|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
2-383 |
0e+00 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 825.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 2 KMNLPPFIEIYRALIATPSISATEEALDQSNATLINLLAGWFSDLGFKVEVQPVPGTRNKFNLLASAGQGAGGLLLTGHT 81
Cdd:PRK05111 1 KMKLPSFIEMYRALIATPSISATDPALDQSNRAVIDLLAGWFEDLGFNVEIQPVPGTRGKFNLLASLGSGEGGLLLAGHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 82 DTVPFDDGRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKPLYILATADEETSMAGARYFSENTSIR 161
Cdd:PRK05111 81 DTVPFDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAEATAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 162 PDCAIIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKERYHYDAFTVPYPTLNL 241
Cdd:PRK05111 161 PDCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQERYHNPAFTVPYPTLNL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 242 GSLHGGDASNRICACCELHMDIRPLPGMTLSDLDGLLNEALAPVSERWPGRLTVAELHPPIPGYECPPDHQLVEVVEKLL 321
Cdd:PRK05111 241 GHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSERWPGRITVAPLHPPIPGYECPADHQLVRVVEKLL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754936012 322 GEKTDVVNYCTEAPFIQTL-CPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVVHHFCWH 383
Cdd:PRK05111 321 GHKAEVVNYCTEAPFIQQLgCPTLVLGPGSIEQAHQPDEYLELSFIKPTRELLRQLIHHFCLH 383
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
10-377 |
0e+00 |
|
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: 581.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 10 EIYRALIATPSISATeealdqSNATLINLLAGWFSDLGFKVEVQPVPGTRNKFNLLASAGQ-GAGGLLLTGHTDTVPFDD 88
Cdd:TIGR01892 1 EILTKLVAFDSTSFR------PNVDLIDWAQAYLEALGFSVEVQPFPDGAEKSNLVAVIGPsGAGGLALSGHTDVVPYDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 89 GRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKPLYILATADEETSMAGARYFSENTSIRPDCAIIG 168
Cdd:TIGR01892 75 AAWTRDPFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIEAGAGRPRHAIIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 169 EPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKERYHYDAFTVPYPTLNLGSLHGGD 248
Cdd:TIGR01892 155 EPTRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDLDEGFTPPYTTLNIGVIQGGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 249 ASNRICACCELHMDIRPLPGMTLSDLDGLLNEALAPVSERWPGRLTVAELHPPIPGYECPPDHQLVEVVEKLLGEKTDVV 328
Cdd:TIGR01892 235 AVNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRDEPGFEVQIEVVSTDPGVNTEPDAELVAFLEELSGNAPEVV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 754936012 329 NYCTEAPFIQTL-CPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVV 377
Cdd:TIGR01892 315 SYGTEAPQFQELgAEAVVCGPGDIRQAHQPDEYVEIEDLVRCRAVLARLV 364
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
10-378 |
2.74e-169 |
|
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349889 [Multi-domain] Cd Length: 367 Bit Score: 477.08 E-value: 2.74e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 10 EIYRALIATPSISAteealdQSNATLINLLAGWFSDLGFKVEVQPVPgTRNKFNLLASAGQ-GAGGLLLTGHTDTVPFDD 88
Cdd:cd03894 1 ELLARLVAFDTVSR------NSNLALIEYVADYLAALGVKSRRVPVP-EGGKANLLATLGPgGEGGLLLSGHTDVVPVDG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 89 GRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKPLYILATADEETSMAGARYFSENTS---IRPDCA 165
Cdd:cd03894 74 QKWSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALAargGRPDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 166 IIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKERYHYDAFTVPYPTLNLGSLH 245
Cdd:cd03894 154 IVGEPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPFDPPYPTLNVGLIH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 246 GGDASNRICACCELHMDIRPLPGMTLSDLDGLLNEALAPVSERWPGRLTVAELHPPiPGYECPPDHQLVEVVEKLLGE-K 324
Cdd:cd03894 234 GGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPEAGIEVEPLFEV-PGLETDEDAPLVRLAAALAGDnK 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 754936012 325 TDVVNYCTEAPFIQTL-CPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVVH 378
Cdd:cd03894 313 VRTVAYGTEAGLFQRAgIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
1-381 |
2.86e-107 |
|
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: 320.29 E-value: 2.86e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 1 MKMNLPPFIEIYRALIATPSISATEEALdqsnatlINLLAGWFSDLGFKVEVQPVPGtrNKFNLLAS--AGQGAGGLLLT 78
Cdd:COG0624 7 IDAHLDEALELLRELVRIPSVSGEEAAA-------AELLAELLEALGFEVERLEVPP--GRPNLVARrpGDGGGPTLLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 79 GHTDTVPFDDG-RWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDVDVT--TLKKPLYILATADEETSMAGARYFS 155
Cdd:COG0624 78 GHLDVVPPGDLeLWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAglRLPGNVTLLFTGDEEVGSPGARALV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 156 ENTS--IRPDCAIIGEPTS-LQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIiqlrDSLKERYHYDAF 232
Cdd:COG0624 158 EELAegLKADAAIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAAL----RDLEFDGRADPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 233 tVPYPTLNLGSLHGGDASNRICACCELHMDIRPLPGMTLSDLDGLLNEALAPVSErwPGRLTVAELHPPIPGYECPPDHQ 312
Cdd:COG0624 234 -FGRTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAP--GVEVEVEVLGDGRPPFETPPDSP 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754936012 313 LVEVVEKLLGE------KTDVVNYCTEAPFIQTL--CPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVVHHFC 381
Cdd:COG0624 311 LVAAARAAIREvtgkepVLSGVGGGTDARFFAEAlgIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
9-362 |
1.07e-95 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 290.55 E-value: 1.07e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISATeealdqSNATLINLLAGWFSDLGFKVEVQPVPgTRNKFNLLASAG-QGAGGLLLTGHTDTVPFD 87
Cdd:PRK07522 7 LDILERLVAFDTVSRD------SNLALIEWVRDYLAAHGVESELIPDP-EGDKANLFATIGpADRGGIVLSGHTDVVPVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 88 DGRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKPLYILATADEETSMAGARYFSE---NTSIRPDC 164
Cdd:PRK07522 80 GQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPSMIArlpERGVKPAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 165 AIIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKERYHYDA-FTVPYPTLNLGS 243
Cdd:PRK07522 160 CIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLAAPGPFDAlFDPPYSTLQTGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 244 LHGGDASNRICACCELHMDIRPLPGMtlsDLDGLLNEALAPVSERWPGRLTVAELHPPI--------PGYECPPDHQLVE 315
Cdd:PRK07522 240 IQGGTALNIVPAECEFDFEFRNLPGD---DPEAILARIRAYAEAELLPEMRAVHPEAAIefeplsayPGLDTAEDAAAAR 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 754936012 316 VVEKLLG-EKTDVVNYCTEAPFIQTL-CPTLVLGPGSINQAHQPDEYLE 362
Cdd:PRK07522 317 LVRALTGdNDLRKVAYGTEAGLFQRAgIPTVVCGPGSIEQAHKPDEFVE 365
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
10-362 |
3.66e-81 |
|
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: 252.61 E-value: 3.66e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 10 EIYRALIATPSISATEEALDQsnatlinLLAGWFSDLGFKVEVQPVPGTRNkfnLLASAGQGAG-GLLLTGHTDTVPFDD 88
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAE-------YLAELLAKRGYGIESTIVEGRGN---LVATVGGGDGpVLLLNGHIDTVPPGD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 89 G-RWTRDPFTLTEHDNKLYGLGTADMKG-----FFAFIldALRDvDVTTLKKPLYILATADEETSMAGARYFSEN-TSIR 161
Cdd:cd08659 71 GdKWSFPPFSGRIRDGRLYGRGACDMKGglaamVAALI--ELKE-AGALLGGRVALLATVDEEVGSDGARALLEAgYADR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 162 PDCAIIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKERYhydafTVPYPTLNL 241
Cdd:cd08659 148 LDALIVGEPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPAHP-----LLGPPTLNV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 242 GSLHGGDASNRICACCELHMDIRPLPGMTLSDLDGLLNEALapvsERWPGRLTVAELHPPIPGYECPPDHQLVEVVEKLL 321
Cdd:cd08659 223 GVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAIL----EEHEAKLTVEVSLDGDPPFFTDPDHPLVQALQAAA 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 754936012 322 GEKTD-----VVNYCTEAPFI--QTLCPTLVLGPGSINQAHQPDEYLE 362
Cdd:cd08659 299 RALGGdpvvrPFTGTTDASYFakDLGFPVVVYGPGDLALAHQPDEYVS 346
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
9-377 |
1.50e-69 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 223.71 E-value: 1.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISATEEALDQsnatLINLLAGWFSDLGFKVEVQPVPGT------RNKFNLLASAGQGAGGLLLTGHTD 82
Cdd:PRK08651 9 VEFLKDLIKIPTVNPPGENYEE----IAEFLRDTLEELGFSTEIIEVPNEyvkkhdGPRPNLIARRGSGNPHLHFNGHYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 83 TVPFDDGRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDVDvTTLKKPLYILATADEETSMAGARYFSENTSIRP 162
Cdd:PRK08651 85 VVPPGEGWSVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLD-PAGDGNIELAIVPDEETGGTGTGYLVEEGKVTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 163 DCAIIGEPTSLQPI-RAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKERYHYDAFTVPYPTLNL 241
Cdd:PRK08651 164 DYVIVGEPSGLDNIcIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYEYDDERGAKPTVTL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 242 G--SLHGGDASNRICACCELHMDIRPLPGMTLSDLDGLLNEALAPVSERWPGRLTVAELhPPIPGYECPPDHQLVEVVEK 319
Cdd:PRK08651 244 GgpTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFEIT-PFSEAFVTDPDSELVKALRE 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754936012 320 LLGEKTDV---VNYCTEA----PFIQTLCPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVV 377
Cdd:PRK08651 323 AIREVLGVepkKTISLGGtdarFFGAKGIPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVL 387
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
76-379 |
2.21e-55 |
|
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: 184.47 E-value: 2.21e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 76 LLTGHTDTVPFDDGrwTRDPFTLTEhDNKLYGLGTADMKGFFAFILDALRDVDVTTLKK-PLYILATADEETSMAGARYF 154
Cdd:pfam01546 1 LLRGHMDVVPDEET--WGWPFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLKKgTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 155 SENTS---IRPDCAI---IGEPTSLQ------PIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDS 222
Cdd:pfam01546 78 IEDGLlerEKVDAVFglhIGEPTLLEggiaigVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 223 LKERYHYDAFTVpyptLNLGSLHGGdaSNRICACCELHMDIRPLPGMTLSDLDGLLNEALAPVSERWPGRLTVaELHPPI 302
Cdd:pfam01546 158 NVDPLDPAVVTV----GNITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEV-EYVEGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 303 PGYECpPDHQLV----EVVEKLLGEKTDVV----NYCTEAPFI-QTLCPTLV-LGPGSiNQAHQPDEYLETRFIKPTREL 372
Cdd:pfam01546 231 APPLV-NDSPLVaalrEAAKELFGLKVELIvsgsMGGTDAAFFlLGVPPTVVfFGPGS-GLAHSPNEYVDLDDLEKGAKV 308
|
....*..
gi 754936012 373 ITQVVHH 379
Cdd:pfam01546 309 LARLLLK 315
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
37-362 |
7.53e-55 |
|
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: 184.51 E-value: 7.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 37 NLLAGWFSDLGFKVEV-QPVPGTRNKFNLLaSAGQGAGGLLLTGHTDTVPFDDGR-WTRDPFTLTEHDNKLYGLGTADMK 114
Cdd:cd08011 25 AYIKLLLEDLGYPVELhEPPEEIYGVVSNI-VGGRKGKRLLFNGHYDVVPAGDGEgWTVDPYSGKIKDGKLYGRGSSDMK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 115 GFFAFILDALRDVDVTTLKKPLYILATA--DEET-SMAGARYFSENTSIRPDCAIIGEPTSLQPIR-AHKGHISTAVRVL 190
Cdd:cd08011 104 GGIAASIIAVARLADAKAPWDLPVVLTFvpDEETgGRAGTKYLLEKVRIKPNDVLIGEPSGSDNIRiGEKGLVWVIIEIT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 191 GQSGHSSDPARGVNAIELMHDAIGRIIQLRdslkeryhydaftvpyPTLNLGSLHGGDASNRICACCELHMDIRPLPGMT 270
Cdd:cd08011 184 GKPAHGSLPHRGESAVKAAMKLIERLYELE----------------KTVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGIS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 271 LSDLDGLLNEALAPVSERWPGRLTVAElhppipGYECPPDHQLVEVVEKLLGE------KTDVVNYCTEAPF-IQTLCPT 343
Cdd:cd08011 248 TDEVLSRIIDHLDSIEEVSFEIKSFYS------PTVSNPDSEIVKKTEEAITEvlgirpKEVISVGASDARFyRNAGIPA 321
|
330
....*....|....*....
gi 754936012 344 LVLGPGSINQAHQPDEYLE 362
Cdd:cd08011 322 IVYGPGRLGQMHAPNEYVE 340
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
9-362 |
1.37e-52 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 179.13 E-value: 1.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISATEEALDqsnaTLINLLAGWFSDLGFKVEVQPVPGTR---NKFNLLASAGQGAGGLL-LTGHTDTV 84
Cdd:TIGR01910 1 VELLKDLISIPSVNPPGGNEE----TIANYIKDLLREFGFSTDVIEITDDRlkvLGKVVVKEPGNGNEKSLiFNGHYDVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 85 PF-DDGRWTRDPFTLTEHDNKLYGLGTADMKGFFA---FILDALRDVDVtTLKKPLYILATADEETSMAGARYFSENTSI 160
Cdd:TIGR01910 77 PAgDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVallYALKAIREAGI-KPNGNIILQSVVDEESGEAGTLYLLQRGYF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 161 R-PDCAIIGEPTSLQPI-RAHKGHISTAVRVLGQSGHSSDPARGVNAIE-LMHDaigrIIQLRDSLKERYH-YDAFTVPY 236
Cdd:TIGR01910 156 KdADGVLIPEPSGGDNIvIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMkLAKL----ITELNELEEHIYArNSYGFIPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 237 P-TLNLGSLHGGDASNRICACCELHMDIRPLPGMtlsDLDGLLNEALAPVSERWPGRLTVAELHPP--IPG-YECPPDHQ 312
Cdd:TIGR01910 232 PiTFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEE---NLDEVKQIIEDVVKALSKSDGWLYENEPVvkWSGpNETPPDSR 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 754936012 313 LV----EVVEKLLGE--KTDVVNYCTEAPF-IQTLCPTLVLGPGSINQAHQPDEYLE 362
Cdd:TIGR01910 309 LVkaleAIIKKVRGIepEVLVSTGGTDARFlRKAGIPSIVYGPGDLETAHQVNEYIS 365
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
43-375 |
1.96e-46 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 162.75 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 43 FSDLGFKVEVQPVPGTRNkfNLLASAGQGAGGLLLTGHTDTV-PFDDGRWTRDPFTLTEHDNKLYGLGTADMKGFFAFIL 121
Cdd:PRK08588 32 FAKHGIESKIVKVNDGRA--NLVAEIGSGSPVLALSGHMDVVaAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 122 DALrdVDVTTLKKPLY----ILATADEETSMAGARYFSEN---TSIrpDCAIIGEPTSLQPIRAHKGHISTAVRVLGQSG 194
Cdd:PRK08588 110 IAM--IELKEQGQLLNgtirLLATAGEEVGELGAKQLTEKgyaDDL--DALIIGEPSGHGIVYAHKGSMDYKVTSTGKAA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 195 HSSDPARGVNAIELMHDAIGRIIQLRDSLKERYHYDAFTVPYPTLnlgsLHGGDASNRICACCELHMDIRPLPGMTLSDL 274
Cdd:PRK08588 186 HSSMPELGVNAIDPLLEFYNEQKEYFDSIKKHNPYLGGLTHVVTI----INGGEQVNSVPDEAELEFNIRTIPEYDNDQV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 275 DGLLNEALAPVSERWPGRLTVaEL---HPPIpgyECPPDHQLV----EVVEKLLGEKTDV--VNYCTEA----------P 335
Cdd:PRK08588 262 ISLLQEIINEVNQNGAAQLSL-DIysnHRPV---ASDKDSKLVqlakDVAKSYVGQDIPLsaIPGATDAssflkkkpdfP 337
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 754936012 336 FIqtlcptlVLGPGSINQAHQPDEYLET----RFIKPTRELITQ 375
Cdd:PRK08588 338 VI-------IFGPGNNLTAHQVDEYVEKdmylKFIDIYKEIIIQ 374
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
18-381 |
6.96e-44 |
|
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: 156.10 E-value: 6.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 18 TPSISATEEAldqSNATLINLLAGWFSDLGFKVEV-QPVPGTRNKFNLLASAGQGAGgLLLTGHTDTVPFDDgrWTRDPF 96
Cdd:cd08013 17 NPSLSATGGA---GEAEIATYVAAWLAHRGIEAHRiEGTPGRPSVVGVVRGTGGGKS-LMLNGHIDTVTLDG--YDGDPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 97 TLTEHDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKPLYILATADEETSMAGARYFSENTsIRPDCAIIGEPTSLQPI 176
Cdd:cd08013 91 SGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGLRGDVILAAVADEEDASLGTQEVLAAG-WRADAAIVTEPTNLQII 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 177 RAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKERyHYDAFTVPyPTLNLGSLHGGDASNRICAC 256
Cdd:cd08013 170 HAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALEEYQQELPER-PVDPLLGR-ASVHASLIKGGEEPSSYPAR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 257 CELHMDIRPLPGMTLSDLDGLLNEALAPVSERWPG---RLTVAELHPpiPGYECPPDHQLVEVV----EKLLGE--KTDV 327
Cdd:cd08013 248 CTLTIERRTIPGETDESVLAELTAILGELAQTVPNfsyREPRITLSR--PPFEVPKEHPFVQLVaahaAKVLGEapQIRS 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 754936012 328 VNYCTEAPFI-QTLCPTLVLGPgSINQAHQPDEYLETRFIKPTRELITQVVHHFC 381
Cdd:cd08013 326 ETFWTDAALLaEAGIPSVVFGP-SGAGLHAKEEWVDVESIRQLREVLSAVVREFC 379
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
8-361 |
1.60e-43 |
|
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: 153.97 E-value: 1.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 8 FIEIYRALIATPSISATEEALDqsnatliNLLAGWFSDLGFKVEVQPVPGTrNKFNLLASAGQGAG-GLLLTGHTDTVP- 85
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVG-------DFLAEYLESLGFTVEKQPVENK-DRFNVYAYPGSSRQpRVLLTSHIDTVPp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 86 -FddgrwtrdPFTLTEHDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKP--LYILATADEETSMAGARYFSENTSIRP 162
Cdd:cd05652 73 fI--------PYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEgdLGLLFVVGEETGGDGMKAFNDLGLNTW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 163 DCAIIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKERYHYDaftvpypTLNLG 242
Cdd:cd05652 145 DAVIFGEPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPSSELLGPT-------TLNIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 243 SLHGGDASNRICACCELHMDIRplpgMTLSDLDGL--LNEALA-------PVSERWPGRLTVAELHPPIPGYEcppdhql 313
Cdd:cd05652 218 RISGGVAANVVPAAAEASVAIR----LAAGPPEVKdiVKEAVAgiltdteDIEVTFTSGYGPVDLDCDVDGFE------- 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 754936012 314 vevvekllgekTDVVNYCTEAPFIQTLCPTLVLGPGSINQAHQPDEYL 361
Cdd:cd05652 287 -----------TDVVAYGTDIPYLKGDHKRYLYGPGSILVAHGPDEAI 323
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
9-362 |
6.92e-42 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 151.25 E-value: 6.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISATEEALdqsnatlINLLAGWFSDLGF-KVEVQPVpGtrnkfNLLASAGQGAGGLLLTGHTDTVPF- 86
Cdd:PRK13004 18 TRFLRDLIRIPSESGDEKRV-------VKRIKEEMEKVGFdKVEIDPM-G-----NVLGYIGHGKKLIAFDAHIDTVGIg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 87 DDGRWTRDPFTLTEHDNKLYGLGTADMKGFFA-------FILDALRDVDVTtlkkpLYILATADEET--SMAgARYFSEN 157
Cdd:PRK13004 85 DIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMAsmvyaakIIKDLGLDDEYT-----LYVTGTVQEEDcdGLC-WRYIIEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 158 TSIRPDCAIIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKERyhydaftvpyP 237
Cdd:PRK13004 159 DKIKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNLKED----------P 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 238 TLNLGSLHGGD---ASNRICAC---CELHMDIRPLPGMT----LSDLDGLLN--EALAPVSERWPGRLTVAELHPPI--- 302
Cdd:PRK13004 229 FLGKGTLTVSDifsTSPSRCAVpdsCAISIDRRLTVGETwesvLAEIRALPAvkKANAKVSMYNYDRPSYTGLVYPTecy 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754936012 303 -PGYECPPDHQLVEVVEK----LLGE--KTDVVNYCTEAPFIQTL--CPTLVLGPGSINQAHQPDEYLE 362
Cdd:PRK13004 309 fPTWLYPEDHEFVKAAVEaykgLFGKapEVDKWTFSTNGVSIAGRagIPTIGFGPGKEPLAHAPNEYTW 377
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
15-362 |
9.88e-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. 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: 145.53 E-value: 9.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 15 LIATPSISAtEEALDQSnatlinLLAGWFSDLGFKVEVQ---------------PVPGTRNKFNLLASA-GQGAGG--LL 76
Cdd:cd03895 6 LVRFPSLRG-EEAAAQD------LVAAALRSRGYTVDRWeidveklkhhpgfspVAVDYAGAPNVVGTHrPRGETGrsLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 77 LTGHTDTVPFDDGR-WTRDPFTLTEHDNKLYGLGTADMKGFFA---FILDALRDVDVTtLKKPLYILATADEETSMAGAR 152
Cdd:cd03895 79 LNGHIDVVPEGPVElWTRPPFEATIVDGWMYGRGAGDMKAGLAanlFALDALRAAGLQ-PAADVHFQSVVEEECTGNGAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 153 ------YfsentsiRPDCAIIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKER 226
Cdd:cd03895 158 aalmrgY-------RADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEREWNAR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 227 YHYD-AF-TVPYP-TLNLGSLHGGDASNRICACCELHMDIRPLPGMTLSDLDGLLNEALAPVS--ERWPGRltvaelHPP 301
Cdd:cd03895 231 KKSHpHFsDHPHPiNFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVADAAatDPWLSN------HPP 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754936012 302 --------IPGYECPPDHQLVEVV----EKLLGEK--TDVVNYCTEAPFIQTL--CPTLVLGPGSINqAHQPDEYLE 362
Cdd:cd03895 305 evewngfqAEGYVLEPGSDAEQVLaaahQAVFGTPpvQSAMTATTDGRFFVLYgdIPALCYGPGSRD-AHGFDESVD 380
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
9-362 |
2.16e-37 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 137.83 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISATEEALdqsnatlINLLAGWFSDLGFKVEvqpvpgtRNKFNLLASAGQGAGG---LLLTGHTDTVP 85
Cdd:cd05651 3 IELLKSLIATPSFSREEHKT-------ADLIENYLEQKGIPFK-------RKGNNVWAENGHFDEGkptLLLNSHHDTVK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 86 FDDGrWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDV-DVTTLKKPLYILATADEETSmaGARYFSentSIRP-- 162
Cdd:cd05651 69 PNAG-WTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLySEGPLNYNLIYAASAEEEIS--GKNGIE---SLLPhl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 163 ---DCAIIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPaRGVNAIelmHDAIGRIIQLRDSLKERYHYdafTVPYPTL 239
Cdd:cd05651 143 pplDLAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAARN-EGDNAI---YKALDDIQWLRDFRFDKVSP---LLGPVKM 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 240 NLGSLHGGDASNRICACCELHMDIRPLPGMTLSD----LDGLLNEALAPVSERwpgrltvaeLHPPipgyECPPDHQLVE 315
Cdd:cd05651 216 TVTQINAGTQHNVVPDSCTFVVDIRTTEAYTNEEifeiIRGNLKSEIKPRSFR---------LNSS----AIPPDHPIVQ 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 754936012 316 VVEKlLGEKTDVVNYCTEAPFIQtlCPTLVLGPGSINQAHQPDEYLE 362
Cdd:cd05651 283 AAIA-AGRTPFGSPTLSDQALMP--FPSVKIGPGDSSRSHTADEFIE 326
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
47-361 |
4.94e-37 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 137.64 E-value: 4.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 47 GFKVEVqpVPGTRNKFNLLASAGQGAggLLLTGHTDTVPFDDGrWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRD 126
Cdd:PRK08737 42 GFQVEV--IDHGAGAVSLYAVRGTPK--YLFNVHLDTVPDSPH-WSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 127 VDvttlkKPLYILATADEE--TSMAGARYFSenTSIRPDCAIIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDP-ARGV 203
Cdd:PRK08737 117 GD-----GDAAFLFSSDEEanDPRCVAAFLA--RGIPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKqDPSA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 204 NAIelmHDAIGRIIQLRDSLKERYHYDAFTVPYPTLNLGSLHGGDASNRICACCELHMDIRPLPGMtlsDLDGLLnEALA 283
Cdd:PRK08737 190 SAL---HQAMRWGGQALDHVESLAHARFGGLTGLRFNIGRVEGGIKANMIAPAAELRFGFRPLPSM---DVDGLL-ATFA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 284 PVSERWPGRLTVAELHPPIPGYECPPDHQ----LVEVVEKLLGEKTDVVNYCTEAP-FIQTLCPTLVLGPGSINQAHQPD 358
Cdd:PRK08737 263 GFAEPAAATFEETFRGPSLPSGDIARAEErrlaARDVADALDLPIGNAVDFWTEASlFSAAGYTALVYGPGDIAQAHTAD 342
|
...
gi 754936012 359 EYL 361
Cdd:PRK08737 343 EFV 345
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
9-362 |
8.68e-37 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 137.17 E-value: 8.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISATEEALdqsnatlINLLAGWFSDLGF-KVEVQPVPgtrnkfNLLASAGQGAGGLLLTGHTDTVPF- 86
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGV-------VERIEEEMEKLGFdEVEIDPMG------NVIGYIGGGKKKILFDGHIDTVGIg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 87 DDGRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALR---DVDVTTLKKPLYILATADEET--SMAgARYFSENTSIR 161
Cdd:cd05649 68 NIDNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKimkDLGLRDFAYTILVAGTVQEEDcdGVC-WQYISKADKIK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 162 PDCAIIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQlrdsLKERYHYDAFtVPYPTLNL 241
Cdd:cd05649 147 PDFVVSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQ----LNPNFPEAPF-LGRGTLTV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 242 GSLHggDASNRICAC---CELHMDIRPLPGMTlsdLDGLLNE--ALAPVSE---------------RWPGrlTVAELHPP 301
Cdd:cd05649 222 TDIF--STSPSRCAVpdsCRISIDRRLTVGET---WEGCLEEirALPAVKKygddvavsmynydrpSYTG--EVYESERY 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754936012 302 IPGYECPPDHQLV----EVVEKLLGEK--TDVVNYCTEAPFIQ--TLCPTLVLGPGSINQAHQPDEYLE 362
Cdd:cd05649 295 FPTWLLPEDHELVkallEAYKALFGARplIDKWTFSTNGVSIMgrAGIPCIGFGPGAENQAHAPNEYTW 363
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
9-373 |
7.47e-33 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 125.64 E-value: 7.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISATEEALdqsnatlINLLAGWFSDLGFKVEVQPVpgtRNKFNLLASAGqgaGGLLLTGHTDTVPFdd 88
Cdd:PRK08652 5 KELLKQLVKIPSPSGQEDEI-------ALHIMEFLESLGYDVHIESD---GEVINIVVNSK---AELFVEVHYDTVPV-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 89 grwTRDPFtltEHDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKPLYILATADEETSMAGARYFSEntSIRPDCAIIG 168
Cdd:PRK08652 70 ---RAEFF---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSDEEEGGRGSALFAE--RYRPKMAIVL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 169 EPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKERYHydaftvpyPTLNLGSLHGGD 248
Cdd:PRK08652 142 EPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFD--------PHIGIQEIIGGS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 249 ASNRICACCELHMDIRPLPGMTLSD----LDGLLNEALA--PVSERWpgrltvaelhppiPGYECPPDHQLVEVVEKLLG 322
Cdd:PRK08652 214 PEYSIPALCRLRLDARIPPEVEVEDvldeIDPILDEYTVkyEYTEIW-------------DGFELDEDEEIVQLLEKAMK 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754936012 323 EK------------TDVVNycteapFIQTLCPTLVLGPGSINQAHQPDEYLETRFIKPTRELI 373
Cdd:PRK08652 281 EVglepeftvmrswTDAIN------FRYNGTKTVVWGPGELDLCHTKFERIDVREVEKAKEFL 337
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
11-323 |
4.14e-29 |
|
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: 117.08 E-value: 4.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 11 IYRALIAtpsISATEEALDQSNAT-LINLLAGWFSDLGFKVEVQPVPGTRNKFNLLAS---AGQGAGGLLLTGHTDTVPF 86
Cdd:cd05675 3 LLQELIR---IDTTNSGDGTGSETrAAEVLAARLAEAGIQTEIFVVESHPGRANLVARiggTDPSAGPLLLLGHIDVVPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 87 DDGRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDV--DVTTLKKPLYILATADEET-SMAGARYFSENtsiRPD 163
Cdd:cd05675 80 DASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYkrEGFKPKRDLVFAFVADEEAgGENGAKWLVDN---HPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 164 C------AI---------IGEPTSLQPIR-AHKGHISTAVRVLGQSGHSSDPARGvNAIELMHDAIGRI------IQLRD 221
Cdd:cd05675 157 LfdgatfALneggggslpVGKGRRLYPIQvAEKGIAWMKLTVRGRAGHGSRPTDD-NAITRLAEALRRLgahnfpVRLTD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 222 SLKERYHYDAFTVPY-------------PTLN-LGS-----------------LHGGDASNRICACCELHMDIRPLPG-- 268
Cdd:cd05675 236 ETAYFAQMAELAGGEggalmltavpvldPALAkLGPsapllnamlrntasptmLDAGYATNVLPGRATAEVDCRILPGqs 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 754936012 269 --MTLSDLDGLLNEAlapvserwpgRLTVAELHPPiPGYECPPDHQLVEVVEKLLGE 323
Cdd:cd05675 316 eeEVLDTLDKLLGDP----------DVSVEAVHLE-PATESPLDSPLVDAMEAAVQA 361
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
8-362 |
9.58e-29 |
|
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: 115.00 E-value: 9.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 8 FIEIYRALIATPSISATEEALDQsnatLINLLAGWFSDLGFKVEVQPVPGTRNkfNLLA-SAGQGAGGLLLTGHTDTVpF 86
Cdd:cd03885 1 MLDLLERLVNIESGTYDKEGVDR----VAELLAEELEALGFTVERRPLGEFGD--HLIAtFKGTGGKRVLLIGHMDTV-F 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 87 DDGRWTRDPFTltEHDNKLYGLGTADMKGFFAFILDALRDVDVT--TLKKPLYILATADEETSMAGARYFSENTSIRPDC 164
Cdd:cd03885 74 PEGTLAFRPFT--VDGDRAYGPGVADMKGGLVVILHALKALKAAggRDYLPITVLLNSDEEIGSPGSRELIEEEAKGADY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 165 AIIGEPTSL--QPIRAHKGHISTAVRVLGQSGHSS-DPARGVNAI-ELMHdaigRIIQLRDSLKeryhYDAFTvpypTLN 240
Cdd:cd03885 152 VLVFEPARAdgNLVTARKGIGRFRLTVKGRAAHAGnAPEKGRSAIyELAH----QVLALHALTD----PEKGT----TVN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 241 LGSLHGGDASNRICACCELHMDIRplpGMTLSDLDGLLNEALAPVSER-WPG---RLTVAELHPPIPgyECPPDHQLVEV 316
Cdd:cd03885 220 VGVISGGTRVNVVPDHAEAQVDVR---FATAEEADRVEEALRAIVATTlVPGtsvELTGGLNRPPME--ETPASRRLLAR 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 754936012 317 VEKLLGE--KTDV---------VNYcTEAPFIQTLCPTLVLGPGsinqAHQPDEYLE 362
Cdd:cd03885 295 AQEIAAElgLTLDweatgggsdANF-TAALGVPTLDGLGPVGGG----AHTEDEYLE 346
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
9-360 |
1.77e-28 |
|
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: 114.14 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISATEealdqsnATLINLLAGWFSDLGFKVEVQPVPGTRNkfnLLASAGQGAGGLLLTGHTDTVPF-D 87
Cdd:cd03891 1 LELAKELIRRPSVTPDD-------AGAQDLIAERLKALGFTCERLEFGGVKN---LWARRGTGGPHLCFAGHTDVVPPgD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 88 DGRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKP--LYILATADEETS-----------MAgARyf 154
Cdd:cd03891 71 LEGWSSDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKgsISFLITSDEEGPaidgtkkvlewLK-AR-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 155 sentSIRPDCAIIGEPTSLQPI-------RahKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQlrdslkerY 227
Cdd:cd03891 148 ----GEKIDYCIVGEPTSEKKLgdtikigR--RGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTA--------T 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 228 HYDAFTVPYP--TLNLGSLHGG-DASNRICACCELHMDIRPLPGMTLSDL----DGLLNEALAPVSERW----------P 290
Cdd:cd03891 214 VLDEGNEFFPpsSLQITNIDVGnGATNVIPGELKAKFNIRFNDEHTGESLkariEAILDKHGLDYDLEWklsgepfltkP 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754936012 291 GRLTVAelhppipgyecppdhqLVEVVEKLLGEKTDVVNY--CTEAPFI-QTLCPTLVLGPgsINQ-AHQPDEY 360
Cdd:cd03891 294 GKLVDA----------------VSAAIKEVTGITPELSTSggTSDARFIaSYGCPVVEFGL--VNAtIHKVNER 349
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
9-362 |
1.63e-27 |
|
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: 111.29 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISATEEALDQsnatlinLLAGWFSDLGFKVEVQPVPgtrnkfNLLASAGQGAGGLLLTGHTDTVPfdd 88
Cdd:cd05653 4 VELLLDLLSIYSPSGEEARAAK-------FLEEIMKELGLEAWVDEAG------NAVGGAGSGPPDVLLLGHIDTVP--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 89 grwtrDPFTLTEHDNKLYGLGTADMKG-FFAFILDALRDVDVTTLKkpLYILATADEETSMAGARYFSEnTSIRPDCAII 167
Cdd:cd05653 68 -----GEIPVRVEGGVLYGRGAVDAKGpLAAMILAASALNEELGAR--VVVAGLVDEEGSSKGARELVR-RGPRPDYIII 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 168 GEPTSLQPIR-AHKGHISTAVRVLGQSGHSSDPARgvNAIELMHDAIGRIIQlRDSLKERYHYDAFTVpYPTLnlgsLHG 246
Cdd:cd05653 140 GEPSGWDGITlGYRGSLLVKIRCEGRSGHSSSPER--NAAEDLIKKWLEVKK-WAEGYNVGGRDFDSV-VPTL----IKG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 247 GDASNRICACCELHMDIRPLPGMTLSDldgLLNEALAPVSErwpGRLTVAELHPPipgYECPPDHQLVEV----VEKLLG 322
Cdd:cd05653 212 GESSNGLPQRAEATIDLRLPPRLSPEE---AIALATALLPT---CELEFIDDTEP---VKVSKNNPLARAfrraIRKQGG 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 754936012 323 EKTDVVNYCTE-----APFIQtlCPTLVLGPGSINQAHQPDEYLE 362
Cdd:cd05653 283 KPRLKRKTGTSdmnvlAPLWT--VPIVAYGPGDSTLDHTPNEHIE 325
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
177-290 |
4.74e-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: 4.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 177 RAHKGHISTAVRVLGQSGHSSDPARGVNAIELMhdaigriIQLRDSLKERYHYDAFTVPYPTLNLGSLHGGDASNRICAC 256
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLL-------ARLLAELPAEYGDIGFDFPRTTLNITGIEGGTATNVIPAE 73
|
90 100 110
....*....|....*....|....*....|....
gi 754936012 257 CELHMDIRPLPGMTLSDLDGLLNEALAPVSERWP 290
Cdd:pfam07687 74 AEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
13-360 |
5.81e-27 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 110.86 E-value: 5.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 13 RALIATPSISaTEEALDQsnatliNLLAGWFSDLGFKV---EVQPV-----PGT-------RNKFNLLASA-GQGAGG-- 74
Cdd:PRK06837 27 QDLVRFPSTR-GAEAPCQ------DFLARAFRERGYEVdrwSIDPDdlkshPGAgpveidySGAPNVVGTYrPAGKTGrs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 75 LLLTGHTDTVPFDD-GRWTRDPFTLTEHDNKLYGLGTADMKGFFA---FILDALRDVDVTtLKKPLYILATADEETSMAG 150
Cdd:PRK06837 100 LILQGHIDVVPEGPlDLWSRPPFDPVIVDGWMYGRGAADMKAGLAamlFALDALRAAGLA-PAARVHFQSVIEEESTGNG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 151 A-----RYFsentsiRPDCAIIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKE 225
Cdd:PRK06837 179 AlstlqRGY------RADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRELEAEWNA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 226 RYHYDAF--TVPYP-TLNLGSLHGGDASNRICACCELHMDIRPLPGMTLSD----LDGLLNEALApvSERWPGRltvael 298
Cdd:PRK06837 253 RKASDPHfeDVPHPiNFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAADaqaeIEACLAAAAR--DDRFLSN------ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 299 HPP--------IPGYECPPDhqlvEVVEKLLGEKTDVVnycTEAPfIQTLC----------------PTLVLGPGSINqA 354
Cdd:PRK06837 325 NPPevvwsgflAEGYVLEPG----SEAEAALARAHAAV---FGGP-LRSFVttaytdtrfyglyygiPALCYGPSGEG-I 395
|
....*.
gi 754936012 355 HQPDEY 360
Cdd:PRK06837 396 HGFDER 401
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
15-364 |
1.39e-26 |
|
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: 108.72 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 15 LIATPSISATEEALDQsnatlinLLAGWFSDLGF-KVEVQPVpgtrnkFNLLAS-AGQGAG-GLLLTGHTDTVPFDDgrw 91
Cdd:cd03896 7 LGEIPAPTFREGARAD-------LVAEWMADLGLgDVERDGR------GNVVGRlRGTGGGpALLFSAHLDTVFPGD--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 92 trDPFTLTEHDNKLYGLGTADMKGFFAFIL---DALRDVDVTtLKKPLYILATADEETS--MAGARYFSENTSIRPDCAI 166
Cdd:cd03896 71 --TPATVRHEGGRIYGPGIGDNKGSLACLLamaRAMKEAGAA-LKGDVVFAANVGEEGLgdLRGARYLLSAHGARLDYFV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 167 IGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMhdaigriIQLRDSLKErYHYDAftVPYPTLNLGSLHG 246
Cdd:cd03896 148 VAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAM-------AKLVEALYE-WAAPY--VPKTTFAAIRGGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 247 GDASNRICACCELHMDIRPLPGMTLSDLDgllNEALAPVSErwpgrltVAELHPPI----------PGYECPPDHQLVEV 316
Cdd:cd03896 218 GTSVNRIANLCSMYLDIRSNPDAELADVQ---REVEAVVSK-------LAAKHLRVkarvkpvgdrPGGEAQGTEPLVNA 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 754936012 317 VEKLLGEKTDVVNY---CTEA-PFIQTLCPTLVLGPGSINQAHQPDEYLETR 364
Cdd:cd03896 288 AVAAHREVGGDPRPgssSTDAnPANSLGIPAVTYGLGRGGNAHRGDEYVLKD 339
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
8-362 |
6.48e-26 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 107.06 E-value: 6.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 8 FIEiyraLIATPSISATEEALdqsnatlINLLAGWFSDLGFKVEVqpvpgtRNKFNLL----ASAGQGAGGLLLTGHTDT 83
Cdd:COG2195 9 FLE----YVKIPTPSDHEEAL-------ADYLVEELKELGLEVEE------DEAGNVIatlpATPGYNVPTIGLQAHMDT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 84 VP----------FDDGRWTRDPFTLtehdnklygLGtADMKGFFAFILDALRDVDVTTLK-KPLYILATADEETSMAGAR 152
Cdd:COG2195 72 VPqfpgdgikpqIDGGLITADGTTT---------LG-ADDKAGVAAILAALEYLKEPEIPhGPIEVLFTPDEEIGLRGAK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 153 YFSENTsIRPDCAII---GEPTSLQpirahkghISTA------VRVLGQSGHSSD-PARGVNAIELMHDAIGRIIQLRDs 222
Cdd:COG2195 142 ALDVSK-LGADFAYTldgGEEGELE--------YECAgaadakITIKGKGGHSGDaKEKMINAIKLAARFLAALPLGRI- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 223 lkeryhyDAFTvpypTLNLGSLHGGDASNRICACCELHMDIRPLpgmtlsDLDGL------LNEALAPVSERWP-GRLTV 295
Cdd:COG2195 212 -------PEET----EGNEGFIHGGSATNAIPREAEAVYIIRDH------DREKLearkaeLEEAFEEENAKYGvGVVEV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 296 aELHPPIPGYECPPDHQLVEVVEKL---LGEKtdvvnycteaPFIQ-----TLC--------PTLVLGPGsINQAHQPDE 359
Cdd:COG2195 275 -EIEDQYPNWKPEPDSPIVDLAKEAyeeLGIE----------PKIKpirggLDGgilsfkglPTPNLGPG-GHNFHSPDE 342
|
...
gi 754936012 360 YLE 362
Cdd:COG2195 343 RVS 345
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
9-376 |
3.99e-25 |
|
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: 104.45 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISATEEAL-DQSNATLINLLagwfsdlgfKVEVqpvpgTRNKFNLLASAGQG-AGGLLLTGHTDTVPF 86
Cdd:cd05647 2 IELTAALVDIPSVSGNEKPIaDEIEAALRTLP---------HLEV-----IRDGNTVVARTERGlASRVILAGHLDTVPV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 87 DD---GRWtrdpftltEHDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKPLYILATADEETSMAG------ARYFSEN 157
Cdd:cd05647 68 AGnlpSRV--------EEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLTLIFYDCEEVAAELnglgrlAEEHPEW 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 158 TSIrpDCAIIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRdslKERYHYDAFTVpYP 237
Cdd:cd05647 140 LAA--DFAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLAAYE---PRTVNIDGLTY-RE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 238 TLNLGSLHGGDASNRICACCELHMDIRPLPgmtlsdlDGLLNEALAPVSERWPG---RLTVAELHP-PIPGYECPPDHQL 313
Cdd:cd05647 214 GLNAVFISGGVAGNVIPDEARVNLNYRFAP-------DKSLAEAIAHVREVFEGlgyEIEVTDLSPgALPGLDHPVARDL 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754936012 314 VEVVEKLLGEK---TDVvnycteAPFIQTLCPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQV 376
Cdd:cd05647 287 IEAVGGKVRAKygwTDV------ARFSALGIPAVNFGPGDPLLAHKRDEQVPVEQITACAAILRRW 346
|
|
| PRK06915 |
PRK06915 |
peptidase; |
69-381 |
5.75e-24 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 102.46 E-value: 5.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 69 GQGAG-GLLLTGHTDTVPFDD-GRWTRDPFTLTEHDNKLYGLGTADMKG-----FFAfiLDALRDVDVtTLKKPLYILAT 141
Cdd:PRK06915 89 GSGGGkSMILNGHIDVVPEGDvNQWDHHPYSGEVIGGRIYGRGTTDMKGgnvalLLA--MEALIESGI-ELKGDVIFQSV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 142 ADEETSMAGaryfSENTSIR---PDCAIIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIE-LMH--DAIGR 215
Cdd:PRK06915 166 IEEESGGAG----TLAAILRgykADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEkSMFviDHLRK 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 216 IIQLR-----DSLkeryhYDAFTVPYPtLNLGSLHGGDASNRICACCELHMDIRPLPGMTLSDLDGLLNEALA------- 283
Cdd:PRK06915 242 LEEKRndritDPL-----YKGIPIPIP-INIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAelndvde 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 284 -----PVSERWPGRLTVaelhppiPGyECPPDHQLVEVV----EKLLGEK--TDVVNYCTEAPFIQTL--CPTLVLGPGS 350
Cdd:PRK06915 316 wfvehPVEVEWFGARWV-------PG-ELEENHPLMTTLehnfVEIEGNKpiIEASPWGTDGGLLTQIagVPTIVFGPGE 387
|
330 340 350
....*....|....*....|....*....|.
gi 754936012 351 INQAHQPDEYLETRFIKPTRELITQVVHHFC 381
Cdd:PRK06915 388 TKVAHYPNEYIEVDKMIAAAKIIALTLLDWC 418
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
9-360 |
1.38e-22 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 97.85 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISATEE-ALDqsnatlinLLAGWFSDLGFKVEVQPVPGTRNkfnLLASAGQGAGGLLLTGHTDTVPF- 86
Cdd:PRK13009 5 LELAQDLIRRPSVTPDDAgCQD--------LLAERLEALGFTCERMDFGDVKN---LWARRGTEGPHLCFAGHTDVVPPg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 87 DDGRWTRDPFTLTEHDNKLYGLGTADMKGFFA-FILDALRDVDVTTLKKP-LYILATADEETS-----------MAgARy 153
Cdd:PRK13009 74 DLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAaFVVAAERFVAAHPDHKGsIAFLITSDEEGPaingtvkvlewLK-AR- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 154 fsentSIRPDCAIIGEPTSLQPI-------RahKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQlrdslker 226
Cdd:PRK13009 152 -----GEKIDYCIVGEPTSTERLgdvikngR--RGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAA-------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 227 YHYDAFTVPYP--TLNLGSLHGG-DASNRICACCELHMDIRPLPGMTLSDLDGLLNEALAPVSERW-------------- 289
Cdd:PRK13009 217 TEWDEGNEFFPptSLQITNIDAGtGATNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDYtlewtlsgepfltp 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 290 PGRLTVAelhppipgyecppdhqLVEVVEKLLGEKT---------DvvnycteAPFIQTLCPTLV-LGPgsINQ-AHQPD 358
Cdd:PRK13009 297 PGKLVDA----------------VVAAIEAVTGITPelstsggtsD-------ARFIADYGAQVVeFGP--VNAtIHKVN 351
|
..
gi 754936012 359 EY 360
Cdd:PRK13009 352 EC 353
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
6-377 |
3.25e-22 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 97.01 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 6 PPFIEIYRALIATPSISATEEALDQsnatLINLLAGWFSDLGFKVEVQPVPGTRNKfNLLAS-AGQGAGGLLLTGHTDTV 84
Cdd:PRK06133 37 PAYLDTLKELVSIESGSGDAEGLKQ----VAALLAERLKALGAKVERAPTPPSAGD-MVVATfKGTGKRRIMLIAHMDTV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 85 pFDDGRWTRDPFTltEHDNKLYGLGTADMKGFFAFILDA---LRDV---DVTTLKkplyILATADEETSMAGARYFSENT 158
Cdd:PRK06133 112 -YLPGMLAKQPFR--IDGDRAYGPGIADDKGGVAVILHAlkiLQQLgfkDYGTLT----VLFNPDEETGSPGSRELIAEL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 159 SIRPDCAIIGEPT----SLqpIRAHKGhISTA-VRVLGQSGHS-SDPARGVNA-IELMHdaigRIIQLRDSLKEryhyda 231
Cdd:PRK06133 185 AAQHDVVFSCEPGrakdAL--TLATSG-IATAlLEVKGKASHAgAAPELGRNAlYELAH----QLLQLRDLGDP------ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 232 ftVPYPTLNLGSLHGGDASNRICACCELHMDIRPL-PGMT---LSDLDGLLNEALAPVSERwpgRLTVAELHPPIPgyEC 307
Cdd:PRK06133 252 --AKGTTLNWTVAKAGTNRNVIPASASAQADVRYLdPAEFdrlEADLQEKVKNKLVPDTEV---TLRFERGRPPLE--AN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 308 PPDHQLV--------------EVVEKLLGEKTD--VVNYCTEAPFIQTLCptlVLGPGsinqAHQPDEYLETRFIKPTRE 371
Cdd:PRK06133 325 AASRALAehaqgiygelgrrlEPIDMGTGGGTDaaFAAGSGKAAVLEGFG---LVGFG----AHSNDEYIELNSIVPRLY 397
|
....*.
gi 754936012 372 LITQVV 377
Cdd:PRK06133 398 LLTRMI 403
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
9-367 |
2.31e-21 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 94.45 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSI---SATEEALDQSNAtlinlLAGWFSDLGFK-VEVQPVPGTRNKF--NLLASAGQGAGGLL-LTGHT 81
Cdd:cd05650 4 IELERDLIRIPAVnpeSGGEGEKEKADY-----LEKKLREYGFYtLERYDAPDERGIIrpNIVAKIPGGNDKTLwIISHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 82 DTVPFDD-GRWTRDPFTLTEHDNKLYGLGTAD-MKGFFA--FILDALRDVDVTTlKKPLYILATADEET-SMAGARYFSE 156
Cdd:cd05650 79 DTVPPGDlSLWETDPWEPVVKDGKIYGRGVEDnQQGIVSslLALKAIIKNGITP-KYNFGLLFVADEEDgSEYGIQYLLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 157 NTSI-RPDCAII----GEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAielMHDAIGRIIQLRDSLKERYHY-- 229
Cdd:cd05650 158 KFDLfKKDDLIIvpdfGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINA---FVAASNFALELDELLHEKFDEkd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 230 DAFTVPYPTLNLGSLHGG-DASNRICACCELHMDIRPLPGMTLSDLDGLLNEALAPVSERWPGRLTVAELHPPIPGYECP 308
Cdd:cd05650 235 DLFNPPYSTFEPTKKEANvPNVNTIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDFENSYGAGITYEIVQKEQAPPATP 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754936012 309 PD----HQLVEVVEKLLGEKTDV--VNYCTEAPFIQTL-CPTLVLGPGsINQAHQPDEYletRFIK 367
Cdd:cd05650 315 EDseivVRLSKAIKKVRGREAKLigIGGGTVAAFLRKKgYPAVVWSTL-DETAHQPNEY---IRIS 376
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
9-362 |
3.21e-21 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 93.48 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISATEEALDQsnatlinLLAGWFSDLGFKVEVQPVpGtrnkfNLLASAGQGAGGLLLTGHTDTVPFD- 87
Cdd:PRK04443 9 RELLKGLVEIPSPSGEEAAAAE-------FLVEFMESHGREAWVDEA-G-----NARGPAGDGPPLVLLLGHIDTVPGDi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 88 -----DGrwtrdpftltehdnKLYGLGTADMKG-FFAFILDALRdvDVTTLKKPLYILATADEETSMAGARYFSENTsIR 161
Cdd:PRK04443 76 pvrveDG--------------VLWGRGSVDAKGpLAAFAAAAAR--LEALVRARVSFVGAVEEEAPSSGGARLVADR-ER 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 162 PDCAIIGEPTSLQPIR-AHKGHISTAVRVLGQSGHSSDParGVNAIELMHDAIGRIIQLRDSLKERYH-YDAFTvpyPTL 239
Cdd:PRK04443 139 PDAVIIGEPSGWDGITlGYKGRLLVTYVATSESFHSAGP--EPNAAEDAIEWWLAVEAWFEANDGRERvFDQVT---PKL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 240 NlgSLHGGDASNRICAccELHMDIRPLPGMTLSDLDGLLNEALAPVSERWPGrltvaelhpPIPGYECPPDHQLVE---- 315
Cdd:PRK04443 214 V--DFDSSSDGLTVEA--EMTVGLRLPPGLSPEEAREILDALLPTGTVTFTG---------AVPAYMVSKRTPLARafrv 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 754936012 316 VVEKLLGE-----KT-----DVVnycteAPFIQtlCPTLVLGPGSINQAHQPDEYLE 362
Cdd:PRK04443 281 AIREAGGTprlkrKTgtsdmNVV-----APAWG--CPMVAYGPGDSDLDHTPDEHLP 330
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
8-216 |
3.52e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 91.60 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 8 FIEIYRALIATPSISATEEALDQSNATLINLLAGWFSDlgfkVEVQPVPGTRNKFNLLAS-AGQGAGG-LLLTGHTDTVP 85
Cdd:PRK09133 39 ARDLYKELIEINTTASTGSTTPAAEAMAARLKAAGFAD----ADIEVTGPYPRKGNLVARlRGTDPKKpILLLAHMDVVE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 86 FDDGRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDAL-----------RDVdvttlkkplyILA-TADEE-TSMAGAR 152
Cdd:PRK09133 115 AKREDWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLirlkregfkpkRDI----------ILAlTGDEEgTPMNGVA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754936012 153 YFSENTS--IRPDCAI----------IGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPaRGVNAIELMHDAIGRI 216
Cdd:PRK09133 185 WLAENHRdlIDAEFALneggggtldeDGKPVLLTVQAGEKTYADFRLEVTNPGGHSSRP-TKDNAIYRLAAALSRL 259
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
31-323 |
7.27e-20 |
|
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: 90.31 E-value: 7.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 31 SNATLINLLAGWFSDLGFKVEVQPVP-------GTRNKFNLLASAGQGAGG--LLLTGHTDTVPFDDGrWTRDPFTLTEH 101
Cdd:cd02697 23 NNAPHAERTAALLQGFGFEAERHPVPeaevrayGMESITNLIVRRRYGDGGrtVALNAHGDVVPPGDG-WTRDPYGAVVE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 102 DNKLYGLGTADMKGFFA---FILDALRDVDVtTLKKPLYILATADEET-SMAGARYFSENTSIRPDCAIIGEpTSLQPIR 177
Cdd:cd02697 102 DGVMYGRAAAVSKSDFAsftFAVRALESLGA-PLRGAVELHFTYDEEFgGELGPGWLLRQGLTKPDLLIAAG-FSYEVVT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 178 AHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKE-RYHYDAFTVPYptLNLGSLHGGDASNRICAC 256
Cdd:cd02697 180 AHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNAQYRQvSSQVEGITHPY--LNVGRIEGGTNTNVVPGK 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754936012 257 CELHMDIRPLPGMTLSDLDGLLNEALAPVSERWPG------RLTVAELHPPIPGyecppDHQLVEVV----EKLLGE 323
Cdd:cd02697 258 VTFKLDRRMIPEENPVEVEAEIRRVIADAAASMPGisvdirRLLLANSMRPLPG-----NAPLVEAIqthgEAVFGE 329
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
9-360 |
3.31e-19 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 88.37 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISAT-------EEAldqsnatliNLLAGWFSDLGFK-VEVQPVPGTRNKF----NLLASAGQGAGGLL 76
Cdd:PRK13983 8 IELLSELIAIPAVNPDfggegekEKA---------EYLESLLKEYGFDeVERYDAPDPRVIEgvrpNIVAKIPGGDGKRT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 77 LT--GHTDTVPF-DDGRWTRDPFTLTEHDNKLYGLGTAD-MKGFFA--FILDALRDVDVTTlKKPLYILATADEET-SMA 149
Cdd:PRK13983 79 LWiiSHMDVVPPgDLSLWETDPFKPVVKDGKIYGRGSEDnGQGIVSslLALKALMDLGIRP-KYNLGLAFVSDEETgSKY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 150 GARY--------FSENTSIR-PDCaiiGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGVNAIELmhdAIGRIIQLR 220
Cdd:PRK13983 158 GIQYllkkhpelFKKDDLILvPDA---GNPDGSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRA---AADFALELD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 221 DSLKEryHYDA----FTVPY----PTLNLGSLhggDASNRICACCELHMDIRPLPGMTLSDLDGLLNEALAPVSERWPGR 292
Cdd:PRK13983 232 EALHE--KFNAkdplFDPPYstfePTKKEANV---DNINTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIADEFEEEYGVK 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754936012 293 LTVAELHPPIPGYECPPDHQLVE----VVEKLLGEKTDVV----NYCTeAPFIQTLCPTLVLGPGsINQAHQPDEY 360
Cdd:PRK13983 307 IEVEIVQREQAPPPTPPDSEIVKklkrAIKEVRGIEPKVGgiggGTVA-AFLRKKGYPAVVWSTL-DETAHQPNEY 380
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
9-360 |
3.41e-19 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 88.66 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 9 IEIYRALIATPSISATEEALdqsnATLINLLAGWFSDLGFKVEV---QPVPGTRNKF---NLLASAGQGAGGLL--LTGH 80
Cdd:PRK13013 17 VALTQDLIRIPTLNPPGRAY----REICEFLAARLAPRGFEVELiraEGAPGDSETYprwNLVARRQGARDGDCvhFNSH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 81 TDTVPFDDGrWTRDPFTLTEHDNKLYGLGTADMKGFFA---FILDALRDVDVtTLKKPLYILATADEETS-------MAG 150
Cdd:PRK13013 93 HDVVEVGHG-WTRDPFGGEVKDGRIYGRGACDMKGGLAasiIAAEAFLAVYP-DFAGSIEISGTADEESGgfggvayLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 151 ARYFSENtsiRPDCAIIGEPTSLQPI-RAHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRIIQLRDSLKERYHY 229
Cdd:PRK13013 171 QGRFSPD---RVQHVIIPEPLNKDRIcLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEIEERLFPLLATRRT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 230 DAFTVP----YPTLNLGSLHGG------DASNRICAC----CELHMDIRPLPGMTLSDLDGLLNEALAPVSERWPGRL-- 293
Cdd:PRK13013 248 AMPVVPegarQSTLNINSIHGGepeqdpDYTGLPAPCvadrCRIVIDRRFLIEEDLDEVKAEITALLERLKRARPGFAye 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754936012 294 --TVAELHPPIPGYECPPDHQLVEVVEKLLGEKTD-VVNYCT----EAPFIQTLCPTLVLGPGSINQAHQPDEY 360
Cdd:PRK13013 328 irDLFEVLPTMTDRDAPVVRSVAAAIERVLGRQADyVVSPGTydqkHIDRIGKLKNCIAYGPGILDLAHQPDEW 401
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
12-361 |
1.18e-18 |
|
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: 87.00 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 12 YRALIATPSISATEEALDQSNaTLINLLAGWFSDLGFKVE-VQPVPGTRNKFNLLASAGqGAGGLLLTGHTDTVPFDD-G 89
Cdd:cd03893 4 LAELVAIPSVSAQPDRREELR-RAAEWLADLLRRLGFTVEiVDTSNGAPVVFAEFPGAP-GAPTVLLYGHYDVQPAGDeD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 90 RWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKPLYI--LATADEETSMAGARYFSENTS--IRPDCA 165
Cdd:cd03893 82 GWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVkfIIEGEEESGSPSLDQLVEAHRdlLAADAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 166 IIGEPTSLQPIR-----AHKGHISTAVRV--LGQSGHSS-------DP-ARGVNAIELMHDAIGRII--QLRDSLK---- 224
Cdd:cd03893 162 VISDSTWVGQEQptltyGLRGNANFDVEVkgLDHDLHSGlyggvvpDPmTALAQLLASLRDETGRILvpGLYDAVRelpe 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 225 ERYHYDAfTVP-------------------YPTLNL----GSLHGGDASNRICACCELHMDIRPLPGMTLSDLDGLLNEA 281
Cdd:cd03893 242 EEFRLDA-GVLeeveiiggttgsvaerlwtRPALTVlgidGGFPGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLEAH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 282 L---APvserWPGRLTV---AELHPpipgYECPPDHQLVEVVEKLL----GEKTDVVNYCTEAPFIQTL-----CPTLVL 346
Cdd:cd03893 321 LekhAP----SGAKVTVsyvEGGMP----WRSDPSDPAYQAAKDALrtayGVEPPLTREGGSIPFISVLqefpqAPVLLI 392
|
410
....*....|....*.
gi 754936012 347 GPGSIN-QAHQPDEYL 361
Cdd:cd03893 393 GVGDPDdNAHSPNESL 408
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
8-383 |
3.75e-17 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 82.39 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 8 FIEIYRALIA--TPSISA--TEEALDQsnatlinlLAGWFSDLGFKVEVQPV-PGTRNKFNLLASAGQGA-GGLLLTGHT 81
Cdd:PRK08596 15 LLELLKTLVRfeTPAPPArnTNEAQEF--------IAEFLRKLGFSVDKWDVyPNDPNVVGVKKGTESDAyKSLIINGHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 82 DTVPFDDGR-WTRDPFTLTEHDNKLYGLGTADMKGFFA---FILDALRDVDVtTLKKPLYILATADEETSMAGARYFSEN 157
Cdd:PRK08596 87 DVAEVSADEaWETNPFEPTIKDGWLYGRGAADMKGGLAgalFAIQLLHEAGI-ELPGDLIFQSVIGEEVGEAGTLQCCER 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 158 tSIRPDCAIIGEPTSLQpIRAHKGHISTAVRVlgQSGHS-SDPAR-----------GVNAIELMhdaiGRIIQlrdSLKE 225
Cdd:PRK08596 166 -GYDADFAVVVDTSDLH-MQGQGGVITGWITV--KSPQTfHDGTRrqmihaggglfGASAIEKM----MKIIQ---SLQE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 226 RYHYDAFTVPYP-------TLNLGSLHGGDASNRICACCELHMDIRPLPGMTLSDL-----DGLLNEALA-------PVS 286
Cdd:PRK08596 235 LERHWAVMKSYPgfppgtnTINPAVIEGGRHAAFIADECRLWITVHFYPNETYEQVikeieEYIGKVAAAdpwlrenPPQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 287 ERWPGRLTVAELHPPIPGYECPPDH----QLVEVVEKLLGEKT--DVVNYCTEAPFIQTL-CPTLVLGPGSINQAHQPDE 359
Cdd:PRK08596 315 FKWGGESMIEDRGEIFPSLEIDSEHpavkTLSSAHESVLSKNAilDMSTTVTDGGWFAEFgIPAVIYGPGTLEEAHSVNE 394
|
410 420
....*....|....*....|....*
gi 754936012 360 YLE-TRFIKPTrELITQVVHHFCWH 383
Cdd:PRK08596 395 KVEiEQLIEYT-KVITAFIYEWCHT 418
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
45-362 |
3.05e-16 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 79.98 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 45 DLGFKvevqpvpgTRNKFNLLASAGQGAG----GLLltGHTDTVPFDDGrWTRDPFTLTEHDNKLYGLGTADMKG----- 115
Cdd:cd03888 50 RLGFK--------TKNIDNYAGYAEYGEGeevlGIL--GHLDVVPAGEG-WTTDPFKPVIKDGKLYGRGTIDDKGptiaa 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 116 FFAfiLDALRDVDVTTLKKPLYILATaDEETSMAG-ARYFSEN-------TsirPDC---AIIGE-------------PT 171
Cdd:cd03888 119 LYA--LKILKDLGLPLKKKIRLIFGT-DEETGWKCiEHYFEHEeypdfgfT---PDAefpVINGEkgivtvdltfkidDD 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 172 SLQPIRAHKGHI------STA--------------------------------VRVLGQSGHSSDPARGVNAIELM---- 209
Cdd:cd03888 193 KGYRLISIKGGEatnmvpDKAeavipgkdkeelalsaatdlkgnieiddggveLTVTGKSAHASAPEKGVNAITLLakfl 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 210 -----HDAIGRIIQ-LRDSLKERYHYDAFTVPYP-------TLNLGSLHGGDASNricaccELHMDIRPLPGMTLSDLDG 276
Cdd:cd03888 273 aelnkDGNDKDFIKfLAKNLHEDYNGKKLGINFEdevmgelTLNPGIITLDDGKL------ELGLNVRYPVGTSAEDIIK 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 277 LLNEALapvsERWPGRLTVAELHPPIpgYeCPPDHQLV----EVVEKLLGEKTDVV-----NYCTEAPFIQTLCPTLvlg 347
Cdd:cd03888 347 QIEEAL----EKYGVEVEGHKHQKPL--Y-VPKDSPLVktllKVYEEQTGKEGEPVaigggTYARELPNGVAFGPEF--- 416
|
410
....*....|....*
gi 754936012 348 PGSINQAHQPDEYLE 362
Cdd:cd03888 417 PGQKDTMHQANEFIP 431
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
8-125 |
2.06e-15 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 77.38 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 8 FIEIYRALIATPSISATEEALDQSnatlINLLAGWFSDLGFKVEVQPVPGtrNKFnLLASAGQGAGG-LLLTGHTDTVPF 86
Cdd:cd05681 1 YLEDLRDLLKIPSVSAQGRGIPET----ADFLKEFLRRLGAEVEIFETDG--NPI-VYAEFNSGDAKtLLFYNHYDVQPA 73
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 754936012 87 D-DGRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALR 125
Cdd:cd05681 74 EpLELWTSDPFELTIRNGKLYARGVADDKGELMARLAALR 113
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
40-216 |
1.65e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 74.50 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 40 AGWFSDLGFKVE-VQPVPGTRNKFNLLASAGQGAGGLLLTGHTDTVPFDDGRWTRDPFTLTEHDNKLYGLGTADMKGFFA 118
Cdd:PRK07906 32 AEKLAEVGLEPTyLESAPGRANVVARLPGADPSRPALLVHGHLDVVPAEAADWSVHPFSGEIRDGYVWGRGAVDMKDMDA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 119 FILDALRDVDVTTLKKP--LYILATADEETSMA-GARYFSENtsiRPD----C--AI---------IGEPTSLQPIR-AH 179
Cdd:PRK07906 112 MMLAVVRHLARTGRRPPrdLVFAFVADEEAGGTyGAHWLVDN---HPElfegVteAIsevggfsltVPGRDRLYLIEtAE 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 754936012 180 KGHISTAVRVLGQSGHSSDPARGvNAIELMHDAIGRI 216
Cdd:PRK07906 189 KGLAWMRLTARGRAGHGSMVNDD-NAVTRLAEAVARI 224
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
75-288 |
1.51e-13 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 71.53 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 75 LLLTGHTDTV-----PFDDGRWtRDpftltehDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKPL-Y-ILATADEET- 146
Cdd:PRK07338 95 VLLTGHMDTVfpadhPFQTLSW-LD-------DGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLgYdVLINPDEEIg 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 147 SMAGARYFSENTSiRPDCAIIGEPT----SLQPIRAHKGHISTAVRvlGQSGHSS-DPARGVNAIELMHDAIGRIIQLRD 221
Cdd:PRK07338 167 SPASAPLLAELAR-GKHAALTYEPAlpdgTLAGARKGSGNFTIVVT--GRAAHAGrAFDEGRNAIVAAAELALALHALNG 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754936012 222 SlkeryhYDAFTVpyptlNLGSLHGGDASNRICACCELHMDIRPLPGMTLSDLDGLLNEALAPVSER 288
Cdd:PRK07338 244 Q------RDGVTV-----NVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQR 299
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
5-302 |
2.52e-13 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 70.20 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 5 LPPFIEIYraliaTPSISateealdQSNATliNLLAGWFSDLGFKVEVQPvpgTRNKFNLlasagqGAGGLLLTGHTDTV 84
Cdd:PRK00466 16 LLDLLSIY-----TPSGN-------ETNAT--KFFEKISNELNLKLEILP---DSNSFIL------GEGDILLASHVDTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 85 PfddGRWtrDPFTLTEhdnKLYGLGTADMKGFFAFILDALRDVDVTTLKkpLYILATADEETSMAGARYFSeNTSIRPDC 164
Cdd:PRK00466 73 P---GYI--EPKIEGE---VIYGRGAVDAKGPLISMIIAAWLLNEKGIK--VMVSGLADEESTSIGAKELV-SKGFNFKH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 165 AIIGEPT-SLQPIRAHKGHISTAVRVLGQSGHSSDPARGvnaieLMHDAIGRIIQlrdSLKERYHYDAFTVpYPTLnlgs 243
Cdd:PRK00466 142 IIVGEPSnGTDIVVEYRGSIQLDIMCEGTPEHSSSAKSN-----LIVDISKKIIE---VYKQPENYDKPSI-VPTI---- 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754936012 244 LHGGDASNRICACCELHMDIR-PLPGMTlsdlDGLLNEalapVSERWPG-RLTVAELHPPI 302
Cdd:PRK00466 209 IRAGESYNVTPAKLYLHFDVRyAINNKR----DDLISE----IKDKFQEcGLKIVDETPPV 261
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
64-189 |
1.48e-12 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 68.65 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 64 LLASAGQGAGGLLLTGHTDTVPFDDGRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKPLYILATAD 143
Cdd:PRK08554 55 VYGEIGEGKPKLLFMAHFDVVPVNPEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLNGKVIFAFTGD 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 754936012 144 EETSMAGARYFSENTS---IRPDCAIIGEPTSLQPI-RAHKGhISTAVRV 189
Cdd:PRK08554 135 EEIGGAMAMHIAEKLReegKLPKYMINADGIGMKPIiRRRKG-FGVTIRV 183
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
68-172 |
1.64e-12 |
|
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: 65.92 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 68 AGQGAGGLLLTGHTDTVPFDDGRWTRDPF-TLTEHDNKLYGLGTADMKGFFAFILDALRDV--DVTTLKKPLYILATADE 144
Cdd:cd18669 8 GGGGGKRVLLGAHIDVVPAGEGDPRDPPFfVDTVEEGRLYGRGALDDKGGVAAALEALKLLkeNGFKLKGTVVVAFTPDE 87
|
90 100 110
....*....|....*....|....*....|...
gi 754936012 145 ETS-----MAGARYFSENTsIRPDCAIIGEPTS 172
Cdd:cd18669 88 EVGsgagkGLLSKDALEED-LKVDYLFVGDATP 119
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
8-115 |
1.90e-12 |
|
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: 68.40 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 8 FIEIYRALIATPSISATEEALDQSNaTLINLLAGWFSDLGFKVEVQPVPgtRNKFN----------LLASAGQ--GAGGL 75
Cdd:cd05676 12 FIERLREAVAIQSVSADPEKRPELI-RMMEWAAERLEKLGFKVELVDIG--TQTLPdgeelplppvLLGRLGSdpSKKTV 88
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 754936012 76 LLTGHTDTVP--FDDGrWTRDPFTLTEHDNKLYGLGTADMKG 115
Cdd:cd05676 89 LIYGHLDVQPakLEDG-WDTDPFELTEKDGKLYGRGSTDDKG 129
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
8-127 |
1.94e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 68.40 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 8 FIEIYRALIATPSISATEEALDQSNATLINLLAGWFSDLGFKVEVQ--PVPGtRNKFnLLASAGQGAG--GLLLTGHTDT 83
Cdd:PRK07079 19 FFADLARRVAYRTESQNPDRAPALRAYLTDEIAPALAALGFTCRIVdnPVAG-GGPF-LIAERIEDDAlpTVLIYGHGDV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 754936012 84 VPFDDGRWT--RDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDV 127
Cdd:PRK07079 97 VRGYDEQWRegLSPWTLTEEGDRWYGRGTADNKGQHTINLAALEQV 142
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
75-216 |
2.15e-11 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 64.97 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 75 LLLTGHTDTVPFDDGR---WTRDPFTLTEHDNKLYGLGTADMKGFFAFILDAL-----------RDVdvttlkkplYILA 140
Cdd:PRK08262 114 IVLMAHQDVVPVAPGTegdWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAeallaqgfqprRTI---------YLAF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 141 TADEETSMAGARYFSE---NTSIRPDCAI-------------IGEPTSLQPIrAHKGHISTAVRVLGQSGHSSDPARGvN 204
Cdd:PRK08262 185 GHDEEVGGLGARAIAEllkERGVRLAFVLdeggaitegvlpgVKKPVALIGV-AEKGYATLELTARATGGHSSMPPRQ-T 262
|
170
....*....|..
gi 754936012 205 AIELMHDAIGRI 216
Cdd:PRK08262 263 AIGRLARALTRL 274
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
16-224 |
5.95e-11 |
|
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: 63.67 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 16 IATPSISATEEALDQSNATLINLLAGWFSDLGFKVEV--QPVPGtRNKFnLLASAGQGAGG--LLLTGHTDTVPFDDGRW 91
Cdd:cd05679 14 VAVPTESQEPARKPELRAYLDQEMRPRFERLGFTVHIhdNPVAG-RAPF-LIAERIEDPSLptLLIYGHGDVVPGYEGRW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 92 T--RDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDVDVT---TLKKPLYILATADEETSMAGARYF--SENTSIRPDC 164
Cdd:cd05679 92 RdgRDPWTVTVWGERWYGRGTADNKGQHSINMAALRQVLEArggKLGFNVKFLIEMGEEMGSPGLRAFcfSHREALKADL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754936012 165 AIIGEPTSLQPIR-----AHKGHISTAVRV-LGQSGHSS--------DPA-RGVNAIELMHDAIGRIiqLRDSLK 224
Cdd:cd05679 172 FIASDGPRLAADRptmflGSRGGLNFELRVnLREGGHHSgnwggllaNPGiILANAIASLVDGKGRI--KLPALK 244
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
75-218 |
1.08e-10 |
|
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: 63.04 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 75 LLLTGHTDTVPFDD---GRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDVdvttLK---KP---LYILATADEE 145
Cdd:cd05674 72 LLLMAHQDVVPVNPeteDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELL----LKrgfKPrrtIILAFGHDEE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 146 TS-MAGARYFSE------------------NTSIRPDcaIIGEPTSLqPIRAHKGHISTAVRVLGQSGHSSDPARGvNAI 206
Cdd:cd05674 148 VGgERGAGAIAElllerygvdglaaildegGAVLEGV--FLGVPFAL-PGVAEKGYMDVEITVHTPGGHSSVPPKH-TGI 223
|
170
....*....|..
gi 754936012 207 ELMHDAIGRIIQ 218
Cdd:cd05674 224 GILSEAVAALEA 235
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
75-287 |
1.20e-10 |
|
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: 62.50 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 75 LLLTGHTDTVPFDDGRWTRDPFT-LTEHDNKLYGLGTADMKGFFAFILDALRDVDVT--TLKKPLYILATADEET-SMAG 150
Cdd:TIGR01880 74 ILLNSHTDVVPVFREHWTHPPFSaFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASgfKFKRTIHISFVPDEEIgGHDG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 151 ARYFSE-------NTSIRPDCAIIGEPTSLQPIRAHKGHISTAVRVLGQSGHSSDPARGvNAIELMHDAIGRIIQLRDSL 223
Cdd:TIGR01880 154 MEKFAKtdefkalNLGFALDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKLMEN-TAMEKLEKSVESIRRFRESQ 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 754936012 224 KERYH--YDAFTVPYPTLNLGSLHGGDASNRICACCELHMDIRPLPGMTLSDLDGLLNEALAPVSE 287
Cdd:TIGR01880 233 FQLLQsnPDLAIGDVTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAGE 298
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
8-206 |
1.32e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 62.40 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 8 FIEIYRALIATPSI-----------SATEEALDQSNATLinllagwfSDLGFKVEVQPvpgtrNKFNLLASAGQGAGGLL 76
Cdd:PRK07205 13 CVAAIKTLVSYPSVlnegengtpfgQAIQDVLEATLDLC--------QGLGFKTYLDP-----KGYYGYAEIGQGEELLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 77 LTGHTDTVPF-DDGRWTRDPFTLTEHDNKLYGLGTADMKG-----FFAfiLDALRDVDVTTLKKPLYILATaDEETSMAG 150
Cdd:PRK07205 80 ILCHLDVVPEgDLSDWQTPPFEAVEKDGCLFGRGTQDDKGpsmaaLYA--VKALLDAGVQFNKRIRFIFGT-DEETLWRC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 151 -ARYFSE----NTSIRPDCA---IIGEPTSLQ----------------------PIRA-HKGHISTAVR----------- 188
Cdd:PRK07205 157 mNRYNEVeeqaTMGFAPDSSfplTYAEKGLLQaklvgpgsdqlelevgqafnvvPAKAsYQGPKLEAVKkeldklgfeyv 236
|
250 260
....*....|....*....|....*
gi 754936012 189 -------VLGQSGHSSDPARGVNAI 206
Cdd:PRK07205 237 vkenevtVLGKSVHAKDAPQGINAV 261
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
79-154 |
1.33e-10 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 62.55 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 79 GHTDTVPFDDGrWTRDPFTLTEHDNKLYGLGTADMKG-----FFAfiLDALRDVDVTTLKKPLYILATaDEETSMAGA-R 152
Cdd:PRK07318 86 GHLDVVPAGDG-WDTDPYEPVIKDGKIYARGTSDDKGptmaaYYA--LKIIKELGLPLSKKVRFIVGT-DEESGWKCMdY 161
|
..
gi 754936012 153 YF 154
Cdd:PRK07318 162 YF 163
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
15-125 |
2.20e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 61.85 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 15 LIATPSISA---TEEALDQSNATLINLlagwFSDLGF-KVEVQPVPGTRNKFNLLAsAGQGAGGLLLTGHTDTVP-FDDG 89
Cdd:PRK07907 27 LVRIPSVAAdpfRREEVARSAEWVADL----LREAGFdDVRVVSADGAPAVIGTRP-APPGAPTVLLYAHHDVQPpGDPD 101
|
90 100 110
....*....|....*....|....*....|....*.
gi 754936012 90 RWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALR 125
Cdd:PRK07907 102 AWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALR 137
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
68-158 |
2.33e-10 |
|
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: 59.75 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 68 AGQGAGGLLLTGHTDTVPFDDGRWTRDPF-TLTEHDNKLYGLGTADMKGFFAFILDALRDV--DVTTLKKPLYILATADE 144
Cdd:cd03873 8 GGEGGKSVALGAHLDVVPAGEGDNRDPPFaEDTEEEGRLYGRGALDDKGGVAAALEALKRLkeNGFKPKGTIVVAFTADE 87
|
90
....*....|....
gi 754936012 145 ETSMaGARYFSENT 158
Cdd:cd03873 88 EVGS-GGGKGLLSK 100
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
35-267 |
1.73e-09 |
|
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: 59.01 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 35 LINLLAGWFSDLGFKVEVQPVPGTRNKFNLLAS-AGQGAGGLL--LTGHTDTVPFDDGRWTRDPFTLTEHDNKLYGLGTA 111
Cdd:cd08012 38 VLEALTPYSTENGGPLVIDHVSYVKGRGNIIVEyPGTVDGKTVsfVGSHMDVVTANPETWEFDPFSLSIDGDKLYGRGTT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 112 DMKGFFAFILDALRDVDVT--TLKKPLYILATADEETS--------MAGARYFSENTSIRP----DCAiigeptSLQPIR 177
Cdd:cd08012 118 DCLGHVALVTELFRQLATEkpALKRTVVAVFIANEENSeipgvgvdALVKSGLLDNLKSGPlywvDSA------DSQPCI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 178 AHKGHISTAVRVLGQSGHSSDPARGVNAIELMHDAIGRI-----IQLRDSLKE-RYHYDAFTVPYPTlnLGSLHGGdASN 251
Cdd:cd08012 192 GTGGMVTWKLTATGKLFHSGLPHKAINALELVMEALAEIqkrfyIDFPPHPKEeVYGFATPSTMKPT--QWSYPGG-SIN 268
|
250
....*....|....*.
gi 754936012 252 RICACCELHMDIRPLP 267
Cdd:cd08012 269 QIPGECTICGDCRLTP 284
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
75-287 |
1.55e-08 |
|
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: 55.74 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 75 LLLTGHTDTVPFDDGRWTRDPFT-LTEHDNKLYGLGTADMKGFFAFILDALRDVDVT--TLKKPLYILATADEE----TS 147
Cdd:cd05646 67 ILLNSHTDVVPVFEEKWTHDPFSaHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASgfKPKRTIHLSFVPDEEigghDG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 148 MAGARYFSENTSIRPDCAI---IGEPTSLQPI----RAhKGHIstAVRVLGQSGHSSDPARGvNAIELMHDAIGRIIQLR 220
Cdd:cd05646 147 MEKFVKTEEFKKLNVGFALdegLASPTEEYRVfygeRS-PWWV--VITAPGTPGHGSKLLEN-TAGEKLRKVIESIMEFR 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754936012 221 DSLKERYHYDAFTVP--YPTLNLGSLHGGDASNRICACCELHMDIRPLPGMTLSDLDGLLNEALAPVSE 287
Cdd:cd05646 223 ESQKQRLKSNPNLTLgdVTTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGR 291
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
43-254 |
6.19e-08 |
|
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349932 [Multi-domain] Cd Length: 368 Bit Score: 53.99 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 43 FSDLGFKV---EVQPVPG--TRNKFNLLASAGQGAGGLLLTGHTDTVpfDDGRWTRDPftlTEHDNKLYGLGT----ADM 113
Cdd:cd05683 33 FENLGLSViedDAGKTTGggAGNLICTLKADKEEVPKILFTSHMDTV--TPGINVKPP---QIADGYIYSDGTtilgADD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 114 KGFFAFILDALRDVDVTTLK-KPLYILATADEETSMAGARY-----------FSENTSIRPDCAIIGEPTslqpirahkg 181
Cdd:cd05683 108 KAGIAAILEAIRVIKEKNIPhGQIQFVITVGEESGLVGAKAldpelidadygYALDSEGDVGTIIVGAPT---------- 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754936012 182 HISTAVRVLGQSGHSS-DPARGVNAIELMHDAIGRIIQLRdslkeryhYDAFTvpypTLNLGSLHGGDASNRIC 254
Cdd:cd05683 178 QDKINAKIYGKTAHAGtSPEKGISAINIAAKAISNMKLGR--------IDEET----TANIGKFQGGTATNIVT 239
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
70-258 |
6.15e-07 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 50.94 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 70 QGAGGLLLTGHTDTV----PFDDGRWTRDpftltehDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKPLYI--LATAD 143
Cdd:PRK07473 73 QGEPGILIAGHMDTVhpvgTLEKLPWRRE-------GNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPItvLFTPD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 144 EETSMAGARYFSENTSIRPDCAIIGEPTslqpiRAHKGHIST-------AVRVLGQSGHS-SDPARGVNAIELMHDAIGR 215
Cdd:PRK07473 146 EEVGTPSTRDLIEAEAARNKYVLVPEPG-----RPDNGVVTGryaiarfNLEATGRPSHAgATLSEGRSAIREMARQILA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 754936012 216 IiqlrdslkeryhyDAFTVPYPTLNLGSLHGGDASNRICACCE 258
Cdd:PRK07473 221 I-------------DAMTTEDCTFSVGIVHGGQWVNCVATTCT 250
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
56-238 |
4.15e-06 |
|
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: 48.49 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 56 PGTRNKFNLLASAGQGAGGLLLTGHTDTVPFDD-GRWTR---DPFTLTE------------------HDNKLYGLGTADM 113
Cdd:cd05654 55 LGRRNVTALVKGKKPSKRTIILISHFDTVGIEDyGELKDiafDPDELTKafseyveeldeevredllSGEWLFGRGTMDM 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 114 KGFFAFILDALRD-VDVTTLKKPLYILATADEETSMAGARY-------FSENTSIRPDCAIIGEPTSLQpiraHKG---- 181
Cdd:cd05654 135 KSGLAVHLALLEQaSEDEDFDGNLLLMAVPDEEVNSRGMRAavpalleLKKKHDLEYKLAINSEPIFPQ----YDGdqtr 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 754936012 182 --HISTAVRVL------GQSGHSSDPARGVNAiELMHDAIGRIIQLRDSLKERYHYDAftVPYPT 238
Cdd:cd05654 211 yiYTGSIGKILpgflcyGKETHVGEPFAGINA-NLMASEITARLELNADLCEKVEGEI--TPPPV 272
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
80-159 |
4.31e-05 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 45.35 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 80 HTDTVPFDDGRW-----TRDPFTLTEHDNKLYGLGTADMKGFFAFILDAL---RDVDVtTLKKPLYILATADEETSMAGA 151
Cdd:PRK06156 117 HADVVPANPELWvldgtRLDPFKVTLVGDRLYGRGTEDDKGAIVTALYAMkaiKDSGL-PLARRIELLVYTTEETDGDPL 195
|
....*...
gi 754936012 152 RYFSENTS 159
Cdd:PRK06156 196 KYYLERYT 203
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
19-115 |
4.77e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 45.13 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 19 PSISATEEALDQSNATLINLLagwfSDLGFKVEVQpvpgtRNKFNLLASAGQGAGG---LLLTGHTDTVPFDD-GRWTRD 94
Cdd:PRK06446 15 PSISATGEGIEETANYLKDTM----EKLGIKANIE-----RTKGHPVVYGEINVGAkktLLIYNHYDVQPVDPlSEWKRD 85
|
90 100
....*....|....*....|.
gi 754936012 95 PFTLTEHDNKLYGLGTADMKG 115
Cdd:PRK06446 86 PFSATIENGRIYARGASDNKG 106
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
14-126 |
1.28e-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: 349929 [Multi-domain] Cd Length: 437 Bit Score: 43.84 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 14 ALIATPSISA-TEEALDQSNATLInlLAGWFSDLGF-KVEVQPVPGtrnkFNLLASAGQGAGG---LLLTGHTDTVPFD- 87
Cdd:cd05680 6 ELLRIPSVSAdPAHKGDVRRAAEW--LADKLTEAGFeHTEVLPTGG----HPLVYAEWLGAPGaptVLVYGHYDVQPPDp 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 754936012 88 -DGrWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRD 126
Cdd:cd05680 80 lEL-WTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEA 118
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
75-115 |
2.54e-04 |
|
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex.
Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 42.72 E-value: 2.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 754936012 75 LLLTGHTDTVPFDD-GRWTRDPFTLTEHDNKLYGLGTADMKG 115
Cdd:cd05677 74 ILFYGHYDVIPAGEtDGWDTDPFTLTCENGYLYGRGVSDNKG 115
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
5-146 |
7.92e-04 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 41.16 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 5 LPPFIEIyralIATPSISATEEALDQSNATL---INLLAGWF---SDLGFKVEVQPVPG-TRNKFNLLASAGQGAGGLLL 77
Cdd:cd05682 3 LPALSDY----IRIPNQSPLFDPEWATNGLLekaANLIADWVkaqNIKGAKVEVVELEGrTPLLFVEIPGTEQDDDTVLL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754936012 78 TGHTDTVPFDDGrWTRD--PFTLTEHDNKLYGLGTADmKGFFAF-ILDALRDVDVTTLKKPLYI-LATADEET 146
Cdd:cd05682 79 YGHMDKQPPFTG-WDEGlgPTKPVIRGDKLYGRGGAD-DGYAIFaSLTAIKALQEQGIPHPRCVvLIEACEES 149
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
13-216 |
1.14e-03 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 40.88 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 13 RALIATPSISA-TEEALDQSNATliNLLAGWFSDLGF-KVEVQPVPGtrnkfNLLASA----GQGAGGLLLTGHTDTVPF 86
Cdd:PRK08201 21 KEFLRIPSISAlSEHKEDVRKAA--EWLAGALEKAGLeHVEIMETAG-----HPIVYAdwlhAPGKPTVLIYGHYDVQPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 87 DD-GRWTRDPFTLTEHDNKLYGLGTADMKGFFAFILDALRDVDVTTLKKPLYI--LATADEETSMAGARYFSENTS--IR 161
Cdd:PRK08201 94 DPlNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVkfCIEGEEEIGSPNLDSFVEEEKdkLA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 162 PDCAIIGEPTSLQP-----IRAHKGHISTAVRVLGQSG--HSSDPARGV-NAI----EL---MHDAIGRI 216
Cdd:PRK08201 174 ADVVLISDTTLLGPgkpaiCYGLRGLAALEIDVRGAKGdlHSGLYGGAVpNALhalvQLlasLHDEHGTV 243
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
187-323 |
4.35e-03 |
|
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: 38.74 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754936012 187 VRVLGQSGHSSDPARGVNAIELMHDAIGR----IIQLRDSLKERyhydaftvpypTLNLGSLHGGDASNRICACCELHMD 262
Cdd:cd03886 176 ITVKGKGGHGASPHLGVDPIVAAAQIVLAlqtvVSRELDPLEPA-----------VVTVGKFHAGTAFNVIPDTAVLEGT 244
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754936012 263 IRPLPGMTLSDLDGLLNEALAPVSERWPGRltvAELHppiPGYECPP---DHQLVEVVEKLLGE 323
Cdd:cd03886 245 IRTFDPEVREALEARIKRLAEGIAAAYGAT---VELE---YGYGYPAvinDPELTELVREAAKE 302
|
|
| |
