|
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: 825.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 2 KNKLPPFIEIYRALIATPSISATEEALDQSNADLITLLADWFKDLGFNVEVQPVPGTRNKFNMLASIGQGAGGLLLAGHT 81
Cdd:PRK05111 1 KMKLPSFIEMYRALIATPSISATDPALDQSNRAVIDLLAGWFEDLGFNVEIQPVPGTRGKFNLLASLGSGEGGLLLAGHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 82 DTVPFDDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYILATADEETSMAGARYFAETTALR 161
Cdd:PRK05111 81 DTVPFDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAEATAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 162 PDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHYEAFTVPYPTLNL 241
Cdd:PRK05111 161 PDCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQERYHNPAFTVPYPTLNL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 242 GHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGRLTVDELHPPIPGYECPPNHQLVEVVEKLL 321
Cdd:PRK05111 241 GHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSERWPGRITVAPLHPPIPGYECPADHQLVRVVEKLL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131795 322 GAKTEVVNYCTEAPFIQTL-CPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVIHHFCWH 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: 628.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 10 EIYRALIATPSISATeealdqSNADLITLLADWFKDLGFNVEVQPVPGTRNKFNMLASIGQ-GAGGLLLAGHTDTVPFDD 88
Cdd:TIGR01892 1 EILTKLVAFDSTSFR------PNVDLIDWAQAYLEALGFSVEVQPFPDGAEKSNLVAVIGPsGAGGLALSGHTDVVPYDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 89 GRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYILATADEETSMAGARYFAETTALRPDCAIIG 168
Cdd:TIGR01892 75 AAWTRDPFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIEAGAGRPRHAIIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 169 EPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHYEAFTVPYPTLNLGHIHGGD 248
Cdd:TIGR01892 155 EPTRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDLDEGFTPPYTTLNIGVIQGGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 249 ASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGRLTVDELHPPIPGYECPPNHQLVEVVEKLLGAKTEVV 328
Cdd:TIGR01892 235 AVNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRDEPGFEVQIEVVSTDPGVNTEPDAELVAFLEELSGNAPEVV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 16131795 329 NYCTEAPFIQTL-CPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVI 377
Cdd:TIGR01892 315 SYGTEAPQFQELgAEAVVCGPGDIRQAHQPDEYVEIEDLVRCRAVLARLV 364
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
10-378 |
8.14e-178 |
|
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: 498.66 E-value: 8.14e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 10 EIYRALIATPSISAteealdQSNADLITLLADWFKDLGFNVEVQPVPgTRNKFNMLASIGQ-GAGGLLLAGHTDTVPFDD 88
Cdd:cd03894 1 ELLARLVAFDTVSR------NSNLALIEYVADYLAALGVKSRRVPVP-EGGKANLLATLGPgGEGGLLLSGHTDVVPVDG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 89 GRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYILATADEETSMAGARYFAETTA---LRPDCA 165
Cdd:cd03894 74 QKWSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALAargGRPDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 166 IIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHYEAFTVPYPTLNLGHIH 245
Cdd:cd03894 154 IVGEPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPFDPPYPTLNVGLIH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 246 GGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGRLTVDELHPPiPGYECPPNHQLVEVVEKLLG-AK 324
Cdd:cd03894 234 GGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPEAGIEVEPLFEV-PGLETDEDAPLVRLAAALAGdNK 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 16131795 325 TEVVNYCTEAPFIQTL-CPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVIH 378
Cdd:cd03894 313 VRTVAYGTEAGLFQRAgIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
1-381 |
1.31e-111 |
|
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: 331.46 E-value: 1.31e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 1 MKNKLPPFIEIYRALIATPSISateealdQSNADLITLLADWFKDLGFNVEVQPVPGtrNKFNMLASI--GQGAGGLLLA 78
Cdd:COG0624 7 IDAHLDEALELLRELVRIPSVS-------GEEAAAAELLAELLEALGFEVERLEVPP--GRPNLVARRpgDGGGPTLLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 79 GHTDTVPFDDG-RWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVT--KLKKPLYILATADEETSMAGARYFA 155
Cdd:COG0624 78 GHLDVVPPGDLeLWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAglRLPGNVTLLFTGDEEVGSPGARALV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 156 ETTA--LRPDCAIIGEPTS-LQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHYeaf 232
Cdd:COG0624 158 EELAegLKADAAIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRADPLF--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 233 tvPYPTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSErwPGRLTVDELHPPIPGYECPPNHQ 312
Cdd:COG0624 235 --GRTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAP--GVEVEVEVLGDGRPPFETPPDSP 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131795 313 LV----EVVEKLLGAKTEV--VNYCTEAPFIQTL--CPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVIHHFC 381
Cdd:COG0624 311 LVaaarAAIREVTGKEPVLsgVGGGTDARFFAEAlgIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
9-362 |
2.43e-98 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 297.49 E-value: 2.43e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATeealdqSNADLITLLADWFKDLGFNVEVQPVPgTRNKFNMLASIG-QGAGGLLLAGHTDTVPFD 87
Cdd:PRK07522 7 LDILERLVAFDTVSRD------SNLALIEWVRDYLAAHGVESELIPDP-EGDKANLFATIGpADRGGIVLSGHTDVVPVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 88 DGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYILATADEETSMAGARYF-AETTAL--RPDC 164
Cdd:PRK07522 80 GQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPSMiARLPERgvKPAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 165 AIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHYEA-FTVPYPTLNLGH 243
Cdd:PRK07522 160 CIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLAAPGPFDAlFDPPYSTLQTGT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 244 IHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSERwPGRLTVDELHPPI------PGYECPPNHQLVEVV 317
Cdd:PRK07522 240 IQGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAELLP-EMRAVHPEAAIEFeplsayPGLDTAEDAAAARLV 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 16131795 318 EKLLG-AKTEVVNYCTEAPFIQTL-CPTLVLGPGSINQAHQPDEYLE 362
Cdd:PRK07522 319 RALTGdNDLRKVAYGTEAGLFQRAgIPTVVCGPGSIEQAHKPDEFVE 365
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
10-362 |
1.10e-83 |
|
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: 259.15 E-value: 1.10e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 10 EIYRALIATPSISATEealdqsnADLITLLADWFKDLGFNVEVQPVPGTRNkfnMLASIGQGAG-GLLLAGHTDTVPFDD 88
Cdd:cd08659 1 SLLQDLVQIPSVNPPE-------AEVAEYLAELLAKRGYGIESTIVEGRGN---LVATVGGGDGpVLLLNGHIDTVPPGD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 89 G-RWTRDPFTLTEHDGKLYGLGTADMKG-----FFAFIldALRDvDVTKLKKPLYILATADEETSMAGARYFAET-TALR 161
Cdd:cd08659 71 GdKWSFPPFSGRIRDGRLYGRGACDMKGglaamVAALI--ELKE-AGALLGGRVALLATVDEEVGSDGARALLEAgYADR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 162 PDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYhyeafTVPYPTLNL 241
Cdd:cd08659 148 LDALIVGEPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPAHP-----LLGPPTLNV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 242 GHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALapvsERWPGRLTVDELHPPIPGYECPPNHQLVEVVEKLL 321
Cdd:cd08659 223 GVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAIL----EEHEAKLTVEVSLDGDPPFFTDPDHPLVQALQAAA 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16131795 322 GAKT-----EVVNYCTEAPFI--QTLCPTLVLGPGSINQAHQPDEYLE 362
Cdd:cd08659 299 RALGgdpvvRPFTGTTDASYFakDLGFPVVVYGPGDLALAHQPDEYVS 346
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
9-377 |
2.18e-68 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 220.63 E-value: 2.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATEEALDqsnaDLITLLADWFKDLGFNVEVQPVPGT------RNKFNMLASIGQGAGGLLLAGHTD 82
Cdd:PRK08651 9 VEFLKDLIKIPTVNPPGENYE----EIAEFLRDTLEELGFSTEIIEVPNEyvkkhdGPRPNLIARRGSGNPHLHFNGHYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 83 TVPFDDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPlyILA-TADEETSMAGARYFAETTALR 161
Cdd:PRK08651 85 VVPPGEGWSVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAGDGNI--ELAiVPDEETGGTGTGYLVEEGKVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 162 PDCAIIGEPTSLQPV-RAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHYEAFTVPYPTLN 240
Cdd:PRK08651 163 PDYVIVGEPSGLDNIcIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYEYDDERGAKPTVT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 241 LG--HIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGRLTVDELhPPIPGYECPPNHQLVEVVE 318
Cdd:PRK08651 243 LGgpTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFEIT-PFSEAFVTDPDSELVKALR 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131795 319 KLLG------AKTEVVNYCTEA-PFIQTLCPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVI 377
Cdd:PRK08651 322 EAIRevlgvePKKTISLGGTDArFFGAKGIPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVL 387
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
76-379 |
3.22e-60 |
|
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: 197.18 E-value: 3.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 76 LLAGHTDTVPFDDGrwTRDPFTLTeHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKK-PLYILATADEETSMAGARYF 154
Cdd:pfam01546 1 LLRGHMDVVPDEET--WGWPFKST-EDGKLYGRGHDDMKGGLLAALEALRALKEEGLKKgTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 155 AETTALR---PDCAI---IGEPTSLQ------PVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDN 222
Cdd:pfam01546 78 IEDGLLErekVDAVFglhIGEPTLLEggiaigVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 223 LKERYHYEAFTVpyptLNLGHIHGGdaSNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGRLTVdELHPPI 302
Cdd:pfam01546 158 NVDPLDPAVVTV----GNITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEV-EYVEGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 303 PGYECPPNH---QLVEVVEKLLGAKTEVV----NYCTEAPFI-QTLCPTLV-LGPGSiNQAHQPDEYLETRFIKPTRELI 373
Cdd:pfam01546 231 APPLVNDSPlvaALREAAKELFGLKVELIvsgsMGGTDAAFFlLGVPPTVVfFGPGS-GLAHSPNEYVDLDDLEKGAKVL 309
|
....*.
gi 16131795 374 TQVIHH 379
Cdd:pfam01546 310 ARLLLK 315
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
39-375 |
6.31e-52 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 177.38 E-value: 6.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 39 LADWFKDLGFNVEVQPVPGTRNkfNMLASIGQGAGGLLLAGHTDTV-PFDDGRWTRDPFTLTEHDGKLYGLGTADMKGFF 117
Cdd:PRK08588 28 LQDLFAKHGIESKIVKVNDGRA--NLVAEIGSGSPVLALSGHMDVVaAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 118 AFILDALrdVDVTKLKKPLY----ILATADEETSMAGARYFAE------TTALrpdcaIIGEPTSLQPVRAHKGHISNAI 187
Cdd:PRK08588 106 AALVIAM--IELKEQGQLLNgtirLLATAGEEVGELGAKQLTEkgyaddLDAL-----IIGEPSGHGIVYAHKGSMDYKV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 188 RIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHYEAFTVPYPTLnlghIHGGDASNRICACCELHMDIRPLP 267
Cdd:PRK08588 179 TSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYFDSIKKHNPYLGGLTHVVTI----INGGEQVNSVPDEAELEFNIRTIP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 268 GMTLNELNGLLNDALAPVSERWPGRLTVDELHPPIPGYEcPPNHQLV----EVVEKLLGAKTEV--VNYCTEA------- 334
Cdd:PRK08588 255 EYDNDQVISLLQEIINEVNQNGAAQLSLDIYSNHRPVAS-DKDSKLVqlakDVAKSYVGQDIPLsaIPGATDAssflkkk 333
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16131795 335 ---PFIqtlcptlVLGPGSINQAHQPDEYLET----RFIKPTRELITQ 375
Cdd:PRK08588 334 pdfPVI-------IFGPGNNLTAHQVDEYVEKdmylKFIDIYKEIIIQ 374
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
39-362 |
1.01e-51 |
|
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: 176.04 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 39 LADWFKDLGFNVEV-QPVPGTRNKFNMLASiGQGAGGLLLAGHTDTVPFDDGR-WTRDPFTLTEHDGKLYGLGTADMKGF 116
Cdd:cd08011 27 IKLLLEDLGYPVELhEPPEEIYGVVSNIVG-GRKGKRLLFNGHYDVVPAGDGEgWTVDPYSGKIKDGKLYGRGSSDMKGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 117 FAFILDALRDVDVTKLKKPLYILATA--DEET-SMAGARYFAETTALRPDCAIIGEPTSLQPVR-AHKGHISNAIRIQGQ 192
Cdd:cd08011 106 IAASIIAVARLADAKAPWDLPVVLTFvpDEETgGRAGTKYLLEKVRIKPNDVLIGEPSGSDNIRiGEKGLVWVIIEITGK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 193 SGHSSDPARGVNAIELMHDAIGHILQLRdnlkeryhyeaftvpyPTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLN 272
Cdd:cd08011 186 PAHGSLPHRGESAVKAAMKLIERLYELE----------------KTVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 273 ELNGLLNDALAPVSERWPGRLTVDElhppipGYECPPNHQLVEVVE----KLLG--AKTEVVNYCTEAPF-IQTLCPTLV 345
Cdd:cd08011 250 EVLSRIIDHLDSIEEVSFEIKSFYS------PTVSNPDSEIVKKTEeaitEVLGirPKEVISVGASDARFyRNAGIPAIV 323
|
330
....*....|....*..
gi 16131795 346 LGPGSINQAHQPDEYLE 362
Cdd:cd08011 324 YGPGRLGQMHAPNEYVE 340
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
9-362 |
4.34e-51 |
|
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: 174.90 E-value: 4.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATEEALDQsnadLITLLADWFKDLGFNVEVQPVPGTRNK--FNMLASIGQGAGGLLLA--GHTDTV 84
Cdd:TIGR01910 1 VELLKDLISIPSVNPPGGNEET----IANYIKDLLREFGFSTDVIEITDDRLKvlGKVVVKEPGNGNEKSLIfnGHYDVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 85 PF-DDGRWTRDPFTLTEHDGKLYGLGTADMKGFFA---FILDALRDVDVtKLKKPLYILATADEETSMAGARYFAETTAL 160
Cdd:TIGR01910 77 PAgDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVallYALKAIREAGI-KPNGNIILQSVVDEESGEAGTLYLLQRGYF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 161 R-PDCAIIGEPT-SLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIE-LMHDaighILQLRDNLKERYH-YEAFTVPY 236
Cdd:TIGR01910 156 KdADGVLIPEPSgGDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMkLAKL----ITELNELEEHIYArNSYGFIPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 237 P-TLNLGHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVS--ERWPGRLTVDELHPpiPGYECPPNHQL 313
Cdd:TIGR01910 232 PiTFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSksDGWLYENEPVVKWS--GPNETPPDSRL 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131795 314 V----EVVEKLLG--AKTEVVNYCTEAPF-IQTLCPTLVLGPGSINQAHQPDEYLE 362
Cdd:TIGR01910 310 VkaleAIIKKVRGiePEVLVSTGGTDARFlRKAGIPSIVYGPGDLETAHQVNEYIS 365
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
9-362 |
2.03e-43 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 155.48 E-value: 2.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATEEaldqsnaDLITLLADWFKDLGFN-VEVQPVpGtrnkfNMLASIGQGAGGLLLAGHTDTVPF- 86
Cdd:PRK13004 18 TRFLRDLIRIPSESGDEK-------RVVKRIKEEMEKVGFDkVEIDPM-G-----NVLGYIGHGKKLIAFDAHIDTVGIg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 87 DDGRWTRDPFTLTEHDGKLYGLGTADMKGFFA-------FILDALRDVDVTklkkpLYILATADEET--SMAgARYFAET 157
Cdd:PRK13004 85 DIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMAsmvyaakIIKDLGLDDEYT-----LYVTGTVQEEDcdGLC-WRYIIEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 158 TALRPDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERyhyeaftvpyP 237
Cdd:PRK13004 159 DKIKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNLKED----------P 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 238 -----TLNLGHIHGgdASNRICAC---CELHMDIRPLPGMT----LNELNGLLNDAL--APVSERWPGRLTVDELHPPI- 302
Cdd:PRK13004 229 flgkgTLTVSDIFS--TSPSRCAVpdsCAISIDRRLTVGETwesvLAEIRALPAVKKanAKVSMYNYDRPSYTGLVYPTe 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131795 303 ---PGYECPPNHQLVEVVEK----LLGAKTEVVNY--CTEAPFIQTL--CPTLVLGPGSINQAHQPDEYLE 362
Cdd:PRK13004 307 cyfPTWLYPEDHEFVKAAVEaykgLFGKAPEVDKWtfSTNGVSIAGRagIPTIGFGPGKEPLAHAPNEYTW 377
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
18-381 |
1.57e-42 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 152.63 E-value: 1.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 18 TPSISATEEAldqSNADLITLLADWFKDLGFnvEVQPVPGTRNKFNMLASIgQGAGG---LLLAGHTDTVPFDDgrWTRD 94
Cdd:cd08013 17 NPSLSATGGA---GEAEIATYVAAWLAHRGI--EAHRIEGTPGRPSVVGVV-RGTGGgksLMLNGHIDTVTLDG--YDGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 95 PFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYILATADEETSMAGARYFAETTaLRPDCAIIGEPTSLQ 174
Cdd:cd08013 89 PLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGLRGDVILAAVADEEDASLGTQEVLAAG-WRADAAIVTEPTNLQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 175 PVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMhdaiGHIL----QLRDNLKERyHYEAFTVPyPTLNLGHIHGGDAS 250
Cdd:cd08013 168 IIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKA----GYFLvaleEYQQELPER-PVDPLLGR-ASVHASLIKGGEEP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 251 NRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSERWPG---RLTVDELHPpiPGYECPPNHQLVEVVEKlLGAKT-- 325
Cdd:cd08013 242 SSYPARCTLTIERRTIPGETDESVLAELTAILGELAQTVPNfsyREPRITLSR--PPFEVPKEHPFVQLVAA-HAAKVlg 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131795 326 -----EVVNYCTEAPFI-QTLCPTLVLGPgSINQAHQPDEYLETRFIKPTRELITQVIHHFC 381
Cdd:cd08013 319 eapqiRSETFWTDAALLaEAGIPSVVFGP-SGAGLHAKEEWVDVESIRQLREVLSAVVREFC 379
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
8-361 |
2.73e-42 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 150.89 E-value: 2.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 8 FIEIYRALIATPSISATEEALDQsnadlitLLADWFKDLGFNVEVQPVPGTrNKFNMLASIGQGAG-GLLLAGHTDTVP- 85
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGD-------FLAEYLESLGFTVEKQPVENK-DRFNVYAYPGSSRQpRVLLTSHIDTVPp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 86 -FddgrwtrdPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKP--LYILATADEETSMAGARYFAETTALRP 162
Cdd:cd05652 73 fI--------PYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEgdLGLLFVVGEETGGDGMKAFNDLGLNTW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 163 DCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHYEaftvpypTLNLG 242
Cdd:cd05652 145 DAVIFGEPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPSSELLGPT-------TLNIG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 243 HIHGGDASNRICACCELHMDIRPL--PGMTLNELNGLLNDALAP---VSERWPGRLTVDELHPPIPGYEcppnhqlvevv 317
Cdd:cd05652 218 RISGGVAANVVPAAAEASVAIRLAagPPEVKDIVKEAVAGILTDtedIEVTFTSGYGPVDLDCDVDGFE----------- 286
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 16131795 318 ekllgakTEVVNYCTEAPFIQTLCPTLVLGPGSINQAHQPDEYL 361
Cdd:cd05652 287 -------TDVVAYGTDIPYLKGDHKRYLYGPGSILVAHGPDEAI 323
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
15-380 |
4.37e-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: 146.30 E-value: 4.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 15 LIATPSISAtEEALDQsnadliTLLADWFKDLGFNVEVQ---------------PVPGTRNKFNMLASI-GQGAGG--LL 76
Cdd:cd03895 6 LVRFPSLRG-EEAAAQ------DLVAAALRSRGYTVDRWeidveklkhhpgfspVAVDYAGAPNVVGTHrPRGETGrsLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 77 LAGHTDTVPFDDGR-WTRDPFTLTEHDGKLYGLGTADMKGFFA---FILDALRDVDVtKLKKPLYILATADEETSMAGAr 152
Cdd:cd03895 79 LNGHIDVVPEGPVElWTRPPFEATIVDGWMYGRGAGDMKAGLAanlFALDALRAAGL-QPAADVHFQSVVEEECTGNGA- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 153 yfaeTTAL----RPDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYH 228
Cdd:cd03895 157 ----LAALmrgyRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEREWNARKK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 229 -YEAF-TVPYP-TLNLGHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVS--ERWPGRltvdelHPP-- 301
Cdd:cd03895 233 sHPHFsDHPHPiNFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVADAAatDPWLSN------HPPev 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 302 ------IPGYECPPNHQLVEVV----EKLLGAK--TEVVNYCTEAPFIQTL--CPTLVLGPGSINqAHQPDEYLEtrfIK 367
Cdd:cd03895 307 ewngfqAEGYVLEPGSDAEQVLaaahQAVFGTPpvQSAMTATTDGRFFVLYgdIPALCYGPGSRD-AHGFDESVD---LE 382
|
410
....*....|...
gi 16131795 368 PTRElITQVIHHF 380
Cdd:cd03895 383 SLRK-ITKTIALF 394
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
9-362 |
6.10e-39 |
|
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: 142.06 E-value: 6.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATEEALdqsnADLITllaDWFKDLGFNVEvqpvpgtRNKFNMLASIGQGAGG---LLLAGHTDTVP 85
Cdd:cd05651 3 IELLKSLIATPSFSREEHKT----ADLIE---NYLEQKGIPFK-------RKGNNVWAENGHFDEGkptLLLNSHHDTVK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 86 FDDGrWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDV-DVTKLKKPLYILATADEETS-MAGARyfaettALRP- 162
Cdd:cd05651 69 PNAG-WTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLySEGPLNYNLIYAASAEEEISgKNGIE------SLLPh 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 163 ----DCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPaRGVNAIelmHDAIGHILQLRDnlkERYHYEAFTVPYPT 238
Cdd:cd05651 142 lpplDLAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAARN-EGDNAI---YKALDDIQWLRD---FRFDKVSPLLGPVK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 239 LNLGHIHGGDASNRICACCELHMDIRPLPGMT----LNELNGLLNDALAPVSERwpgrltvdeLHPPipgyECPPNHQLV 314
Cdd:cd05651 215 MTVTQINAGTQHNVVPDSCTFVVDIRTTEAYTneeiFEIIRGNLKSEIKPRSFR---------LNSS----AIPPDHPIV 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16131795 315 EVVEKlLGAKTEVVNYCTEAPFIQtlCPTLVLGPGSINQAHQPDEYLE 362
Cdd:cd05651 282 QAAIA-AGRTPFGSPTLSDQALMP--FPSVKIGPGDSSRSHTADEFIE 326
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
9-362 |
1.16e-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. 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: 139.48 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATEEALdqsnadlITLLADWFKDLGFN-VEVQPVPgtrnkfNMLASIGQGAGGLLLAGHTDTVPF- 86
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGV-------VERIEEEMEKLGFDeVEIDPMG------NVIGYIGGGKKKILFDGHIDTVGIg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 87 DDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALR---DVDVTKLKKPLYILATADEET--SMAgARYFAETTALR 161
Cdd:cd05649 68 NIDNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKimkDLGLRDFAYTILVAGTVQEEDcdGVC-WQYISKADKIK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 162 PDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKeryhyEAFTVPYPTLNL 241
Cdd:cd05649 147 PDFVVSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFP-----EAPFLGRGTLTV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 242 GHIHggDASNRICAC---CELHMDIRPLPGMT----LNELNGL-----LNDALAPVSERWPGRLTVDELHPP---IPGYE 306
Cdd:cd05649 222 TDIF--STSPSRCAVpdsCRISIDRRLTVGETwegcLEEIRALpavkkYGDDVAVSMYNYDRPSYTGEVYESeryFPTWL 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131795 307 CPPNHQLV----EVVEKLLGAKTEVVNY--CTEAPFIQ--TLCPTLVLGPGSINQAHQPDEYLE 362
Cdd:cd05649 300 LPEDHELVkallEAYKALFGARPLIDKWtfSTNGVSIMgrAGIPCIGFGPGAENQAHAPNEYTW 363
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
47-361 |
5.16e-36 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 134.94 E-value: 5.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 47 GFNVEVqpVPGTRNKFNMLASIGQGAggLLLAGHTDTVPFDDGrWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRD 126
Cdd:PRK08737 42 GFQVEV--IDHGAGAVSLYAVRGTPK--YLFNVHLDTVPDSPH-WSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 127 VDvtklkKPLYILATADEE--TSMAGARYFAetTALRPDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDP-ARGV 203
Cdd:PRK08737 117 GD-----GDAAFLFSSDEEanDPRCVAAFLA--RGIPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKqDPSA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 204 NAIelmHDAIGHILQLRDNLKERYHYEAFTVPYPTLNLGHIHGGDASNRICACCELHMDIRPLPGMT----LNELNGLLN 279
Cdd:PRK08737 190 SAL---HQAMRWGGQALDHVESLAHARFGGLTGLRFNIGRVEGGIKANMIAPAAELRFGFRPLPSMDvdglLATFAGFAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 280 DALAPVSERWPGrltvdelhPPIPGYECPPNHQ----LVEVVEKLLGAKTEVVNYCTEAP-FIQTLCPTLVLGPGSINQA 354
Cdd:PRK08737 267 PAAATFEETFRG--------PSLPSGDIARAEErrlaARDVADALDLPIGNAVDFWTEASlFSAAGYTALVYGPGDIAQA 338
|
....*..
gi 16131795 355 HQPDEYL 361
Cdd:PRK08737 339 HTADEFV 345
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
9-360 |
1.91e-34 |
|
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: 130.32 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATEealdqsnADLITLLADWFKDLGFNVEVQPVPGTRNkfnMLASIGQGAGGLLLAGHTDTVPF-D 87
Cdd:cd03891 1 LELAKELIRRPSVTPDD-------AGAQDLIAERLKALGFTCERLEFGGVKN---LWARRGTGGPHLCFAGHTDVVPPgD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 88 DGRWTRDPFTLTEHDGKLYGLGTADMKGFFA-FILDALRDVDVTK-LKKPLYILATADEETSmA--GARYFAETTA---L 160
Cdd:cd03891 71 LEGWSSDPFSPTIKDGMLYGRGAADMKGGIAaFVAAAERFVAKHPnHKGSISFLITSDEEGP-AidGTKKVLEWLKargE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 161 RPDCAIIGEPTSLQPV-------RahKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLR-DNlkeryHYEAF 232
Cdd:cd03891 150 KIDYCIVGEPTSEKKLgdtikigR--RGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVlDE-----GNEFF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 233 TvpyPT-LNLGHIHGG-DASNRICACCELHMDIR--PL--PGMTLNELNGLLNDALAPVSERW----------PGRLTvd 296
Cdd:cd03891 223 P---PSsLQITNIDVGnGATNVIPGELKAKFNIRfnDEhtGESLKARIEAILDKHGLDYDLEWklsgepfltkPGKLV-- 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131795 297 elhppipgyecppnHQLVEVVEKLLGAKTEVVNY--CTEAPFI-QTLCPTLVLGPgsINQ-AHQPDEY 360
Cdd:cd03891 298 --------------DAVSAAIKEVTGITPELSTSggTSDARFIaSYGCPVVEFGL--VNAtIHKVNER 349
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
8-377 |
1.80e-31 |
|
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: 122.31 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 8 FIEIYRALIATPSISATEEALDQsNADLitlLADWFKDLGFNVEVQPVPGTRNkfNMLASI-GQGAGGLLLAGHTDTVpF 86
Cdd:cd03885 1 MLDLLERLVNIESGTYDKEGVDR-VAEL---LAEELEALGFTVERRPLGEFGD--HLIATFkGTGGKRVLLIGHMDTV-F 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 87 DDGRWTRDPFTltEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKK--PLYILATADEETSMAGARYFAETTALRPDC 164
Cdd:cd03885 74 PEGTLAFRPFT--VDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDylPITVLLNSDEEIGSPGSRELIEEEAKGADY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 165 AIIGEPTSL--QPVRAHKGHISNAIRIQGQSGHSS-DPARGVNAI-ELMHdaigHILQLRDNLKeryhYEAFTvpypTLN 240
Cdd:cd03885 152 VLVFEPARAdgNLVTARKGIGRFRLTVKGRAAHAGnAPEKGRSAIyELAH----QVLALHALTD----PEKGT----TVN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 241 LGHIHGGDASNRICACCELHMDIRplpGMTLNELNGLLNDALAPVSER-WPG---RLTVDELHPPIPgyECPPNHQLVEV 316
Cdd:cd03885 220 VGVISGGTRVNVVPDHAEAQVDVR---FATAEEADRVEEALRAIVATTlVPGtsvELTGGLNRPPME--ETPASRRLLAR 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131795 317 VEKL-----LGAKTEVVNYCTEAPFI-QTLCPTL-VLGP---GsinqAHQPDEYLETRFIKPTRELITQVI 377
Cdd:cd03885 295 AQEIaaelgLTLDWEATGGGSDANFTaALGVPTLdGLGPvggG----AHTEDEYLELDSLVPRIKLLARLL 361
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
9-373 |
5.49e-31 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 120.63 E-value: 5.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATEEALdqsnADLITllaDWFKDLGFNVEVQPVPGTRNKFnmlasIGQGAGgLLLAGHTDTVPFdd 88
Cdd:PRK08652 5 KELLKQLVKIPSPSGQEDEI----ALHIM---EFLESLGYDVHIESDGEVINIV-----VNSKAE-LFVEVHYDTVPV-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 89 grwTRDPFtltEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYILATADEETSMAGARYFAETtaLRPDCAIIG 168
Cdd:PRK08652 70 ---RAEFF---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSDEEEGGRGSALFAER--YRPKMAIVL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 169 EPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHyeaftvpyPTLNLGHIHGGD 248
Cdd:PRK08652 142 EPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFD--------PHIGIQEIIGGS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 249 ASNRICACCELHMDIRPLPGMTLN----ELNGLLNDALA--PVSERWpgrltvdelhppiPGYECPPNHQLVEVVEKLLG 322
Cdd:PRK08652 214 PEYSIPALCRLRLDARIPPEVEVEdvldEIDPILDEYTVkyEYTEIW-------------DGFELDEDEEIVQLLEKAMK 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131795 323 AKTEVVNYC-----TEA-PFIQTLCPTLVLGPGSINQAHQPDEYLETRFIKPTRELI 373
Cdd:PRK08652 281 EVGLEPEFTvmrswTDAiNFRYNGTKTVVWGPGELDLCHTKFERIDVREVEKAKEFL 337
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
9-362 |
1.04e-30 |
|
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: 119.76 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATEEALDQsnadlitLLADWFKDLGFNVEVQPVPgtrnkfNMLASIGQGAGGLLLAGHTDTVPfdd 88
Cdd:cd05653 4 VELLLDLLSIYSPSGEEARAAK-------FLEEIMKELGLEAWVDEAG------NAVGGAGSGPPDVLLLGHIDTVP--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 89 grwtrDPFTLTEHDGKLYGLGTADMKG-FFAFILDALRdvdvTKLKKP--LYILATADEETSMAGARYFAEtTALRPDCA 165
Cdd:cd05653 68 -----GEIPVRVEGGVLYGRGAVDAKGpLAAMILAASA----LNEELGarVVVAGLVDEEGSSKGARELVR-RGPRPDYI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 166 IIGEPTSLQPVR-AHKGHISNAIRIQGQSGHSSDPARgvNAIELMHDAIGHILQLRDNLkERYHYEAFTVpYPTLnlghI 244
Cdd:cd05653 138 IIGEPSGWDGITlGYRGSLLVKIRCEGRSGHSSSPER--NAAEDLIKKWLEVKKWAEGY-NVGGRDFDSV-VPTL----I 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 245 HGGDASNRICACCELHMDIRpLPGMTLNELNGLLNDALAPVSErwpgrLTVDELHPPipgYECPPNHQLVEV-------- 316
Cdd:cd05653 210 KGGESSNGLPQRAEATIDLR-LPPRLSPEEAIALATALLPTCE-----LEFIDDTEP---VKVSKNNPLARAfrrairkq 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 16131795 317 -VEKLLGAKTEVVNYCTEAPFIQtlCPTLVLGPGSINQAHQPDEYLE 362
Cdd:cd05653 281 gGKPRLKRKTGTSDMNVLAPLWT--VPIVAYGPGDSTLDHTPNEHIE 325
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
15-364 |
4.13e-30 |
|
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: 118.74 E-value: 4.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 15 LIATPSISATEEALdqsnADLItllADWFKDLGF-NVEVQPVpgtrnkFNMLASI-GQGAG-GLLLAGHTDTVPFDDgrw 91
Cdd:cd03896 7 LGEIPAPTFREGAR----ADLV---AEWMADLGLgDVERDGR------GNVVGRLrGTGGGpALLFSAHLDTVFPGD--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 92 trDPFTLTEHDGKLYGLGTADMKGFFAFIL---DALRDVDVtKLKKPLYILATADEETS--MAGARYFAETTALRPDCAI 166
Cdd:cd03896 71 --TPATVRHEGGRIYGPGIGDNKGSLACLLamaRAMKEAGA-ALKGDVVFAANVGEEGLgdLRGARYLLSAHGARLDYFV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 167 IGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMhdaighiLQLRDNLkerYHYEAFTVPYPTLNLGHIHG 246
Cdd:cd03896 148 VAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAM-------AKLVEAL---YEWAAPYVPKTTFAAIRGGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 247 GDASNRICACCELHMDIRPLPGmtlNELNGLLNDALAPVSERWPGRLTVDELHPPI---PGYECPPNHQLVE---VVEKL 320
Cdd:cd03896 218 GTSVNRIANLCSMYLDIRSNPD---AELADVQREVEAVVSKLAAKHLRVKARVKPVgdrPGGEAQGTEPLVNaavAAHRE 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 16131795 321 LGAKTEVVNYCTEA-PFIQTLCPTLVLGPGSINQAHQPDEYLETR 364
Cdd:cd03896 295 VGGDPRPGSSSTDAnPANSLGIPAVTYGLGRGGNAHRGDEYVLKD 339
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
69-360 |
1.34e-28 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 115.48 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 69 GQGAGG--LLLAGHTDTVPFDD-GRWTRDPFTLTEHDGKLYGLGTADMKGFFA---FILDALRDVDVtKLKKPLYILATA 142
Cdd:PRK06837 92 PAGKTGrsLILQGHIDVVPEGPlDLWSRPPFDPVIVDGWMYGRGAADMKAGLAamlFALDALRAAGL-APAARVHFQSVI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 143 DEETSMAGARyfaeTTALR---PDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQL 219
Cdd:PRK06837 171 EEESTGNGAL----STLQRgyrADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALREL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 220 RDNLKERY----HYEafTVPYP-TLNLGHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVS--ERWPGR 292
Cdd:PRK06837 247 EAEWNARKasdpHFE--DVPHPiNFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAADAQAEIEACLAAAArdDRFLSN 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 293 ltvdelHPP--------IPGYECPPN----------HQLV-------EVVEKLLGAKTEVVNYCTeapfiqtlcPTLVLG 347
Cdd:PRK06837 325 ------NPPevvwsgflAEGYVLEPGseaeaalaraHAAVfggplrsFVTTAYTDTRFYGLYYGI---------PALCYG 389
|
330
....*....|...
gi 16131795 348 PGSINqAHQPDEY 360
Cdd:PRK06837 390 PSGEG-IHGFDER 401
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
177-290 |
2.80e-27 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 103.96 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 177 RAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHilqlrdnLKERYHYEAFTVPYPTLNLGHIHGGDASNRICAC 256
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAE-------LPAEYGDIGFDFPRTTLNITGIEGGTATNVIPAE 73
|
90 100 110
....*....|....*....|....*....|....
gi 16131795 257 CELHMDIRPLPGMTLNELNGLLNDALAPVSERWP 290
Cdd:pfam07687 74 AEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
11-323 |
3.07e-27 |
|
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.
Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 111.68 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 11 IYRALIATPSiSATEEALDQSNAdLITLLADWFKDLGFNVEVQPVPGTRNKFNMLASIGQG---AGGLLLAGHTDTVPFD 87
Cdd:cd05675 3 LLQELIRIDT-TNSGDGTGSETR-AAEVLAARLAEAGIQTEIFVVESHPGRANLVARIGGTdpsAGPLLLLGHIDVVPAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 88 DGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDV--DVTKLKKPLYILATADEET-SMAGARYFAETtalRPDC 164
Cdd:cd05675 81 ASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYkrEGFKPKRDLVFAFVADEEAgGENGAKWLVDN---HPEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 165 ------AI---------IGEPTSLQPVR-AHKGHISNAIRIQGQSGHSSDPARGvNAIELMHDAIGHI------LQLRDN 222
Cdd:cd05675 158 fdgatfALneggggslpVGKGRRLYPIQvAEKGIAWMKLTVRGRAGHGSRPTDD-NAITRLAEALRRLgahnfpVRLTDE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 223 LKERYHYEAFTVPY-------------PTLN-LGH-----------------IHGGDASNRICACCELHMDIRPLPGMTL 271
Cdd:cd05675 237 TAYFAQMAELAGGEggalmltavpvldPALAkLGPsapllnamlrntasptmLDAGYATNVLPGRATAEVDCRILPGQSE 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 16131795 272 NELNGLLNDALAPvserwPgRLTVDELHPPiPGYECPPNHQLVEVVEKLLGA 323
Cdd:cd05675 317 EEVLDTLDKLLGD-----P-DVSVEAVHLE-PATESPLDSPLVDAMEAAVQA 361
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
8-362 |
4.52e-27 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 110.14 E-value: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 8 FIEiyraLIATPSISATEEALdqsnADLitlLADWFKDLGFNVEVqpvpgtRNKFNML----ASIGQGAGGLLLAGHTDT 83
Cdd:COG2195 9 FLE----YVKIPTPSDHEEAL----ADY---LVEELKELGLEVEE------DEAGNVIatlpATPGYNVPTIGLQAHMDT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 84 VP----------FDDGRWTRDPFTLtehdgklygLGtADMKGFFAFILDALRDVDVTKLK-KPLYILATADEETSMAGAR 152
Cdd:COG2195 72 VPqfpgdgikpqIDGGLITADGTTT---------LG-ADDKAGVAAILAALEYLKEPEIPhGPIEVLFTPDEEIGLRGAK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 153 YFaETTALRPDCAII---GEPTSLQpvrahkghISNA------IRIQGQSGHSSD-PARGVNAIELMHDAIGHILQLRdn 222
Cdd:COG2195 142 AL-DVSKLGADFAYTldgGEEGELE--------YECAgaadakITIKGKGGHSGDaKEKMINAIKLAARFLAALPLGR-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 223 LKERYhyeaftvpypTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSERWP-GRLTVdELHPP 301
Cdd:COG2195 211 IPEET----------EGNEGFIHGGSATNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGvGVVEV-EIEDQ 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131795 302 IPGYECPPNHQLVEVVEKL---LG--AKTEVVNYCTEAPFIQT--LcPTLVLGPGsINQAHQPDEYLE 362
Cdd:COG2195 280 YPNWKPEPDSPIVDLAKEAyeeLGiePKIKPIRGGLDGGILSFkgL-PTPNLGPG-GHNFHSPDERVS 345
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
9-264 |
9.47e-27 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 109.41 E-value: 9.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATEealdqsnADLITLLADWFKDLGFNVEVQPVPGTRNkfnMLASIGQGAGGLLLAGHTDTVPF-D 87
Cdd:PRK13009 5 LELAQDLIRRPSVTPDD-------AGCQDLLAERLEALGFTCERMDFGDVKN---LWARRGTEGPHLCFAGHTDVVPPgD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 88 DGRWTRDPFTLTEHDGKLYGLGTADMKGFFA-FILDALRDVDVTKLKKP-LYILATADEETSmA--GARYFAETTA---L 160
Cdd:PRK13009 75 LEAWTSPPFEPTIRDGMLYGRGAADMKGSLAaFVVAAERFVAAHPDHKGsIAFLITSDEEGP-AinGTVKVLEWLKargE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 161 RPDCAIIGEPTSLQPV-------RahKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLR-DNlkeryHYEAF 232
Cdd:PRK13009 154 KIDYCIVGEPTSTERLgdvikngR--RGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEwDE-----GNEFF 226
|
250 260 270
....*....|....*....|....*....|...
gi 16131795 233 tvPYPTLNLGHIHGG-DASNRICACCELHMDIR 264
Cdd:PRK13009 227 --PPTSLQITNIDAGtGATNVIPGELEAQFNFR 257
|
|
| PRK06915 |
PRK06915 |
peptidase; |
69-381 |
1.13e-26 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 110.17 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 69 GQGAG-GLLLAGHTDTVPFDD-GRWTRDPFTLTEHDGKLYGLGTADMKG-----FFAfiLDALRDVDVTkLKKPLYILAT 141
Cdd:PRK06915 89 GSGGGkSMILNGHIDVVPEGDvNQWDHHPYSGEVIGGRIYGRGTTDMKGgnvalLLA--MEALIESGIE-LKGDVIFQSV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 142 ADEETSMAGARyfaeTTALR---PDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQ 218
Cdd:PRK06915 166 IEEESGGAGTL----AAILRgykADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRK 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 219 LRDNLKERYH---YEAFTVPYPtLNLGHIHGGDASNRICACCELHMDIRPLPGMTLN----ELNGLLND--------ALA 283
Cdd:PRK06915 242 LEEKRNDRITdplYKGIPIPIP-INIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEaakeEFENWIAElndvdewfVEH 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 284 PVSERWPGRLTVdelhppiPGyECPPNHQLVevveKLLGAKTEVVNycTEAPFIQTL--------------CPTLVLGPG 349
Cdd:PRK06915 321 PVEVEWFGARWV-------PG-ELEENHPLM----TTLEHNFVEIE--GNKPIIEASpwgtdgglltqiagVPTIVFGPG 386
|
330 340 350
....*....|....*....|....*....|..
gi 16131795 350 SINQAHQPDEYLETRFIKPTRELITQVIHHFC 381
Cdd:PRK06915 387 ETKVAHYPNEYIEVDKMIAAAKIIALTLLDWC 418
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
9-377 |
8.65e-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: 103.68 E-value: 8.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATEEALdqsnADLITlladwfKDLGFN--VEVqpvpgTRNKFNMLASIGQG-AGGLLLAGHTDTVP 85
Cdd:cd05647 2 IELTAALVDIPSVSGNEKPI----ADEIE------AALRTLphLEV-----IRDGNTVVARTERGlASRVILAGHLDTVP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 86 FDD---GRWtrdpftltEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYILATADEETSMA--GARYFAETTA- 159
Cdd:cd05647 67 VAGnlpSRV--------EEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLTLIFYDCEEVAAElnGLGRLAEEHPe 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 160 -LRPDCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIElmhdaighilQLRDNLKERYHYEAFTVP--- 235
Cdd:cd05647 139 wLAADFAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIH----------KLAPILARLAAYEPRTVNidg 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 236 ---YPTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALapvsERWPGRLTVDELHP-PIPGYECPPNH 311
Cdd:cd05647 209 ltyREGLNAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVF----EGLGYEIEVTDLSPgALPGLDHPVAR 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131795 312 QLVEVVEKLLGAK---TEVvnycteAPFIQTLCPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVI 377
Cdd:cd05647 285 DLIEAVGGKVRAKygwTDV------ARFSALGIPAVNFGPGDPLLAHKRDEQVPVEQITACAAILRRWL 347
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
6-377 |
2.79e-24 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 103.17 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 6 PPFIEIYRALIATPSISATEEALDQSNAdlitLLADWFKDLGFNVEVQPVPGTRNKfNMLASI-GQGAGGLLLAGHTDTV 84
Cdd:PRK06133 37 PAYLDTLKELVSIESGSGDAEGLKQVAA----LLAERLKALGAKVERAPTPPSAGD-MVVATFkGTGKRRIMLIAHMDTV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 85 pFDDGRWTRDPFTltEHDGKLYGLGTADMKGFFAFILDA---LRDVDVTKLKKpLYILATADEETSMAGARYFAETTALR 161
Cdd:PRK06133 112 -YLPGMLAKQPFR--IDGDRAYGPGIADDKGGVAVILHAlkiLQQLGFKDYGT-LTVLFNPDEETGSPGSRELIAELAAQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 162 PDCAIIGEPT----SLqpVRAHKGHISNAIRIQGQSGHS-SDPARGVNA-IELMHdaigHILQLRDNLKEryhyeaftVP 235
Cdd:PRK06133 188 HDVVFSCEPGrakdAL--TLATSGIATALLEVKGKASHAgAAPELGRNAlYELAH----QLLQLRDLGDP--------AK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 236 YPTLNLGHIHGGDASNRICACCELHMDIRPL-PGMT---LNELNGLLNDALAPVSERwpgRLTVDELHPPIPgyECPPNH 311
Cdd:PRK06133 254 GTTLNWTVAKAGTNRNVIPASASAQADVRYLdPAEFdrlEADLQEKVKNKLVPDTEV---TLRFERGRPPLE--ANAASR 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131795 312 QLVEVVEKL---LGAKTEVVNYC----TEAPFI--QTLCPTL----VLGPGsinqAHQPDEYLETRFIKPTRELITQVI 377
Cdd:PRK06133 329 ALAEHAQGIygeLGRRLEPIDMGtgggTDAAFAagSGKAAVLegfgLVGFG----AHSNDEYIELNSIVPRLYLLTRMI 403
|
|
| dapE-gram_pos |
TIGR01900 |
succinyl-diaminopimelate desuccinylase; This model represents a clade of ... |
9-363 |
3.46e-23 |
|
succinyl-diaminopimelate desuccinylase; This model represents a clade of succinyl-diaminopimelate desuccinylases from actinobacteria (high-GC gram positives), delta-proteobacteria and aquificales and is based on the characterization of the enzyme from Corynebacterium glutamicum. This enzyme is involved in the biosynthesis of lysine, and is related to the enzyme acetylornithine deacetylase and other amidases and peptidases found within pfam01546. Other sequences included in the seed of this model were assessed to confirm that 1) the related genes DapC (succinyl-diaminopimelate transaminase) and DapD (2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase) are also found in the genome, 2) each is found only once in those genomes, 3) the lysine biosynthesis pathway is complete and 4) the direct (TIGR03540 or TIGR03542) or acetylated (GenProp0787) aminotransferase pathways are absent in thes genomes. Additionally, a number of the seed members are observed adjacent to either DapC or DapD (often as a divergon with a putative promoter site between them. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273864 [Multi-domain] Cd Length: 351 Bit Score: 99.28 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATEEALdqsnADLItllADWFKDL-GFNVEvqpvpgtRNKFNMLASIGQG-AGGLLLAGHTDTVPF 86
Cdd:TIGR01900 6 AELTAALVDIPSVSGDERAL----ADAV---ESALRALpHLEVI-------RHGNSVVARTNLGrPSRVILAGHLDTVPI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 87 DDGrwtrdpFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYILATADEETSmagaryfAETTALRP---- 162
Cdd:TIGR01900 72 ADN------LPSRVEGGRLYGRGAVDMKGGLAVMLALAATLDRTEPRHDLTLVFYEREEGP-------AEENGLGRllre 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 163 -------DCAIIGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIelmhDAIGHILQLRDNLKERY------HY 229
Cdd:TIGR01900 139 hpewlagDLAVLLEPTDGKIEAGCQGTLRATVTFHGRRAHSARSWMGENAI----HKAAPILARLAAYEPREvtvdglTY 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 230 eaftvpYPTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDalapVSERWPGRLTVDELHPP-IPGYECP 308
Cdd:TIGR01900 215 ------REGLNAVRIEGGVAGNVIPDECEVNVNYRFAPDRSLEQARAHVRE----LFEGDGAEVEVTDLSPGaRPGLDNP 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 16131795 309 PNHQLVEVVEKLLGAK---TEVvnycteAPFIQTLCPTLVLGPGSINQAHQPDEYLET 363
Cdd:TIGR01900 285 LAAELVAAVGGEVRAKygwTDV------ARFSALGIPAVNFGPGDPALAHQDDEHVPV 336
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
9-367 |
8.22e-23 |
|
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: 98.68 E-value: 8.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSI---SATEEALDQSNAdlitlLADWFKDLGFN-VEVQPVPGTRNKF--NMLASIGQGAGGLL-LAGHT 81
Cdd:cd05650 4 IELERDLIRIPAVnpeSGGEGEKEKADY-----LEKKLREYGFYtLERYDAPDERGIIrpNIVAKIPGGNDKTLwIISHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 82 DTVPFDD-GRWTRDPFTLTEHDGKLYGLGTAD-MKGFFA--FILDALRDVDVTKlKKPLYILATADEET-SMAGARYFAE 156
Cdd:cd05650 79 DTVPPGDlSLWETDPWEPVVKDGKIYGRGVEDnQQGIVSslLALKAIIKNGITP-KYNFGLLFVADEEDgSEYGIQYLLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 157 TTAL-RPDCAII----GEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAielMHDAIGHILQLRDNLKERYHY-- 229
Cdd:cd05650 158 KFDLfKKDDLIIvpdfGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINA---FVAASNFALELDELLHEKFDEkd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 230 EAFTVPYPTL----------NLGHIHGGDasnricaccELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGRLTVDELH 299
Cdd:cd05650 235 DLFNPPYSTFeptkkeanvpNVNTIPGYD---------VFYFDCRVLPTYKLDEVLKFVNKIISDFENSYGAGITYEIVQ 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131795 300 PPIPGYECPPN----HQLVEVVEKLLG--AKTEVVNYCTEAPFIQTL-CPTLVLGPGsINQAHQPDEYletRFIK 367
Cdd:cd05650 306 KEQAPPATPEDseivVRLSKAIKKVRGreAKLIGIGGGTVAAFLRKKgYPAVVWSTL-DETAHQPNEY---IRIS 376
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
9-362 |
1.22e-22 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 97.72 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATEEALDQsnadlitLLADWFKDLGFNVEVQPVpGtrnkfNMLASIGQGAGGLLLAGHTDTVPFDd 88
Cdd:PRK04443 9 RELLKGLVEIPSPSGEEAAAAE-------FLVEFMESHGREAWVDEA-G-----NARGPAGDGPPLVLLLGHIDTVPGD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 89 grwtrDPFTLteHDGKLYGLGTADMKG-FFAFILDALRdvDVTKLKKPLYILATADEETSMAGARYFAETTaLRPDCAII 167
Cdd:PRK04443 75 -----IPVRV--EDGVLWGRGSVDAKGpLAAFAAAAAR--LEALVRARVSFVGAVEEEAPSSGGARLVADR-ERPDAVII 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 168 GEPTSLQPVR-AHKGHISNAIRIQGQSGHSSDParGVNAIElmhDAIGHILQLRDNLKERYHYE-AFTVPYPTLNLGHIH 245
Cdd:PRK04443 145 GEPSGWDGITlGYKGRLLVTYVATSESFHSAGP--EPNAAE---DAIEWWLAVEAWFEANDGRErVFDQVTPKLVDFDSS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 246 GGDASNRicacCELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGrltvdelhpPIPGYECPPNHQLV----------- 314
Cdd:PRK04443 220 SDGLTVE----AEMTVGLRLPPGLSPEEAREILDALLPTGTVTFTG---------AVPAYMVSKRTPLArafrvaireag 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 16131795 315 -EVVEKLlgaKT-----EVVnycteAPFIQtlCPTLVLGPGSINQAHQPDEYLE 362
Cdd:PRK04443 287 gTPRLKR---KTgtsdmNVV-----APAWG--CPMVAYGPGDSDLDHTPDEHLP 330
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
12-361 |
1.90e-22 |
|
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: 98.17 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 12 YRALIATPSISATEEALDQS--NADLItllADWFKDLGFNVE-VQPVPGTRNkfnMLASIG--QGAGGLLLAGHTDTVPF 86
Cdd:cd03893 4 LAELVAIPSVSAQPDRREELrrAAEWL---ADLLRRLGFTVEiVDTSNGAPV---VFAEFPgaPGAPTVLLYGHYDVQPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 87 DD-GRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYI--LATADEETSMAGARYFAETTA--LR 161
Cdd:cd03893 78 GDeDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVkfIIEGEEESGSPSLDQLVEAHRdlLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 162 PDCAIIGEPTSL---QP--VRAHKGHISNAIRIQGQSG--HSS-------DP-ARGVNAIELMHDAIGHIL------QLR 220
Cdd:cd03893 158 ADAIVISDSTWVgqeQPtlTYGLRGNANFDVEVKGLDHdlHSGlyggvvpDPmTALAQLLASLRDETGRILvpglydAVR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 221 DNLKERYH-----YEAFTVP-------------YPTLNL----GHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLL 278
Cdd:cd03893 238 ELPEEEFRldagvLEEVEIIggttgsvaerlwtRPALTVlgidGGFPGEGSKTVIPPRARAKISIRLVPGQDPEEASRLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 279 NDAL---APvserWPGRLTV---DELHPpipgYECPPNHQLVEVVEKLL----GAKTEVVNYCTEAPFIQTL-----CPT 343
Cdd:cd03893 318 EAHLekhAP----SGAKVTVsyvEGGMP----WRSDPSDPAYQAAKDALrtayGVEPPLTREGGSIPFISVLqefpqAPV 389
|
410
....*....|....*....
gi 16131795 344 LVLGPGSIN-QAHQPDEYL 361
Cdd:cd03893 390 LLIGVGDPDdNAHSPNESL 408
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
9-360 |
2.50e-21 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 94.53 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISAT-----EEAldqsNADLItllADWFKDLGFN-VEVQPVPGTRNKF----NMLASI--GQGAGGLL 76
Cdd:PRK13983 8 IELLSELIAIPAVNPDfggegEKE----KAEYL---ESLLKEYGFDeVERYDAPDPRVIEgvrpNIVAKIpgGDGKRTLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 77 LAGHTDTVPF-DDGRWTRDPFTLTEHDGKLYGLGTAD-MKGFFA--FILDALRDVDVtKLKKPLYILATADEET-SMAGA 151
Cdd:PRK13983 81 IISHMDVVPPgDLSLWETDPFKPVVKDGKIYGRGSEDnGQGIVSslLALKALMDLGI-RPKYNLGLAFVSDEETgSKYGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 152 RYFAETTA--LRPDCAII----GEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELmhdAIGHILQLRDNLKE 225
Cdd:PRK13983 160 QYLLKKHPelFKKDDLILvpdaGNPDGSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRA---AADFALELDEALHE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 226 RYHY--EAFTVPY----PTL------NLGHIHGGDasnricaccELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGRL 293
Cdd:PRK13983 237 KFNAkdPLFDPPYstfePTKkeanvdNINTIPGRD---------VFYFDCRVLPDYDLDEVLKDIKEIADEFEEEYGVKI 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131795 294 TVDELHPPIPGYECPPNHqlvEVVEKLLGAKTEVVN----YC-----TEAPFIQTL-CPTLVLGPGsINQAHQPDEY 360
Cdd:PRK13983 308 EVEIVQREQAPPPTPPDS---EIVKKLKRAIKEVRGiepkVGgigggTVAAFLRKKgYPAVVWSTL-DETAHQPNEY 380
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
31-319 |
3.48e-21 |
|
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: 94.16 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 31 SNADLITLLADWFKDLGFNVEVQPVP-------GTRNKFNMLASIGQGAGGLLLA--GHTDTVPFDDGrWTRDPFTLTEH 101
Cdd:cd02697 23 NNAPHAERTAALLQGFGFEAERHPVPeaevrayGMESITNLIVRRRYGDGGRTVAlnAHGDVVPPGDG-WTRDPYGAVVE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 102 DGKLYGLGTADMKGFFA---FILDALRDVDVTkLKKPLYILATADEET-SMAGARYFAETTALRPDCAIIGEpTSLQPVR 177
Cdd:cd02697 102 DGVMYGRAAAVSKSDFAsftFAVRALESLGAP-LRGAVELHFTYDEEFgGELGPGWLLRQGLTKPDLLIAAG-FSYEVVT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 178 AHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKE-RYHYEAFTVPYptLNLGHIHGGDASNRICAC 256
Cdd:cd02697 180 AHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNAQYRQvSSQVEGITHPY--LNVGRIEGGTNTNVVPGK 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131795 257 CELHMDIRPLPGMTLNELNGLLNDALAPVSERWPG------RLTVDELHPPIPGyecppNHQLVEVVEK 319
Cdd:cd02697 258 VTFKLDRRMIPEENPVEVEAEIRRVIADAAASMPGisvdirRLLLANSMRPLPG-----NAPLVEAIQT 321
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
9-360 |
1.17e-20 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 92.90 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISATEEALdqsnADLITLLADWFKDLGFNVEV---QPVPGTRNKF---NMLASIGQGAGGLL--LAGH 80
Cdd:PRK13013 17 VALTQDLIRIPTLNPPGRAY----REICEFLAARLAPRGFEVELiraEGAPGDSETYprwNLVARRQGARDGDCvhFNSH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 81 TDTVPFDDGrWTRDPFTLTEHDGKLYGLGTADMKGFFA---FILDALRDVDVtKLKKPLYILATADEET-SMAGARYFAE 156
Cdd:PRK13013 93 HDVVEVGHG-WTRDPFGGEVKDGRIYGRGACDMKGGLAasiIAAEAFLAVYP-DFAGSIEISGTADEESgGFGGVAYLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 157 T---TALRPDCAIIGEPTSLQPV-RAHKGHISNAIRIQGQSGHSSDPARGVNAIELMhdaiGHILQ-LRDNLKERYHYEA 231
Cdd:PRK13013 171 QgrfSPDRVQHVIIPEPLNKDRIcLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHM----GAVLAeIEERLFPLLATRR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 232 FTVP-------YPTLNLGHIHGG------DASNRICAC----CELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGRL- 293
Cdd:PRK13013 247 TAMPvvpegarQSTLNINSIHGGepeqdpDYTGLPAPCvadrCRIVIDRRFLIEEDLDEVKAEITALLERLKRARPGFAy 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131795 294 ---TVDELHPPIPGYECPPNHQLVEVVEKLLGAKTE-VVNYCT----EAPFIQTLCPTLVLGPGSINQAHQPDEY 360
Cdd:PRK13013 327 eirDLFEVLPTMTDRDAPVVRSVAAAIERVLGRQADyVVSPGTydqkHIDRIGKLKNCIAYGPGILDLAHQPDEW 401
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
8-216 |
3.36e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 91.60 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 8 FIEIYRALIATPSISATeealdQSNADLITLLADWFKDLGF-NVEVQPVPGTRNKFNMLASI-GQGAGG-LLLAGHTDTV 84
Cdd:PRK09133 39 ARDLYKELIEINTTAST-----GSTTPAAEAMAARLKAAGFaDADIEVTGPYPRKGNLVARLrGTDPKKpILLLAHMDVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 85 PFDDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALrdvdvTKLK----KP---LYILATADEE-TSMAGARYFAE 156
Cdd:PRK09133 114 EAKREDWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATL-----IRLKregfKPkrdIILALTGDEEgTPMNGVAWLAE 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131795 157 TT--ALRPDCAI----------IGEPTSLQPVRAHKGHISNAIRIQGQSGHSSDPaRGVNAIELMHDAIGHI 216
Cdd:PRK09133 189 NHrdLIDAEFALneggggtldeDGKPVLLTVQAGEKTYADFRLEVTNPGGHSSRP-TKDNAIYRLAAALSRL 259
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
8-383 |
2.99e-19 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 88.56 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 8 FIEIYRALIA--TPSISA--TEEALDQsnadlitlLADWFKDLGFNVEVQPV-PGTRNKFNMLASIGQGA-GGLLLAGHT 81
Cdd:PRK08596 15 LLELLKTLVRfeTPAPPArnTNEAQEF--------IAEFLRKLGFSVDKWDVyPNDPNVVGVKKGTESDAyKSLIINGHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 82 DTVPFDDGR-WTRDPFTLTEHDGKLYGLGTADMKGFFA---FILDALRDVDVtKLKKPLYILATADEETSMAGARYFAEt 157
Cdd:PRK08596 87 DVAEVSADEaWETNPFEPTIKDGWLYGRGAADMKGGLAgalFAIQLLHEAGI-ELPGDLIFQSVIGEEVGEAGTLQCCE- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 158 TALRPDCAIIGEPTSLQpVRAHKGHISNAIRIQG----------QSGHSSDPARGVNAIELMHDAIGHILQLrdnlkERy 227
Cdd:PRK08596 165 RGYDADFAVVVDTSDLH-MQGQGGVITGWITVKSpqtfhdgtrrQMIHAGGGLFGASAIEKMMKIIQSLQEL-----ER- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 228 HYeAFTVPYP-------TLNLGHIHGGDASNRICACCELHMDIRPLPGMT----LNELNGLLNDALA--------PVSER 288
Cdd:PRK08596 238 HW-AVMKSYPgfppgtnTINPAVIEGGRHAAFIADECRLWITVHFYPNETyeqvIKEIEEYIGKVAAadpwlrenPPQFK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 289 WPGRLTVDELHPPIPGYECPPNH----QLVEVVEKLLGAKTE--VVNYCTEAPFIQTL-CPTLVLGPGSINQAHQPDEYL 361
Cdd:PRK08596 317 WGGESMIEDRGEIFPSLEIDSEHpavkTLSSAHESVLSKNAIldMSTTVTDGGWFAEFgIPAVIYGPGTLEEAHSVNEKV 396
|
410 420
....*....|....*....|...
gi 16131795 362 E-TRFIKPTrELITQVIHHFCWH 383
Cdd:PRK08596 397 EiEQLIEYT-KVITAFIYEWCHT 418
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
8-362 |
1.70e-18 |
|
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: 86.53 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 8 FIEIYRALIATPSI--SATEEA-LDQSNADLITLLADWFKDLGFNvevqpvpgTRNKFNMLASIGQGAGGLLLA--GHTD 82
Cdd:cd03888 10 ILEDLKELVAIPSVrdEATEGApFGEGPRKALDKFLDLAKRLGFK--------TKNIDNYAGYAEYGEGEEVLGilGHLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 83 TVPFDDGrWTRDPFTLTEHDGKLYGLGTADMKG-----FFAfiLDALRDVDVtKLKKPLYILATADEETSMAG-ARYFAE 156
Cdd:cd03888 82 VVPAGEG-WTTDPFKPVIKDGKLYGRGTIDDKGptiaaLYA--LKILKDLGL-PLKKKIRLIFGTDEETGWKCiEHYFEH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 157 ----TTALRPDC---AIIGE------------------------------------------PTSLQPVRAHKGHISNA- 186
Cdd:cd03888 158 eeypDFGFTPDAefpVINGEkgivtvdltfkidddkgyrlisikggeatnmvpdkaeavipgKDKEELALSAATDLKGNi 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 187 --------IRIQGQSGHSSDPARGVNAIELM----------HDAIGHILQLRDNLKERYHYEAFTVPYP-------TLNL 241
Cdd:cd03888 238 eiddggveLTVTGKSAHASAPEKGVNAITLLakflaelnkdGNDKDFIKFLAKNLHEDYNGKKLGINFEdevmgelTLNP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 242 GHIHGGDASNricaccELHMDIRPLPGMTLNElnglLNDALAPVSERWPGRLTVDELHPPIpgYeCPPNHQLV----EVV 317
Cdd:cd03888 318 GIITLDDGKL------ELGLNVRYPVGTSAED----IIKQIEEALEKYGVEVEGHKHQKPL--Y-VPKDSPLVktllKVY 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 16131795 318 EKLLGAKTEVV-----NYCTEAPFIQTLCPTLvlgPGSINQAHQPDEYLE 362
Cdd:cd03888 385 EEQTGKEGEPVaigggTYARELPNGVAFGPEF---PGQKDTMHQANEFIP 431
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
8-362 |
3.16e-18 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 85.89 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 8 FIEIYRALIATPSI----SATEEA-LDQSNADLITLLADWFKDLGFNVEvqpvpgTRNKFNMLASIGQGAGGLLLAGHTD 82
Cdd:TIGR01887 4 ILEDLKELIAIDSVedleKAKEGApFGEGPRKALDKFLEIAKRDGFTTE------NVDNYAGYIEYGQGEEVLGILGHLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 83 TVPFDDGrWTRDPFTLTEHDGKLYGLGTADMKG-----FFAfiLDALRDVDVtKLKKPLYILATADEETSMAG-ARYF-- 154
Cdd:TIGR01887 78 VVPAGDG-WTSPPFEPTIKDGRIYGRGTLDDKGptiaaYYA--MKILKELGL-KLKKKIRFIFGTDEESGWKCiDYYFeh 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 155 --AETTALRPDC---------------------------------------------AIIGEPTSLQPVRAHKGHISNA- 186
Cdd:TIGR01887 154 eeMPDIGFTPDAefpiiygekgittleikfkddtegdvvlesfkageaynmvpdhatAVISGKKLTEVEQLKFVFFIAKe 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 187 -------------IRIQGQSGHSSDPARGVNAI----------ELMHDAIGHILQLRDNLKERYHYEAFTVPYP------ 237
Cdd:TIGR01887 234 legdfevndgtltITLEGKSAHGSAPEKGINAAtylalflaqlNLAGGAKAFLQFLAEYLHEDHYGEKLGIKFHddvsgd 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 238 -TLNLGHI---HGGDASNRIcaccelhmDIR-PLpgmtLNELNGLLNDALAPVSErwPGRLTVDELHPPIpgYeCPPNHQ 312
Cdd:TIGR01887 314 lTMNVGVIdyeNAEAGLIGL--------NVRyPV----GNDPDTMLKNELAKESG--VVEVTLNGYLKPL--Y-VPKDDP 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131795 313 LV----EVVEKLLGAKTEVV-----NYCTEAPFIQTLCPtlvLGPGSINQAHQPDEYLE 362
Cdd:TIGR01887 377 LVqtlmKVYEKQTGDEGEPVaigggTYARLMPNGVAFGA---LFPGEEDTMHQANEYIM 432
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
8-217 |
1.64e-17 |
|
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: 83.54 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 8 FIEIYRALIATPSISATEEALDQSnADLitlLADWFKDLGFNVEVQPVPGtrNKFnMLASIGQGAGG-LLLAGHTDTVPF 86
Cdd:cd05681 1 YLEDLRDLLKIPSVSAQGRGIPET-ADF---LKEFLRRLGAEVEIFETDG--NPI-VYAEFNSGDAKtLLFYNHYDVQPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 87 D-DGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYI--LATADEETSMAGARYFAETTA--LR 161
Cdd:cd05681 74 EpLELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIkfLVEGEEEVGSPNLEKFVAEHAdlLK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 162 PDCAI-----IGEPTSLQPVRAHKGHISNAIRIQGQSG--HSS------DPA-RGVNAIELMHDAIGHIL 217
Cdd:cd05681 154 ADGCIwegggKNPKGRPQISLGVKGIVYVELRVKTADFdlHSSygaiveNPAwRLVQALNSLRDEDGRVL 223
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
75-367 |
5.57e-15 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 75.60 E-value: 5.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 75 LLLAGHTDTVPFDDGRWTRDPFT-LTEHDGKLYGLGTADMKGFFAFILDALRDVDVT--KLKKPLYILATADEET-SMAG 150
Cdd:TIGR01880 74 ILLNSHTDVVPVFREHWTHPPFSaFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASgfKFKRTIHISFVPDEEIgGHDG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 151 ARYFAETT---ALRPDCAI---IGEPTSLQPV-RAHKGHISNAIRIQGQSGHSSDPARGvNAIELMHDAIGHILQLRDNL 223
Cdd:TIGR01880 154 MEKFAKTDefkALNLGFALdegLASPDDVYRVfYAERVPWWVVVTAPGNPGHGSKLMEN-TAMEKLEKSVESIRRFRESQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 224 KERYH--YEAFTVPYPTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPV--------SERWPgrl 293
Cdd:TIGR01880 233 FQLLQsnPDLAIGDVTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAgegvtyefSQHSG--- 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 294 tvdeLHPPIPGYECPPNHQLVEVVEKLLG--AKTEVVNYCTEAPFIQTL-CPTLVLGPgsINQ----AHQPDEYL-ETRF 365
Cdd:TIGR01880 310 ----KPLVTPHDDSNPWWVAFKDAVKEMGctFKPEILPGSTDSRYIRAAgVPALGFSP--MNNtpvlLHDHNEFLnEAVF 383
|
..
gi 16131795 366 IK 367
Cdd:TIGR01880 384 LR 385
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
69-188 |
6.87e-15 |
|
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 72.47 E-value: 6.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 69 GQGAGGLLLAGHTDTVPFDDGRWTRDPF-TLTEHDGKLYGLGTADMKGFFAFILDALRDV--DVTKLKKPLYILATADEE 145
Cdd:cd18669 9 GGGGKRVLLGAHIDVVPAGEGDPRDPPFfVDTVEEGRLYGRGALDDKGGVAAALEALKLLkeNGFKLKGTVVVAFTPDEE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 16131795 146 TSMAGARYFAETTALRP----DCAIIGEPTS-LQPVRAHKGHISNAIR 188
Cdd:cd18669 89 VGSGAGKGLLSKDALEEdlkvDYLFVGDATPaPQKGVGIRTPLVDALS 136
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
2-302 |
3.07e-14 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 73.28 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 2 KNKLPPFIEIYraliaTPSisateealdQSNADLITLLADWFKDLGFNVEVQPvpgTRNKFNMlasigqGAGGLLLAGHT 81
Cdd:PRK00466 13 KELLLDLLSIY-----TPS---------GNETNATKFFEKISNELNLKLEILP---DSNSFIL------GEGDILLASHV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 82 DTVPfddGRWtrDPFTLTEhdgKLYGLGTADMKGFFAFILDALRDVDVTKLKkpLYILATADEETSMAGARYFAeTTALR 161
Cdd:PRK00466 70 DTVP---GYI--EPKIEGE---VIYGRGAVDAKGPLISMIIAAWLLNEKGIK--VMVSGLADEESTSIGAKELV-SKGFN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 162 PDCAIIGEPT-SLQPVRAHKGHISNAIRIQGQSGHSSDPARgvNAIELMHDAIGHILQLRDNlkeryhYEAFTVpYPTLn 240
Cdd:PRK00466 139 FKHIIVGEPSnGTDIVVEYRGSIQLDIMCEGTPEHSSSAKS--NLIVDISKKIIEVYKQPEN------YDKPSI-VPTI- 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131795 241 lghIHGGDASNRICACCELHMDIRplpgmtlNELNGLLNDALAPVSERWPG-RLTVDELHPPI 302
Cdd:PRK00466 209 ---IRAGESYNVTPAKLYLHFDVR-------YAINNKRDDLISEIKDKFQEcGLKIVDETPPV 261
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
8-115 |
6.40e-14 |
|
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: 72.63 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 8 FIEIYRALIATPSISATEEALDQSNaDLITLLADWFKDLGFNVEVQPVPgtRNKFN----------MLASIGQ--GAGGL 75
Cdd:cd05676 12 FIERLREAVAIQSVSADPEKRPELI-RMMEWAAERLEKLGFKVELVDIG--TQTLPdgeelplppvLLGRLGSdpSKKTV 88
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 16131795 76 LLAGHTDTVP--FDDGrWTRDPFTLTEHDGKLYGLGTADMKG 115
Cdd:cd05676 89 LIYGHLDVQPakLEDG-WDTDPFELTEKDGKLYGRGSTDDKG 129
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
71-163 |
1.45e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 71.42 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 71 GAGGLLLAGHTDTVPFDDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKP--LYILATADEETSM 148
Cdd:PRK07906 64 SRPALLVHGHLDVVPAEAADWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPrdLVFAFVADEEAGG 143
|
90
....*....|....*.
gi 16131795 149 A-GARYFAETtalRPD 163
Cdd:PRK07906 144 TyGAHWLVDN---HPE 156
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
75-265 |
2.30e-13 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 70.76 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 75 LLLAGHTDTV-----PFDDGRWtRDpftltehDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPL-Y-ILATADEET- 146
Cdd:PRK07338 95 VLLTGHMDTVfpadhPFQTLSW-LD-------DGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLgYdVLINPDEEIg 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 147 SMAGARYFAEtTALRPDCAIIGEPT----SLQPVRAHKGHISnaIRIQGQSGHSS-DPARGVNAIELMHDAIG--HILQ- 218
Cdd:PRK07338 167 SPASAPLLAE-LARGKHAALTYEPAlpdgTLAGARKGSGNFT--IVVTGRAAHAGrAFDEGRNAIVAAAELALalHALNg 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16131795 219 LRDNLkeryhyeaftvpypTLNLGHIHGGDASNRICACCELHMDIRP 265
Cdd:PRK07338 244 QRDGV--------------TVNVAKIDGGGPLNVVPDNAVLRFNIRP 276
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
64-181 |
3.68e-13 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 70.57 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 64 MLASIGQGAGGLLLAGHTDTVPFDDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYILATAD 143
Cdd:PRK08554 55 VYGEIGEGKPKLLFMAHFDVVPVNPEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLNGKVIFAFTGD 134
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 16131795 144 EETSMAGARYFAETTA---LRPDCAIIGEPTSLQP-VRAHKG 181
Cdd:PRK08554 135 EEIGGAMAMHIAEKLReegKLPKYMINADGIGMKPiIRRRKG 176
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
1-146 |
7.78e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 69.34 E-value: 7.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 1 MKNKLPP-----FIEIYRALIATPSIsaTEEALD-----QSNADLITLLADWFKDLGFNVEVQPvpgtrNKFNMLASIGQ 70
Cdd:PRK07205 1 MKSYITEkvqdaCVAAIKTLVSYPSV--LNEGENgtpfgQAIQDVLEATLDLCQGLGFKTYLDP-----KGYYGYAEIGQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 71 GAGGLLLAGHTDTVPF-DDGRWTRDPFTLTEHDGKLYGLGTADMKG-----FFAfiLDALRDVDVTKLKKPLYILATaDE 144
Cdd:PRK07205 74 GEELLAILCHLDVVPEgDLSDWQTPPFEAVEKDGCLFGRGTQDDKGpsmaaLYA--VKALLDAGVQFNKRIRFIFGT-DE 150
|
..
gi 16131795 145 ET 146
Cdd:PRK07205 151 ET 152
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
63-171 |
8.56e-13 |
|
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 66.68 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 63 NMLASIG--QGAGGLLLAGHTDTVPFDDGRWTRDPF-TLTEHDGKLYGLGTADMKGFFAFILDALRDV--DVTKLKKPLY 137
Cdd:cd03873 1 NLIARLGggEGGKSVALGAHLDVVPAGEGDNRDPPFaEDTEEEGRLYGRGALDDKGGVAAALEALKRLkeNGFKPKGTIV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 16131795 138 ILATADEETSMAGARYFAETTALR----PDCAIIGEPT 171
Cdd:cd03873 81 VAFTADEEVGSGGGKGLLSKFLLAedlkVDAAFVIDAT 118
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
14-235 |
1.61e-12 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 68.43 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 14 ALIATPSISATEEALDQSNA--DLITLLADWFKDLGFNVEVQPVPGtrnkFNMLASIgQGAGG----LLLAGHTDTVPFD 87
Cdd:PRK08262 52 EAIRFRTISNRDRAEDDAAAfdALHAHLEESYPAVHAALEREVVGG----HSLLYTW-KGSDPslkpIVLMAHQDVVPVA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 88 DGR---WTRDPFTLTEHDGKLYGLGTADMKGFFAFILDAL-----------RDVdvtklkkplYILATADEETSMAGARY 153
Cdd:PRK08262 127 PGTegdWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAeallaqgfqprRTI---------YLAFGHDEEVGGLGARA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 154 FAETTA---LRPDCAI-------------IGEPTSLQPVrAHKGHISNAIRIQGQSGHSSDPARGvNAIELMHDAIGHI- 216
Cdd:PRK08262 198 IAELLKergVRLAFVLdeggaitegvlpgVKKPVALIGV-AEKGYATLELTARATGGHSSMPPRQ-TAIGRLARALTRLe 275
|
250 260
....*....|....*....|....
gi 16131795 217 -----LQLRDNLKERYHYEAFTVP 235
Cdd:PRK08262 276 dnplpMRLRGPVAEMFDTLAPEMS 299
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
15-125 |
3.53e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 67.24 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 15 LIATPSISA---TEEALDQSnADLItllADWFKDLGF-NVEVQPVPGTrnkfnmLASIGQ-----GAGGLLLAGHTDTVP 85
Cdd:PRK07907 27 LVRIPSVAAdpfRREEVARS-AEWV---ADLLREAGFdDVRVVSADGA------PAVIGTrpappGAPTVLLYAHHDVQP 96
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 16131795 86 -FDDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALR 125
Cdd:PRK07907 97 pGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALR 137
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
75-287 |
5.05e-12 |
|
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: 66.53 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 75 LLLAGHTDTVPFDDGRWTRDPFT-LTEHDGKLYGLGTADMKGFFAFILDALRDVDVT--KLKKPLYILATADEET-SMAG 150
Cdd:cd05646 67 ILLNSHTDVVPVFEEKWTHDPFSaHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASgfKPKRTIHLSFVPDEEIgGHDG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 151 ARYFAETT---ALRPDCAI---IGEPTSLQPV----RAhKGHIsnAIRIQGQSGHSSDPARGvNAIELMHDAIGHILQLR 220
Cdd:cd05646 147 MEKFVKTEefkKLNVGFALdegLASPTEEYRVfygeRS-PWWV--VITAPGTPGHGSKLLEN-TAGEKLRKVIESIMEFR 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131795 221 DNLKERYHYEAFTVP--YPTLNLGHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSE 287
Cdd:cd05646 223 ESQKQRLKSNPNLTLgdVTTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGR 291
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
8-127 |
1.10e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 63.01 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 8 FIEIYRALIATPSISATEEALDQSNADLITLLADWFKDLGFNVEVQ--PVPGtRNKFnMLASIGQGAG--GLLLAGHTDT 83
Cdd:PRK07079 19 FFADLARRVAYRTESQNPDRAPALRAYLTDEIAPALAALGFTCRIVdnPVAG-GGPF-LIAERIEDDAlpTVLIYGHGDV 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 16131795 84 VPFDDGRWT--RDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDV 127
Cdd:PRK07079 97 VRGYDEQWRegLSPWTLTEEGDRWYGRGTADNKGQHTINLAALEQV 142
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
75-213 |
1.43e-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: 62.66 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 75 LLLAGHTDTVPFDD---GRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVdvtkLK---KP---LYILATADEE 145
Cdd:cd05674 72 LLLMAHQDVVPVNPeteDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELL----LKrgfKPrrtIILAFGHDEE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 146 TS-MAGARYFAET------------------TALRPDcaIIGEPTSLqPVRAHKGHISNAIRIQGQSGHSSDPARGvNAI 206
Cdd:cd05674 148 VGgERGAGAIAELllerygvdglaaildeggAVLEGV--FLGVPFAL-PGVAEKGYMDVEITVHTPGGHSSVPPKH-TGI 223
|
....*..
gi 16131795 207 ELMHDAI 213
Cdd:cd05674 224 GILSEAV 230
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
79-154 |
1.81e-10 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 62.17 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 79 GHTDTVPFDDGrWTRDPFTLTEHDGKLYGLGTADMKG-----FFAfiLDALRDVDVTKLKKPLYILATaDEETSMAGA-R 152
Cdd:PRK07318 86 GHLDVVPAGDG-WDTDPYEPVIKDGKIYARGTSDDKGptmaaYYA--LKIIKELGLPLSKKVRFIVGT-DEESGWKCMdY 161
|
..
gi 16131795 153 YF 154
Cdd:PRK07318 162 YF 163
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
16-159 |
2.22e-10 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 61.75 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 16 IATPSISATEEALDQSNADLITLLADWFKDLGFNVEV--QPVPGtRNKFNMLASIGQGAG-GLLLAGHTDTVPFDDGRWT 92
Cdd:cd05679 14 VAVPTESQEPARKPELRAYLDQEMRPRFERLGFTVHIhdNPVAG-RAPFLIAERIEDPSLpTLLIYGHGDVVPGYEGRWR 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131795 93 --RDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVT---KLKKPLYILATADEETSMAGARYFAETTA 159
Cdd:cd05679 93 dgRDPWTVTVWGERWYGRGTADNKGQHSINMAALRQVLEArggKLGFNVKFLIEMGEEMGSPGLRAFCFSHR 164
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
29-216 |
9.67e-10 |
|
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: 59.78 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 29 DQSNADLITLLADWFKDLGFNVEVQPVPGTRNKFNMLASI-GQGAGGLL--LAGHTDTVPFDDGRWTRDPFTLTEHDGKL 105
Cdd:cd08012 32 DNAGRHVLEALTPYSTENGGPLVIDHVSYVKGRGNIIVEYpGTVDGKTVsfVGSHMDVVTANPETWEFDPFSLSIDGDKL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 106 YGLGTADMKGFFAFILDALRDVDVTK--LKKPLYILATADEETSM-------------------AGARYFAETtalrpdc 164
Cdd:cd08012 112 YGRGTTDCLGHVALVTELFRQLATEKpaLKRTVVAVFIANEENSEipgvgvdalvksglldnlkSGPLYWVDS------- 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16131795 165 aiigepTSLQPVRAHKGHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHI 216
Cdd:cd08012 185 ------ADSQPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVMEALAEI 230
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
70-258 |
3.67e-08 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 54.79 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 70 QGAGGLLLAGHTDTV----PFDDGRWTRDpftltehDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKPLYI--LATAD 143
Cdd:PRK07473 73 QGEPGILIAGHMDTVhpvgTLEKLPWRRE-------GNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPItvLFTPD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 144 EETSMAGARYFAETTALRPDCAIIGEPTslqpvRAHKGHISN--AI-----RIQGQSGHS-SDPARGVNAIELMHDAIGH 215
Cdd:PRK07473 146 EEVGTPSTRDLIEAEAARNKYVLVPEPG-----RPDNGVVTGryAIarfnlEATGRPSHAgATLSEGRSAIREMARQILA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131795 216 IlqlrdnlkeryhyEAFTVPYPTLNLGHIHGGDASNRICACCE 258
Cdd:PRK07473 221 I-------------DAMTTEDCTFSVGIVHGGQWVNCVATTCT 250
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
38-377 |
7.74e-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: 53.61 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 38 LLADWFKDLGFNV---EVQPVPG--TRNKFNMLASIGQGAGGLLLAGHTDTVpfDDGRWTRDPftlTEHDGKLYGLGT-- 110
Cdd:cd05683 28 VLKKKFENLGLSViedDAGKTTGggAGNLICTLKADKEEVPKILFTSHMDTV--TPGINVKPP---QIADGYIYSDGTti 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 111 --ADMKGFFAFILDALRDVDVTKLK-KPLYILATADEETSMAGARyfaettALRPDC-------AI--IGEPTSLQpVRA 178
Cdd:cd05683 103 lgADDKAGIAAILEAIRVIKEKNIPhGQIQFVITVGEESGLVGAK------ALDPELidadygyALdsEGDVGTII-VGA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 179 HKGHISNAIrIQGQSGHSS-DPARGVNAIELMHDAIGHILQLRdnlkeryhYEAFTvpypTLNLGHIHGGDASNRICACC 257
Cdd:cd05683 176 PTQDKINAK-IYGKTAHAGtSPEKGISAINIAAKAISNMKLGR--------IDEET----TANIGKFQGGTATNIVTDEV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 258 ELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGR--LTVDELHPPIPGYEcppNHQLVEVVEKLLG-----AKTEVVNY 330
Cdd:cd05683 243 NIEAEARSLDEEKLDAQVKHMKETFETTAKEKGAHaeVEVETSYPGFKINE---DEEVVKLAKRAANnlgleINTTYSGG 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 16131795 331 CTEAPFIQTL-CPTLVLGPGSINqAHQPDEYLETRFIKPTRELITQVI 377
Cdd:cd05683 320 GSDANIINGLgIPTVNLGIGYEN-IHTTNERIPIEDLYDTAVLVVEII 366
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
19-115 |
1.56e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 49.75 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 19 PSISATEEALDQSnadlITLLADWFKDLGFNVEVQPVPGtrNKFnMLASIGQGAG-GLLLAGHTDTVPFDD-GRWTRDPF 96
Cdd:PRK06446 15 PSISATGEGIEET----ANYLKDTMEKLGIKANIERTKG--HPV-VYGEINVGAKkTLLIYNHYDVQPVDPlSEWKRDPF 87
|
90
....*....|....*....
gi 16131795 97 TLTEHDGKLYGLGTADMKG 115
Cdd:PRK06446 88 SATIENGRIYARGASDNKG 106
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
14-126 |
5.04e-06 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 48.07 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 14 ALIATPSISAtEEALDQSNADLITLLADWFKDLGF-NVEVQPVPGtrnkFNMLASIGQGAGG---LLLAGHTDTVPFD-- 87
Cdd:cd05680 6 ELLRIPSVSA-DPAHKGDVRRAAEWLADKLTEAGFeHTEVLPTGG----HPLVYAEWLGAPGaptVLVYGHYDVQPPDpl 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 16131795 88 DGrWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRD 126
Cdd:cd05680 81 EL-WTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEA 118
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
9-115 |
7.49e-06 |
|
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: 47.72 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 9 IEIYRALIATPSISA---TEEALDQSNAdlITLLADWFKDLGF-NVEVQPVPGTRN-----KFNMLASIGQGAGgLLLAG 79
Cdd:cd05677 2 LNTLSEFIAFQTVSQsptTENAEDSRRC--AIFLRQLFKKLGAtNCLLLPSGPGTNpivlaTFSGNSSDAKRKR-ILFYG 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 16131795 80 HTDTVPFDD-GRWTRDPFTLTEHDGKLYGLGTADMKG 115
Cdd:cd05677 79 HYDVIPAGEtDGWDTDPFTLTCENGYLYGRGVSDNKG 115
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
80-166 |
1.84e-05 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 46.50 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 80 HTDTVPFDDGRW-----TRDPFTLTEHDGKLYGLGTADMKGFFAFILDALRDVDVTKLKKP----LYILATadEETSMAG 150
Cdd:PRK06156 117 HADVVPANPELWvldgtRLDPFKVTLVGDRLYGRGTEDDKGAIVTALYAMKAIKDSGLPLArrieLLVYTT--EETDGDP 194
|
90
....*....|....*.
gi 16131795 151 ARYFAETTALrPDCAI 166
Cdd:PRK06156 195 LKYYLERYTP-PDYNI 209
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
36-146 |
5.79e-05 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 45.02 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 36 ITLLADWFKD---LGFNVEVQPVPGtRNKFNM--LASIGQGAGGLLLAGHTDTVPFDDGrWTRD--PFTLTEHDGKLYGL 108
Cdd:cd05682 33 ANLIADWVKAqniKGAKVEVVELEG-RTPLLFveIPGTEQDDDTVLLYGHMDKQPPFTG-WDEGlgPTKPVIRGDKLYGR 110
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 16131795 109 GTADmKGFFAF-ILDALRDVDVTKLKKPLYI-LATADEET 146
Cdd:cd05682 111 GGAD-DGYAIFaSLTAIKALQEQGIPHPRCVvLIEACEES 149
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
14-238 |
6.51e-05 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 45.03 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 14 ALIATPSISATEEalDQSNADLITLLA---DWFKDLGFNVEVQPVP---GTRNKFNMLASIGQGAGGLLLAGHTDTVPFD 87
Cdd:cd05654 9 SLVSWPSVTGTEG--ERSFADFLKEILkelPYFKENPSHVWQLLPPddlGRRNVTALVKGKKPSKRTIILISHFDTVGIE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 88 D-GRWTR---DPFTLTE--HDGK----------------LYGLGTADMKGFFAFILDALRD-VDVTKLKKPLYILATADE 144
Cdd:cd05654 87 DyGELKDiafDPDELTKafSEYVeeldeevredllsgewLFGRGTMDMKSGLAVHLALLEQaSEDEDFDGNLLLMAVPDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 145 ETSMAGARyfAETTALRPDC---------AIIGEPTS-LQPVRAHK-------GHISNAIRIQGQSGHSSDPARGVNAiE 207
Cdd:cd05654 167 EVNSRGMR--AAVPALLELKkkhdleyklAINSEPIFpQYDGDQTRyiytgsiGKILPGFLCYGKETHVGEPFAGINA-N 243
|
250 260 270
....*....|....*....|....*....|.
gi 16131795 208 LMHDAIGHILQLRDNLKERYHYEAftVPYPT 238
Cdd:cd05654 244 LMASEITARLELNADLCEKVEGEI--TPPPV 272
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
187-322 |
7.21e-04 |
|
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: 41.43 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 187 IRIQGQSGHSSDPARGVNAIELMHDAIGHiLQlrdNLKERYHYEAFTVpypTLNLGHIHGGDASNRICACCELHMDIRpl 266
Cdd:cd03886 176 ITVKGKGGHGASPHLGVDPIVAAAQIVLA-LQ---TVVSRELDPLEPA---VVTVGKFHAGTAFNVIPDTAVLEGTIR-- 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131795 267 pGMTlNELNGLLNDALAPVSERWPGRLTVD-ELHppiPGYECPP--NH-----QLVEVVEKLLG 322
Cdd:cd03886 247 -TFD-PEVREALEARIKRLAEGIAAAYGATvELE---YGYGYPAviNDpelteLVREAAKELLG 305
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
39-151 |
1.37e-03 |
|
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.
Pssm-ID: 349885 [Multi-domain] Cd Length: 474 Bit Score: 40.58 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 39 LADWFKDLGFNVEVQPV-------PGTRNKFNmlasigqgAGGLLLAGHTDTVP-------FDdgrWTRDPFTLTEHDGK 104
Cdd:cd03890 28 LVKFAKKLGLEVIQDEVgnviirkPATPGYEN--------APPVILQGHMDMVCeknadseHD---FEKDPIKLRIDGDW 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 16131795 105 LYGLGT---AD----MkgffAFILDALRDVDVtkLKKPLYILATADEETSMAGA 151
Cdd:cd03890 97 LKATGTtlgADngigV----AYALAILEDKDI--EHPPLEVLFTVDEETGMTGA 144
|
|
| PRK12890 |
PRK12890 |
allantoate amidohydrolase; Reviewed |
38-155 |
1.54e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 237248 [Multi-domain] Cd Length: 414 Bit Score: 40.27 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 38 LLADWFKDLGFNVEVQPVpGtrNKFNMLASIGQGAGGLLLAGHTDTVPfDDGRWtrdpftltehDGkLYG--LGTAdmkg 115
Cdd:PRK12890 43 LLAAWMRAAGLEVRRDAA-G--NLFGRLPGRDPDLPPLMTGSHLDTVP-NGGRY----------DG-ILGvlAGLE---- 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 16131795 116 ffafILDALRDVDVTkLKKPLYILATADEE-----TSMAGARYFA 155
Cdd:PRK12890 104 ----VVAALREAGIR-PPHPLEVIAFTNEEgvrfgPSMIGSRALA 143
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
13-115 |
2.29e-03 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 39.73 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131795 13 RALIATPSISAteeaLDQSNADLITL---LADWFKDLGF-NVEVQPVPG----TRNKFNmlasiGQGAGGLLLAGHTDTV 84
Cdd:PRK08201 21 KEFLRIPSISA----LSEHKEDVRKAaewLAGALEKAGLeHVEIMETAGhpivYADWLH-----APGKPTVLIYGHYDVQ 91
|
90 100 110
....*....|....*....|....*....|..
gi 16131795 85 PFDD-GRWTRDPFTLTEHDGKLYGLGTADMKG 115
Cdd:PRK08201 92 PVDPlNLWETPPFEPTIRDGKLYARGASDDKG 123
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