|
Name |
Accession |
Description |
Interval |
E-value |
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
15-429 |
2.32e-56 |
|
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: 190.87 E-value: 2.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 15 PAMAAIERDVEVAVDDLARMIEVDTsfPPGLGYDAfADLMAELLSPLGFEFERVVVPrdlwyvaggpasGERTNLIATR- 93
Cdd:COG0624 2 AVLAAIDAHLDEALELLRELVRIPS--VSGEEAAA-AELLAELLEALGFEVERLEVP------------PGRPNLVARRp 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 94 -DTGKPVCGLYYHVDTVPAAP--GWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDE 170
Cdd:COG0624 67 gDGGGPTLLLYGHLDVVPPGDleLWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 171 EGGlYPGIRYLAEQG--MLKG-HILNFNGSAAPRIWAGCFGVFHLQVTIRGRAVHAGegnRTGAGINAIEGALPLLNALM 247
Cdd:COG0624 147 EVG-SPGARALVEELaeGLKAdAAIVGEPTGVPTIVTGHKGSLRFELTVRGKAAHSS---RPELGVNAIEALARALAALR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 248 ALKPDVasRASALTPpphasgplRPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIRDsvAGTGLG 327
Cdd:COG0624 223 DLEFDG--RADPLFG--------RTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAA--AAPGVE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 328 LEMALVGHLIPT--NDPEGPHWPRWQKALSLGFGYKPEDFQKWGAascSDFGYVQKSGFAQEVLLGGLGRpeSCIHSPEE 405
Cdd:COG0624 291 VEVEVLGDGRPPfeTPPDSPLVAAARAAIREVTGKEPVLSGVGGG---TDARFFAEALGIPTVVFGPGDG--AGAHAPDE 365
|
410 420
....*....|....*....|....
gi 653801302 406 HTTRRDIIALAKsILAYLAADFAA 429
Cdd:COG0624 366 YVELDDLEKGAR-VLARLLERLAG 388
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
27-423 |
2.64e-44 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 159.00 E-value: 2.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 27 AVDDLARMIEVDTSFPPGLGYDAFADLMAELLSPLGFEFERVVVPRDlwYVAGGpaSGERTNLIATRDTGKPVCGLYYHV 106
Cdd:PRK08651 8 IVEFLKDLIKIPTVNPPGENYEEIAEFLRDTLEELGFSTEIIEVPNE--YVKKH--DGPRPNLIARRGSGNPHLHFNGHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 107 DTVPAAPGWAR-DPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLplyYDPMLLLCTDEE-GGLypGIRYLAEQ 184
Cdd:PRK08651 84 DVVPPGEGWSVnVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAGD---GNIELAIVPDEEtGGT--GTGYLVEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 185 GMLKGHILNF-NGSAAPRIWAGCFGVFHLQVTIRGRAVHAGEGNRtgaGINAIEGALPLLNALMALKPDvasRASALTPP 263
Cdd:PRK08651 159 GKVTPDYVIVgEPSGLDNICIGHRGLVWGVVKVYGKQAHASTPWL---GINAFEAAAKIAERLKSSLST---IKSKYEYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 264 PHASGPLRPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIRDSVAGTGLGLEMALVGHLIPT-NDP 342
Cdd:PRK08651 233 DERGAKPTVTLGGPTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFEITPFSEAFvTDP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 343 EGPHWPRWQKALSLGFGYKPEdfqKWGAASCSDFGYVQKSGfaQEVLLGGLGRPEScIHSPEEHTTRRDIIALAKSILAY 422
Cdd:PRK08651 313 DSELVKALREAIREVLGVEPK---KTISLGGTDARFFGAKG--IPTVVYGPGELEL-AHAPDEYVEVKDVEKAAKVYEEV 386
|
.
gi 653801302 423 L 423
Cdd:PRK08651 387 L 387
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
28-330 |
2.29e-35 |
|
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: 134.45 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 28 VDDLARMIEVDTSFPPGLGYDAFADLMAELLSPLGFEFervvvprDLWYVAGGPASGERTNLIATRDTGK-PVCGLYYHV 106
Cdd:TIGR01910 1 VELLKDLISIPSVNPPGGNEETIANYIKDLLREFGFST-------DVIEITDDRLKVLGKVVVKEPGNGNeKSLIFNGHY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 107 DTVPAAP--GWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGLYpGIRYLAEQ 184
Cdd:TIGR01910 74 DVVPAGDleLWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEA-GTLYLLQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 185 GMLKGHILNFNG--SAAPRIWAGCFGVFHLQVTIRGRAVHAGEGNRtgaGINAIEGALPLLNALMALKPDVASRASALTP 262
Cdd:TIGR01910 153 GYFKDADGVLIPepSGGDNIVIGHKGSIWFKLRVKGKQAHASFPQF---GVNAIMKLAKLITELNELEEHIYARNSYGFI 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653801302 263 pphasgPLRPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIRDSVAGTGLGLEM 330
Cdd:TIGR01910 230 ------PGPITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYEN 291
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
31-421 |
2.21e-32 |
|
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: 125.87 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 31 LARMIEVDTSFPPGlgyDAFADLMAELLSPLGFEFERVVVPRdlwyvaggpasgeRTNLIATRDTG-KPVCGLYYHVDTV 109
Cdd:cd08659 3 LQDLVQIPSVNPPE---AEVAEYLAELLAKRGYGIESTIVEG-------------RGNLVATVGGGdGPVLLLNGHIDTV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 110 PAAPG--WARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGLYpGIRYLAEQGML 187
Cdd:cd08659 67 PPGDGdkWSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSD-GARALLEAGYA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 188 KghilnfNGSAA-------PRIWAGCFGVFHLQVTIRGRAVHAGegnRTGAGINAIEGALPLLNALmalkpdvasraSAL 260
Cdd:cd08659 146 D------RLDALivgeptgLDVVYAHKGSLWLRVTVHGKAAHSS---MPELGVNAIYALADFLAEL-----------RTL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 261 TPPPHASGPL-RPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIRDSVAgtGLGLEMALVGHLIPT 339
Cdd:cd08659 206 FEELPAHPLLgPPTLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEA--KLTVEVSLDGDPPFF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 340 NDPEGPhwprWQKALSLGFGYKPEDFQ--KWGAAscSDFGYVQKSGfAQEVLLGGLGRPEScIHSPEEHTTRRDIIALAK 417
Cdd:cd08659 284 TDPDHP----LVQALQAAARALGGDPVvrPFTGT--TDASYFAKDL-GFPVVVYGPGDLAL-AHQPDEYVSLEDLLRAAE 355
|
....
gi 653801302 418 SILA 421
Cdd:cd08659 356 IYKE 359
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
31-323 |
1.77e-27 |
|
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: 113.03 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 31 LARMIEVDTSFPPGlGYDAFADLMAELLSPLGFEFERVVVPRDLWYVAGGPASgerTNLIATR---DTGKPVcGLYYHVD 107
Cdd:cd02697 9 LQKLVRVPTDTPPG-NNAPHAERTAALLQGFGFEAERHPVPEAEVRAYGMESI---TNLIVRRrygDGGRTV-ALNAHGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 108 TVPAAPGWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGLYPGIRYLAEQGML 187
Cdd:cd02697 84 VVPPGDGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGELGPGWLLRQGLT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 188 KGHILNFNGSAAPRIWA--GCfgvFHLQVTIRGRAVHAGegnRTGAGINAIEGALPLLNALMALKPDVASRASALtppph 265
Cdd:cd02697 164 KPDLLIAAGFSYEVVTAhnGC---LQMEVTVHGKQAHAA---IPDTGVDALQGAVAILNALYALNAQYRQVSSQV----- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 653801302 266 aSGPLRPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIRDSVAG 323
Cdd:cd02697 233 -EGITHPYLNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAAS 289
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
101-425 |
1.20e-24 |
|
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: 103.58 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 101 GLYYHVDTVPAAPGWaRDPLKlSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYydPMLLLCT-DEEGGLYpGIR 179
Cdd:pfam01546 1 LLRGHMDVVPDEETW-GWPFK-STEDGKLYGRGHDDMKGGLLAALEALRALKEEGLKKG--TVKLLFQpDEEGGMG-GAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 180 YLAEQGMLKG---------HIL---NFNGSAAPRIWAGCFGVFHLQVTIRGRAVHAGegnRTGAGINAIEGALPLLNALM 247
Cdd:pfam01546 76 ALIEDGLLERekvdavfglHIGeptLLEGGIAIGVVTGHRGSLRFRVTVKGKGGHAS---TPHLGVNAIVAAARLILALQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 248 ALkpdvASRASALTPPPHASGplrpqLLISAVNGGTAggQVPAEIKILVSRRYAPEESYEDALAEIESLIRDSVAGTGLG 327
Cdd:pfam01546 153 DI----VSRNVDPLDPAVVTV-----GNITGIPGGVN--VIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 328 LEMALVGHLIPTNDPEGPHWPRWQKALSLGFGYKPEDfQKWGAASCSDFGYvqksgFAQEVL--LGGLGRPESCIHSPEE 405
Cdd:pfam01546 222 VEVEYVEGGAPPLVNDSPLVAALREAAKELFGLKVEL-IVSGSMGGTDAAF-----FLLGVPptVVFFGPGSGLAHSPNE 295
|
330 340
....*....|....*....|
gi 653801302 406 HTTRRDIIALAKSILAYLAA 425
Cdd:pfam01546 296 YVDLDDLEKGAKVLARLLLK 315
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
24-319 |
4.44e-24 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 103.69 E-value: 4.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 24 VEVAVDDLAR----MIEVDTSFPPGLGYDAFADLMAELLSPLGFEFERVVVprdlwyvAGGPASGE---RTNLIATRDTG 96
Cdd:PRK13013 9 IEARRDDLVAltqdLIRIPTLNPPGRAYREICEFLAARLAPRGFEVELIRA-------EGAPGDSEtypRWNLVARRQGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 97 KPVCGLYY--HVDTVPAAPGWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGL 174
Cdd:PRK13013 82 RDGDCVHFnsHHDVVEVGHGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 175 YPGIRYLAEQGMLK----GHILNFNGSAAPRIWAGCFGVFHLQVTIRGRAVHageGNRTGAGINAIEGALPLLNALMA-L 249
Cdd:PRK13013 162 FGGVAYLAEQGRFSpdrvQHVIIPEPLNKDRICLGHRGVWWAEVETRGRIAH---GSMPFLGDSAIRHMGAVLAEIEErL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 250 KPDVASRASALTPPPhaSGPLRPQLLISAVNGGTAGGQ----------VPAEIKILVSRRYAPEESYEDALAEIESLIRD 319
Cdd:PRK13013 239 FPLLATRRTAMPVVP--EGARQSTLNINSIHGGEPEQDpdytglpapcVADRCRIVIDRRFLIEEDLDEVKAEITALLER 316
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
28-423 |
1.35e-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. 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: 101.31 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 28 VDDLARMIEVDTSFPPGLGYDAFADLMAELLSPLGFEFERVVVPRDLWYVaggpasgeRTNLIATRdtGKPVCGLYYHVD 107
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDNTSAIAAYIKLLLEDLGYPVELHEPPEEIYGV--------VSNIVGGR--KGKRLLFNGHYD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 108 TVPAAP--GWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGLYPGIRYLAEQG 185
Cdd:cd08011 71 VVPAGDgeGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYLLEKV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 186 MLKGHILNFNG-SAAPRIWAGCFGVFHLQVTIRGRAVHAGEGNRtgaGINAIEGALPLLNALmalkpdvasrasaltppp 264
Cdd:cd08011 151 RIKPNDVLIGEpSGSDNIRIGEKGLVWVIIEITGKPAHGSLPHR---GESAVKAAMKLIERL------------------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 265 hasGPLRPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIrdsvaGTGLGLEMA-LVGHLIPTNDPE 343
Cdd:cd08011 210 ---YELEKTVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHL-----DSIEEVSFEiKSFYSPTVSNPD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 344 GPHWPRWQKALSLGFGYKPEDFQKWGAascSDFGYVQKSGFAQEVLlgGLGRPEScIHSPEEHTTRRDIIALAKSILAYL 423
Cdd:cd08011 282 SEIVKKTEEAITEVLGIRPKEVISVGA---SDARFYRNAGIPAIVY--GPGRLGQ-MHAPNEYVEIDELIKVIKVHALVA 355
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
31-329 |
2.82e-22 |
|
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: 97.66 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 31 LARMIEVDT-SFPPGLgydAFADLMAELLSPLGFEFERVVVPrdlwyvaggpaSGERTNLIATRDTGkPVCGLYY--HVD 107
Cdd:cd03894 3 LARLVAFDTvSRNSNL---ALIEYVADYLAALGVKSRRVPVP-----------EGGKANLLATLGPG-GEGGLLLsgHTD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 108 TVPAA-PGWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLyydPMLLLCT-DEEGGlYPGIRYLAEqg 185
Cdd:cd03894 68 VVPVDgQKWSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRK---PLHLAFSyDEEVG-CLGVRHLIA-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 186 mlkghilnfNGSAAPRIWAGCF--------------GVFHLQVTIRGRAVHAgegNRTGAGINAIEGALPLLNALMALKP 251
Cdd:cd03894 142 ---------ALAARGGRPDAAIvgeptslqpvvahkGIASYRIRVRGRAAHS---SLPPLGVNAIEAAARLIGKLRELAD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 252 DVA--SRASALTPPphasgplRPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESyedaLAEIESLIRDSVAGTGLGLE 329
Cdd:cd03894 210 RLApgLRDPPFDPP-------YPTLNVGLIHGGNAVNIVPAECEFEFEFRPLPGED----PEAIDARLRDYAEALLEFPE 278
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
28-406 |
4.84e-17 |
|
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: 82.25 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 28 VDDLARMIEVD--TSFPPGLgyDAFADLMAELLSPLGFEFERVvvprdlwyvaggPASGERTNLIAT-RDTGKPVCGLYY 104
Cdd:cd03885 2 LDLLERLVNIEsgTYDKEGV--DRVAELLAEELEALGFTVERR------------PLGEFGDHLIATfKGTGGKRVLLIG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 105 HVDTVPAAPGWARDPLklSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGlYPGIR-YLAE 183
Cdd:cd03885 68 HMDTVFPEGTLAFRPF--TVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIG-SPGSReLIEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 184 QGMLKGHILNFNGSAAP-RIWAGCFGVFHLQVTIRGRAVHAgeGNRTGAGINAIEGALPLLNALMALkpdvASRASALTp 262
Cdd:cd03885 145 EAKGADYVLVFEPARADgNLVTARKGIGRFRLTVKGRAAHA--GNAPEKGRSAIYELAHQVLALHAL----TDPEKGTT- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 263 pphasgplrpqLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIR-DSVAGTglglEMALVGHLIPTND 341
Cdd:cd03885 218 -----------VNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVAtTLVPGT----SVELTGGLNRPPM 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 342 PEGPH----WPRWQK-ALSLGFGYKPEDfqkwgAASCSDFGYVQKSGFAqevLLGGLGRPESCIHSPEEH 406
Cdd:cd03885 283 EETPAsrrlLARAQEiAAELGLTLDWEA-----TGGGSDANFTAALGVP---TLDGLGPVGGGAHTEDEY 344
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
28-319 |
1.28e-16 |
|
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: 81.25 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 28 VDDLARMIEVDTSFPPGLGYD--AFADLMAELLSPLGFEFERVVVPRdlwyvaggpaSGERTNLIAT---RDTGKPVCGL 102
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTGSetRAAEVLAARLAEAGIQTEIFVVES----------HPGRANLVARiggTDPSAGPLLL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 103 YYHVDTVPA-APGWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGLYPGIRYL 181
Cdd:cd05675 71 LGHIDVVPAdASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 182 ----------AEQGMLKG---HILNFNGSAAPRIWAGCFGVFHLQVTIRGRAVHAGEGNRTGAgINAIEGALPLLNA--- 245
Cdd:cd05675 151 vdnhpelfdgATFALNEGgggSLPVGKGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRPTDDNA-ITRLAEALRRLGAhnf 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 246 -------------LMALKP----DVASRASALTPP---------PHASGPLRPQLLISAVNGGTAGGQVPAEIKILVSRR 299
Cdd:cd05675 230 pvrltdetayfaqMAELAGgeggALMLTAVPVLDPalaklgpsaPLLNAMLRNTASPTMLDAGYATNVLPGRATAEVDCR 309
|
330 340
....*....|....*....|
gi 653801302 300 YAPEESYEDALAEIESLIRD 319
Cdd:cd05675 310 ILPGQSEEEVLDTLDKLLGD 329
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
81-345 |
2.68e-16 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 79.93 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 81 PASGERTNLIATRDTGKPVCGLYYHVDTVpaAPG----WARDPLKLsVERED-LFGLGAADMKGTIAATLLALRAAKKCG 155
Cdd:PRK08588 43 KVNDGRANLVAEIGSGSPVLALSGHMDVV--AAGdvdkWTYDPFEL-TEKDGkLYGRGATDMKSGLAALVIAMIELKEQG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 156 LPLYYDPMLLLCTDEEGGlYPGIRYLAEQGMLK-----------GHILNF--NGSaapriwagcfgvFHLQVTIRGRAVH 222
Cdd:PRK08588 120 QLLNGTIRLLATAGEEVG-ELGAKQLTEKGYADdldaliigepsGHGIVYahKGS------------MDYKVTSTGKAAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 223 AGEGNRtgaGINAIEGALPLLNALMALKPDVASRASALtppphasGPLRPqlLISAVNGGTAGGQVPAEIKILVSRRYAP 302
Cdd:PRK08588 187 SSMPEL---GVNAIDPLLEFYNEQKEYFDSIKKHNPYL-------GGLTH--VVTIINGGEQVNSVPDEAELEFNIRTIP 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 653801302 303 EESYEDALAEIESLIRDSVAGTGLGLEMALVGHLIP-TNDPEGP 345
Cdd:PRK08588 255 EYDNDQVISLLQEIINEVNQNGAAQLSLDIYSNHRPvASDKDSK 298
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
27-319 |
8.54e-15 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 75.61 E-value: 8.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 27 AVDDLARMIEVDT-SFPPGLgydAFADLMAELLSPLGFEFERVVVPrdlwyvaggpaSGERTNLIAT---RDTGKPVcgL 102
Cdd:PRK07522 6 SLDILERLVAFDTvSRDSNL---ALIEWVRDYLAAHGVESELIPDP-----------EGDKANLFATigpADRGGIV--L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 103 YYHVDTVPAA-PGWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGL--PLYydpmLLLCTDEE-G--GLYP 176
Cdd:PRK07522 70 SGHTDVVPVDgQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLrrPLH----LAFSYDEEvGclGVPS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 177 GIRYLAEQGmlkghilnfngsAAPriwAGCF--------------GVFHLQVTIRGRAVHAGegnRTGAGINAIEGALPL 242
Cdd:PRK07522 146 MIARLPERG------------VKP---AGCIvgeptsmrpvvghkGKAAYRCTVRGRAAHSS---LAPQGVNAIEYAARL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 243 LNALMalkpDVASRASALTP------PPHASgplrpqLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESL 316
Cdd:PRK07522 208 IAHLR----DLADRLAAPGPfdalfdPPYST------LQTGTIQGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAY 277
|
...
gi 653801302 317 IRD 319
Cdd:PRK07522 278 AEA 280
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
40-322 |
2.94e-14 |
|
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: 73.88 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 40 SFPPGLGYDAFA-DLMAELLSPLGFEFERVVV-PRDL------WYVAGGPAsgERTNLIAT----RDTGKPVCgLYYHVD 107
Cdd:cd03895 8 RFPSLRGEEAAAqDLVAAALRSRGYTVDRWEIdVEKLkhhpgfSPVAVDYA--GAPNVVGThrprGETGRSLI-LNGHID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 108 TVPAAPG--WARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGlypGIRYLAeqG 185
Cdd:cd03895 85 VVPEGPVelWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECT---GNGALA--A 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 186 MLKGHilnfNGSAA-------PRIWAGCFGVFHLQVTIRGRAVHAGEgnrTGAGINAIEGALPLLNALMALKPDVASRAS 258
Cdd:cd03895 160 LMRGY----RADAAlipepteLKLVRAQVGVIWFRVKVRGTPAHVAE---ASEGVNAIEKAMHLIQALQELEREWNARKK 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653801302 259 ALTPPPHASGPLRpqLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIRDSVA 322
Cdd:cd03895 233 SHPHFSDHPHPIN--FNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVADAAA 294
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
88-330 |
6.32e-14 |
|
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: 72.47 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 88 NLIATRDTGKPV-CGLYYHVDTVPAApgwARDPLKLSvEREDLFGLGAADMKGTIAATLLALRAAKKCGLPlyYDPMLLL 166
Cdd:cd05647 43 TVVARTERGLASrVILAGHLDTVPVA---GNLPSRVE-EDGVLYGCGATDMKAGDAVQLKLAATLAAATLK--HDLTLIF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 167 CTDEEG-----GLYPGIRYLAEqgMLKGHILNFNGSAAPRIWAGCFGVFHLQVTIRGRAVHAGegnRTGAGINAIEGALP 241
Cdd:cd05647 117 YDCEEVaaelnGLGRLAEEHPE--WLAADFAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSA---RSWLGENAIHKLAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 242 LLNALMALKPDVASrASALTppphasgpLRPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEieslIRDSV 321
Cdd:cd05647 192 ILARLAAYEPRTVN-IDGLT--------YREGLNAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAH----VREVF 258
|
....*....
gi 653801302 322 AGTGLGLEM 330
Cdd:cd05647 259 EGLGYEIEV 267
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
52-250 |
1.37e-13 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 71.78 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 52 DLMAELLSPLGFEFErvVVPrdlwyVAGGPAsgeRTNLIATRDTGKPVCGLYYHVDTVPAAPG-WARDPLKLsVERED-L 129
Cdd:PRK05111 36 DLLAGWFEDLGFNVE--IQP-----VPGTRG---KFNLLASLGSGEGGLLLAGHTDTVPFDEGrWTRDPFTL-TEHDGkL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 130 FGLGAADMKG--TIAATLLALRAAKKCGLPLYydpmlLLCT-DEEGGLyPGIRYLAEQG-------------------ML 187
Cdd:PRK05111 105 YGLGTADMKGffAFILEALRDIDLTKLKKPLY-----ILATaDEETSM-AGARAFAEATairpdcaiigeptslkpvrAH 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 653801302 188 KGHILNfngsaapriwagcfgvfhlQVTIRGRAVHAGEGNRtgaGINAIEGALPLLNALMALK 250
Cdd:PRK05111 179 KGHMSE-------------------AIRITGQSGHSSDPAL---GVNAIELMHDVIGELLQLR 219
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
52-319 |
2.59e-13 |
|
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: 71.00 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 52 DLMAELLSPLGFEFERVVvprdlwyvaggpaSGERTNLIATRDTGKPVCGLYYHVDTVPAAP--GWARDPLKLSVEREDL 129
Cdd:cd03891 22 DLIAERLKALGFTCERLE-------------FGGVKNLWARRGTGGPHLCFAGHTDVVPPGDleGWSSDPFSPTIKDGML 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 130 FGLGAADMKGTIAATLLALRAAKKCglplYYDP----MLLLCTDEEGGLYPGIRYLAEQGMLKGHILNF----------- 194
Cdd:cd03891 89 YGRGAADMKGGIAAFVAAAERFVAK----HPNHkgsiSFLITSDEEGPAIDGTKKVLEWLKARGEKIDYcivgeptsekk 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 195 ------NGSaapRiwagcfGVFHLQVTIRGRAVHAGEGNRTgagINAIEGALPLLNALMALKPDvasRASALTPPPHasg 268
Cdd:cd03891 165 lgdtikIGR---R------GSLNGKLTIKGKQGHVAYPHLA---DNPIHLLAPILAELTATVLD---EGNEFFPPSS--- 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 653801302 269 plrpqLLISAVNGGTAGGQV-PAEIKILVSRRYAPEESYEDALAEIESLIRD 319
Cdd:cd03891 227 -----LQITNIDVGNGATNViPGELKAKFNIRFNDEHTGESLKARIEAILDK 273
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
27-425 |
1.57e-12 |
|
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: 68.15 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 27 AVDDLARMIEVDTsfPPGLGYDAfADLMAELLSPLGFEFERvvvprdlwyvaggpasGERTNLIATRDTGKPVCGLYYHV 106
Cdd:cd05653 3 AVELLLDLLSIYS--PSGEEARA-AKFLEEIMKELGLEAWV----------------DEAGNAVGGAGSGPPDVLLLGHI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 107 DTVPAapgwardPLKLSVEREDLFGLGAADMKG---TIAATLLALRAAKKCGLplyydpMLLLCTDEEGGlYPGIRYLAE 183
Cdd:cd05653 64 DTVPG-------EIPVRVEGGVLYGRGAVDAKGplaAMILAASALNEELGARV------VVAGLVDEEGS-SKGARELVR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 184 QGMLKGHILNFNGSAAPRIWAGCFGVFHLQVTIRGRAVHAgegnrTGAGINAIEgalPLLNALMALKPDVASRAsaltpp 263
Cdd:cd05653 130 RGPRPDYIIIGEPSGWDGITLGYRGSLLVKIRCEGRSGHS-----SSPERNAAE---DLIKKWLEVKKWAEGYN------ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 264 phASGPLRPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIRdsvagtglGLEMALVGHLIPTN-DP 342
Cdd:cd05653 196 --VGGRDFDSVVPTLIKGGESSNGLPQRAEATIDLRLPPRLSPEEAIALATALLP--------TCELEFIDDTEPVKvSK 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 343 EGPHWPRWQKALsLGFGYKPEDFQKWGAascSDFGYVQKSgFAQEVLLGGLGRPeSCIHSPEEHTTRRDIIalaKSILAY 422
Cdd:cd05653 266 NNPLARAFRRAI-RKQGGKPRLKRKTGT---SDMNVLAPL-WTVPIVAYGPGDS-TLDHTPNEHIELAEIE---RAAAVL 336
|
...
gi 653801302 423 LAA 425
Cdd:cd05653 337 KGA 339
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
52-141 |
3.27e-12 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 67.42 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 52 DLMAELLSPLGFEFERVVvprdlwyvaggpaSGERTNLIATRDTGKPVCGLYYHVDTVPAAP--GWARDPLKLSVEREDL 129
Cdd:PRK13009 26 DLLAERLEALGFTCERMD-------------FGDVKNLWARRGTEGPHLCFAGHTDVVPPGDleAWTSPPFEPTIRDGML 92
|
90
....*....|..
gi 653801302 130 FGLGAADMKGTI 141
Cdd:PRK13009 93 YGRGAADMKGSL 104
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
3-319 |
5.28e-12 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 67.33 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 3 MPQPASSQQIlgpaMAAIERDVEVAVDDLARMIEvdtsFPPGLGYDAFA-DLMAELLSPLGFEFERVVV-PRDLWYVAG- 79
Cdd:PRK06837 2 MLTPDLTQRI----LAAVDAGFDAQVAFTQDLVR----FPSTRGAEAPCqDFLARAFRERGYEVDRWSIdPDDLKSHPGa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 80 GPAS---GERTNLIAT----RDTGKPVCgLYYHVDTVPAAPG--WARDPLKLSVEREDLFGLGAADMKGTIAATLLALRA 150
Cdd:PRK06837 74 GPVEidySGAPNVVGTyrpaGKTGRSLI-LQGHIDVVPEGPLdlWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 151 AKKCGLPLYYDPMLLLCTDEE----GGLYPGIR-YLA---------EQGMLKGHIlnfngsaapriwagcfGVFHLQVTI 216
Cdd:PRK06837 153 LRAAGLAPAARVHFQSVIEEEstgnGALSTLQRgYRAdaclipeptGEKLVRAQV----------------GVIWFRLRV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 217 RGRAVHAGEgnrTGAGINAIEGALPLLNALMALKPDVASRASAltpPPHASGPLRP-QLLISAVNGGTAGGQVPAEIKIL 295
Cdd:PRK06837 217 RGAPVHVRE---AGTGANAIDAAYHLIQALRELEAEWNARKAS---DPHFEDVPHPiNFNVGIIKGGDWASSVPAWCDLD 290
|
330 340
....*....|....*....|....
gi 653801302 296 VSRRYAPEESYEDALAEIESLIRD 319
Cdd:PRK06837 291 CRIAIYPGVTAADAQAEIEACLAA 314
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
6-184 |
1.37e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 66.18 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 6 PASSQQILGPAMAAIERDVEVAVDDLAR-MIEVDTSFPPGLGYDAfADLMAELLSPLGFEFERVVVprdlwyvagGPASG 84
Cdd:PRK09133 17 AAAATGAAAAAAPAAPTADQQAARDLYKeLIEINTTASTGSTTPA-AEAMAARLKAAGFADADIEV---------TGPYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 85 ERTNLIAT---RDTGKPVCgLYYHVDTVPAAP-GWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYY 160
Cdd:PRK09133 87 RKGNLVARlrgTDPKKPIL-LLAHMDVVEAKReDWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKR 165
|
170 180
....*....|....*....|....
gi 653801302 161 DPMLLLCTDEEGGLYPGIRYLAEQ 184
Cdd:PRK09133 166 DIILALTGDEEGTPMNGVAWLAEN 189
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
27-318 |
1.47e-11 |
|
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: 65.41 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 27 AVDDLARMIEVdtsfpPGLGYDAF--ADLMAELLSPLGFEFERVvvPRDLWYVAGGPASGERTNLIATrdtgkpvcglyy 104
Cdd:cd05651 2 AIELLKSLIAT-----PSFSREEHktADLIENYLEQKGIPFKRK--GNNVWAENGHFDEGKPTLLLNS------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 105 HVDTVPAAPGWARDPLKlSVERED-LFGLGAADMKGTIAATLLALRAAKKCGlPLYYDPMLLLCTDEEGGLYPGIRYLAE 183
Cdd:cd05651 63 HHDTVKPNAGWTKDPFE-PVEKGGkLYGLGSNDAGASVVSLLATFLHLYSEG-PLNYNLIYAASAEEEISGKNGIESLLP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 184 Q-GMLKGHIL----NFNGSAAPRiwagcfGVFHLQVTIRGRAVHAGEGNrtgaGINAIEGALPLLNALMALKPDvasRAS 258
Cdd:cd05651 141 HlPPLDLAIVgeptEMQPAIAEK------GLLVLDCTARGKAGHAARNE----GDNAIYKALDDIQWLRDFRFD---KVS 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 259 ALTPPPHASgplrpqllISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIR 318
Cdd:cd05651 208 PLLGPVKMT--------VTQINAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLK 259
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
207-319 |
2.85e-11 |
|
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: 60.05 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 207 FGVFHLQVTIRGRAVHAGEGnrtGAGINAIEGALPLLNALMALKPDVASRasaltppphasgPLRPQLLISAVNGGTAGG 286
Cdd:pfam07687 4 KGLAGGHLTVKGKAGHSGAP---GKGVNAIKLLARLLAELPAEYGDIGFD------------FPRTTLNITGIEGGTATN 68
|
90 100 110
....*....|....*....|....*....|...
gi 653801302 287 QVPAEIKILVSRRYAPEESYEDALAEIESLIRD 319
Cdd:pfam07687 69 VIPAEAEAKFDIRLLPGEDLEELLEEIEAILEK 101
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
51-424 |
4.15e-11 |
|
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: 64.27 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 51 ADLMAELLSPLGFEFERVVVPRdlwyvaGGPAsgertnLIATR--DTGKPVCGLYYHVDTVPAAP--GWARDPLKLSVER 126
Cdd:cd03893 27 AEWLADLLRRLGFTVEIVDTSN------GAPV------VFAEFpgAPGAPTVLLYGHYDVQPAGDedGWDSDPFELTERD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 127 EDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGLYPGIRYLAEQGMLKG--HIL----NFNGSAAP 200
Cdd:cd03893 95 GRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEESGSPSLDQLVEAHRDLLAadAIVisdsTWVGQEQP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 201 RIWAGCFGVFHLQVTIRGRAVHAGEGNRTGAGINAIEGALPLLNALMALKPD--VASRASALTPPPHA------------ 266
Cdd:cd03893 175 TLTYGLRGNANFDVEVKGLDHDLHSGLYGGVVPDPMTALAQLLASLRDETGRilVPGLYDAVRELPEEefrldagvleev 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 267 ------SGPL------RPQLLISAVNGGTAGGQ----VPAEIKILVSRRYAPEESYEDALAEIESLIRDSV-AGTGLGLE 329
Cdd:cd03893 255 eiiggtTGSVaerlwtRPALTVLGIDGGFPGEGsktvIPPRARAKISIRLVPGQDPEEASRLLEAHLEKHApSGAKVTVS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 330 MALVGH--LIPTNDPegphWPRWQKALSLGFGYKPEDFQKWGAA--SCSDFG-YVQKSgfaqeVLLGGLGRPESCIHSPE 404
Cdd:cd03893 335 YVEGGMpwRSDPSDP----AYQAAKDALRTAYGVEPPLTREGGSipFISVLQeFPQAP-----VLLIGVGDPDDNAHSPN 405
|
410 420
....*....|....*....|
gi 653801302 405 EHTTRRDIIALAKSILAYLA 424
Cdd:cd03893 406 ESLRLGNYKEGTQAEAALLY 425
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
25-333 |
9.62e-11 |
|
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: 63.25 E-value: 9.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 25 EVAVDDLARMIEVDTSFPP--GLGYDAFADLMAELLSPLGF-EFERVVVPRDlwYVaggpasGERTNLIATRDTGKP-VC 100
Cdd:cd05650 1 EEIIELERDLIRIPAVNPEsgGEGEKEKADYLEKKLREYGFyTLERYDAPDE--RG------IIRPNIVAKIPGGNDkTL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 101 GLYYHVDTVPaaPG----WARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGLYP 176
Cdd:cd05650 73 WIISHLDTVP--PGdlslWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 177 GIRYLAEQGMLKGH-----ILNFNGSAAPRIWAGCFGVFHLQVTIRGRAVHAgegNRTGAGINAIEGALPLLNALMALKP 251
Cdd:cd05650 151 GIQYLLNKFDLFKKddliiVPDFGTEDGEFIEIAEKSILWIKVNVKGKQCHA---STPENGINAFVAASNFALELDELLH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 252 DVASRASALTPPPHAS-GPLRPQLLISAVNggtaggQVPAEIKILVSRRYAPEESYEDALAEIESLIRDSVAGTGLGLEM 330
Cdd:cd05650 228 EKFDEKDDLFNPPYSTfEPTKKEANVPNVN------TIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDFENSYGAGITY 301
|
...
gi 653801302 331 ALV 333
Cdd:cd05650 302 EIV 304
|
|
| PRK06915 |
PRK06915 |
peptidase; |
19-319 |
1.82e-09 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 59.32 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 19 AIERDVEVAVDDLARMIEVDTSFPPGLGYDAfadLMAELLSPLGFEFervvvprDLWYVAGG-----PA-SGERT----- 87
Cdd:PRK06915 11 YIESHEEEAVKLLKRLIQEKSVSGDESGAQA---IVIEKLRELGLDL-------DIWEPSFKklkdhPYfVSPRTsfsds 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 88 -NLIAT---RDTGKPVCgLYYHVDTVPAA--PGWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYD 161
Cdd:PRK06915 81 pNIVATlkgSGGGKSMI-LNGHIDVVPEGdvNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 162 PMLLLCTDEEGGlypGIRYLAeqGMLKGHilNFNGSAAP-----RIWAGCFGVFHLQVTIRGRAVHAgeGNRTgAGINAI 236
Cdd:PRK06915 160 VIFQSVIEEESG---GAGTLA--AILRGY--KADGAIIPeptnmKFFPKQQGSMWFRLHVKGKAAHG--GTRY-EGVSAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 237 EGALPLLNALMALKpdvASRASALTPPPHASGPLRPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESL 316
Cdd:PRK06915 230 EKSMFVIDHLRKLE---EKRNDRITDPLYKGIPIPIPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENW 306
|
...
gi 653801302 317 IRD 319
Cdd:PRK06915 307 IAE 309
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
49-327 |
2.34e-09 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 58.52 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 49 AFADLMAELLSPLGFEFERvvvprDlwyvaggpasgERTNLI----ATRDTGKPVCGLYYHVDTVPAAPGwarDPLKLSV 124
Cdd:COG2195 24 ALADYLVEELKELGLEVEE-----D-----------EAGNVIatlpATPGYNVPTIGLQAHMDTVPQFPG---DGIKPQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 125 ErEDLF---G---LGAADmkgtiaatllalraakKCGL------------------PLYydpmLLLCTDEEGGLYpGIRY 180
Cdd:COG2195 85 D-GGLItadGtttLGADD----------------KAGVaailaaleylkepeiphgPIE----VLFTPDEEIGLR-GAKA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 181 LAEqGMLKGHIL-NFNGSAAPRIWAGCFGVFHLQVTIRGRAVHAGEGNrtGAGINAIEgalpllnalmalkpdVASRA-S 258
Cdd:COG2195 143 LDV-SKLGADFAyTLDGGEEGELEYECAGAADAKITIKGKGGHSGDAK--EKMINAIK---------------LAARFlA 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 653801302 259 ALtppPHASGPLRPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIRDSVAGTGLG 327
Cdd:COG2195 205 AL---PLGRIPEETEGNEGFIHGGSATNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGVG 270
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
28-317 |
3.09e-09 |
|
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: 58.26 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 28 VDDLARMIEVDTSFP-----PGLGYDAFADLMAELLSPLGFEFERVvvprdlwyvAGGPAsgeRTNLIAT-RDTG--KPV 99
Cdd:cd08013 4 VSLTQTLVRINSSNPslsatGGAGEAEIATYVAAWLAHRGIEAHRI---------EGTPG---RPSVVGVvRGTGggKSL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 100 CgLYYHVDTVPAApGWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKcgLPLYYDPMLLLCTDEEGglypgir 179
Cdd:cd08013 72 M-LNGHIDTVTLD-GYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKE--AGLRGDVILAAVADEED------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 180 ylAEQGMLKGHILNFNGSAA----PRIWAGCF---GVFHLQVTIRGRAVHageGNRTGAGINAIEGALPLLNALMALKPD 252
Cdd:cd08013 141 --ASLGTQEVLAAGWRADAAivtePTNLQIIHahkGFVWFEVDIHGRAAH---GSRPDLGVDAILKAGYFLVALEEYQQE 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 653801302 253 VASRasaltpPPHAS-GPlrPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLI 317
Cdd:cd08013 216 LPER------PVDPLlGR--ASVHASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTAIL 273
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
31-317 |
3.30e-09 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 58.51 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 31 LARMIEVDTSFPPGLGYDAFADLMAELLSPLGFEFER-VVVPRDlWYVAG---GPASGERTNLIatrdtgkpvcgLYYHV 106
Cdd:PRK08596 19 LKTLVRFETPAPPARNTNEAQEFIAEFLRKLGFSVDKwDVYPND-PNVVGvkkGTESDAYKSLI-----------INGHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 107 D--TVPAAPGWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGlYPGIRYLAEQ 184
Cdd:PRK08596 87 DvaEVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEVG-EAGTLQCCER 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 185 GMLKGHILNFNGSAAPRIWAGcfGVFHLQVTI----------RGRAVHAGEGNRtgaGINAIEGALPLLNALMALKPDVA 254
Cdd:PRK08596 166 GYDADFAVVVDTSDLHMQGQG--GVITGWITVkspqtfhdgtRRQMIHAGGGLF---GASAIEKMMKIIQSLQELERHWA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653801302 255 SRASALTPPPhASGPLRPqllisAVnggTAGGQVPA----EIKILVSRRYAPEESYEDALAEIESLI 317
Cdd:PRK08596 241 VMKSYPGFPP-GTNTINP-----AV---IEGGRHAAfiadECRLWITVHFYPNETYEQVIKEIEEYI 298
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
88-316 |
1.87e-08 |
|
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: 55.89 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 88 NLIATRDTGKPVCGLYYHVDTVPAA--PGWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGL-PLYYDPML 164
Cdd:cd05649 43 NVIGYIGGGKKKILFDGHIDTVGIGniDNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLrDFAYTILV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 165 LLCTDEE--GGLYPgiRYLAEQGMLKGHILNFNGSAAPRIWAGCFGVFHLQVTIRGRAVHageGNRTGAGINAIEGALPL 242
Cdd:cd05649 123 AGTVQEEdcDGVCW--QYISKADKIKPDFVVSGEPTDGNIYRGQRGRMEIRVDTKGVSCH---GSAPERGDNAVYKMADI 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 653801302 243 LNALMALKPDVAsrasalTPPPHASGPLRPQLLISAVNGGTAggqVPAEIKILVSRRYAPEESYEDALAEIESL 316
Cdd:cd05649 198 IQDIRQLNPNFP------EAPFLGRGTLTVTDIFSTSPSRCA---VPDSCRISIDRRLTVGETWEGCLEEIRAL 262
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
27-224 |
4.07e-08 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 55.02 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 27 AVDDLARMIEVD--TSFPPGLgyDAFADLMAELLSPLGFEFERVVVPrdlwyvaggPASGerTNLIAT-RDTGKPVCGLY 103
Cdd:PRK06133 39 YLDTLKELVSIEsgSGDAEGL--KQVAALLAERLKALGAKVERAPTP---------PSAG--DMVVATfKGTGKRRIMLI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 104 YHVDTVPAAPGWARDPLKLSVERedLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGlYPGIRYL-A 182
Cdd:PRK06133 106 AHMDTVYLPGMLAKQPFRIDGDR--AYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETG-SPGSRELiA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 653801302 183 EQGMLKGHILNFNGSAAP---RIWAGCFGVFHLQVTirGRAVHAG 224
Cdd:PRK06133 183 ELAAQHDVVFSCEPGRAKdalTLATSGIATALLEVK--GKASHAG 225
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
29-141 |
4.71e-08 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 55.04 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 29 DDLARMIEVDTSFPPGLGYDAFADLMAELLSPLGFEFErvvvprdLWYVAGGPAsgertnLIATRDTGKPVCGLYY-HVD 107
Cdd:cd05681 3 EDLRDLLKIPSVSAQGRGIPETADFLKEFLRRLGAEVE-------IFETDGNPI------VYAEFNSGDAKTLLFYnHYD 69
|
90 100 110
....*....|....*....|....*....|....*.
gi 653801302 108 TVPAAP--GWARDPLKLSVEREDLFGLGAADMKGTI 141
Cdd:cd05681 70 VQPAEPleLWTSDPFELTIRNGKLYARGVADDKGEL 105
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
88-323 |
9.51e-08 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 53.79 E-value: 9.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 88 NLIATRDTGKPVCGLYYHVDTVPA--APGWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLL 165
Cdd:PRK13004 60 NVLGYIGHGKKLIAFDAHIDTVGIgdIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 166 LCTDEE--GGLYPgiRYLAEQGMLKGhilNFNGSAAP---RIWAGCFGVFHLQVTIRGRAVHAGEGNRtgaGINAIEGAL 240
Cdd:PRK13004 140 GTVQEEdcDGLCW--RYIIEEDKIKP---DFVVITEPtdlNIYRGQRGRMEIRVETKGVSCHGSAPER---GDNAIYKMA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 241 PLLNALMALKPDVASRasaltpPPHASGPLRPQLLISAVNGGTAggqVPAEIKILVSRRYAPEESYEDALAEIESLIRDS 320
Cdd:PRK13004 212 PILNELEELNPNLKED------PFLGKGTLTVSDIFSTSPSRCA---VPDSCAISIDRRLTVGETWESVLAEIRALPAVK 282
|
...
gi 653801302 321 VAG 323
Cdd:PRK13004 283 KAN 285
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
29-224 |
1.71e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 53.38 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 29 DDLARMIEVDT-SFPPGLG---YDAFADLMAELLSPLGFEFERVVVPRDlwyvAGGPAsgertnLIATR--DTGKPVCGL 102
Cdd:PRK07079 21 ADLARRVAYRTeSQNPDRApalRAYLTDEIAPALAALGFTCRIVDNPVA----GGGPF------LIAERieDDALPTVLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 103 YYHVDTVPAAPG-W--ARDPLKLSVEREDLFGLGAADMKG--TIAATLLALRAAKKCGlPLYYDPMLLLCTDEEGGlYPG 177
Cdd:PRK07079 91 YGHGDVVRGYDEqWreGLSPWTLTEEGDRWYGRGTADNKGqhTINLAALEQVLAARGG-RLGFNVKLLIEMGEEIG-SPG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 653801302 178 IRYLAEQ--GMLKGHIlnFNGSAAPRIWA-------GCFGV--FHLQVTIRGRAVHAG 224
Cdd:PRK07079 169 LAEVCRQhrEALAADV--LIASDGPRLSAerptlflGSRGAvnFRLRVNLRDGAHHSG 224
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
88-173 |
1.88e-07 |
|
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: 51.28 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 88 NLIAT---RDTGKPVCgLYYHVDTVPAAPGWARDPLK--LSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDP 162
Cdd:cd18669 1 NVIARyggGGGGKRVL-LGAHIDVVPAGEGDPRDPPFfvDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTV 79
|
90
....*....|.
gi 653801302 163 MLLLCTDEEGG 173
Cdd:cd18669 80 VVAFTPDEEVG 90
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
52-224 |
1.24e-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: 349928 [Multi-domain] Cd Length: 448 Bit Score: 50.58 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 52 DLMAELLSPLGFEFErvvvprdlwyVAGGPASGERTNLIATR--DTGKPVCGLYYHVDTVPAAPG-W--ARDPLKLSVER 126
Cdd:cd05679 35 QEMRPRFERLGFTVH----------IHDNPVAGRAPFLIAERieDPSLPTLLIYGHGDVVPGYEGrWrdGRDPWTVTVWG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 127 EDLFGLGAADMKG--TIAATLLALRAAKKCGlPLYYDPMLLLCTDEEGGlYPGIRYLAEQG--MLKGHIlnFNGSAAPRI 202
Cdd:cd05679 105 ERWYGRGTADNKGqhSINMAALRQVLEARGG-KLGFNVKFLIEMGEEMG-SPGLRAFCFSHreALKADL--FIASDGPRL 180
|
170 180 190
....*....|....*....|....*....|.
gi 653801302 203 WA-------GCFGV--FHLQVTIRGRAVHAG 224
Cdd:cd05679 181 AAdrptmflGSRGGlnFELRVNLREGGHHSG 211
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
88-185 |
5.32e-06 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 48.27 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 88 NLIATRdtGKPVCGLYYHVDTVPAAPGWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKcglplyyDPMLLLC 167
Cdd:PRK08737 56 SLYAVR--GTPKYLFNVHLDTVPDSPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANAGDG-------DAAFLFS 126
|
90
....*....|....*...
gi 653801302 168 TDEEGGLYPGIRYLAEQG 185
Cdd:PRK08737 127 SDEEANDPRCVAAFLARG 144
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
95-173 |
5.37e-06 |
|
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: 48.40 E-value: 5.37e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 653801302 95 TGKPVCGLYYHVDTVPAAPGWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGG 173
Cdd:cd03888 69 EGEEVLGILGHLDVVPAGEGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETG 147
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
18-141 |
6.16e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 48.36 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 18 AAIERDVEVAVDDLARMIEVDT-SFPPGL--GYDAFADLMAELLSPLGFEFERVVVPrdlwyvAGGPAsgertnLIATRD 94
Cdd:PRK07907 11 ARVAELLPRVRADLEELVRIPSvAADPFRreEVARSAEWVADLLREAGFDDVRVVSA------DGAPA------VIGTRP 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 653801302 95 T--GKPVCGLYYHVDTVPAAP--GWARDPLKLsVERED-LFGLGAADMKGTI 141
Cdd:PRK07907 79 AppGAPTVLLYAHHDVQPPGDpdAWDSPPFEL-TERDGrLYGRGAADDKGGI 129
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
102-383 |
6.80e-06 |
|
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: 47.86 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 102 LYYHVDTVPAAP-GWARDPLKLSVERE-DLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGLYPGIR 179
Cdd:TIGR01880 76 LNSHTDVVPVFReHWTHPPFSAFKDEDgNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGME 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 180 YLAEQGMLKGHILNF---NGSAAP----RIWAGCFGVFHLQVTIRGRAVHAGEGNRTGAGinaiEGALPLLNALMALKpd 252
Cdd:TIGR01880 156 KFAKTDEFKALNLGFaldEGLASPddvyRVFYAERVPWWVVVTAPGNPGHGSKLMENTAM----EKLEKSVESIRRFR-- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 253 vASRASALTPPPHASGPLRPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIRDsvAGTGLGLEMA- 331
Cdd:TIGR01880 230 -ESQFQLLQSNPDLAIGDVTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCAD--AGEGVTYEFSq 306
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 653801302 332 LVGHLIPT-NDPEGPHWPRWQKAL-SLGFGYKPEDFqkwgaASCSDFGYVQKSG 383
Cdd:TIGR01880 307 HSGKPLVTpHDDSNPWWVAFKDAVkEMGCTFKPEIL-----PGSTDSRYIRAAG 355
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
51-246 |
1.08e-05 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 47.54 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 51 ADLMAELLSPLGF-EFERVVVPRDLwyvagGPaSGERTNLIATRDTGKPVCGLYY--HVDTVPaaPG----WARDPLKLS 123
Cdd:PRK13983 33 AEYLESLLKEYGFdEVERYDAPDPR-----VI-EGVRPNIVAKIPGGDGKRTLWIisHMDVVP--PGdlslWETDPFKPV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 124 VEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGLYPGIRYLAEQ----------------GML 187
Cdd:PRK13983 105 VKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYGIQYLLKKhpelfkkddlilvpdaGNP 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 653801302 188 KG--------HILnfngsaapriWagcfgvfhLQVTIRGRAVHAgegNRTGAGINAIEGALPLLNAL 246
Cdd:PRK13983 185 DGsfieiaekSIL----------W--------LKFTVKGKQCHA---STPENGINAHRAAADFALEL 230
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
48-319 |
1.10e-05 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 47.06 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 48 DAFADLMAELLSPLGFEferVVVPRDlwyvaggpasGERTNLIAtrdtgKPVCGLYY--HVDTVPAAPGWardplklSVE 125
Cdd:PRK08652 22 DEIALHIMEFLESLGYD---VHIESD----------GEVINIVV-----NSKAELFVevHYDTVPVRAEF-------FVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 126 REDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDpMLLLCTDEEGGLypGIRYLAEQ---GM--------LKGHIlnf 194
Cdd:PRK08652 77 GVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVG-IAFVSDEEEGGR--GSALFAERyrpKMaivleptdLKVAI--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 195 ngsaapriwAGCfGVFHLQVTIRGRAVHageGNRTGAGINAIEGALPLLNALMALKPDVASRASaltppphasgplrPQL 274
Cdd:PRK08652 151 ---------AHY-GNLEAYVEVKGKPSH---GACPESGVNAIEKAFEMLEKLKELLKALGKYFD-------------PHI 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 653801302 275 LISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIRD 319
Cdd:PRK08652 205 GIQEIIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDE 249
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
88-184 |
1.12e-05 |
|
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: 45.88 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 88 NLIATR--DTGKPVCGLYYHVDTVPAAPGWARDPLK--LSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPM 163
Cdd:cd03873 1 NLIARLggGEGGKSVALGAHLDVVPAGEGDNRDPPFaeDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
|
90 100
....*....|....*....|.
gi 653801302 164 LLLCTDEEGGLYPGIRYLAEQ 184
Cdd:cd03873 81 VAFTADEEVGSGGGKGLLSKF 101
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
27-183 |
1.38e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 44.07 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 27 AVDDLARMIEVDTS---FPPGLGYDAFADLMAELLSPLGFEFErvvvprdlwYVAGGPAsgeRTNLIAT---RDTGKPVC 100
Cdd:PRK07906 1 VVDLCSELIRIDTTntgDGTGKGEREAAEYVAEKLAEVGLEPT---------YLESAPG---RANVVARlpgADPSRPAL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 101 GLYYHVDTVPA-APGWARDPlkLSVERED--LFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEE-GGLYp 176
Cdd:PRK07906 69 LVHGHLDVVPAeAADWSVHP--FSGEIRDgyVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEaGGTY- 145
|
....*..
gi 653801302 177 GIRYLAE 183
Cdd:PRK07906 146 GAHWLVD 152
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
96-141 |
2.16e-04 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 43.22 E-value: 2.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 653801302 96 GKPVCGLYYHVDTVPAAPG-WARDPLKLSVEREDLFGLGAADMKGTI 141
Cdd:PRK08554 62 GKPKLLFMAHFDVVPVNPEeWNTEPFKLTVKGDKAYGRGSADDKGNV 108
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
49-323 |
7.04e-04 |
|
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: 41.49 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 49 AFADLMAELLSPLGFEFERVVVPrdlwyvaggpaSGERTNLIAT-RDTGKPVCGLYYHVDTVPaaPGWardPLKLSVERE 127
Cdd:cd05652 20 AVGDFLAEYLESLGFTVEKQPVE-----------NKDRFNVYAYpGSSRQPRVLLTSHIDTVP--PFI---PYSISDGGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 128 DLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGlypGIrylaeqGMLKghilnFNGSAAPRIWAGCF 207
Cdd:cd05652 84 TIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETG---GD------GMKA-----FNDLGLNTWDAVIF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 208 -------------GVFHLQVTIRGRAVHAGEGNrtgAGINAIEGALPLLNALMALKPDVASRASALTppphasgplrpqL 274
Cdd:cd05652 150 geptelklasghkGMLGFKLTAKGKAGHSGYPW---LGISAIEILVEALVKLIDADLPSSELLGPTT------------L 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 653801302 275 LISAVNGGTAGGQVPAEIKILVSRRYAPEESyedalaEIESLIRDSVAG 323
Cdd:cd05652 215 NIGRISGGVAANVVPAAAEASVAIRLAAGPP------EVKDIVKEAVAG 257
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
48-237 |
8.05e-04 |
|
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: 41.68 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 48 DAFADLMAELLSPLGFEFERVVVPRDLWYVAGgpasgeRTNLI----ATRDtGKPVCGLYYHVDTVPAAP-GWARDPLKL 122
Cdd:cd08012 32 DNAGRHVLEALTPYSTENGGPLVIDHVSYVKG------RGNIIveypGTVD-GKTVSFVGSHMDVVTANPeTWEFDPFSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 123 SVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGLYPGIrylAEQGMLKGHILNfNGSAAPRI 202
Cdd:cd08012 105 SIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVVAVFIANEENSEIPGV---GVDALVKSGLLD-NLKSGPLY 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 653801302 203 WA---------GCFGVFHLQVTIRGRAVHAGEGNRTgagINAIE 237
Cdd:cd08012 181 WVdsadsqpciGTGGMVTWKLTATGKLFHSGLPHKA---INALE 221
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
96-315 |
1.11e-03 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 40.92 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 96 GKPVCGLYYHVDTVPAApgwardpLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGlplyYDPMLLLCTDEEGGlY 175
Cdd:PRK00466 59 GEGDILLASHVDTVPGY-------IEPKIEGEVIYGRGAVDAKGPLISMIIAAWLLNEKG----IKVMVSGLADEEST-S 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 176 PGIRYLAEQGMLKGHILNFNGSAAPRIWAGCFGVFHLQVTIRGRAVHAGEGNRtgaginaiegalpllNALMALKPDVAS 255
Cdd:PRK00466 127 IGAKELVSKGFNFKHIIVGEPSNGTDIVVEYRGSIQLDIMCEGTPEHSSSAKS---------------NLIVDISKKIIE 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 256 rasaLTPPPhaSGPLRPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIES 315
Cdd:PRK00466 192 ----VYKQP--ENYDKPSIVPTIIRAGESYNVTPAKLYLHFDVRYAINNKRDDLISEIKD 245
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
93-139 |
1.29e-03 |
|
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: 41.05 E-value: 1.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 653801302 93 RDTGKPVCGLYYHVDTVPAAP--GWARDPLKLSVEREDLFGLGAADMKG 139
Cdd:cd05676 81 SDPSKKTVLIYGHLDVQPAKLedGWDTDPFELTEKDGKLYGRGSTDDKG 129
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
96-173 |
1.31e-03 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 40.98 E-value: 1.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 653801302 96 GKPVCGLYYHVDTVPAAPGWARDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGG 173
Cdd:PRK07318 78 GEEVLGILGHLDVVPAGDGWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRFIVGTDEESG 155
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
170-424 |
1.56e-03 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 40.66 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 170 EEGGLypGIRYLAEQGMLKG----HILNF-------NGSAAPRIWAGCFGVFHLQVTIRGRAVHAGEGNrtgAGINAIEG 238
Cdd:cd03886 123 EEGPG--GAKAMIEEGVLENpgvdAAFGLhvwpglpVGTVGVRSGALMASADEFEITVKGKGGHGASPH---LGVDPIVA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 239 ALPLLNALMALKpdvasraSALTPPPHASgplrpQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIR 318
Cdd:cd03886 198 AAQIVLALQTVV-------SRELDPLEPA-----VVTVGKFHAGTAFNVIPDTAVLEGTIRTFDPEVREALEARIKRLAE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 319 DSVAGTGLGLEMALVGHLIPT-NDPEGPHwpRWQKALS--LGFGYKPEDFQKWGAascSDFGYvqksgFAQEV-----LL 390
Cdd:cd03886 266 GIAAAYGATVELEYGYGYPAViNDPELTE--LVREAAKelLGEEAVVEPEPVMGS---EDFAY-----YLEKVpgaffWL 335
|
250 260 270
....*....|....*....|....*....|....*.
gi 653801302 391 G--GLGRPESCIHSPEEhTTRRDIIALAKSILAYLA 424
Cdd:cd03886 336 GagEPDGENPGLHSPTF-DFDEDALPIGAALLAELA 370
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
46-264 |
3.19e-03 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 39.63 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 46 GYDAFADLMAELLSPLGFEFERvvvPRDLWYVAGGPASGER--TNLIATRDTGKPVCGLYYHVDTVPAA-----PGWARD 118
Cdd:cd05654 21 GERSFADFLKEILKELPYFKEN---PSHVWQLLPPDDLGRRnvTALVKGKKPSKRTIILISHFDTVGIEdygelKDIAFD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 119 PLKL------SVE------RED------LFGLGAADMkgtiaatllalraakKCGLPLY------------YDPMLLLCT 168
Cdd:cd05654 98 PDELtkafseYVEeldeevREDllsgewLFGRGTMDM---------------KSGLAVHlalleqasededFDGNLLLMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 169 --DEEG---GLYPGIRYLAE-----QGMLKGHILN------FNGSAAPRIWAGCFGVFHLQVTIRGRAVHAGEgnrTGAG 232
Cdd:cd05654 163 vpDEEVnsrGMRAAVPALLElkkkhDLEYKLAINSepifpqYDGDQTRYIYTGSIGKILPGFLCYGKETHVGE---PFAG 239
|
250 260 270
....*....|....*....|....*....|...
gi 653801302 233 INAIEGAlPLLNALMALKPDVASRASA-LTPPP 264
Cdd:cd05654 240 INANLMA-SEITARLELNADLCEKVEGeITPPP 271
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
28-325 |
5.80e-03 |
|
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: 38.62 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 28 VDDLARMIEVDTsfPPGLGYDAfADLMAELLSPLGFEfervvvprdlwyvagGPASGERTNLIATR--DTGKPVCGLYYH 105
Cdd:cd03896 1 VDTAIELGEIPA--PTFREGAR-ADLVAEWMADLGLG---------------DVERDGRGNVVGRLrgTGGGPALLFSAH 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 106 VDTVPAApgwaRDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLL-LCTDEEGGLYPGIRYLAEQ 184
Cdd:cd03896 63 LDTVFPG----DTPATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAaNVGEEGLGDLRGARYLLSA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 185 gmlKGHILNFNGSAapriwAGCFGVFHLQV--TIRGRAVHAGEGNRTGaginaieGALPLLNALMALkpdvASRASALTP 262
Cdd:cd03896 139 ---HGARLDYFVVA-----EGTDGVPHTGAvgSKRFRITTVGPGGHSY-------GAFGSPSAIVAM----AKLVEALYE 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 653801302 263 PPHASGPlRPQLLISAVNGGTAGGQVPAEIKILVSRRYAPEESYEDALAEIESLIRDSVAGTG 325
Cdd:cd03896 200 WAAPYVP-KTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPDAELADVQREVEAVVSKLAAKHL 261
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
27-180 |
5.81e-03 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 38.80 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 27 AVDDLARMIEVDTSFPPGLGYD------AFADLMAELLSPLGFEFERVvvprdlwyvaggpasGERTNLIATRDTGKPVC 100
Cdd:PRK06156 48 AIESLRELVAFPTVRVEGVPQHenpefiGFKKLLKSLARDFGLDYRNV---------------DNRVLEIGLGGSGSDKV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 653801302 101 GLYYHVDTVPAAPG-WA-----RDPLKLSVEREDLFGLGAADMKGTIAATLLALRAAKKCGLPLYYDPMLLLCTDEEGGl 174
Cdd:PRK06156 113 GILTHADVVPANPElWVldgtrLDPFKVTLVGDRLYGRGTEDDKGAIVTALYAMKAIKDSGLPLARRIELLVYTTEETD- 191
|
....*.
gi 653801302 175 YPGIRY 180
Cdd:PRK06156 192 GDPLKY 197
|
|
| |
