|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
6-377 |
0e+00 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 710.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 6 VLELARELVRRPSVTPEDAGCQALMAERLERIGFQVERQRYGEVDNFWARRGHAGPLLCFAGHTDVVPTGPLDAWTHPPF 85
Cdd:PRK13009 4 VLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDFGDVKNLWARRGTEGPHLCFAGHTDVVPPGDLEAWTSPPF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 86 EAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGPAQDGTKKVIEALEARGEKIDWCLVGEP 165
Cdd:PRK13009 84 EPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVLEWLKARGEKIDYCIVGEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 166 SSRERLGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIEWDAGNASFPPTSLQLTNLHSGTGFR 245
Cdd:PRK13009 164 TSTERLGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEGNEFFPPTSLQITNIDAGTGAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 246 NVIPGSAELKFNLRYSTEQTMAGLQERIEALLQRHGLDYEVSWRDAGRPFLTRPGPFLSAVQEVVRDIAGVDPELSTGGG 325
Cdd:PRK13009 244 NVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDYTLEWTLSGEPFLTPPGKLVDAVVAAIEAVTGITPELSTSGG 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1819677128 326 TSDGRFIAPTGAAVVELGPVNASIHKIDEHVRVDDLEPLKDLYLGVMRRLLA 377
Cdd:PRK13009 324 TSDARFIADYGAQVVEFGPVNATIHKVNECVSVADLEKLTRIYERILERLLA 375
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
7-372 |
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: 654.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 7 LELARELVRRPSVTPEDAGCQALMAERLERIGFQVERQRYGEVDNFWARRGHAGPLLCFAGHTDVVPTGPLDAWTHPPFE 86
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFGGVKNLWARRGTGGPHLCFAGHTDVVPPGDLEGWSSDPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 87 AEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGPAQDGTKKVIEALEARGEKIDWCLVGEPS 166
Cdd:cd03891 81 PTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKIDYCIVGEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 167 SRERLGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIEWDAGNASFPPTSLQLTNLHSGTGFRN 246
Cdd:cd03891 161 SEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLDEGNEFFPPSSLQITNIDVGNGATN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 247 VIPGSAELKFNLRYSTEQTMAGLQERIEALLQRHGLDYEVSWRDAGRPFLTRPGPFLSAVQEVVRDIAGVDPELSTGGGT 326
Cdd:cd03891 241 VIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELSTSGGT 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1819677128 327 SDGRFIAPTGAAVVELGPVNASIHKIDEHVRVDDLEPLKDLYLGVM 372
Cdd:cd03891 321 SDARFIASYGCPVVEFGLVNATIHKVNERVSVADLEKLTDIYERIL 366
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
6-375 |
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: 578.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 6 VLELARELVRRPSVTPEDAGCQALMAERLERIGFQVERQRYGEVDNFWARRGHAGPLLCFAGHTDVVPTGPLDAWTHPPF 85
Cdd:TIGR01246 1 VTELAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGDTKNLWATRGTGEPVLAFAGHTDVVPAGPEEQWSSPPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 86 EAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGPAQDGTKKVIEALEARGEKIDWCLVGEP 165
Cdd:TIGR01246 81 EPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVETLMARDELIDYCIVGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 166 SSRERLGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIEWDAGNASFPPTSLQLTNLHSGTGFR 245
Cdd:TIGR01246 161 SSVKKLGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAIKWDEGNEFFPPTSLQITNIHAGTGAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 246 NVIPGSAELKFNLRYSTEQTMAGLQERIEALLQRHGLDYEVSWRDAGRPFLTRPGPFLSAVQEVVRDIAGVDPELSTGGG 325
Cdd:TIGR01246 241 NVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELSTGGG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1819677128 326 TSDGRFIAPTGAAVVELGPVNASIHKIDEHVRVDDLEPLKDLYLGVMRRL 375
Cdd:TIGR01246 321 TSDGRFIALMGAEVVEFGPVNATIHKVNECVSIEDLEKLSDVYQDLLENL 370
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
5-377 |
2.14e-127 |
|
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: 371.53 E-value: 2.14e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 5 RVLELARELVRRPSVTPEDAGCQALMAERLERIGFQVERQR-YGEVDNFWARR--GHAGPLLCFAGHTDVVPTGPLDAWT 81
Cdd:COG0624 13 EALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEvPPGRPNLVARRpgDGGGPTLLLYGHLDVVPPGDLELWT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 82 HPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGPAqDGTKKVIEALeARGEKIDWCL 161
Cdd:COG0624 93 SDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGS-PGARALVEEL-AEGLKADAAI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 162 VGEPSSrerlGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIEWDAG-NASFPPTSLQLTNLHS 240
Cdd:COG0624 171 VGEPTG----VPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRaDPLFGRTTLNVTGIEG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 241 GTGfRNVIPGSAELKFNLRYSTEQTMAGLQERIEALLQRHGLDYEVSWR---DAGRPFLTRP-GPFLSAVQEVVRDIAGV 316
Cdd:COG0624 247 GTA-VNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEVEvlgDGRPPFETPPdSPLVAAARAAIREVTGK 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819677128 317 DPELSTGGGTSDGRFIA-PTGAAVVELGPVN-ASIHKIDEHVRVDDLEPLKDLYLGVMRRLLA 377
Cdd:COG0624 326 EPVLSGVGGGTDARFFAeALGIPTVVFGPGDgAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
8-371 |
1.19e-104 |
|
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: 312.31 E-value: 1.19e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 8 ELARELVRRPSVTPEDAGCQALMAERLERIGFQVERQRYGEVDNFWARRGHA-GPLLCFAGHTDVVPTGPLDAWTHPPFE 86
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVATVGGGdGPVLLLNGHIDTVPPGDGDKWSFPPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 87 AEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGpAQDGTKKVIEALeaRGEKIDWCLVGEPS 166
Cdd:cd08659 81 GRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEV-GSDGARALLEAG--YADRLDALIVGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 167 srerlGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIEWDAG-NASFPPTSLQLTNLHSGTGFr 245
Cdd:cd08659 158 -----GLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPaHPLLGPPTLNVGVINGGTQV- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 246 NVIPGSAELKFNLRYSTEQTMAGLQERIEALLQRHGLDYEVSWRDAGRP--FLTRPGPFLSAVQEVVRDiAGVDPELSTG 323
Cdd:cd08659 232 NSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPpfFTDPDHPLVQALQAAARA-LGGDPVVRPF 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1819677128 324 GGTSDGRFIAPT-GAAVVELGP-VNASIHKIDEHVRVDDLEPLKDLYLGV 371
Cdd:cd08659 311 TGTTDASYFAKDlGFPVVVYGPgDLALAHQPDEYVSLEDLLRAAEIYKEI 360
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
64-374 |
4.00e-80 |
|
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 248.03 E-value: 4.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 64 CFAGHTDVVPTGPLDAWthpPFEAEVkDGLLWGRGAADMKASLAAMIVACEEFLAARPDhRGSLAFLVTSDEEGPaQDGT 143
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGG-MGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 144 KKVIEALEARGEKIDWCL---VGEPSS-RERLGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGI 219
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFglhIGEPTLlEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 220 EWDAGNASFPP--TSLQLTNLHSGTgfrNVIPGSAELKFNLRYSTEQTMAGLQERIEALL----QRHGLDYEVSWRDAGR 293
Cdd:pfam01546 155 VSRNVDPLDPAvvTVGNITGIPGGV---NVIPGEAELKGDIRLLPGEDLEELEERIREILeaiaAAYGVKVEVEYVEGGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 294 PFLTRPGPFLSAVQEVVRDIAGVDPELSTGG--GTSDGRFIAP-TGAAVVELGPVNASIHKIDEHVRVDDLEPLKDLYLG 370
Cdd:pfam01546 232 PPLVNDSPLVAALREAAKELFGLKVELIVSGsmGGTDAAFFLLgVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLAR 311
|
....
gi 1819677128 371 VMRR 374
Cdd:pfam01546 312 LLLK 315
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
8-377 |
2.24e-53 |
|
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: 180.48 E-value: 2.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 8 ELARELVRRPSVTPE-DAGCQALMAERLERIGFQVERQRYGEVD--NFWARRG-HAGPLLCFAGHTDVVPT-GPldAWTH 82
Cdd:cd03894 1 ELLARLVAFDTVSRNsNLALIEYVADYLAALGVKSRRVPVPEGGkaNLLATLGpGGEGGLLLSGHTDVVPVdGQ--KWSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 83 PPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPdhRGSLAFLVTSDEE-GPAqdGTKKVIEALEARGEKIDWCL 161
Cdd:cd03894 79 DPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKL--RKPLHLAFSYDEEvGCL--GVRHLIAALAARGGRPDAAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 162 VGEPSSRErlgdmLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGI--EWDAGNASF----PPTSLQL 235
Cdd:cd03894 155 VGEPTSLQ-----PVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELadRLAPGLRDPpfdpPYPTLNV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 236 TNLHSGTGfRNVIPGSAELKFNLRYSTEQTMAGLQERIEALLQRHGLDY----EVSWRDAGRPFLTRP-GPFLSAVQEVV 310
Cdd:cd03894 230 GLIHGGNA-VNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPeagiEVEPLFEVPGLETDEdAPLVRLAAALA 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 311 RDIAGvdpelSTGGGTSDGRFIAPTGAAVVELGPvnASI---HKIDEHVRVDDLEPlkdlYLGVMRRLLA 377
Cdd:cd03894 309 GDNKV-----RTVAYGTEAGLFQRAGIPTVVCGP--GSIaqaHTPDEFVELEQLDR----CEEFLRRLIA 367
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
1-377 |
1.31e-52 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 179.42 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 1 MSAGRVLELARELVRRPSVTPED---AGCQALMAERLERIGFQVE---------RQRYGEVDNFWARRGHAGPLLCFAGH 68
Cdd:PRK08651 3 AMMFDIVEFLKDLIKIPTVNPPGenyEEIAEFLRDTLEELGFSTEiievpneyvKKHDGPRPNLIARRGSGNPHLHFNGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 69 TDVVPTGPLDAwTHPPFEAEVKDGLLWGRGAADMKASLAAMIVAceeFLAARPDHRGSLAFLVTSDEEgPAQDGTKKVIE 148
Cdd:PRK08651 83 YDVVPPGEGWS-VNVPFEPKVKDGKVYGRGASDMKGGIAALLAA---FERLDPAGDGNIELAIVPDEE-TGGTGTGYLVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 149 ALEARGekiDWCLVGEPSSRERLGdmlrIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGI--------E 220
Cdd:PRK08651 158 EGKVTP---DYVIVGEPSGLDNIC----IGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSlstikskyE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 221 WDAGNASFPPTSLQLTNLHSGTGFrNVIPGSAELKFNLRYSTEQTMAGLQERIEALLQR----HGLDYEVSWRDAGRPFL 296
Cdd:PRK08651 231 YDDERGAKPTVTLGGPTVEGGTKT-NIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEvapeLGIEVEFEITPFSEAFV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 297 TRPG-PFLSAVQEVVRDIAGVDPE--LSTGGGtsDGRFIAPTGAAVVELGP-VNASIHKIDEHVRVDDLEPLKDLYLGVM 372
Cdd:PRK08651 310 TDPDsELVKALREAIREVLGVEPKktISLGGT--DARFFGAKGIPTVVYGPgELELAHAPDEYVEVKDVEKAAKVYEEVL 387
|
....*
gi 1819677128 373 RRLLA 377
Cdd:PRK08651 388 KRLAK 392
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
7-362 |
8.82e-52 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 176.82 E-value: 8.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 7 LELARELVRRPSVTP---EDAGCQALMAERLERIGFQVERQRYGEVDNFWARR------GHAG-PLLCFAGHTDVVPTGP 76
Cdd:TIGR01910 1 VELLKDLISIPSVNPpggNEETIANYIKDLLREFGFSTDVIEITDDRLKVLGKvvvkepGNGNeKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 77 LDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGpAQDGTKKVIEaleaRG-- 154
Cdd:TIGR01910 81 LELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEES-GEAGTLYLLQ----RGyf 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 155 EKIDWCLVGEPSSrerlGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPF---LQELVgIEWDAGNASFP-- 229
Cdd:TIGR01910 156 KDADGVLIPEPSG----GDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLiteLNELE-EHIYARNSYGFip 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 230 -PTSLQLTNLHSGTgFRNVIPGSAELKFNLRYSTEQTMAGLQERIEALLQRhgLDYEVSWRDAGRPFLTRPGP------- 301
Cdd:TIGR01910 231 gPITFNPGVIKGGD-WVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKA--LSKSDGWLYENEPVVKWSGPnetppds 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1819677128 302 -FLSAVQEVVRDIAGVDPELSTGGGTSDGRFIAPTGAAVVELGP-VNASIHKIDEHVRVDDLE 362
Cdd:TIGR01910 308 rLVKALEAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPgDLETAHQVNEYISIKNLV 370
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-362 |
4.39e-49 |
|
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: 169.10 E-value: 4.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 7 LELARELVRRPSVTP---EDAGCQALMAERLERIGFQVER-----QRYGEVDNFWArrGHAGPLLCFAGHTDVVPTGPLD 78
Cdd:cd08011 1 VKLLQELVQIPSPNPpgdNTSAIAAYIKLLLEDLGYPVELheppeEIYGVVSNIVG--GRKGKRLLFNGHYDVVPAGDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 79 AWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGPAQDGTKKVIEALEARGekiD 158
Cdd:cd08011 79 GWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYLLEKVRIKP---N 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 159 WCLVGEPSSrerlGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIEwdagnasfppTSLQLTNL 238
Cdd:cd08011 156 DVLIGEPSG----SDNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELE----------KTVNPGVI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 239 HSGTGFrNVIPGSAELKFNLRYSTEQTMAGLQERIEALLqrhGLDYEVSWRDAGRPFLTRPGP---FLSAVQEVVRDIAG 315
Cdd:cd08011 222 KGGVKV-NLVPDYCEFSVDIRLPPGISTDEVLSRIIDHL---DSIEEVSFEIKSFYSPTVSNPdseIVKKTEEAITEVLG 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1819677128 316 VDPELSTGGGTSDGRFIAPTGAAVVELGPVNAS-IHKIDEHVRVDDLE 362
Cdd:cd08011 298 IRPKEVISVGASDARFYRNAGIPAIVYGPGRLGqMHAPNEYVEIDELI 345
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
6-377 |
5.88e-44 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 156.64 E-value: 5.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 6 VLELARELVRRPSVTPEDAGCQALMAERLERIGF-QVERQRYGevdNFWARRGHAGPLLCFAGHTDVVPTGPLDAWTHPP 84
Cdd:PRK13004 17 MTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFdKVEIDPMG---NVLGYIGHGKKLIAFDAHIDTVGIGDIKNWDFDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 85 FEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEE---GPAQDgtkkviEALEARGEKIDWCL 161
Cdd:PRK13004 94 FEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEEdcdGLCWR------YIIEEDKIKPDFVV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 162 VGEPSSRErlgdmLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIEWDAGNASF-PPTSLQLTNLHS 240
Cdd:PRK13004 168 ITEPTDLN-----IYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNLKEDPFlGKGTLTVSDIFS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 241 GTGFRNVIPGSAELKFNLRYSTEQTMAGLQERIEALLQRHGLDYEVSWRDAGRPFLTR---------PG-------PFLS 304
Cdd:PRK13004 243 TSPSRCAVPDSCAISIDRRLTVGETWESVLAEIRALPAVKKANAKVSMYNYDRPSYTGlvyptecyfPTwlypedhEFVK 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819677128 305 AVQEVVRDIAGVDPEL-----STGGGTSDGRFIAPTgaavVELGPVNASI-HKIDEHVRVDDLEPLKDLYLGVMRRLLA 377
Cdd:PRK13004 323 AAVEAYKGLFGKAPEVdkwtfSTNGVSIAGRAGIPT----IGFGPGKEPLaHAPNEYTWKEQLVKAAAMYAAIPKSLLK 397
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
6-363 |
2.87e-43 |
|
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: 153.90 E-value: 2.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 6 VLELARELVRRPSVTPEDAGCQA---LMAERLERIGFQVERQRYGEV-DNFWAR-RGHAGPLLCFAGHTDVV-PTGPLDA 79
Cdd:cd03885 1 MLDLLERLVNIESGTYDKEGVDRvaeLLAEELEALGFTVERRPLGEFgDHLIATfKGTGGKRVLLIGHMDTVfPEGTLAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 80 WthpPFEaeVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEgPAQDGTKKVIEAlEARGEKIdw 159
Cdd:cd03885 81 R---PFT--VDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEE-IGSPGSRELIEE-EAKGADY-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 160 CLVGEPSsreRLGDMLRIGRRGSLSCDLLVHGIQGHV-AYPEKARNPLHQLAPFLQELVGIewdagNASFPPTSLQLTNL 238
Cdd:cd03885 152 VLVFEPA---RADGNLVTARKGIGRFRLTVKGRAAHAgNAPEKGRSAIYELAHQVLALHAL-----TDPEKGTTVNVGVI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 239 HSGTGfRNVIPGSAELKFNLRYSTEQTMAGLQERIEALLQRHGL-DYEVSW-RDAGRPFLtRPGP----FLSAVQEVVRD 312
Cdd:cd03885 224 SGGTR-VNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTLVpGTSVELtGGLNRPPM-EETPasrrLLARAQEIAAE 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1819677128 313 IAGVDPELSTGGGtSDGRFIAPTGAAVVE-LGPVNASIHKIDEHVRVDDLEP 363
Cdd:cd03885 302 LGLTLDWEATGGG-SDANFTAALGVPTLDgLGPVGGGAHTEDEYLELDSLVP 352
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
8-375 |
2.31e-39 |
|
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: 142.88 E-value: 2.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 8 ELARELVRRPSVTPEDAGCQALMAERLERIGFQVERQrygEVDNFWARRGHAGPLLCFAGHTDVVPtGPLdawthppfEA 87
Cdd:cd05653 5 ELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVD---EAGNAVGGAGSGPPDVLLLGHIDTVP-GEI--------PV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 88 EVKDGLLWGRGAADMKASLAAMIVAceeFLAARPDHRGSLAFLVTSDEEGPAQdGTKKVIEaleaRGEKIDWCLVGEPSS 167
Cdd:cd05653 73 RVEGGVLYGRGAVDAKGPLAAMILA---ASALNEELGARVVVAGLVDEEGSSK-GARELVR----RGPRPDYIIIGEPSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 168 rerlGDMLRIGRRGSLSCDLLVHGIQGHVAYPEkaRNPLHQLAPFLQELVgiEWDAG--NASFPPTSLQLTNLHSGTgFR 245
Cdd:cd05653 145 ----WDGITLGYRGSLLVKIRCEGRSGHSSSPE--RNAAEDLIKKWLEVK--KWAEGynVGGRDFDSVVPTLIKGGE-SS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 246 NVIPGSAELKFNLRYSTEQTmaglqeRIEALLQRHGL--DYEVSWRDAGRPFLTRP-GPFLSAVQEVVRDiAGVDPELST 322
Cdd:cd05653 216 NGLPQRAEATIDLRLPPRLS------PEEAIALATALlpTCELEFIDDTEPVKVSKnNPLARAFRRAIRK-QGGKPRLKR 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1819677128 323 GGGTSDGRFIAPT-GAAVVELGPVNASI-HKIDEHVRVDDLEPLKDLYLGVMRRL 375
Cdd:cd05653 289 KTGTSDMNVLAPLwTVPIVAYGPGDSTLdHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
57-377 |
4.83e-38 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 140.40 E-value: 4.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 57 GHAGPLLCFAGHTDVVPTGPLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEE 136
Cdd:PRK08588 56 GSGSPVLALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 137 ----GPAQ---DGTKKVIEALeargekidwcLVGEPSsrerlGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQL 209
Cdd:PRK08588 136 vgelGAKQlteKGYADDLDAL----------IIGEPS-----GHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 210 APFLQELvgiewDAGNASFPPTSLQLTNL-HSGTGFR-----NVIPGSAELKFNLR----YSTEQTMAGLQERIEALLQR 279
Cdd:PRK08588 201 LEFYNEQ-----KEYFDSIKKHNPYLGGLtHVVTIINggeqvNSVPDEAELEFNIRtipeYDNDQVISLLQEIINEVNQN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 280 HG----LDYEVSWrdagRPFLTRP-GPFLSAVQEVVRDIAGVDPELSTGGGTSDG-RFI-APTGAAVVELGP-VNASIHK 351
Cdd:PRK08588 276 GAaqlsLDIYSNH----RPVASDKdSKLVQLAKDVAKSYVGQDIPLSAIPGATDAsSFLkKKPDFPVIIFGPgNNLTAHQ 351
|
330 340
....*....|....*....|....*.
gi 1819677128 352 IDEHVRVDDLEPLKDLYLGVMRRLLA 377
Cdd:PRK08588 352 VDEYVEKDMYLKFIDIYKEIIIQYLK 377
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-371 |
2.10e-35 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 133.32 E-value: 2.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 7 LELARELVRRPSVTPEDAGCQALMAERLERIGF-QVERQRYGevdNFWARRGHAGPLLCFAGHTDVVPTGPLDAWTHPPF 85
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGFdEVEIDPMG---NVIGYIGGGKKKILFDGHIDTVGIGNIDNWKFDPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 86 EAEVKDGLLWGRGAADMKASLAAMIVACEEF--LAARPDhRGSLAFLVTSDEE---GPAQDgtkkviEALEARGEKIDWC 160
Cdd:cd05649 78 EGYETDGKIYGRGTSDQKGGLASMVYAAKIMkdLGLRDF-AYTILVAGTVQEEdcdGVCWQ------YISKADKIKPDFV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 161 LVGEPSsrerlgDM-LRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIEWDAGNASF-PPTSLQLTNL 238
Cdd:cd05649 151 VSGEPT------DGnIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFPEAPFlGRGTLTVTDI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 239 HSGTGFRNVIPGSAELKFNLRYSTEQTMAGLQERIEAL--LQRHGLDYEVSWRDAGRPFLTR---------PG------- 300
Cdd:cd05649 225 FSTSPSRCAVPDSCRISIDRRLTVGETWEGCLEEIRALpaVKKYGDDVAVSMYNYDRPSYTGevyeseryfPTwllpedh 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819677128 301 PFLSAVQEVVRDIAGVDPEL-----STGGGTSDGRFIAPTgaavVELGP-VNASIHKIDEHVRVDDLEPLKDLYLGV 371
Cdd:cd05649 305 ELVKALLEAYKALFGARPLIdkwtfSTNGVSIMGRAGIPC----IGFGPgAENQAHAPNEYTWKEDLVRCAAGYAAI 377
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
8-366 |
2.41e-34 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 130.89 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 8 ELARELVRRPSVTPEDAGCQALMAERLERIGFQVERQR-----------YGEVDNFWAR----------RGHAGPLLCFA 66
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDRWEidveklkhhpgFSPVAVDYAGapnvvgthrpRGETGRSLILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 67 GHTDVVPTGPLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGpAQDGTKKV 146
Cdd:cd03895 81 GHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEEC-TGNGALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 147 IEaleaRGEKIDWCLVGEPSsrerlGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIE--WDAG 224
Cdd:cd03895 160 LM----RGYRADAALIPEPT-----ELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEreWNAR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 225 NASFP-------PTSLQLTNLHSGTGFRNVipgSAELKFNLRY------STEQTMAGLQERIEALLQRH----GLDYEVS 287
Cdd:cd03895 231 KKSHPhfsdhphPINFNIGKIEGGDWPSSV---PAWCVLDCRIgiypgeSPEEARREIEECVADAAATDpwlsNHPPEVE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 288 WRDAG-RPFLTRPG-PFLSAVQEVVRDIAGVDPELSTGGGTSDGRFIAPTGA--AVVeLGPVNASIHKIDEHVrvdDLEP 363
Cdd:cd03895 308 WNGFQaEGYVLEPGsDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGDipALC-YGPGSRDAHGFDESV---DLES 383
|
...
gi 1819677128 364 LKD 366
Cdd:cd03895 384 LRK 386
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
8-375 |
2.44e-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: 121.85 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 8 ELARELVRRPSVT-PEDAGCQALMAERLERIGFQVERQRY---GEVDNFWARRGHAGPL-LCFAGHTDVVPTGPlDAWTH 82
Cdd:TIGR01892 1 EILTKLVAFDSTSfRPNVDLIDWAQAYLEALGFSVEVQPFpdgAEKSNLVAVIGPSGAGgLALSGHTDVVPYDD-AAWTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 83 PPFEAEVKDGLLWGRGAADMKASLAAMIVACEEfLAARPdHRGSLAFLVTSDEEGPAQdGTKKVIEALEARGekiDWCLV 162
Cdd:TIGR01892 80 DPFRLTEKDGRLYGRGTCDMKGFLACALAAAPD-LAAEQ-LKKPLHLALTADEEVGCT-GAPKMIEAGAGRP---RHAII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 163 GEPSsrerlgDMLRI-GRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGI-----EWDAGNASFPP-TSLQL 235
Cdd:TIGR01892 154 GEPT------RLIPVrAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLadtllREDLDEGFTPPyTTLNI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 236 TNLHSGTGfRNVIPGSAELKFNLRYSTEQTMA---GLQERIEALLQRHGLDYEVSWR--DAGRPFLTRPGpflSAVQEVV 310
Cdd:TIGR01892 228 GVIQGGKA-VNIIPGACEFVFEWRPIPGMDPEellQLLETIAQALVRDEPGFEVQIEvvSTDPGVNTEPD---AELVAFL 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819677128 311 RDIAGVDPELSTGGgtSDGRFIAPTGAAVVELGPvnASI---HKIDEHVRVDDLEPLKdlylGVMRRL 375
Cdd:TIGR01892 304 EELSGNAPEVVSYG--TEAPQFQELGAEAVVCGP--GDIrqaHQPDEYVEIEDLVRCR----AVLARL 363
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-369 |
1.17e-30 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 119.72 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 6 VLELARELVRRPSVTPEDAGCQALMAERLERIGFQVERQRygevDNFWARRGH---AGPLLCFAGHTDVVPtgPLDAWTH 82
Cdd:cd05651 2 AIELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRKG----NNVWAENGHfdeGKPTLLLNSHHDTVK--PNAGWTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 83 PPFEAEVKDGLLWGRGAADMKASLAAMIVAceeF--LAARPDHRGSLAFLVTSDEEGPAQDGTKKVIEALeargEKIDWC 160
Cdd:cd05651 76 DPFEPVEKGGKLYGLGSNDAGASVVSLLAT---FlhLYSEGPLNYNLIYAASAEEEISGKNGIESLLPHL----PPLDLA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 161 LVGEPSSRErlgdmLRIGRRGSLSCDLLVHGIQGHVAYPEkARNPLHQLAPFLQELVGIEWDAGNASFPPTSLQLTNLHS 240
Cdd:cd05651 149 IVGEPTEMQ-----PAIAEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDIQWLRDFRFDKVSPLLGPVKMTVTQINA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 241 GTGfRNVIPGSAELKFNLR----YSTEQTMAGLQERIEALLQRHGLDYEVSWRDAGRpfltrpgPFLSAVQEVVRDIAGv 316
Cdd:cd05651 223 GTQ-HNVVPDSCTFVVDIRtteaYTNEEIFEIIRGNLKSEIKPRSFRLNSSAIPPDH-------PIVQAAIAAGRTPFG- 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1819677128 317 DPELstgggtSDGRFIA-PTgaavVELGPVNAS-IHKIDEHVRVDDLEPLKDLYL 369
Cdd:cd05651 294 SPTL------SDQALMPfPS----VKIGPGDSSrSHTADEFIELSEIEEGIDIYI 338
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
7-362 |
1.47e-30 |
|
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: 120.93 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 7 LELARELVRRPSVTPEDAGCQA-----LMAERLERIGFQVE---RQRYGEVDNFWAR-RG---HAGPLLcFAGHTDVVPT 74
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTGSEtraaeVLAARLAEAGIQTEifvVESHPGRANLVARiGGtdpSAGPLL-LLGHIDVVPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 75 GPLDaWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGPAQDGTKKVIEALEARG 154
Cdd:cd05675 80 DASD-WSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDNHPELF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 155 EKIDWCLvGE------PSSRERLGDMLRIGRRGSLSCDLLVHGIQGHVAYPeKARNPLHQLAPFLQELVGIEW------- 221
Cdd:cd05675 159 DGATFAL-NEggggslPVGKGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRP-TDDNAITRLAEALRRLGAHNFpvrltde 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 222 -------------DAGNASFPPTSLQ-----------------LTNLHSGTGFR-----NVIPGSAELKFNLRYSTEQTM 266
Cdd:cd05675 237 tayfaqmaelaggEGGALMLTAVPVLdpalaklgpsapllnamLRNTASPTMLDagyatNVLPGRATAEVDCRILPGQSE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 267 AGLQERIEALLqrhgLDYEVSWRDAGRPFLTRP---GPFLSAVQEVVRDI---AGVDPELSTGGgtSDGRFIAPT----- 335
Cdd:cd05675 317 EEVLDTLDKLL----GDPDVSVEAVHLEPATESpldSPLVDAMEAAVQAVdpgAPVVPYMSPGG--TDAKYFRRLgipgy 390
|
410 420 430
....*....|....*....|....*....|
gi 1819677128 336 GAAVVELGP---VNASIHKIDEHVRVDDLE 362
Cdd:cd05675 391 GFAPLFLPPeldYTGLFHGVDERVPVESLY 420
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
6-362 |
1.49e-30 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 121.02 E-value: 1.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 6 VLELARELVRRPSVTP---EDAGCQALMAERLERIGFQVERQRY----GEVD-----NFWARR--GHAGPLLCFAGHTDV 71
Cdd:PRK13013 16 LVALTQDLIRIPTLNPpgrAYREICEFLAARLAPRGFEVELIRAegapGDSEtyprwNLVARRqgARDGDCVHFNSHHDV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 72 VPTGplDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGPAQDGTKKVIEALE 151
Cdd:PRK13013 96 VEVG--HGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGGVAYLAEQGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 152 ARGEKIDWCLVGEPSSRERLGdmlrIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQElvgIE------WDAGN 225
Cdd:PRK13013 174 FSPDRVQHVIIPEPLNKDRIC----LGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAE---IEerlfplLATRR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 226 ASFPPT-------SLQLTNLHSG--------TGFRN-VIPGSAELKFNLRYSTEQTMAGLQERIEALL-----QRHGLDY 284
Cdd:PRK13013 247 TAMPVVpegarqsTLNINSIHGGepeqdpdyTGLPApCVADRCRIVIDRRFLIEEDLDEVKAEITALLerlkrARPGFAY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 285 EVSWRDAGRPFLT-RPGPFLSAVQEVVRDIAGVDPELSTGGGTSDGRFIAPTGAA--VVELGP-VNASIHKIDEHVRVDD 360
Cdd:PRK13013 327 EIRDLFEVLPTMTdRDAPVVRSVAAAIERVLGRQADYVVSPGTYDQKHIDRIGKLknCIAYGPgILDLAHQPDEWVGIAD 406
|
..
gi 1819677128 361 LE 362
Cdd:PRK13013 407 MV 408
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-285 |
2.96e-30 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal, and have been inferred by similarity as being related to both ArgE and DapE.
Pssm-ID: 349903 [Multi-domain] Cd Length: 340 Bit Score: 118.53 E-value: 2.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 6 VLELARELVRRPSVTPEDAGCQALMAERLERIGFQVERQR--YGEVDNFWARRG-HAGPLLCFAGHTDVVPtgPldawtH 82
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKQPveNKDRFNVYAYPGsSRQPRVLLTSHIDTVP--P-----F 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 83 PPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFL-VTSDEEGpaQDGTKKVIEALEARGEKIdwcL 161
Cdd:cd05652 74 IPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLfVVGEETG--GDGMKAFNDLGLNTWDAV---I 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 162 VGEPSSRErlgdmLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIEWdAGNASFPPTSLQLTNLHSG 241
Cdd:cd05652 149 FGEPTELK-----LASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADL-PSSELLGPTTLNIGRISGG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1819677128 242 TGfRNVIPGSAELKFNLRYSTEqtMAGLQERIEALLQRHGLDYE 285
Cdd:cd05652 223 VA-ANVVPAAAEASVAIRLAAG--PPEVKDIVKEAVAGILTDTE 263
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
7-366 |
5.71e-30 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 119.34 E-value: 5.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 7 LELARELVRRPSVTPEDAGCQALMAERLERIGFQVERQR-----------YG--EVDNFWAR--------RGHAGPLLCF 65
Cdd:PRK06837 23 VAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDRWSidpddlkshpgAGpvEIDYSGAPnvvgtyrpAGKTGRSLIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 66 AGHTDVVPTGPLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAA--RPDHRgslAFLVTSDEEGPAQDGt 143
Cdd:PRK06837 103 QGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAglAPAAR---VHFQSVIEEESTGNG- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 144 kkvieALEA--RGEKIDWCLVGEPssrerLGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIE- 220
Cdd:PRK06837 179 -----ALSTlqRGYRADACLIPEP-----TGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRELEa 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 221 -WDAGNASFP-------PTSLQLTNLHSGTGFRNVipgSAELKFNLR------YSTEQTMAGLQERIEALLQRHgldyev 286
Cdd:PRK06837 249 eWNARKASDPhfedvphPINFNVGIIKGGDWASSV---PAWCDLDCRiaiypgVTAADAQAEIEACLAAAARDD------ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 287 SWRDAGRPFLTRPGpFLS--AVQEvvrdiAGVDPE--------LSTGG--------GTSDGRFIA-----PTgaavVELG 343
Cdd:PRK06837 320 RFLSNNPPEVVWSG-FLAegYVLE-----PGSEAEaalarahaAVFGGplrsfvttAYTDTRFYGlyygiPA----LCYG 389
|
410 420
....*....|....*....|...
gi 1819677128 344 PVNASIHKIDEHVrvdDLEPLKD 366
Cdd:PRK06837 390 PSGEGIHGFDERV---DLESVRK 409
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
51-362 |
8.90e-30 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 117.98 E-value: 8.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 51 NFWARRG-HAGPLLCFAGHTDVVP-TGPldAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAA---RPDHrg 125
Cdd:PRK07522 54 NLFATIGpADRGGIVLSGHTDVVPvDGQ--AWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAplrRPLH-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 126 sLAFlvTSDEE-GPAqdGTKKVIEALEARGEKIDWCLVGEPSSrerlgdmLR--IGRRGSLSCDLLVHGIQGHVAYPEKA 202
Cdd:PRK07522 130 -LAF--SYDEEvGCL--GVPSMIARLPERGVKPAGCIVGEPTS-------MRpvVGHKGKAAYRCTVRGRAAHSSLAPQG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 203 RNPLHQLAPFLQELVGI-EWDAGNASF-----PP-TSLQLTNLHSGTGFrNVIPGSAELKFNLRY----STEQTMAGLQE 271
Cdd:PRK07522 198 VNAIEYAARLIAHLRDLaDRLAAPGPFdalfdPPySTLQTGTIQGGTAL-NIVPAECEFDFEFRNlpgdDPEAILARIRA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 272 RIEALL----QRHGLDYEVSW--RDAGRPFLTRPGpflSAVQEVVRDIAGVDPELSTGGGTSDGRFIAPTGAAVVeLGPv 345
Cdd:PRK07522 277 YAEAELlpemRAVHPEAAIEFepLSAYPGLDTAED---AAAARLVRALTGDNDLRKVAYGTEAGLFQRAGIPTVV-CGP- 351
|
330 340
....*....|....*....|
gi 1819677128 346 nASI---HKIDEHVRVDDLE 362
Cdd:PRK07522 352 -GSIeqaHKPDEFVELAQLA 370
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
8-375 |
1.27e-29 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 116.98 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 8 ELARELVRRPSVTPEDAGCQALMAERLERIGFQVerqRYGEVDNFWARRGHAGPLLCFAGHTDVVPtG--PLdawthppf 85
Cdd:PRK04443 10 ELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREA---WVDEAGNARGPAGDGPPLVLLLGHIDTVP-GdiPV-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 86 eaEVKDGLLWGRGAADMKASLAAMIVACEEfLAARPDHRGSLAFLVtsDEEGPAQDGTKkvieaLEARGEKIDWCLVGEP 165
Cdd:PRK04443 78 --RVEDGVLWGRGSVDAKGPLAAFAAAAAR-LEALVRARVSFVGAV--EEEAPSSGGAR-----LVADRERPDAVIIGEP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 166 SSRERlgdmLRIGRRGSLSCDLLVHGIQGHVAYPEkaRNPLHQLAPFLQELVgiEWDAGNAS----FPPTSLQLTNLHSG 241
Cdd:PRK04443 148 SGWDG----ITLGYKGRLLVTYVATSESFHSAGPE--PNAAEDAIEWWLAVE--AWFEANDGrervFDQVTPKLVDFDSS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 242 T-GFRnvipGSAELKFNLR----YSTeqtmaglqERIEALLQRHGLDYEVSWRDAGRPFLTRP-GPFLSAVQEVVRDiAG 315
Cdd:PRK04443 220 SdGLT----VEAEMTVGLRlppgLSP--------EEAREILDALLPTGTVTFTGAVPAYMVSKrTPLARAFRVAIRE-AG 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819677128 316 VDPELSTGGGTSDGRFIAPT-GAAVVELGPVNASI-HKIDEHVRVDDLEPLKDLYLGVMRRL 375
Cdd:PRK04443 287 GTPRLKRKTGTSDMNVVAPAwGCPMVAYGPGDSDLdHTPDEHLPLAEYLRAIAVLTDVLERL 348
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
5-366 |
4.23e-29 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 116.49 E-value: 4.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 5 RVLELARELVRRPSVTPEDAG------CQALmAERLERIGFqVERQRYGEVD---------NFWARRGHAGP--LLCFAG 67
Cdd:PRK13983 6 EMIELLSELIAIPAVNPDFGGegekekAEYL-ESLLKEYGF-DEVERYDAPDprviegvrpNIVAKIPGGDGkrTLWIIS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 68 HTDVVPTGPLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEF--LAARPDHRGSLAFLvtSDEEgpaqDGTKK 145
Cdd:PRK13983 84 HMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALmdLGIRPKYNLGLAFV--SDEE----TGSKY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 146 VIEAL-EARGE---KIDWCLVgePSSRERLGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGI-- 219
Cdd:PRK13983 158 GIQYLlKKHPElfkKDDLILV--PDAGNPDGSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRAAADFALELDEAlh 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 220 -EWDAGNASF-PPTS-LQLTNLHSGTGFRNVIPGSAELKFNLR----YSTEQTMAGLQERIEALLQRHG--LDYEVSWRD 290
Cdd:PRK13983 236 eKFNAKDPLFdPPYStFEPTKKEANVDNINTIPGRDVFYFDCRvlpdYDLDEVLKDIKEIADEFEEEYGvkIEVEIVQRE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819677128 291 AGRPFLTRPGPFLSAVQEVVRDIAGVDPEL-STGGGTSdGRFIAPTGAAVVELGPVNASIHKIDEHVRVDDLepLKD 366
Cdd:PRK13983 316 QAPPPTPPDSEIVKKLKRAIKEVRGIEPKVgGIGGGTV-AAFLRKKGYPAVVWSTLDETAHQPNEYAKISNL--IED 389
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-361 |
4.60e-29 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349901 [Multi-domain] Cd Length: 389 Bit Score: 116.02 E-value: 4.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 5 RVLELARELVRRPSVTPEDAG-CQALMAERLERI----GFQvERQRYGEVDNFWARR--------GHAGPLLCFAGHTDV 71
Cdd:cd05650 2 EIIELERDLIRIPAVNPESGGeGEKEKADYLEKKlreyGFY-TLERYDAPDERGIIRpnivakipGGNDKTLWIISHLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 72 VPTGPLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAA--RPDHRGSLAFLvtSDEEGPAQDGTKKVIEA 149
Cdd:cd05650 81 VPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNgiTPKYNFGLLFV--ADEEDGSEYGIQYLLNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 150 LEARGeKIDWCLVgePSSRERLGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPF---LQELVGIEWDAGNA 226
Cdd:cd05650 159 FDLFK-KDDLIIV--PDFGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFaleLDELLHEKFDEKDD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 227 SF-PPTS-LQLTNLHSGTGFRNVIPGSAELKFNLR----YSTEQTMAGLQERIEAlLQRH---GLDYEVSWRDAGRPFLT 297
Cdd:cd05650 236 LFnPPYStFEPTKKEANVPNVNTIPGYDVFYFDCRvlptYKLDEVLKFVNKIISD-FENSygaGITYEIVQKEQAPPATP 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819677128 298 RPGPFLSAVQEVVRDIAGVDPELSTGGGTSDGRFIAPTGAAVVELGPVNASIHKIDEHVRVDDL 361
Cdd:cd05650 315 EDSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYIRISHI 378
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
53-377 |
2.02e-28 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 115.81 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 53 WARRGHAGPLLCFAGHTDVVPTGP--LDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAA--RPDHRGSLA 128
Cdd:PRK08262 104 WKGSDPSLKPIVLMAHQDVVPVAPgtEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQgfQPRRTIYLA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 129 FlvTSDEEgPAQDGTKKVIEALEARGEKIDWCL-----VGE---PSSRERLGdMLRIGRRGSLSCDLLVHGIQGHVAYP- 199
Cdd:PRK08262 184 F--GHDEE-VGGLGARAIAELLKERGVRLAFVLdeggaITEgvlPGVKKPVA-LIGVAEKGYATLELTARATGGHSSMPp 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 200 ---------------EKARNP----------LHQLAP----FLQELVGIEWD-------------AGNASFpPTSLQLTN 237
Cdd:PRK08262 260 rqtaigrlaraltrlEDNPLPmrlrgpvaemFDTLAPemsfAQRVVLANLWLfeplllrvlakspETAAML-RTTTAPTM 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 238 LHSGTGFrNVIPGSAELKFNLRYSTEQTMAGLQERIEALLqrHGLDYEVSWRDA---GRPFLTRPGPFLSAVQEVVRDI- 313
Cdd:PRK08262 339 LKGSPKD-NVLPQRATATVNFRILPGDSVESVLAHVRRAV--ADDRVEIEVLGGnsePSPVSSTDSAAYKLLAATIREVf 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819677128 314 --AGVDPELSTGGgtSDGRFIAPTGAAVVELGPVNAS------IHKIDEHVRVDDLEPLKDLYLGVMRRLLA 377
Cdd:PRK08262 416 pdVVVAPYLVVGA--TDSRHYSGISDNVYRFSPLRLSpedlarFHGTNERISVANYARMIRFYYRLIENAAG 485
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
5-376 |
3.74e-28 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 112.93 E-value: 3.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 5 RVLELARELVRRPSVTPEDAGCQALMAERLERIGFQVERQRYGEVDNFWARrghAGPLLCFAGHTDVVPtgpldawthPP 84
Cdd:PRK08652 3 RAKELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIESDGEVINIVVN---SKAELFVEVHYDTVP---------VR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 85 FEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLvtSDEEGPAQdGTKKVIEALEARgekidWCLVGE 164
Cdd:PRK08652 71 AEFFVDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFV--SDEEEGGR-GSALFAERYRPK-----MAIVLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 165 PSSRErlgdmLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIEWDAGNASFPPTSLQLTnlhSGTGF 244
Cdd:PRK08652 143 PTDLK-----VAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPHIGIQEI---IGGSP 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 245 RNVIPGSAELKFNLRYSTEQTMAGLQERIEALLQRHGLDYEVSWRDAGrpFLTRPGPFLSAVQEVVRDIAGVDPELSTGG 324
Cdd:PRK08652 215 EYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEYTEIWDG--FELDEDEEIVQLLEKAMKEVGLEPEFTVMR 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1819677128 325 GTSDGRFIAPTGAAVVELGPVNASI-HKIDEHVRVDDLEPLKDLYLGVMRRLL 376
Cdd:PRK08652 293 SWTDAINFRYNGTKTVVWGPGELDLcHTKFERIDVREVEKAKEFLKALNEILL 345
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
177-285 |
2.76e-27 |
|
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: 103.96 E-value: 2.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 177 IGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIEWDAGNaSFPPTSLQLTNLHSGTgFRNVIPGSAELKF 256
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGF-DFPRTTLNITGIEGGT-ATNVIPAEAEAKF 78
|
90 100
....*....|....*....|....*....
gi 1819677128 257 NLRYSTEQTMAGLQERIEALLQRHGLDYE 285
Cdd:pfam07687 79 DIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
6-362 |
3.35e-26 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 107.53 E-value: 3.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 6 VLELARELVRRPSVTpedaGCQALMAERLE---RIGFQVERQRYGevDNFWARRgHAGPL--LCFAGHTDVVPTgpldAW 80
Cdd:cd05647 1 PIELTAALVDIPSVS----GNEKPIADEIEaalRTLPHLEVIRDG--NTVVART-ERGLAsrVILAGHLDTVPV----AG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 81 THPPFEAEvkDGLLWGRGAADMKASLAAMIVACEEFLAARPDHrgSLAFLVTSDEEGPA-QDGTKKVIEALearGE--KI 157
Cdd:cd05647 70 NLPSRVEE--DGVLYGCGATDMKAGDAVQLKLAATLAAATLKH--DLTLIFYDCEEVAAeLNGLGRLAEEH---PEwlAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 158 DWCLVGEPSsrerlGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELvgiewdagnASFPPTSLQLTN 237
Cdd:cd05647 143 DFAVLGEPT-----DGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARL---------AAYEPRTVNIDG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 238 LH----------SGTGFRNVIPGSAELKFNLRYSTEQTMAGLQERIEALLQRHGLDYEVSWRDAG-RPFLTRP--GPFLS 304
Cdd:cd05647 209 LTyreglnavfiSGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEIEVTDLSPGaLPGLDHPvaRDLIE 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1819677128 305 AVQEVVRdiagvdPELstgGGTSDGRFIApTGAAVVELGPVNASI-HKIDEHVRVDDLE 362
Cdd:cd05647 289 AVGGKVR------AKY---GWTDVARFSA-LGIPAVNFGPGDPLLaHKRDEQVPVEQIT 337
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
11-362 |
1.16e-25 |
|
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation.
Pssm-ID: 349888 [Multi-domain] Cd Length: 426 Bit Score: 107.03 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 11 RELVRRPSVTPEDAGCQAL------MAERLERIGFQVERQRYGEVDNF-WARRGHAG--PLLCFAGHTDVVPTGPLDAWT 81
Cdd:cd03893 5 AELVAIPSVSAQPDRREELrraaewLADLLRRLGFTVEIVDTSNGAPVvFAEFPGAPgaPTVLLYGHYDVQPAGDEDGWD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 82 HPPFEAEVKDGLLWGRGAADMKASLAAMIVAceefLAARPDHRGSLA----FLVTSDEEGpAQDGTKKVIEAlEARGEKI 157
Cdd:cd03893 85 SDPFELTERDGRLYGRGAADDKGPILAHLAA----LRALMQQGGDLPvnvkFIIEGEEES-GSPSLDQLVEA-HRDLLAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 158 DWCLVGEPSSRERLGDMLRIGRRGSLSCDLLVHGIQGHV---AYPEKARNPLHQLAPFLQELV----------------- 217
Cdd:cd03893 159 DAIVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLDHDLhsgLYGGVVPDPMTALAQLLASLRdetgrilvpglydavre 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 218 --------------GIEWDAGNASFPPT------SLQLTNLHS---GTGFRNVIPGSAELKFNLRYSTEQTMAGLQERIE 274
Cdd:cd03893 239 lpeeefrldagvleEVEIIGGTTGSVAErlwtrpALTVLGIDGgfpGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 275 ALLQRH---GLDYEVSWRDAGRPFLTRP-GPFLSAVQEVVRDIAGVDPELSTGGGT--SDGRFIAPTGAAVVELGPVNA- 347
Cdd:cd03893 319 AHLEKHapsGAKVTVSYVEGGMPWRSDPsDPAYQAAKDALRTAYGVEPPLTREGGSipFISVLQEFPQAPVLLIGVGDPd 398
|
410
....*....|....*.
gi 1819677128 348 -SIHKIDEHVRVDDLE 362
Cdd:cd03893 399 dNAHSPNESLRLGNYK 414
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
6-376 |
3.09e-25 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 106.01 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 6 VLELARELVRRPSVTPEDAG------CQALMAERLERIGFQVErqrYGEVDNFWARRGHAG---PLLCFAGHTDVVPTGP 76
Cdd:PRK08554 3 VLELLSSLVSFETVNDPSKGikpskeCPKFIKDTLESWGIESE---LIEKDGYYAVYGEIGegkPKLLFMAHFDVVPVNP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 77 lDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFlaARPDHRGSLAFLVTSDEEGPAQDGTkKVIEALEARGEK 156
Cdd:PRK08554 80 -EEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKEL--SKEPLNGKVIFAFTGDEEIGGAMAM-HIAEKLREEGKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 157 IDWCLVGE-----PSSRER--LGDMLRI--------GRRGSLSCDLLVHGIQG-HVAY--PEKARNPLHQLAPFLQE--- 215
Cdd:PRK08554 156 PKYMINADgigmkPIIRRRkgFGVTIRVpsekvkvkGKLREQTFEIRTPVVETrHAAYflPGVDTHPLIAASHFLREsnv 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 216 ----LVGiEWDAGNASfpPTSLQLTNLHSGTG------------FRNVIP---------------------------GSA 252
Cdd:PRK08554 236 lavsLEG-KFLKGNVV--PGEVTLTYLEPGEGeevevdlgltrlLKAIVPlvrapikaekysdygvsitpnvysfaeGKH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 253 ELKFNLR---YSTEQTMAGLQERIEALLQRHGLDYEVSWRdAGRPFLTRPGPFLSAVQEVVRDIaGVDPELSTGGGTSDG 329
Cdd:PRK08554 313 VLKLDIRamsYSKEDIERTLKEVLEFNLPEAEVEIRTNEK-AGYLFTPPDEEIVKVALRVLKEL-GEDAEPVEGPGASDS 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1819677128 330 RFIAPTGAAVVELGPVNASIHKIDEHVRVDDLEPLKDLYLGVMRRLL 376
Cdd:PRK08554 391 RYFTPYGVKAIDFGPKGGNIHGPNEYVEIDSLKKMPEVYKRIALRLL 437
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
59-377 |
2.15e-23 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 99.47 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 59 AGPLLCFAGHTDVVPtgpldAWTHPPFEAEVkdglLWGRGAADMKASLAAMIVAceeflAARPDHRG-SLAFLVTSDEEg 137
Cdd:PRK00466 59 GEGDILLASHVDTVP-----GYIEPKIEGEV----IYGRGAVDAKGPLISMIIA-----AWLLNEKGiKVMVSGLADEE- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 138 paqdGTKKVIEALEARGEKIDWCLVGEPSSrerlGDMLRIGRRGSLSCDLLVHGIQGHVAYPEkaRNPLHQLAPFLQELV 217
Cdd:PRK00466 124 ----STSIGAKELVSKGFNFKHIIVGEPSN----GTDIVVEYRGSIQLDIMCEGTPEHSSSAK--SNLIVDISKKIIEVY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 218 GIEWDAGNASFPPTSLQltnlhSGTGFrNVIPGSAELKFNLRYSteqtMAGLQERIEALLQRHGLDYEVSWRDAGRPflT 297
Cdd:PRK00466 194 KQPENYDKPSIVPTIIR-----AGESY-NVTPAKLYLHFDVRYA----INNKRDDLISEIKDKFQECGLKIVDETPP--V 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 298 RPGPFLSAVQEVVRDI--AGVDPELSTGGGTSDGRFIAPTGAAVVELGPVNASI-HKIDEHVRVDdleplkDLYLGVMRR 374
Cdd:PRK00466 262 KVSINNPVVKALMRALlkQNIKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLeHTNQEKITLD------EIYIAVKTY 335
|
...
gi 1819677128 375 LLA 377
Cdd:PRK00466 336 MLA 338
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
7-360 |
2.32e-23 |
|
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: 100.49 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 7 LELARELVRRPSVTPEDAG---CQALMAERLERIGFQVERQR-------YGEVDNfwarrgHAGPLLCFAGHTDVVPTGP 76
Cdd:cd05681 2 LEDLRDLLKIPSVSAQGRGipeTADFLKEFLRRLGAEVEIFEtdgnpivYAEFNS------GDAKTLLFYNHYDVQPAEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 77 LDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLaarpDHRGSL----AFLVtsdeEGPAQDGTKKVIEALEA 152
Cdd:cd05681 76 LELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALL----QHLGELpvniKFLV----EGEEEVGSPNLEKFVAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 153 RGEKI--DWCLVgEPSSRERLGD-MLRIGRRGSLSCDLLVHGIQG--HVAYPEKARNPLHQLAPFLQELVG--------- 218
Cdd:cd05681 148 HADLLkaDGCIW-EGGGKNPKGRpQISLGVKGIVYVELRVKTADFdlHSSYGAIVENPAWRLVQALNSLRDedgrvlipg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 219 ----IEW---------------------DAGNASF----PPTSLQLTNLH------------SGTGFRNVIPGSAELKFN 257
Cdd:cd05681 227 fyddVRPlseaeralidtydfdpeelrkTYGLKRPlqveGKDPLRALFTEptcningiysgyTGEGSKTILPSEAFAKLD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 258 LRYSTEQTMAGLQERIEALLQRHGL-DYEVSWRDAGRPFLTRPG-PFLSAVQEVVRDIAGVDP--ELSTGGGTSDGRFIA 333
Cdd:cd05681 307 FRLVPDQDPAKILSLLRKHLDKNGFdDIEIHDLLGEKPFRTDPDaPFVQAVIESAKEVYGQDPivLPNSAGTGPMYPFYD 386
|
410 420
....*....|....*....|....*....
gi 1819677128 334 PTGAAVVELGPVNA--SIHKIDEHVRVDD 360
Cdd:cd05681 387 ALEVPVVAIGVGNAgsNAHAPNENIRIAD 415
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
12-361 |
5.67e-22 |
|
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: 96.61 E-value: 5.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 12 ELVRRPSVT--PEDAG----CQALMAERLERIGFQ-VERQRYGEVDNFWARRGHAG--PLLCFAGHTDVVPTGPLDAWTH 82
Cdd:cd05680 6 ELLRIPSVSadPAHKGdvrrAAEWLADKLTEAGFEhTEVLPTGGHPLVYAEWLGAPgaPTVLVYGHYDVQPPDPLELWTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 83 PPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEE-GPAQdgtkkvIEA-LEARGEKI--D 158
Cdd:cd05680 86 PPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEiGSPS------LPAfLEENAERLaaD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 159 WCLVGEPSSRERLGDMLRIGRRGSLSCDLLVHGIQ-----GHvaYPEKARNPLHQLA----------------------- 210
Cdd:cd05680 160 VVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNrdlhsGS--YGGAVPNPANALArllaslhdedgrvaipgfyddvr 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 211 -------------PF----LQELVGIEWDAGNASFPPT-------SLQLTNL---HSGTGFRNVIPGSAELKFNLRYSTE 263
Cdd:cd05680 238 pltdaereawaalPFdeaaFKASLGVPALGGEAGYTTLerlwarpTLDVNGIwggYQGEGSKTVIPSKAHAKISMRLVPG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 264 QTMAGLQERIEALLQRH---GLDYEVSWRDAGRPFLTRPG-PFLSAVQEVVRDIAGVDPELSTGGGT--SDGRFIAPTGA 337
Cdd:cd05680 318 QDPDAIADLLEAHLRAHappGVTLSVKPLHGGRPYLVPTDhPALQAAERALEEAFGKPPVFVREGGSipIVALFEKVLGI 397
|
410 420
....*....|....*....|....*..
gi 1819677128 338 AVVELG---PVNAsIHKIDEHVRVDDL 361
Cdd:cd05680 398 PTVLMGfglPDDA-IHAPNEKFRLECF 423
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
51-178 |
6.54e-22 |
|
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: 92.11 E-value: 6.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 51 NFWARRGH--AGPLLCFAGHTDVVPTGPLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLA 128
Cdd:cd18669 1 NVIARYGGggGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1819677128 129 FLVTSDEEGPAQDGTKKVIEALEARGEKIDWCLVGEPSSRERLGDMLRIG 178
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTP 130
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
5-172 |
2.58e-21 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 94.72 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 5 RVLELARELVRRPSVTP---EDAGCQALMAERLERIGFQVER-QRYGEVDNFWA-RRGHAGP---LLCFAGHTDVVPTGP 76
Cdd:PRK08596 14 ELLELLKTLVRFETPAPparNTNEAQEFIAEFLRKLGFSVDKwDVYPNDPNVVGvKKGTESDaykSLIINGHMDVAEVSA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 77 LDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAF-LVTSDEEGPAqdGTKKVIEaleaRGE 155
Cdd:PRK08596 94 DEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFqSVIGEEVGEA--GTLQCCE----RGY 167
|
170
....*....|....*..
gi 1819677128 156 KIDWCLVGEPSSRERLG 172
Cdd:PRK08596 168 DADFAVVVDTSDLHMQG 184
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
60-373 |
4.82e-21 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349935 [Multi-domain] Cd Length: 379 Bit Score: 93.31 E-value: 4.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 60 GPLLCFAGHTDVVPtgpLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPdhRGSLAFLVTSDEEGPA 139
Cdd:cd08013 68 GKSLMLNGHIDTVT---LDGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGL--RGDVILAAVADEEDAS 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 140 QdGTKKVIEAlearGEKIDWCLVGEPSSRErlgdmLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGI 219
Cdd:cd08013 143 L-GTQEVLAA----GWRADAAIVTEPTNLQ-----IIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALEEY 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 220 EwdagnasfppTSLQLTNLHSGTGFRNV----IPGSAEL-------KFNLRYST------EQTMAGLQERIEALLQRH-G 281
Cdd:cd08013 213 Q----------QELPERPVDPLLGRASVhaslIKGGEEPssyparcTLTIERRTipgetdESVLAELTAILGELAQTVpN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 282 LDYEVSWRDAGRPFLTRP--GPFLSAVQEVVRDIAGVDPELSTGGGTSDGRFIAPTGAAVVELGPVNASIHKIDEHVRVD 359
Cdd:cd08013 283 FSYREPRITLSRPPFEVPkeHPFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGAGLHAKEEWVDVE 362
|
330
....*....|....
gi 1819677128 360 DLEPLKDLYLGVMR 373
Cdd:cd08013 363 SIRQLREVLSAVVR 376
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
6-376 |
8.87e-21 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 92.77 E-value: 8.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 6 VLELARELVRRPSVTPEDAGCQ---ALMAERLERIGFQVERQRYGEV--DNFWAR---RGHAGPLLcfAGHTDVV-PTGP 76
Cdd:PRK06133 39 YLDTLKELVSIESGSGDAEGLKqvaALLAERLKALGAKVERAPTPPSagDMVVATfkgTGKRRIML--IAHMDTVyLPGM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 77 LDAwthPPFEaeVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEgPAQDGTKKVIEALearGEK 156
Cdd:PRK06133 117 LAK---QPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEE-TGSPGSRELIAEL---AAQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 157 IDWCLVGEPSSRErlgDMLRIGRRGSLSCDLLVHGIQGHV-AYPEKARNPLHQLAPFLQELVgiewDAGNASfPPTSLQL 235
Cdd:PRK06133 188 HDVVFSCEPGRAK---DALTLATSGIATALLEVKGKASHAgAAPELGRNALYELAHQLLQLR----DLGDPA-KGTTLNW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 236 TNLHSGTGfRNVIPGSAELKFNLRYS----TEQTMAGLQERIEALLQRhglDYEVSWR-DAGRPFLTR--PGPFLSAV-- 306
Cdd:PRK06133 260 TVAKAGTN-RNVIPASASAQADVRYLdpaeFDRLEADLQEKVKNKLVP---DTEVTLRfERGRPPLEAnaASRALAEHaq 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819677128 307 ---QEVVRDIAGVDPelSTGGGTsDGRFIAPTG-AAVVE-LGPVNASIHKIDEHVRVDDLEPlkDLYLgvMRRLL 376
Cdd:PRK06133 336 giyGELGRRLEPIDM--GTGGGT-DAAFAAGSGkAAVLEgFGLVGFGAHSNDEYIELNSIVP--RLYL--LTRMI 403
|
|
| PRK06915 |
PRK06915 |
peptidase; |
9-361 |
2.42e-20 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 91.68 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 9 LARELVRRPSVTPEDAGCQALMAERLERIGFQV------------------ERQRYGEVDNFWARRGHAG--PLLCFAGH 68
Cdd:PRK06915 22 LLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLdiwepsfkklkdhpyfvsPRTSFSDSPNIVATLKGSGggKSMILNGH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 69 TDVVPTGPLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEE-GPAqdGTKKVI 147
Cdd:PRK06915 102 IDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEEsGGA--GTLAAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 148 EaleaRGEKIDWCLVGEPSSRErlgdmLRIGRRGSLSCDLLVHGIQGH--------------------VAYPEKARN--- 204
Cdd:PRK06915 180 L----RGYKADGAIIPEPTNMK-----FFPKQQGSMWFRLHVKGKAAHggtryegvsaieksmfvidhLRKLEEKRNdri 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 205 --PLHQLAPFlqelvgiewdagnasfpPTSLQLTNLHSGTGFRNViPGSAELKFNLRYSTEQTMAGLQERIEALLQRhgL 282
Cdd:PRK06915 251 tdPLYKGIPI-----------------PIPINIGKIEGGSWPSSV-PDSVILEGRCGIAPNETIEAAKEEFENWIAE--L 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 283 DY----------EVSWrdagrpFLTR--PG------PFLSAVQEVVRDIAGVDPEL-STGGGTSDGRFIAPTGAAVVELG 343
Cdd:PRK06915 311 NDvdewfvehpvEVEW------FGARwvPGeleenhPLMTTLEHNFVEIEGNKPIIeASPWGTDGGLLTQIAGVPTIVFG 384
|
410
....*....|....*....
gi 1819677128 344 P-VNASIHKIDEHVRVDDL 361
Cdd:PRK06915 385 PgETKVAHYPNEYIEVDKM 403
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
51-368 |
3.29e-20 |
|
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: 87.48 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 51 NFWARRG--HAGPLLCFAGHTDVVPTGPLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLA 128
Cdd:cd03873 1 NLIARLGggEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 129 FLVTSDEEGPAQDGTKKVIEALEARGEKIDWCLVGEPSSrerlgdmlrigrrgslscdllvhgiqghvaypekarnplhq 208
Cdd:cd03873 81 VAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDATA----------------------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 209 lAPFLQELVGIEWdagnasfpptslqltnlhsgtgfrnvipgsaelkfnlrysteqtmaglqerieallqrhgldyevsw 288
Cdd:cd03873 120 -GPILQKGVVIRN------------------------------------------------------------------- 131
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 289 rdagrpfltrpgPFLSAVQEVVRDIAGVDPELSTGGGTSDGRFIAPTGAAVVELG-PVNASIHKIDEHVRVDDLEPLKDL 367
Cdd:cd03873 132 ------------PLVDALRKAAREVGGKPQRASVIGGGTDGRLFAELGIPGVTLGpPGDKGAHSPNEFLNLDDLEKATKV 199
|
.
gi 1819677128 368 Y 368
Cdd:cd03873 200 Y 200
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
61-362 |
3.80e-20 |
|
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: 91.55 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 61 PLLcFAGHTDVVPT--GPLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGP 138
Cdd:cd05674 71 PLL-LMAHQDVVPVnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTIILAFGHDEEVG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 139 AQDGTKKVIEALEAR-GEKIDWCLVGEPSSRERLGD------MLRIGRRGSLSCDLLVHGIQGHVAYPEK---------- 201
Cdd:cd05674 150 GERGAGAIAELLLERyGVDGLAAILDEGGAVLEGVFlgvpfaLPGVAEKGYMDVEITVHTPGGHSSVPPKhtgigilsea 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 202 ----ARNP----LHQLAPFLQELVGIewdAGNASFPP----------------------------------TSLQLTNLH 239
Cdd:cd05674 230 vaalEANPfppkLTPGNPYYGMLQCL---AEHSPLPPrslksnlwlaspllkallasellstspltrallrTTQAVDIIN 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 240 SGTGFrNVIPGSAELKFNLRYSTEQTMAGLQERIEALL----QRHGL-----DYEVSWRDAGRPFLTRPGPFLSAVQ--- 307
Cdd:cd05674 307 GGVKI-NALPETATATVNHRIAPGSSVEEVLEHVKNLIadiaVKYGLglsafGGDVIYSTNGTKLLTSLLSPEPSPVsst 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 308 --EVVRDIAG--------------VDPELSTGGgtSDGRF----------IAPTGAAVVELGpvnaSIHKIDEHVRVDDL 361
Cdd:cd05674 386 ssPVWQLLAGtirqvfeqfgedlvVAPGIMTGN--TDTRHywnltkniyrFTPIRLNPEDLG----RIHGVNERISIDDY 459
|
.
gi 1819677128 362 E 362
Cdd:cd05674 460 L 460
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
5-375 |
1.07e-19 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 90.00 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 5 RVLELARELVRRPSV-------TPEDAGCQALMAERL---ERIGFQVERqrygeVDNFWAR--RGHAGPLLCFAGHTDVV 72
Cdd:cd03888 9 EILEDLKELVAIPSVrdeategAPFGEGPRKALDKFLdlaKRLGFKTKN-----IDNYAGYaeYGEGEEVLGILGHLDVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 73 PTGplDAWTHPPFEAEVKDGLLWGRGAADMK----ASLAAM----------------IVACEE----------F------ 116
Cdd:cd03888 84 PAG--EGWTTDPFKPVIKDGKLYGRGTIDDKgptiAALYALkilkdlglplkkkirlIFGTDEetgwkciehyFeheeyp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 117 -LAARPD--------HRGSLAFLVTS--DEEGPAQDGTKKVIEA-------LEARGEKIDWCLVGEPSSRERLGDMLRIG 178
Cdd:cd03888 162 dFGFTPDaefpvingEKGIVTVDLTFkiDDDKGYRLISIKGGEAtnmvpdkAEAVIPGKDKEELALSAATDLKGNIEIDD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 179 RRGslscDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVG-------IEWDA---------------------GNASFPP 230
Cdd:cd03888 242 GGV----ELTVTGKSAHASAPEKGVNAITLLAKFLAELNKdgndkdfIKFLAknlhedyngkklginfedevmGELTLNP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 231 TSLQLTNlhsgtgfrnvipGSAELKFNLRY---STEQTMaglQERIEALLQRHGLDYEVSwrDAGRPFLTRP-GPFLSAV 306
Cdd:cd03888 318 GIITLDD------------GKLELGLNVRYpvgTSAEDI---IKQIEEALEKYGVEVEGH--KHQKPLYVPKdSPLVKTL 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819677128 307 QEVVRDIAGVDPEL-STGGGTSdGRFIaPTGaavVELGP----VNASIHKIDEHVRVDDLEPLKDLYLGVMRRL 375
Cdd:cd03888 381 LKVYEEQTGKEGEPvAIGGGTY-AREL-PNG---VAFGPefpgQKDTMHQANEFIPIDDLIKALAIYAEAIYEL 449
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
7-374 |
1.92e-19 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 88.73 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 7 LELARELVRRPSVT---PE-DAGCQA---LMAERLERIGFQVERQrygEVD------NFWARRGH-AGPLLcFAGHTDVV 72
Cdd:PRK05111 8 IEMYRALIATPSISatdPAlDQSNRAvidLLAGWFEDLGFNVEIQ---PVPgtrgkfNLLASLGSgEGGLL-LAGHTDTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 73 PTGPlDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAA---RPdhrgsLAFLVTSDEEgPAQDGTKKVIEA 149
Cdd:PRK05111 84 PFDE-GRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTklkKP-----LYILATADEE-TSMAGARAFAEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 150 LEARGekiDWCLVGEPSSrerlgdmLRIGR--RGSLSCDLLVHGIQGHVAYPEKARNPL---HQLapfLQELVGI--EWD 222
Cdd:PRK05111 157 TAIRP---DCAIIGEPTS-------LKPVRahKGHMSEAIRITGQSGHSSDPALGVNAIelmHDV---IGELLQLrdELQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 223 AG--NASFP---PTsLQLTNLHSGTGfRNVIPGSAELKFNLR----YSTEQTMAGLQERIEALLQRHGLDYEVSWRDAGR 293
Cdd:PRK05111 224 ERyhNPAFTvpyPT-LNLGHIHGGDA-PNRICGCCELHFDIRplpgMTLEDLRGLLREALAPVSERWPGRITVAPLHPPI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 294 P-FLTRPGpflSAVQEVVRDIAGVDPElSTGGGTsDGRFIAPTGAAVVELGPvnASI---HKIDEHVRVDDLEPLKDLYL 369
Cdd:PRK05111 302 PgYECPAD---HQLVRVVEKLLGHKAE-VVNYCT-EAPFIQQLGCPTLVLGP--GSIeqaHQPDEYLELSFIKPTRELLR 374
|
....*
gi 1819677128 370 GVMRR 374
Cdd:PRK05111 375 QLIHH 379
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
7-371 |
7.66e-18 |
|
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: 83.68 E-value: 7.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 7 LELARELVRRPSVTPEDAGCQALMAERLERIGFQ-VERQRYGEVDNFWARRGhAGPLLCFAGHTDVVPTGPLDAwthppf 85
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGLGdVERDGRGNVVGRLRGTG-GGPALLFSAHLDTVFPGDTPA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 86 EAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGPAQD-GTKKVIEALEARgekIDWCLVGE 164
Cdd:cd03896 74 TVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEGLGDLrGARYLLSAHGAR---LDYFVVAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 165 PSsrerlGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVgiEWDAGNAsfPPTSLQLTNLHSGTGF 244
Cdd:cd03896 151 GT-----DGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALY--EWAAPYV--PKTTFAAIRGGGGTSV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 245 rNVIPGSAELKFNLRYSTEQTMAGLQERIEALLQRHGLDY-----EVSWrdagrpFLTRPGPFLSAVQEVVRDI------ 313
Cdd:cd03896 222 -NRIANLCSMYLDIRSNPDAELADVQREVEAVVSKLAAKHlrvkaRVKP------VGDRPGGEAQGTEPLVNAAvaahre 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1819677128 314 AGVDPELstGGGTSDGRFIAPTGAAVVELG-PVNASIHKIDEHVRVDDLEPLKDLYLGV 371
Cdd:cd03896 295 VGGDPRP--GSSSTDANPANSLGIPAVTYGlGRGGNAHRGDEYVLKDDMLKGAKAYLML 351
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
65-361 |
1.84e-17 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 83.09 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 65 FAGHTDVV--PTGPLDAWTHppfeaeVKDGLLWGRGAADMKASLAAMIVACEEFLAArpDHRGSLAF--LVTSDEE--GP 138
Cdd:PRK07338 97 LTGHMDTVfpADHPFQTLSW------LDDGTLNGPGVADMKGGIVVMLAALLAFERS--PLADKLGYdvLINPDEEigSP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 139 AqdgTKKVIEALeARGEKIdwCLVGEPSSRErlGDMLRiGRRGSLSCDLLVHGIQGHVAY-PEKARNPLHQLAPFLQELV 217
Cdd:PRK07338 169 A---SAPLLAEL-ARGKHA--ALTYEPALPD--GTLAG-ARKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAELALALH 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 218 GIEWDAGNASFPPTSLQltnlhsGTGFRNVIPGSAELKFNLRYSTEQTMAGLQERIEALL----QRHGLDYEVSwRDAGR 293
Cdd:PRK07338 240 ALNGQRDGVTVNVAKID------GGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIaqvnQRHGVSLHLH-GGFGR 312
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1819677128 294 PfltrPGPFLSAVQ---EVVRDIA---GVDPELSTGGGTSDGRFIAPTGAAVVE-LGPVNASIHKIDEHVRVDDL 361
Cdd:PRK07338 313 P----PKPIDAAQQrlfEAVQACGaalGLTIDWKDSGGVCDGNNLAAAGLPVVDtLGVRGGNIHSEDEFVILDSL 383
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
38-372 |
5.47e-17 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 81.40 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 38 GFQVERQRYGE-VDNFWARRGHagPLLCFAGHTDVVPTGPldAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEF 116
Cdd:PRK08737 42 GFQVEVIDHGAgAVSLYAVRGT--PKYLFNVHLDTVPDSP--HWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANAG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 117 LaarpdhrGSLAFLVTSDEEGpaqdGTKKVIEALEARGEKIDWCLVGEPSSRERLgdmlrIGRRGSLSCDLLVHGIQGHV 196
Cdd:PRK08737 118 D-------GDAAFLFSSDEEA----NDPRCVAAFLARGIPYEAVLVAEPTMSEAV-----LAHRGISSVLMRFAGRAGHA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 197 AYPEK-ARNPLHQLAPFLQElvGIEWDAGNASFPPTSLQLTNLHSGT---GFR-NVIPGSAELKFNLRYSTEQTMAGLQE 271
Cdd:PRK08737 182 SGKQDpSASALHQAMRWGGQ--ALDHVESLAHARFGGLTGLRFNIGRvegGIKaNMIAPAAELRFGFRPLPSMDVDGLLA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 272 RIEALLQRHGLDYEVSWRDAGRPfltrPGPFLSA--VQEVVRDIA-GVDPELSTGGG--TSDGRFIApTGAAVVELGPVN 346
Cdd:PRK08737 260 TFAGFAEPAAATFEETFRGPSLP----SGDIARAeeRRLAARDVAdALDLPIGNAVDfwTEASLFSA-AGYTALVYGPGD 334
|
330 340
....*....|....*....|....*..
gi 1819677128 347 -ASIHKIDEHVRVDDLEPLKDLYLGVM 372
Cdd:PRK08737 335 iAQAHTADEFVTLDQLQRYAESVHRII 361
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
6-369 |
8.26e-17 |
|
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: 81.27 E-value: 8.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 6 VLELARELVRRPSV---------TPEDAGCQALMAERLE---RIGFQVErqrygEVDNF--WARRGHAGPLLCFAGHTDV 71
Cdd:TIGR01887 4 ILEDLKELIAIDSVedlekakegAPFGEGPRKALDKFLEiakRDGFTTE-----NVDNYagYIEYGQGEEVLGILGHLDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 72 VPTGplDAWTHPPFEAEVKDGLLWGRGAADMK----ASLAAM----------------IV--------ACEEF------- 116
Cdd:TIGR01887 79 VPAG--DGWTSPPFEPTIKDGRIYGRGTLDDKgptiAAYYAMkilkelglklkkkirfIFgtdeesgwKCIDYyfeheem 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 117 --LAARPD--------HRGSLAFLVT--SDEEGPAQDGTKKVIEAL-----EARG---EKIDWCLVGEPSSRERLGDMLR 176
Cdd:TIGR01887 157 pdIGFTPDaefpiiygEKGITTLEIKfkDDTEGDVVLESFKAGEAYnmvpdHATAvisGKKLTEVEQLKFVFFIAKELEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 177 IGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIEWDAGNASFppTSLQLTNLHSGTGFR----------- 245
Cdd:TIGR01887 237 DFEVNDGTLTITLEGKSAHGSAPEKGINAATYLALFLAQLNLAGGAKAFLQF--LAEYLHEDHYGEKLGikfhddvsgdl 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 246 ----NVIP----GSAELKFNLRYSTEQTMaglQERIEALLQRHGLDYEVSWRDAGRP-FLTRPGPFLSAVQEVVRDIAGV 316
Cdd:TIGR01887 315 tmnvGVIDyenaEAGLIGLNVRYPVGNDP---DTMLKNELAKESGVVEVTLNGYLKPlYVPKDDPLVQTLMKVYEKQTGD 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1819677128 317 D-PELSTGGGTSdGRFiAPTGAAvveLGPV----NASIHKIDEHVRVDDLEPLKDLYL 369
Cdd:TIGR01887 392 EgEPVAIGGGTY-ARL-MPNGVA---FGALfpgeEDTMHQANEYIMIDDLLLATAIYA 444
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
11-361 |
2.73e-16 |
|
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: 79.52 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 11 RELVRRPSVTP--EDAGCQALMAERLERIGFQVER--------QRYG--EVDNFWARR--GHAGPLLCFAGHTDVVPTGp 76
Cdd:cd02697 10 QKLVRVPTDTPpgNNAPHAERTAALLQGFGFEAERhpvpeaevRAYGmeSITNLIVRRryGDGGRTVALNAHGDVVPPG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 77 lDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGPAQDGTKKVieaLEARGEK 156
Cdd:cd02697 89 -DGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGELGPGWL---LRQGLTK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 157 IDWcLVGEPSSRErlgdmLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVgiewdAGNASFPPTSLQLT 236
Cdd:cd02697 165 PDL-LIAAGFSYE-----VVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALY-----ALNAQYRQVSSQVE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 237 NLHS---------GTGFRNVIPGSAELKFNLRYSTEQTMAGLQERIEALLQRH-----GLDYEVSWRDAGRPFLTRPG-- 300
Cdd:cd02697 234 GITHpylnvgrieGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAaasmpGISVDIRRLLLANSMRPLPGna 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819677128 301 PFLSAVQEVVRDIAGvdpELSTGGGT---SDGRFIAPTGAAVVELGP-----VNASIHKIDEHVRVDDL 361
Cdd:cd02697 314 PLVEAIQTHGEAVFG---EPVPAMGTplyTDVRLYAEAGIPGVIYGAgprtvLESHAKRADERLQLEDL 379
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
61-346 |
2.17e-15 |
|
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: 76.75 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 61 PLLCFAGHTDVVPTGPlDAWTHPPFEAEV-KDGLLWGRGAADMKAslaamiVACEEFLAARPDHRGSLAFLVT------S 133
Cdd:TIGR01880 72 PSILLNSHTDVVPVFR-EHWTHPPFSAFKdEDGNIYARGAQDMKC------VGVQYLEAVRNLKASGFKFKRTihisfvP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 134 DEEGPAQDGTKKVIEALEARGEKIDWCL-VGEPSSrerlGDMLRI--GRRGSLSCDLLVHGIQGHVA--YPEKARNPLHQ 208
Cdd:TIGR01880 145 DEEIGGHDGMEKFAKTDEFKALNLGFALdEGLASP----DDVYRVfyAERVPWWVVVTAPGNPGHGSklMENTAMEKLEK 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 209 LAPFLQELVGIEWD-----AGNASFPPTSLQLTNLHSGTGFrNVIPGSAELKFNLRYSTEQTMAGLQERIEALLQR--HG 281
Cdd:TIGR01880 221 SVESIRRFRESQFQllqsnPDLAIGDVTSVNLTKLKGGVQS-NVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADagEG 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819677128 282 LDYEVSwRDAGRPFLT---RPGPFLSAVQEVVRDIA-GVDPELSTggGTSDGRFIAPTGAAVVELGPVN 346
Cdd:TIGR01880 300 VTYEFS-QHSGKPLVTphdDSNPWWVAFKDAVKEMGcTFKPEILP--GSTDSRYIRAAGVPALGFSPMN 365
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
7-326 |
7.80e-15 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 75.55 E-value: 7.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 7 LELARELVRRPSVTP-----ED-AGCQALMAERLERIGFQ-VERQRYGEVDNFWARRGHA--GPLLCFAGHTDVVPTGPL 77
Cdd:PRK08201 17 LEELKEFLRIPSISAlsehkEDvRKAAEWLAGALEKAGLEhVEIMETAGHPIVYADWLHApgKPTVLIYGHYDVQPVDPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 78 DAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAArpdhRGSLAFLVTSDEEGPAQDGTKKVIEALEARGEKI 157
Cdd:PRK08201 97 NLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKV----EGTLPVNVKFCIEGEEEIGSPNLDSFVEEEKDKL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 158 --DWCLVGEPSSRERLGDMLRIGRRGSLSCDLLVHGIQGHV---AYPEKARNPLHQLAPFLQELVGIEWDAGNASF---- 228
Cdd:PRK08201 173 aaDVVLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLhsgLYGGAVPNALHALVQLLASLHDEHGTVAVEGFydgv 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 229 -PPT-------------------SLQLTNLH--------------------------SGTGFRNVIPGSAELKFNLRYST 262
Cdd:PRK08201 253 rPLTpeereefaalgfdeeklkrELGVDELFgeegytalertwarptlelngvyggfQGEGTKTVIPAEAHAKITCRLVP 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1819677128 263 EQTMAGLQERIEALLQRH---GLDYEVSWRDAGRPFLTRPG-PFLSAVQEVVRDIAGVDPELSTGGGT 326
Cdd:PRK08201 333 DQDPQEILDLIEAHLQAHtpaGVRVTIRRFDKGPAFVAPIDhPAIQAAARAYEAVYGTEAAFTRMGGS 400
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
6-136 |
1.81e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 74.12 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 6 VLELARELVRRPSV------TPEDAGCQALMAERLERIGFQVErqrYGEVD----NFWAR-RGH---AGPLLcFAGHTDV 71
Cdd:PRK07906 1 VVDLCSELIRIDTTntgdgtGKGEREAAEYVAEKLAEVGLEPT---YLESApgraNVVARlPGAdpsRPALL-VHGHLDV 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819677128 72 VPTGPLDaWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAA--RPDHRGSLAFLvtSDEE 136
Cdd:PRK07906 77 VPAEAAD-WSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTgrRPPRDLVFAFV--ADEE 140
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
65-375 |
1.69e-13 |
|
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex.
Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 71.22 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 65 FAGHTDVVPTGPLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEfLAARPDHRGSLAFLVTSDEEGPAQdGTK 144
Cdd:cd05677 76 FYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAE-LFQEGELDNDVVFLIEGEEESGSP-GFK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 145 KVIEALEARGEKIDWCLVgepSSRERLGD---MLRIGRRGSLSCDLLV-------H-GIQGHVaypekARNPLHQLAPFL 213
Cdd:cd05677 154 EVLRKNKELIGDIDWILL---SNSYWLDDnipCLNYGLRGVIHATIVVssdkpdlHsGVDGGV-----LREPTADLIKLL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 214 QELVGIEWDAGNASF-----PPT--------------------------------SLQLTNLH-SGTGFRNVIPGSAELK 255
Cdd:cd05677 226 SKLQDPDGRILIPHFydpvkPLTeaerarftaiaetalihedttvdsliakwrkpSLTVHTVKvSGPGNTTVIPKSASAS 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 256 FNLRYSTEQTMAGLQERIEALLQRH--------GLDYEVSwrDAGRPFLTRP-GPFLSAVQEVVRDIAGVDPELSTGGGT 326
Cdd:cd05677 306 VSIRLVPDQDLDVIKQDLTDYIQSCfaelksqnHLDIEVL--NEAEPWLGDPdNPAYQILREAVTAAWGVEPLYIREGGS 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1819677128 327 SDG-RFIAPT-GAAVVEL--GPVNASIHKIDEHVRVDDLEPLKDLYLGVMRRL 375
Cdd:cd05677 384 IPTiRFLEKEfNAPAVQLpcGQSSDNAHLDNERLRIKNLYKMREILSRVFNRL 436
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
11-156 |
2.63e-13 |
|
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: 70.71 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 11 RELVRRPSVT--PEDAG--CQAL--MAERLERIGFQVE-----RQRY--GEVDNF----WARRG--HAGPLLCFAGHTDV 71
Cdd:cd05676 17 REAVAIQSVSadPEKRPelIRMMewAAERLEKLGFKVElvdigTQTLpdGEELPLppvlLGRLGsdPSKKTVLIYGHLDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 72 VPTGPLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEgpaqDGTKKVIEALE 151
Cdd:cd05676 97 QPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEGMEE----SGSEGLDELIE 172
|
....*
gi 1819677128 152 ARGEK 156
Cdd:cd05676 173 ARKDT 177
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
7-136 |
3.73e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 67.41 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 7 LELARELVRRPSVTPE-DAGC---QAL------MAERLERIGFQVerqrYGEVDNFW--ARRGHAGPLLCFAGHTDVVPT 74
Cdd:PRK07205 14 VAAIKTLVSYPSVLNEgENGTpfgQAIqdvleaTLDLCQGLGFKT----YLDPKGYYgyAEIGQGEELLAILCHLDVVPE 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1819677128 75 GPLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEE 136
Cdd:PRK07205 90 GDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGTDEE 151
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
107-324 |
2.99e-11 |
|
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: 64.16 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 107 AAMIVACEEFLAARPDH-RGSLAFLVTSDEEGPAqdGTKKVIEALEARGEKIDWCL---------VGEPSSRErlgdmlr 176
Cdd:cd03886 94 TAMLLGAAKLLAERRDPlKGTVRFIFQPAEEGPG--GAKAMIEEGVLENPGVDAAFglhvwpglpVGTVGVRS------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 177 igrrGSLSC-----DLLVHGIQGHVAYPEKARNPLHQLAPF---LQELVGIEWDagnaSFPPTSLQLTNLHSGTGFrNVI 248
Cdd:cd03886 165 ----GALMAsadefEITVKGKGGHGASPHLGVDPIVAAAQIvlaLQTVVSRELD----PLEPAVVTVGKFHAGTAF-NVI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 249 PGSAELKFNLRYSTEQTMAGLQERIEALLQR----HGLDYEVSWRDAGRPFLTRPGP---FLSAVQEVVRDIAGVDPELS 321
Cdd:cd03886 236 PDTAVLEGTIRTFDPEVREALEARIKRLAEGiaaaYGATVELEYGYGYPAVINDPELtelVREAAKELLGEEAVVEPEPV 315
|
...
gi 1819677128 322 TGG 324
Cdd:cd03886 316 MGS 318
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
7-324 |
3.86e-11 |
|
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1L2 family contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.
Pssm-ID: 349945 [Multi-domain] Cd Length: 366 Bit Score: 63.80 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 7 LELARELVRRPSVTPEDAGCQALMAERLERIGFQVERQRyGEVDNFWA--RRGHAGPLLCFAGHTDVVPTGPLDAWTHPP 84
Cdd:cd08660 2 INIRRDIHEHPELGFEEVETSKKIRRWLEEEQIEILDVP-QLKTGVIAeiKGGEDGPVIAIRADIDALPIQEQTNLPFAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 85 FEAevkdgllwGRGAADMKASLAAMIVACEEFLAARPDH-RGSLAFLVTSDEEGPAqdGTKKVIEALEARGekIDWCLVG 163
Cdd:cd08660 81 KVD--------GT*HACGHDFHTTSIIGTA*LLNQRRAElKGTVVFIFQPAEEGAA--GARKVLEAGVLNG--VSAIFGI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 164 EPSSRERLGDMLRIGRRGSLSCDLL---VHGIQGHVAYPEKARNPLH---QLAPFLQELVGIEWDagnaSFPPTSLQLTN 237
Cdd:cd08660 149 HNKPDLPVGTIGVKEGPL*ASVDVFeivIKGKGGHASIPNNSIDPIAaagQIISGLQSVVSRNIS----SLQNAVVSITR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 238 LHSGTGFrNVIPGSAELKFNLRYSTEQTMAGLQE----RIEALLQRHGLDYEVSWRDAGRPFLTRPGPFLSAVQEVVRDI 313
Cdd:cd08660 225 VQGGTAW-NVIPDQAE*EGTVRAFTKEARQAVPEh*rrVAEGIAAGYGCQAEFKWFPNGPSEVQNDGTLLNAFSKAAARL 303
|
330
....*....|...
gi 1819677128 314 AG--VDPELSTGG 324
Cdd:cd08660 304 GYatVHAEQSPGS 316
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
181-324 |
6.49e-11 |
|
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 63.21 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 181 GSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQELVGIewdaGNASFPPTS---LQLTNLHSGTGFrNVIPGSAELKFN 257
Cdd:COG1473 182 AADSFEITIKGKGGHAAAPHLGIDPIVAAAQIVTALQTI----VSRNVDPLDpavVTVGIIHGGTAP-NVIPDEAELEGT 256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819677128 258 LRYSTEQTMAGLQERIEALLQR----HGLDYEVSWRDAGRPflTRPGPFLSA-VQEVVRDIAG----VDPELSTGG 324
Cdd:COG1473 257 VRTFDPEVRELLEERIERIAEGiaaaYGATAEVEYLRGYPP--TVNDPELTElAREAAREVLGeenvVDAEPSMGS 330
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
5-276 |
7.17e-11 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 63.34 E-value: 7.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 5 RVLELARELVRRPSVTPEDAgcQALMAERLERI-----GFQVERQRYGEVD---------NFWARRGHAGP---LLCFAG 67
Cdd:COG4187 9 QLEELLCELVSIPSVTGTEG--EKEVAEFIYEKlselpYFQENPEHLGLHPlpddplgrkNVTALVKGKGEskkTVILIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 68 HTDVVPT---GPLDAW-THP----------PFEAEVKDGL-----LWGRGAADMKASLA---AMIvacEEFlAARPDHRG 125
Cdd:COG4187 87 HFDVVDVedyGSLKPLaFDPeeltealkeiKLPEDVRKDLesgewLFGRGTMDMKAGLAlhlALL---EEA-SENEEFPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 126 SLAFLVTSDEEGPAQdGTKKVIEALEARGEKIDW----CLVGEPSSRERLGDMLR---IGRRGSLSCDLLVHGIQGHVAY 198
Cdd:COG4187 163 NLLLLAVPDEEVNSA-GMRAAVPLLAELKEKYGLeyklAINSEPSFPKYPGDETRyiyTGSIGKLMPGFYCYGKETHVGE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 199 PEKARNPlHQLAPFLQELvgIEWDA-------GNASFPPTSLQLTNLHSgtgFRNV-IPGSAELKFNlrYST-EQTMAGL 269
Cdd:COG4187 242 PFSGLNA-NLLASELTRE--LELNPdfceevgGEVTPPPVSLKQKDLKE---EYSVqTPHRAVAYFN--VLTlERSPKEI 313
|
....*..
gi 1819677128 270 QERIEAL 276
Cdd:COG4187 314 LEKLKKI 320
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
2-148 |
8.47e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 63.10 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 2 SAGRVLELARELVRRPSV-----TPEDAgcqALMAERLERIGFQVERQR----YGEVDNFWAR---RGHAGPLLcFAGHT 69
Cdd:PRK09133 35 DQQAARDLYKELIEINTTastgsTTPAA---EAMAARLKAAGFADADIEvtgpYPRKGNLVARlrgTDPKKPIL-LLAHM 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819677128 70 DVVPTGPLDaWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEGPAQDGTKKVIE 148
Cdd:PRK09133 111 DVVEAKRED-WTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEGTPMNGVAWLAE 188
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
8-324 |
1.09e-10 |
|
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: 62.36 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 8 ELARELVRRPSVTPEDAGCQALMAERLERIGFQVERqRYGEVDNFWARRGHAGPLLCFAGHTDVvPTGPLDAWTHPPFEA 87
Cdd:TIGR01891 3 DIRRHLHEHPELSFEEFKTSSLIAEALESLGIEVRR-GVGGATGVVATIGGGKPGPVVALRADM-DALPIQEQTDLPYKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 88 EVKdgllwGRGAADMKASLAAMIVACEEFLAARPDH-RGSLAFLVTSDEEGPAqdGTKKVIEALEARGekIDWCLVGEPS 166
Cdd:TIGR01891 81 TNP-----GVMHACGHDLHTAILLGTAKLLKKLADLlEGTVRLIFQPAEEGGG--GATKMIEDGVLDD--VDAILGLHPD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 167 SRERLGDmLRIGRRGSLS----CDLLVHGIQGHVAYPEKARNPL---HQLAPFLQELVGIEWDAgnasFPPTSLQLTNLH 239
Cdd:TIGR01891 152 PSIPAGT-VGLRPGTIMAaadkFEVTIHGKGAHAARPHLGRDALdaaAQLVVALQQIVSRNVDP----SRPAVVSVGIIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 240 SGTGFrNVIPGSAELKFNLRYSTEQTMAGLQERIEALL----QRHGLDYEVSWRDaGRPFLTRPGPFLSAVQEVVRDIAG 315
Cdd:TIGR01891 227 AGGAP-NVIPDKASMSGTVRSLDPEVRDQIIDRIERIVegaaAMYGAKVELNYDR-GLPAVTNDPALTQILKEVARHVVG 304
|
330
....*....|....
gi 1819677128 316 V-----DPELSTGG 324
Cdd:TIGR01891 305 PenvaeDPEVTMGS 318
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
27-108 |
1.19e-10 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 62.55 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 27 QAL--MAERLERIGFQVErqrygEVDNFwarRGHA---------GPLlcfaGHTDVVPTGplDAWTHPPFEAEVKDGLLW 95
Cdd:PRK07318 47 KALekFLEIAERDGFKTK-----NVDNY---AGHIeygegeevlGIL----GHLDVVPAG--DGWDTDPYEPVIKDGKIY 112
|
90
....*....|....
gi 1819677128 96 GRGAADMKA-SLAA 108
Cdd:PRK07318 113 ARGTSDDKGpTMAA 126
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
12-360 |
1.35e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 62.46 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 12 ELVRRPSVTPEDAGCQ---ALMAERLERIGFQVERQR-------YGEVDNfwarrGHAGPLLCFaGHTDVVPTGPLDAWT 81
Cdd:PRK06446 10 EFLKKPSISATGEGIEetaNYLKDTMEKLGIKANIERtkghpvvYGEINV-----GAKKTLLIY-NHYDVQPVDPLSEWK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 82 HPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAarpdhRGSLAFLVTSDEEGPAQDGTKKVIEALEARGEKI--DW 159
Cdd:PRK06446 84 RDPFSATIENGRIYARGASDNKGTLMARLFAIKHLID-----KHKLNVNVKFLYEGEEEIGSPNLEDFIEKNKNKLkaDS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 160 CLVG----EPSSRErlgdMLRIGRRGSLSCDLLVHGIQG--HVAYPEKARNPLHQLAPFLQELVG-------------IE 220
Cdd:PRK06446 159 VIMEgaglDPKGRP----QIVLGVKGLLYVELVLRTGTKdlHSSNAPIVRNPAWDLVKLLSTLVDgegrvlipgfyddVR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 221 W-----------DAGNASFPPTSLQLTNL--------------------------HSGTGFRNVIPGSAELKFNLRYSTE 263
Cdd:PRK06446 235 ElteeerellkkYDIDVEELRKALGFKELkysdrekiaeallteptcnidgfysgYTGKGSKTIVPSRAFAKLDFRLVPN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 264 QTMAGLQERIEALLQRHGLDYEVSWRDAGRPFLTRP-GPFLSAVQEVVRDIAGVDPE-LSTGGGTSD-GRFIAPTG---- 336
Cdd:PRK06446 315 QDPYKIFELLKKHLQKVGFNGEIIVHGFEYPVRTSVnSKVVKAMIESAKRVYGTEPVvIPNSAGTQPmGLFVYKLGirdi 394
|
410 420
....*....|....*....|....
gi 1819677128 337 AAVVELGPVNASIHKIDEHVRVDD 360
Cdd:PRK06446 395 VSAIGVGGYYSNAHAPNENIRIDD 418
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
9-162 |
3.07e-10 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 61.46 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 9 LAR--ELVRRPSVT--PEDAG-CQA---LMAERLERIGFQVERQrygevdnfwARRGH------------AGPLLCFAGH 68
Cdd:PRK09104 20 LERlfALLRIPSIStdPAYAAdCRKaadWLVADLASLGFEASVR---------DTPGHpmvvahhegptgDAPHVLFYGH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 69 TDVVPTGPLDAWTHPPFEAEVKDG-----LLWGRGAADMKASLAAMIVACEEFLAArpdhRGSLAFLVTSDEEGPAQDGT 143
Cdd:PRK09104 91 YDVQPVDPLDLWESPPFEPRIKETpdgrkVIVARGASDDKGQLMTFVEACRAWKAV----TGSLPVRVTILFEGEEESGS 166
|
170 180
....*....|....*....|.
gi 1819677128 144 KKVIEALEARGE--KIDWCLV 162
Cdd:PRK09104 167 PSLVPFLEANAEelKADVALV 187
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
5-112 |
1.35e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 59.53 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 5 RVLELARELVRRPSVTPE-------DAGCQALmAERLERIGFQ-VERQRYG---EVDNFWARRGHAGPLLCFAgHTDVVP 73
Cdd:PRK07907 19 RVRADLEELVRIPSVAADpfrreevARSAEWV-ADLLREAGFDdVRVVSADgapAVIGTRPAPPGAPTVLLYA-HHDVQP 96
|
90 100 110
....*....|....*....|....*....|....*....
gi 1819677128 74 TGPLDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVA 112
Cdd:PRK07907 97 PGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAA 135
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
66-275 |
1.49e-09 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 59.28 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 66 AGHTDVVPT---GPLDAWTHPP-------------FEAEVKDGL-----LWGRGAADMKASLaAMIVACEEFLAARPDHR 124
Cdd:cd05654 77 ISHFDTVGIedyGELKDIAFDPdeltkafseyveeLDEEVREDLlsgewLFGRGTMDMKSGL-AVHLALLEQASEDEDFD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 125 GSLAFLVTSDEEGPAQdGTKKVIEALEARGEKIDW----CLVGEPSSRERLGDMLR---IGRRGSLSCDLLVHGIQGHVA 197
Cdd:cd05654 156 GNLLLMAVPDEEVNSR-GMRAAVPALLELKKKHDLeyklAINSEPIFPQYDGDQTRyiyTGSIGKILPGFLCYGKETHVG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 198 YPEKARNPLHQLAPFLQElvgIEWDA-------GNASFPPTSLQLTNLHSGTgfrNV-IPGSAELKFNLrYSTEQTMAGL 269
Cdd:cd05654 235 EPFAGINANLMASEITAR---LELNAdlcekveGEITPPPVCLKQKDLKESY---SVqTPVRAVAYFNL-FLHKKTAKEL 307
|
....*.
gi 1819677128 270 QERIEA 275
Cdd:cd05654 308 MELLRK 313
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
68-359 |
3.22e-09 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 58.05 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 68 HTDVVPTGPlDAWTHPPFEAEV-KDGLLWGRGAADMK-------ASLAAMIVACEEFLaaRPDHrgsLAFLvtSDEEGPA 139
Cdd:cd05646 72 HTDVVPVFE-EKWTHDPFSAHKdEDGNIYARGAQDMKcvgiqylEAIRRLKASGFKPK--RTIH---LSFV--PDEEIGG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 140 QDGTKKVIEALEARGEKIDWCL---VGEPSSR------ERLGDMLRI---GRRGslscdllvHG---IQGHVAypEKARN 204
Cdd:cd05646 144 HDGMEKFVKTEEFKKLNVGFALdegLASPTEEyrvfygERSPWWVVItapGTPG--------HGsklLENTAG--EKLRK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 205 PLHQLAPFLQElvgiEWD--AGNASFPP---TSLQLTNLHSGTGFrNVIPGSAELKFNLRYSTEQTMAGLQERIEALLQR 279
Cdd:cd05646 214 VIESIMEFRES----QKQrlKSNPNLTLgdvTTVNLTMLKGGVQM-NVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAE 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 280 HGLD--YEVSWRDAGRPF--LTRPGPFLSAVQEVVRDI-AGVDPELSTGGgtSDGRFIAPTGAAVVELGPVNAS---IHK 351
Cdd:cd05646 289 AGRGvtYEFEQKSPEKDPtsLDDSNPWWAAFKKAVKEMgLKLKPEIFPAA--TDSRYIRALGIPALGFSPMNNTpilLHD 366
|
....*...
gi 1819677128 352 IDEHVRVD 359
Cdd:cd05646 367 HNEFLNED 374
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
28-375 |
4.65e-08 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 54.41 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 28 ALMAERLERIGFQVER--QRYGEVDNFWARRGH---AGPLLCFAGHTDVV-PTGPLDAWthpPFEAEvkDGLLWGRGAAD 101
Cdd:PRK07473 38 DLAARDMAIMGATIERipGRQGFGDCVRARFPHprqGEPGILIAGHMDTVhPVGTLEKL---PWRRE--GNKCYGPGILD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 102 MKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEEgPAQDGTKKVIEAlEARGEKidWCLVGEPSsreRLGDMLRIGRRG 181
Cdd:PRK07473 113 MKGGNYLALEAIRQLARAGITTPLPITVLFTPDEE-VGTPSTRDLIEA-EAARNK--YVLVPEPG---RPDNGVVTGRYA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 182 SLSCDLLVHGIQGHV-AYPEKARNPLHQLApflQELVGIEWDAGNasfpPTSLQLTNLHSGTgFRNVIPGSAELKfnlRY 260
Cdd:PRK07473 186 IARFNLEATGRPSHAgATLSEGRSAIREMA---RQILAIDAMTTE----DCTFSVGIVHGGQ-WVNCVATTCTGE---AL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 261 STEQTMAGLQERIEALLQRHGLDYEVSW---RDAGRPfLTRPGPFLSAVQEVVRDIA---GVD-PELSTGGGtSDGRFIA 333
Cdd:PRK07473 255 SMAKRQADLDRGVARMLALSGTEDDVTFtvtRGVTRP-VWEPDAGTMALYEKARAIAgqlGLSlPHGSAGGG-SDGNFTG 332
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1819677128 334 PTGAAVVE-LGPVNASIHKIDEHVRVDDLEPLKDLYLGVMRRL 375
Cdd:PRK07473 333 AMGIPTLDgLGVRGADYHTLNEHIEVDSLAERGRLMAGLLATL 375
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
186-324 |
1.63e-07 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 52.66 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 186 DLLVHGIQGHVAYPEKARNPL---HQLAPFLQELVGIEWDAgnasFPPTSLQLTNLHSGTGFrNVIPGSAELKFNLRYST 262
Cdd:cd08021 185 DITIKGKGGHGSMPHETVDPIviaAQIVTALQTIVSRRVDP----LDPAVVTIGTFQGGTSF-NVIPDTVELKGTVRTFD 259
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819677128 263 EQTMAGLQERIEALL----QRHGLDYEVSWRDaGRPFLTRPgpflSAVQEVVRDIAG--------VDPELSTGG 324
Cdd:cd08021 260 EEVREQVPKRIERIVkgicEAYGASYELEYQP-GYPVVYND----PEVTELVKKAAKevligvenVEPQLMMGG 328
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
189-290 |
2.49e-07 |
|
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: 51.90 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 189 VHGIQGHVAYPEKARNPLHQLAPFLQELVGIEWDAGNasfpPTSLQLTNLHSGTGFRNVIPGSAELKFNLRYSTEQTMAG 268
Cdd:cd08018 174 IKGKQAHGARPHLGINAIEAASAIVNAVNAIHLDPNI----PWSVKMTKLQAGGEATNIIPDKAKFALDLRAQSNEAMEE 249
|
90 100
....*....|....*....|....*.
gi 1819677128 269 LQER----IEALLQRHGLDYEVSWRD 290
Cdd:cd08018 250 LKEKvehaIEAAAALYGASIEITEKG 275
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
28-279 |
7.29e-07 |
|
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: 50.80 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 28 ALMAERLERIGFQVER--QRYGEVDNFwarRGHAGPLLCFAGHTDVVPtgpLDAWTHPPFEAEVKDGLLWGRGAADMKAS 105
Cdd:cd05664 25 AKIAEELRKLGFEVTTgiGGTGVVAVL---RNGEGPTVLLRADMDALP---VEENTGLPYASTVRMKDWDGKEVPVMHAC 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 106 -----LAAMIVACEEFLAARPDHRGSLAFLVTSDEEGPAqdGTKKVIE-ALEARGEKIDWCLvGEPSSRERLGDM-LRIG 178
Cdd:cd05664 99 ghdmhVAALLGAARLLVEAKDAWSGTLIAVFQPAEETGG--GAQAMVDdGLYDKIPKPDVVL-AQHVMPGPAGTVgTRPG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 179 RRGSL--SCDLLVHGIQGHVAYPEKARNPLHQLAPF---LQELVGIEWDAGNASFpptsLQLTNLHSGTGfRNVIPGSAE 253
Cdd:cd05664 176 RFLSAadSLDITIFGRGGHGSMPHLTIDPVVMAASIvtrLQTIVSREVDPQEFAV----VTVGSIQAGSA-ENIIPDEAE 250
|
250 260
....*....|....*....|....*.
gi 1819677128 254 LKFNLRYSTEQTmaglQERIEALLQR 279
Cdd:cd05664 251 LKLNVRTFDPEV----REKVLNAIKR 272
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
181-317 |
9.85e-07 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349916 [Multi-domain] Cd Length: 373 Bit Score: 50.22 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 181 GSLSCDLLVHGIQGHVAYPEKARNPL---HQLAPFLQELVGIEWDAGNASFpptsLQLTNLHSGTGFrNVIPGSAELKFN 257
Cdd:cd05666 171 SADTFEITIRGKGGHAAMPHLGVDPIvaaAQLVQALQTIVSRNVDPLDAAV----VSVTQIHAGDAY-NVIPDTAELRGT 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819677128 258 LRYSTEQTMAGLQERIEALLQR----HGLDYEVSWRDaGRPFLTRPGPFLSAVQEVVRDIAGVD 317
Cdd:cd05666 246 VRAFDPEVRDLIEERIREIADGiaaaYGATAEVDYRR-GYPVTVNDAEETAFAAEVAREVVGAE 308
|
|
| M20_IAA_Hyd |
cd08017 |
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ... |
181-295 |
9.42e-06 |
|
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349938 [Multi-domain] Cd Length: 376 Bit Score: 47.31 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 181 GSLSCDLLVHGIQGHVAYPEKARNPLhqLAP-----FLQELVGIEWDAgnasFPPTSLQLTNLHSGTGFrNVIPGSAELK 255
Cdd:cd08017 167 GAGRFEVVIRGKGGHAAMPHHTVDPV--VAAssavlALQQLVSRETDP----LDSQVVSVTRFNGGHAF-NVIPDSVTFG 239
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1819677128 256 FNLRYSTEQTMAGLQERIEALLQR----HGLDYEVSWRDAGRPF 295
Cdd:cd08017 240 GTLRALTTEGFYRLRQRIEEVIEGqaavHRCNATVDFSEDERPP 283
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
14-336 |
1.74e-05 |
|
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.
Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 46.36 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 14 VRRPSVTPEDAGCQALMAERLERIGFQVERQRYGevdNFWARR----GHAGPLLCfaG-HTDVVPT-----GPL------ 77
Cdd:cd03884 19 VTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVG---NLFGRLegtdPDAPPVLT--GsHLDTVPNggrydGILgvlagl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 78 -------DAWTHPPFEAEVkdgLLWG-----RGAADMKASLAAMIVACEEFLAARPDHRGslaflvtsdeegpaqdgtKK 145
Cdd:cd03884 94 ealralkEAGIRPRRPIEV---VAFTneegsRFPPSMLGSRAFAGTLDLEELLSLRDADG------------------VS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 146 VIEALEARGEKIDwclvgEPSSRERLGDM------------------LRIGrrgslscdlLVHGIQGHVAY--------- 198
Cdd:cd03884 153 LAEALKAIGYDGD-----RPASARRPGDIkayvelhieqgpvleeegLPIG---------VVTGIAGQRWLevtvtgeag 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 199 -----PEKAR-NPLHQLAPFLQELVgiewDAGNASFPPTSLQLTNLHSGTGFRNVIPGSAELKFNLRYSTEQTMAGLQER 272
Cdd:cd03884 219 hagttPMALRrDALLAAAELILAVE----EIALEHGDDLVATVGRIEVKPNAVNVIPGEVEFTLDLRHPDDAVLDAMVER 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819677128 273 IEALL----QRHGLDYEV--SWRDAgrpfltrPGPFLSAVQEVVRDIA---GVDPELSTGGGTSDGRFIA---PTG 336
Cdd:cd03884 295 IRAEAeaiaAERGVEVEVerLWDSP-------PVPFDPELVAALEAAAealGLSYRRMPSGAGHDAMFMAricPTA 363
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
5-373 |
2.54e-05 |
|
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: 45.90 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 5 RVLELARELVRRPSVTPEDAGCQALMAERLERIGFQVERQRYGEVDNF--------WARRGHAGPLLCFAGHTDVVPTGP 76
Cdd:cd05683 4 RLINTFLELVQIDSETLHEKEISKVLKKKFENLGLSVIEDDAGKTTGGgagnlictLKADKEEVPKILFTSHMDTVTPGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 77 LDAwthPPFEAevkDGLLWGRG----AADMKASLAAMIVACEEFLAARPDHrGSLAFLVTSDEEGP---AQDGTKKVIEA 149
Cdd:cd05683 84 NVK---PPQIA---DGYIYSDGttilGADDKAGIAAILEAIRVIKEKNIPH-GQIQFVITVGEESGlvgAKALDPELIDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 150 -----LEARGEkidwclVGEpssrerlgdmLRIGRRGSLSCDLLVHGIQGHVA-YPEKARNPLHQLAPFLQELVGIEWDA 223
Cdd:cd05683 157 dygyaLDSEGD------VGT----------IIVGAPTQDKINAKIYGKTAHAGtSPEKGISAINIAAKAISNMKLGRIDE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 224 gnasfpPTSLQLTNLHSGTGfRNVIPGSAELKFNLRYSTEQTM----AGLQERIEALLQRHGLDYEVSWRDAGRPFLTRP 299
Cdd:cd05683 221 ------ETTANIGKFQGGTA-TNIVTDEVNIEAEARSLDEEKLdaqvKHMKETFETTAKEKGAHAEVEVETSYPGFKINE 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819677128 300 GpflSAVQEVVRDIA---GVDPELSTGGGTSDGRFIAPTGAAVVELGPVNASIHKIDEHVRVDDLEPLKDLYLGVMR 373
Cdd:cd05683 294 D---EEVVKLAKRAAnnlGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAVLVVEIIK 367
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
58-274 |
3.29e-05 |
|
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: 45.53 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 58 HAGPLLCFAG-HTDVVPTGPlDAWTHPPFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARPDHRGSLAFLVTSDEE 136
Cdd:cd08012 75 VDGKTVSFVGsHMDVVTANP-ETWEFDPFSLSIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVVAVFIANEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 137 GPAQDGTKkvIEALEARGeKIDWCLVGEPSSRERLGDMLRIGRRGSLSCDLLVHGIQGHVAYPEKARNPLHQLAPFLQEL 216
Cdd:cd08012 154 NSEIPGVG--VDALVKSG-LLDNLKSGPLYWVDSADSQPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVMEALAEI 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1819677128 217 VGIEWdagnASFPP------------TSLQLTNLHSGTGFRNVIPGSAELKFNLR----YSTEQTMAGLQERIE 274
Cdd:cd08012 231 QKRFY----IDFPPhpkeevygfatpSTMKPTQWSYPGGSINQIPGECTICGDCRltpfYDVKEVREKLEEYVD 300
|
|
| PRK13799 |
PRK13799 |
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional |
238-375 |
6.90e-05 |
|
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional
Pssm-ID: 106740 [Multi-domain] Cd Length: 591 Bit Score: 44.62 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 238 LHSGTGFRNVIPGSAELKFNLRYST----EQTMAGLQERIEALLQRHGLDY--EVSWRDAGRPfltrPGPFLSAVQEVVR 311
Cdd:PRK13799 447 LNVPSGSTNVIPGRCQFSLDIRAATdeirDAAVADILAEIAAIAARRGIEYkaELAMKAAAAP----CAPELMKQLEAAT 522
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1819677128 312 DIAGVDP-ELSTGGGTSDGRFIAPTGAAVVELGPVNASI-HKIDEHVRVDDLEPLKDLYLGVMRRL 375
Cdd:PRK13799 523 DAAGVPLfELASGAGHDAMKIAEIMDQAMLFTRCGNAGIsHNPLESMTADDMELSADAFLDFLNNF 588
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
184-273 |
1.23e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 43.86 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 184 SCDLL---VHGIQGHVAYPEKARNPLHQLAPFLQELVGIeWDAGNASFPPTSLQLTNLHSGTGFrNVIPGSAELKFNLRY 260
Cdd:cd08019 167 SADIFkieVKGKGGHGSMPHQGIDAVLAAASIVMNLQSI-VSREIDPLEPVVVTVGKLNSGTRF-NVIADEAKIEGTLRT 244
|
90
....*....|....*.
gi 1819677128 261 ---STEQTMAGLQERI 273
Cdd:cd08019 245 fnpETREKTPEIIERI 260
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
187-324 |
2.45e-04 |
|
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349919 [Multi-domain] Cd Length: 371 Bit Score: 42.67 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 187 LLVHGIQGHVAYPEKARNP---LHQLAPFLQELVgiewdAGN-ASFPPTSLQLTNLHSGTGFrNVIPGSAELKFNLRYST 262
Cdd:cd05669 177 IEIAGKGAHAAKPENGVDPivaASQIINALQTIV-----SRNiSPLESAVVSVTRIHAGNTW-NVIPDSAELEGTVRTFD 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1819677128 263 EQTMAGLQER----IEALLQRHGLDYEVSWrDAGRPFLTRPGPFLSAVQEVVRDiAG---VDPELSTGG 324
Cdd:cd05669 251 AEVRQLVKERfeqiVEGIAAAFGAKIEFKW-HSGPPAVINDEELTDLASEVAAQ-AGyevVHAEPSLGG 317
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
29-132 |
4.16e-04 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 42.10 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 29 LMAERLERIGFQVERqrygeVDN--------FWARRGHAG--PLLCFAGHTDVVPtGPLDAWTH--PPFEAEVKDGLLWG 96
Cdd:cd05679 36 EMRPRFERLGFTVHI-----HDNpvagrapfLIAERIEDPslPTLLIYGHGDVVP-GYEGRWRDgrDPWTVTVWGERWYG 109
|
90 100 110
....*....|....*....|....*....|....*.
gi 1819677128 97 RGAADMKASLAAMIVACEEFLAARpdhRGSLAFLVT 132
Cdd:cd05679 110 RGTADNKGQHSINMAALRQVLEAR---GGKLGFNVK 142
|
|
| M20_Acy1_IAAspH |
cd05665 |
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, ... |
197-317 |
4.87e-04 |
|
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, bacterial and archaeal aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349915 [Multi-domain] Cd Length: 415 Bit Score: 41.92 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 197 AYPEKARNPLHQLAPFLQELVGIEWDAGNAsfppTSLQLTNLHSGTGfRNVIPGSAELKFNLRYSTEQTMAGLQERIEAL 276
Cdd:cd05665 232 AAPEDGRNALLAAATAALNLHAIPRHGEGA----TRINVGVLGAGEG-RNVIPASAELQVETRGETTAINEYMFEQAQRV 306
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1819677128 277 L----QRHGLDYEVswRDAGRPFLTRPGPFLSA-VQEVVRDIAGVD 317
Cdd:cd05665 307 IkgaaTMYGVTVEI--RTMGEAISAESDPELVAlLREQAARVPGVQ 350
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
3-132 |
6.19e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 41.82 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 3 AGRVLELARELVRRPSVTPEDAGCQAL-------MAERLERIGFQVERqrygeVDNFWARRG-------HAGP----LLC 64
Cdd:PRK07079 16 SGAFFADLARRVAYRTESQNPDRAPALrayltdeIAPALAALGFTCRI-----VDNPVAGGGpfliaerIEDDalptVLI 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 65 FaGHTDVVPtGPLDAWTHP--PFEAEVKDGLLWGRGAADMKASLAAMIVACEEFLAARpdhRGSLAFLVT 132
Cdd:PRK07079 91 Y-GHGDVVR-GYDEQWREGlsPWTLTEEGDRWYGRGTADNKGQHTINLAALEQVLAAR---GGRLGFNVK 155
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
14-75 |
2.62e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 39.75 E-value: 2.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1819677128 14 VRRPSVTPEDAGCQALMAERLERIGFQVERQRYGevdNFWARRG----HAGPLLCfaG-HTDVVPTG 75
Cdd:PRK09290 27 VTRLALSPEDLQARDLFAEWMEAAGLTVRVDAVG---NLFGRLEgrdpDAPAVLT--GsHLDTVPNG 88
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
189-278 |
4.96e-03 |
|
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349920 [Multi-domain] Cd Length: 367 Bit Score: 38.78 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1819677128 189 VHGIQGHVAYPEKARNPLHQLAPFLQELVGIewDAGNASfPPTSLQLT--NLHSGTGfRNVIPGSAELKFNLRYSTEQTM 266
Cdd:cd05670 179 FIGKSGHAAYPHNANDMVVAAANFVTQLQTI--VSRNVD-PIDGAVVTigKIHAGTA-RNVIAGTAHLEGTIRTLTQEMM 254
|
90
....*....|..
gi 1819677128 267 AGLQERIEALLQ 278
Cdd:cd05670 255 ELVKQRVRDIAE 266
|
|
| |
