|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
1-380 |
0e+00 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 727.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 1 MPLPSLKDQFGALIAASSVSCTQPELDQTNRPVVDLLASWLGDLGFRCEIREV--SPGKFNLLASYGSGPGGLVLAGHTD 78
Cdd:PRK05111 2 MKLPSFIEMYRALIATPSISATDPALDQSNRAVIDLLAGWFEDLGFNVEIQPVpgTRGKFNLLASLGSGEGGLLLAGHTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 79 TVPYDEALWSSDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQPLMILATCDEESSMAGARALAESGRPLG 158
Cdd:PRK05111 82 TVPFDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAEATAIRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 159 RATVIGEPTNLRPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGEWQRAWNNPQFSVPQPTLNFG 238
Cdd:PRK05111 162 DCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQERYHNPAFTVPYPTLNLG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 239 CIHGGDNPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAERHQVSIDYQPLFPAVPPFEQAQDSELVRVAERLTG 318
Cdd:PRK05111 242 HIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSERWPGRITVAPLHPPIPGYECPADHQLVRVVEKLLG 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600399 319 HRAEAVAFGTEAPYFQRLGSETLVLGAGDIACAHQPDEHLELARIEPMVGVLRRLIQHYCLT 380
Cdd:PRK05111 322 HKAEVVNYCTEAPFIQQLGCPTLVLGPGSIEQAHQPDEYLELSFIKPTRELLRQLIHHFCLH 383
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
12-375 |
1.48e-149 |
|
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: 427.01 E-value: 1.48e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 12 ALIAASSVSCtqpeldQTNRPVVDLLASWLGDLGFRCEIREVS-PGKFNLLASYGSGP-GGLVLAGHTDTVPYDEALWSS 89
Cdd:cd03894 5 RLVAFDTVSR------NSNLALIEYVADYLAALGVKSRRVPVPeGGKANLLATLGPGGeGGLLLSGHTDVVPVDGQKWSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 90 DPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQPLMILATCDEESSMAGARALAESGRPLG---RATVIGEP 166
Cdd:cd03894 79 DPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALAARGgrpDAAIVGEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 167 TNLRPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGEWQRAWNNPQFSVPQPTLNFGCIHGGDNP 246
Cdd:cd03894 159 TSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPFDPPYPTLNVGLIHGGNAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 247 NRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAERHQVSIDYQPLFPaVPPFEQAQDSELVRVAERLTG-HRAEAVA 325
Cdd:cd03894 239 NIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPEAGIEVEPLFE-VPGLETDEDAPLVRLAAALAGdNKVRTVA 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15600399 326 FGTEAPYFQRLGSETLVLGAGDIACAHQPDEHLELARIEPMVGVLRRLIQ 375
Cdd:cd03894 318 YGTEAGLFQRAGIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
8-374 |
1.82e-122 |
|
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: 358.36 E-value: 1.82e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 8 DQFGALIAASSVSCTqpeldqTNRPVVDLLASWLGDLGFRCEIREVSPG--KFNLLASYG-SGPGGLVLAGHTDTVPYDE 84
Cdd:TIGR01892 1 EILTKLVAFDSTSFR------PNVDLIDWAQAYLEALGFSVEVQPFPDGaeKSNLVAVIGpSGAGGLALSGHTDVVPYDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 85 ALWSSDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQPLMILATCDEESSMAGARALAESGRPLGRATVIG 164
Cdd:TIGR01892 75 AAWTRDPFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIEAGAGRPRHAIIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 165 EPTNLRPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGEWQRAWNNPQFSVPQPTLNFGCIHGGD 244
Cdd:TIGR01892 155 EPTRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDLDEGFTPPYTTLNIGVIQGGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 245 NPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAERHQVSIDYQPLFPAVPPFEQAQDSELVRVAERLTGHRAEAV 324
Cdd:TIGR01892 235 AVNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRDEPGFEVQIEVVSTDPGVNTEPDAELVAFLEELSGNAPEVV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15600399 325 AFGTEAPYFQRLGSETLVLGAGDIACAHQPDEHLELARIEPMVGVLRRLI 374
Cdd:TIGR01892 315 SYGTEAPQFQELGAEAVVCGPGDIRQAHQPDEYVEIEDLVRCRAVLARLV 364
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
12-378 |
1.16e-103 |
|
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: 311.05 E-value: 1.16e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 12 ALIAASSVSctqpeldQTNRPVVDLLASWLGDLGFRCEIREVSPGKFNLLASY-GSGPG-GLVLAGHTDTVPYDE-ALWS 88
Cdd:COG0624 20 ELVRIPSVS-------GEEAAAAELLAELLEALGFEVERLEVPPGRPNLVARRpGDGGGpTLLLYGHLDVVPPGDlELWT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 89 SDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQP--LMILATCDEESSMAGARALAESGRPLGRAT--VIG 164
Cdd:COG0624 93 SDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPgnVTLLFTGDEEVGSPGARALVEELAEGLKADaaIVG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 165 EPTN-LRPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGEWQRawnNPQFsvPQPTLNFGCIHGG 243
Cdd:COG0624 173 EPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRA---DPLF--GRTTLNVTGIEGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 244 DNPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAErhQVSIDYQPLFPAVPPFEQAQDSELVR----VAERLTGH 319
Cdd:COG0624 248 TAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAP--GVEVEVEVLGDGRPPFETPPDSPLVAaaraAIREVTGK 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600399 320 RAE--AVAFGTEAPYFQR-LGSETLVLGAGDIACAHQPDEHLELARIEPMVGVLRRLIQHYC 378
Cdd:COG0624 326 EPVlsGVGGGTDARFFAEaLGIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
13-376 |
7.28e-90 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 275.53 E-value: 7.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 13 LIAASSVSCTqpeldqTNRPVVDLLASWLGDLGFRCEireVSPG----KFNLLASYG-SGPGGLVLAGHTDTVPYDEALW 87
Cdd:PRK07522 13 LVAFDTVSRD------SNLALIEWVRDYLAAHGVESE---LIPDpegdKANLFATIGpADRGGIVLSGHTDVVPVDGQAW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 88 SSDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQPLMILATCDEESSMAGAR----ALAESG-RPLGraTV 162
Cdd:PRK07522 84 TSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPsmiaRLPERGvKPAG--CI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 163 IGEPTNLRPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGEW-QRAWNNPQFSVPQPTLNFGCIH 241
Cdd:PRK07522 162 VGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLaAPGPFDALFDPPYSTLQTGTIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 242 GGDNPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPL------AERHQVSIDYQPLFpAVPPFEQAQDSELVRVAER 315
Cdd:PRK07522 242 GGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAEllpemrAVHPEAAIEFEPLS-AYPGLDTAEDAAAARLVRA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600399 316 LTGHRA-EAVAFGTEAPYFQRLGSETLVLGAGDIACAHQPDEHLELARIEPMVGVLRRLIQH 376
Cdd:PRK07522 321 LTGDNDlRKVAYGTEAGLFQRAGIPTVVCGPGSIEQAHKPDEFVELAQLAACEAFLRRLLAS 382
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
12-374 |
9.61e-80 |
|
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: 249.14 E-value: 9.61e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 12 ALIAASSVSCtqPEldqtnRPVVDLLASWLGDLGFRCEiREVSPGKFNLLASYGSGPG-GLVLAGHTDTVP-YDEALWSS 89
Cdd:cd08659 5 DLVQIPSVNP--PE-----AEVAEYLAELLAKRGYGIE-STIVEGRGNLVATVGGGDGpVLLLNGHIDTVPpGDGDKWSF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 90 DPLRLDERDGRWYGLGSCDMKGffPLA--IEALLPLLD--QPFRQPLMILATCDEESSMAGARALAESGR-PLGRATVIG 164
Cdd:cd08659 77 PPFSGRIRDGRLYGRGACDMKG--GLAamVAALIELKEagALLGGRVALLATVDEEVGSDGARALLEAGYaDRLDALIVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 165 EPTNLRPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGEWQRawnNPQFsvPQPTLNFGCIHGGD 244
Cdd:cd08659 155 EPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPA---HPLL--GPPTLNVGVINGGT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 245 NPNRICGQCSLEFDLRPLPGMQPkqlrEAIRQRLRPLAERHQVSIDYQPLFPAVPPFEQAQDSELVRV---AERLTGHRA 321
Cdd:cd08659 230 QVNSIPDEATLRVDIRLVPGETN----EGVIARLEAILEEHEAKLTVEVSLDGDPPFFTDPDHPLVQAlqaAARALGGDP 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600399 322 EAVAFG--TEAPYF-QRLGSETLVLGAGDIACAHQPDEHLELARIEPMVGVLRRLI 374
Cdd:cd08659 306 VVRPFTgtTDASYFaKDLGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
72-376 |
1.66e-64 |
|
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: 208.35 E-value: 1.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 72 VLAGHTDTVPyDEALWSsDPLRLDErDGRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQ-PLMILATCDEESSMAGARAL 150
Cdd:pfam01546 1 LLRGHMDVVP-DEETWG-WPFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLKKgTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 151 AESGRPLGR------ATVIGEPTNL------RPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGE 218
Cdd:pfam01546 78 IEDGLLEREkvdavfGLHIGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 219 WQRAWNNPQFSVpqptLNFGCIHGGDNPnrICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAERHQVSIDYQPLFPAV 298
Cdd:pfam01546 158 NVDPLDPAVVTV----GNITGIPGGVNV--IPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEYVEGGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 299 PPFeqAQDSELV----RVAERLTGHRAEAVAF----GTEAPYF-QRLGSETLVLGAGDiACAHQPDEHLELARIEPMVGV 369
Cdd:pfam01546 232 PPL--VNDSPLVaalrEAAKELFGLKVELIVSgsmgGTDAAFFlLGVPPTVVFFGPGS-GLAHSPNEYVDLDDLEKGAKV 308
|
....*..
gi 15600399 370 LRRLIQH 376
Cdd:pfam01546 309 LARLLLK 315
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
31-375 |
3.98e-56 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 188.66 E-value: 3.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 31 RPVVDLLASWLGDLGFRCEIREVS--------PGKFNLLASYGSGPGGLVLAGHTDTVPYDEALWSSDPLRLDERDGRWY 102
Cdd:PRK08651 29 EEIAEFLRDTLEELGFSTEIIEVPneyvkkhdGPRPNLIARRGSGNPHLHFNGHYDVVPPGEGWSVNVPFEPKVKDGKVY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 103 GLGSCDMKGffPLA-IEALLPLLDQPFRQPLMILATCDEESSMAGARALAESGRPLGRATVIGEPTNLRPIRL-HKGVMM 180
Cdd:PRK08651 109 GRGASDMKG--GIAaLLAAFERLDPAGDGNIELAIVPDEETGGTGTGYLVEEGKVTPDYVIVGEPSGLDNICIgHRGLVW 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 181 ERIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGEWQRAWNNPQFSVPQPTLNFG--CIHGGDNPNRICGQCSLEFD 258
Cdd:PRK08651 187 GVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYEYDDERGAKPTVTLGgpTVEGGTKTNIVPGYCAFSID 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 259 LRPLPGMQPKQLREAIRQRLRPLAERHQVSIDYQPLfPAVPPFEQAQDSELVRV----AERLTGHRAEAVAF--GTEAPY 332
Cdd:PRK08651 267 RRLIPEETAEEVRDELEALLDEVAPELGIEVEFEIT-PFSEAFVTDPDSELVKAlreaIREVLGVEPKKTISlgGTDARF 345
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 15600399 333 FQRLGSETLVLGAGDIACAHQPDEHLELARIEPMVGVLRRLIQ 375
Cdd:PRK08651 346 FGAKGIPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVLK 388
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
5-369 |
4.36e-44 |
|
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: 156.79 E-value: 4.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 5 SLKDqfgaLIAASSVSCTQPELDqtnrPVVDLLASWLGDLGFRCEIREVSPGKFNLLAS---YGSGPGG---LVLAGHTD 78
Cdd:TIGR01910 3 LLKD----LISIPSVNPPGGNEE----TIANYIKDLLREFGFSTDVIEITDDRLKVLGKvvvKEPGNGNeksLIFNGHYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 79 TVPY-DEALWSSDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPL--LDQPFRQPLMILATCDEESSMAGARALAESG- 154
Cdd:TIGR01910 75 VVPAgDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIreAGIKPNGNIILQSVVDEESGEAGTLYLLQRGy 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 155 RPLGRATVIGEPTNLRPI-RLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELmalrGEWQRAWNN---PQFSV 230
Cdd:TIGR01910 155 FKDADGVLIPEPSGGDNIvIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITEL----NELEEHIYArnsYGFIP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 231 PQPTLNFGCIHGGDNPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAERHQVSIDYQPLFPAVPPFEQAQDSELV 310
Cdd:TIGR01910 231 GPITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYENEPVVKWSGPNETPPDSRLV 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600399 311 RVAE----RLTGHRAEAVAF--GTEAPYFQRLGSETLVLGAGDIACAHQPDEHLELARIEPMVGV 369
Cdd:TIGR01910 311 KALEaiikKVRGIEPEVLVStgGTDARFLRKAGIPSIVYGPGDLETAHQVNEYISIKNLVESTKV 375
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-374 |
2.82e-42 |
|
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: 151.39 E-value: 2.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 13 LIAASSVSctqPELDQTnRPVVDLLASWLGDLGFRCEIREVSPGKFNLLASYGSGPGG--LVLAGHTDTVPYDEAL-WSS 89
Cdd:cd08011 7 LVQIPSPN---PPGDNT-SAIAAYIKLLLEDLGYPVELHEPPEEIYGVVSNIVGGRKGkrLLFNGHYDVVPAGDGEgWTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 90 DPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLD--QPFRQPLMILATCDEES-SMAGARALAESGRPLGRATVIGEP 166
Cdd:cd08011 83 DPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADakAPWDLPVVLTFVPDEETgGRAGTKYLLEKVRIKPNDVLIGEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 167 TNLRPIRL-HKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMALrgewqrawnnpqfsvpQPTLNFGCIHGGDN 245
Cdd:cd08011 163 SGSDNIRIgEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYEL----------------EKTVNPGVIKGGVK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 246 PNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAErhqvsidYQPLFPAVP-PFEQAQDSELVRVAER----LTGHR 320
Cdd:cd08011 227 VNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSIEE-------VSFEIKSFYsPTVSNPDSEIVKKTEEaiteVLGIR 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600399 321 AEAV--AFGTEAPYFQRLGSETLVLGAGDIACAHQPDEHLELARIEPMVGVLRRLI 374
Cdd:cd08011 300 PKEVisVGASDARFYRNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
33-378 |
1.46e-40 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 147.24 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 33 VVDLLASWLGDLGFRCEIREVSPGKFNLLASY-GSGPG-GLVLAGHTDTVPYDEalWSSDPLRLDERDGRWYGLGSCDMK 110
Cdd:cd08013 31 IATYVAAWLAHRGIEAHRIEGTPGRPSVVGVVrGTGGGkSLMLNGHIDTVTLDG--YDGDPLSGEIADGRVYGRGTLDMK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 111 GFFPLAIEALLPLLDQPFRQPLMILATCDEESSMAGARALAESG-RplGRATVIGEPTNLRPIRLHKGVMMERIEILGQS 189
Cdd:cd08013 109 GGLAACMAALADAKEAGLRGDVILAAVADEEDASLGTQEVLAAGwR--ADAAIVTEPTNLQIIHAHKGFVWFEVDIHGRA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 190 GHSSDPNLGRSALEAMHATIGELMALRGEWQRAWNNPQFSvpQPTLNFGCIHGGDNPNRICGQCSLEFDLRPLPGMQPKQ 269
Cdd:cd08013 187 AHGSRPDLGVDAILKAGYFLVALEEYQQELPERPVDPLLG--RASVHASLIKGGEEPSSYPARCTLTIERRTIPGETDES 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 270 LREAIRQRLRPLAERH-QVSIDYQPLFPAVPPFEQAQDSELVRVAERLTG--------HRAEavAFGTEAPYFQRLGSET 340
Cdd:cd08013 265 VLAELTAILGELAQTVpNFSYREPRITLSRPPFEVPKEHPFVQLVAAHAAkvlgeapqIRSE--TFWTDAALLAEAGIPS 342
|
330 340 350
....*....|....*....|....*....|....*...
gi 15600399 341 LVLGAgDIACAHQPDEHLELARIEPMVGVLRRLIQHYC 378
Cdd:cd08013 343 VVFGP-SGAGLHAKEEWVDVESIRQLREVLSAVVREFC 379
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
45-374 |
3.94e-37 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 137.64 E-value: 3.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 45 GFRCEIREVSPGKFNLLASYGSgPGGLvLAGHTDTVPyDEALWSSDPLRLDERDGRWYGLGSCDMKGffplAIEALLPLL 124
Cdd:PRK08737 42 GFQVEVIDHGAGAVSLYAVRGT-PKYL-FNVHLDTVP-DSPHWSADPHVMRRTDDRVIGLGVCDIKG----AAAALLAAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 125 DQPfRQPLMILATCDEE--SSMAGARALAESgrPLGRATVIGEPTNLRPIRLHKGVMMERIEILGQSGHSSDP-NLGRSA 201
Cdd:PRK08737 115 NAG-DGDAAFLFSSDEEanDPRCVAAFLARG--IPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKqDPSASA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 202 L-EAM--------------HATIGELMALRgewqrawnnpqfsvpqptLNFGCIHGGDNPNRICGQCSLEFDLRPLPGMQ 266
Cdd:PRK08737 192 LhQAMrwggqaldhveslaHARFGGLTGLR------------------FNIGRVEGGIKANMIAPAAELRFGFRPLPSMD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 267 PKQLReairQRLRPLAERHQVSIDYQPLFPAVPPFEQA----QDSELVRVAERLTGHRAEAVAFGTEAPYFQRLGSETLV 342
Cdd:PRK08737 254 VDGLL----ATFAGFAEPAAATFEETFRGPSLPSGDIAraeeRRLAARDVADALDLPIGNAVDFWTEASLFSAAGYTALV 329
|
330 340 350
....*....|....*....|....*....|..
gi 15600399 343 LGAGDIACAHQPDEHLELARIEPMVGVLRRLI 374
Cdd:PRK08737 330 YGPGDIAQAHTADEFVTLDQLQRYAESVHRII 361
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
31-375 |
4.16e-36 |
|
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: 134.32 E-value: 4.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 31 RPVVDLLASWLGDLGFRCEIREVSP-GKFNLLASYGSGPG-GLVLAGHTDTV-PYDealwssdPLRLDERDGRWYGLGSC 107
Cdd:cd05652 19 AAVGDFLAEYLESLGFTVEKQPVENkDRFNVYAYPGSSRQpRVLLTSHIDTVpPFI-------PYSISDGGDTIYGRGSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 108 DMKGffPLA--IEALLPLLDQPFRQP--LMILATCDEESSMAGARALAESGRPLGRATVIGEPTNLRPIRLHKGVMMERI 183
Cdd:cd05652 92 DAKG--SVAaqIIAVEELLAEGEVPEgdLGLLFVVGEETGGDGMKAFNDLGLNTWDAVIFGEPTELKLASGHKGMLGFKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 184 EILGQSGHSSDPNLGRSALEAMHATIGELMALRGEWQRAWNNpqfsvpqPTLNFGCIHGGDNPNRICGQCSLEFDLR--- 260
Cdd:cd05652 170 TAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPSSELLGP-------TTLNIGRISGGVAANVVPAAAEASVAIRlaa 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 261 -PLPGMqpKQLREAIRQRLRP--------LAERHQVSIDYQplfpaVPPFEqaqdselvrvaerltghrAEAVAFGTEAP 331
Cdd:cd05652 243 gPPEVK--DIVKEAVAGILTDtedievtfTSGYGPVDLDCD-----VDGFE------------------TDVVAYGTDIP 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15600399 332 YFQrlGSETLVL-GAGDIACAHQPDEHLELARIEPMVGVLRRLIQ 375
Cdd:cd05652 298 YLK--GDHKRYLyGPGSILVAHGPDEAITVSELEEAVEGYKKLIL 340
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
33-374 |
1.16e-35 |
|
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: 133.87 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 33 VVDLLASWLGDLGFRCEIREVSPGKFNLLASY-GSGPGGLVLAGHTDTVpYDEALWSSDPLRLDerDGRWYGLGSCDMKG 111
Cdd:cd03885 24 VAELLAEELEALGFTVERRPLGEFGDHLIATFkGTGGKRVLLIGHMDTV-FPEGTLAFRPFTVD--GDRAYGPGVADMKG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 112 FFPLAIEALLPLLDQPFRQ--PLMILATCDEESSMAGARAL-AESGRpLGRATVIGEPT----NLRPIRlhKGVMMERIE 184
Cdd:cd03885 101 GLVVILHALKALKAAGGRDylPITVLLNSDEEIGSPGSRELiEEEAK-GADYVLVFEPAradgNLVTAR--KGIGRFRLT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 185 ILGQSGHSS-DPNLGRSALEAMHATIGELMALrgewqrawNNPQfsvPQPTLNFGCIHGGDNPNRICGQCSLEFDLRPLP 263
Cdd:cd03885 178 VKGRAAHAGnAPEKGRSAIYELAHQVLALHAL--------TDPE---KGTTVNVGVISGGTRVNVVPDHAEAQVDVRFAT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 264 GMQPKQLREAIRqRLRPLAERHQVSIDYQPLFpAVPPFEQAQDSE-LVRVAERLTG-----HRAEAVAFGTEAPYFQRLG 337
Cdd:cd03885 247 AEEADRVEEALR-AIVATTLVPGTSVELTGGL-NRPPMEETPASRrLLARAQEIAAelgltLDWEATGGGSDANFTAALG 324
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 15600399 338 SETL----VLGAGdiacAHQPDEHLELARIEPMVGVLRRLI 374
Cdd:cd03885 325 VPTLdglgPVGGG----AHTEDEYLELDSLVPRIKLLARLL 361
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
38-377 |
1.89e-35 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 133.47 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 38 ASWLGDL----GFRCEIREVSPGKFNLLASYGSGPGGLVLAGHTDTV-PYDEALWSSDPLRLDERDGRWYGLGSCDMK-G 111
Cdd:PRK08588 25 ANYLQDLfakhGIESKIVKVNDGRANLVAEIGSGSPVLALSGHMDVVaAGDVDKWTYDPFELTEKDGKLYGRGATDMKsG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 112 FFPLAIeALLPLLDQpfRQPLM----ILATCDEESSMAGARALAEsgrpLGRAT-----VIGEPTNLRPIRLHKGVMMER 182
Cdd:PRK08588 105 LAALVI-AMIELKEQ--GQLLNgtirLLATAGEEVGELGAKQLTE----KGYADdldalIIGEPSGHGIVYAHKGSMDYK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 183 IEILGQSGHSSDPNLGRSALEAmhatigeLMALRGEWQRAWNNpqFSVPQPTL-----NFGCIHGGDNPNRICGQCSLEF 257
Cdd:PRK08588 178 VTSTGKAAHSSMPELGVNAIDP-------LLEFYNEQKEYFDS--IKKHNPYLgglthVVTIINGGEQVNSVPDEAELEF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 258 DLRPLP---GMQPKQLREAIRQRLRPlAERHQVSID-YQPLfpavPPFEQAQDSELVRVAERLTGHRAE------AVAFG 327
Cdd:PRK08588 249 NIRTIPeydNDQVISLLQEIINEVNQ-NGAAQLSLDiYSNH----RPVASDKDSKLVQLAKDVAKSYVGqdiplsAIPGA 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15600399 328 TEAPYFqrLGSET----LVLGAGDIACAHQPDEHLELARIEPMVGVLRRLIQHY 377
Cdd:PRK08588 324 TDASSF--LKKKPdfpvIIFGPGNNLTAHQVDEYVEKDMYLKFIDIYKEIIIQY 375
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
31-374 |
1.78e-34 |
|
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: 130.16 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 31 RPVVDLLASWLGDLGFRCEIREVSpgkfNLLASYGSGPGGLVLAGHTDTVPYDEalwssdPLRLDErdGRWYGLGSCDMK 110
Cdd:cd05653 21 ARAAKFLEEIMKELGLEAWVDEAG----NAVGGAGSGPPDVLLLGHIDTVPGEI------PVRVEG--GVLYGRGAVDAK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 111 GffPLA--IEALLpLLDQPFRQPLMILATCDEESSMAGARALAESG-RPLgrATVIGEPTNLRPIRL-HKGVMMERIEIL 186
Cdd:cd05653 89 G--PLAamILAAS-ALNEELGARVVVAGLVDEEGSSKGARELVRRGpRPD--YIIIGEPSGWDGITLgYRGSLLVKIRCE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 187 GQSGHSSDPnlGRSALEAMHATIGELMALRGEWQRAwNNPQFSVpQPTLnfgcIHGGDNPNRICGQCSLEFDLRpLPgmq 266
Cdd:cd05653 164 GRSGHSSSP--ERNAAEDLIKKWLEVKKWAEGYNVG-GRDFDSV-VPTL----IKGGESSNGLPQRAEATIDLR-LP--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 267 PKQLREAIRQRLRPLAERHQVSIdyqplFPAVPPFEQAQDSELVRVAER----LTGHRAEAVAFGTE-----APyfqRLG 337
Cdd:cd05653 232 PRLSPEEAIALATALLPTCELEF-----IDDTEPVKVSKNNPLARAFRRairkQGGKPRLKRKTGTSdmnvlAP---LWT 303
|
330 340 350
....*....|....*....|....*....|....*..
gi 15600399 338 SETLVLGAGDIACAHQPDEHLELARIEPMVGVLRRLI 374
Cdd:cd05653 304 VPIVAYGPGDSTLDHTPNEHIELAEIERAAAVLKGAL 340
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
55-361 |
1.62e-31 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 123.19 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 55 PGKFNLLASY-GSGPGG--LVLAGHTDTVPYDE-ALWSSDPLRLDERDGRWYGLGSCDMKG---FFPLAIEALLPLLDQP 127
Cdd:cd03895 58 AGAPNVVGTHrPRGETGrsLILNGHIDVVPEGPvELWTRPPFEATIVDGWMYGRGAGDMKAglaANLFALDALRAAGLQP 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 128 fRQPLMILATCDEESSMAGARALAESGRPlGRATVIGEPTNLRPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHA 207
Cdd:cd03895 138 -AADVHFQSVVEEECTGNGALAALMRGYR-ADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 208 TIGELMALRGEW-QRAWNNPQFS-VPQP-TLNFGCIHGGDNPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAER 284
Cdd:cd03895 216 LIQALQELEREWnARKKSHPHFSdHPHPiNFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVADAAAT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 285 ------HQVSIDYQPlFPAvPPFEQAQDSELV----RVAERLTGHRAEAVAF--GTEAPYFQRLGS-ETLVLGAGDIAcA 351
Cdd:cd03895 296 dpwlsnHPPEVEWNG-FQA-EGYVLEPGSDAEqvlaAAHQAVFGTPPVQSAMtaTTDGRFFVLYGDiPALCYGPGSRD-A 372
|
330
....*....|
gi 15600399 352 HQPDEHLELA 361
Cdd:cd03895 373 HGFDESVDLE 382
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
31-378 |
4.68e-31 |
|
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: 121.05 E-value: 4.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 31 RPVVDLLASWLGDLGFRCEIREvspGKFNLLASY-GSGPG-GLVLAGHTDTVpydeaLWSSDPLRLDERDGRWYGLGSCD 108
Cdd:cd03896 18 GARADLVAEWMADLGLGDVERD---GRGNVVGRLrGTGGGpALLFSAHLDTV-----FPGDTPATVRHEGGRIYGPGIGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 109 MKGFFP--LAIEALLPLLDQPFRQPLMILATCDEE--SSMAGARALAESGRPLGRATVIGEPTNLRPIRLHKGVMMERIE 184
Cdd:cd03896 90 NKGSLAclLAMARAMKEAGAALKGDVVFAANVGEEglGDLRGARYLLSAHGARLDYFVVAEGTDGVPHTGAVGSKRFRIT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 185 ILGQSGHSSDPNLGRSALEAMHATIGELmalrgewqRAWNNPqfSVPQPTLNFGCIHGGDNPNRICGQCSLEFDLRPLPG 264
Cdd:cd03896 170 TVGPGGHSYGAFGSPSAIVAMAKLVEAL--------YEWAAP--YVPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 265 MQPKQLREAIRQRLRPLAERH-QVSIDYQPlFPAVPPFEQAQDSELVRVAErlTGHRAEAV-----AFGTEAPYFQRLGS 338
Cdd:cd03896 240 AELADVQREVEAVVSKLAAKHlRVKARVKP-VGDRPGGEAQGTEPLVNAAV--AAHREVGGdprpgSSSTDANPANSLGI 316
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15600399 339 ETLVLGAGDIACAHQPDEHLELARIEPMVGVLRRLIQHYC 378
Cdd:cd03896 317 PAVTYGLGRGGNAHRGDEYVLKDDMLKGAKAYLMLAAALC 356
|
|
| PRK06915 |
PRK06915 |
peptidase; |
65-360 |
6.45e-29 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 116.33 E-value: 6.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 65 GSGPG-GLVLAGHTDTVPY-DEALWSSDPLRLDERDGRWYGLGSCDMKG---FFPLAIEALLPlLDQPFRQPLMILATCD 139
Cdd:PRK06915 89 GSGGGkSMILNGHIDVVPEgDVNQWDHHPYSGEVIGGRIYGRGTTDMKGgnvALLLAMEALIE-SGIELKGDVIFQSVIE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 140 EESSMAGARALAESGRPlGRATVIGEPTNLRPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGEW 219
Cdd:PRK06915 168 EESGGAGTLAAILRGYK-ADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEEKR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 220 QRAWNNPQF-SVPQPT-LNFGCIHGGDNPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAER------HQVSIDY 291
Cdd:PRK06915 247 NDRITDPLYkGIPIPIpINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAELNDVdewfveHPVEVEW 326
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600399 292 qplFPAV-PPFEQAQDSELVRVA----ERLTGHRA--EAVAFGTEAPYFQRLGS-ETLVLGAGDIACAHQPDEHLEL 360
Cdd:PRK06915 327 ---FGARwVPGELEENHPLMTTLehnfVEIEGNKPiiEASPWGTDGGLLTQIAGvPTIVFGPGETKVAHYPNEYIEV 400
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
33-373 |
8.76e-28 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 111.78 E-value: 8.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 33 VVDLLASWLGDLGFRCEIREVSPGKfNLLASygsGPGGLVLAGHTDTVPYDEalwssdplRLDERDGRWYGLGSCDMKGf 112
Cdd:PRK08652 24 IALHIMEFLESLGYDVHIESDGEVI-NIVVN---SKAELFVEVHYDTVPVRA--------EFFVDGVYVYGTGACDAKG- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 113 fplAIEALLPLLDQ---PFRQP-LMILATCDEESSMAGARALAESGRPlGRATVIgEPTNLRPIRLHKGVMMERIEILGQ 188
Cdd:PRK08652 91 ---GVAAILLALEElgkEFEDLnVGIAFVSDEEEGGRGSALFAERYRP-KMAIVL-EPTDLKVAIAHYGNLEAYVEVKGK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 189 SGHSSDPNLGRSALEAMHATIGELMALRGEWQRAWNnpqfsvpqPTLNFGCIHGGDNPNRICGQCSLEFDLRpLPgmqPK 268
Cdd:PRK08652 166 PSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFD--------PHIGIQEIIGGSPEYSIPALCRLRLDAR-IP---PE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 269 QLREAIRQRLRPLAERHQVSIDYQPLFPAvppFEQAQDSELVRVAERLTGHRAEAVAFG-----TEAPYFQRLGSETLVL 343
Cdd:PRK08652 234 VEVEDVLDEIDPILDEYTVKYEYTEIWDG---FELDEDEEIVQLLEKAMKEVGLEPEFTvmrswTDAINFRYNGTKTVVW 310
|
330 340 350
....*....|....*....|....*....|
gi 15600399 344 GAGDIACAHQPDEHLELARIEPMVGVLRRL 373
Cdd:PRK08652 311 GPGELDLCHTKFERIDVREVEKAKEFLKAL 340
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
175-285 |
5.11e-27 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 103.19 E-value: 5.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 175 HKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGEWQRAWnnpqfsvPQPTLNFGCIHGGDNPNRICGQCS 254
Cdd:pfam07687 3 HKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGFDF-------PRTTLNITGIEGGTATNVIPAEAE 75
|
90 100 110
....*....|....*....|....*....|.
gi 15600399 255 LEFDLRPLPGMQPKQLREAIRQRLRPLAERH 285
Cdd:pfam07687 76 AKFDIRLLPGEDLEELLEEIEAILEKELPEG 106
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
31-375 |
6.40e-26 |
|
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: 108.22 E-value: 6.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 31 RPVVDLLASWLGDLGF--RCEIREVSPGKFNLLASYGSG---PGGLVLAGHTDTVPYDEALWSSDPLRLDERDGRWYGLG 105
Cdd:cd05675 23 TRAAEVLAARLAEAGIqtEIFVVESHPGRANLVARIGGTdpsAGPLLLLGHIDVVPADASDWSVDPFSGEIKDGYVYGRG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 106 SCDMKGFFPLAIEALLPLLDQPF--RQPLMILATCDEES-SMAGARALAESGRPL--GRATVIGE----------PTNLR 170
Cdd:cd05675 103 AVDMKNMAAMMLAVLRHYKREGFkpKRDLVFAFVADEEAgGENGAKWLVDNHPELfdGATFALNEggggslpvgkGRRLY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 171 PIRL-HKGVMMERIEILGQSGHSSDPN--------------LGRSAL-----------EAMHATIGE------------- 211
Cdd:cd05675 183 PIQVaEKGIAWMKLTVRGRAGHGSRPTddnaitrlaealrrLGAHNFpvrltdetayfAQMAELAGGeggalmltavpvl 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 212 --LMALRGEWQRAWNnpqfSVPQPTLNFGCIHGGDNPNRICGQCSLEFDLRPLPGmqpkQLREAIRQRLRPLAERHQVSI 289
Cdd:cd05675 263 dpALAKLGPSAPLLN----AMLRNTASPTMLDAGYATNVLPGRATAEVDCRILPG----QSEEEVLDTLDKLLGDPDVSV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 290 DYQPLFPA-VPPFeqaqDSELVRVAERLTGH---RAEAVAF----GTEAPYFQRLGSET-----LVLGAGDIAC--AHQP 354
Cdd:cd05675 335 EAVHLEPAtESPL----DSPLVDAMEAAVQAvdpGAPVVPYmspgGTDAKYFRRLGIPGygfapLFLPPELDYTglFHGV 410
|
410 420
....*....|....*....|.
gi 15600399 355 DEHLELARIEPMVGVLRRLIQ 375
Cdd:cd05675 411 DERVPVESLYFGVRFLDRLVK 431
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
31-356 |
8.34e-26 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 107.54 E-value: 8.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 31 RPVVDLLASWLGDLGFRCE-IR-EVSPG------KFNLLASY-GSGPGGLV-LAGHTDTVPYDEAlWSSDPLRLDERDGR 100
Cdd:PRK13013 37 REICEFLAARLAPRGFEVElIRaEGAPGdsetypRWNLVARRqGARDGDCVhFNSHHDVVEVGHG-WTRDPFGGEVKDGR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 101 WYGLGSCDMKGFFPLAIEALLPLLDQ--PFRQPLMILATCDEES-SMAGARALAESGR---PLGRATVIGEPTNLRPIRL 174
Cdd:PRK13013 116 IYGRGACDMKGGLAASIIAAEAFLAVypDFAGSIEISGTADEESgGFGGVAYLAEQGRfspDRVQHVIIPEPLNKDRICL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 175 -HKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGE-------LMALRgewqrawnnpQFSVP-------QPTLNFGC 239
Cdd:PRK13013 196 gHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEieerlfpLLATR----------RTAMPvvpegarQSTLNINS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 240 IHGGD-----------NPNrICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLA-ERHQVSIDYQPLFpAVPPFEQAQDS 307
Cdd:PRK13013 266 IHGGEpeqdpdytglpAPC-VADRCRIVIDRRFLIEEDLDEVKAEITALLERLKrARPGFAYEIRDLF-EVLPTMTDRDA 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600399 308 ELVRVA----ERLTGHRAEAVAF-GT-EAPYFQRLGS--ETLVLGAGDIACAHQPDE 356
Cdd:PRK13013 344 PVVRSVaaaiERVLGRQADYVVSpGTyDQKHIDRIGKlkNCIAYGPGILDLAHQPDE 400
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
35-374 |
8.51e-24 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 101.38 E-value: 8.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 35 DLLASWLGDLGF----RCEIREVSPG-KFNLLASYGSGPGG-LVLAGHTDTVPY-DEALWSSDPLRLDERDGRWYGLGSC 107
Cdd:cd05650 30 DYLEKKLREYGFytleRYDAPDERGIiRPNIVAKIPGGNDKtLWIISHLDTVPPgDLSLWETDPWEPVVKDGKIYGRGVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 108 D-MKGFFP--LAIEALLPLLDQPFRQPLMILATCDEESSMAGARALAES---------------GRPLGRATVIGEptnl 169
Cdd:cd05650 110 DnQQGIVSslLALKAIIKNGITPKYNFGLLFVADEEDGSEYGIQYLLNKfdlfkkddliivpdfGTEDGEFIEIAE---- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 170 rpirlhKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGEWQRAWN---NPQFSVPQPTLNFGCIhggDNP 246
Cdd:cd05650 186 ------KSILWIKVNVKGKQCHASTPENGINAFVAASNFALELDELLHEKFDEKDdlfNPPYSTFEPTKKEANV---PNV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 247 NRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAERHQVSIDYQPLFPAVPPFEQAQDSELV----RVAERLTGHRAE 322
Cdd:cd05650 257 NTIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDFENSYGAGITYEIVQKEQAPPATPEDSEIVvrlsKAIKKVRGREAK 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15600399 323 AVAF--GTEAPYFQRLGSETLVLGAGDIACaHQPDEHLELARIEPMVGVLRRLI 374
Cdd:cd05650 337 LIGIggGTVAAFLRKKGYPAVVWSTLDETA-HQPNEYIRISHIVKDAKVFAEML 389
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
12-374 |
1.15e-23 |
|
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: 100.66 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 12 ALIAASSVSctqPELDQTNrpvvDLLASWLGDLGFRCEIREVSPGKfNLLASYGSGPGGLVLAGHTDTVPY-DEALWSSD 90
Cdd:cd03891 6 ELIRRPSVT---PDDAGAQ----DLIAERLKALGFTCERLEFGGVK-NLWARRGTGGPHLCFAGHTDVVPPgDLEGWSSD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 91 PLRLDERDGRWYGLGSCDMKGffplAIEALLP----LLDQPFRQPLMI--LATCDEE-SSMAGARALAESGRPLGRA--- 160
Cdd:cd03891 78 PFSPTIKDGMLYGRGAADMKG----GIAAFVAaaerFVAKHPNHKGSIsfLITSDEEgPAIDGTKKVLEWLKARGEKidy 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 161 TVIGEPTNLRPI-------RlhKGVMMERIEILGQSGHSSDPNLgrsALEAMHATIGELMALRGEwqrAWN--NPQFsvp 231
Cdd:cd03891 154 CIVGEPTSEKKLgdtikigR--RGSLNGKLTIKGKQGHVAYPHL---ADNPIHLLAPILAELTAT---VLDegNEFF--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 232 QPT-LNFGCIHGGdNP--NRICGQCSLEFDLRplpgMQPKQLREAIRQRLRPLAERHQVSIDYQpLFPAVPPFeQAQDSE 308
Cdd:cd03891 223 PPSsLQITNIDVG-NGatNVIPGELKAKFNIR----FNDEHTGESLKARIEAILDKHGLDYDLE-WKLSGEPF-LTKPGK 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600399 309 LVRVA----ERLTGHRAE-AVAFGT-EAPYFQRLGSETLVLGAGDiACAHQPDEHLELARIEPMVGVLRRLI 374
Cdd:cd03891 296 LVDAVsaaiKEVTGITPElSTSGGTsDARFIASYGCPVVEFGLVN-ATIHKVNERVSVADLEKLTDIYERIL 366
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
31-376 |
1.92e-22 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 96.95 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 31 RPVVDLLASWLGDLGFRCEIREVSpgkfNLLASYGSGPGGLVLAGHTDTVPYDEalwssdPLRLdeRDGRWYGLGSCDMK 110
Cdd:PRK04443 26 AAAAEFLVEFMESHGREAWVDEAG----NARGPAGDGPPLVLLLGHIDTVPGDI------PVRV--EDGVLWGRGSVDAK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 111 GffPLAIEALLPLLDQPFRQPLMILATCDEE--SSMAGARALAESGRPLgrATVIGEPTNLRPIRL-HKGVMMERIEILG 187
Cdd:PRK04443 94 G--PLAAFAAAAARLEALVRARVSFVGAVEEeaPSSGGARLVADRERPD--AVIIGEPSGWDGITLgYKGRLLVTYVATS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 188 QSGHSSDPnlGRSALEAMHA---TIGELMALRGEWQRAwnnpqFSVPQPTLNFGCIHGGDnpnrICGQCSLEFDLRPLPG 264
Cdd:PRK04443 170 ESFHSAGP--EPNAAEDAIEwwlAVEAWFEANDGRERV-----FDQVTPKLVDFDSSSDG----LTVEAEMTVGLRLPPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 265 MQPKQLREAIRQrlrpLAERHQVSIDyqplfPAVPPFEQAQDSELVR---VAERLTGHRaeaVAF----GTE-----APY 332
Cdd:PRK04443 239 LSPEEAREILDA----LLPTGTVTFT-----GAVPAYMVSKRTPLARafrVAIREAGGT---PRLkrktGTSdmnvvAPA 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 15600399 333 FqrlGSETLVLGAGDIACAHQPDEHLELARIEPMVGVLRRLIQH 376
Cdd:PRK04443 307 W---GCPMVAYGPGDSDLDHTPDEHLPLAEYLRAIAVLTDVLER 347
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
35-368 |
4.91e-22 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 96.46 E-value: 4.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 35 DLLASWLGDLGFRcEIREV-SPGKF-------NLLASYGSGPGGLVL--AGHTDTVPY-DEALWSSDPLRLDERDGRWYG 103
Cdd:PRK13983 34 EYLESLLKEYGFD-EVERYdAPDPRviegvrpNIVAKIPGGDGKRTLwiISHMDVVPPgDLSLWETDPFKPVVKDGKIYG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 104 LGSCD-MKGFFP--LAIEALLPLLDQPFRQPLMILATcDEE-SSMAGARALAE----------------SGRPLGRATVI 163
Cdd:PRK13983 113 RGSEDnGQGIVSslLALKALMDLGIRPKYNLGLAFVS-DEEtGSKYGIQYLLKkhpelfkkddlilvpdAGNPDGSFIEI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 164 GEptnlrpirlhKGVMMERIEILGQSGHSSDPNLGRSAL-EAMHAtigeLMALRGEWQRAWN------NPQFSVPQPTln 236
Cdd:PRK13983 192 AE----------KSILWLKFTVKGKQCHASTPENGINAHrAAADF----ALELDEALHEKFNakdplfDPPYSTFEPT-- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 237 fgcIHGG--DNPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAERHQVSIDYQPLFPAVPPFEQAQDSELV---- 310
Cdd:PRK13983 256 ---KKEAnvDNINTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIADEFEEEYGVKIEVEIVQREQAPPPTPPDSEIVkklk 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 311 RVAERLTGHRAEAVAFG--TEAPYFQRLGSETLVLGAGDiACAHQPDEHlelARIEPMVG 368
Cdd:PRK13983 333 RAIKEVRGIEPKVGGIGggTVAAFLRKKGYPAVVWSTLD-ETAHQPNEY---AKISNLIE 388
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
56-285 |
2.97e-21 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 94.68 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 56 GKFNLLASY-GSGPGG--LVLAGHTDTVPYDEA-LWSSDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLDQPFrQP 131
Cdd:PRK06837 82 GAPNVVGTYrPAGKTGrsLILQGHIDVVPEGPLdLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGL-AP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 132 L--MILATCDEESSmAGARALAEsgrpLGR-----ATVIGEPTNLRPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEA 204
Cdd:PRK06837 161 AarVHFQSVIEEES-TGNGALST----LQRgyradACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 205 MHATIGELMALRGEW-QRAWNNPQFS-VPQP-TLNFGCIHGGDNPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPL 281
Cdd:PRK06837 236 AYHLIQALRELEAEWnARKASDPHFEdVPHPiNFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAADAQAEIEACLAAA 315
|
....
gi 15600399 282 AERH 285
Cdd:PRK06837 316 ARDD 319
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
35-377 |
1.82e-20 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 91.69 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 35 DLLASWLGDLGFRCEIREVSPGKfNLLASYGSGPGGLVLAGHTDTVPY-DEALWSSDPLRLDERDGRWYGLGSCDMKG-- 111
Cdd:PRK13009 26 DLLAERLEALGFTCERMDFGDVK-NLWARRGTEGPHLCFAGHTDVVPPgDLEAWTSPPFEPTIRDGMLYGRGAADMKGsl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 112 -FFPLAIEALLPllDQP-FRQPLMILATCDEESSmA--GARALAESGRPLGR---ATVIGEPTNlrPIRLhkGVMME--- 181
Cdd:PRK13009 105 aAFVVAAERFVA--AHPdHKGSIAFLITSDEEGP-AinGTVKVLEWLKARGEkidYCIVGEPTS--TERL--GDVIKngr 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 182 ------RIEILGQSGHSSDPNLGRSALEAMHATIGELMAlrgewqRAWN--NPQFsvpQPT-LNFGCIHGGdNP--NRIC 250
Cdd:PRK13009 178 rgsltgKLTVKGVQGHVAYPHLADNPIHLAAPALAELAA------TEWDegNEFF---PPTsLQITNIDAG-TGatNVIP 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 251 GQCSLEFDLRplpgMQPKQLREAIRQRLRPLAERHQVSIDYQPLFPAvPPFEQaQDSELVRVA----ERLTGHRAEA-VA 325
Cdd:PRK13009 248 GELEAQFNFR----FSTEHTAESLKARVEAILDKHGLDYTLEWTLSG-EPFLT-PPGKLVDAVvaaiEAVTGITPELsTS 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 15600399 326 FGT-EAPYFQRLGSETLVLGA-GdiACAHQPDEHLELARIEPMVGVLRRLIQHY 377
Cdd:PRK13009 322 GGTsDARFIADYGAQVVEFGPvN--ATIHKVNECVSVADLEKLTRIYERILERL 373
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
12-374 |
9.13e-20 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 89.29 E-value: 9.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 12 ALIAASSVSctqPELDQTnrpvVDLLASWLGDLGFRceIREVSPGKFNLLASYGSGPGGLVLAGHTDTVPYDEAlWSSDP 91
Cdd:cd05651 8 SLIATPSFS---REEHKT----ADLIENYLEQKGIP--FKRKGNNVWAENGHFDEGKPTLLLNSHHDTVKPNAG-WTKDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 92 LRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLDQ-PFRQPLMILATCDEESS-MAGARALAESGRPLGRAtVIGEPTNL 169
Cdd:cd05651 78 FEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEgPLNYNLIYAASAEEEISgKNGIESLLPHLPPLDLA-IVGEPTEM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 170 RPIRLHKGVMMERIEILGQSGHSSDPNlgrsALEAMHATIGELmalrgEWQRAWNNPQFS--VPQPTLNFGCIHGGDNPN 247
Cdd:cd05651 157 QPAIAEKGLLVLDCTARGKAGHAARNE----GDNAIYKALDDI-----QWLRDFRFDKVSplLGPVKMTVTQINAGTQHN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 248 RICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAERHqvSIDYQPlfPAVPPfeqaqDSELVRVAerltgHRAEAVAFG 327
Cdd:cd05651 228 VVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLKSEIKPR--SFRLNS--SAIPP-----DHPIVQAA-----IAAGRTPFG 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15600399 328 TEAPYFQRLGS-ETLVLGAGDIACAHQPDEHLELARIEPMVGVLRRLI 374
Cdd:cd05651 294 SPTLSDQALMPfPSVKIGPGDSSRSHTADEFIELSEIEEGIDIYIELL 341
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
12-364 |
1.07e-19 |
|
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: 90.08 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 12 ALIAASSVScTQPELDQTNRPVVDLLASWLGDLGFRCEIREVSPGKFNLLASYGSGPGG--LVLAGHTDTVP-YDEALWS 88
Cdd:cd03893 6 ELVAIPSVS-AQPDRREELRRAAEWLADLLRRLGFTVEIVDTSNGAPVVFAEFPGAPGAptVLLYGHYDVQPaGDEDGWD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 89 SDPLRLDERDGRWYGLGSCDMKGffPL-----AIEALLPLLDQPFRQPLMILATCdEESSMAGARALAESGRPLGRATVI 163
Cdd:cd03893 85 SDPFELTERDGRLYGRGAADDKG--PIlahlaALRALMQQGGDLPVNVKFIIEGE-EESGSPSLDQLVEAHRDLLAADAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 164 ----------GEPT---NLRpirlhkGVMMERIEI--LGQSGHSS-------DPN-LGRSALEAMHATIGELM------- 213
Cdd:cd03893 162 visdstwvgqEQPTltyGLR------GNANFDVEVkgLDHDLHSGlyggvvpDPMtALAQLLASLRDETGRILvpglyda 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 214 ----------ALRG---EW-----------QRAWNNPQFSVpqptLNFGCIHGGDNP-NRICGQCSLEFDLRPLPGMQPK 268
Cdd:cd03893 236 vrelpeeefrLDAGvleEVeiiggttgsvaERLWTRPALTV----LGIDGGFPGEGSkTVIPPRARAKISIRLVPGQDPE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 269 QLREAIRQRLrplaERH-----QVSIDYQPLF-PAVPPFeqaqDSELVRvaerlTGHRAEAVAFGTEAPY---------- 332
Cdd:cd03893 312 EASRLLEAHL----EKHapsgaKVTVSYVEGGmPWRSDP----SDPAYQ-----AAKDALRTAYGVEPPLtreggsipfi 378
|
410 420 430
....*....|....*....|....*....|....*.
gi 15600399 333 --FQR-LGSETLVLGAGDIAC-AHQPDEHLELARIE 364
Cdd:cd03893 379 svLQEfPQAPVLLIGVGDPDDnAHSPNESLRLGNYK 414
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
3-376 |
2.17e-19 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 88.92 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 3 LPSLKDqfgaLIAASSVSCTQPELDQtnrpVVDLLASWLGDLGFRCEIREVSPGKF-NLLASY-GSGPGGLVLAGHTDTV 80
Cdd:PRK06133 40 LDTLKE----LVSIESGSGDAEGLKQ----VAALLAERLKALGAKVERAPTPPSAGdMVVATFkGTGKRRIMLIAHMDTV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 81 pYDEALWSSDPLRLDerDGRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQ--PLMILATCDEESSMAGARALAESgrpLG 158
Cdd:PRK06133 112 -YLPGMLAKQPFRID--GDRAYGPGIADDKGGVAVILHALKILQQLGFKDygTLTVLFNPDEETGSPGSRELIAE---LA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 159 R---ATVIGEPT----NLRPIRlhKGVMMERIEILGQSGHS-SDPNLGRSAL-EAMHatigELMALRGEWQrawnnpqfS 229
Cdd:PRK06133 186 AqhdVVFSCEPGrakdALTLAT--SGIATALLEVKGKASHAgAAPELGRNALyELAH----QLLQLRDLGD--------P 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 230 VPQPTLNFGCIHGGDNPNRICGQCSLEFDLRPLpgmQP-------KQLREAIRQRLRPLAERhQVSIDyqplfPAVPPFE 302
Cdd:PRK06133 252 AKGTTLNWTVAKAGTNRNVIPASASAQADVRYL---DPaefdrleADLQEKVKNKLVPDTEV-TLRFE-----RGRPPLE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 303 QAQDSE-LVRVAERL---TGHRAEAVAF----GTEAPYFQRLGS----ETL-VLGAGdiacAHQPDEHLELARIEPMVGV 369
Cdd:PRK06133 323 ANAASRaLAEHAQGIygeLGRRLEPIDMgtggGTDAAFAAGSGKaavlEGFgLVGFG----AHSNDEYIELNSIVPRLYL 398
|
....*..
gi 15600399 370 LRRLIQH 376
Cdd:PRK06133 399 LTRMIME 405
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
13-215 |
1.21e-18 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 86.53 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 13 LIAASSVSCTQPEldqtnrpVVDLLASWLGDLGFRCEIREvspGKFNLLASYGSGPGGLVLAGHTDTVPY-DEALWSSDP 91
Cdd:PRK13004 24 LIRIPSESGDEKR-------VVKRIKEEMEKVGFDKVEID---PMGNVLGYIGHGKKLIAFDAHIDTVGIgDIKNWDFDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 92 LRLDERDGRWYGLGSCDMKGFFPLAIEA--LLPLLDQPFRQPLMILATCDEE--SSMAGARALAESG-RPlgRATVIGEP 166
Cdd:PRK13004 94 FEGEEDDGRIYGRGTSDQKGGMASMVYAakIIKDLGLDDEYTLYVTGTVQEEdcDGLCWRYIIEEDKiKP--DFVVITEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15600399 167 TNLRPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMAL 215
Cdd:PRK13004 172 TDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEEL 220
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
12-364 |
1.95e-17 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 82.85 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 12 ALIAASSVSCTQPEldqtnrpVVDLLASWLGDLGFRcEIREVSPGkfNLLASYGSGPGGLVLAGHTDTVPY-DEALWSSD 90
Cdd:cd05649 6 DLIQIPSESGEEKG-------VVERIEEEMEKLGFD-EVEIDPMG--NVIGYIGGGKKKILFDGHIDTVGIgNIDNWKFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 91 PLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLD---QPFRQPLMILATCDEE--SSMAgARALAESGRPLGRATVIGE 165
Cdd:cd05649 76 PYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDlglRDFAYTILVAGTVQEEdcDGVC-WQYISKADKIKPDFVVSGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 166 PTNLRPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGEWQRAwnnpqfsvpqPTLNFGCIHGGD- 244
Cdd:cd05649 155 PTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFPEA----------PFLGRGTLTVTDi 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 245 ---NPNR--ICGQCSLEFDLRPLPGmqpkQLREAIRQRLRPLA----ERHQVSIDY---------------QPLFPA-VP 299
Cdd:cd05649 225 fstSPSRcaVPDSCRISIDRRLTVG----ETWEGCLEEIRALPavkkYGDDVAVSMynydrpsytgevyesERYFPTwLL 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600399 300 PfeqaQDSELVRVA----ERLTGHRAEAV--AFGTEAPYFQ-RLGSETLVLGAGDIACAHQPDEHLELARIE 364
Cdd:cd05649 301 P----EDHELVKALleayKALFGARPLIDkwTFSTNGVSIMgRAGIPCIGFGPGAENQAHAPNEYTWKEDLV 368
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
30-195 |
3.84e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 82.74 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 30 NRPVVDLLASWLGDLGFR---CEIREVSPGKFNLLASY-GSGPGG-LVLAGHTDTVPYDEALWSSDPLRLDERDGRWYGL 104
Cdd:PRK09133 58 TTPAAEAMAARLKAAGFAdadIEVTGPYPRKGNLVARLrGTDPKKpILLLAHMDVVEAKREDWTRDPFKLVEENGYFYGR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 105 GSCDMKGFFPLAIEALLPLLDQPF--RQPLMILATCDEESS-MAGARALAESGRPLGRAT-VIGEPTNLRPIRLHKGVMM 180
Cdd:PRK09133 138 GTSDDKADAAIWVATLIRLKREGFkpKRDIILALTGDEEGTpMNGVAWLAENHRDLIDAEfALNEGGGGTLDEDGKPVLL 217
|
170 180
....*....|....*....|....*.
gi 15600399 181 E-----------RIEILGQSGHSSDP 195
Cdd:PRK09133 218 TvqagektyadfRLEVTNPGGHSSRP 243
|
|
| dapE-gram_pos |
TIGR01900 |
succinyl-diaminopimelate desuccinylase; This model represents a clade of ... |
2-372 |
1.18e-16 |
|
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: 80.41 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 2 PLPSLKDQFGALIAASSVSCTQpeldqtnRPVVDLLASWLGDLGFRceirEVSPGKFNLLASYGSG-PGGLVLAGHTDTV 80
Cdd:TIGR01900 1 LTEDLAELTAALVDIPSVSGDE-------RALADAVESALRALPHL----EVIRHGNSVVARTNLGrPSRVILAGHLDTV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 81 PYDEALwssdPLRLDerDGRWYGLGSCDMKG--FFPLAIEALLPLLDqPFRQPLMILATCDE-ESSMAGARALAESGRPL 157
Cdd:TIGR01900 70 PIADNL----PSRVE--GGRLYGRGAVDMKGglAVMLALAATLDRTE-PRHDLTLVFYEREEgPAEENGLGRLLREHPEW 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 158 GRA--TVIGEPTNLRpIRLH-KGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMAlrgewqRAWNNPQFS--VPQ 232
Cdd:TIGR01900 143 LAGdlAVLLEPTDGK-IEAGcQGTLRATVTFHGRRAHSARSWMGENAIHKAAPILARLAA------YEPREVTVDglTYR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 233 PTLNFGCIHGGDNPNRICGQCSLEFDLRPLPGmqpKQLREAiRQRLRPLAERHQVSIDYQPLFPAVPPFEQAQdselvrv 312
Cdd:TIGR01900 216 EGLNAVRIEGGVAGNVIPDECEVNVNYRFAPD---RSLEQA-RAHVRELFEGDGAEVEVTDLSPGARPGLDNP------- 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15600399 313 aerLTGHRAEAVAFGTEAPY-------FQRLGSETLVLGAGDIACAHQPDEHLELARIEPMVGVLRR 372
Cdd:TIGR01900 285 ---LAAELVAAVGGEVRAKYgwtdvarFSALGIPAVNFGPGDPALAHQDDEHVPVAQLTACAAILRR 348
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
59-372 |
3.67e-16 |
|
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: 78.64 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 59 NLLASYGSGPGGLV-LAGHTDTVPYDEALwssdPLRLDErDGRWYGLGSCDMKG----FFPLAIEALLPLLDqpfRQPLM 133
Cdd:cd05647 43 TVVARTERGLASRViLAGHLDTVPVAGNL----PSRVEE-DGVLYGCGATDMKAgdavQLKLAATLAAATLK---HDLTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 134 ILATCDE-ESSMAGARALAESGRPLGRA--TVIGEPTNLRPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIG 210
Cdd:cd05647 115 IFYDCEEvAAELNGLGRLAEEHPEWLAAdfAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 211 ELMALRgewqrawnnpqfsvPQPT----------LNFGCIHGGDNPNRICGQCSLEFDLRPLPGmqpKQLREAIrQRLRP 280
Cdd:cd05647 195 RLAAYE--------------PRTVnidgltyregLNAVFISGGVAGNVIPDEARVNLNYRFAPD---KSLAEAI-AHVRE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 281 LAERHQVSIDYQPLFPAVPPfeqAQDSELVRVAERLTGHRAEAVAFGTEAPYFQRLGSETLVLGAGDIACAHQPDEHLEL 360
Cdd:cd05647 257 VFEGLGYEIEVTDLSPGALP---GLDHPVARDLIEAVGGKVRAKYGWTDVARFSALGIPAVNFGPGDPLLAHKRDEQVPV 333
|
330
....*....|..
gi 15600399 361 ARIEPMVGVLRR 372
Cdd:cd05647 334 EQITACAAILRR 345
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
31-377 |
3.89e-16 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 78.94 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 31 RPVVDLLASWLGDLGFRCEIREVSpgkfNLLASYGSGPG----GLVLAGHTDTVPydeaLWSSDPLRLDERDGRWYG--- 103
Cdd:COG2195 23 EALADYLVEELKELGLEVEEDEAG----NVIATLPATPGynvpTIGLQAHMDTVP----QFPGDGIKPQIDGGLITAdgt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 104 --LGSCDMKGffpLA--IEALLPLLDQ----PfrqPLMILATCDEESSMAGARALAES-----------GRPLGRAtVIG 164
Cdd:COG2195 95 ttLGADDKAG---VAaiLAALEYLKEPeiphG---PIEVLFTPDEEIGLRGAKALDVSklgadfaytldGGEEGEL-EYE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 165 EPTnlrpirlhkGVMMErIEILGQSGHSSD-PNLGRSALEAMHATIGELmalrgewqrawnnPQFSVPQPT-LNFGCIHG 242
Cdd:COG2195 168 CAG---------AADAK-ITIKGKGGHSGDaKEKMINAIKLAARFLAAL-------------PLGRIPEETeGNEGFIHG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 243 GDNPNRICGQCSLEFDLRPLpgmQPKQLR---EAIRQRLRPLAERH---QVSIDYQPLFPAvppFEQAQDSELVRVAERL 316
Cdd:COG2195 225 GSATNAIPREAEAVYIIRDH---DREKLEarkAELEEAFEEENAKYgvgVVEVEIEDQYPN---WKPEPDSPIVDLAKEA 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600399 317 ---TGHRAEAVAF--GTEAPYFQRLGSETLVLGAGdIACAHQPDEHLELARIEPMVGVLRRLIQHY 377
Cdd:COG2195 299 yeeLGIEPKIKPIrgGLDGGILSFKGLPTPNLGPG-GHNFHSPDERVSIESMEKAWELLVEILKLI 363
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
30-360 |
5.68e-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: 78.75 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 30 NRPVVDLLASWLGDLGFRCEiREVSPGKF----------NLLA--SYGSGPGGLVLAGHTDTVPYDEAlWSSDPLRLDER 97
Cdd:cd02697 24 NAPHAERTAALLQGFGFEAE-RHPVPEAEvraygmesitNLIVrrRYGDGGRTVALNAHGDVVPPGDG-WTRDPYGAVVE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 98 DGRWYGLGSCDMKG---FFPLAIEALlPLLDQPFRQPLMILATCDEE-SSMAGARALAESG--RPlgrATVIGEPTNLRP 171
Cdd:cd02697 102 DGVMYGRAAAVSKSdfaSFTFAVRAL-ESLGAPLRGAVELHFTYDEEfGGELGPGWLLRQGltKP---DLLIAAGFSYEV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 172 IRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGEWQRAWNNPQfSVPQPTLNFGCIHGGDNPNRICG 251
Cdd:cd02697 178 VTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNAQYRQVSSQVE-GITHPYLNVGRIEGGTNTNVVPG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 252 QCSLEFDLRPLPGMQPKQLREAIRQRLR-PLAERHQVSIDYQPLFPAVPPFEQAQDSELVRV----AERLTGHRAEA--V 324
Cdd:cd02697 257 KVTFKLDRRMIPEENPVEVEAEIRRVIAdAAASMPGISVDIRRLLLANSMRPLPGNAPLVEAiqthGEAVFGEPVPAmgT 336
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15600399 325 AFGTEAPYFQRLGSETLVLGAGDI----ACAHQPDEHLEL 360
Cdd:cd02697 337 PLYTDVRLYAEAGIPGVIYGAGPRtvleSHAKRADERLQL 376
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
31-381 |
1.30e-15 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 77.77 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 31 RPVVDLLASWLGDLGFRCEIREVSPGKFNLLA----SYGSGPGGLVLAGHTD--TVPYDEAlWSSDPLRLDERDGRWYGL 104
Cdd:PRK08596 36 NEAQEFIAEFLRKLGFSVDKWDVYPNDPNVVGvkkgTESDAYKSLIINGHMDvaEVSADEA-WETNPFEPTIKDGWLYGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 105 GSCDMKGFFPLAIEALLPLLDQPFRQP--LMILATCDEESSMAGARALAESG--------------RPLGRATVI-GEPT 167
Cdd:PRK08596 115 GAADMKGGLAGALFAIQLLHEAGIELPgdLIFQSVIGEEVGEAGTLQCCERGydadfavvvdtsdlHMQGQGGVItGWIT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 168 NLRPIRLHKGVMMERIeilgqsgHSSDPNLGRSALEAMHATIGELMALRGEWQRAWNNPQFSVPQPTLNFGCIHGGDNPN 247
Cdd:PRK08596 195 VKSPQTFHDGTRRQMI-------HAGGGLFGASAIEKMMKIIQSLQELERHWAVMKSYPGFPPGTNTINPAVIEGGRHAA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 248 RICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAER---------------HQVSIDYQPLFPAVP-PFEQAQDSELVR 311
Cdd:PRK08596 268 FIADECRLWITVHFYPNETYEQVIKEIEEYIGKVAAAdpwlrenppqfkwggESMIEDRGEIFPSLEiDSEHPAVKTLSS 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15600399 312 VAERLTGHRAE-----AVafgTEAPYFQRLGSETLVLGAGDIACAHQPDEHLELARIEPMVGVLRRLIQHYCLTP 381
Cdd:PRK08596 348 AHESVLSKNAIldmstTV---TDGGWFAEFGIPAVIYGPGTLEEAHSVNEKVEIEQLIEYTKVITAFIYEWCHTK 419
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
23-341 |
3.24e-15 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 76.37 E-value: 3.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 23 QPELDQTnrPVVDLLASWLGDLGFRCEIREVSPGK-FNLLASYGSGPG--GLVLAGHTDTVPYDEALWSSDPLRLD-ERD 98
Cdd:TIGR01880 25 QPNPDYA--ACVDFLIKQADELGLARKTIEFVPGKpVVVLTWPGSNPElpSILLNSHTDVVPVFREHWTHPPFSAFkDED 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 99 GRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQPLMILAT--CDEE-SSMAGARALAESG--RPLGRATVIGE----PTN- 168
Cdd:TIGR01880 103 GNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISfvPDEEiGGHDGMEKFAKTDefKALNLGFALDEglasPDDv 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 169 LRPIRLHKGVMMERIEILGQSGHSSD--PNlgrSALEAMHATIGELMALR-GEWQRAWNNPQFSVPQ-PTLNFGCIHGGD 244
Cdd:TIGR01880 183 YRVFYAERVPWWVVVTAPGNPGHGSKlmEN---TAMEKLEKSVESIRRFReSQFQLLQSNPDLAIGDvTSVNLTKLKGGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 245 NPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAErhQVSIDYQPLFPAVPP------------FEQAQDSELVRV 312
Cdd:TIGR01880 260 QSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAGE--GVTYEFSQHSGKPLVtphddsnpwwvaFKDAVKEMGCTF 337
|
330 340
....*....|....*....|....*....
gi 15600399 313 aerltghRAEAVAFGTEAPYFQRLGSETL 341
Cdd:TIGR01880 338 -------KPEILPGSTDSRYIRAAGVPAL 359
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
59-153 |
6.46e-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: 72.85 E-value: 6.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 59 NLLASYGSGPGG--LVLAGHTDTVP-YDEALWSSDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQP--LM 133
Cdd:cd18669 1 NVIARYGGGGGGkrVLLGAHIDVVPaGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKgtVV 80
|
90 100
....*....|....*....|
gi 15600399 134 ILATCDEESSMAGARALAES 153
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLSK 100
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
59-153 |
9.84e-13 |
|
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: 66.29 E-value: 9.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 59 NLLASYGSGPGG--LVLAGHTDTVPYDE-ALWSSDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQP--LM 133
Cdd:cd03873 1 NLIARLGGGEGGksVALGAHLDVVPAGEgDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKgtIV 80
|
90 100
....*....|....*....|
gi 15600399 134 ILATCDEESSMAGARALAES 153
Cdd:cd03873 81 VAFTADEEVGSGGGKGLLSK 100
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
31-377 |
1.16e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 68.72 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 31 RPVVDLLASWLGDLGFRCEIREVSPGKFNLLASY-GSGP--GGLVLAGHTDTVPYDEALWSSDPLRLDERDGRWYGLGSC 107
Cdd:PRK07906 25 REAAEYVAEKLAEVGLEPTYLESAPGRANVVARLpGADPsrPALLVHGHLDVVPAEAADWSVHPFSGEIRDGYVWGRGAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 108 DMKGFFPLAIEALLPLLDQPFRQP--LMILATCDEESSMA-GARALAESGRPL--GRATVIGE--------PTNLR--PI 172
Cdd:PRK07906 105 DMKDMDAMMLAVVRHLARTGRRPPrdLVFAFVADEEAGGTyGAHWLVDNHPELfeGVTEAISEvggfsltvPGRDRlyLI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 173 RL-HKGVMMERIEILGQSGHSSDPN--------------LGR--------SALEAMHATIGELMALrgEWQRawNNPQFS 229
Cdd:PRK07906 185 ETaEKGLAWMRLTARGRAGHGSMVNddnavtrlaeavarIGRhrwplvltPTVRAFLDGVAELTGL--EFDP--DDPDAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 230 VPQ--PTLNF--GCIHGGDNP---------NRICGQCSLEFDLRPLPGMQpKQLREAIRQRLRPLAERHQVSIDyqplfp 296
Cdd:PRK07906 261 LAKlgPAARMvgATLRNTANPtmlkagykvNVIPGTAEAVVDGRFLPGRE-EEFLATVDELLGPDVEREWVHRD------ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 297 avPPFEQAQDSELV-RVAERLTGHRAEAVAF------GTEAPYFQRLGSE-----TLVLGAG-D-IACAHQPDEHLELAR 362
Cdd:PRK07906 334 --PALETPFDGPLVdAMNAALLAEDPGARVVpymlsgGTDAKAFSRLGIRcygfaPLRLPPDlDfAALFHGVDERVPVDA 411
|
410
....*....|....*
gi 15600399 363 IEPMVGVLRRLIQHY 377
Cdd:PRK07906 412 LRFGVRVLDRFLRTC 426
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
23-300 |
1.33e-11 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 65.37 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 23 QPELDQTnrPVVDLLASWLGDLGFRCEIREVSPGKFNLLASY-GSGPG--GLVLAGHTDTVPYDEALWSSDPLR--LDEr 97
Cdd:cd05646 18 HPNPDYD--ACVEFLKRQADELGLPVRVIEVVPGKPVVVLTWeGSNPElpSILLNSHTDVVPVFEEKWTHDPFSahKDE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 98 DGRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQPLMILATC--DEE-SSMAGARALAESgrPLGRATVIG--------EP 166
Cdd:cd05646 95 DGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFvpDEEiGGHDGMEKFVKT--EEFKKLNVGfaldeglaSP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 167 TNlrPIRLHKGvmmER------IEILGQSGHSSD--PNlgrSALEAMHATIGELMALR-GEWQRAWNNPQFSVPQ-PTLN 236
Cdd:cd05646 173 TE--EYRVFYG---ERspwwvvITAPGTPGHGSKllEN---TAGEKLRKVIESIMEFReSQKQRLKSNPNLTLGDvTTVN 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600399 237 FGCIHGGDNPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAErhQVSIDYQPLFPAVPP 300
Cdd:cd05646 245 LTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGR--GVTYEFEQKSPEKDP 306
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
3-367 |
1.12e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 62.62 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 3 LPSLKDQFGALIAASSVSCTqPELDQTNRPVVDLLASWLGDLGFRCEIREVSPGKFNLLASYGSGPGG--LVLAGHTDTV 80
Cdd:PRK07907 17 LPRVRADLEELVRIPSVAAD-PFRREEVARSAEWVADLLREAGFDDVRVVSADGAPAVIGTRPAPPGAptVLLYAHHDVQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 81 PY-DEALWSSDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLDQPfrqPLMI--LATCDEESSMAGARALAESGRPL 157
Cdd:PRK07907 96 PPgDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRALGGDL---PVGVtvFVEGEEEMGSPSLERLLAEHPDL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 158 GRATVI----------GEP---TNLRpirlhkGVMMERIEI--LGQSGHSS---------------------DPNlGRSA 201
Cdd:PRK07907 173 LAADVIviadsgnwsvGVPaltTSLR------GNADVVVTVrtLEHAVHSGqfggaapdaltalvrllatlhDED-GNVA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 202 LEAMHATIG---------------------ELMAlRGEW-QRAWNNPQFSVpqptLNFGCIHGGDNPNRICGQCSLEFDL 259
Cdd:PRK07907 246 VDGLDATEPwlgvdydeerfradagvldgvELIG-TGSVaDRLWAKPAITV----IGIDAPPVAGASNALPPSARARLSL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 260 RPLPGMQPKQLREAIRQRLRPLAERH-QVSIDYQplfPAVPPFEQAQDSELVRVAErltghRAEAVAFGTEA-------- 330
Cdd:PRK07907 321 RVAPGQDAAEAQDALVAHLEAHAPWGaHVTVERG---DAGQPFAADASGPAYDAAR-----AAMREAWGKDPvdmgmggs 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 15600399 331 ----PYFQRL--GSETLVLGAGDIAC-AHQPDEHLELARIEPMV 367
Cdd:PRK07907 393 ipfiAELQEAfpQAEILVTGVEDPKTrAHSPNESVHLGELERAA 436
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
13-119 |
1.44e-10 |
|
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: 62.62 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 13 LIAASSVSCtQPELDQTNRPVVDLLASWLGDLGFRCEIREVSPGKFN----------LLASYGSGPGG--LVLAGHTDTV 80
Cdd:cd05676 19 AVAIQSVSA-DPEKRPELIRMMEWAAERLEKLGFKVELVDIGTQTLPdgeelplppvLLGRLGSDPSKktVLIYGHLDVQ 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15600399 81 PYD-EALWSSDPLRLDERDGRWYGLGSCDMKGffPL-----AIEA 119
Cdd:cd05676 98 PAKlEDGWDTDPFELTEKDGKLYGRGSTDDKG--PVlgwlnAIEA 140
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
35-260 |
1.89e-10 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 61.72 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 35 DLLASWLGDLGFRCEIREVSpgkfnllASYGSGPGGLVLAGHTDTVP-YDEALWSSDPLrlderdgrwYGLGSCDMKGff 113
Cdd:PRK00466 34 KFFEKISNELNLKLEILPDS-------NSFILGEGDILLASHVDTVPgYIEPKIEGEVI---------YGRGAVDAKG-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 114 PLA--IEALLPLLDQPFRqpLMILATCDEESSMAGARALAESG-RPLgrATVIGEPTNLRPIRL-HKGVMMERIEILGQS 189
Cdd:PRK00466 96 PLIsmIIAAWLLNEKGIK--VMVSGLADEESTSIGAKELVSKGfNFK--HIIVGEPSNGTDIVVeYRGSIQLDIMCEGTP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600399 190 GHSSDPNlgRSALEAMHATIGELmalrgeWQRAWNNPQFSVpQPTLnfgcIHGGDNPNRICGQCSLEFDLR 260
Cdd:PRK00466 172 EHSSSAK--SNLIVDISKKIIEV------YKQPENYDKPSI-VPTI----IRAGESYNVTPAKLYLHFDVR 229
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
3-134 |
3.87e-10 |
|
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: 61.20 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 3 LPSLKDqfgaLIAASSVSCTQPELDQTnrpvVDLLASWLGDLGFRCEIREvSPGKFNLLASYGSG-PGGLVLAGHTDTVP 81
Cdd:cd05681 2 LEDLRD----LLKIPSVSAQGRGIPET----ADFLKEFLRRLGAEVEIFE-TDGNPIVYAEFNSGdAKTLLFYNHYDVQP 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15600399 82 YDE-ALWSSDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQPLMI 134
Cdd:cd05681 73 AEPlELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNI 126
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
182-355 |
4.91e-10 |
|
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: 60.31 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 182 RIEILGQSGHSSDPNLGRSALEAMHATIGELMAL--RgewqrawnnpQFSVPQP-TLNFGCIHGGDNPNRICGQCSLEFD 258
Cdd:cd03886 175 EITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVvsR----------ELDPLEPaVVTVGKFHAGTAFNVIPDTAVLEGT 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 259 LRplpGMQPkQLREAIRQRLRPLAER------HQVSIDYQPLFPAVppfeqAQDSELV----RVAERLTGHRAEAVA--- 325
Cdd:cd03886 245 IR---TFDP-EVREALEARIKRLAEGiaaaygATVELEYGYGYPAV-----INDPELTelvrEAAKELLGEEAVVEPepv 315
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600399 326 FGTE--APYFQRLGSETLVLGAGD----IACAHQPD 355
Cdd:cd03886 316 MGSEdfAYYLEKVPGAFFWLGAGEpdgeNPGLHSPT 351
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
67-256 |
5.26e-10 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 60.57 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 67 GPGGLVLAGHTDTVPYDEALwSSDPLRldeRDG-RWYGLGSCDMKGFFPLAIEALLPLLDQPFRQPLMI--LATCDEESS 143
Cdd:PRK07473 74 GEPGILIAGHMDTVHPVGTL-EKLPWR---REGnKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPItvLFTPDEEVG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 144 MAGARALAESGRPLGRATVIGEPTnlrpiRLHKGVMMER-------IEILGQSGHS-SDPNLGRSALEAMHATIGELMAL 215
Cdd:PRK07473 150 TPSTRDLIEAEAARNKYVLVPEPG-----RPDNGVVTGRyaiarfnLEATGRPSHAgATLSEGRSAIREMARQILAIDAM 224
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15600399 216 RGEwqrawnNPQFSVpqptlnfGCIHGGDNPNRICGQCSLE 256
Cdd:PRK07473 225 TTE------DCTFSV-------GIVHGGQWVNCVATTCTGE 252
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
33-177 |
2.77e-08 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 55.16 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 33 VVDLLASWlgdlGFRCEIREVSpGKFNLLASYGSGPGGLVLAGHTDTVPYDEALWSSDPLRLDERDGRWYGLGSCDMKGF 112
Cdd:PRK08554 33 IKDTLESW----GIESELIEKD-GYYAVYGEIGEGKPKLLFMAHFDVVPVNPEEWNTEPFKLTVKGDKAYGRGSADDKGN 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600399 113 FPLAIEALLPLLDQPFRQPLMILATCDEESSMAGARALAESGRPLGRA---TVIGEPTNLRPI-RLHKG 177
Cdd:PRK08554 108 VASVMLALKELSKEPLNGKVIFAFTGDEEIGGAMAMHIAEKLREEGKLpkyMINADGIGMKPIiRRRKG 176
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
71-318 |
3.88e-08 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 54.58 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 71 LVLAGHTDTV-----PYDEALWssdplrLDerDGRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQPL--MILATCDEE-S 142
Cdd:PRK07338 95 VLLTGHMDTVfpadhPFQTLSW------LD--DGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLgyDVLINPDEEiG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 143 SMAGARALAESGRPlGRATVIGEPT----NLRPIRlhKGVMMERIEILGQSGHSS-DPNLGRSALEAMHATIGELMALRG 217
Cdd:PRK07338 167 SPASAPLLAELARG-KHAALTYEPAlpdgTLAGAR--KGSGNFTIVVTGRAAHAGrAFDEGRNAIVAAAELALALHALNG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 218 ewQRawnnpqfsvPQPTLNFGCIHGGDNPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAERHQVSIDYQPLFPA 297
Cdd:PRK07338 244 --QR---------DGVTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHGVSLHLHGGFGR 312
|
250 260
....*....|....*....|....
gi 15600399 298 VP-PFEQAQDS--ELVRVAERLTG 318
Cdd:PRK07338 313 PPkPIDAAQQRlfEAVQACGAALG 336
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
51-375 |
4.53e-08 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 54.56 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 51 REVSPGkFNLLASY-GSGPGG--LVLAGHTDTVPYD---EALWSSDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLL 124
Cdd:PRK08262 92 REVVGG-HSLLYTWkGSDPSLkpIVLMAHQDVVPVApgtEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 125 DQPF--RQPLMILATCDEESSMAGARALAE--------------SGRPLGRATV--IGEPTNLRPIrLHKGVMMERIEIL 186
Cdd:PRK08262 171 AQGFqpRRTIYLAFGHDEEVGGLGARAIAEllkergvrlafvldEGGAITEGVLpgVKKPVALIGV-AEKGYATLELTAR 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 187 GQSGHSSDP----NLGR-----SALEA------MHATIGEL-------------MALRGEW--------QRAWNNPQFSV 230
Cdd:PRK08262 250 ATGGHSSMPprqtAIGRlaralTRLEDnplpmrLRGPVAEMfdtlapemsfaqrVVLANLWlfeplllrVLAKSPETAAM 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 231 PQPTLNFGCIHGGDNPNRICGQCSLEFDLRPLPGmqpkQLREAIRQRLRPLAerHQVSIDYQPLF-----PAVPPFEQAQ 305
Cdd:PRK08262 330 LRTTTAPTMLKGSPKDNVLPQRATATVNFRILPG----DSVESVLAHVRRAV--ADDRVEIEVLGgnsepSPVSSTDSAA 403
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15600399 306 DSELVRVAERLTGHRAEAVAF---GTEAPYFQRLGSET-----LVLGAGDIACAHQPDEHLELARIEPMVGVLRRLIQ 375
Cdd:PRK08262 404 YKLLAATIREVFPDVVVAPYLvvgATDSRHYSGISDNVyrfspLRLSPEDLARFHGTNERISVANYARMIRFYYRLIE 481
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
8-373 |
4.81e-08 |
|
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: 54.62 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 8 DQFGALIAASSVScTQPELDQTNRPVVDLLASWLGDLGFRcEIREVSPGKFNLL-ASYGSGPGG--LVLAGHTDTVPYD- 83
Cdd:cd05680 2 EELFELLRIPSVS-ADPAHKGDVRRAAEWLADKLTEAGFE-HTEVLPTGGHPLVyAEWLGAPGAptVLVYGHYDVQPPDp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 84 EALWSSDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLDQPFRQPLMI--LATCDEESSMAGARALAESGRPLGRAT 161
Cdd:cd05680 80 LELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVkfLIEGEEEIGSPSLPAFLEENAERLAAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 162 VI----------GEPT---NLRPI------------RLHKGV--------MMERIEILGqSGHSSDpnlGRSALEAMHAT 208
Cdd:cd05680 160 VVlvsdtsmwspDTPTityGLRGLayleisvtgpnrDLHSGSyggavpnpANALARLLA-SLHDED---GRVAIPGFYDD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 209 IGELMAlrgEWQRAWNNPQFS---------VP----------------QPTLNFGCIHGG----DNPNRICGQCSLEFDL 259
Cdd:cd05680 236 VRPLTD---AEREAWAALPFDeaafkaslgVPalggeagyttlerlwaRPTLDVNGIWGGyqgeGSKTVIPSKAHAKISM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 260 RPLPGMQPKQLREAIRQRLRPLAERHqVSIDYQPLFPAvPPFEQAQDSELVRVAErltghRAEAVAFGTEaPYFQR---- 335
Cdd:cd05680 313 RLVPGQDPDAIADLLEAHLRAHAPPG-VTLSVKPLHGG-RPYLVPTDHPALQAAE-----RALEEAFGKP-PVFVReggs 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 15600399 336 ----------LGSETLVLGAG--DIAcAHQPDEHLELAR----IEPMVGVLRRL 373
Cdd:cd05680 385 ipivalfekvLGIPTVLMGFGlpDDA-IHAPNEKFRLECfhkgIEAIAHLLARL 437
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
24-275 |
1.08e-07 |
|
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: 53.23 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 24 PELDQTNRPVVDLLASWLGDLGFRCEIREVS--PGKFNLLASY-GSGPGGLV--LAGHTDTVPYDEALWSSDPLRLdERD 98
Cdd:cd08012 29 PKEDNAGRHVLEALTPYSTENGGPLVIDHVSyvKGRGNIIVEYpGTVDGKTVsfVGSHMDVVTANPETWEFDPFSL-SID 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 99 G-RWYGLGSCDMKGFFPLAIEALLPLLDQ--PFRQPLMILATCDEESSM---AGARALAESGR--PLGRATVIG-EPTNL 169
Cdd:cd08012 108 GdKLYGRGTTDCLGHVALVTELFRQLATEkpALKRTVVAVFIANEENSEipgVGVDALVKSGLldNLKSGPLYWvDSADS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 170 RPIRLHKGVMMERIEILGQSGHSSDPNLGRSALEAMHATIGELMalrgewQRAWNN----PQ-----FSVP---QPTLnF 237
Cdd:cd08012 188 QPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVMEALAEIQ------KRFYIDfpphPKeevygFATPstmKPTQ-W 260
|
250 260 270
....*....|....*....|....*....|....*...
gi 15600399 238 GCIHGGdnPNRICGQCSLEFDLRPLPGMQPKQLREAIR 275
Cdd:cd08012 261 SYPGGS--INQIPGECTICGDCRLTPFYDVKEVREKLE 296
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
62-142 |
3.07e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 52.00 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 62 ASYGSGPGGLVLAGHTDTVPY-DEALWSSDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLDQ--PFRQPLMILATC 138
Cdd:PRK07205 69 AEIGQGEELLAILCHLDVVPEgDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAgvQFNKRIRFIFGT 148
|
....
gi 15600399 139 DEES 142
Cdd:PRK07205 149 DEET 152
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
140-298 |
3.79e-07 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 51.50 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 140 EESSMAGARALAESGRPLGRATVIGE----PTNLRPIRLHKGVMMER-----IEILGQSGHSSDPNLGRSALEAMHATIg 210
Cdd:cd08021 134 EEVPPGGAKPMIEAGVLEGVDAVFGLhlwsTLPTGTIAVRPGAIMAApdefdITIKGKGGHGSMPHETVDPIVIAAQIV- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 211 elMALRGEWQRAWNnpqfSVPQPTLNFGCIHGGDNPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAERH--QVS 288
Cdd:cd08021 213 --TALQTIVSRRVD----PLDPAVVTIGTFQGGTSFNVIPDTVELKGTVRTFDEEVREQVPKRIERIVKGICEAYgaSYE 286
|
170
....*....|
gi 15600399 289 IDYQPLFPAV 298
Cdd:cd08021 287 LEYQPGYPVV 296
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
35-120 |
3.80e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 51.84 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 35 DLLASWLGDLGFRCEIREvSP----GKFnLLASYGSGPGGL-VLA-GHTDTVPYDEALWSS--DPLRLDERDGRWYGLGS 106
Cdd:PRK07079 48 DEIAPALAALGFTCRIVD-NPvaggGPF-LIAERIEDDALPtVLIyGHGDVVRGYDEQWREglSPWTLTEEGDRWYGRGT 125
|
90
....*....|....
gi 15600399 107 CDMKGFFPLAIEAL 120
Cdd:PRK07079 126 ADNKGQHTINLAAL 139
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
62-146 |
9.45e-07 |
|
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: 50.71 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 62 ASYGSGPGGLVLAGHTDTVPYDEaLWSSDPLRLDERDGRWYGLGSCDMKGFFPLAIEALLPLLD---QPFRQPLMILATc 138
Cdd:cd03888 65 AEYGEGEEVLGILGHLDVVPAGE-GWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDlglPLKKKIRLIFGT- 142
|
....*...
gi 15600399 139 DEESSMAG 146
Cdd:cd03888 143 DEETGWKC 150
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
137-358 |
3.47e-06 |
|
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: 48.60 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 137 TCDEESSMAGARAL------------AESGRPLGrATVIGEPTNlrpirlhkgvMMERIEILGQSGHSS-DPNLGRSALE 203
Cdd:cd05683 136 TVGEESGLVGAKALdpelidadygyaLDSEGDVG-TIIVGAPTQ----------DKINAKIYGKTAHAGtSPEKGISAIN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 204 AMHATIGELMALRGEwqrawnnpqfsvPQPTLNFGCIHGGDNPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAE 283
Cdd:cd05683 205 IAAKAISNMKLGRID------------EETTANIGKFQGGTATNIVTDEVNIEAEARSLDEEKLDAQVKHMKETFETTAK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 284 RHQVSIDYQpLFPAVPPFEQAQDSELVRVAERLTGH-----RAEAVAFGTEAPYFQRLGSETLVLGAGdIACAHQPDEHL 358
Cdd:cd05683 273 EKGAHAEVE-VETSYPGFKINEDEEVVKLAKRAANNlgleiNTTYSGGGSDANIINGLGIPTVNLGIG-YENIHTTNERI 350
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
56-195 |
1.27e-04 |
|
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: 43.78 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 56 GKFNLLASY-GSGPG--GLVLAGHTDTVP---YDEALWSSDPLRLDERDGRWYGLGSCDMK----GFFPlAIEALLPLLD 125
Cdd:cd05674 54 NEYGLLYTWeGSDPSlkPLLLMAHQDVVPvnpETEDQWTHPPFSGHYDGGYIWGRGALDDKnsliGILE-AVELLLKRGF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 126 QPFRQplMILAT-CDEESS-MAGARALAE----------------SGRPLGRATVIGEPTNLrPIRLHKGVMMERIEILG 187
Cdd:cd05674 133 KPRRT--IILAFgHDEEVGgERGAGAIAElllerygvdglaaildEGGAVLEGVFLGVPFAL-PGVAEKGYMDVEITVHT 209
|
....*...
gi 15600399 188 QSGHSSDP 195
Cdd:cd05674 210 PGGHSSVP 217
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
71-120 |
1.80e-04 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 43.26 E-value: 1.80e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15600399 71 LVLAGHTDTVPYDEALWSS--DPLRLDERDGRWYGLGSCDMKGFFPLAIEAL 120
Cdd:cd05679 75 LLIYGHGDVVPGYEGRWRDgrDPWTVTVWGERWYGRGTADNKGQHSINMAAL 126
|
|
| PRK12892 |
PRK12892 |
allantoate amidohydrolase; Reviewed |
35-299 |
5.20e-04 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 183817 [Multi-domain] Cd Length: 412 Bit Score: 42.00 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 35 DLLASWLGDLGfrCEIREVSPGkfNLLASY-GSGPGGLVLAG-HTDTVPYDEalwssdplRLDERDGRWYGLgscdmkgf 112
Cdd:PRK12892 43 RRLAAWCEAAG--LAVRIDGIG--NVFGRLpGPGPGPALLVGsHLDSQNLGG--------RYDGALGVVAGL-------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 113 fpLAIEALLPLLDQPfRQPLMILATCDEESS-----MAGARALA--------------ESGRPLGRA-TVIGEPTNLRP- 171
Cdd:PRK12892 103 --EAARALNEHGIAT-RHPLDVVAWCDEEGSrftpgFLGSRAYAgrldpadalaarcrSDGVPLRDAlAAAGLAGRPRPa 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 172 ---------IRLH--KGVMME------------------RIEILGQSGHS-SDPNLGRSalEAMHATIGELMALRGEWQR 221
Cdd:PRK12892 180 adrarpkgyLEAHieQGPVLEqaglpvgvvtgivgiwqyRITVTGEAGHAgTTPMALRR--DAGLAAAEMIAAIDEHFPR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 222 A-----WNNPQFSVPQptlnfgcihggDNPNRICGQCSLEFDLRPLPGMQPKQLREAIRQRLRPLAERHQVSIDYQPLFP 296
Cdd:PRK12892 258 VcgpavVTVGRVALDP-----------GSPSIIPGRVEFSFDARHPSPPVLQRLVALLEALCREIARRRGCRVSVDRIAE 326
|
...
gi 15600399 297 AVP 299
Cdd:PRK12892 327 YAP 329
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
182-285 |
2.41e-03 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 39.63 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 182 RIEILGQSGHSSDPNLGRSALEAMHATIGELmalrgewQRAWNNpQFSVPQP-TLNFGCIHGGDNPNRICGQCSLEFDLR 260
Cdd:cd08019 172 KIEVKGKGGHGSMPHQGIDAVLAAASIVMNL-------QSIVSR-EIDPLEPvVVTVGKLNSGTRFNVIADEAKIEGTLR 243
|
90 100
....*....|....*....|....*
gi 15600399 261 plpgmqpkQLREAIRQRLRPLAERH 285
Cdd:cd08019 244 --------TFNPETREKTPEIIERI 260
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
12-150 |
2.42e-03 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 40.02 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 12 ALIAASSVSCTQPEldqtnRPVVDLLASWLGDLG-FR-------CEIREVSPGKFNLLASY-GSGPG--GLVLAGHTDTV 80
Cdd:cd05654 9 SLVSWPSVTGTEGE-----RSFADFLKEILKELPyFKenpshvwQLLPPDDLGRRNVTALVkGKKPSkrTIILISHFDTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 81 PYDE-ALWSS---DPLRL-----------DER------DGRW-YGLGSCDMKGFFPLAIEALLPLL-DQPFRQPLMILAT 137
Cdd:cd05654 84 GIEDyGELKDiafDPDELtkafseyveelDEEvredllSGEWlFGRGTMDMKSGLAVHLALLEQASeDEDFDGNLLLMAV 163
|
170
....*....|...
gi 15600399 138 CDEESSMAGARAL 150
Cdd:cd05654 164 PDEEVNSRGMRAA 176
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
182-300 |
2.52e-03 |
|
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: 39.56 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 182 RIEILGQSGHSSDPNLGRSALEAMHATIGELMALRGEWQrawnNPQfsvpQPT-LNFGCIHGGDNPNRICGQCSLEFDLR 260
Cdd:cd08014 174 EIRIQGEGGHGARPHLTVDLVWAAAQVVTDLPQAISRRI----DPR----SPVvLTWGSIEGGRAPNVIPDSVELSGTVR 245
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15600399 261 PLP----GMQPKQLREAIRQRLRPLAERHQVSIDYqplfpAVPP 300
Cdd:cd08014 246 TLDpdtwAQLPDLVEEIVAGICAPYGAKYELEYRR-----GVPP 284
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
182-299 |
4.92e-03 |
|
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349920 [Multi-domain] Cd Length: 367 Bit Score: 38.78 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 182 RIEILGQSGHSSDPNLGRSALEAMHATIGEL--MALRGEwqrawNNPQFSVpqptLNFGCIHGGDNPNRICGQCSLEFDL 259
Cdd:cd05670 176 HIDFIGKSGHAAYPHNANDMVVAAANFVTQLqtIVSRNV-----DPIDGAV----VTIGKIHAGTARNVIAGTAHLEGTI 246
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 15600399 260 RplpGMQPKQLrEAIRQRLRPLAE------RHQVSIDYQPLFPAVP 299
Cdd:cd05670 247 R---TLTQEMM-ELVKQRVRDIAEgielafDCEVKVDLGQGYYPVE 288
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
12-111 |
6.99e-03 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 38.34 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600399 12 ALIAASSVScTQPELDQTNRPVVDLLASWLGDLGFRCEIREvSPGKFNLLASY-GSGPGGL-VL-AGHTDTVPYD-EALW 87
Cdd:PRK09104 25 ALLRIPSIS-TDPAYAADCRKAADWLVADLASLGFEASVRD-TPGHPMVVAHHeGPTGDAPhVLfYGHYDVQPVDpLDLW 102
|
90 100
....*....|....*....|....*....
gi 15600399 88 SSDPL--RLDER-DGR--WYGLGSCDMKG 111
Cdd:PRK09104 103 ESPPFepRIKETpDGRkvIVARGASDDKG 131
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
75-121 |
7.91e-03 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 38.19 E-value: 7.91e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15600399 75 GHTDTVPYDEA-LWSSDPLRLDERDGRWYGLGSCDMKG--FFPL-AIEALL 121
Cdd:PRK08201 86 GHYDVQPVDPLnLWETPPFEPTIRDGKLYARGASDDKGqvFMHLkAVEALL 136
|
|
| |
