|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
1-377 |
0e+00 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 738.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 1 MQLPTFLEVYEGLISTSSISSTDPKWDQGNAKVIEKLASWFKDLGFSVEVVEVE--PGKHNMIARMGEGEGGLLLAGHSD 78
Cdd:PRK05111 2 MKLPSFIEMYRALIATPSISATDPALDQSNRAVIDLLAGWFEDLGFNVEIQPVPgtRGKFNLLASLGSGEGGLLLAGHTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 79 TVPFDEGRWNFDPHKLTEKDNRFYGLGTADMKGFFAFIYEAVKKVDWSKQKKPLYVLATCDEETTMLGARHFTANAPFKP 158
Cdd:PRK05111 82 TVPFDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAEATAIRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 159 DYCIIGEPTSLVPIRGHKGHVANAIRVTGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLIKEYHHPGFAIPNPTLNLG 238
Cdd:PRK05111 162 DCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQERYHNPAFTVPYPTLNLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 239 HIHGGDSANRICGCCELHYDVRPLPGISLDGLENMLRGALKEVEAKWPGRIEIVPLHESIPGYECPHDHPFIGGVEELCE 318
Cdd:PRK05111 242 HIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSERWPGRITVAPLHPPIPGYECPADHQLVRVVEKLLG 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 319 TSSQTVNYCTEAPFLQEL-CPTLVLGPGSIDQAHQPDEFLAFDFIDPTIDVLSKAMVKYC 377
Cdd:PRK05111 322 HKAEVVNYCTEAPFIQQLgCPTLVLGPGSIEQAHQPDEYLELSFIKPTRELLRQLIHHFC 381
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
27-373 |
9.59e-169 |
|
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: 475.54 E-value: 9.59e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 27 DQGNAKVIEKLASWFKDLGFSVEVVEV-EPGKHNMIARMG-EGEGGLLLAGHSDTVPFDEGRWNFDPHKLTEKDNRFYGL 104
Cdd:cd03894 14 RNSNLALIEYVADYLAALGVKSRRVPVpEGGKANLLATLGpGGEGGLLLSGHTDVVPVDGQKWSSDPFTLTERDGRLYGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 105 GTADMKGFFAFIYEAVKKVDWSKQKKPLYVLATCDEETTMLGARHFTANA---PFKPDYCIIGEPTSLVPIRGHKGHVAN 181
Cdd:cd03894 94 GTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALaarGGRPDAAIVGEPTSLQPVVAHKGIASY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 182 AIRVTGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLIKEYHHPGFAIPNPTLNLGHIHGGDSANRICGCCELHYDVRP 261
Cdd:cd03894 174 RIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPFDPPYPTLNVGLIHGGNAVNIVPAECEFEFEFRP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 262 LPGISLDGLENMLRGALKEVEAKWPGRIEIVPLHESiPGYECPHDHPFIGGVEELCETS-SQTVNYCTEAPFLQEL-CPT 339
Cdd:cd03894 254 LPGEDPEAIDARLRDYAEALLEFPEAGIEVEPLFEV-PGLETDEDAPLVRLAAALAGDNkVRTVAYGTEAGLFQRAgIPT 332
|
330 340 350
....*....|....*....|....*....|....
gi 503999166 340 LVLGPGSIDQAHQPDEFLAFDFIDPTIDVLSKAM 373
Cdd:cd03894 333 VVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLI 366
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
30-372 |
6.38e-152 |
|
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: 432.71 E-value: 6.38e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 30 NAKVIEKLASWFKDLGFSVEVVEVEPG--KHNMIARMG-EGEGGLLLAGHSDTVPFDEGRWNFDPHKLTEKDNRFYGLGT 106
Cdd:TIGR01892 17 NVDLIDWAQAYLEALGFSVEVQPFPDGaeKSNLVAVIGpSGAGGLALSGHTDVVPYDDAAWTRDPFRLTEKDGRLYGRGT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 107 ADMKGFFAFIYEAVKKVDWSKQKKPLYVLATCDEETTMLGARHFTANAPFKPDYCIIGEPTSLVPIRGHKGHVANAIRVT 186
Cdd:TIGR01892 97 CDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIEAGAGRPRHAIIGEPTRLIPVRAHKGYASAEVTVR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 187 GKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLIKEYHHPGFAIPNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGIS 266
Cdd:TIGR01892 177 GRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDLDEGFTPPYTTLNIGVIQGGKAVNIIPGACEFVFEWRPIPGMD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 267 LDGLENMLRGALKEVEAKWPGRIEIVPLHESIPGYECPHDHPFIGGVEELCETSSQTVNYCTEAPFLQEL-CPTLVLGPG 345
Cdd:TIGR01892 257 PEELLQLLETIAQALVRDEPGFEVQIEVVSTDPGVNTEPDAELVAFLEELSGNAPEVVSYGTEAPQFQELgAEAVVCGPG 336
|
330 340
....*....|....*....|....*..
gi 503999166 346 SIDQAHQPDEFLAFDFIDPTIDVLSKA 372
Cdd:TIGR01892 337 DIRQAHQPDEYVEIEDLVRCRAVLARL 363
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
27-377 |
1.14e-102 |
|
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: 308.35 E-value: 1.14e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 27 DQGNAKVIEKLASWFKDLGFSVEVVEVEPGKHNMIARM--GEGEGGLLLAGHSDTVPFDEG-RWNFDPHKLTEKDNRFYG 103
Cdd:COG0624 28 SGEEAAAAELLAELLEALGFEVERLEVPPGRPNLVARRpgDGGGPTLLLYGHLDVVPPGDLeLWTSDPFEPTIEDGRLYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 104 LGTADMKGFFAFIYEAVKKVDWS--KQKKPLYVLATCDEETTMLGARHFTANAP--FKPDYCIIGEPTS-LVPIRGHKGH 178
Cdd:COG0624 108 RGAADMKGGLAAMLAALRALLAAglRLPGNVTLLFTGDEEVGSPGARALVEELAegLKADAAIVGEPTGvPTIVTGHKGS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 179 VANAIRVTGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLIKeyhHPGFaiPNPTLNLGHIHGGDSANRICGCCELHYD 258
Cdd:COG0624 188 LRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRA---DPLF--GRTTLNVTGIEGGTAVNVIPDEAEAKVD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 259 VRPLPGISLDGLENMLRGALKEVEAkwPGRIEIVPLHESIPGYECPHDHPFIGGVEELC------ETSSQTVNYCTEAPF 332
Cdd:COG0624 263 IRLLPGEDPEEVLAALRALLAAAAP--GVEVEVEVLGDGRPPFETPPDSPLVAAARAAIrevtgkEPVLSGVGGGTDARF 340
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 503999166 333 LQEL--CPTLVLGPGSIDQAHQPDEFLAFDFIDPTIDVLSKAMVKYC 377
Cdd:COG0624 341 FAEAlgIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
30-360 |
3.91e-83 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 258.20 E-value: 3.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 30 NAKVIEKLASWFKDLGFSVEVVEVEPG-KHNMIARMG-EGEGGLLLAGHSDTVPFDEGRWNFDPHKLTEKDNRFYGLGTA 107
Cdd:PRK07522 24 NLALIEWVRDYLAAHGVESELIPDPEGdKANLFATIGpADRGGIVLSGHTDVVPVDGQAWTSDPFRLTERDGRLYGRGTC 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 108 DMKGFFAFIYEAVKKVDWSKQKKPLYVLATCDEETTMLGARHFTA---NAPFKPDYCIIGEPTSLVPIRGHKGHVANAIR 184
Cdd:PRK07522 104 DMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPSMIArlpERGVKPAGCIVGEPTSMRPVVGHKGKAAYRCT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 185 VTGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLIKEYHH-PGFAIPNPTLNLGHIHGGDSANRICGCCELHYDVRPLP 263
Cdd:PRK07522 184 VRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLAAPGPFdALFDPPYSTLQTGTIQGGTALNIVPAECEFDFEFRNLP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 264 GISLDGLENMLRGA-----LKEVEAKWPG-RIEIVPLhESIPGYECPHDHPFIGGVEELCE-TSSQTVNYCTEAPFLQEL 336
Cdd:PRK07522 264 GDDPEAILARIRAYaeaelLPEMRAVHPEaAIEFEPL-SAYPGLDTAEDAAAARLVRALTGdNDLRKVAYGTEAGLFQRA 342
|
330 340
....*....|....*....|....*
gi 503999166 337 -CPTLVLGPGSIDQAHQPDEFLAFD 360
Cdd:PRK07522 343 gIPTVVCGPGSIEQAHKPDEFVELA 367
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
31-369 |
2.00e-73 |
|
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: 232.58 E-value: 2.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 31 AKVIEKLASWFKDLGFSVEVVEVEpGKHNMIARMGEGEG-GLLLAGHSDTVPF-DEGRWNFDPHKLTEKDNRFYGLGTAD 108
Cdd:cd08659 17 AEVAEYLAELLAKRGYGIESTIVE-GRGNLVATVGGGDGpVLLLNGHIDTVPPgDGDKWSFPPFSGRIRDGRLYGRGACD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 109 MKG-----FFAFIyEAVKKVDwsKQKKPLYVLATCDEETTMLGARHFTANAPFK-PDYCIIGEPTSLVPIRGHKGHVANA 182
Cdd:cd08659 96 MKGglaamVAALI-ELKEAGA--LLGGRVALLATVDEEVGSDGARALLEAGYADrLDALIVGEPTGLDVVYAHKGSLWLR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 183 IRVTGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLIkeyHHPGfaIPNPTLNLGHIHGGDSANRICGCCELHYDVRPL 262
Cdd:cd08659 173 VTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELP---AHPL--LGPPTLNVGVINGGTQVNSIPDEATLRVDIRLV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 263 PGISLDGLENMLRGALKEVEAKwpgrIEIVPLHESIPGYECPHDHPFIGGVEELCETSSQ-----TVNYCTEAPFLQEL- 336
Cdd:cd08659 248 PGETNEGVIARLEAILEEHEAK----LTVEVSLDGDPPFFTDPDHPLVQALQAAARALGGdpvvrPFTGTTDASYFAKDl 323
|
330 340 350
....*....|....*....|....*....|....
gi 503999166 337 -CPTLVLGPGSIDQAHQPDEFLAFDFIDPTIDVL 369
Cdd:cd08659 324 gFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIY 357
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
32-373 |
7.14e-65 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 211.39 E-value: 7.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 32 KVIEKLASWFKDLGFSVEVVEVE--------PGKHNMIARMGEGEGGLLLAGHSDTVPFDEGRWNFDPHKLTEKDNRFYG 103
Cdd:PRK08651 30 EIAEFLRDTLEELGFSTEIIEVPneyvkkhdGPRPNLIARRGSGNPHLHFNGHYDVVPPGEGWSVNVPFEPKVKDGKVYG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 104 LGTADMKGFFAFIYEAVKKVDwSKQKKPLYVLATCDEETTMLGARHFTANAPFKPDYCIIGEPTSLVPI-RGHKGHVANA 182
Cdd:PRK08651 110 RGASDMKGGIAALLAAFERLD-PAGDGNIELAIVPDEETGGTGTGYLVEEGKVTPDYVIVGEPSGLDNIcIGHRGLVWGV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 183 IRVTGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLIKEYHHPGFAIPNPTLNLG--HIHGGDSANRICGCCELHYDVR 260
Cdd:PRK08651 189 VKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYEYDDERGAKPTVTLGgpTVEGGTKTNIVPGYCAFSIDRR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 261 PLPGISLDGLENMLRGALKEVEAKWPGRIEIVPLhESIPGYECPHDHPFiggVEELCETSSQTVNY------CTEA---- 330
Cdd:PRK08651 269 LIPEETAEEVRDELEALLDEVAPELGIEVEFEIT-PFSEAFVTDPDSEL---VKALREAIREVLGVepkktiSLGGtdar 344
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 503999166 331 PFLQELCPTLVLGPGSIDQAHQPDEFLAFDFIDPTIDVLSKAM 373
Cdd:PRK08651 345 FFGAKGIPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVL 387
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
72-375 |
5.52e-59 |
|
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: 193.72 E-value: 5.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 72 LLAGHSDTVPfDEGRWNFdPHKLTEkDNRFYGLGTADMKGFFAFIYEAVKKVDWSKQKK-PLYVLATCDEETTMLGARHF 150
Cdd:pfam01546 1 LLRGHMDVVP-DEETWGW-PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLKKgTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 151 TAN---APFKPDYCI---IGEPTSLV------PIRGHKGHVANAIRVTGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDK 218
Cdd:pfam01546 78 IEDgllEREKVDAVFglhIGEPTLLEggiaigVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 219 LIKEYHHPGFAIpnptLNLGHIHGGDsaNRICGCCELHYDVRPLPGISLDGLENMLRGALKEVEAKWPGRIEIVPlHESI 298
Cdd:pfam01546 158 NVDPLDPAVVTV----GNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEY-VEGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 299 PGYECPhDHPFIGGVEELCE--------TSSQTVNYCTEAPF-LQELCPTLV-LGPGSiDQAHQPDEFLAFDFIDPTIDV 368
Cdd:pfam01546 231 APPLVN-DSPLVAALREAAKelfglkveLIVSGSMGGTDAAFfLLGVPPTVVfFGPGS-GLAHSPNEYVDLDDLEKGAKV 308
|
....*..
gi 503999166 369 LSKAMVK 375
Cdd:pfam01546 309 LARLLLK 315
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
32-373 |
1.69e-54 |
|
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: 183.36 E-value: 1.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 32 KVIEKLASWFKDLGFSVEVVEVEPGKHNMIARMGEGEGG--LLLAGHSDTVPFDEGR-WNFDPHKLTEKDNRFYGLGTAD 108
Cdd:cd08011 22 AIAAYIKLLLEDLGYPVELHEPPEEIYGVVSNIVGGRKGkrLLFNGHYDVVPAGDGEgWTVDPYSGKIKDGKLYGRGSSD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 109 MKGFFAFIYEAVKKVDWSKQKKPLYVLAT--CDEETT-MLGARHFTANAPFKPDYCIIGEPTSLVPIR-GHKGHVANAIR 184
Cdd:cd08011 102 MKGGIAASIIAVARLADAKAPWDLPVVLTfvPDEETGgRAGTKYLLEKVRIKPNDVLIGEPSGSDNIRiGEKGLVWVIIE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 185 VTGKSGHSSDPALGVNAIEimyevmfAMMQLRDKLIKEyhhpgfaipNPTLNLGHIHGGDSANRICGCCELHYDVRPLPG 264
Cdd:cd08011 182 ITGKPAHGSLPHRGESAVK-------AAMKLIERLYEL---------EKTVNPGVIKGGVKVNLVPDYCEFSVDIRLPPG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 265 ISLDGLENMLRGALKEVEAKWPGRIeivplhESIPGYECPHDHPFiggVEELCETSSQTVNY---------CTEAPFL-Q 334
Cdd:cd08011 246 ISTDEVLSRIIDHLDSIEEVSFEIK------SFYSPTVSNPDSEI---VKKTEEAITEVLGIrpkevisvgASDARFYrN 316
|
330 340 350
....*....|....*....|....*....|....*....
gi 503999166 335 ELCPTLVLGPGSIDQAHQPDEFLAFDFIDPTIDVLSKAM 373
Cdd:cd08011 317 AGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
35-368 |
4.98e-48 |
|
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: 166.81 E-value: 4.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 35 EKLASWFKDL----GFSVEVVEVEPGK-----HNMIARMGEGEGGLL-LAGHSDTVPF-DEGRWNFDPHKLTEKDNRFYG 103
Cdd:TIGR01910 21 ETIANYIKDLlrefGFSTDVIEITDDRlkvlgKVVVKEPGNGNEKSLiFNGHYDVVPAgDLELWKTDPFKPVEKDGKLYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 104 LGTADMKGFFAFIYEAVKKVDWSKQKKP--LYVLATCDEETTMLGARHFTANAPFK-PDYCIIGEPTSLVPI-RGHKGHV 179
Cdd:TIGR01910 101 RGATDMKGGLVALLYALKAIREAGIKPNgnIILQSVVDEESGEAGTLYLLQRGYFKdADGVLIPEPSGGDNIvIGHKGSI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 180 ANAIRVTGKSGHSSDPALGVNAIEIMYEVMFAMmqlrDKLIKEYH---HPGFAIPNPTLNLGHIHGGDSANRICGCCELH 256
Cdd:TIGR01910 181 WFKLRVKGKQAHASFPQFGVNAIMKLAKLITEL----NELEEHIYarnSYGFIPGPITFNPGVIKGGDWVNSVPDYCEFS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 257 YDVRPLPGISLDGLENMLRGALKEVEAKWPGRIE-IVPLHESIPGYECPhDHPFIG----------GVEELCETSSQTvn 325
Cdd:TIGR01910 257 IDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYEnEPVVKWSGPNETPP-DSRLVKaleaiikkvrGIEPEVLVSTGG-- 333
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 503999166 326 ycTEAPFL-QELCPTLVLGPGSIDQAHQPDEFLAFDFIDPTIDV 368
Cdd:TIGR01910 334 --TDARFLrKAGIPSIVYGPGDLETAHQVNEYISIKNLVESTKV 375
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
31-376 |
1.60e-45 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 160.43 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 31 AKVIEKLaswFKDLGFSVEVVEVEPGKHNMIARMGEGEGGLLLAGHSDTV-PFDEGRWNFDPHKLTEKDNRFYGLGTADM 109
Cdd:PRK08588 25 ANYLQDL---FAKHGIESKIVKVNDGRANLVAEIGSGSPVLALSGHMDVVaAGDVDKWTYDPFELTEKDGKLYGRGATDM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 110 K-GFFAFiyeAVKKVDWSKQKKPLY----VLATCDEETTMLGARHFTANAPFKP-DYCIIGEPTSLVPIRGHKGHVANAI 183
Cdd:PRK08588 102 KsGLAAL---VIAMIELKEQGQLLNgtirLLATAGEEVGELGAKQLTEKGYADDlDALIIGEPSGHGIVYAHKGSMDYKV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 184 RVTGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLIKEYHHPGFAIPNPTLnlghIHGGDSANRICGCCELHYDVRPLP 263
Cdd:PRK08588 179 TSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYFDSIKKHNPYLGGLTHVVTI----INGGEQVNSVPDEAELEFNIRTIP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 264 GISLDGLENMLRGALKEVEAKWPGRIEIVPLHESIPGYECPhDHPFIGGVEELCEtssqtvNYCTEAPFLQELC------ 337
Cdd:PRK08588 255 EYDNDQVISLLQEIINEVNQNGAAQLSLDIYSNHRPVASDK-DSKLVQLAKDVAK------SYVGQDIPLSAIPgatdas 327
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 503999166 338 ---------PTLVLGPGSIDQAHQPDEFLAFDFIDPTIDVLSKAMVKY 376
Cdd:PRK08588 328 sflkkkpdfPVIIFGPGNNLTAHQVDEYVEKDMYLKFIDIYKEIIIQY 375
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
37-360 |
6.82e-38 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 138.95 E-value: 6.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 37 LASWFKDLGFSVEVVEVEP-GKHNMIARMGEGEG-GLLLAGHSDTVPfdegrwNFDPHKLTEKDNRFYGLGTADMKGFFA 114
Cdd:cd05652 25 LAEYLESLGFTVEKQPVENkDRFNVYAYPGSSRQpRVLLTSHIDTVP------PFIPYSISDGGDTIYGRGSVDAKGSVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 115 FIYEAVKKVDWSKQKKP-----LYVLAtcdEETTMLGARHFTANAPFKPDYCIIGEPTSLVPIRGHKGHVANAIRVTGKS 189
Cdd:cd05652 99 AQIIAVEELLAEGEVPEgdlglLFVVG---EETGGDGMKAFNDLGLNTWDAVIFGEPTELKLASGHKGMLGFKLTAKGKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 190 GHSSDPALGVNAIEIMYEVMFAMMQLrdklikeyhhpgfAIP------NPTLNLGHIHGGDSANRICGCCELHYDVR--- 260
Cdd:cd05652 176 GHSGYPWLGISAIEILVEALVKLIDA-------------DLPssellgPTTLNIGRISGGVAANVVPAAAEASVAIRlaa 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 261 PLPGIsLDGLENMLRGALKE---VEAKWPGRIEIVPLHESIPGYEcphdhpfiggveelcetsSQTVNYCTEAPFLQELC 337
Cdd:cd05652 243 GPPEV-KDIVKEAVAGILTDtedIEVTFTSGYGPVDLDCDVDGFE------------------TDVVAYGTDIPYLKGDH 303
|
330 340
....*....|....*....|...
gi 503999166 338 PTLVLGPGSIDQAHQPDEFLAFD 360
Cdd:cd05652 304 KRYLYGPGSILVAHGPDEAITVS 326
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
29-377 |
2.21e-37 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 138.76 E-value: 2.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 29 GNAKVIEKLASWFKDLGFSVEVVEVEPGKHNMIARMgEGEGG---LLLAGHSDTVPFDEgrWNFDPHKLTEKDNRFYGLG 105
Cdd:cd08013 27 GEAEIATYVAAWLAHRGIEAHRIEGTPGRPSVVGVV-RGTGGgksLMLNGHIDTVTLDG--YDGDPLSGEIADGRVYGRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 106 TADMKGFFAFIYEAVKKVDWSKQKKPLYVLATCDEETTMLGARHFTAnAPFKPDYCIIGEPTSLVPIRGHKGHVANAIRV 185
Cdd:cd08013 104 TLDMKGGLAACMAALADAKEAGLRGDVILAAVADEEDASLGTQEVLA-AGWRADAAIVTEPTNLQIIHAHKGFVWFEVDI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 186 TGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLIKEYHHPgfAIPNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGI 265
Cdd:cd08013 183 HGRAAHGSRPDLGVDAILKAGYFLVALEEYQQELPERPVDP--LLGRASVHASLIKGGEEPSSYPARCTLTIERRTIPGE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 266 SLDGLENMLRGALKEVEAKWPG---RIEIVPLHEsiPGYECPHDHPFI-------GGV-EELCETSSQTvnYCTEAPFLQ 334
Cdd:cd08013 261 TDESVLAELTAILGELAQTVPNfsyREPRITLSR--PPFEVPKEHPFVqlvaahaAKVlGEAPQIRSET--FWTDAALLA 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 503999166 335 EL-CPTLVLGPgSIDQAHQPDEFLAFDFIDPTIDVLSKAMVKYC 377
Cdd:cd08013 337 EAgIPSVVFGP-SGAGLHAKEEWVDVESIRQLREVLSAVVREFC 379
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
45-360 |
2.96e-35 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 132.63 E-value: 2.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 45 GFSVEVVEVEPGKHNMIARMGEGEggLLLAGHSDTVPfDEGRWNFDPHKLTEKDNRFYGLGTADMKGFFAFIYEAVKKVD 124
Cdd:PRK08737 42 GFQVEVIDHGAGAVSLYAVRGTPK--YLFNVHLDTVP-DSPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANAGD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 125 wskqkKPLYVLATCDEET-TMLGARHFTANAPfkpDY--CIIGEPTSLVPIRGHKGHVANAIRVTGKSGHSSDP-ALGVN 200
Cdd:PRK08737 119 -----GDAAFLFSSDEEAnDPRCVAAFLARGI---PYeaVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKqDPSAS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 201 AIeimYEVMFAMMQLRDKLIKEYHHPGFAIPNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGISLDGLENMLRG---- 276
Cdd:PRK08737 191 AL---HQAMRWGGQALDHVESLAHARFGGLTGLRFNIGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFAGfaep 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 277 ALKEVEAKWPGrieivplhESIPGYECPH-DHPFIGGVE---ELCETSSQTVNYCTEAP-FLQELCPTLVLGPGSIDQAH 351
Cdd:PRK08737 268 AAATFEETFRG--------PSLPSGDIARaEERRLAARDvadALDLPIGNAVDFWTEASlFSAAGYTALVYGPGDIAQAH 339
|
....*....
gi 503999166 352 QPDEFLAFD 360
Cdd:PRK08737 340 TADEFVTLD 348
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
32-355 |
1.58e-34 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 131.22 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 32 KVIEKLASWFKDLGFsvEVVEVEP-GkhNMIARMGEGEGGLLLAGHSDTVPF-DEGRWNFDPHKLTEKDNRFYGLGTADM 109
Cdd:PRK13004 36 RVVKRIKEEMEKVGF--DKVEIDPmG--NVLGYIGHGKKLIAFDAHIDTVGIgDIKNWDFDPFEGEEDDGRIYGRGTSDQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 110 KGFFA-FIYeAVK--KVDWSKQKKPLYVLATCDEET-TMLGARHFTANAPFKPDYCIIGEPTSLVPIRGHKGHVANAIRV 185
Cdd:PRK13004 112 KGGMAsMVY-AAKiiKDLGLDDEYTLYVTGTVQEEDcDGLCWRYIIEEDKIKPDFVVITEPTDLNIYRGQRGRMEIRVET 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 186 TGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLikeYHHP--GFAipnpTLNLGHIHGGD-SANRICGCCELHYDVRPL 262
Cdd:PRK13004 191 KGVSCHGSAPERGDNAIYKMAPILNELEELNPNL---KEDPflGKG----TLTVSDIFSTSpSRCAVPDSCAISIDRRLT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 263 PGISLDGLENMLR--GALKEVEAK----------WPGriEIVPLHESIPGYECPHDHPF----IGGVEELCETSSQTVNY 326
Cdd:PRK13004 264 VGETWESVLAEIRalPAVKKANAKvsmynydrpsYTG--LVYPTECYFPTWLYPEDHEFvkaaVEAYKGLFGKAPEVDKW 341
|
330 340 350
....*....|....*....|....*....|....*...
gi 503999166 327 --CT-------EAPFlqelcPTLVLGPGSIDQAHQPDE 355
Cdd:PRK13004 342 tfSTngvsiagRAGI-----PTIGFGPGKEPLAHAPNE 374
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
32-355 |
7.41e-33 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 126.38 E-value: 7.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 32 KVIEKLASWFKDLGFsvEVVEVEPgKHNMIARMGEGEGGLLLAGHSDTVPF-DEGRWNFDPHKLTEKDNRFYGLGTADMK 110
Cdd:cd05649 19 GVVERIEEEMEKLGF--DEVEIDP-MGNVIGYIGGGKKKILFDGHIDTVGIgNIDNWKFDPYEGYETDGKIYGRGTSDQK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 111 G-FFAFIYEA--VKKVDWSKQKKPLYVLATCDEET-TMLGARHFTANAPFKPDYCIIGEPTSLVPIRGHKGHVANAIRVT 186
Cdd:cd05649 96 GgLASMVYAAkiMKDLGLRDFAYTILVAGTVQEEDcDGVCWQYISKADKIKPDFVVSGEPTDGNIYRGQRGRMEIRVDTK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 187 GKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLIkeyHHPgfAIPNPTLNLGHIHGGD-SANRICGCCELHYD------- 258
Cdd:cd05649 176 GVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFP---EAP--FLGRGTLTVTDIFSTSpSRCAVPDSCRISIDrrltvge 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 259 --------VRPLPGISLDGLENMLRGALKEvEAKWPGriEIVPLHESIPGYECPHDHPFIGGVEE------LCETSSQTV 324
Cdd:cd05649 251 twegcleeIRALPAVKKYGDDVAVSMYNYD-RPSYTG--EVYESERYFPTWLLPEDHELVKALLEaykalfGARPLIDKW 327
|
330 340 350
....*....|....*....|....*....|...
gi 503999166 325 NYCTEAPFLQ--ELCPTLVLGPGSIDQAHQPDE 355
Cdd:cd05649 328 TFSTNGVSIMgrAGIPCIGFGPGAENQAHAPNE 360
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
28-260 |
2.12e-32 |
|
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.
Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 124.63 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 28 QGNAKVIEKLASWFKDLGFSVEVVEVEPGKHNMIARM-GEGEGGLLLAGHSDTVpFDEGrwNFDPHKLTEKDNRFYGLGT 106
Cdd:cd03885 19 EGVDRVAELLAEELEALGFTVERRPLGEFGDHLIATFkGTGGKRVLLIGHMDTV-FPEG--TLAFRPFTVDGDRAYGPGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 107 ADMKGFFAFIYEAVK--KVDWSKQKKPLYVLATCDEETTMLGARHFTANAPFKPDYCIIGEPT----SLVPIRghKGhVA 180
Cdd:cd03885 96 ADMKGGLVVILHALKalKAAGGRDYLPITVLLNSDEEIGSPGSRELIEEEAKGADYVLVFEPAradgNLVTAR--KG-IG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 181 NA-IRVTGKSGHSS-DPALGVNAIEIMYEVMFAMMQLRDKlikeyhhpgfaIPNPTLNLGHIHGGDSANRICGCCELHYD 258
Cdd:cd03885 173 RFrLTVKGRAAHAGnAPEKGRSAIYELAHQVLALHALTDP-----------EKGTTVNVGVISGGTRVNVVPDHAEAQVD 241
|
..
gi 503999166 259 VR 260
Cdd:cd03885 242 VR 243
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
65-360 |
8.08e-32 |
|
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: 123.96 E-value: 8.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 65 GEGEGG--LLLAGHSDTVPFDEGR-WNFDPHKLTEKDNRFYGLGTADMKGFFA---FIYEAVKKVDWsKQKKPLYVLATC 138
Cdd:cd03895 69 PRGETGrsLILNGHIDVVPEGPVElWTRPPFEATIVDGWMYGRGAGDMKAGLAanlFALDALRAAGL-QPAADVHFQSVV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 139 DEETTMLGA-----RHFTANApfkpdyCIIGEPTSLVPIRGHKGHVANAIRVTGKSGHSSDPALGVNAIEIMYEVMFAMM 213
Cdd:cd03895 148 EEECTGNGAlaalmRGYRADA------ALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 214 QLRDKLIKEYH-HPGFA-IPNP-TLNLGHIHGGDSANRICGCCELHYDVRPLPGISLD----GLENMLRGA------LKE 280
Cdd:cd03895 222 ELEREWNARKKsHPHFSdHPHPiNFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEearrEIEECVADAaatdpwLSN 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 281 --VEAKWPGRieivplheSIPGYECPHDHPFIG----------GVEELCETSSQTvnycTEAPFLQEL--CPTLVLGPGS 346
Cdd:cd03895 302 hpPEVEWNGF--------QAEGYVLEPGSDAEQvlaaahqavfGTPPVQSAMTAT----TDGRFFVLYgdIPALCYGPGS 369
|
330
....*....|....
gi 503999166 347 IDqAHQPDEFLAFD 360
Cdd:cd03895 370 RD-AHGFDESVDLE 382
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
173-286 |
2.72e-29 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 109.36 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 173 RGHKGHVANAIRVTGKSGHSSDPALGVNAIEIMyevmfamMQLRDKLIKEYHHPGFAIPNPTLNLGHIHGGDSANRICGC 252
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLL-------ARLLAELPAEYGDIGFDFPRTTLNITGIEGGTATNVIPAE 73
|
90 100 110
....*....|....*....|....*....|....
gi 503999166 253 CELHYDVRPLPGISLDGLENMLRGALKEVEAKWP 286
Cdd:pfam07687 74 AEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
37-377 |
2.55e-28 |
|
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: 113.35 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 37 LASWFKDLGF-SVEVVevepGKHNMIARM-GEGEG-GLLLAGHSDTVpFDEGrwnfDPHKLTEKDNRFYGLGTADMKGFF 113
Cdd:cd03896 24 VAEWMADLGLgDVERD----GRGNVVGRLrGTGGGpALLFSAHLDTV-FPGD----TPATVRHEGGRIYGPGIGDNKGSL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 114 AFIY---EAVKKVDwSKQKKPLYVLATCDEE--TTMLGARHFTANAPFKPDYCIIGEPTSLVPIRGHKGHVANAIRVTGK 188
Cdd:cd03896 95 ACLLamaRAMKEAG-AALKGDVVFAANVGEEglGDLRGARYLLSAHGARLDYFVVAEGTDGVPHTGAVGSKRFRITTVGP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 189 SGHSSDPALGVNAIEimyevmfAMMQLRDKLiKEYHHPgfAIPNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGISLD 268
Cdd:cd03896 174 GGHSYGAFGSPSAIV-------AMAKLVEAL-YEWAAP--YVPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPDAELA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 269 GLENMLRGALKEVEAKWPGRIEIVPLHESIPGYECPHDHPFIGGVEELCETSSQTVNY---CTEA-PFLQELCPTLVLGP 344
Cdd:cd03896 244 DVQREVEAVVSKLAAKHLRVKARVKPVGDRPGGEAQGTEPLVNAAVAAHREVGGDPRPgssSTDAnPANSLGIPAVTYGL 323
|
330 340 350
....*....|....*....|....*....|...
gi 503999166 345 GSIDQAHQPDEFLAFDFIDPTIDVLSKAMVKYC 377
Cdd:cd03896 324 GRGGNAHRGDEYVLKDDMLKGAKAYLMLAAALC 356
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
43-371 |
4.15e-27 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 109.85 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 43 DLGFSVEVVEVEPGKHNMIarmgEGEGGLLLAGHSDTVPFDEGrwnfdphkLTEKDNRFYGLGTADMKGFFAFIYEAVKK 122
Cdd:PRK08652 34 SLGYDVHIESDGEVINIVV----NSKAELFVEVHYDTVPVRAE--------FFVDGVYVYGTGACDAKGGVAAILLALEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 123 VDWSKQKKPLYVLATCDEETTMLGARHFTANapFKPDYCIIGEPTSL-VPIRgHKGHVANAIRVTGKSGHSSDPALGVNA 201
Cdd:PRK08652 102 LGKEFEDLNVGIAFVSDEEEGGRGSALFAER--YRPKMAIVLEPTDLkVAIA-HYGNLEAYVEVKGKPSHGACPESGVNA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 202 IEIMYEVMFAMMQLRDKLIKEYhhpgfaipNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGISLDGLENMLRGALKEV 281
Cdd:PRK08652 179 IEKAFEMLEKLKELLKALGKYF--------DPHIGIQEIIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 282 EAKwpgrieiVPLHESIPGYECPHDHPFIGGVEELCETSSQTVNYC-----TEA-PFLQELCPTLVLGPGSIDQAHQPDE 355
Cdd:PRK08652 251 TVK-------YEYTEIWDGFELDEDEEIVQLLEKAMKEVGLEPEFTvmrswTDAiNFRYNGTKTVVWGPGELDLCHTKFE 323
|
330
....*....|....*.
gi 503999166 356 FLAFDFIDPTIDVLSK 371
Cdd:PRK08652 324 RIDVREVEKAKEFLKA 339
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
37-285 |
5.49e-27 |
|
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: 109.90 E-value: 5.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 37 LASWFKDLGFSVEVVEVEpGKHNMIARMGEGEGGLLLAGHSDTVPF-DEGRWNFDPHKLTEKDNRFYGLGTADMKG---- 111
Cdd:cd03891 24 IAERLKALGFTCERLEFG-GVKNLWARRGTGGPHLCFAGHTDVVPPgDLEGWSSDPFSPTIKDGMLYGRGAADMKGgiaa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 112 FFAFIYEAVKKvdWSKQKKPLYVLATCDEET-----TMLGARHFTANApFKPDYCIIGEPTS------LVPIrGHKGHVA 180
Cdd:cd03891 103 FVAAAERFVAK--HPNHKGSISFLITSDEEGpaidgTKKVLEWLKARG-EKIDYCIVGEPTSekklgdTIKI-GRRGSLN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 181 NAIRVTGKSGHSSDPALGVNAIEimyevmfAMMQLRDKLIKEYHHPGFAIPNPT-LNLGHIHGGDSA-NRICGCCELHYD 258
Cdd:cd03891 179 GKLTIKGKQGHVAYPHLADNPIH-------LLAPILAELTATVLDEGNEFFPPSsLQITNIDVGNGAtNVIPGELKAKFN 251
|
250 260
....*....|....*....|....*..
gi 503999166 259 VRPLPGISLDGLENMLRGALKEVEAKW 285
Cdd:cd03891 252 IRFNDEHTGESLKARIEAILDKHGLDY 278
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
29-308 |
8.47e-27 |
|
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: 110.53 E-value: 8.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 29 GNAKVIEKLASWFKDLGFSVEVVEVE--PGKHNMIARMGEG---EGGLLLAGHSDTVPFDEGRWNFDPHKLTEKDNRFYG 103
Cdd:cd05675 21 SETRAAEVLAARLAEAGIQTEIFVVEshPGRANLVARIGGTdpsAGPLLLLGHIDVVPADASDWSVDPFSGEIKDGYVYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 104 LGTADMKGFFAFIYEAVKKVDWS--KQKKPLYVLATCDEET-TMLGARHFTANAP--FKP-DYCI---------IGEPTS 168
Cdd:cd05675 101 RGAVDMKNMAAMMLAVLRHYKREgfKPKRDLVFAFVADEEAgGENGAKWLVDNHPelFDGaTFALneggggslpVGKGRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 169 LVPIR-GHKGHVANAIRVTGKSGHSSDP-----------AL--------------------------GVNAIEIMYEVMF 210
Cdd:cd05675 181 LYPIQvAEKGIAWMKLTVRGRAGHGSRPtddnaitrlaeALrrlgahnfpvrltdetayfaqmaelaGGEGGALMLTAVP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 211 AMMQLRDKLI---KEYHhpgfAIPNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGISLDGLENMLRGALK--EVEAKW 285
Cdd:cd05675 261 VLDPALAKLGpsaPLLN----AMLRNTASPTMLDAGYATNVLPGRATAEVDCRILPGQSEEEVLDTLDKLLGdpDVSVEA 336
|
330 340
....*....|....*....|...
gi 503999166 286 pgrieivpLHeSIPGYECPHDHP 308
Cdd:cd05675 337 --------VH-LEPATESPLDSP 350
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
31-372 |
3.96e-26 |
|
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: 107.05 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 31 AKVIEKLASWFKDLGFSVEVVEVEpgkhNMIARMGEGEGGLLLAGHSDTVPfdegrwNFDPHKLteKDNRFYGLGTADMK 110
Cdd:cd05653 21 ARAAKFLEEIMKELGLEAWVDEAG----NAVGGAGSGPPDVLLLGHIDTVP------GEIPVRV--EGGVLYGRGAVDAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 111 G-FFAFIYEAVKKVdwSKQKKPLYVLATCDEETTMLGARHFTANAPfKPDYCIIGEPTSLVPIR-GHKGHVANAIRVTGK 188
Cdd:cd05653 89 GpLAAMILAASALN--EELGARVVVAGLVDEEGSSKGARELVRRGP-RPDYIIIGEPSGWDGITlGYRGSLLVKIRCEGR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 189 SGHSSDPalGVNAIEIMYEVMFAMmqlrDKLIKEYHHPGFAIPN--PTLnlghIHGGDSANRICGCCELHYDVRPLPGIS 266
Cdd:cd05653 166 SGHSSSP--ERNAAEDLIKKWLEV----KKWAEGYNVGGRDFDSvvPTL----IKGGESSNGLPQRAEATIDLRLPPRLS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 267 LDGLENMLRGALKEVEAKWPGRIEIVPLHESIP------------GYEcphdhPFIggveeLCETSSQTVNycTEAPFLQ 334
Cdd:cd05653 236 PEEAIALATALLPTCELEFIDDTEPVKVSKNNPlarafrrairkqGGK-----PRL-----KRKTGTSDMN--VLAPLWT 303
|
330 340 350
....*....|....*....|....*....|....*...
gi 503999166 335 elCPTLVLGPGSIDQAHQPDEFLAFDFIDPTIDVLSKA 372
Cdd:cd05653 304 --VPIVAYGPGDSTLDHTPNEHIELAEIERAAAVLKGA 339
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
37-368 |
4.81e-25 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 103.93 E-value: 4.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 37 LASWFKDLGFSVEVVevepgKHNMIARMG---EGEGGLLLAGHSDTVPFDEGrWNFDPHKLTEKDNRFYGLGTADMKG-- 111
Cdd:cd05651 26 IENYLEQKGIPFKRK-----GNNVWAENGhfdEGKPTLLLNSHHDTVKPNAG-WTKDPFEPVEKGGKLYGLGSNDAGAsv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 112 ---FFAFIYEAVKkvdwSKQKKPLYVLATCDEETTmlGARHFTANAPFKP--DYCIIGEPTSLVPIRGHKGHVANAIRVT 186
Cdd:cd05651 100 vslLATFLHLYSE----GPLNYNLIYAASAEEEIS--GKNGIESLLPHLPplDLAIVGEPTEMQPAIAEKGLLVLDCTAR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 187 GKSGHSSDPAlGVNAIeimYEVMFAMMQLRD-KLIKEYHHPGfaipNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGI 265
Cdd:cd05651 174 GKAGHAARNE-GDNAI---YKALDDIQWLRDfRFDKVSPLLG----PVKMTVTQINAGTQHNVVPDSCTFVVDIRTTEAY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 266 SLDGLENMLRGALKEveakwpgriEIVPLHESIPGYECPHDHPFI-GGVEELCET-SSQTVNYCTEAPFlqelcPTLVLG 343
Cdd:cd05651 246 TNEEIFEIIRGNLKS---------EIKPRSFRLNSSAIPPDHPIVqAAIAAGRTPfGSPTLSDQALMPF-----PSVKIG 311
|
330 340
....*....|....*....|....*
gi 503999166 344 PGSIDQAHQPDEFLAFDFIDPTIDV 368
Cdd:cd05651 312 PGDSSRSHTADEFIELSEIEEGIDI 336
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
31-372 |
3.68e-24 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 101.57 E-value: 3.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 31 AKVIEKLASWFKDLGFSVEVVEVEpgkhNMIARMGEGEGGLLLAGHSDTVPFDEgrwnfdPHKLteKDNRFYGLGTADMK 110
Cdd:PRK04443 26 AAAAEFLVEFMESHGREAWVDEAG----NARGPAGDGPPLVLLLGHIDTVPGDI------PVRV--EDGVLWGRGSVDAK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 111 G-FFAFIYEAVKKVDWSKQKkpLYVLATCDEETTMLGARHFTANApFKPDYCIIGEPTSLVPIR-GHKGHVANAIRVTGK 188
Cdd:PRK04443 94 GpLAAFAAAAARLEALVRAR--VSFVGAVEEEAPSSGGARLVADR-ERPDAVIIGEPSGWDGITlGYKGRLLVTYVATSE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 189 SGHSSDPalGVNAIEIMYEVMFAmmqlrdklIKEY------HHPGFAIPNPTLNLGHIHGGDSANRicgcCELHYDVRPL 262
Cdd:PRK04443 171 SFHSAGP--EPNAAEDAIEWWLA--------VEAWfeandgRERVFDQVTPKLVDFDSSSDGLTVE----AEMTVGLRLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 263 PGISLDGLENMLRGALKEVEAKWPGRieivplhesIPGYECPHDHP----FIGGVEE-------LCETSSQTVNYCteAP 331
Cdd:PRK04443 237 PGLSPEEAREILDALLPTGTVTFTGA---------VPAYMVSKRTPlaraFRVAIREaggtprlKRKTGTSDMNVV--AP 305
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 503999166 332 FLQelCPTLVLGPGSIDQAHQPDEFLAFDFIDPTIDVLSKA 372
Cdd:PRK04443 306 AWG--CPMVAYGPGDSDLDHTPDEHLPLAEYLRAIAVLTDV 344
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
31-357 |
2.85e-23 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 99.35 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 31 AKVIEKLASWFKDLGFSVEVVEVepgkHNMIAR----MGEGEGGLLLAGHSDTVPFDEGrwnfDPHKLTEKDNRFYGLGT 106
Cdd:COG2195 23 EALADYLVEELKELGLEVEEDEA----GNVIATlpatPGYNVPTIGLQAHMDTVPQFPG----DGIKPQIDGGLITADGT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 107 ----ADMKGFFAFIYEAVKkVDWSKQKK--PLYVLATCDEETTMLGARHFTANApFKPDYCII---GEPTSLVpirghkg 177
Cdd:COG2195 95 ttlgADDKAGVAAILAALE-YLKEPEIPhgPIEVLFTPDEEIGLRGAKALDVSK-LGADFAYTldgGEEGELE------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 178 hVANA------IRVTGKSGHSSD-PALGVNAIEIMYEVMFAMMQLRdklIKEYHhpgfaipnpTLNLGHIHGGDSANRIC 250
Cdd:COG2195 166 -YECAgaadakITIKGKGGHSGDaKEKMINAIKLAARFLAALPLGR---IPEET---------EGNEGFIHGGSATNAIP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 251 GCCELHYDVRPLpgiSLDGLE---NMLRGALKEVEAKWP-GRIEIVpLHESIPGYECPHDHPFIGGVEELCETSSQTVNY 326
Cdd:COG2195 233 REAEAVYIIRDH---DREKLEarkAELEEAFEEENAKYGvGVVEVE-IEDQYPNWKPEPDSPIVDLAKEAYEELGIEPKI 308
|
330 340 350
....*....|....*....|....*....|....*...
gi 503999166 327 C-----TEAPFLQE--LcPTLVLGPGsIDQAHQPDEFL 357
Cdd:COG2195 309 KpirggLDGGILSFkgL-PTPNLGPG-GHNFHSPDERV 344
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
34-271 |
6.66e-23 |
|
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: 98.64 E-value: 6.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 34 IEKLASWFKDLGFSVEVVEVEPGKhNMIARMGEGEGGLLLAGHSDTVPF-DEGRWNFDPHKLTEKDNRFYGLGTADMKGF 112
Cdd:TIGR01246 22 QDIIAERLEKLGFEIEWMHFGDTK-NLWATRGTGEPVLAFAGHTDVVPAgPEEQWSSPPFEPVERDGKLYGRGAADMKGS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 113 FAFIYEAVKK--VDWSKQKKPLYVLATCDEETTML-GARH---FTANAPFKPDYCIIGEPTSLVPI-----RGHKGHVAN 181
Cdd:TIGR01246 101 LAAFIVAAERfvKKNPDHKGSISLLITSDEEGTAIdGTKKvveTLMARDELIDYCIVGEPSSVKKLgdvikNGRRGSITG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 182 AIRVTGKSGHSSDPALGVNAIEIMYEVMfammqlrDKLIKEYHHPGFA-IPNPTLNLGHIHGG-DSANRICGCCELHYDV 259
Cdd:TIGR01246 181 NLTIKGIQGHVAYPHLANNPIHKAAPAL-------AELTAIKWDEGNEfFPPTSLQITNIHAGtGANNVIPGELYVQFNL 253
|
250
....*....|..
gi 503999166 260 RPLPGISLDGLE 271
Cdd:TIGR01246 254 RFSTEVSDEILK 265
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
65-268 |
2.68e-22 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 97.38 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 65 GEGEGG--LLLAGHSDTVPfdEG---RWNFDPHKLTEKDNRFYGLGTADMKGFFA---FIYEAVKKVDWsKQKKPLYVLA 136
Cdd:PRK06837 92 PAGKTGrsLILQGHIDVVP--EGpldLWSRPPFDPVIVDGWMYGRGAADMKAGLAamlFALDALRAAGL-APAARVHFQS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 137 TCDEETTMLGA-----RHFTANApfkpdyCIIGEPTSLVPIRGHKGHVANAIRVTGKSGHSSDPALGVNAIEIMYEVMFA 211
Cdd:PRK06837 169 VIEEESTGNGAlstlqRGYRADA------CLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQA 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 212 MMQLRDKLIKEYH-HPGFA-IPNP-TLNLGHIHGGDSANRICGCCELHYDVRPLPGISLD 268
Cdd:PRK06837 243 LRELEAEWNARKAsDPHFEdVPHPiNFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAA 302
|
|
| PRK06915 |
PRK06915 |
peptidase; |
31-377 |
4.78e-22 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 96.68 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 31 AKVIEKLaswfKDLGFSVEVVEVEpGKH------------------NMIARM-GEGEG-GLLLAGHSDTVPF-DEGRWNF 89
Cdd:PRK06915 41 AIVIEKL----RELGLDLDIWEPS-FKKlkdhpyfvsprtsfsdspNIVATLkGSGGGkSMILNGHIDVVPEgDVNQWDH 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 90 DPHKLTEKDNRFYGLGTADMKG-----FFAFiyEAVKKVDWSkQKKPLYVLATCDEETTMLGA-----RHFTANApfkpd 159
Cdd:PRK06915 116 HPYSGEVIGGRIYGRGTTDMKGgnvalLLAM--EALIESGIE-LKGDVIFQSVIEEESGGAGTlaailRGYKADG----- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 160 yCIIGEPTSLVPIRGHKGHVANAIRVTGKSGHSSDPALGVNAIEIMYEVMFAMMQL---RDKLIKEYHHPGFAIPNPtLN 236
Cdd:PRK06915 188 -AIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLeekRNDRITDPLYKGIPIPIP-IN 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 237 LGHIHGGD----SANRI-----CGCCelhydvrplPGISLDGLENMLRGALKEVEAK--W----PGRIEIVPLHeSIPGy 301
Cdd:PRK06915 266 IGKIEGGSwpssVPDSVilegrCGIA---------PNETIEAAKEEFENWIAELNDVdeWfvehPVEVEWFGAR-WVPG- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 302 ECPHDHPFIG----------GVEELCETSSqtvnYCTEAPFLQEL--CPTLVLGPGSIDQAHQPDEFLAFDFIDPTIDVL 369
Cdd:PRK06915 335 ELEENHPLMTtlehnfveieGNKPIIEASP----WGTDGGLLTQIagVPTIVFGPGETKVAHYPNEYIEVDKMIAAAKII 410
|
....*...
gi 503999166 370 SKAMVKYC 377
Cdd:PRK06915 411 ALTLLDWC 418
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
29-249 |
5.10e-20 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 90.85 E-value: 5.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 29 GNAKVIEKLASWFKDLGFSVEVVEVEPGKHNMI-ARM-GEGEGGLLLAGHSDTVpFDEGRWNFDPHKltEKDNRFYGLGT 106
Cdd:PRK06133 58 GLKQVAALLAERLKALGAKVERAPTPPSAGDMVvATFkGTGKRRIMLIAHMDTV-YLPGMLAKQPFR--IDGDRAYGPGI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 107 ADMKGFFAFIYEAV---KKVDWsKQKKPLYVLATCDEETTMLGARHFTANAPFKPDYCIIGEPT----SLVpiRGHKGHV 179
Cdd:PRK06133 135 ADDKGGVAVILHALkilQQLGF-KDYGTLTVLFNPDEETGSPGSRELIAELAAQHDVVFSCEPGrakdALT--LATSGIA 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503999166 180 ANAIRVTGKSGHS-SDPALGVNAIeimYEVMFAMMQLRDKlikeyhhpGFAIPNPTLNLGHIHGGDSANRI 249
Cdd:PRK06133 212 TALLEVKGKASHAgAAPELGRNAL---YELAHQLLQLRDL--------GDPAKGTTLNWTVAKAGTNRNVI 271
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
35-356 |
1.02e-19 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 89.52 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 35 EKLASWFKDLGF-SVEVVEVE----PGKH--NMIARM--GEGEGGLLLAGHSDTVPF-DEGRWNFDPHKLTEKDNRFYGL 104
Cdd:PRK13983 34 EYLESLLKEYGFdEVERYDAPdprvIEGVrpNIVAKIpgGDGKRTLWIISHMDVVPPgDLSLWETDPFKPVVKDGKIYGR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 105 GTAD-MKGFFAFIYeAVKKVdWSKQKKPLYVLATC---DEET-TMLGARHFTANAP--FKPDYCII----GEPT-SLVPI 172
Cdd:PRK13983 114 GSEDnGQGIVSSLL-ALKAL-MDLGIRPKYNLGLAfvsDEETgSKYGIQYLLKKHPelFKKDDLILvpdaGNPDgSFIEI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 173 rGHKGHVANAIRVTGKSGHSSDPALGVNAIEIMYevMFAMMqLRDKLIKEYH--HPGFAIPN----PTlnlghIHGG--D 244
Cdd:PRK13983 192 -AEKSILWLKFTVKGKQCHASTPENGINAHRAAA--DFALE-LDEALHEKFNakDPLFDPPYstfePT-----KKEAnvD 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 245 SANRICGCCELHYDVRPLPGISLDGLENMLRGALKEVEAKWPGRIEIVPLHESIPGYECPHDHPFiggVEELC----ETS 320
Cdd:PRK13983 263 NINTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIADEFEEEYGVKIEVEIVQREQAPPPTPPDSEI---VKKLKraikEVR 339
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 503999166 321 SQTVNYC-----TEAPFLQEL-CPTLVLGPGsIDQAHQPDEF 356
Cdd:PRK13983 340 GIEPKVGgigggTVAAFLRKKgYPAVVWSTL-DETAHQPNEY 380
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
37-355 |
2.13e-19 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 88.94 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 37 LASWFKDLGFSVEVVEVEPGKHNMIARMgEGEG-----GLLLAGHSDTVPFDEGR-WNFDPHKLTEKDNRFYGLGTADMK 110
Cdd:PRK08596 42 IAEFLRKLGFSVDKWDVYPNDPNVVGVK-KGTEsdaykSLIINGHMDVAEVSADEaWETNPFEPTIKDGWLYGRGAADMK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 111 GFFAFIYEAVKKVDWSKQKKP--LYVLATCDEETTMLGARHFTANAPfKPDYCIIGEpTSLVPIRGHKGHVANAIRVTGK 188
Cdd:PRK08596 121 GGLAGALFAIQLLHEAGIELPgdLIFQSVIGEEVGEAGTLQCCERGY-DADFAVVVD-TSDLHMQGQGGVITGWITVKSP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 189 SG----------HSSDPALGVNAIEIMYEVMFAMMQL-RD-KLIKEYhhPGFAIPNPTLNLGHIHGGDSANRICGCCELH 256
Cdd:PRK08596 199 QTfhdgtrrqmiHAGGGLFGASAIEKMMKIIQSLQELeRHwAVMKSY--PGFPPGTNTINPAVIEGGRHAAFIADECRLW 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 257 YDVRPLPGISLDGL-----ENMLRGA-----LKE--VEAKWPGRIEIVPLHESIPGYECPHDHPfigGVEELCETS---- 320
Cdd:PRK08596 277 ITVHFYPNETYEQVikeieEYIGKVAaadpwLREnpPQFKWGGESMIEDRGEIFPSLEIDSEHP---AVKTLSSAHesvl 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 503999166 321 --------SQTVnycTEAPFLQEL-CPTLVLGPGSIDQAHQPDE 355
Cdd:PRK08596 354 sknaildmSTTV---TDGGWFAEFgIPAVIYGPGTLEEAHSVNE 394
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
37-202 |
5.05e-19 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 87.45 E-value: 5.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 37 LASWFKDLGFSVEVVEVEPGKhNMIARMGEGEGGLLLAGHSDTVPF-DEGRWNFDPHKLTEKDNRFYGLGTADMKGFFA- 114
Cdd:PRK13009 28 LAERLEALGFTCERMDFGDVK-NLWARRGTEGPHLCFAGHTDVVPPgDLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 115 FIYeAVKKVdwsKQKKP-----LYVLATCDEE------TT----MLGARHftanapFKPDYCIIGEPTS------LVPIr 173
Cdd:PRK13009 107 FVV-AAERF---VAAHPdhkgsIAFLITSDEEgpaingTVkvleWLKARG------EKIDYCIVGEPTSterlgdVIKN- 175
|
170 180
....*....|....*....|....*....
gi 503999166 174 GHKGHVANAIRVTGKSGHSSDPALGVNAI 202
Cdd:PRK13009 176 GRRGSLTGKLTVKGVQGHVAYPHLADNPI 204
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
35-360 |
4.14e-18 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 85.20 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 35 EKLASWFKDLGFSVEVVEVE--PG------KHNMIARM-GEGEGGLL-LAGHSDTVPFDEGrWNFDPHKLTEKDNRFYGL 104
Cdd:PRK13013 41 EFLAARLAPRGFEVELIRAEgaPGdsetypRWNLVARRqGARDGDCVhFNSHHDVVEVGHG-WTRDPFGGEVKDGRIYGR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 105 GTADMK-GFFAFIY--EAVKKV--DWSKQkkpLYVLATCDEETTMLGARHFTAN----APFKPDYCIIGEPTSLVPI-RG 174
Cdd:PRK13013 120 GACDMKgGLAASIIaaEAFLAVypDFAGS---IEISGTADEESGGFGGVAYLAEqgrfSPDRVQHVIIPEPLNKDRIcLG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 175 HKGHVANAIRVTGKSGHSSDPALGVNAIEIMYEVMFAMmqlRDKLIKEYHHPGFAIP-------NPTLNLGHIHGGDS-- 245
Cdd:PRK13013 197 HRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEI---EERLFPLLATRRTAMPvvpegarQSTLNINSIHGGEPeq 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 246 --------ANRICGCCELHYDVRPLPGISLDGLENMLRGALKEVEAKWPG-RIEIVPLHESIPGYeCPHDHPFIGGVEEL 316
Cdd:PRK13013 274 dpdytglpAPCVADRCRIVIDRRFLIEEDLDEVKAEITALLERLKRARPGfAYEIRDLFEVLPTM-TDRDAPVVRSVAAA 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 503999166 317 CET--SSQTVNYCTEAPFLQE-------LCPTLVLGPGSIDQAHQPDEFLAFD 360
Cdd:PRK13013 353 IERvlGRQADYVVSPGTYDQKhidrigkLKNCIAYGPGILDLAHQPDEWVGIA 405
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
30-202 |
1.21e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 83.90 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 30 NAKVIEKLASWFKDLGFS---VEVVEVEPGKHNMIARM-GEGEGG-LLLAGHSDTVPFDEGRWNFDPHKLTEKDNRFYGL 104
Cdd:PRK09133 58 TTPAAEAMAARLKAAGFAdadIEVTGPYPRKGNLVARLrGTDPKKpILLLAHMDVVEAKREDWTRDPFKLVEENGYFYGR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 105 GTADMKgFFAFIYEAV----KKVDWsKQKKPLYVLATCDEE-TTMLGARHFTANAP--FKPDYCI----------IGEPT 167
Cdd:PRK09133 138 GTSDDK-ADAAIWVATlirlKREGF-KPKRDIILALTGDEEgTPMNGVAWLAENHRdlIDAEFALneggggtldeDGKPV 215
|
170 180 190
....*....|....*....|....*....|....*
gi 503999166 168 SLVPIRGHKGHVANAIRVTGKSGHSSDPAlGVNAI 202
Cdd:PRK09133 216 LLTVQAGEKTYADFRLEVTNPGGHSSRPT-KDNAI 249
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
28-211 |
1.69e-16 |
|
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: 80.37 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 28 QGNAKVIEKLASWFKDLGFSVEVVEvepgKHNMIARMGEGEGGLLLAGHSDTVPFDEGrWNFDPHKLTEKDNRFYGLGTA 107
Cdd:cd03888 35 EGPRKALDKFLDLAKRLGFKTKNID----NYAGYAEYGEGEEVLGILGHLDVVPAGEG-WTTDPFKPVIKDGKLYGRGTI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 108 DMKG-----FFAFiyEAVKKVDWSKQKKPLYVLATcDEETTMLGARHFTANAP-----FKPDY---CIIGE--------- 165
Cdd:cd03888 110 DDKGptiaaLYAL--KILKDLGLPLKKKIRLIFGT-DEETGWKCIEHYFEHEEypdfgFTPDAefpVINGEkgivtvdlt 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 166 ----PTSLVPIRGHKG-----HV---ANA------------------------------IRVTGKSGHSSDPALGVNAI- 202
Cdd:cd03888 187 fkidDDKGYRLISIKGgeatnMVpdkAEAvipgkdkeelalsaatdlkgnieiddggveLTVTGKSAHASAPEKGVNAIt 266
|
250
....*....|..
gi 503999166 203 ---EIMYEVMFA 211
Cdd:cd03888 267 llaKFLAELNKD 278
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
24-328 |
3.85e-16 |
|
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: 79.43 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 24 PKWDQGNAKVIEKLASWFKDLGFSVEV--VEVEPGKHNMIARM-GEGEGGLL--LAGHSDTVPFDEGRWNFDPHKLTEKD 98
Cdd:cd08012 29 PKEDNAGRHVLEALTPYSTENGGPLVIdhVSYVKGRGNIIVEYpGTVDGKTVsfVGSHMDVVTANPETWEFDPFSLSIDG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 99 NRFYGLGTADMKGFFAFIYEAVKKVDWSKQKKPLYVLAT--CDEETT--------MLGARHFTANAPFKPDYCIigEPTS 168
Cdd:cd08012 109 DKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVVAVfiANEENSeipgvgvdALVKSGLLDNLKSGPLYWV--DSAD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 169 LVPIRGHKGHVANAIRVTGKSGHSSDPALGVNAIEIMYEVMfAMMQLRdkLIKEYH-HP-----GFAIPN---PTLnlgH 239
Cdd:cd08012 187 SQPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVMEAL-AEIQKR--FYIDFPpHPkeevyGFATPStmkPTQ---W 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 240 IHGGDSANRICGCCELHYDVRPLPGISLDGLENMLRG-------ALKEVEAKWP------------GRIEIVPLHESIPG 300
Cdd:cd08012 261 SYPGGSINQIPGECTICGDCRLTPFYDVKEVREKLEEyvddinaNIEELPTRGPvskyvlpaeglrGRVSLEFDEAAASG 340
|
330 340
....*....|....*....|....*...
gi 503999166 301 YECPHDHPfigGVEELCETSSQTVNYCT 328
Cdd:cd08012 341 VACNLDSP---GFHALCKATSEVVGYVK 365
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
30-291 |
8.16e-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: 77.98 E-value: 8.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 30 NAKVIEKLASWFKDLGFSVE---VVEVEPGKH------NMIARMGEGEGGLLLA--GHSDTVPFDEGrWNFDPHKLTEKD 98
Cdd:cd02697 24 NAPHAERTAALLQGFGFEAErhpVPEAEVRAYgmesitNLIVRRRYGDGGRTVAlnAHGDVVPPGDG-WTRDPYGAVVED 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 99 NRFYGLGTADMKGFFA---FIYEAVKKVDwSKQKKPLYVLATCDEETT-MLGARHFTANAPFKPDYcIIGEPTSLVPIRG 174
Cdd:cd02697 103 GVMYGRAAAVSKSDFAsftFAVRALESLG-APLRGAVELHFTYDEEFGgELGPGWLLRQGLTKPDL-LIAAGFSYEVVTA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 175 HKGHVANAIRVTGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLiKEYHHPGFAIPNPTLNLGHIHGGDSANRICGCCE 254
Cdd:cd02697 181 HNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNAQY-RQVSSQVEGITHPYLNVGRIEGGTNTNVVPGKVT 259
|
250 260 270
....*....|....*....|....*....|....*...
gi 503999166 255 LHYDVRPLPGISLDGLENMLRGALKEVEAKWPG-RIEI 291
Cdd:cd02697 260 FKLDRRMIPEENPVEVEAEIRRVIADAAASMPGiSVDI 297
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
59-168 |
1.11e-15 |
|
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: 74.78 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 59 NMIARMGEGEGG--LLLAGHSDTVP-FDEGRWNFDPHKLTEKDNRFYGLGTADMKGFFAFIYEAVK--KVDWSKQKKPLY 133
Cdd:cd18669 1 NVIARYGGGGGGkrVLLGAHIDVVPaGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKllKENGFKLKGTVV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 503999166 134 VLATCDEET-----TMLGARHFTANApFKPDYCIIGEPTS 168
Cdd:cd18669 81 VAFTPDEEVgsgagKGLLSKDALEED-LKVDYLFVGDATP 119
|
|
| dapE-gram_pos |
TIGR01900 |
succinyl-diaminopimelate desuccinylase; This model represents a clade of ... |
52-355 |
1.26e-15 |
|
succinyl-diaminopimelate desuccinylase; This model represents a clade of succinyl-diaminopimelate desuccinylases from actinobacteria (high-GC gram positives), delta-proteobacteria and aquificales and is based on the characterization of the enzyme from Corynebacterium glutamicum. This enzyme is involved in the biosynthesis of lysine, and is related to the enzyme acetylornithine deacetylase and other amidases and peptidases found within pfam01546. Other sequences included in the seed of this model were assessed to confirm that 1) the related genes DapC (succinyl-diaminopimelate transaminase) and DapD (2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase) are also found in the genome, 2) each is found only once in those genomes, 3) the lysine biosynthesis pathway is complete and 4) the direct (TIGR03540 or TIGR03542) or acetylated (GenProp0787) aminotransferase pathways are absent in thes genomes. Additionally, a number of the seed members are observed adjacent to either DapC or DapD (often as a divergon with a putative promoter site between them. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273864 [Multi-domain] Cd Length: 351 Bit Score: 77.32 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 52 EVEPGKHNMIARMGEGEGG-LLLAGHSDTVPFDE---GRWNfdphkltekDNRFYGLGTADMKGFFAFIYEAVKKVDWSK 127
Cdd:TIGR01900 40 EVIRHGNSVVARTNLGRPSrVILAGHLDTVPIADnlpSRVE---------GGRLYGRGAVDMKGGLAVMLALAATLDRTE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 128 QKKPL-YVLATCDE---ETTMLGarHFTANAP--FKPDYCIIGEPTSLVPIRGHKGHVANAIRVTGKSGHSSDPALGVNA 201
Cdd:TIGR01900 111 PRHDLtLVFYEREEgpaEENGLG--RLLREHPewLAGDLAVLLEPTDGKIEAGCQGTLRATVTFHGRRAHSARSWMGENA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 202 IEIMYEVMFAmmqLRDKLIKEYHHPG---FAIPNPTLnlghIHGGDSANRICGCCELHYDVRPLPGISLDGLENMLRGAL 278
Cdd:TIGR01900 189 IHKAAPILAR---LAAYEPREVTVDGltyREGLNAVR----IEGGVAGNVIPDECEVNVNYRFAPDRSLEQARAHVRELF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 279 KEVEAKWpgriEIVPLHESIPgyecPH-DHPfigGVEELCETSSQTVN----YCTEAPFLQELCPTLVLGPGSIDQAHQP 353
Cdd:TIGR01900 262 EGDGAEV----EVTDLSPGAR----PGlDNP---LAAELVAAVGGEVRakygWTDVARFSALGIPAVNFGPGDPALAHQD 330
|
..
gi 503999166 354 DE 355
Cdd:TIGR01900 331 DE 332
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
51-355 |
4.32e-15 |
|
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: 75.56 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 51 VEVEPGKHNMIARMGEG-EGGLLLAGHSDTVPFDEgrwNFdPHKLtEKDNRFYGLGTADMKGFFAFIYEAVKKVDWSKQK 129
Cdd:cd05647 35 LEVIRDGNTVVARTERGlASRVILAGHLDTVPVAG---NL-PSRV-EEDGVLYGCGATDMKAGDAVQLKLAATLAAATLK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 130 KPL-YVLATCDEETTML-GARHFTANAP--FKPDYCIIGEPTSLVPIRGHKGHVANAIRVTGKSGHSSDPALGVNAIEIM 205
Cdd:cd05647 110 HDLtLIFYDCEEVAAELnGLGRLAEEHPewLAADFAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 206 YEVMFAMMQLRDKLIK----EYHHpgfaipnpTLNLGHIHGGDSANRICGCCELHYDVRPLPGISLDGLENMLRGALKEV 281
Cdd:cd05647 190 APILARLAAYEPRTVNidglTYRE--------GLNAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGL 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503999166 282 EAKWpgriEIVPLHES-IPGYecphDHPFIGG-VEELCETSSQTVNYCTEAPFLQELCPTLVLGPGSIDQAHQPDE 355
Cdd:cd05647 262 GYEI----EVTDLSPGaLPGL----DHPVARDlIEAVGGKVRAKYGWTDVARFSALGIPAVNFGPGDPLLAHKRDE 329
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
28-356 |
4.64e-15 |
|
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: 75.96 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 28 QGNAKVIEKLASWFKDLGFS-VEVVEV--EPGKH--NMIARMGEGEGGLL-LAGHSDTVPF-DEGRWNFDPHKLTEKDNR 100
Cdd:cd05650 23 EGEKEKADYLEKKLREYGFYtLERYDApdERGIIrpNIVAKIPGGNDKTLwIISHLDTVPPgDLSLWETDPWEPVVKDGK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 101 FYGLGTAD-MKGFFAFIYEAVKKVDWS-KQKKPLYVLATCDEET-TMLGARHF-TANAPFKPDYCII----GEPTSLVPI 172
Cdd:cd05650 103 IYGRGVEDnQQGIVSSLLALKAIIKNGiTPKYNFGLLFVADEEDgSEYGIQYLlNKFDLFKKDDLIIvpdfGTEDGEFIE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 173 RGHKGHVANAIRVTGKSGHSSDPALGVNAieimYEVMFAMMQLRDKLIKEYH-------HPGFAIPNPTLNLGHIhggDS 245
Cdd:cd05650 183 IAEKSILWIKVNVKGKQCHASTPENGINA----FVAASNFALELDELLHEKFdekddlfNPPYSTFEPTKKEANV---PN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 246 ANRICGCCELHYDVRPLPGISLDGLENMLRGALKEVEAKWPGRIEIVPLHESIPGYECPHDHPFIGGVEELC------ET 319
Cdd:cd05650 256 VNTIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDFENSYGAGITYEIVQKEQAPPATPEDSEIVVRLSKAIkkvrgrEA 335
|
330 340 350
....*....|....*....|....*....|....*...
gi 503999166 320 SSQTVNYCTEAPFLQEL-CPTLVLGPGsIDQAHQPDEF 356
Cdd:cd05650 336 KLIGIGGGTVAAFLRKKgYPAVVWSTL-DETAHQPNEY 372
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
3-284 |
8.74e-15 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 74.82 E-value: 8.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 3 LPTFLEVYEglistssisstdPKWDQGNAK-VIEKLASWFkDLGFsvevvEVEPGKHNMIArmgeGEGGLLLAGHSDTVP 81
Cdd:PRK00466 16 LLDLLSIYT------------PSGNETNATkFFEKISNEL-NLKL-----EILPDSNSFIL----GEGDILLASHVDTVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 82 fdeGRwnFDPHKLTEKdnrFYGLGTADMKG-FFAFIYEAvkkvdWSKQKKPL--YVLATCDEETTMLGARHFTANApFKP 158
Cdd:PRK00466 74 ---GY--IEPKIEGEV---IYGRGAVDAKGpLISMIIAA-----WLLNEKGIkvMVSGLADEESTSIGAKELVSKG-FNF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 159 DYCIIGEPTSLVPIR-GHKGHVANAIRVTGKSGHSSDPALGvnaieimyevmfAMMQLRDKLIKEYHHPGfAIPNPTLNL 237
Cdd:PRK00466 140 KHIIVGEPSNGTDIVvEYRGSIQLDIMCEGTPEHSSSAKSN------------LIVDISKKIIEVYKQPE-NYDKPSIVP 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 503999166 238 GHIHGGDSANRICGCCELHYDVRPLPGISLDGLENMLRGALKEVEAK 284
Cdd:PRK00466 207 TIIRAGESYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQECGLK 253
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
59-167 |
1.54e-14 |
|
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: 71.69 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 59 NMIARMGEGEGG--LLLAGHSDTVPFDEGRWNFDP-HKLTEKDNRFYGLGTADMKGFFAFIYEAVK--KVDWSKQKKPLY 133
Cdd:cd03873 1 NLIARLGGGEGGksVALGAHLDVVPAGEGDNRDPPfAEDTEEEGRLYGRGALDDKGGVAAALEALKrlKENGFKPKGTIV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 503999166 134 VLATCDEETTMlGARHFTAN-----APFKPDYCIIGEPT 167
Cdd:cd03873 81 VAFTADEEVGS-GGGKGLLSkfllaEDLKVDAAFVIDAT 118
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
32-357 |
6.93e-14 |
|
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: 72.36 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 32 KVIEKLASWFKDLGFSVEVVEVEPGKHNMIARMGEGEGG--LLLAGHSDTVP-FDEGRWNFDPHKLTEKDNRFYGLGTAD 108
Cdd:cd03893 25 RAAEWLADLLRRLGFTVEIVDTSNGAPVVFAEFPGAPGAptVLLYGHYDVQPaGDEDGWDSDPFELTERDGRLYGRGAAD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 109 MKGFFAFIYEAVKKVDWSKQKKPLYV--LATCDEETTMLGARHFTANAP--FKPDYCII--------GEPTSLVPIRGhk 176
Cdd:cd03893 105 DKGPILAHLAALRALMQQGGDLPVNVkfIIEGEEESGSPSLDQLVEAHRdlLAADAIVIsdstwvgqEQPTLTYGLRG-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 177 ghVANA-IRV-TGKSGHSSDPALGVnaieiMYEVMFAMMQLRDKLIKE--------YHHPGFAIPN-------------- 232
Cdd:cd03893 183 --NANFdVEVkGLDHDLHSGLYGGV-----VPDPMTALAQLLASLRDEtgrilvpgLYDAVRELPEeefrldagvleeve 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 233 ----------------PTLNL----GHIHGGDSANRICGCCELHYDVRPLPGISLDGLENMLRGALKEVeAKWPGRIEIV 292
Cdd:cd03893 256 iiggttgsvaerlwtrPALTVlgidGGFPGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLEAHLEKH-APSGAKVTVS 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503999166 293 PLHESIPgYECPHDHPFI-GGVEELCETSSQTVNYCTEA---PFLQEL-----CPTLVLGPGSID-QAHQPDEFL 357
Cdd:cd03893 335 YVEGGMP-WRSDPSDPAYqAAKDALRTAYGVEPPLTREGgsiPFISVLqefpqAPVLLIGVGDPDdNAHSPNESL 408
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
33-155 |
9.98e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 69.11 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 33 VIEKLAswfkDLGFSVEVVEVEPGKHNMIARMgEGE----GGLLLAGHSDTVPFDEGRWNFDPHKLTEKDNRFYGLGTAD 108
Cdd:PRK07906 31 VAEKLA----EVGLEPTYLESAPGRANVVARL-PGAdpsrPALLVHGHLDVVPAEAADWSVHPFSGEIRDGYVWGRGAVD 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 503999166 109 MKGFFAFIYEAVKkvDWS----KQKKPLyVLA-TCDEETTM-LGARHFTANAP 155
Cdd:PRK07906 106 MKDMDAMMLAVVR--HLArtgrRPPRDL-VFAfVADEEAGGtYGAHWLVDNHP 155
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
37-185 |
1.41e-12 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 68.65 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 37 LASWfkdlGFSVEVVEVEpGKHNMIARMGEGEGGLLLAGHSDTVPFDEGRWNFDPHKLTEKDNRFYGLGTADMKGFFAFI 116
Cdd:PRK08554 37 LESW----GIESELIEKD-GYYAVYGEIGEGKPKLLFMAHFDVVPVNPEEWNTEPFKLTVKGDKAYGRGSADDKGNVASV 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503999166 117 YEAVKKVDWSKQKKPLYVLATCDEETTMLGARHFT---ANAPFKPDYCIIGEPTSLVPI-RGHKGHVAnAIRV 185
Cdd:PRK08554 112 MLALKELSKEPLNGKVIFAFTGDEEIGGAMAMHIAeklREEGKLPKYMINADGIGMKPIiRRRKGFGV-TIRV 183
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
71-283 |
1.20e-10 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 62.29 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 71 LLLAGHSDTV-----PFDEGRWnfdphkltEKDNRFYGLGTADMKGFFAFIYEAVKKVDWSKQKKPL-Y-VLATCDEETT 143
Cdd:PRK07338 95 VLLTGHMDTVfpadhPFQTLSW--------LDDGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLgYdVLINPDEEIG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 144 MLGARHFTANAPFKPDYCIIGEPT----SLVPIRghKGHVANAIRVTGKSGHSS-DPALGVNAIEIMYEVMFAMMQLRDK 218
Cdd:PRK07338 167 SPASAPLLAELARGKHAALTYEPAlpdgTLAGAR--KGSGNFTIVVTGRAAHAGrAFDEGRNAIVAAAELALALHALNGQ 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503999166 219 LikeyhhpgfaiPNPTLNLGHIHGGDSANRICGCCELHYDVRPLPGISLDGLENMLRGALKEVEA 283
Cdd:PRK07338 245 R-----------DGVTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQ 298
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
35-111 |
1.25e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 62.63 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 35 EKLASWFKDLGFSVEVVE--VEPGKHNMIARMGEGEG--GLLLAGHSDTVPFDEGRWN--FDPHKLTEKDNRFYGLGTAD 108
Cdd:PRK07079 48 DEIAPALAALGFTCRIVDnpVAGGGPFLIAERIEDDAlpTVLIYGHGDVVRGYDEQWRegLSPWTLTEEGDRWYGRGTAD 127
|
...
gi 503999166 109 MKG 111
Cdd:PRK07079 128 NKG 130
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
31-275 |
9.13e-10 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 59.59 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 31 AKVIEKLASWFKDLGFSVEVVEVEPGKHNMIARMgEGEG----GLLLAGHSDTVPFDEGRWNFDP---HKltEKDNRFYG 103
Cdd:cd05646 24 DACVEFLKRQADELGLPVRVIEVVPGKPVVVLTW-EGSNpelpSILLNSHTDVVPVFEEKWTHDPfsaHK--DEDGNIYA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 104 LGTADMKGFFAFIYEAVK--KVDWSKQKKPLYVLATCDEET-TMLGARHFTANAPFK---PDYCI---IGEPTSLVPI-R 173
Cdd:cd05646 101 RGAQDMKCVGIQYLEAIRrlKASGFKPKRTIHLSFVPDEEIgGHDGMEKFVKTEEFKklnVGFALdegLASPTEEYRVfY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 174 GHKG--HVanAIRVTGKSGHSSDpALGVNAIEIMYEVMFAMMQLRDKLIKEYH-HPGFAIPNPT-LNLGHIHGGDSANRI 249
Cdd:cd05646 181 GERSpwWV--VITAPGTPGHGSK-LLENTAGEKLRKVIESIMEFRESQKQRLKsNPNLTLGDVTtVNLTMLKGGVQMNVV 257
|
250 260
....*....|....*....|....*.
gi 503999166 250 CGCCELHYDVRPLPGISLDGLENMLR 275
Cdd:cd05646 258 PSEAEAGFDLRIPPTVDLEEFEKQID 283
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
26-111 |
2.40e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 58.76 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 26 WDQGNAKVIEKLASW----FKDLGF-SVEVVEvEPGKHNMIARMgEGEGG---LLLAGHSDTVP-FDEGRWNFDPHKLTE 96
Cdd:PRK07907 35 ADPFRREEVARSAEWvadlLREAGFdDVRVVS-ADGAPAVIGTR-PAPPGaptVLLYAHHDVQPpGDPDAWDSPPFELTE 112
|
90
....*....|....*
gi 503999166 97 KDNRFYGLGTADMKG 111
Cdd:PRK07907 113 RDGRLYGRGAADDKG 127
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
41-123 |
9.94e-09 |
|
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: 56.74 E-value: 9.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 41 FKDLGFSVEVVE--VEPGKHNMIARMGEGEGG--LLLAGHSDTVPFDEGRWN--FDPHKLTEKDNRFYGLGTADMKGFFA 114
Cdd:cd05679 41 FERLGFTVHIHDnpVAGRAPFLIAERIEDPSLptLLIYGHGDVVPGYEGRWRdgRDPWTVTVWGERWYGRGTADNKGQHS 120
|
....*....
gi 503999166 115 FIYEAVKKV 123
Cdd:cd05679 121 INMAALRQV 129
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
29-291 |
5.23e-08 |
|
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: 53.99 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 29 GNAKVIEK-LASWFKDLGFsvEVVEVEPGKH------NMIARM-GEGEGG--LLLAGHSDTVpfDEGRWNFDPHKlteKD 98
Cdd:cd05683 20 LHEKEISKvLKKKFENLGL--SVIEDDAGKTtgggagNLICTLkADKEEVpkILFTSHMDTV--TPGINVKPPQI---AD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 99 NRFYGLGT----ADMKGFFAFIYEAVKKVdwSKQKKP---LYVLATCDEETTMLGARHFTANApFKPDYCII----GEPT 167
Cdd:cd05683 93 GYIYSDGTtilgADDKAGIAAILEAIRVI--KEKNIPhgqIQFVITVGEESGLVGAKALDPEL-IDADYGYAldseGDVG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 168 SLVpIRGHKGHVANAIrVTGKSGHSS-DPALGVNAIEIMYEVMFAMMQLRdklIKEYhhpgfaipnPTLNLGHIHGGDSA 246
Cdd:cd05683 170 TII-VGAPTQDKINAK-IYGKTAHAGtSPEKGISAINIAAKAISNMKLGR---IDEE---------TTANIGKFQGGTAT 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 503999166 247 NRICGCCELHYDVRPLPGISLDGLENMLRGALKEVEAKWPGRIEI 291
Cdd:cd05683 236 NIVTDEVNIEAEARSLDEEKLDAQVKHMKETFETTAKEKGAHAEV 280
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
32-111 |
1.63e-07 |
|
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: 52.99 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 32 KVIEKLASWFKDLGFSVEVVEVepGKHNM------------IARMGE--GEGGLLLAGHSDTVPFD-EGRWNFDPHKLTE 96
Cdd:cd05676 37 RMMEWAAERLEKLGFKVELVDI--GTQTLpdgeelplppvlLGRLGSdpSKKTVLIYGHLDVQPAKlEDGWDTDPFELTE 114
|
90
....*....|....*
gi 503999166 97 KDNRFYGLGTADMKG 111
Cdd:cd05676 115 KDGKLYGRGSTDDKG 129
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
71-205 |
2.50e-07 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 52.25 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 71 LLLAGHSDTVPFD---EGRWNFDPHKLTEKDNRFYGLGTADMKGFFAFIYEAVKKVDWS--KQKKPLYVLATCDEETTML 145
Cdd:PRK08262 114 IVLMAHQDVVPVApgtEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQgfQPRRTIYLAFGHDEEVGGL 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503999166 146 GARH---FTANAPFKPDYCI-------------IGEPTSLVPIrGHKGHVANAIRVTGKSGHSSDPALGvNAIEIM 205
Cdd:PRK08262 194 GARAiaeLLKERGVRLAFVLdeggaitegvlpgVKKPVALIGV-AEKGYATLELTARATGGHSSMPPRQ-TAIGRL 267
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
71-237 |
2.89e-07 |
|
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: 52.26 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 71 LLLAGHSDTVP---FDEGRWNFDPHKLTEKDNRFYGLGTADMKGFFAFIYEAVK---KVDWsKQKKPLYVLATCDEETT- 143
Cdd:cd05674 72 LLLMAHQDVVPvnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVElllKRGF-KPRRTIILAFGHDEEVGg 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 144 MLGARHfTANAPFKP-----------------DYCIIGEPTSLVPIrGHKGHVANAIRVTGKSGHSSDPALGvNAIEIMY 206
Cdd:cd05674 151 ERGAGA-IAELLLERygvdglaaildeggavlEGVFLGVPFALPGV-AEKGYMDVEITVHTPGGHSSVPPKH-TGIGILS 227
|
170 180 190
....*....|....*....|....*....|.
gi 503999166 207 EvmfammqLRDKLIKEYHHPGFAIPNPTLNL 237
Cdd:cd05674 228 E-------AVAALEANPFPPKLTPGNPYYGM 251
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
31-299 |
7.13e-07 |
|
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: 50.95 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 31 AKVIEKLASWFKDLGFSVEVVEVEPGKHNMIARMGEGEGGL---LLAGHSDTVPFDEGRWNFDP---HKltEKDNRFYGL 104
Cdd:TIGR01880 31 AACVDFLIKQADELGLARKTIEFVPGKPVVVLTWPGSNPELpsiLLNSHTDVVPVFREHWTHPPfsaFK--DEDGNIYAR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 105 GTADMKGFFAFIYEAVK--KVDWSKQKKPLYVLATCDEET-TMLGARHFTA-------NAPFKPDYCIIGEPTSLVPIRG 174
Cdd:TIGR01880 109 GAQDMKCVGVQYLEAVRnlKASGFKFKRTIHISFVPDEEIgGHDGMEKFAKtdefkalNLGFALDEGLASPDDVYRVFYA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 175 HKGHVANAIRVTGKSGHSSDpALGVNAIEIMYEVMFAMMQLRDK---LIKEyhHPGFAIPN-PTLNLGHIHGGDSANRIC 250
Cdd:TIGR01880 189 ERVPWWVVVTAPGNPGHGSK-LMENTAMEKLEKSVESIRRFRESqfqLLQS--NPDLAIGDvTSVNLTKLKGGVQSNVIP 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 503999166 251 GCCELHYDVRPLPGISLDGLENML--------RGALKEVEAKWpGRIEIVPLHESIP 299
Cdd:TIGR01880 266 SEAEAGFDIRLAPSVDFEEMENRLdewcadagEGVTYEFSQHS-GKPLVTPHDDSNP 321
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
34-217 |
1.29e-06 |
|
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: 50.03 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 34 IEKLASW----FKDLGFSVEVVEvEPGKHNMIARMGEG-EGGLLLAGHSDTVPFDE-GRWNFDPHKLTEKDNRFYGLGTA 107
Cdd:cd05681 21 IPETADFlkefLRRLGAEVEIFE-TDGNPIVYAEFNSGdAKTLLFYNHYDVQPAEPlELWTSDPFELTIRNGKLYARGVA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 108 DMKGFFAFIYEAVKKVDWSKQKKPLYV--LATCDEETTMLGARHFTANAP--FKPDYCI-----IGEPTSLVPIRGHKGH 178
Cdd:cd05681 100 DDKGELMARLAALRALLQHLGELPVNIkfLVEGEEEVGSPNLEKFVAEHAdlLKADGCIwegggKNPKGRPQISLGVKGI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503999166 179 VANAIRVTG--KSGHSSDPALGVNAIeimYEVMFAMMQLRD 217
Cdd:cd05681 180 VYVELRVKTadFDLHSSYGAIVENPA---WRLVQALNSLRD 217
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
183-378 |
8.50e-06 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 47.21 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 183 IRVTGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLIKEyHHPGfaipnpTLNLGHIHGGDSANRICGCCELHYDVRPL 262
Cdd:cd03886 176 ITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVVSRELDP-LEPA------VVTVGKFHAGTAFNVIPDTAVLEGTIRTF 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 263 PGISLDGLENMLRGALKEVEAKWPGRIEIvplhESIPGYECPHDHPfiggveELCETSSQTV-----NYCTEAP------ 331
Cdd:cd03886 249 DPEVREALEARIKRLAEGIAAAYGATVEL----EYGYGYPAVINDP------ELTELVREAAkellgEEAVVEPepvmgs 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503999166 332 ----FLQELCPT--LVLGPGSIDQA----HQPDeflaFDFIDPTIDVLSKAMVKYCC 378
Cdd:cd03886 319 edfaYYLEKVPGafFWLGAGEPDGEnpglHSPT----FDFDEDALPIGAALLAELAL 371
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
23-360 |
3.42e-05 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 45.38 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 23 DPKWDQGNAKVIEKLASWFKDLGFS-VEVveVEPGKHNMIAR---MGEGEGGLLLAGHSDTVPFD-EGRWNFDPHKLTEK 97
Cdd:cd05680 16 DPAHKGDVRRAAEWLADKLTEAGFEhTEV--LPTGGHPLVYAewlGAPGAPTVLVYGHYDVQPPDpLELWTSPPFEPVVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 98 DNRFYGLGTADMKGFFAFIYEAVKkvDWSKQKKPLYV----LATCDEET--TMLGArHFTANAP-FKPDYCII------- 163
Cdd:cd05680 94 DGRLYARGASDDKGQVFIHIKAVE--AWLAVEGALPVnvkfLIEGEEEIgsPSLPA-FLEENAErLAADVVLVsdtsmws 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 164 -GEPTSLVPIRG---------------HKGH----VANAIRVTGK---SGHSSDpalGVNAIEIMYE----------VMF 210
Cdd:cd05680 171 pDTPTITYGLRGlayleisvtgpnrdlHSGSyggaVPNPANALARllaSLHDED---GRVAIPGFYDdvrpltdaerEAW 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 211 AMMQLRDKL------IKEYHHP-GFAI-----PNPTLNLGHIHGG-----------DSANRICGCcelhydvRPLPGISL 267
Cdd:cd05680 248 AALPFDEAAfkaslgVPALGGEaGYTTlerlwARPTLDVNGIWGGyqgegsktvipSKAHAKISM-------RLVPGQDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 268 DGLENMLRGALKEVEAkwPG-RIEIVPLHESIPgYECPHDHPFIGGVEELCETSSQTVNYCTE--------APFLQEL-C 337
Cdd:cd05680 321 DAIADLLEAHLRAHAP--PGvTLSVKPLHGGRP-YLVPTDHPALQAAERALEEAFGKPPVFVReggsipivALFEKVLgI 397
|
410 420
....*....|....*....|....
gi 503999166 338 PTLVLGPGSIDQA-HQPDEFLAFD 360
Cdd:cd05680 398 PTVLMGFGLPDDAiHAPNEKFRLE 421
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
24-254 |
3.86e-05 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 45.16 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 24 PKWDQgnAKVIEKLASWFKDLGFSVEVVEVEPGkhnmiaRMG-------------EGEGGLLLAGHSDTV---------P 81
Cdd:PRK07473 26 PTWDA--AAVNRMLDLAARDMAIMGATIERIPG------RQGfgdcvrarfphprQGEPGILIAGHMDTVhpvgtleklP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 82 F-DEGrwnfdphkltekdNRFYGLGTADMKGFFAFIYEAVKKVDWSKQKKPL--YVLATCDEETTMLGARHFTANAPFKP 158
Cdd:PRK07473 98 WrREG-------------NKCYGPGILDMKGGNYLALEAIRQLARAGITTPLpiTVLFTPDEEVGTPSTRDLIEAEAARN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 159 DYCIIGEPTslvpiRGHKGHVAN--AI-----RVTGKSGHS-SDPALGVNAIEIMYEVMFAMMQLRDKlikeyhhpgfai 230
Cdd:PRK07473 165 KYVLVPEPG-----RPDNGVVTGryAIarfnlEATGRPSHAgATLSEGRSAIREMARQILAIDAMTTE------------ 227
|
250 260
....*....|....*....|....
gi 503999166 231 pNPTLNLGHIHGGDSANRICGCCE 254
Cdd:PRK07473 228 -DCTFSVGIVHGGQWVNCVATTCT 250
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
183-291 |
5.44e-05 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of uncharacterized 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: 349936 [Multi-domain] Cd Length: 371 Bit Score: 44.96 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 183 IRVTGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLIKEYHhpgfaipnPT-LNLGHIHGGDSANRICGCCELHYDVRP 261
Cdd:cd08014 175 IRIQGEGGHGARPHLTVDLVWAAAQVVTDLPQAISRRIDPRS--------PVvLTWGSIEGGRAPNVIPDSVELSGTVRT 246
|
90 100 110
....*....|....*....|....*....|
gi 503999166 262 LPGISLDGLENMLRGALKEVEAKWPGRIEI 291
Cdd:cd08014 247 LDPDTWAQLPDLVEEIVAGICAPYGAKYEL 276
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
23-108 |
7.63e-05 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 44.63 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 23 DPKWDQgNA---KVIEKLASWFKD---LGFSVEVVEVE---PGKHNMIARMGEGEGGLLLAGHSDTVP----FDEGrwnF 89
Cdd:cd05682 20 DPEWAT-NGlleKAANLIADWVKAqniKGAKVEVVELEgrtPLLFVEIPGTEQDDDTVLLYGHMDKQPpftgWDEG---L 95
|
90
....*....|....*....
gi 503999166 90 DPHKLTEKDNRFYGLGTAD 108
Cdd:cd05682 96 GPTKPVIRGDKLYGRGGAD 114
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
54-226 |
7.85e-05 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 44.64 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 54 EPGKHNMIARM-GEGEG--GLLLAGHSDTVPFDE-GRWN---FDPHKLTEK--------DNR----------FYGLGTAD 108
Cdd:cd05654 54 DLGRRNVTALVkGKKPSkrTIILISHFDTVGIEDyGELKdiaFDPDELTKAfseyveelDEEvredllsgewLFGRGTMD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 109 MKG----FFAFIYEAVKKVDWSKQkkpLYVLATCDEETT---MLGAR------------HFTAnapfkpdyCIIGEPTS- 168
Cdd:cd05654 134 MKSglavHLALLEQASEDEDFDGN---LLLMAVPDEEVNsrgMRAAVpallelkkkhdlEYKL--------AINSEPIFp 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503999166 169 LVP---IR----GHKGHVANAIRVTGKSGHSSDPALGVNAIEIMYEVMFAM---MQLRDKLIKEYHHP 226
Cdd:cd05654 203 QYDgdqTRyiytGSIGKILPGFLCYGKETHVGEPFAGINANLMASEITARLelnADLCEKVEGEITPP 270
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
34-122 |
1.60e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 40.12 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 34 IEKLASWFKD----LGFSVEVVEvEPGKHNMIARMGEG-EGGLLLAGHSDTVPFDE-GRWNFDPHKLTEKDNRFYGLGTA 107
Cdd:PRK06446 24 IEETANYLKDtmekLGIKANIER-TKGHPVVYGEINVGaKKTLLIYNHYDVQPVDPlSEWKRDPFSATIENGRIYARGAS 102
|
90 100
....*....|....*....|
gi 503999166 108 DMKG-----FFAfIYEAVKK 122
Cdd:PRK06446 103 DNKGtlmarLFA-IKHLIDK 121
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
183-290 |
1.61e-03 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 40.33 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 183 IRVTGKSGHSSDPALGVNAIEIMYEVMFAMMQLRDKLIKeyhhpgfAIPNPTLNLGHIHGGDSANRICGCCELHYDVRpl 262
Cdd:cd08021 186 ITIKGKGGHGSMPHETVDPIVIAAQIVTALQTIVSRRVD-------PLDPAVVTIGTFQGGTSFNVIPDTVELKGTVR-- 256
|
90 100
....*....|....*....|....*...
gi 503999166 263 pgiSLDglenmlrgalKEVEAKWPGRIE 290
Cdd:cd08021 257 ---TFD----------EEVREQVPKRIE 271
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
141-260 |
3.47e-03 |
|
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: 39.24 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503999166 141 ETTMLGARHFTANAPF----KPDYC----IIGEPTSLVPIRghKGHVANA-----IRVTGKSGHSSDPALGVNAIeimye 207
Cdd:cd05664 133 EETGGGAQAMVDDGLYdkipKPDVVlaqhVMPGPAGTVGTR--PGRFLSAadsldITIFGRGGHGSMPHLTIDPV----- 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 503999166 208 VMFA--MMQLRDKLIKEYHHPGFAIpnptLNLGHIHGGDSANRICGCCELHYDVR 260
Cdd:cd05664 206 VMAAsiVTRLQTIVSREVDPQEFAV----VTVGSIQAGSAENIIPDEAELKLNVR 256
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
71-119 |
3.49e-03 |
|
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: 39.25 E-value: 3.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 503999166 71 LLLAGHSDTVPFDE-GRWNFDPHKLTEKDNRFYGLGTADMKG-FFAFIYEA 119
Cdd:cd05677 74 ILFYGHYDVIPAGEtDGWDTDPFTLTCENGYLYGRGVSDNKGpLLAAIYAV 124
|
|
| |
