELSNALDAAIRA 314
Cdd:COG0624 243 GIEGGT-AVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEVEVlgdGRPPFETPpDSPLVAAARAAIRE 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656189 315 ETGVSPELSTTGGTSDGRFIAR-ICPQVIEFGPPN-ASIHKIDEHIDVRFVDPLKNVYRRVLEQL 377
Cdd:COG0624 322 VTGKEPVLSGVGGGTDARFFAEaLGIPTVVFGPGDgAGAHAPDEYVELDDLEKGARVLARLLERL 386
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
6-360 |
8.14e-94 |
|
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: 284.96 E-value: 8.14e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 6 ALTEQLIARASVTPDDQHCQQLMIERLAALGFECETIASHGVTNFWAvKRGTAGraGKLLAFAGHTDVVPTGPLEQWSSP 85
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVA-TVGGGD--GPVLLLNGHIDTVPPGDGDKWSFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 86 PFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGpATDGTVKVVEALAArgERLDYCIVG 165
Cdd:cd08659 78 PFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEV-GSDGARALLEAGYA--DRLDALIVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 166 EPTstatlGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDEG-NEYFPPTTWQVSNLRAGT 244
Cdd:cd08659 155 EPT-----GLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPaHPLLGPPTLNVGVINGGT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 245 gATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLDYTLNWSVSGLP--FLTPRGELSNALDAAIRAETGvSPEL 322
Cdd:cd08659 230 -QVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPpfFTDPDHPLVQALQAAARALGG-DPVV 307
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 490656189 323 STTGGTSDGRFIARI--CPqVIEFGPPNAS-IHKIDEHIDV 360
Cdd:cd08659 308 RPFTGTTDASYFAKDlgFP-VVVYGPGDLAlAHQPDEYVSL 347
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
66-376 |
6.41e-77 |
|
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: 239.94 E-value: 6.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 66 AFAGHTDVVPTGPLEQWsspPFVPTHrDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQhRGSIGFLITSDEEGPaTDGT 145
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGG-MGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 146 VKVVEALAARGERLDYCI---VGEPTS-TATLGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAE 221
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFglhIGEPTLlEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 222 QWDEGNEYFPPTTwQVSNLRAGTGATNVIPGHADLLFNFRFSTASTVEGLQARVHAILD----RHGLDYTLNWSVSGLPF 297
Cdd:pfam01546 155 VSRNVDPLDPAVV-TVGNITGIPGGVNVIPGEAELKGDIRLLPGEDLEELEERIREILEaiaaAYGVKVEVEYVEGGAPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 298 LTPRGELSNALDAAIRAETGVSPELSTTG--GTSDGRFIA-RICPQVIEFGPPNASIHKIDEHIDVRFVDPLKNVYRRVL 374
Cdd:pfam01546 234 LVNDSPLVAALREAAKELFGLKVELIVSGsmGGTDAAFFLlGVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLL 313
|
..
gi 490656189 375 EQ 376
Cdd:pfam01546 314 LK 315
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
6-375 |
3.78e-49 |
|
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: 169.70 E-value: 3.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 6 ALTEQLIARASVTPddqHCQQLMIE----RLAALGFECETIASHGVT--NFWAVkRGTAGRAGklLAFAGHTDVVPT-GP 78
Cdd:cd03894 1 ELLARLVAFDTVSR---NSNLALIEyvadYLAALGVKSRRVPVPEGGkaNLLAT-LGPGGEGG--LLLSGHTDVVPVdGQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 79 LeqWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPqhRGSIGFLITSDEEgpATD-GTVKVVEALAARGE 157
Cdd:cd03894 75 K--WSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKL--RKPLHLAFSYDEE--VGClGVRHLIAALAARGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 158 RLDYCIVGEPTSTatlgDVVkNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLL----APALAELAAEQWDEGNEYF--P 231
Cdd:cd03894 149 RPDAAIVGEPTSL----QPV-VAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAarliGKLRELADRLAPGLRDPPFdpP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 232 PTTWQVSNLRAGTgATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLDYTLNWSVSglPFLTPRGELSNALDAA 311
Cdd:cd03894 224 YPTLNVGLIHGGN-AVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPEAGIEVE--PLFEVPGLETDEDAPL 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 312 IRAETGVSPELSTTG---GTSDGRFIARICPQVIeFGPpnASI---HKIDEHIDVRFVDPLKNVYRRVLE 375
Cdd:cd03894 301 VRLAAALAGDNKVRTvayGTEAGLFQRAGIPTVV-CGP--GSIaqaHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
5-379 |
1.01e-47 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 166.70 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 5 LALTEQLIARASVTPDDQH---CQQLMIERLAALGFECETIashGVTNFWAVKRGTAGRA--------GKLLAFAGHTDV 73
Cdd:PRK08651 9 VEFLKDLIKIPTVNPPGENyeeIAEFLRDTLEELGFSTEII---EVPNEYVKKHDGPRPNliarrgsgNPHLHFNGHYDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 74 VPTGPLEQwSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAaeeFVAAHPQHRGSIGFLITSDEEgpaTDGTvkVVEALA 153
Cdd:PRK08651 86 VPPGEGWS-VNVPFEPKVKDGKVYGRGASDMKGGIAALLAA---FERLDPAGDGNIELAIVPDEE---TGGT--GTGYLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 154 ARGE-RLDYCIVGEPTSTatlgDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHL--------LAPALAELAAEQWD 224
Cdd:PRK08651 157 EEGKvTPDYVIVGEPSGL----DNICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAaakiaerlKSSLSTIKSKYEYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 225 EGNEYFPPTTWQVSNLRAGTgATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDR----HGLDYTLNWSVSGLPFLT- 299
Cdd:PRK08651 233 DERGAKPTVTLGGPTVEGGT-KTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEvapeLGIEVEFEITPFSEAFVTd 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 300 PRGELSNALDAAIRAETGVSPELSTTGGTSDGRFIARICPQVIEFGP-PNASIHKIDEHIDVRFVDPLKNVYRRVLEQLI 378
Cdd:PRK08651 312 PDSELVKALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPgELELAHAPDEYVEVKDVEKAAKVYEEVLKRLA 391
|
.
gi 490656189 379 A 379
Cdd:PRK08651 392 K 392
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
5-360 |
9.27e-47 |
|
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: 163.72 E-value: 9.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 5 LALTEQLIARASVTPDDQH---CQQLMIERLAALGFECETIASHGVTNFWAVKRGTAG---RAGKLLAFAGHTDVVPTGP 78
Cdd:TIGR01910 1 VELLKDLISIPSVNPPGGNeetIANYIKDLLREFGFSTDVIEITDDRLKVLGKVVVKEpgnGNEKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 79 LEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGpATDGTvkvvEALAARGER 158
Cdd:TIGR01910 81 LELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEES-GEAGT----LYLLQRGYF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 159 --LDYCIVGEPTStatlGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAEL--AAEQWDEGNEYFP--- 231
Cdd:TIGR01910 156 kdADGVLIPEPSG----GDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELneLEEHIYARNSYGFipg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 232 PTTWQVSNLRAGTGAtNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHG------LDYTLNWSVSGLPFLTPRGELS 305
Cdd:TIGR01910 232 PITFNPGVIKGGDWV-NSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSksdgwlYENEPVVKWSGPNETPPDSRLV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 490656189 306 NALDAAIRAETGVSPELSTTGGTSDGRFIARICPQVIEFGP-PNASIHKIDEHIDV 360
Cdd:TIGR01910 311 KALEAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPgDLETAHQVNEYISI 366
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
58-374 |
6.98e-37 |
|
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: 136.75 E-value: 6.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 58 AGRAGKLLAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDE 137
Cdd:cd08011 56 GGRKGKRLLFNGHYDVVPAGDGEGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 138 EGPATDGTVKVVEALAARGerlDYCIVGEPTSTatlgDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIhllapalAE 217
Cdd:cd08011 136 ETGGRAGTKYLLEKVRIKP---NDVLIGEPSGS----DNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAV-------KA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 218 LAAEQWDEGNEYfppTTWQVSNLRAGTgATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGldyTLNWSV---SG 294
Cdd:cd08011 202 AMKLIERLYELE---KTVNPGVIKGGV-KVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSIE---EVSFEIksfYS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 295 LPFLTPRGELSNALDAAIRAETGVSPELSTTGGTSDGRFIARICPQVIEFGPPNAS-IHKIDEHIDVR-FVDPLKnVYRR 372
Cdd:cd08011 275 PTVSNPDSEIVKKTEEAITEVLGIRPKEVISVGASDARFYRNAGIPAIVYGPGRLGqMHAPNEYVEIDeLIKVIK-VHAL 353
|
..
gi 490656189 373 VL 374
Cdd:cd08011 354 VA 355
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
1-360 |
2.34e-33 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 128.00 E-value: 2.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 1 MSATLALTEQLIARASV--TPDDQhcqqlMIE----RLAALGFECETIASHGVT--NFWAVKrGTAGRAGKLLAfaGHTD 72
Cdd:PRK07522 3 SMSSLDILERLVAFDTVsrDSNLA-----LIEwvrdYLAAHGVESELIPDPEGDkaNLFATI-GPADRGGIVLS--GHTD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 73 VVP-TGPleQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAhPQHRGsIGFLITSDEEGpatdGTVKV--- 148
Cdd:PRK07522 75 VVPvDGQ--AWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAA-PLRRP-LHLAFSYDEEV----GCLGVpsm 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 149 VEALAARGERLDYCIVGEPTStatLGDVVknGRRGSMSGELVVKGVQGHIAYPHLAKNPIHL--------LAPALAELAA 220
Cdd:PRK07522 147 IARLPERGVKPAGCIVGEPTS---MRPVV--GHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYaarliahlRDLADRLAAP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 221 EQWDEGneYFPP-TTWQVSNLRAGTgATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGL--------DYTLNWS 291
Cdd:PRK07522 222 GPFDAL--FDPPySTLQTGTIQGGT-ALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAELLpemravhpEAAIEFE 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656189 292 -VSGLPFLTPrgELSNALDAAIRAETGvSPELSTTG-GTSDGRFIARICPQVIeFGPpnASI---HKIDEHIDV 360
Cdd:PRK07522 299 pLSAYPGLDT--AEDAAAARLVRALTG-DNDLRKVAyGTEAGLFQRAGIPTVV-CGP--GSIeqaHKPDEFVEL 366
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
5-360 |
4.21e-33 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 127.95 E-value: 4.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 5 LALTEQLIARASVTPDDQH---CQQLMIERLAALGFECETIASHGV---------TNFWAVKRGtaGRAGKLLAFAGHTD 72
Cdd:PRK13013 17 VALTQDLIRIPTLNPPGRAyreICEFLAARLAPRGFEVELIRAEGApgdsetyprWNLVARRQG--ARDGDCVHFNSHHD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 73 VVPTGplEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGPATDGtvkvVEAL 152
Cdd:PRK13013 95 VVEVG--HGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGG----VAYL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 153 AARG----ERLDYCIVGEPTSTatlgDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAaeqwdegNE 228
Cdd:PRK13013 169 AEQGrfspDRVQHVIIPEPLNK----DRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEIE-------ER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 229 YFP-----------------PTTWQVSNLRAG--------TG-ATNVIPGHADLLFNFRFSTASTVEGLQARVHAILD-- 280
Cdd:PRK13013 238 LFPllatrrtampvvpegarQSTLNINSIHGGepeqdpdyTGlPAPCVADRCRIVIDRRFLIEEDLDEVKAEITALLErl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 281 ---RHGLDYTLNWSVSGLPFLTPRGE-LSNALDAAIRAETGVSPELSTTGGTSDGRFIARI--CPQVIEFGPPNASI-HK 353
Cdd:PRK13013 318 kraRPGFAYEIRDLFEVLPTMTDRDApVVRSVAAAIERVLGRQADYVVSPGTYDQKHIDRIgkLKNCIAYGPGILDLaHQ 397
|
....*..
gi 490656189 354 IDEHIDV 360
Cdd:PRK13013 398 PDEWVGI 404
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
31-373 |
3.44e-31 |
|
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130947 [Multi-domain] Cd Length: 364 Bit Score: 121.47 E-value: 3.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 31 RLAALGFECETIASHGV---TNFWAVKrGTAGRAGklLAFAGHTDVVPTGPlEQWSSPPFVPTHRDGKLYGRGAADMKTS 107
Cdd:TIGR01892 27 YLEALGFSVEVQPFPDGaekSNLVAVI-GPSGAGG--LALSGHTDVVPYDD-AAWTRDPFRLTEKDGRLYGRGTCDMKGF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 108 LAgFVVAAEEFVAAHPQhRGSIGFLITSDEEGPATdGTVKVVEALAARGerlDYCIVGEPTSTATLgdvvkNGRRGSMSG 187
Cdd:TIGR01892 103 LA-CALAAAPDLAAEQL-KKPLHLALTADEEVGCT-GAPKMIEAGAGRP---RHAIIGEPTRLIPV-----RAHKGYASA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 188 ELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDEGNEYF-----PP-TTWQVSNLRAGTgATNVIPGHADLLFNFR 261
Cdd:TIGR01892 172 EVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDLdegftPPyTTLNIGVIQGGK-AVNIIPGACEFVFEWR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 262 FSTASTVEGLQARVHAI---LDRHGLDYTLNWSV-SGLPFLTPRGElsNALDAAIRAETGVSPElSTTGGTSDGRFIARI 337
Cdd:TIGR01892 251 PIPGMDPEELLQLLETIaqaLVRDEPGFEVQIEVvSTDPGVNTEPD--AELVAFLEELSGNAPE-VVSYGTEAPQFQELG 327
|
330 340 350
....*....|....*....|....*....|....*....
gi 490656189 338 CPQVIeFGPpnASI---HKIDEHIDVRFVDPLKNVYRRV 373
Cdd:TIGR01892 328 AEAVV-CGP--GDIrqaHQPDEYVEIEDLVRCRAVLARL 363
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
59-379 |
1.90e-30 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 119.60 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 59 GRAGKLLAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAA-HPQHrGSIGFLITSDE 137
Cdd:PRK08588 56 GSGSPVLALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQgQLLN-GTIRLLATAGE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 138 E----GPAT---DGTVKVVEALaargerldycIVGEPTstatlGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHL 210
Cdd:PRK08588 135 EvgelGAKQlteKGYADDLDAL----------IIGEPS-----GHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 211 --LAPALAELAAEQWDEGNEYFPPTTWQVSNLRAGTgATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHG----- 283
Cdd:PRK08588 200 llEFYNEQKEYFDSIKKHNPYLGGLTHVVTIINGGE-QVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNqngaa 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 284 ---LDYTLNWSvsglPFLT-PRGELSNALDAAIRAETGVSPELSTTGGTSDGRFIARICP--QVIEFGP-PNASIHKIDE 356
Cdd:PRK08588 279 qlsLDIYSNHR----PVASdKDSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKPdfPVIIFGPgNNLTAHQVDE 354
|
330 340
....*....|....*....|....*..
gi 490656189 357 HID----VRFVDplknVYRRVLEQLIA 379
Cdd:PRK08588 355 YVEkdmyLKFID----IYKEIIIQYLK 377
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
55-377 |
3.48e-28 |
|
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: 112.83 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 55 RGTAGRAGKLLAFAGHTDVVPtGPLEqwssppfvPTHRDGKLYGRGAADMKTSLAGFVVAAeefVAAHPQHRGSIGFLIT 134
Cdd:cd05653 47 VGGAGSGPPDVLLLGHIDTVP-GEIP--------VRVEGGVLYGRGAVDAKGPLAAMILAA---SALNEELGARVVVAGL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 135 SDEEgpatdGTVKVVEALAARGERLDYCIVGEPTSTAtlGDVVknGRRGSMSGELVVKGVQGHIAYPhlAKNPIhlLAPA 214
Cdd:cd05653 115 VDEE-----GSSKGARELVRRGPRPDYIIIGEPSGWD--GITL--GYRGSLLVKIRCEGRSGHSSSP--ERNAA--EDLI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 215 LAELAAEQWDEGNE--YFPPTTWQVSNLRAGTgATNVIPGHADLLFNFRFSTASTVEglQARVHAildrHGLDYTLNWSV 292
Cdd:cd05653 182 KKWLEVKKWAEGYNvgGRDFDSVVPTLIKGGE-SSNGLPQRAEATIDLRLPPRLSPE--EAIALA----TALLPTCELEF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 293 SGL--PFLTP-RGELSNALDAAIRAEtGVSPELSTTGGTSDGRFIARI--CPQViEFGPPNASI-HKIDEHIDVRFVDPL 366
Cdd:cd05653 255 IDDtePVKVSkNNPLARAFRRAIRKQ-GGKPRLKRKTGTSDMNVLAPLwtVPIV-AYGPGDSTLdHTPNEHIELAEIERA 332
|
330
....*....|.
gi 490656189 367 KNVYRRVLEQL 377
Cdd:cd05653 333 AAVLKGALEEL 343
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-360 |
3.88e-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: 110.86 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 6 ALTEQLIARASVTPDDQHCQQLMIERLAALGFE-------CETIASH-----------GVTNFWAVKRGTaGRAGKLLAF 67
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTvdrweidVEKLKHHpgfspvavdyaGAPNVVGTHRPR-GETGRSLIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 68 AGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEgpatdgtVK 147
Cdd:cd03895 80 NGHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEE-------CT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 148 VVEALAA--RGERLDYCIVGEPTstatlGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAA--EQW 223
Cdd:cd03895 153 GNGALAAlmRGYRADAALIPEPT-----ELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQEleREW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 224 DE---GNEYFP----PTTWQVSNLRAGTGATNVipgHADLLFNFR------FSTASTVEGLQARVHAILDRH----GLDY 286
Cdd:cd03895 228 NArkkSHPHFSdhphPINFNIGKIEGGDWPSSV---PAWCVLDCRigiypgESPEEARREIEECVADAAATDpwlsNHPP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 287 TLNWS-VSGLPF-LTPRGELSNALDAAIRAETGVSPELSTTGGTSDGRF------IARICpqvieFGPPNASIHKIDEHI 358
Cdd:cd03895 305 EVEWNgFQAEGYvLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFfvlygdIPALC-----YGPGSRDAHGFDESV 379
|
..
gi 490656189 359 DV 360
Cdd:cd03895 380 DL 381
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
26-360 |
4.31e-27 |
|
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: 110.37 E-value: 4.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 26 QLMIERLAALGFECETI--ASHGVTNFWAVKrgtaGRAGKLLAFAGHTDVV-PTGPLEQWsspPFvpTHRDGKLYGRGAA 102
Cdd:cd03885 26 ELLAEELEALGFTVERRplGEFGDHLIATFK----GTGGKRVLLIGHMDTVfPEGTLAFR---PF--TVDGDRAYGPGVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 103 DMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEgPATDGTVKVVEALAARGerlDYCIVGEPTSTatlGDVVKNGRR 182
Cdd:cd03885 97 DMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEE-IGSPGSRELIEEEAKGA---DYVLVFEPARA---DGNLVTARK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 183 GSMSGELVVKGVQGHI-AYPHLAKNPI----HLLAPALAElaaeqwdegNEYFPPTTWQVSNLRAGTGaTNVIPGHADLL 257
Cdd:cd03885 170 GIGRFRLTVKGRAAHAgNAPEKGRSAIyelaHQVLALHAL---------TDPEKGTTVNVGVISGGTR-VNVVPDHAEAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 258 FNFRFSTASTVEGLQARVHAILDRH---GLDYTLNWSVSGLPFltPRGELSNALDAAIRA---ETGVSPELSTTGGTSDG 331
Cdd:cd03885 240 VDVRFATAEEADRVEEALRAIVATTlvpGTSVELTGGLNRPPM--EETPASRRLLARAQEiaaELGLTLDWEATGGGSDA 317
|
330 340 350
....*....|....*....|....*....|
gi 490656189 332 RFIARICPQVIE-FGPPNASIHKIDEHIDV 360
Cdd:cd03885 318 NFTAALGVPTLDgLGPVGGGAHTEDEYLEL 347
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
3-360 |
4.65e-26 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 108.17 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 3 ATLALTEQLIARASVTPDDQHCQQLMIERLAALGFECET-------IASH-----------GVTNFWAVKRGtAGRAGKL 64
Cdd:PRK06837 21 AQVAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDRwsidpddLKSHpgagpveidysGAPNVVGTYRP-AGKTGRS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 65 LAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGPAtdg 144
Cdd:PRK06837 100 LILQGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEESTG--- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 145 tvkvVEALAA--RGERLDYCIVGEPTS-TATLGDVvkngrrGSMSGELVVKGVQGHIAYPHLAKNPIHLLAP--ALAELA 219
Cdd:PRK06837 177 ----NGALSTlqRGYRADACLIPEPTGeKLVRAQV------GVIWFRLRVRGAPVHVREAGTGANAIDAAYHliQALREL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 220 AEQWDE---GNEYFP----PTTWQVSNLRAGTGATNViPGHADLLFNFRFSTASTVE----GLQARVHAILDRHGLdytl 288
Cdd:PRK06837 247 EAEWNArkaSDPHFEdvphPINFNVGIIKGGDWASSV-PAWCDLDCRIAIYPGVTAAdaqaEIEACLAAAARDDRF---- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 289 nwsVSGLP-------F------LTPRGELSNALDAAIRAETGVSPELSTTGGTSDGRF------IARICpqvieFGPPNA 349
Cdd:PRK06837 322 ---LSNNPpevvwsgFlaegyvLEPGSEAEAALARAHAAVFGGPLRSFVTTAYTDTRFyglyygIPALC-----YGPSGE 393
|
410
....*....|.
gi 490656189 350 SIHKIDEHIDV 360
Cdd:PRK06837 394 GIHGFDERVDL 404
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
49-180 |
5.24e-25 |
|
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: 100.58 E-value: 5.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 49 NFWAVKRGTAGraGKLLAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGS 128
Cdd:cd18669 1 NVIARYGGGGG--GKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 490656189 129 IGFLITSDEEGPATDGTVKVVEALAARGERLDYCIVGEPTSTATLGDVVKNG 180
Cdd:cd18669 79 VVVAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTP 130
|
|
| PRK06915 |
PRK06915 |
peptidase; |
3-197 |
2.29e-24 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 103.62 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 3 ATLALTEQLIARASVTPDDQHCQQLMIERLAALG------------------FECETIASHGVTNFWAVKRGTAGraGKL 64
Cdd:PRK06915 18 EAVKLLKRLIQEKSVSGDESGAQAIVIEKLRELGldldiwepsfkklkdhpyFVSPRTSFSDSPNIVATLKGSGG--GKS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 65 LAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEE-GPAtd 143
Cdd:PRK06915 96 MILNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEEsGGA-- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490656189 144 GTVKVVEalaaRGERLDYCIVGEPTSTATLgdvVKngRRGSMSGELVVKGVQGH 197
Cdd:PRK06915 174 GTLAAIL----RGYKADGAIIPEPTNMKFF---PK--QQGSMWFRLHVKGKAAH 218
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
9-378 |
2.96e-24 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 102.59 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 9 EQLIARASVTP-DDQHCQ--QLMIERLA----ALGFECETIA---SHGVTNFWAvKRGTaGRAGKLLAfaGHTDVVPTGP 78
Cdd:PRK05111 12 RALIATPSISAtDPALDQsnRAVIDLLAgwfeDLGFNVEIQPvpgTRGKFNLLA-SLGS-GEGGLLLA--GHTDTVPFDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 79 lEQWSSPPFVPTHRDGKLYGRGAADMKTSLAgFVVAAEEFVAAHPQHRgSIGFLITSDEEgpatdGTVKVVEALAARGE- 157
Cdd:PRK05111 88 -GRWTRDPFTLTEHDGKLYGLGTADMKGFFA-FILEALRDIDLTKLKK-PLYILATADEE-----TSMAGARAFAEATAi 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 158 RLDYCIVGEPTStatLGDVvkNGRRGSMSGELVVKGVQGHIAYPHLAKNPI---HlLAPALAELAAEQWDEG--NEYFP- 231
Cdd:PRK05111 160 RPDCAIIGEPTS---LKPV--RAHKGHMSEAIRITGQSGHSSDPALGVNAIelmH-DVIGELLQLRDELQERyhNPAFTv 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 232 --PTTwqvsNLRA--GTGATNVIPGHADLLFNFRFSTASTVEGLQA----RVHAILDRHGLDytlnWSVSGL-----PFL 298
Cdd:PRK05111 234 pyPTL----NLGHihGGDAPNRICGCCELHFDIRPLPGMTLEDLRGllreALAPVSERWPGR----ITVAPLhppipGYE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 299 TPRgelSNALDAAIRAETGVSPElSTTGGTsDGRFIARICPQVIEFGPpnASI---HKIDEHIDVRFVDPLknvyRRVLE 375
Cdd:PRK05111 306 CPA---DHQLVRVVEKLLGHKAE-VVNYCT-EAPFIQQLGCPTLVLGP--GSIeqaHQPDEYLELSFIKPT----RELLR 374
|
...
gi 490656189 376 QLI 378
Cdd:PRK05111 375 QLI 377
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-290 |
3.03e-24 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 101.97 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 5 LALTEQLIARASVTPDDQHCQQLMIERLAALGF--ECETIASHGVTNFWAVKRGTagRAGKLLaFAGHTDVVPtgpleqw 82
Cdd:cd05652 2 LSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFtvEKQPVENKDRFNVYAYPGSS--RQPRVL-LTSHIDTVP------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 83 sspPFVP---THRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEgpaTDGTvKVVEALAARGERL 159
Cdd:cd05652 72 ---PFIPysiSDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEE---TGGD-GMKAFNDLGLNTW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 160 DYCIVGEPTSTAtLGdvvkNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWdEGNEYFPPTTWQVSN 239
Cdd:cd05652 145 DAVIFGEPTELK-LA----SGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADL-PSSELLGPTTLNIGR 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 490656189 240 LRAGTgATNVIPGHADLLFNFRFStASTVEGlQARVHAILDRHGLDY---TLNW 290
Cdd:cd05652 219 ISGGV-AANVVPAAAEASVAIRLA-AGPPEV-KDIVKEAVAGILTDTediEVTF 269
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
38-377 |
4.09e-24 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 103.49 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 38 ECETIASHGVTNFWavkRGTAgRAGKLLAFAGHTDVVPTGP--LEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAA 115
Cdd:PRK08262 91 EREVVGGHSLLYTW---KGSD-PSLKPIVLMAHQDVVPVAPgtEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 116 EEFVAAHPQHRGSIGFLITSDEEgPATDGTVKVVEALAARGERLDYCI-------------VGEPTStatlgdVVKNGRR 182
Cdd:PRK08262 167 EALLAQGFQPRRTIYLAFGHDEE-VGGLGARAIAELLKERGVRLAFVLdeggaitegvlpgVKKPVA------LIGVAEK 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 183 GSMSGELVVKGVQGHIAYP--------------HLAKNP----IHLLAPALAELAAEQWDEGNE-------YFPP----- 232
Cdd:PRK08262 240 GYATLELTARATGGHSSMPprqtaigrlaraltRLEDNPlpmrLRGPVAEMFDTLAPEMSFAQRvvlanlwLFEPlllrv 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 233 ------------TTWQVSNLRAGTGAtNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLDytlnwsVSGLPFLTP 300
Cdd:PRK08262 320 lakspetaamlrTTTAPTMLKGSPKD-NVLPQRATATVNFRILPGDSVESVLAHVRRAVADDRVE------IEVLGGNSE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 301 RGELSN-------ALDAAIR---AETGVSPELsTTGGTsDGRFIARICPQVIEFGPPNAS------IHKIDEHIDVRFVD 364
Cdd:PRK08262 393 PSPVSStdsaaykLLAATIRevfPDVVVAPYL-VVGAT-DSRHYSGISDNVYRFSPLRLSpedlarFHGTNERISVANYA 470
|
410
....*....|...
gi 490656189 365 PLKNVYRRVLEQL 377
Cdd:PRK08262 471 RMIRFYYRLIENA 483
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
66-360 |
6.89e-24 |
|
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: 100.98 E-value: 6.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 66 AFAGHTDVVPTgpleqwssPPFVPTHR--DGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHrgSIGFLITSDEEGPAT- 142
Cdd:cd05647 57 ILAGHLDTVPV--------AGNLPSRVeeDGVLYGCGATDMKAGDAVQLKLAATLAAATLKH--DLTLIFYDCEEVAAEl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 143 DGTVKVVEALaarGERL--DYCIVGEPTSTAtlgdvVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELaa 220
Cdd:cd05647 127 NGLGRLAEEH---PEWLaaDFAVLGEPTDGT-----IEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARL-- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 221 eqwdegNEYfPPTTWQVSNLR----------AGTGATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLDYTL-N 289
Cdd:cd05647 197 ------AAY-EPRTVNIDGLTyreglnavfiSGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEIEVtD 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656189 290 WSVSGLPfltprgELSNALDAAIRAETGVSPElSTTGGTSDGRFIARICPQViEFGPPNASI-HKIDEHIDV 360
Cdd:cd05647 270 LSPGALP------GLDHPVARDLIEAVGGKVR-AKYGWTDVARFSALGIPAV-NFGPGDPLLaHKRDEQVPV 333
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
6-377 |
3.49e-23 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 98.87 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 6 ALTEQLIARASVTPDDQHCQQLMIERLAALGFECETIASHGVtnfwavkRGTAGRAGKLLAFAGHTDVVPtGPLeqwssP 85
Cdd:PRK04443 10 ELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREAWVDEAGNA-------RGPAGDGPPLVLLLGHIDTVP-GDI-----P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 86 PFVPthrDGKLYGRGAADMKTSLAGFVVAAeefVAAHPQHRGSIGFLITSDEEGPATDGTvkvveALAARGERLDYCIVG 165
Cdd:PRK04443 77 VRVE---DGVLWGRGSVDAKGPLAAFAAAA---ARLEALVRARVSFVGAVEEEAPSSGGA-----RLVADRERPDAVIIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 166 EPTSTatlgDVVKNGRRGSMSGELVVKGVQGHIAYP------HLAknpihllapaLAELAAEQWDEGNEYFPPTTWQVS- 238
Cdd:PRK04443 146 EPSGW----DGITLGYKGRLLVTYVATSESFHSAGPepnaaeDAI----------EWWLAVEAWFEANDGRERVFDQVTp 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 239 NLRAGTGATNVIPGHADLLFNFRFSTASTVEglqaRVHAILDRHGLDYTLNWSVSGLPFLT-PRGELSNALDAAIRAETG 317
Cdd:PRK04443 212 KLVDFDSSSDGLTVEAEMTVGLRLPPGLSPE----EAREILDALLPTGTVTFTGAVPAYMVsKRTPLARAFRVAIREAGG 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656189 318 vSPELSTTGGTSDGRFIARI--CPQViEFGPPNASI-HKIDEHIDVRFVDPLKNVYRRVLEQL 377
Cdd:PRK04443 288 -TPRLKRKTGTSDMNVVAPAwgCPMV-AYGPGDSDLdHTPDEHLPLAEYLRAIAVLTDVLERL 348
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
49-177 |
9.94e-23 |
|
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: 94.41 E-value: 9.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 49 NFWAVKRGTAGraGKLLAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGS 128
Cdd:cd03873 1 NLIARLGGGEG--GKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 490656189 129 IGFLITSDEEGPATDGTVKVVEALAARGERLDYCIVGEPTSTATLGDVV 177
Cdd:cd03873 79 IVVAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDATAGPILQKGV 127
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
6-209 |
1.94e-22 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 97.70 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 6 ALTEQLIARASVTPDDQHCQQLMIERLAALGFECETIASHGvtNFWavkrGTAGRAGKLLAFAGHTDVVPTGPLEQWSSP 85
Cdd:PRK13004 19 RFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFDKVEIDPMG--NVL----GYIGHGKKLIAFDAHIDTVGIGDIKNWDFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 86 PFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFvaahpqhrgsigflitsDEEGPATDGTVKVV--------EALAAR-- 155
Cdd:PRK13004 93 PFEGEEDDGRIYGRGTSDQKGGMASMVYAAKII-----------------KDLGLDDEYTLYVTgtvqeedcDGLCWRyi 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490656189 156 ----GERLDYCIVGEPTStatLGdvVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIH 209
Cdd:PRK13004 156 ieedKIKPDFVVITEPTD---LN--IYRGQRGRMEIRVETKGVSCHGSAPERGDNAIY 208
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
179-287 |
2.54e-22 |
|
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: 90.48 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 179 NGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDEGNeYFPPTTWQVSNLRAGTgATNVIPGHADLLF 258
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGF-DFPRTTLNITGIEGGT-ATNVIPAEAEAKF 78
|
90 100
....*....|....*....|....*....
gi 490656189 259 NFRFSTASTVEGLQARVHAILDRHGLDYT 287
Cdd:pfam07687 79 DIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
6-359 |
1.13e-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: 95.86 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 6 ALTEqLIARASVTPDDQHCQQL--MIERLAAL----GFECETIASHGVTNFWAVKRGTAGRAGKLLaFAGHTDVVPTGPL 79
Cdd:cd03893 3 TLAE-LVAIPSVSAQPDRREELrrAAEWLADLlrrlGFTVEIVDTSNGAPVVFAEFPGAPGAPTVL-LYGHYDVQPAGDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 80 EQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAaeefVAAHPQHRGSIG----FLITSDEEGpATDGTVKVVEALAAR 155
Cdd:cd03893 81 DGWDSDPFELTERDGRLYGRGAADDKGPILAHLAA----LRALMQQGGDLPvnvkFIIEGEEES-GSPSLDQLVEAHRDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 156 GeRLDYCIVGEPTSTATLGDVVKNGRRGSMSGELVVKGV------------------------------QGHIA----YP 201
Cdd:cd03893 156 L-AADAIVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLdhdlhsglyggvvpdpmtalaqllaslrdeTGRILvpglYD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 202 HLAKNPIHLLAPALAELAAEQWDEGNEY-FPPTTWQVSNL--------RAGTGATNVIPGHADLLFNFRFSTASTVEGLQ 272
Cdd:cd03893 235 AVRELPEEEFRLDAGVLEEVEIIGGTTGsVAERLWTRPALtvlgidggFPGEGSKTVIPPRARAKISIRLVPGQDPEEAS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 273 ARVHAILDRH---GLDYTLNWSVSGLPFLTP-RGELSNALDAAIRAETGVSPELSTTGGT-SDGRFIARIcPQ----VIE 343
Cdd:cd03893 315 RLLEAHLEKHapsGAKVTVSYVEGGMPWRSDpSDPAYQAAKDALRTAYGVEPPLTREGGSiPFISVLQEF-PQapvlLIG 393
|
410
....*....|....*.
gi 490656189 344 FGPPNASIHKIDEHID 359
Cdd:cd03893 394 VGDPDDNAHSPNESLR 409
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
59-358 |
5.77e-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. 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: 90.21 E-value: 5.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 59 GRAGKLLAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEE 138
Cdd:cd05650 66 GGNDKTLWIISHLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 139 GPATDGTVKVVEALAARGERlDYCIV---GEPTstatlGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPAL 215
Cdd:cd05650 146 DGSEYGIQYLLNKFDLFKKD-DLIIVpdfGTED-----GEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 216 A---ELAAEQWDEGNEYFPP--TTWQVSNLRAGTGATNVIPGHADLLFNFRFSTASTVEGLQARVHAIL---DRH---GL 284
Cdd:cd05650 220 LeldELLHEKFDEKDDLFNPpySTFEPTKKEANVPNVNTIPGYDVFYFDCRVLPTYKLDEVLKFVNKIIsdfENSygaGI 299
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656189 285 DYTLNWSVSGLPFLTPRGELSNALDAAIRAETGVSPELSTTGGTSDGRFIARICPQVIEFGPPNASIHKIDEHI 358
Cdd:cd05650 300 TYEIVQKEQAPPATPEDSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYI 373
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
27-323 |
1.06e-19 |
|
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: 89.08 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 27 LMIERLAALGFEceTIASHGVTNFWAVKRGTAGRAGklLAFAGHTDVVPTGpleqwsSPPFVPTHRDGKLYGRGAADMKT 106
Cdd:cd03896 23 LVAEWMADLGLG--DVERDGRGNVVGRLRGTGGGPA--LLFSAHLDTVFPG------DTPATVRHEGGRIYGPGIGDNKG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 107 SLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGPATDGTVKvvEALAARGERLDYCIVGEPTstatlGDVVKNGRRGSMS 186
Cdd:cd03896 93 SLACLLAMARAMKEAGAALKGDVVFAANVGEEGLGDLRGAR--YLLSAHGARLDYFVVAEGT-----DGVPHTGAVGSKR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 187 GELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDegneYFPPTTWQVSNLRAGTGAtNVIPGHADLLFNFRFSTAS 266
Cdd:cd03896 166 FRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAP----YVPKTTFAAIRGGGGTSV-NRIANLCSMYLDIRSNPDA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656189 267 TVEGLQARVHAILDRHGLDYT-----LNWSVSGLPFLTPR-GELSNALDAAIRaETGVSPELS 323
Cdd:cd03896 241 ELADVQREVEAVVSKLAAKHLrvkarVKPVGDRPGGEAQGtEPLVNAAVAAHR-EVGGDPRPG 302
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
5-174 |
1.14e-19 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 89.71 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 5 LALTEQLIARASVTP---DDQHCQQLMIERLAALGFECETIASH-GVTNFWAVKRGTAGRAGKLLAFAGHTDVVPTGPLE 80
Cdd:PRK08596 16 LELLKTLVRFETPAPparNTNEAQEFIAEFLRKLGFSVDKWDVYpNDPNVVGVKKGTESDAYKSLIINGHMDVAEVSADE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 81 QWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFL-ITSDEEGPAtdGTVKVVEalaaRGERL 159
Cdd:PRK08596 96 AWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQsVIGEEVGEA--GTLQCCE----RGYDA 169
|
170
....*....|....*
gi 490656189 160 DYCIVGEPTSTATLG 174
Cdd:PRK08596 170 DFAVVVDTSDLHMQG 184
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
5-337 |
5.58e-19 |
|
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.
Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 87.80 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 5 LALTEQLIARASVTPDDQHCQ-----QLMIERLAALGF--ECETIASH-GVTNFWAVKRGTAGRAGKLLaFAGHTDVVPT 76
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTGSetraaEVLAARLAEAGIqtEIFVVESHpGRANLVARIGGTDPSAGPLL-LLGHIDVVPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 77 GPlEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGPATDGTVKVVEALAARG 156
Cdd:cd05675 80 DA-SDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDNHPELF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 157 ERLDYCIVGEPTSTATLGD-----VVKNGRRGSMSGELVVKGVQGHIAYPHlAKNPIHLLAPALAELAAEQW----DEGN 227
Cdd:cd05675 159 DGATFALNEGGGGSLPVGKgrrlyPIQVAEKGIAWMKLTVRGRAGHGSRPT-DDNAITRLAEALRRLGAHNFpvrlTDET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 228 EYF-------PPTTWQV--------------------------SN------LRAGTgATNVIPGHADLLFNFRFSTASTV 268
Cdd:cd05675 238 AYFaqmaelaGGEGGALmltavpvldpalaklgpsapllnamlRNtasptmLDAGY-ATNVLPGRATAEVDCRILPGQSE 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656189 269 EGLQARVHAILDRHGLDYTLNWSVSGLPfLTPRGELSNALDAAIRA---ETGVSPELSTtgGTSDGRFIARI 337
Cdd:cd05675 317 EEVLDTLDKLLGDPDVSVEAVHLEPATE-SPLDSPLVDAMEAAVQAvdpGAPVVPYMSP--GGTDAKYFRRL 385
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
52-376 |
8.08e-18 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 84.07 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 52 AVKRGTAGraGKLLAFAGHTDVVPtgpLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPqhRGSIGF 131
Cdd:cd08013 60 GVVRGTGG--GKSLMLNGHIDTVT---LDGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGL--RGDVIL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 132 LITSDEEGpATDGTVKVVEAlaarGERLDYCIVGEPTSTAtlgdvVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPI--- 208
Cdd:cd08013 133 AAVADEED-ASLGTQEVLAA----GWRADAAIVTEPTNLQ-----IIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAIlka 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 209 -HLLAPALAELAAEQWDEGNEYFPPTTWQVSNLRAGTgATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRhgldyt 287
Cdd:cd08013 203 gYFLVALEEYQQELPERPVDPLLGRASVHASLIKGGE-EPSSYPARCTLTIERRTIPGETDESVLAELTAILGE------ 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 288 LNWSVSGLPFLTPRGELSNA-------------LDAAIRAETGVSPELSTTGGTSDGRFIARICPQVIEFGPPNASIHKI 354
Cdd:cd08013 276 LAQTVPNFSYREPRITLSRPpfevpkehpfvqlVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGAGLHAK 355
|
330 340
....*....|....*....|..
gi 490656189 355 DEHIDVRFVDPLKNVYRRVLEQ 376
Cdd:cd08013 356 EEWVDVESIRQLREVLSAVVRE 377
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
63-360 |
9.83e-18 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 84.23 E-value: 9.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 63 KLLAFAGHTDVVPT--GPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGP 140
Cdd:cd05674 70 KPLLLMAHQDVVPVnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTIILAFGHDEEVG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 141 ATDGTVKVVEALAAR-GERLDYCIVGEptSTATLGDVVKN--------GRRGSMSGELVVKGVQGH-------------- 197
Cdd:cd05674 150 GERGAGAIAELLLERyGVDGLAAILDE--GGAVLEGVFLGvpfalpgvAEKGYMDVEITVHTPGGHssvppkhtgigils 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 198 --IA-------------------------------YPHLAKNPIHLLAPALAELAA--EQWDEGNEYFPPTTWQVSNLRA 242
Cdd:cd05674 228 eaVAaleanpfppkltpgnpyygmlqclaehsplpPRSLKSNLWLASPLLKALLASelLSTSPLTRALLRTTQAVDIING 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 243 GTgATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLDYTLNWSVSG--LPFLTPRGELSNALDA---------- 310
Cdd:cd05674 308 GV-KINALPETATATVNHRIAPGSSVEEVLEHVKNLIADIAVKYGLGLSAFGgdVIYSTNGTKLLTSLLSpepspvssts 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656189 311 ---------AIRA-------ETGVSPELStTGGTsDGRF-------IARICPQVIEFGPPNaSIHKIDEHIDV 360
Cdd:cd05674 387 spvwqllagTIRQvfeqfgeDLVVAPGIM-TGNT-DTRHywnltknIYRFTPIRLNPEDLG-RIHGVNERISI 456
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
70-374 |
5.10e-17 |
|
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: 81.20 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 70 HTDVVPtgPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQhRGSIGFLITSDEEGPATDGtvkvV 149
Cdd:cd05651 63 HHDTVK--PNAGWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGPL-NYNLIYAASAEEEISGKNG----I 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 150 EALAARGERLDYCIVGEPTST--ATlgdvvknGRRGSMSGELVVKGVQGHIAYPHlAKNPIHLLAPALAELAAEQWDEGN 227
Cdd:cd05651 136 ESLLPHLPPLDLAIVGEPTEMqpAI-------AEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDIQWLRDFRFDKVS 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 228 EYFPPTTWQVSNLRAGTgATNVIPGHADLLFNFR----FSTASTVEGLQARVHAILDRHGLDYtlnwSVSGLPFLTPrge 303
Cdd:cd05651 208 PLLGPVKMTVTQINAGT-QHNVVPDSCTFVVDIRtteaYTNEEIFEIIRGNLKSEIKPRSFRL----NSSAIPPDHP--- 279
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656189 304 lsnALDAAIRAetGVSPELSTTggTSDGRFIAriCPQViEFGP-PNASIHKIDEHIDVRFVDPLKNVYRRVL 374
Cdd:cd05651 280 ---IVQAAIAA--GRTPFGSPT--LSDQALMP--FPSV-KIGPgDSSRSHTADEFIELSEIEEGIDIYIELL 341
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
68-377 |
6.25e-17 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 80.98 E-value: 6.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 68 AGHTDVVPtGPLEqwssppfvPTHRDGKLYGRGAADMKTSLAGFVVAAEEFvaahpQHRG-SIGFLITSDEEGpatdgTV 146
Cdd:PRK00466 66 ASHVDTVP-GYIE--------PKIEGEVIYGRGAVDAKGPLISMIIAAWLL-----NEKGiKVMVSGLADEES-----TS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 147 KVVEALAARGERLDYCIVGEPTStaTLGDVVknGRRGSMSGELVVKGVQGHiayphlAKNPIHLLAPALAELAAEQWDEG 226
Cdd:PRK00466 127 IGAKELVSKGFNFKHIIVGEPSN--GTDIVV--EYRGSIQLDIMCEGTPEH------SSSAKSNLIVDISKKIIEVYKQP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 227 NEYFPPTTwQVSNLRAGTgATNVIPGHADLLFNFRFSTASTVEGLQARVHAILdrHGLDYTlnwSVSGLP--FLTPRGEL 304
Cdd:PRK00466 197 ENYDKPSI-VPTIIRAGE-SYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKF--QECGLK---IVDETPpvKVSINNPV 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656189 305 SNALDAAIRAEtGVSPELSTTGGTSDGRFIARICPQVIEFGPPNASI-HKIDEHIDVRFVDPLKNVYRRVLEQL 377
Cdd:PRK00466 270 VKALMRALLKQ-NIKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLeHTNQEKITLDEIYIAVKTYMLAIEEL 342
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
56-209 |
5.12e-16 |
|
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: 78.62 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 56 GTAGRAGKLLAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFvaAHPQHRGSIGFLITS 135
Cdd:cd05649 46 GYIGGGKKKILFDGHIDTVGIGNIDNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIM--KDLGLRDFAYTILVA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 136 deegpatdGTV--KVVEALAAR------GERLDYCIVGEPTStatLGdvVKNGRRGSMSGELVVKGVQGHIAYPHLAKNP 207
Cdd:cd05649 124 --------GTVqeEDCDGVCWQyiskadKIKPDFVVSGEPTD---GN--IYRGQRGRMEIRVDTKGVSCHGSAPERGDNA 190
|
..
gi 490656189 208 IH 209
Cdd:cd05649 191 VY 192
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
65-377 |
6.49e-16 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 77.88 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 65 LAFAGHTDVVPTgpleqwSSPPFVpthRDGKLYGRGAADMKTSLAGFVVAAEEFvaAHPQHRGSIGFLITSDEEgPATDG 144
Cdd:PRK08652 58 LFVEVHYDTVPV------RAEFFV---DGVYVYGTGACDAKGGVAAILLALEEL--GKEFEDLNVGIAFVSDEE-EGGRG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 145 TVKVVEALAARgerldYCIVGEPTSTAtlgdvVKNGRRGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWD 224
Cdd:PRK08652 126 SALFAERYRPK-----MAIVLEPTDLK-----VAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 225 EGNEYFPPTTWQVsnLRAGTgATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLDYTLNWSVSGLpFLTPRGEL 304
Cdd:PRK08652 196 LGKYFDPHIGIQE--IIGGS-PEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEYTEIWDGF-ELDEDEEI 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656189 305 SNALDAAIRaETGVSPELSTTGGTSDG-RFIARiCPQVIEFGPPNASI-HKIDEHIDVRFVDPLKNVYRRVLEQL 377
Cdd:PRK08652 272 VQLLEKAMK-EVGLEPEFTVMRSWTDAiNFRYN-GTKTVVWGPGELDLcHTKFERIDVREVEKAKEFLKALNEIL 344
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
24-378 |
8.82e-16 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 78.28 E-value: 8.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 24 CQQLMIERLAALGFECETIASHGVtnfWAVkRGTAGRAGKLLAFAGHTDVVPTGPlEQWSSPPFVPTHRDGKLYGRGAAD 103
Cdd:PRK08554 29 CPKFIKDTLESWGIESELIEKDGY---YAV-YGEIGEGKPKLLFMAHFDVVPVNP-EEWNTEPFKLTVKGDKAYGRGSAD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 104 MKTSLAGFVVAAEEFvaAHPQHRGSIGFLITSDEE-GPATdgTVKVVEALAARGERLDYCIVGEPTSTATL-------GD 175
Cdd:PRK08554 104 DKGNVASVMLALKEL--SKEPLNGKVIFAFTGDEEiGGAM--AMHIAEKLREEGKLPKYMINADGIGMKPIirrrkgfGV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 176 VVK--------NGRRGSMSGELVVKGVQG-HIAY--------PHLAKNPIHLLAPALAELAAEQWDEGNeyFPPTTWQVS 238
Cdd:PRK08554 180 TIRvpsekvkvKGKLREQTFEIRTPVVETrHAAYflpgvdthPLIAASHFLRESNVLAVSLEGKFLKGN--VVPGEVTLT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 239 NLRAGTGATNV-----------------IPGHADLLFNFRFSTASTVEGLQARVHAIL--------DRHGLDYTLNWSVS 293
Cdd:PRK08554 258 YLEPGEGEEVEvdlgltrllkaivplvrAPIKAEKYSDYGVSITPNVYSFAEGKHVLKldiramsySKEDIERTLKEVLE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 294 glpFLTPRGEL------------SNALDAAIRAETGVSPELSTTG------GTSDGRFIARICPQVIEFGPPNASIHKID 355
Cdd:PRK08554 338 ---FNLPEAEVeirtnekagylfTPPDEEIVKVALRVLKELGEDAepvegpGASDSRYFTPYGVKAIDFGPKGGNIHGPN 414
|
410 420
....*....|....*....|...
gi 490656189 356 EHIDVRFVDPLKNVYRRVLEQLI 378
Cdd:PRK08554 415 EYVEIDSLKKMPEVYKRIALRLL 437
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
30-207 |
3.12e-15 |
|
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: 76.61 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 30 ERLAALGFECETIASHGVTNFWA-VKRGTAgragKLLAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKTSL 108
Cdd:cd05681 30 EFLRRLGAEVEIFETDGNPIVYAeFNSGDA----KTLLFYNHYDVQPAEPLELWTSDPFELTIRNGKLYARGVADDKGEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 109 AGFVVAAEEFVAAHPQHRGSIGFLITSDEEgpatDGTVKVVEALAARGERL--DYCIVgeptSTATLGD----VVKNGRR 182
Cdd:cd05681 106 MARLAALRALLQHLGELPVNIKFLVEGEEE----VGSPNLEKFVAEHADLLkaDGCIW----EGGGKNPkgrpQISLGVK 177
|
170 180
....*....|....*....|....*..
gi 490656189 183 GSMSGELVVKG--VQGHIAYPHLAKNP 207
Cdd:cd05681 178 GIVYVELRVKTadFDLHSSYGAIVENP 204
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
1-280 |
4.01e-15 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 76.01 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 1 MSATLALTEQLIARASVTPDDQHCQQLMIERL-AAL-GFECETI-ASHGVTNFWAVkRGTAgragKLLaFAGHTDVVPTG 77
Cdd:PRK08737 5 LESTLDHLQALVSFDTRNPPRAITTGGIFDYLrAQLpGFQVEVIdHGAGAVSLYAV-RGTP----KYL-FNVHLDTVPDS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 78 PleQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEefvaahpQHRGSIGFLITSDEEGpatdGTVKVVEALAARGE 157
Cdd:PRK08737 79 P--HWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAAN-------AGDGDAAFLFSSDEEA----NDPRCVAAFLARGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 158 RLDYCIVGEPT-STATLgdvvknGRRGSMSGELVVKGVQGHIAYPH-LAKNPIHLLAPALAELAAEQWDEGNEYFPPTTW 235
Cdd:PRK08737 146 PYEAVLVAEPTmSEAVL------AHRGISSVLMRFAGRAGHASGKQdPSASALHQAMRWGGQALDHVESLAHARFGGLTG 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490656189 236 QVSNLRAGTGA--TNVIPGHADLLFNFRFSTASTVEGLQARVHAILD 280
Cdd:PRK08737 220 LRFNIGRVEGGikANMIAPAAELRFGFRPLPSMDVDGLLATFAGFAE 266
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
9-109 |
5.56e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 76.10 E-value: 5.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 9 EQLIARASVTPD---DQHCQ---QLMIERLAALGFEC-ETIASHGVTNFWAVKRGTAGRAGKLLAFagHTDVVPTGPLEQ 81
Cdd:PRK07907 25 EELVRIPSVAADpfrREEVArsaEWVADLLREAGFDDvRVVSADGAPAVIGTRPAPPGAPTVLLYA--HHDVQPPGDPDA 102
|
90 100
....*....|....*....|....*...
gi 490656189 82 WSSPPFVPTHRDGKLYGRGAADMKTSLA 109
Cdd:PRK07907 103 WDSPPFELTERDGRLYGRGAADDKGGIA 130
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
59-360 |
2.62e-14 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 73.82 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 59 GRAGKLLAFAGHTDVVPTGplEQWSSPPFVPTHRDGKLYGRGAADMKtslaGFVVAA----------------------- 115
Cdd:cd03888 68 GEGEEVLGILGHLDVVPAG--EGWTTDPFKPVIKDGKLYGRGTIDDK----GPTIAAlyalkilkdlglplkkkirlifg 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 116 --EE--------FVAAHPQhrGSIGFliTSDEEGPATDG-----TVKVVEALA-ARGERLDYCIVGE------PTSTATL 173
Cdd:cd03888 142 tdEEtgwkciehYFEHEEY--PDFGF--TPDAEFPVINGekgivTVDLTFKIDdDKGYRLISIKGGEatnmvpDKAEAVI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 174 --------GDVVKNGRRGSMS-----GELVVKGVQGHIAYPHLAKNPI---------------HLLAPALAELAAEQWDE 225
Cdd:cd03888 218 pgkdkeelALSAATDLKGNIEiddggVELTVTGKSAHASAPEKGVNAItllakflaelnkdgnDKDFIKFLAKNLHEDYN 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 226 GNEYFPPTTWQVS-NLRAGTGATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLDYTLnwSVSGLPFLTPR-GE 303
Cdd:cd03888 298 GKKLGINFEDEVMgELTLNPGIITLDDGKLELGLNVRYPVGTSAEDIIKQIEEALEKYGVEVEG--HKHQKPLYVPKdSP 375
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656189 304 LSNALDAAIRAETGV-SPELSTTGGTSdgrfiARICPQVIEFGP--PNA--SIHKIDEHIDV 360
Cdd:cd03888 376 LVKTLLKVYEEQTGKeGEPVAIGGGTY-----ARELPNGVAFGPefPGQkdTMHQANEFIPI 432
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
18-193 |
2.93e-14 |
|
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: 73.50 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 18 TPDDQHCQQLMIERLAALGFE-CETIASHG---VTNFWAvkrgTAGRAGKLLAFaGHTDVVPTGPLEQWSSPPFVPTHRD 93
Cdd:cd05680 20 KGDVRRAAEWLADKLTEAGFEhTEVLPTGGhplVYAEWL----GAPGAPTVLVY-GHYDVQPPDPLELWTSPPFEPVVRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 94 GKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEE-GPATDGTVkvveaLAARGERL--DYCIV------ 164
Cdd:cd05680 95 GRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEiGSPSLPAF-----LEENAERLaaDVVLVsdtsmw 169
|
170 180 190
....*....|....*....|....*....|.
gi 490656189 165 --GEPTSTAtlgdvvknGRRGSMSGELVVKG 193
Cdd:cd05680 170 spDTPTITY--------GLRGLAYLEISVTG 192
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
59-138 |
1.33e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 68.57 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 59 GRAGKLLAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMK--TSLAGFVVAAEEFVAAHPQHRgsIGFLITSD 136
Cdd:PRK07205 72 GQGEELLAILCHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKgpSMAALYAVKALLDAGVQFNKR--IRFIFGTD 149
|
..
gi 490656189 137 EE 138
Cdd:PRK07205 150 EE 151
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
20-209 |
2.38e-12 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 67.85 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 20 DDQHCQQLMIERLAALGFE-CETIASHG---VTNFWAVKRGtagraGKLLAFAGHTDVVPTGPLEQWSSPPFVPTHRDGK 95
Cdd:PRK08201 38 DVRKAAEWLAGALEKAGLEhVEIMETAGhpiVYADWLHAPG-----KPTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 96 LYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEgpatDGTVKVVEALAARGERL--DYCIVGEPTSTATL 173
Cdd:PRK08201 113 LYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEE----IGSPNLDSFVEEEKDKLaaDVVLISDTTLLGPG 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 490656189 174 GDVVKNGRRGSMSGELVVKGVQGHI---AYPHLAKNPIH 209
Cdd:PRK08201 189 KPAICYGLRGLAALEIDVRGAKGDLhsgLYGGAVPNALH 227
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
69-206 |
3.76e-12 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 67.18 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 69 GHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGPATDGtvkv 148
Cdd:PRK13983 83 SHMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYG---- 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656189 149 VEALAARGERL----DYCIV---GEPTstatlGDVVKNGRRGSMSGELVVKGVQGHIAYPHLAKN 206
Cdd:PRK13983 159 IQYLLKKHPELfkkdDLILVpdaGNPD-----GSFIEIAEKSILWLKFTVKGKQCHASTPENGIN 218
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
2-155 |
4.38e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 66.95 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 2 SATLALTEQLIA------RASVTPddqhCQQLMIERLAALGF---ECETIASHGVT-NFWAVKRGTAgrAGKLLAFAGHT 71
Cdd:PRK09133 37 QAARDLYKELIEinttasTGSTTP----AAEAMAARLKAAGFadaDIEVTGPYPRKgNLVARLRGTD--PKKPILLLAHM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 72 DVVPTGPlEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGpatdGTVKVVEA 151
Cdd:PRK09133 111 DVVEAKR-EDWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEG----TPMNGVAW 185
|
....
gi 490656189 152 LAAR 155
Cdd:PRK09133 186 LAEN 189
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
9-122 |
1.08e-11 |
|
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.
Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 66.09 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 9 EQLIARASVT------PDDQHCQQLMIERLAALGFECET--IASHGVTNFWAVKR-----GTAGR--AGKLLAFAGHTDV 73
Cdd:cd05676 17 REAVAIQSVSadpekrPELIRMMEWAAERLEKLGFKVELvdIGTQTLPDGEELPLppvllGRLGSdpSKKTVLIYGHLDV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 490656189 74 VPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAH 122
Cdd:cd05676 97 QPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLG 145
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
26-209 |
2.41e-11 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 64.92 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 26 QLMIERLAALGFECETIASHGVTNFWAVKRGTAGRAGKLLaFAGHTDVVPTGPLEQWSSPPFVP---THRDGK--LYGRG 100
Cdd:PRK09104 47 DWLVADLASLGFEASVRDTPGHPMVVAHHEGPTGDAPHVL-FYGHYDVQPVDPLDLWESPPFEPrikETPDGRkvIVARG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 101 AADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGpatdGTVKVVEALAARGERL--DYCIV--------GEPTST 170
Cdd:PRK09104 126 ASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEES----GSPSLVPFLEANAEELkaDVALVcdtgmwdrETPAIT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490656189 171 ATLgdvvkngrRGSMSGELVVKGV-----QGHiaYPHLAKNPIH 209
Cdd:PRK09104 202 TSL--------RGLVGEEVTITAAdrdlhSGL--FGGAAANPIR 235
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
70-358 |
2.69e-11 |
|
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: 64.43 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 70 HTDVVPTGPlEQWSSPPFvPTHRD--GKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGPATDGTVK 147
Cdd:TIGR01880 79 HTDVVPVFR-EHWTHPPF-SAFKDedGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 148 VVEALAARGERLDYCI-VGEPTSTATLgdVVKNGRRGSMSGELVVKGVQGHIA--YPHLAKNPIHLLAPALAELAAEQWD 224
Cdd:TIGR01880 157 FAKTDEFKALNLGFALdEGLASPDDVY--RVFYAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRRFRESQFQ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 225 --EGNE---YFPPTTWQVSNLRAGTgATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLDYTLNWS-VSGLPFL 298
Cdd:TIGR01880 235 llQSNPdlaIGDVTSVNLTKLKGGV-QSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAGEGVTYEFSqHSGKPLV 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 299 TPR-------GELSNALDAAIRAETgvsPELSTtgGTSDGRFIARICPQVIEFGPPNAS---IHKIDEHI 358
Cdd:TIGR01880 314 TPHddsnpwwVAFKDAVKEMGCTFK---PEILP--GSTDSRYIRAAGVPALGFSPMNNTpvlLHDHNEFL 378
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
58-111 |
4.80e-11 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 63.94 E-value: 4.80e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490656189 58 AGRAGKLLAFAGHTDVVPTGplEQWSSPPFVPTHRDGKLYGRGAADMK-TSLAGF 111
Cdd:TIGR01887 63 YGQGEEVLGILGHLDVVPAG--DGWTSPPFEPTIKDGRIYGRGTLDDKgPTIAAY 115
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
18-202 |
6.19e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 63.33 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 18 TPDDQHCQQLMIERLAALGFECETIASH-GVTNFWAVKRGTAGRAGKLLaFAGHTDVVPTGPlEQWSSPPFVPTHRDGKL 96
Cdd:PRK07906 21 GKGEREAAEYVAEKLAEVGLEPTYLESApGRANVVARLPGADPSRPALL-VHGHLDVVPAEA-ADWSVHPFSGEIRDGYV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 97 YGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEGPATDGTVKVVEalaARGERLDYCI--VGEPTS-TATL 173
Cdd:PRK07906 99 WGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEAGGTYGAHWLVD---NHPELFEGVTeaISEVGGfSLTV 175
|
170 180 190
....*....|....*....|....*....|....
gi 490656189 174 GD-----VVKNGRRGSMSGELVVKGVQGHIAYPH 202
Cdd:PRK07906 176 PGrdrlyLIETAEKGLAWMRLTARGRAGHGSMVN 209
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
60-207 |
1.61e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 62.08 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 60 RAGKLLAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRgSIGFLITSDEEg 139
Cdd:PRK06446 60 GAKKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKHKLNV-NVKFLYEGEEE- 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656189 140 patDGTVKVVEALAARGERL--DYCIVgEPTSTATLG-DVVKNGRRGSMSGELVVKGVQG--HIAYPHLAKNP 207
Cdd:PRK06446 138 ---IGSPNLEDFIEKNKNKLkaDSVIM-EGAGLDPKGrPQIVLGVKGLLYVELVLRTGTKdlHSSNAPIVRNP 206
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
67-358 |
2.26e-10 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 61.52 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 67 FAGHTDVV--PTGPLEQwssppfVPTHRDGKLYGRGAADMKTSLAGFVVAAEEFvAAHPqHRGSIGF--LITSDEEgPAT 142
Cdd:PRK07338 97 LTGHMDTVfpADHPFQT------LSWLDDGTLNGPGVADMKGGIVVMLAALLAF-ERSP-LADKLGYdvLINPDEE-IGS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 143 DGTVKVVEALAARGerlDYCIVGEPtSTATlGDVVKNgRRGSMSGELVVKGVQGHIAY-PHLAKNPIhllapALAELAAE 221
Cdd:PRK07338 168 PASAPLLAELARGK---HAALTYEP-ALPD-GTLAGA-RKGSGNFTIVVTGRAAHAGRaFDEGRNAI-----VAAAELAL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 222 QWDEGNEYFPPTTWQVSNLrAGTGATNVIPGHADLLFNFRFSTASTVEGLQARVHAILD----RHGLDYTLNWSVSGLPf 297
Cdd:PRK07338 237 ALHALNGQRDGVTVNVAKI-DGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAqvnqRHGVSLHLHGGFGRPP- 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490656189 298 lTPRGELSNALDAAIR---AETGVSPELSTTGGTSDGRFIARI-CPQVIEFGPPNASIHKIDEHI 358
Cdd:PRK07338 315 -KPIDAAQQRLFEAVQacgAALGLTIDWKDSGGVCDGNNLAAAgLPVVDTLGVRGGNIHSEDEFV 378
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
3-365 |
3.61e-10 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 61.19 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 3 ATLALTEQLIARASVTPDDQHCQQ---LMIERLAALGFECETIASHGV--TNFWAVKRGTAGRAGKLLAfagHTDVV-PT 76
Cdd:PRK06133 38 AYLDTLKELVSIESGSGDAEGLKQvaaLLAERLKALGAKVERAPTPPSagDMVVATFKGTGKRRIMLIA---HMDTVyLP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 77 GPLEQwssPPFvptHRDG-KLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEgPATDGTVKVVEALAAR 155
Cdd:PRK06133 115 GMLAK---QPF---RIDGdRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEE-TGSPGSRELIAELAAQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 156 GerlDYCIVGEPTSTAtlgDVVKNGRRGSMSGELVVKGVQGHI-AYPHLAKNPI----HLLAPALaelaaeqwDEGNEYf 230
Cdd:PRK06133 188 H---DVVFSCEPGRAK---DALTLATSGIATALLEVKGKASHAgAAPELGRNALyelaHQLLQLR--------DLGDPA- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 231 PPTT--WQVSnlRAGTgATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLDYTlnwSVS-----GLPFLtPRGE 303
Cdd:PRK06133 253 KGTTlnWTVA--KAGT-NRNVIPASASAQADVRYLDPAEFDRLEADLQEKVKNKLVPDT---EVTlrferGRPPL-EANA 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490656189 304 LSNALDA---AIRAETGVSPELST--TGGTSDGRFIARIC-PQVIE-FGPPNASIHKIDEHIDVRFVDP 365
Cdd:PRK06133 326 ASRALAEhaqGIYGELGRRLEPIDmgTGGGTDAAFAAGSGkAAVLEgFGLVGFGAHSNDEYIELNSIVP 394
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
61-164 |
1.39e-09 |
|
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: 59.28 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 61 AGKLLAFAGHTDVVPTGPLEQWSSPPFVPTHRDGKLYGRGAADMKtslaGFVVAAeEFVAAHPQHRGSIG----FLITSD 136
Cdd:cd05677 70 KRKRILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNK----GPLLAA-IYAVAELFQEGELDndvvFLIEGE 144
|
90 100
....*....|....*....|....*...
gi 490656189 137 EEGpATDGTVKVVEALAARGERLDYCIV 164
Cdd:cd05677 145 EES-GSPGFKEVLRKNKELIGDIDWILL 171
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
56-105 |
2.24e-09 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 58.70 E-value: 2.24e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 490656189 56 GTAGRA--GK---LLAFAGHTDVVPTGplEQWSSPPFVPTHRDGKLYGRGAADMK 105
Cdd:PRK07318 68 NYAGHIeyGEgeeVLGILGHLDVVPAG--DGWDTDPYEPVIKDGKIYARGTSDDK 120
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
40-337 |
2.67e-08 |
|
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: 55.04 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 40 ETIASHGVTNFWAVKRGTA-------GRAGKLLAFAGHTDVVPtgpLEQWSSPPFVPTHrDGKLYGRGA-ADMKTSLAGF 111
Cdd:TIGR01891 27 EALESLGIEVRRGVGGATGvvatiggGKPGPVVALRADMDALP---IQEQTDLPYKSTN-PGVMHACGHdLHTAILLGTA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 112 VVAAEEFVAAHpqhrGSIGFLITSDEEGpaTDGTVKVVEALAARGerLDYCIVGEPTSTATLGdVVKNGRRGSMSG---- 187
Cdd:TIGR01891 103 KLLKKLADLLE----GTVRLIFQPAEEG--GGGATKMIEDGVLDD--VDAILGLHPDPSIPAG-TVGLRPGTIMAAadkf 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 188 ELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEqwdegneyfppTTWQVSNLRAGT---------GATNVIPGHADLLF 258
Cdd:TIGR01891 174 EVTIHGKGAHAARPHLGRDALDAAAQLVVALQQI-----------VSRNVDPSRPAVvsvgiieagGAPNVIPDKASMSG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 259 NFRFSTASTVEGLQARVHAILDR----HGLDYTLNWsVSGLPFLTPRGELSNALDAAIRAETGVSPE----LSTTGGTSD 330
Cdd:TIGR01891 243 TVRSLDPEVRDQIIDRIERIVEGaaamYGAKVELNY-DRGLPAVTNDPALTQILKEVARHVVGPENVaedpEVTMGSEDF 321
|
....*..
gi 490656189 331 GRFIARI 337
Cdd:TIGR01891 322 AYYSQKV 328
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
26-138 |
5.94e-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: 54.10 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 26 QLMIERLAALGFECET-------IASHG---VTNFwaVKRGTAGRAGKLLAFAGHTDVVPTGplEQWSSPPFVPTHRDGK 95
Cdd:cd02697 29 ERTAALLQGFGFEAERhpvpeaeVRAYGmesITNL--IVRRRYGDGGRTVALNAHGDVVPPG--DGWTRDPYGAVVEDGV 104
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 490656189 96 LYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEE 138
Cdd:cd02697 105 MYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEE 147
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
224-339 |
9.31e-08 |
|
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: 53.68 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 224 DEGNEYFPPTTWQVSNLRAGTGATNVIPGHADLLFNFRFSTAST----VEGLQARVHAILDRHGLDYTL--NWSVSGLPF 297
Cdd:cd03884 244 EIALEHGDDLVATVGRIEVKPNAVNVIPGEVEFTLDLRHPDDAVldamVERIRAEAEAIAAERGVEVEVerLWDSPPVPF 323
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 490656189 298 ltpRGELSNALDAAIRAEtGVSPELSTTGGTSDGRFIARICP 339
Cdd:cd03884 324 ---DPELVAALEAAAEAL-GLSYRRMPSGAGHDAMFMARICP 361
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
70-105 |
1.19e-06 |
|
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: 49.96 E-value: 1.19e-06
10 20 30
....*....|....*....|....*....|....*...
gi 490656189 70 HTDVVPTGPlEQWSSPPFvPTHRD--GKLYGRGAADMK 105
Cdd:cd05646 72 HTDVVPVFE-EKWTHDPF-SAHKDedGNIYARGAQDMK 107
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
25-290 |
1.48e-06 |
|
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: 49.52 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 25 QQLMIERLAALGFECETIAshGVTNFWAVKRGtaGRAGKLLAFAGHTDVVPtgpLEQWSSPPFVPTHrDGKLYGRGAaDM 104
Cdd:cd03886 22 AARIAEELRELGLEVRTGV--GGTGVVATLKG--GGPGPTVALRADMDALP---IQEETGLPFASKH-EGVMHACGH-DG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 105 KTSLAgfVVAAEEFVAAHPQHRGSIGFLITSDEEGPAtdGTVKVVEALAARGERLDYCIVGEPTSTATLGDVVknGRRGS 184
Cdd:cd03886 93 HTAML--LGAAKLLAERRDPLKGTVRFIFQPAEEGPG--GAKAMIEEGVLENPGVDAAFGLHVWPGLPVGTVG--VRSGA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 185 -MSG----ELVVKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDEGNEyFPPTTWQVSNLRAGTgATNVIPGHADLLFN 259
Cdd:cd03886 167 lMASadefEITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVVSRELDP-LEPAVVTVGKFHAGT-AFNVIPDTAVLEGT 244
|
250 260 270
....*....|....*....|....*....|....*
gi 490656189 260 FRFSTASTVEGLQAR----VHAILDRHGLDYTLNW 290
Cdd:cd03886 245 IRTFDPEVREALEARikrlAEGIAAAYGATVELEY 279
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
62-326 |
3.40e-06 |
|
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: 48.61 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 62 GKLLAFAG-HTDVVPTGPlEQWSSPPFVPThRDG-KLYGRGAADMKTSLAGFVVAAEEFVAAHPQHRGSIGFLITSDEEG 139
Cdd:cd08012 77 GKTVSFVGsHMDVVTANP-ETWEFDPFSLS-IDGdKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVVAVFIANEEN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 140 PATDGTvkVVEALAARGErLDYCIVGeP---TSTATLGDVVKNGrrGSMSGELVVKGVQGHIAYPHLAKNPIHLLAPALA 216
Cdd:cd08012 155 SEIPGV--GVDALVKSGL-LDNLKSG-PlywVDSADSQPCIGTG--GMVTWKLTATGKLFHSGLPHKAINALELVMEALA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 217 ELAAEQWDEgneyFP-----------------PTTWQVSnlragTGATNVIPGHADLLFNFRFSTASTVEGLQARVHAIL 279
Cdd:cd08012 229 EIQKRFYID----FPphpkeevygfatpstmkPTQWSYP-----GGSINQIPGECTICGDCRLTPFYDVKEVREKLEEYV 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 490656189 280 DrhgldyTLNWSVSGLPFLTP-----------RGELSNALDAAirAETGVSPELSTTG 326
Cdd:cd08012 300 D------DINANIEELPTRGPvskyvlpaeglRGRVSLEFDEA--AASGVACNLDSPG 349
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
21-278 |
2.31e-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: 46.18 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 21 DQHCQQLMIERLAALGFECET-IASHGVTnfwAV-KRGTagraGKLLAFAGHTDVVPtgpLEQWSSPPFVPTHR----DG 94
Cdd:cd05664 20 EHRTAAKIAEELRKLGFEVTTgIGGTGVV---AVlRNGE----GPTVLLRADMDALP---VEENTGLPYASTVRmkdwDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 95 KLYGRGAA---DMKTslAGFVVAAEEFVAAHPQHRGSIGFLITSDEEgPATDGTVKVVEALAARGERLDYCIVGEPTSTA 171
Cdd:cd05664 90 KEVPVMHAcghDMHV--AALLGAARLLVEAKDAWSGTLIAVFQPAEE-TGGGAQAMVDDGLYDKIPKPDVVLAQHVMPGP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 172 TLGDVVKNGRRGSMSG--ELVVKGVQGHIAYPHLAKNPIhllAPALAELAAEQWDEGNEYFP--PTTWQVSNLRAGTgAT 247
Cdd:cd05664 167 AGTVGTRPGRFLSAADslDITIFGRGGHGSMPHLTIDPV---VMAASIVTRLQTIVSREVDPqeFAVVTVGSIQAGS-AE 242
|
250 260 270
....*....|....*....|....*....|.
gi 490656189 248 NVIPGHADLLFNFRFSTASTVEGLQARVHAI 278
Cdd:cd05664 243 NIIPDEAELKLNVRTFDPEVREKVLNAIKRI 273
|
|
| PRK12890 |
PRK12890 |
allantoate amidohydrolase; Reviewed |
240-359 |
4.03e-05 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 237248 [Multi-domain] Cd Length: 414 Bit Score: 45.28 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 240 LRAGTGATNVIPGHADLLFNFRFST----ASTVEGLQARVHAILDRHGLDYTLN--WSVSGLPFltpRGELSNALDAAIR 313
Cdd:PRK12890 270 LDVEPNAINVVPGRVVFTLDLRSPDdavlEAAEAALLAELEAIAAARGVRIELErlSRSEPVPC---DPALVDAVEAAAA 346
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 490656189 314 AEtGVSPELSTTGGTSDGRFIARICPQVIEFGPPNASI-HKIDEHID 359
Cdd:PRK12890 347 RL-GYPSRRMPSGAGHDAAAIARIGPSAMIFVPCRGGIsHNPEEAMD 392
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
26-358 |
5.41e-05 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 44.80 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 26 QLMIERLAALGFECETIAS--HGVTNFWAVKRGTAGRAGKLLAFaGHTDVVPtGPLEQWSS--PPFVPTHRDGKLYGRGA 101
Cdd:cd05679 35 QEMRPRFERLGFTVHIHDNpvAGRAPFLIAERIEDPSLPTLLIY-GHGDVVP-GYEGRWRDgrDPWTVTVWGERWYGRGT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 102 ADMKTSLAGFVVAAEEFVAAhpqHRGSIGFLITSDEEGPATDGTVKVVEALAARGERL--DYCIVGEPTSTATLGDVVKN 179
Cdd:cd05679 113 ADNKGQHSINMAALRQVLEA---RGGKLGFNVKFLIEMGEEMGSPGLRAFCFSHREALkaDLFIASDGPRLAADRPTMFL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 180 GRRGSMSGELVVK------------------------------GVQGHIAYPHL-----------AKNPIHLLAPALAEL 218
Cdd:cd05679 190 GSRGGLNFELRVNlregghhsgnwggllanpgiilanaiaslvDGKGRIKLPALkpahlpnsvrsALADVEVGGGPDDPS 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 219 AAEQWDEGN-----EYFPPTTWQVSNLRAGT--GATNVIPGHADLLFNFRFSTASTVEGLQARVHAILDRHGLD---YTL 288
Cdd:cd05679 270 IDPWWGEPGltaaeRVFGWNTLEVLAFKTGNpdAPVNAIPGHAEAICQIRFVVGTDPDTFIPAVRAHLDANGFDgveVTA 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490656189 289 NWSVSGLPFLTPRGELSNALDAAIRAETGVSPE-LSTTGGTSDGRFIARICPQVIEFGP---PNASIHKIDEHI 358
Cdd:cd05679 350 SQMVFAATRLDPDSPWVGWALASLQKTTGKKPAlLPNLGGSLPNDVFSEVLGLPTLWVPhsyPACSQHAPNEHI 423
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
26-105 |
6.66e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 44.52 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 26 QLMIERLAALGFECETIASHGVTN--FWAVKRGTAGRAGKLLAFaGHTDVVPtGPLEQWSSP--PFVPTHRDGKLYGRGA 101
Cdd:PRK07079 48 DEIAPALAALGFTCRIVDNPVAGGgpFLIAERIEDDALPTVLIY-GHGDVVR-GYDEQWREGlsPWTLTEEGDRWYGRGT 125
|
....
gi 490656189 102 ADMK 105
Cdd:PRK07079 126 ADNK 129
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
45-175 |
2.82e-04 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 42.92 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 45 HGVTNFWAVKRGtAGRAGKLLAFAGHTDVVPT---GPLEQWSsppFVP---------------THRD---GK-LYGRGAA 102
Cdd:COG4187 63 LGRKNVTALVKG-KGESKKTVILISHFDVVDVedyGSLKPLA---FDPeeltealkeiklpedVRKDlesGEwLFGRGTM 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656189 103 DMKTSLAGFVVAAEEFvAAHPQHRGSIGFLITSDEEGPATdGTVKVVEALA--ARGERLDY--CIVGEPTSTATLGD 175
Cdd:COG4187 139 DMKAGLALHLALLEEA-SENEEFPGNLLLLAVPDEEVNSA-GMRAAVPLLAelKEKYGLEYklAINSEPSFPKYPGD 213
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
36-103 |
3.73e-04 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 42.32 E-value: 3.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 36 GFECETIASHGVTNFWAVKRGTAGRAGKLLAFAGHTDVVPtgPLEQWSSP--PFVPTHRDGKLYGRGAAD 103
Cdd:cd05682 47 GAKVEVVELEGRTPLLFVEIPGTEQDDDTVLLYGHMDKQP--PFTGWDEGlgPTKPVIRGDKLYGRGGAD 114
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
114-327 |
3.91e-04 |
|
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: 42.27 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 114 AAEEFVAAHPQHRGSIGFLITSDEEgpATDGTVKVVEALAARGerLDYcIVG---EPTSTATLGDV---VKNGRRGSMSG 187
Cdd:cd08018 98 AAELLKKIGLVKKGKLKFLFQPAEE--KGTGALKMIEDGVLDD--VDY-LFGvhlRPIQELPFGTAapaIYHGASTFLEG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 188 ELvvKGVQGHIAYPHLAKNPIHLLAPALAELAAEQWDEGNeyfpPTTWQVSNLRAGTGATNVIPGHADLLFNFRFSTAST 267
Cdd:cd08018 173 TI--KGKQAHGARPHLGINAIEAASAIVNAVNAIHLDPNI----PWSVKMTKLQAGGEATNIIPDKAKFALDLRAQSNEA 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490656189 268 VEGLQARV-HAIL---DRHGLDYTLNWsVSGLPFLTPRGELSNALDAAIR---AETGVSPELSTTGG 327
Cdd:cd08018 247 MEELKEKVeHAIEaaaALYGASIEITE-KGGMPAAEYDEEAVELMEEAITevlGEEKLAGPCVTPGG 312
|
|
| PRK13799 |
PRK13799 |
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional |
237-344 |
5.87e-04 |
|
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional
Pssm-ID: 106740 [Multi-domain] Cd Length: 591 Bit Score: 41.92 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 237 VSNLRAGTGATNVIPGHADLLFNFRFSTAS----TVEGLQARVHAILDRHGLDYTLNWSVSGlPFLTPRGELSNALDAAI 312
Cdd:PRK13799 444 MGQLNVPSGSTNVIPGRCQFSLDIRAATDEirdaAVADILAEIAAIAARRGIEYKAELAMKA-AAAPCAPELMKQLEAAT 522
|
90 100 110
....*....|....*....|....*....|..
gi 490656189 313 RAeTGVSPELSTTGGTSDGRFIARICPQVIEF 344
Cdd:PRK13799 523 DA-AGVPLFELASGAGHDAMKIAEIMDQAMLF 553
|
|
| PRK12892 |
PRK12892 |
allantoate amidohydrolase; Reviewed |
232-357 |
1.43e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 183817 [Multi-domain] Cd Length: 412 Bit Score: 40.46 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 232 PTTWQVSNLRAGTGATNVIPGHADLLFNFRFSTASTVEGLQARVHAILD----RHGLDYTLNWSVSGLPFLTPRGeLSNA 307
Cdd:PRK12892 261 PAVVTVGRVALDPGSPSIIPGRVEFSFDARHPSPPVLQRLVALLEALCReiarRRGCRVSVDRIAEYAPAPCDAA-LVDA 339
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 490656189 308 LDAAIRAETGVSPELStTGGTSDGRFIARICPQVIEFGPpnaSIHKIDEH 357
Cdd:PRK12892 340 LRAAAEAAGGPYLEMP-SGAGHDAQNMARIAPSAMLFVP---SKGGISHN 385
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
16-370 |
1.84e-03 |
|
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: 40.13 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 16 SVTPDDQHCQQLMIERLAALGFE-----CETIASHGVTNFWAVKRGTAGRAGKLLaFAGHTDVVPTGPleqwSSPPfvPT 90
Cdd:cd05683 17 SETLHEKEISKVLKKKFENLGLSvieddAGKTTGGGAGNLICTLKADKEEVPKIL-FTSHMDTVTPGI----NVKP--PQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 91 HRDGKLYGRG----AADMKTSLAGFVVAAEEFVAAHPQHrGSIGFLITSDEEgpatdgtVKVVEALAARGERLD----YC 162
Cdd:cd05683 90 IADGYIYSDGttilGADDKAGIAAILEAIRVIKEKNIPH-GQIQFVITVGEE-------SGLVGAKALDPELIDadygYA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 163 I-----VGEPTSTATLGDVVKngrrgsmsgeLVVKGVQGHIA-YPHLAKNPIHLLAPALAELAAEQWDEgneyfpPTTWQ 236
Cdd:cd05683 162 LdsegdVGTIIVGAPTQDKIN----------AKIYGKTAHAGtSPEKGISAINIAAKAISNMKLGRIDE------ETTAN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 237 VSNLRAGTgATNVIPGHADLLFNFRFSTASTVEGLQARV-----HAILDRHG-LDYTLNWSVSGLPFltprGELSNALDA 310
Cdd:cd05683 226 IGKFQGGT-ATNIVTDEVNIEAEARSLDEEKLDAQVKHMketfeTTAKEKGAhAEVEVETSYPGFKI----NEDEEVVKL 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490656189 311 AIRA--ETGVSPELSTTGGTSDGRFIARICPQVIEFGPPNASIHKIDEHIdvrfvdPLKNVY 370
Cdd:cd05683 301 AKRAanNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERI------PIEDLY 356
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
245-339 |
5.29e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 38.60 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 245 GATNVIPGHADLLFNFRfST-----ASTVEGLQARVHAILDRHGLDYTLnwsvsGLPFLTPRGELSNALDAAIRA---ET 316
Cdd:PRK09290 274 NSVNVIPGEVTFTLDIR-HPddavlDALVAELRAAAEAIAARRGVEVEI-----ELISRRPPVPFDPGLVAALEEaaeRL 347
|
90 100
....*....|....*....|...
gi 490656189 317 GVSPELSTTGGTSDGRFIARICP 339
Cdd:PRK09290 348 GLSYRRLPSGAGHDAQILAAVVP 370
|
|
| PRK12893 |
PRK12893 |
Zn-dependent hydrolase; |
224-359 |
5.94e-03 |
|
Zn-dependent hydrolase;
Pssm-ID: 237250 [Multi-domain] Cd Length: 412 Bit Score: 38.32 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 224 DEGNEYFPPTTWQVSNLRAGTGATNVIPGHADLLFNFRFSTASTVEG----LQARVHAILDRHGLDYTLN--WSVSGLPF 297
Cdd:PRK12893 252 RIAAALAPDGVATVGRLRVEPNSRNVIPGKVVFTVDIRHPDDARLDAmeaaLRAACAKIAAARGVQVTVEtvWDFPPVPF 331
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490656189 298 ltPRGeLSNALDAAIRAeTGVSPELSTTGGTSDGRFIARICPQVIEFGPPNASI-HKIDEHID 359
Cdd:PRK12893 332 --DPA-LVALVEAAAEA-LGLSHMRMVSGAGHDAMFLARVAPAAMIFVPCRGGIsHNEAEDTE 390
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
96-207 |
8.76e-03 |
|
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: 38.09 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490656189 96 LYGRGAADMKTSLAGFVVAAEEFvAAHPQHRGSIGFLITSDEEGpATDGTVKVVEALAARGERLDY----CIVGEPTSTA 171
Cdd:cd05654 126 LFGRGTMDMKSGLAVHLALLEQA-SEDEDFDGNLLLMAVPDEEV-NSRGMRAAVPALLELKKKHDLeyklAINSEPIFPQ 203
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 490656189 172 TLGDVVKNGRRGS----MSGELVVkGVQGHIAYPHLAKNP 207
Cdd:cd05654 204 YDGDQTRYIYTGSigkiLPGFLCY-GKETHVGEPFAGINA 242
|
|
| |
