|
Name |
Accession |
Description |
Interval |
E-value |
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
9-344 |
2.03e-159 |
|
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: 449.80 E-value: 2.03e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 9 VEKRLLEYMSHSSTTGNEAAFADVVAKDLEENGWTVYKQSIPNSDRYNIYATFRNSdpKHVKVLLNTHLDTVPPYFPPTQ 88
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKQPVENKDRFNVYAYPGSS--RQPRVLLTSHIDTVPPFIPYSI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 89 D--EQNIYGNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEEFDHIGMIEANKLEIL-PEYLLVGEPTELKFG 165
Cdd:cd05652 79 SdgGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGDGMKAFNDLGLNtWDAVIFGEPTELKLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 166 TIQKGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQLAKWPCDATNGATTYNIGKISGGQALNAWAANCEADIFF 245
Cdd:cd05652 159 SGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPSSELLGPTTLNIGRISGGVAANVVPAAAEASVAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 246 RVVTSVKDIQNQLLALVNG------RAEVSLLSFNDPVILDVPPIEAELDHVSFNTDIAYFDARDKvkaKYLFGGGSIKN 319
Cdd:cd05652 239 RLAAGPPEVKDIVKEAVAGiltdteDIEVTFTSGYGPVDLDCDVDGFETDVVAYGTDIPYLKGDHK---RYLYGPGSILV 315
|
330 340
....*....|....*....|....*
gi 17551016 320 AHSKNEFIPKDELHKCTATLVKLVN 344
Cdd:cd05652 316 AHGPDEAITVSELEEAVEGYKKLIL 340
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
21-346 |
6.11e-72 |
|
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: 228.62 E-value: 6.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 21 STTGNEAAFADVVAKDLEENGWTVYKQSIPnSDRYNIYATFRNSDPKHVkVLLNTHLDTVPPY---------FPPTQDEQ 91
Cdd:COG0624 26 SVSGEEAAAAELLAELLEALGFEVERLEVP-PGRPNLVARRPGDGGGPT-LLLYGHLDVVPPGdlelwtsdpFEPTIEDG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 92 NIYGNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEEFDHIG---MIEANKLEILPEYLLVGEPTElkFGTI- 167
Cdd:COG0624 104 RLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSPGaraLVEELAEGLKADAAIVGEPTG--VPTIv 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 168 --QKGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQLAKWP--CDATNGATTYNIGKISGGQALNAWAANCEADI 243
Cdd:COG0624 182 tgHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDgrADPLFGRTTLNVTGIEGGTAVNVIPDEAEAKV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 244 FFRVVT--SVKDIQNQLLALVNG-----RAEVSLLSFNDP----------------VILDVPPIEAELDHVSFNTDIAYF 300
Cdd:COG0624 262 DIRLLPgeDPEEVLAALRALLAAaapgvEVEVEVLGDGRPpfetppdsplvaaaraAIREVTGKEPVLSGVGGGTDARFF 341
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 17551016 301 DARDKVKAkYLFGGGSIKNAHSKNEFIPKDELHKCTATLVKLVNHL 346
Cdd:COG0624 342 AEALGIPT-VVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERL 386
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
21-343 |
3.84e-54 |
|
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: 181.73 E-value: 3.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 21 STTGNEAAFADVVAKDLEENGWTVykQSIPNSDRYNIYATFRNSDPKHVkvLLNTHLDTVPPY---------FPPTQDEQ 91
Cdd:cd08659 11 SVNPPEAEVAEYLAELLAKRGYGI--ESTIVEGRGNLVATVGGGDGPVL--LLNGHIDTVPPGdgdkwsfppFSGRIRDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 92 NIYGNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEEFDHIGM---IEANKLEiLPEYLLVGEPTELKFGTIQ 168
Cdd:cd08659 87 RLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGAralLEAGYAD-RLDALIVGEPTGLDVVYAH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 169 KGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQ--LAKWPCDATNGATTYNIGKISGGQALNAWAANCEADIFFR 246
Cdd:cd08659 166 KGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRtlFEELPAHPLLGPPTLNVGVINGGTQVNSIPDEATLRVDIR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 247 VVTS------VKDIQnQLLALVNGRAEVSLLSFNDPVI---LDVPPI------------EAELDHVSFNTDIAYFDARDK 305
Cdd:cd08659 246 LVPGetnegvIARLE-AILEEHEAKLTVEVSLDGDPPFftdPDHPLVqalqaaaralggDPVVRPFTGTTDASYFAKDLG 324
|
330 340 350
....*....|....*....|....*....|....*...
gi 17551016 306 VKAkYLFGGGSIKNAHSKNEFIPKDELHKCTATLVKLV 343
Cdd:cd08659 325 FPV-VVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
26-344 |
4.20e-45 |
|
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: 158.14 E-value: 4.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 26 EAAFADVVAKDLEENGWTVYKQSIPNSDRYNIYATFRNSDPKhvKVLLNTHLDTVP--------PYFPPTQDEQNIYGNG 97
Cdd:cd03894 17 NLALIEYVADYLAALGVKSRRVPVPEGGKANLLATLGPGGEG--GLLLSGHTDVVPvdgqkwssDPFTLTERDGRLYGRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 98 SNDAKGQLAAMVTAATIISKtdEDVARALGLLFVVGEEFDHIG---MIEANK-LEILPEYLLVGEPTELKFGTIQKGALK 173
Cdd:cd03894 95 TCDMKGFLAAVLAAVPRLLA--AKLRKPLHLAFSYDEEVGCLGvrhLIAALAaRGGRPDAAIVGEPTSLQPVVAHKGIAS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 174 VKLTVTGQAGHSGYPNSGSSAIHKMIEVL-----HDVQLAKWPCDA--TNGATTYNIGKISGGQALNAWAANCEADIFFR 246
Cdd:cd03894 173 YRIRVRGRAAHSSLPPLGVNAIEAAARLIgklreLADRLAPGLRDPpfDPPYPTLNVGLIHGGNAVNIVPAECEFEFEFR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 247 VV--TSVKDIQNQLLALVN-------GRAEVSLLSfndpvilDVPPIEAELDH-----------------VSFNTDIAYF 300
Cdd:cd03894 253 PLpgEDPEAIDARLRDYAEallefpeAGIEVEPLF-------EVPGLETDEDAplvrlaaalagdnkvrtVAYGTEAGLF 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 17551016 301 DAR--DKVkakyLFGGGSIKNAHSKNEFIPKDELHKCTATLVKLVN 344
Cdd:cd03894 326 QRAgiPTV----VCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
72-345 |
3.23e-37 |
|
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: 135.94 E-value: 3.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 72 LLNTHLDTVPPY------FPPTQDEqNIYGNGSNDAKGQLAAMVTAATIISKTDEDvARALGLLFVVGEEFDHIG---MI 142
Cdd:pfam01546 1 LLRGHMDVVPDEetwgwpFKSTEDG-KLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGGMGGaraLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 143 EANKLE-ILPEY---LLVGEPTEL------KFGTIQKGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQLAKWPC 212
Cdd:pfam01546 79 EDGLLErEKVDAvfgLHIGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 213 DATNGATTYNIGKISGGQ-ALNAWAANCEADIFFRVVT--SVKDIQNQLLALVNGRA-------EVSLLSFNDPVILDVP 282
Cdd:pfam01546 159 VDPLDPAVVTVGNITGIPgGVNVIPGEAELKGDIRLLPgeDLEELEERIREILEAIAaaygvkvEVEYVEGGAPPLVNDS 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17551016 283 PIEAELDHV----------------SFNTDIAYFdaRDKVKAKYLFGGGSIKNAHSKNEFIPKDELHKCTATLVKLVNH 345
Cdd:pfam01546 239 PLVAALREAakelfglkvelivsgsMGGTDAAFF--LLGVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
7-337 |
1.60e-34 |
|
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: 130.21 E-value: 1.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 7 VEVEKRLLEYMSHSSTTGNEAAFADVVAKDLEENG-----WTVYKQSiPNSDRYNIYATFRNSDPKhvKVLLNTHLDTVP 81
Cdd:TIGR01910 1 VELLKDLISIPSVNPPGGNEETIANYIKDLLREFGfstdvIEITDDR-LKVLGKVVVKEPGNGNEK--SLIFNGHYDVVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 82 PY---------FPPTQDEQNIYGNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEEFDHIGMIEANK--LEIL 150
Cdd:TIGR01910 78 AGdlelwktdpFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLLQrgYFKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 151 PEYLLVGEPTELKFGTI-QKGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQ--LAKWPCDAT----NGATTYNI 223
Cdd:TIGR01910 158 ADGVLIPEPSGGDNIVIgHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNelEEHIYARNSygfiPGPITFNP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 224 GKISGGQALNAWAANCEADIFFRVVT--SVKDIQNQLLALVNGRAEVSLLSFNDPVILDVPP------------------ 283
Cdd:TIGR01910 238 GVIKGGDWVNSVPDYCEFSIDVRIIPeeNLDEVKQIIEDVVKALSKSDGWLYENEPVVKWSGpnetppdsrlvkaleaii 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 17551016 284 -----IEAELDHVSFNTDIAYFdaRDKVKAKYLFGGGSIKNAHSKNEFIPKDELHKCTA 337
Cdd:TIGR01910 318 kkvrgIEPEVLVSTGGTDARFL--RKAGIPSIVYGPGDLETAHQVNEYISIKNLVESTK 374
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
50-346 |
4.73e-33 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 126.46 E-value: 4.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 50 PNSDRYNIYATFrnsDPKHVK-VLLNTHLDTVP--------PYFPPTQDEQNIYGNGSNDAKGQLAAMVTAATIISKTDe 120
Cdd:PRK07522 48 PEGDKANLFATI---GPADRGgIVLSGHTDVVPvdgqawtsDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAP- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 121 dVARALGLLFVVGEEfdhIG------MIEA-NKLEILPEYLLVGEPTELKFGTIQKGALKVKLTVTGQAGHSGYPNSGSS 193
Cdd:PRK07522 124 -LRRPLHLAFSYDEE---VGclgvpsMIARlPERGVKPAGCIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 194 AIHKMIEVL-HDVQLAkwpcD--ATNGA---------TTYNIGKISGGQALNAWAANCEADIFFRVVTSVkDIQnQLLAL 261
Cdd:PRK07522 200 AIEYAARLIaHLRDLA----DrlAAPGPfdalfdppySTLQTGTIQGGTALNIVPAECEFDFEFRNLPGD-DPE-AILAR 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 262 VNGRAEVSLLSFN---DP-------VILDVPPIEAELD-----------------HVSFNTDIAYFDArdkvkAKY---L 311
Cdd:PRK07522 274 IRAYAEAELLPEMravHPeaaiefePLSAYPGLDTAEDaaaarlvraltgdndlrKVAYGTEAGLFQR-----AGIptvV 348
|
330 340 350
....*....|....*....|....*....|....*
gi 17551016 312 FGGGSIKNAHSKNEFIPKDELHKCTATLVKLVNHL 346
Cdd:PRK07522 349 CGPGSIEQAHKPDEFVELAQLAACEAFLRRLLASL 383
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
27-343 |
7.07e-32 |
|
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130947 [Multi-domain] Cd Length: 364 Bit Score: 122.62 E-value: 7.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 27 AAFADVVAKDLEENGWTVYKQSIPN-SDRYNIYATFRNSDPKhvKVLLNTHLDTVP----PY----FPPTQDEQNIYGNG 97
Cdd:TIGR01892 18 VDLIDWAQAYLEALGFSVEVQPFPDgAEKSNLVAVIGPSGAG--GLALSGHTDVVPyddaAWtrdpFRLTEKDGRLYGRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 98 SNDAKGQLAAMVTAATIISKTDedVARALGLLFVVGEEFDHIG---MIEANKLEilPEYLLVGEPTELKFGTIQKGALKV 174
Cdd:TIGR01892 96 TCDMKGFLACALAAAPDLAAEQ--LKKPLHLALTADEEVGCTGapkMIEAGAGR--PRHAIIGEPTRLIPVRAHKGYASA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 175 KLTVTGQAGHSGYPNSGSSAIHKMIEVL-HDVQLA-----KWPCDA-TNGATTYNIGKISGGQALNAWAANCEADIFFRV 247
Cdd:TIGR01892 172 EVTVRGRSGHSSYPDSGVNAIFRAGRFLqRLVHLAdtllrEDLDEGfTPPYTTLNIGVIQGGKAVNIIPGACEFVFEWRP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 248 VTSVKdiQNQLLALVNGRAEVslLSFNDP----VILDVPPIEA---ELDH----------------VSFNTDIAYFDaRD 304
Cdd:TIGR01892 252 IPGMD--PEELLQLLETIAQA--LVRDEPgfevQIEVVSTDPGvntEPDAelvafleelsgnapevVSYGTEAPQFQ-EL 326
|
330 340 350
....*....|....*....|....*....|....*....
gi 17551016 305 KVKAkYLFGGGSIKNAHSKNEFIPKDELHKCTATLVKLV 343
Cdd:TIGR01892 327 GAEA-VVCGPGDIRQAHQPDEYVEIEDLVRCRAVLARLV 364
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
7-347 |
1.00e-28 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 114.70 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 7 VEVEKRLLEYMSHSSTTGNEAAFADVVAKDLEENGWTVYKQSIPNS--DRYNIYATF----RNSDPKHVkvLLNTHLDTV 80
Cdd:PRK08651 9 VEFLKDLIKIPTVNPPGENYEEIAEFLRDTLEELGFSTEIIEVPNEyvKKHDGPRPNliarRGSGNPHL--HFNGHYDVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 81 PPY--------FPPTQDEQNIYGNGSNDAKGQLAAMVTAatiISKTDEDVARALGLLFVVGEEfdhIGMIEA----NKLE 148
Cdd:PRK08651 87 PPGegwsvnvpFEPKVKDGKVYGRGASDMKGGIAALLAA---FERLDPAGDGNIELAIVPDEE---TGGTGTgylvEEGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 149 ILPEYLLVGEPTELKFGTI-QKGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQLAKWPC-------DATNGATT 220
Cdd:PRK08651 161 VTPDYVIVGEPSGLDNICIgHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIkskyeydDERGAKPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 221 YNIG--KISGGQALNAWAANCEADIFFRVV--TSVKDIQNQLLALVNGRAEVSLLSFNDPVILDVPPIEAELDH-----V 291
Cdd:PRK08651 241 VTLGgpTVEGGTKTNIVPGYCAFSIDRRLIpeETAEEVRDELEALLDEVAPELGIEVEFEITPFSEAFVTDPDSelvkaL 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17551016 292 SF-----------------NTDIAYFDARDKVKAKYlfGGGSIKNAHSKNEFIPKDELHKCTATLVKLVNHLY 347
Cdd:PRK08651 321 REairevlgvepkktislgGTDARFFGAKGIPTVVY--GPGELELAHAPDEYVEVKDVEKAAKVYEEVLKRLA 391
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
8-343 |
2.20e-28 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 113.22 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 8 EVEKRLLEYMSHSSTTGNEAAFADVVAKDLEENGWTVYKqsipnSDRYNIYATFRNSDPKHVK-VLLNTHLDTVPPyFP- 85
Cdd:COG2195 4 RLLERFLEYVKIPTPSDHEEALADYLVEELKELGLEVEE-----DEAGNVIATLPATPGYNVPtIGLQAHMDTVPQ-FPg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 86 ----PTQDEQNIYGNGSN----DAKGQLAAMVTAATIIskTDEDVAR-ALGLLFVVGEEfdhIGMIEANKL--EILP-EY 153
Cdd:COG2195 78 dgikPQIDGGLITADGTTtlgaDDKAGVAAILAALEYL--KEPEIPHgPIEVLFTPDEE---IGLRGAKALdvSKLGaDF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 154 LLV---GEPTELKFGTIqkGALKVKLTVTGQAGHSGY-PNSGSSAIHKMIEVLHDVQLAKWPcdatnGATTYNIGKISGG 229
Cdd:COG2195 153 AYTldgGEEGELEYECA--GAADAKITIKGKGGHSGDaKEKMINAIKLAARFLAALPLGRIP-----EETEGNEGFIHGG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 230 QALNAWAANCEADIFFR--VVTSVKDIQNQLLALVN------GRAEVSL----------LSFNDPVI---------LDVP 282
Cdd:COG2195 226 SATNAIPREAEAVYIIRdhDREKLEARKAELEEAFEeenakyGVGVVEVeiedqypnwkPEPDSPIVdlakeayeeLGIE 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17551016 283 PI--------------EAELDHVSFNTDiayfdardkvkakylfgggsIKNAHSKNEFIPKDELHKCTATLVKLV 343
Cdd:COG2195 306 PKikpirggldggilsFKGLPTPNLGPG--------------------GHNFHSPDERVSIESMEKAWELLVEIL 360
|
|
| dapE-gram_pos |
TIGR01900 |
succinyl-diaminopimelate desuccinylase; This model represents a clade of ... |
21-339 |
1.28e-27 |
|
succinyl-diaminopimelate desuccinylase; This model represents a clade of succinyl-diaminopimelate desuccinylases from actinobacteria (high-GC gram positives), delta-proteobacteria and aquificales and is based on the characterization of the enzyme from Corynebacterium glutamicum. This enzyme is involved in the biosynthesis of lysine, and is related to the enzyme acetylornithine deacetylase and other amidases and peptidases found within pfam01546. Other sequences included in the seed of this model were assessed to confirm that 1) the related genes DapC (succinyl-diaminopimelate transaminase) and DapD (2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase) are also found in the genome, 2) each is found only once in those genomes, 3) the lysine biosynthesis pathway is complete and 4) the direct (TIGR03540 or TIGR03542) or acetylated (GenProp0787) aminotransferase pathways are absent in thes genomes. Additionally, a number of the seed members are observed adjacent to either DapC or DapD (often as a divergon with a putative promoter site between them. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 273864 [Multi-domain] Cd Length: 351 Bit Score: 110.84 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 21 STTGNEAAFADVVAKDL-EENGWTVYkqsipnsdRYNIYATFRNSDPKHVKVLLNTHLDTVPPY--FPPTQDEQNIYGNG 97
Cdd:TIGR01900 17 SVSGDERALADAVESALrALPHLEVI--------RHGNSVVARTNLGRPSRVILAGHLDTVPIAdnLPSRVEGGRLYGRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 98 SNDAKGQLAAMV-TAATIiskTDEDVARALGLLFVVGEEfdhiGMIEANKLEIL----PEYL-----LVGEPTElkfGTI 167
Cdd:TIGR01900 89 AVDMKGGLAVMLaLAATL---DRTEPRHDLTLVFYEREE----GPAEENGLGRLlrehPEWLagdlaVLLEPTD---GKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 168 Q---KGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHdvQLAKW-PCDATNGATTY----NIGKISGGQALNAWAANC 239
Cdd:TIGR01900 159 EagcQGTLRATVTFHGRRAHSARSWMGENAIHKAAPILA--RLAAYePREVTVDGLTYreglNAVRIEGGVAGNVIPDEC 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 240 EADIFFRVVTSvKDIQN---QLLALVNG-RAEVSL--LSFNDPVILDVPPIEAELDHVSFN-------TDIAYFDAR--D 304
Cdd:TIGR01900 237 EVNVNYRFAPD-RSLEQaraHVRELFEGdGAEVEVtdLSPGARPGLDNPLAAELVAAVGGEvrakygwTDVARFSALgiP 315
|
330 340 350
....*....|....*....|....*....|....*
gi 17551016 305 KVKakylFGGGSIKNAHSKNEFIPKDELHKCTATL 339
Cdd:TIGR01900 316 AVN----FGPGDPALAHQDDEHVPVAQLTACAAIL 346
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
21-247 |
5.29e-26 |
|
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: 106.24 E-value: 5.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 21 STTGNEAAFADVVAKDLEENGWTVYKQSipnsdrYNIYATFRNSDPKHVKVLLNTHLDTVPPY-------FPPTQDEQNI 93
Cdd:cd05651 14 SFSREEHKTADLIENYLEQKGIPFKRKG------NNVWAENGHFDEGKPTLLLNSHHDTVKPNagwtkdpFEPVEKGGKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 94 YGNGSNDAKGQLAAMVTAATIISKTdEDVARALGLLFVVGEEFDHIGMIEAnKLEILP--EYLLVGEPTELKFGTIQKGA 171
Cdd:cd05651 88 YGLGSNDAGASVVSLLATFLHLYSE-GPLNYNLIYAASAEEEISGKNGIES-LLPHLPplDLAIVGEPTEMQPAIAEKGL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17551016 172 LKVKLTVTGQAGHSGYPNsGSSAIHKM---IEVLHDVQLAKwpCDATNGATTYNIGKISGGQALNAWAANCEADIFFRV 247
Cdd:cd05651 166 LVLDCTARGKAGHAARNE-GDNAIYKAlddIQWLRDFRFDK--VSPLLGPVKMTVTQINAGTQHNVVPDSCTFVVDIRT 241
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
4-337 |
4.93e-24 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 101.56 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 4 KWEVEVEKRLLEYMSHSSTTGNEAAFADVVAKDLEENGWTvyKQSIpnsDRY-NIYATFRNSDPKhvkVLLNTHLDTVPP 82
Cdd:PRK13004 12 KYKADMTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFD--KVEI---DPMgNVLGYIGHGKKL---IAFDAHIDTVGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 83 ------YFPP---TQDEQNIYGNGSNDAKGQLAAMVTAATIISKTDEDVAralGLLFVVG----EEFDHIG---MIEANK 146
Cdd:PRK13004 84 gdiknwDFDPfegEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDE---YTLYVTGtvqeEDCDGLCwryIIEEDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 147 leILPEYLLVGEPTELKFGTIQKGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDV-QL-AKWPCDATNGATTYNIG 224
Cdd:PRK13004 161 --IKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELeELnPNLKEDPFLGKGTLTVS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 225 KI-SGGQALNAWAANCEADIFFRVV------TSVKDIQNqLLALVNGRAEVSLLSFNDP----------------VILDV 281
Cdd:PRK13004 239 DIfSTSPSRCAVPDSCAISIDRRLTvgetweSVLAEIRA-LPAVKKANAKVSMYNYDRPsytglvyptecyfptwLYPED 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 282 PPI--------------EAELDHVSFNTDIAYFDARDKVKAkYLFGGGSIKNAHSKNEFIPKDELHKCTA 337
Cdd:PRK13004 318 HEFvkaaveaykglfgkAPEVDKWTFSTNGVSIAGRAGIPT-IGFGPGKEPLAHAPNEYTWKEQLVKAAA 386
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-337 |
6.66e-24 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 100.96 E-value: 6.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 13 LLEYMSHSSTTGNEAAFADVVAKDLEENGWTvyKQSIpnsDRY-NIYATFRNSDPKhvkVLLNTHLDTVP---------- 81
Cdd:cd05649 4 LRDLIQIPSESGEEKGVVERIEEEMEKLGFD--EVEI---DPMgNVIGYIGGGKKK---ILFDGHIDTVGignidnwkfd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 82 PYFPPTQDEQnIYGNGSNDAKGQLAAMVTAATIISktDEDVARALGLLFVVG----EEFDHIGMIE-ANKLEILPEYLLV 156
Cdd:cd05649 76 PYEGYETDGK-IYGRGTSDQKGGLASMVYAAKIMK--DLGLRDFAYTILVAGtvqeEDCDGVCWQYiSKADKIKPDFVVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 157 GEPTELKFGTIQKGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQL--AKWPCDATNGATTYNIGKI-SGGQALN 233
Cdd:cd05649 153 GEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQlnPNFPEAPFLGRGTLTVTDIfSTSPSRC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 234 AWAANCEADIFFRVV------TSVKDIQNqLLALVNGRAEVSLLSFNdpviLDVP-------PIEA-------------- 286
Cdd:cd05649 233 AVPDSCRISIDRRLTvgetweGCLEEIRA-LPAVKKYGDDVAVSMYN----YDRPsytgevyESERyfptwllpedhelv 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17551016 287 ---------------ELDHVSFNTDIAYFDARDKVKAkYLFGGGSIKNAHSKNEFIPKDELHKCTA 337
Cdd:cd05649 308 kalleaykalfgarpLIDKWTFSTNGVSIMGRAGIPC-IGFGPGAENQAHAPNEYTWKEDLVRCAA 372
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
13-340 |
2.50e-23 |
|
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: 98.96 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 13 LLEYMSHSSTTGNEAAFADVVAKDLEENGWTVYKQSIPNsdryniYATFRNSDPkhVKVLLNTHLDTVPPYFPPTQDEQN 92
Cdd:cd05653 7 LLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEAGN------AVGGAGSGP--PDVLLLGHIDTVPGEIPVRVEGGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 93 IYGNGSNDAKGQLAAMVTAATIISKTDEDVARALGLlfvVGEEFDHIGMIEANKLEILPEYLLVGEPTELKFGTIQ-KGA 171
Cdd:cd05653 79 LYGRGAVDAKGPLAAMILAASALNEELGARVVVAGL---VDEEGSSKGARELVRRGPRPDYIIIGEPSGWDGITLGyRGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 172 LKVKLTVTGQAGHSGYPNSGS--SAIHKMIEVLHDVQLAKWPcDATNGATTYNIgkISGGQALNAWAANCEADIFFRVvt 249
Cdd:cd05653 156 LLVKIRCEGRSGHSSSPERNAaeDLIKKWLEVKKWAEGYNVG-GRDFDSVVPTL--IKGGESSNGLPQRAEATIDLRL-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 250 SVKDIQNQLLALVNGRAEVSLLSFNDpvilDVPPIEaeldhVSFNTDIAYFDARDKVKAKY------------------- 310
Cdd:cd05653 231 PPRLSPEEAIALATALLPTCELEFID----DTEPVK-----VSKNNPLARAFRRAIRKQGGkprlkrktgtsdmnvlapl 301
|
330 340 350
....*....|....*....|....*....|....*.
gi 17551016 311 ------LFGGGSIKNAHSKNEFIPKDELHKCTATLV 340
Cdd:cd05653 302 wtvpivAYGPGDSTLDHTPNEHIELAEIERAAAVLK 337
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
24-335 |
5.05e-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: 98.23 E-value: 5.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 24 GNEAAFADVVAKDLEENGWTVYKQSIPNSdRYNIYATFRNSDPKHvKVLLNTHLDTVPPY------FPPTQ---DEQNIY 94
Cdd:cd08011 18 DNTSAIAAYIKLLLEDLGYPVELHEPPEE-IYGVVSNIVGGRKGK-RLLFNGHYDVVPAGdgegwtVDPYSgkiKDGKLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 95 GNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEE-FDHIG---MIEanKLEILPEYLLVGEPTEL---KFGti 167
Cdd:cd08011 96 GRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEEtGGRAGtkyLLE--KVRIKPNDVLIGEPSGSdniRIG-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 168 QKGALKVKLTVTGQAGHSGYPNSGSSAIH---KMIEVLHDVQlakwpcdatngaTTYNIGKISGGQALNAWAANCEADIF 244
Cdd:cd08011 172 EKGLVWVIIEITGKPAHGSLPHRGESAVKaamKLIERLYELE------------KTVNPGVIKGGVKVNLVPDYCEFSVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 245 FRVV--TSVKDIQNQLLALVNGRAEVS--LLSFNDP---------------VILDVPPIEAELdhvsfNTDIAYFDARDK 305
Cdd:cd08011 240 IRLPpgISTDEVLSRIIDHLDSIEEVSfeIKSFYSPtvsnpdseivkkteeAITEVLGIRPKE-----VISVGASDARFY 314
|
330 340 350
....*....|....*....|....*....|...
gi 17551016 306 VKA---KYLFGGGSIKNAHSKNEFIPKDELHKC 335
Cdd:cd08011 315 RNAgipAIVYGPGRLGQMHAPNEYVEIDELIKV 347
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
21-332 |
5.74e-23 |
|
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: 97.94 E-value: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 21 STTGNEAAFADVVAKDLEENGWtvykQSIPNSDRYNIYATFRNSDPKhVKVLLNTHLDTVppyFP------PTQDEQNIY 94
Cdd:cd03896 12 APTFREGARADLVAEWMADLGL----GDVERDGRGNVVGRLRGTGGG-PALLFSAHLDTV---FPgdtpatVRHEGGRIY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 95 GNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEE--FDHIGM---IEANKLEIlpEYLLVGEPTELKFGTIQK 169
Cdd:cd03896 84 GPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEglGDLRGArylLSAHGARL--DYFVVAEGTDGVPHTGAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 170 GALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDvqLAKWPCDATNgATTYNIGKISGGQALNAWAANCEADIFFRVVT 249
Cdd:cd03896 162 GSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEA--LYEWAAPYVP-KTTFAAIRGGGGTSVNRIANLCSMYLDIRSNP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 250 SVK--DIQNQLLALVNGRAEvsllsfndpvilDVPPIEAELDHVSF--------------NTDIAY----------FDAR 303
Cdd:cd03896 239 DAElaDVQREVEAVVSKLAA------------KHLRVKARVKPVGDrpggeaqgteplvnAAVAAHrevggdprpgSSST 306
|
330 340 350
....*....|....*....|....*....|....*
gi 17551016 304 DKVKAKYL------FGGGSIKNAHSKNEFIPKDEL 332
Cdd:cd03896 307 DANPANSLgipavtYGLGRGGNAHRGDEYVLKDDM 341
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
13-349 |
2.33e-22 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 96.37 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 13 LLEYMSHSSTTGNEAAFADVVAKDLEENGWTVYKQSipNSDRYNIyatFRNSDPKhvkVLLNTHLDTVPPYFPPTQDEQN 92
Cdd:PRK08652 8 LKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIES--DGEVINI---VVNSKAE---LFVEVHYDTVPVRAEFFVDGVY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 93 IYGNGSNDAKGQLAAMVTAATIISKTDEDVarALGLLFVVGEEfdHIGMIEANKLEIL-PEYLLVGEPTELKFGTIQKGA 171
Cdd:PRK08652 80 VYGTGACDAKGGVAAILLALEELGKEFEDL--NVGIAFVSDEE--EGGRGSALFAERYrPKMAIVLEPTDLKVAIAHYGN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 172 LKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQlAKWPCDATNGATTYNIGKISGGQALNAWAANCEADIFFRVV--T 249
Cdd:PRK08652 156 LEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLK-ELLKALGKYFDPHIGIQEIIGGSPEYSIPALCRLRLDARIPpeV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 250 SVKDIQNQLLALVNG-RAEVSLLSFNDPVILD------------VPPIEAELDHVSFN--TDIAYFdaRDKVKAKYLFGG 314
Cdd:PRK08652 235 EVEDVLDEIDPILDEyTVKYEYTEIWDGFELDedeeivqllekaMKEVGLEPEFTVMRswTDAINF--RYNGTKTVVWGP 312
|
330 340 350
....*....|....*....|....*....|....*
gi 17551016 315 GSIKNAHSKNEFIPKDELHKCTATLVKLvNHLYLE 349
Cdd:PRK08652 313 GELDLCHTKFERIDVREVEKAKEFLKAL-NEILLE 346
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
168-263 |
2.26e-21 |
|
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: 87.40 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 168 QKGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQLAKWPCDATNGATTYNIGKISGGQALNAWAANCEADIFFRV 247
Cdd:pfam07687 3 HKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGFDFPRTTLNITGIEGGTATNVIPAEAEAKFDIRL 82
|
90
....*....|....*...
gi 17551016 248 VT--SVKDIQNQLLALVN 263
Cdd:pfam07687 83 LPgeDLEELLEEIEAILE 100
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
7-264 |
2.50e-21 |
|
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: 93.34 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 7 VEVEKRLLEYmshSSTTGNEAAFADVVAKDLEENGWTVYKqsIPNSDRYNIYATfRNSDPKHVkvLLNTHLDTVPP---- 82
Cdd:cd03891 1 LELAKELIRR---PSVTPDDAGAQDLIAERLKALGFTCER--LEFGGVKNLWAR-RGTGGPHL--CFAGHTDVVPPgdle 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 83 -----YFPPTQDEQNIYGNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEEFDHI-G---MIEA-NKLEILPE 152
Cdd:cd03891 73 gwssdPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIdGtkkVLEWlKARGEKID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 153 YLLVGEPT-ELKFGTIQK----GALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDvqLAKWPCDATN---GATTYNIG 224
Cdd:cd03891 153 YCIVGEPTsEKKLGDTIKigrrGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAE--LTATVLDEGNeffPPSSLQIT 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17551016 225 KI-SGGQALNAWAANCEADIFFRV--VTSVKDIQNQLLALVNG 264
Cdd:cd03891 231 NIdVGNGATNVIPGELKAKFNIRFndEHTGESLKARIEAILDK 273
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
27-263 |
1.37e-20 |
|
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: 91.50 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 27 AAFADVVAKDLEENGWTVykQSIPNSDRYN-IYATFRNSDPKHVkvLLNTHLDTVppyFPP--------TQDEQNIYGNG 97
Cdd:cd03885 22 DRVAELLAEELEALGFTV--ERRPLGEFGDhLIATFKGTGGKRV--LLIGHMDTV---FPEgtlafrpfTVDGDRAYGPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 98 SNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEEfdhIGMIEANKLeILPE-----YLLVGEPT----ELKFGTiq 168
Cdd:cd03885 95 VADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEE---IGSPGSREL-IEEEakgadYVLVFEPAradgNLVTAR-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 169 KGALKVKLTVTGQAGHSG-YPNSGSSAI----HKMIEVLHDVQLAKwpcdatngATTYNIGKISGGQALNAWAANCEADI 243
Cdd:cd03885 169 KGIGRFRLTVKGRAAHAGnAPEKGRSAIyelaHQVLALHALTDPEK--------GTTVNVGVISGGTRVNVVPDHAEAQV 240
|
250 260
....*....|....*....|..
gi 17551016 244 FFRVVTS--VKDIQNQLLALVN 263
Cdd:cd03885 241 DVRFATAeeADRVEEALRAIVA 262
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-339 |
4.75e-20 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 90.45 E-value: 4.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 13 LLEYMSHSSTTGNEAAFADVVAKDLEENGWTVYKQSI------------PN----SDRYNIYATFRNSDPKHVKVLLNTH 76
Cdd:cd03895 3 LQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDRWEIdveklkhhpgfsPVavdyAGAPNVVGTHRPRGETGRSLILNGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 77 LDTVP---------PYFPPTQDEQNIYGNGSNDAKGQLAAMVTAAtiisktdeDVARALGL------LF--VVGEEFDHI 139
Cdd:cd03895 83 IDVVPegpvelwtrPPFEATIVDGWMYGRGAGDMKAGLAANLFAL--------DALRAAGLqpaadvHFqsVVEEECTGN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 140 GMIEAnkleILPEY----LLVGEPTELKFGTIQKGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQL--AKWpcD 213
Cdd:cd03895 155 GALAA----LMRGYradaALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQEleREW--N 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 214 ATNGAT----------TYNIGKISGGQALNAWAANCEAD--IFFRVVTSVKDIQNQLlalvngRAEVSLLSFNDPVILDV 281
Cdd:cd03895 229 ARKKSHphfsdhphpiNFNIGKIEGGDWPSSVPAWCVLDcrIGIYPGESPEEARREI------EECVADAAATDPWLSNH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 282 PP-------------IEAELDHVS---------FNTDI------AYFDARdkVKAKY------LFGGGSiKNAHSKNEFI 327
Cdd:cd03895 303 PPevewngfqaegyvLEPGSDAEQvlaaahqavFGTPPvqsamtATTDGR--FFVLYgdipalCYGPGS-RDAHGFDESV 379
|
410
....*....|..
gi 17551016 328 PKDELHKCTATL 339
Cdd:cd03895 380 DLESLRKITKTI 391
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
11-350 |
3.35e-19 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 87.15 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 11 KRLLEYMSHSSTTGNEAAFADVVAKDLEENGWTVYKQSIPNSdryniyatFRNSDPKhvkVLLNTHLDTVPPYFPPTQDE 90
Cdd:PRK00466 14 ELLLDLLSIYTPSGNETNATKFFEKISNELNLKLEILPDSNS--------FILGEGD---ILLASHVDTVPGYIEPKIEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 91 QNIYGNGSNDAKGQLAAMVTAATIISKTDEDVArALGLlfvVGEEFDHIGMIEANKLEILPEYLLVGEPTElKFGTI--Q 168
Cdd:PRK00466 83 EVIYGRGAVDAKGPLISMIIAAWLLNEKGIKVM-VSGL---ADEESTSIGAKELVSKGFNFKHIIVGEPSN-GTDIVveY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 169 KGALKVKLTVTGQAGHSGYPNSGS--SAIHKMIEVLhdvqlaKWPCDATNGATTYNIgkISGGQALNAWAANceADIFFR 246
Cdd:PRK00466 158 RGSIQLDIMCEGTPEHSSSAKSNLivDISKKIIEVY------KQPENYDKPSIVPTI--IRAGESYNVTPAK--LYLHFD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 247 VVTSVKDIQNQLLALVNGRAEVSLLSfndpVILDVPPIEaeldhVSFNTDIAYFDARDKVKAKY---------------- 310
Cdd:PRK00466 228 VRYAINNKRDDLISEIKDKFQECGLK----IVDETPPVK-----VSINNPVVKALMRALLKQNIkprlvrkagtsdmnil 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 17551016 311 --------LFGGGSIKNAHSKNEFIPKDELHKCTATLVKLVNHLYLEH 350
Cdd:PRK00466 299 qkittsiaTYGPGNSMLEHTNQEKITLDEIYIAVKTYMLAIEELWQKS 346
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
21-247 |
3.78e-19 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 86.93 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 21 STTGNEAAFADVVAKDLEENGWTVYkqsIPNSDryNIYATfRNSDPkhVKVLLNTHLDTVPPYFPPTQDEQNIYGNGSND 100
Cdd:PRK04443 20 SPSGEEAAAAEFLVEFMESHGREAW---VDEAG--NARGP-AGDGP--PLVLLLGHIDTVPGDIPVRVEDGVLWGRGSVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 101 AKGQLAAMVTAATIISKTdedvaRALGLLFV--VGEEFDHIG--MIEANKLEilPEYLLVGEPTELKFGTI-QKGALKVK 175
Cdd:PRK04443 92 AKGPLAAFAAAAARLEAL-----VRARVSFVgaVEEEAPSSGgaRLVADRER--PDAVIIGEPSGWDGITLgYKGRLLVT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17551016 176 LTVTGQAGHSGYPnsGSSAIHKMIEVLHDVqlAKWpCDATNGAT------TYNIGKI-SGGQALNAWAancEADIFFRV 247
Cdd:PRK04443 165 YVATSESFHSAGP--EPNAAEDAIEWWLAV--EAW-FEANDGRErvfdqvTPKLVDFdSSSDGLTVEA---EMTVGLRL 235
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
17-339 |
5.90e-19 |
|
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: 86.34 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 17 MSHSSTTGNEAAFADVVAKDLEENG-WTVYkqsipnsdRYNIYATFRNSDPKHVKVLLNTHLDTVP--PYFPPTQDEQNI 93
Cdd:cd05647 9 VDIPSVSGNEKPIADEIEAALRTLPhLEVI--------RDGNTVVARTERGLASRVILAGHLDTVPvaGNLPSRVEEDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 94 -YGNGSNDAKGQLAAMV-TAATIiskTDEDVARALGLLFVVGEEFDHigmiEANKL----EILPEYL-----LVGEPTEl 162
Cdd:cd05647 81 lYGCGATDMKAGDAVQLkLAATL---AAATLKHDLTLIFYDCEEVAA----ELNGLgrlaEEHPEWLaadfaVLGEPTD- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 163 kfGTIQ---KGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQLAKwPCDATNGATTY----NIGKISGGQALNAW 235
Cdd:cd05647 153 --GTIEggcQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLAAYE-PRTVNIDGLTYreglNAVFISGGVAGNVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 236 AANCEADIFFRVV--TSVKDIQNQLLALVNGraEVSLLSFND------PViLDVPPIEAELDHVSFN-------TDIAYF 300
Cdd:cd05647 230 PDEARVNLNYRFApdKSLAEAIAHVREVFEG--LGYEIEVTDlspgalPG-LDHPVARDLIEAVGGKvrakygwTDVARF 306
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 17551016 301 DAR--DKVKakylFGGGSIKNAHSKNEFIPKDELHKCTATL 339
Cdd:cd05647 307 SALgiPAVN----FGPGDPLLAHKRDEQVPVEQITACAAIL 343
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
18-290 |
6.18e-19 |
|
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: 86.76 E-value: 6.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 18 SHSSTTG-NEAAFADVVAKDLEENGWTVYK-QSIPnsDRYNIYATFRNSDPKHvKVLLNTHLDTVP-------PYFPPTQ 88
Cdd:cd08013 19 SLSATGGaGEAEIATYVAAWLAHRGIEAHRiEGTP--GRPSVVGVVRGTGGGK-SLMLNGHIDTVTldgydgdPLSGEIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 89 DEQnIYGNGSNDAKGQLAAMVTAATiisktdedVARALGL------LFVVGEEFDHIGMIEANKLEILPEYLLVGEPTEL 162
Cdd:cd08013 96 DGR-VYGRGTLDMKGGLAACMAALA--------DAKEAGLrgdvilAAVADEEDASLGTQEVLAAGWRADAAIVTEPTNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 163 KFGTIQKGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVL-----HDVQLAKWPCDATNGATTYNIGKISGGQALNAWAA 237
Cdd:cd08013 167 QIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLvaleeYQQELPERPVDPLLGRASVHASLIKGGEEPSSYPA 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 17551016 238 NCEADIFFRVVTSVKD--IQNQLLALVNGRA-EVSLLSFNDP-VILDVPPIEAELDH 290
Cdd:cd08013 247 RCTLTIERRTIPGETDesVLAELTAILGELAqTVPNFSYREPrITLSRPPFEVPKEH 303
|
|
| dapE-lys-deAc |
TIGR01902 |
N-acetyl-ornithine/N-acetyl-lysine deacetylase; This clade of mainly archaeal and related ... |
13-200 |
1.65e-18 |
|
N-acetyl-ornithine/N-acetyl-lysine deacetylase; This clade of mainly archaeal and related bacterial species contains two characterized enzymes, an deacetylase with specificity for both N-acetyl-ornithine and N-acetyl-lysine from Thermus, which is found within a lysine biosynthesis operon, and a fusion protein with acetyl-glutamate kinase (an enzyme of ornithine biosynthesis) from Lactobacillus. It is possible that all of the sequences within this clade have dual specificity, or that a mix of specificities have evolved within this clade.
Pssm-ID: 130957 [Multi-domain] Cd Length: 336 Bit Score: 85.29 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 13 LLEYMSHSSTTGNEAAFADVVAKDLEENGWTVYkqsIPNSDryNIYAtfrNSDPKHVKVLLNTHLDTVPPYFPPTQDEQN 92
Cdd:TIGR01902 3 LKDLLEIYSPSGKEANAAKFLEEISKDLGLKLI---IDDAG--NFIL---GKGDGHKKILLAGHVDTVPGYIPVKIEGGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 93 IYGNGSNDAKGQLAAMVTAATIISKTDEDVaRALGLlfvVGEEFDHIGMIEA-NKLEilPEYLLVGEPTELKFGTIQ-KG 170
Cdd:TIGR01902 75 LYGRGAVDAKGPLIAMIFATWLLNEKGIKV-IVSGL---VDEESSSKGAREViDKNY--PFYVIVGEPSGAEGITLGyKG 148
|
170 180 190
....*....|....*....|....*....|
gi 17551016 171 ALKVKLTVTGQAGHSGypnSGSSAIHKMIE 200
Cdd:TIGR01902 149 SLQLKIMCEGTPFHSS---SAGNAAELLID 175
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
70-344 |
1.70e-17 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 82.56 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 70 KVLLNTHLDTVPPYFPPTQD-------EQNIYGNGSNDAKGQLAAMVTAAtiiSKTDEDVAralgLLFVVGEEFDHIGMI 142
Cdd:PRK08737 65 KYLFNVHLDTVPDSPHWSADphvmrrtDDRVIGLGVCDIKGAAAALLAAA---NAGDGDAA----FLFSSDEEANDPRCV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 143 EANkLEILPEY--LLVGEPTELKFGTIQKGALKVKLTVTGQAGHSGYPNSGS-SAIHkmievlhdvQLAKWPCDATNGAT 219
Cdd:PRK08737 138 AAF-LARGIPYeaVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKQDPSaSALH---------QAMRWGGQALDHVE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 220 T-------------YNIGKISGGQALNAWAANCEADIFFRVVTSvkDIQNQLLALVNGRAEVSLLSFND----PVI---- 278
Cdd:PRK08737 208 SlaharfggltglrFNIGRVEGGIKANMIAPAAELRFGFRPLPS--MDVDGLLATFAGFAEPAAATFEEtfrgPSLpsgd 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 279 -----------------LDVPPIEAeldhVSFNTDIAYFDArdkvkAKY---LFGGGSIKNAHSKNEFIPKDELHKCTAT 338
Cdd:PRK08737 286 iaraeerrlaardvadaLDLPIGNA----VDFWTEASLFSA-----AGYtalVYGPGDIAQAHTADEFVTLDQLQRYAES 356
|
....*.
gi 17551016 339 LVKLVN 344
Cdd:PRK08737 357 VHRIIN 362
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
21-334 |
2.75e-17 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 81.85 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 21 STTGNEAAFADVVAKDLEENGWTVYKQSIpNSDRYNIYATFRNSDPkhvkVL-LNTHLDTVPP------YFPP---TQDE 90
Cdd:PRK08588 16 SVNDNEIEVANYLQDLFAKHGIESKIVKV-NDGRANLVAEIGSGSP----VLaLSGHMDVVAAgdvdkwTYDPfelTEKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 91 QNIYGNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEEFDHIG---MIEANKLEILpEYLLVGEPTELKFGTI 167
Cdd:PRK08588 91 GKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGELGakqLTEKGYADDL-DALIIGEPSGHGIVYA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 168 QKGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQLAKWPCDATN---GATTYNIGKISGGQALNAWAANCEADIF 244
Cdd:PRK08588 170 HKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYFDSIKKHNpylGGLTHVVTIINGGEQVNSVPDEAELEFN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 245 FRVV-----TSVKDIQNQLLALVNgRAEVSLLSFNdpVILDVPPI----EAELDHVS-------FNTDIAYF------DA 302
Cdd:PRK08588 250 IRTIpeydnDQVISLLQEIINEVN-QNGAAQLSLD--IYSNHRPVasdkDSKLVQLAkdvaksyVGQDIPLSaipgatDA 326
|
330 340 350
....*....|....*....|....*....|....*..
gi 17551016 303 RDKVKAKY-----LFGGGSIKNAHSKNEFIPKDELHK 334
Cdd:PRK08588 327 SSFLKKKPdfpviIFGPGNNLTAHQVDEYVEKDMYLK 363
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
10-343 |
3.62e-17 |
|
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349932 [Multi-domain] Cd Length: 368 Bit Score: 81.73 E-value: 3.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 10 EKRL----LEYMSHSSTTGNEAAFADVVAKDLEENGWTVYK---QSIPNSDRYNIYATFrNSDPKHV-KVLLNTHLDTVP 81
Cdd:cd05683 2 EDRLintfLELVQIDSETLHEKEISKVLKKKFENLGLSVIEddaGKTTGGGAGNLICTL-KADKEEVpKILFTSHMDTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 82 P---YFPPTQDEQNIYGNGSN----DAKGQLAAMVTAATIISKTDEDVARaLGLLFVVGEEFDHIGMIEANKLEILPEYL 154
Cdd:cd05683 81 PginVKPPQIADGYIYSDGTTilgaDDKAGIAAILEAIRVIKEKNIPHGQ-IQFVITVGEESGLVGAKALDPELIDADYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 155 LVGEpTELKFGTIQKGA---LKVKLTVTGQAGHSG-YPNSGSSAIHKMIEVLHDVQLAKwpcdaTNGATTYNIGKISGGQ 230
Cdd:cd05683 160 YALD-SEGDVGTIIVGAptqDKINAKIYGKTAHAGtSPEKGISAINIAAKAISNMKLGR-----IDEETTANIGKFQGGT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 231 ALNawaanceadiffrVVTSVKDIQNQLLALVNGRAEVSLLSFNDPVILDVPPIEAeldHVSFNTDIAY----FDARDKV 306
Cdd:cd05683 234 ATN-------------IVTDEVNIEAEARSLDEEKLDAQVKHMKETFETTAKEKGA---HAEVEVETSYpgfkINEDEEV 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17551016 307 --KAKYLF------------GGGS------------------IKNAHSKNEFIPKDELHKCTATLVKLV 343
Cdd:cd05683 298 vkLAKRAAnnlgleinttysGGGSdaniinglgiptvnlgigYENIHTTNERIPIEDLYDTAVLVVEII 366
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
9-343 |
6.29e-16 |
|
peptidase T-like protein; This model represents a clade of enzymes closely related to Peptidase T, an aminotripeptidase found in bacteria. This clade consists of gram positive bacteria of which several additionally contain a Peptidase T gene.
Pssm-ID: 162579 [Multi-domain] Cd Length: 361 Bit Score: 78.05 E-value: 6.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 9 VEKRLLEYMSHSSTTGNEAAFADVVAKDLEENGWTVYKQSIPN--SDRYNIYATFRNSdPKHVKVLLNTHLDTVPPYFPP 86
Cdd:TIGR01883 2 LKKYFLELIQIDSESGKEKAILTYLKKQITKLGIPVSLDEVPAevSNDNNLIARLPGT-VKFDTIFFCGHMDTVPPGAGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 87 T-QDEQNIYGNGSN-----DAKGQLAAMVTAATIIsKTDEDVARALGLLFVVGEEFDHIGMIEANKLEILPEYLLVGEpT 160
Cdd:TIGR01883 81 EpVVEDGIFTSLGGtilgaDDKAGVAAMLEAMDVL-STEETPHGTIEFIFTVKEELGLIGMRLFDESKITAAYGYCLD-A 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 161 ELKFGTIQKGA---LKVKLTVTGQAGHSGY-PNSGSSAIHKMIEVLHDVQLAKwpcdaTNGATTYNIGKISGGQALN--- 233
Cdd:TIGR01883 159 PGEVGNIQLAAptqVKVDATIAGKDAHAGLvPEDGISAISVARMAIHAMRLGR-----IDEETTANIGSFSGGVNTNivq 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 234 ------AWAANCEADIFFRVVTSVKDIQNQLLALVNGRAEVSllsfndpVILDVPPIEAELDHVSFNTDIAYFDARDKVK 307
Cdd:TIGR01883 234 deqlivAEARSLSFRKAEAQVQTMRERFEQAAEKYGATLEEE-------TRLIYEGFKIHPQHPLMNIFKKAAKKIGLKT 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 17551016 308 AKYLFGGGSIKN------------------AHSKNEFIPKDELHKCTATLVKLV 343
Cdd:TIGR01883 307 SEIFSGGGSDANvlnekgvptvnlsagyvhAHTEKETISIEQLVKLAELVIALA 360
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
18-345 |
9.14e-16 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 77.56 E-value: 9.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 18 SHSSTT-----GNEAaFADVVAKDLEENGWTVYKQSIPNS-DRYNIYATFRNSDPKhvkVLLNTHLDTVPpyFPP---TQ 88
Cdd:PRK05111 19 SISATDpaldqSNRA-VIDLLAGWFEDLGFNVEIQPVPGTrGKFNLLASLGSGEGG---LLLAGHTDTVP--FDEgrwTR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 89 D-----EQN--IYGNGSNDAKGQLAAMVTAA------------TIISKTDEDV----ARALgllfvvgeefdhigmIEAN 145
Cdd:PRK05111 93 DpftltEHDgkLYGLGTADMKGFFAFILEALrdidltklkkplYILATADEETsmagARAF---------------AEAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 146 KleILPEYLLVGEPTELKFGTIQKGALKVKLTVTGQAGHSGYPNSGSSAihkmIEVLHDV--QLAKW------------- 210
Cdd:PRK05111 158 A--IRPDCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNA----IELMHDVigELLQLrdelqeryhnpaf 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 211 ----PcdatngatTYNIGKISGGQALNAWAANCEADIFFRVV--TSVKDIQNQL---LALVNGRAEVSLlsFNDPVILDV 281
Cdd:PRK05111 232 tvpyP--------TLNLGHIHGGDAPNRICGCCELHFDIRPLpgMTLEDLRGLLreaLAPVSERWPGRI--TVAPLHPPI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 282 PPIEAELDH----------------VSFNTDiayfdardkvkAKYL---------FGGGSIKNAHSKNEFIPKDELHKCT 336
Cdd:PRK05111 302 PGYECPADHqlvrvvekllghkaevVNYCTE-----------APFIqqlgcptlvLGPGSIEQAHQPDEYLELSFIKPTR 370
|
....*....
gi 17551016 337 ATLVKLVNH 345
Cdd:PRK05111 371 ELLRQLIHH 379
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
22-231 |
1.23e-15 |
|
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: 77.40 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 22 TTGNEAAFADVVAKDLEENGWTVYKQSIPNS-DRYNIYATFRNSDPKHVKVLLNTHLDTVP--------PYFPPTQDEQN 92
Cdd:cd05675 18 GTGSETRAAEVLAARLAEAGIQTEIFVVESHpGRANLVARIGGTDPSAGPLLLLGHIDVVPadasdwsvDPFSGEIKDGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 93 IYGNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEE---FDHIGMIEANKLEILPEY-----------LLVGE 158
Cdd:cd05675 98 VYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEaggENGAKWLVDNHPELFDGAtfalneggggsLPVGK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17551016 159 PTELKF-GTIQKGALKVKLTVTGQAGHSGYPNSgSSAIHKMIEVLHDVQLAKWPC---DATNGATTynIGKISGGQA 231
Cdd:cd05675 178 GRRLYPiQVAEKGIAWMKLTVRGRAGHGSRPTD-DNAITRLAEALRRLGAHNFPVrltDETAYFAQ--MAELAGGEG 251
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
19-343 |
8.01e-15 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 75.04 E-value: 8.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 19 HSSTTGNEAAFADVVAKDLEENGWTV----------------YKQSIPNSDRYNIYATFRNSDPKHVKVLLNTHLDTVP- 81
Cdd:PRK06837 32 FPSTRGAEAPCQDFLARAFRERGYEVdrwsidpddlkshpgaGPVEIDYSGAPNVVGTYRPAGKTGRSLILQGHIDVVPe 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 82 ---------PYFPPTQDEQnIYGNGSNDAKGQLAAMVTAAtiisktdeDVARALGLL--------FVVGEEFDHIGMIEA 144
Cdd:PRK06837 112 gpldlwsrpPFDPVIVDGW-MYGRGAADMKAGLAAMLFAL--------DALRAAGLApaarvhfqSVIEEESTGNGALST 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 145 nkleILPEY----LLVGEPTELKFGTIQKGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQL--AKWPCDATNGA 218
Cdd:PRK06837 183 ----LQRGYradaCLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALREleAEWNARKASDP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 219 --------TTYNIGKISGGQalnaWA----ANCEADIffRVVT----SVKDIQNQLLALVNGRAEV-SLLSFNDP----- 276
Cdd:PRK06837 259 hfedvphpINFNVGIIKGGD----WAssvpAWCDLDC--RIAIypgvTAADAQAEIEACLAAAARDdRFLSNNPPevvws 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 277 -------VILDVPPIEAELDHV---SFNTDI------AYFDAR-----DKVKAkyLFGGGSIKNAHSKNEFIPKDELHKC 335
Cdd:PRK06837 333 gflaegyVLEPGSEAEAALARAhaaVFGGPLrsfvttAYTDTRfyglyYGIPA--LCYGPSGEGIHGFDERVDLESVRKV 410
|
....*...
gi 17551016 336 TATLVKLV 343
Cdd:PRK06837 411 TKTIALFV 418
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
21-263 |
2.11e-14 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 73.58 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 21 STTGNEAAFADVVAKDLEENGWTVYKqsIPNSDRYNIYATfRNSDPKHVkvLLNTHLDTVP---------PYFPPTQDEQ 91
Cdd:PRK13009 16 SVTPDDAGCQDLLAERLEALGFTCER--MDFGDVKNLWAR-RGTEGPHL--CFAGHTDVVPpgdleawtsPPFEPTIRDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 92 NIYGNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEEFDHI-G---MIEAnkLE---ILPEYLLVGEPT-ELK 163
Cdd:PRK13009 91 MLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAInGtvkVLEW--LKargEKIDYCIVGEPTsTER 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 164 FGTIQK----GALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDvqLAKWPCDATN---GATTYNIGKISGG-QALNAW 235
Cdd:PRK13009 169 LGDVIKngrrGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAE--LAATEWDEGNeffPPTSLQITNIDAGtGATNVI 246
|
250 260 270
....*....|....*....|....*....|
gi 17551016 236 AANCEADIFFRVVT--SVKDIQNQLLALVN 263
Cdd:PRK13009 247 PGELEAQFNFRFSTehTAESLKARVEAILD 276
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
11-347 |
2.32e-13 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 70.45 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 11 KRLLEYMSHSSTTGNEAAFADVVAKDLEENG-----WTVYkqsiPNSDryNIYATFRNSDPKHVKVL-LNTHLD------ 78
Cdd:PRK08596 20 KTLVRFETPAPPARNTNEAQEFIAEFLRKLGfsvdkWDVY----PNDP--NVVGVKKGTESDAYKSLiINGHMDvaevsa 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 79 ----TVPPyFPPTQDEQNIYGNGSNDAKGQLAAMVTAATIIskTDEDVARALGLLF--VVGEEFDHIGMIEANKLEILPE 152
Cdd:PRK08596 94 deawETNP-FEPTIKDGWLYGRGAADMKGGLAGALFAIQLL--HEAGIELPGDLIFqsVIGEEVGEAGTLQCCERGYDAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 153 YLLVGEPTELKF---GTIQKGALKVKLTVTGQAG------HSGYPNSGSSAIHKMIEVLHDVQ--------LAKWPcDAT 215
Cdd:PRK08596 171 FAVVVDTSDLHMqgqGGVITGWITVKSPQTFHDGtrrqmiHAGGGLFGASAIEKMMKIIQSLQelerhwavMKSYP-GFP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 216 NGATTYNIGKISGGQALNAWAANCEADI--FFRVVTSVKDIQNQLLALVNGRAEVSL-LSFNDPV--------ILD---- 280
Cdd:PRK08596 250 PGTNTINPAVIEGGRHAAFIADECRLWItvHFYPNETYEQVIKEIEEYIGKVAAADPwLRENPPQfkwggesmIEDrgei 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 281 VPPIEAELDHVSFNTDIAYFDARDKVKAKY--------------------LFGGGSIKNAHSKNEFIPKDELHKCTATLV 340
Cdd:PRK08596 330 FPSLEIDSEHPAVKTLSSAHESVLSKNAILdmsttvtdggwfaefgipavIYGPGTLEEAHSVNEKVEIEQLIEYTKVIT 409
|
....*..
gi 17551016 341 KLVNHLY 347
Cdd:PRK08596 410 AFIYEWC 416
|
|
| PRK06915 |
PRK06915 |
peptidase; |
12-229 |
5.25e-13 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 69.34 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 12 RLL-EYMSHSSTTGNEAAFADVVAKDLEENG-----WTVYKQSIPN-----SDRyniyATFRNSdPKHVKVL-------- 72
Cdd:PRK06915 21 KLLkRLIQEKSVSGDESGAQAIVIEKLRELGldldiWEPSFKKLKDhpyfvSPR----TSFSDS-PNIVATLkgsgggks 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 73 --LNTHLDTVPP------YFPPTQDEQ---NIYGNGSNDAKG-QLAAMVTAATIIS-----KTDedvaralgLLF--VVG 133
Cdd:PRK06915 96 miLNGHIDVVPEgdvnqwDHHPYSGEViggRIYGRGTTDMKGgNVALLLAMEALIEsgielKGD--------VIFqsVIE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 134 EEFDHIGMIEAnkleILPEY----LLVGEPTELKFGTIQKGALKVKLTVTGQAGHSGYPNSGSSAIHK-MIEVLHDVQLA 208
Cdd:PRK06915 168 EESGGAGTLAA----ILRGYkadgAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKsMFVIDHLRKLE 243
|
250 260 270
....*....|....*....|....*....|...
gi 17551016 209 KwpcdATNGATT------------YNIGKISGG 229
Cdd:PRK06915 244 E----KRNDRITdplykgipipipINIGKIEGG 272
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
21-270 |
2.80e-09 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 58.10 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 21 STTGNEAAF---ADVVAKDLEENGWTVYKQSIPNSDRYNIYATFRNSDPKhvKVLLNTHLDTVppyFPP----TQ----D 89
Cdd:PRK06133 51 SGSGDAEGLkqvAALLAERLKALGAKVERAPTPPSAGDMVVATFKGTGKR--RIMLIAHMDTV---YLPgmlaKQpfriD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 90 EQNIYGNGSNDAKGQLAAMVTAATIISKTD-EDVARaLGLLFVVGEEFDHIG---MIEanKLEILPEYLLVGEPTE---- 161
Cdd:PRK06133 126 GDRAYGPGIADDKGGVAVILHALKILQQLGfKDYGT-LTVLFNPDEETGSPGsreLIA--ELAAQHDVVFSCEPGRakda 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 162 LKFGTiqKGALKVKLTVTGQAGHSGY-PNSGSSAIhkmIEVLHDVQLAKWPCDATNGaTTYNIGKISGGQALNAW--AAN 238
Cdd:PRK06133 203 LTLAT--SGIATALLEVKGKASHAGAaPELGRNAL---YELAHQLLQLRDLGDPAKG-TTLNWTVAKAGTNRNVIpaSAS 276
|
250 260 270
....*....|....*....|....*....|....*.
gi 17551016 239 CEADIFFRVVTSVKDIQNQLLALVNGR----AEVSL 270
Cdd:PRK06133 277 AQADVRYLDPAEFDRLEADLQEKVKNKlvpdTEVTL 312
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-194 |
5.21e-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. 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: 57.08 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 7 VEVEKRL--LEYMSHSSTTGNEAAFADVVAKDLEENGWTVYKQ-SIPNS---DRYNIYATFrnsDPKHVKVL-LNTHLDT 79
Cdd:cd05650 4 IELERDLirIPAVNPESGGEGEKEKADYLEKKLREYGFYTLERyDAPDErgiIRPNIVAKI---PGGNDKTLwIISHLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 80 VPP---------YFPPTQDEQNIYGNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEEF-DHIGMIE-ANKLE 148
Cdd:cd05650 81 VPPgdlslwetdPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDgSEYGIQYlLNKFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 17551016 149 IL-PEYLLV----GEPTELKFGTIQKGALKVKLTVTGQAGHSGYPNSGSSA 194
Cdd:cd05650 161 LFkKDDLIIvpdfGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINA 211
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
60-211 |
1.21e-07 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 53.02 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 60 TFRNSDPKHVKVLLNTHLDTVP-----------PYFPPTQDEQNIYGNGSNDAKGQLAAMVTAA------------TII- 115
Cdd:PRK08262 103 TWKGSDPSLKPIVLMAHQDVVPvapgtegdwthPPFSGVIADGYVWGRGALDDKGSLVAILEAAeallaqgfqprrTIYl 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 116 -SKTDEDV----ARALG---------LLFVVgeefDHIGMIEANkleILPeylLVGEPTELkFGTIQKGALKVKLTVTGQ 181
Cdd:PRK08262 183 aFGHDEEVgglgARAIAellkergvrLAFVL----DEGGAITEG---VLP---GVKKPVAL-IGVAEKGYATLELTARAT 251
|
170 180 190
....*....|....*....|....*....|
gi 17551016 182 AGHSGYPnSGSSAIHKMIEVLHDVQLAKWP 211
Cdd:PRK08262 252 GGHSSMP-PRQTAIGRLARALTRLEDNPLP 280
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
8-238 |
1.63e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 52.70 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 8 EVEKRLLEYMShSSTTGNEAAFADVVAKDLEENGWTVYKQSI--PNSDRYNIYATFRNSDPKHvKVLLNTHLDTV----- 80
Cdd:PRK09133 41 DLYKELIEINT-TASTGSTTPAAEAMAARLKAAGFADADIEVtgPYPRKGNLVARLRGTDPKK-PILLLAHMDVVeakre 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 81 -----PpyFPPTQDEQNIYGNGSNDAKGQlAAMVTAATIISKTDEDV-ARALGLLFVVGEEFDHIGMIEA---NKLEIL- 150
Cdd:PRK09133 119 dwtrdP--FKLVEENGYFYGRGTSDDKAD-AAIWVATLIRLKREGFKpKRDIILALTGDEEGTPMNGVAWlaeNHRDLId 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 151 PEYLL----------VGEPTELkfgTIQkGALKV----KLTVTGQAGHSGYPNSgSSAIHKMIEVLHDVQLAKWPC---D 213
Cdd:PRK09133 196 AEFALneggggtldeDGKPVLL---TVQ-AGEKTyadfRLEVTNPGGHSSRPTK-DNAIYRLAAALSRLAAYRFPVmlnD 270
|
250 260
....*....|....*....|....*...
gi 17551016 214 ATNGATTyNIGKISGGQ---ALNAWAAN 238
Cdd:PRK09133 271 VTRAYFK-QSAAIETGPlaaAMRAFAAN 297
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
30-231 |
1.69e-07 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 52.45 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 30 ADVVAKDLEENGWTV---YKQSIP-NSDRY---NIYATFRNSDPKHVkVLLNTHLDTVP--------PyFPPTQDEQNIY 94
Cdd:PRK13013 40 CEFLAARLAPRGFEVeliRAEGAPgDSETYprwNLVARRQGARDGDC-VHFNSHHDVVEvghgwtrdP-FGGEVKDGRIY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 95 GNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEEFDHIGMIE--ANKLEILPE---YLLVGEPTELKFGTI-Q 168
Cdd:PRK13013 118 GRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGGVAylAEQGRFSPDrvqHVIIPEPLNKDRICLgH 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17551016 169 KGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQLAKWPCDAT---------NGA--TTYNIGKISGGQA 231
Cdd:PRK13013 198 RGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEIEERLFPLLATrrtampvvpEGArqSTLNINSIHGGEP 271
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
60-258 |
2.18e-07 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 52.10 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 60 TFRNSDPKHVKVLLNTHLDTVPPY-----FPPTQ----DEQNIYGNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLF 130
Cdd:TIGR01880 63 TWPGSNPELPSILLNSHTDVVPVFrehwtHPPFSafkdEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 131 VVGEE-FDHIGMI------EANKLEI---LPEYLlvGEPTE-LKFGTIQKGALKVKLTVTGQAGHSG--YPNSGSSAIHK 197
Cdd:TIGR01880 143 VPDEEiGGHDGMEkfaktdEFKALNLgfaLDEGL--ASPDDvYRVFYAERVPWWVVVTAPGNPGHGSklMENTAMEKLEK 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17551016 198 MIEVL-----HDVQLAKWPCDATNG-ATTYNIGKISGGQALNAWAANCEADIFFRVVTSV--KDIQNQL 258
Cdd:TIGR01880 221 SVESIrrfreSQFQLLQSNPDLAIGdVTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVdfEEMENRL 289
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
30-204 |
2.24e-07 |
|
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: 52.33 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 30 ADVVAKDLEENGWTVykQSIPNSDRYNIYATFRNSDPKHVKVLLNTHLDTVPPY---------FPPTQDEQNIYGNGSND 100
Cdd:cd03893 27 AEWLADLLRRLGFTV--EIVDTSNGAPVVFAEFPGAPGAPTVLLYGHYDVQPAGdedgwdsdpFELTERDGRLYGRGAAD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 101 AKGQLAAMVTAATIISKTDEDVarALGLLFVV-GEE------FDHIgmIEANKLEILPEYLLVG-------EPTELKFGT 166
Cdd:cd03893 105 DKGPILAHLAALRALMQQGGDL--PVNVKFIIeGEEesgspsLDQL--VEAHRDLLAADAIVISdstwvgqEQPTLTYGL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17551016 167 iqKGALKVKLTVTG--QAGHSGY-----PNSGSSAIhKMIEVLHD 204
Cdd:cd03893 181 --RGNANFDVEVKGldHDLHSGLyggvvPDPMTALA-QLLASLRD 222
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
31-242 |
2.53e-07 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 51.71 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 31 DVVAKDLEENGWTVykQSIPNSDRYN--IYATFRNSDPKHVKVLLNTHLDTVPPY-----FPPTQDEQNIYGNGSNDAKG 103
Cdd:PRK07473 38 DLAARDMAIMGATI--ERIPGRQGFGdcVRARFPHPRQGEPGILIAGHMDTVHPVgtlekLPWRREGNKCYGPGILDMKG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 104 qlAAMVTAATIISKTDEDVARAL--GLLFVVGEEfdhIG------MIEA----NKleilpeYLLVGEPTELKFG-TIQKG 170
Cdd:PRK07473 116 --GNYLALEAIRQLARAGITTPLpiTVLFTPDEE---VGtpstrdLIEAeaarNK------YVLVPEPGRPDNGvVTGRY 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17551016 171 AL-KVKLTVTGQAGHSG-YPNSGSSAIHKMIEVLHDVqlakwpcDATNGA-TTYNIGKISGGQALNAWAANCEAD 242
Cdd:PRK07473 185 AIaRFNLEATGRPSHAGaTLSEGRSAIREMARQILAI-------DAMTTEdCTFSVGIVHGGQWVNCVATTCTGE 252
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
69-233 |
1.38e-06 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 49.58 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 69 VKVLLNTHLDTVppyFPPTQ--------DEQNIYGNGSNDAKGQLAAMVTAATIISKTDedVARALGLLFVVG--EEfdh 138
Cdd:PRK07338 93 RQVLLTGHMDTV---FPADHpfqtlswlDDGTLNGPGVADMKGGIVVMLAALLAFERSP--LADKLGYDVLINpdEE--- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 139 IGMIEANKLeiLPEYL------LVGEPTeLKFGTI---QKGALKVKLTVTGQAGHSGY-PNSGSSAI---HKMIEVLHDV 205
Cdd:PRK07338 165 IGSPASAPL--LAELArgkhaaLTYEPA-LPDGTLagaRKGSGNFTIVVTGRAAHAGRaFDEGRNAIvaaAELALALHAL 241
|
170 180
....*....|....*....|....*...
gi 17551016 206 QlakwpcDATNGaTTYNIGKISGGQALN 233
Cdd:PRK07338 242 N------GQRDG-VTVNVAKIDGGGPLN 262
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
56-167 |
2.93e-06 |
|
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: 47.43 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 56 NIYATFRNSDPKHVkVLLNTHLDTVP---------PYFPPTQDEQNIYGNGSNDAKGQLAAMVTAATIISKTDEDVARAL 126
Cdd:cd18669 1 NVIARYGGGGGGKR-VLLGAHIDVVPagegdprdpPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 17551016 127 GLLFVVGEEFDHIG-----MIEANKLEILPEYLLVGEPTELKFGTI 167
Cdd:cd18669 80 VVAFTPDEEVGSGAgkgllSKDALEEDLKVDYLFVGDATPAPQKGV 125
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
7-191 |
7.68e-06 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 47.15 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 7 VEVEKRLLEYMSHSSTTG--NEAAFADVVAKDLEENGWTVYKQ------SIPNSDRYNIYATFRNSDPKHVKVLLnTHLD 78
Cdd:PRK13983 8 IELLSELIAIPAVNPDFGgeGEKEKAEYLESLLKEYGFDEVERydapdpRVIEGVRPNIVAKIPGGDGKRTLWII-SHMD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 79 TVPP---------YFPPTQDEQNIYGNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVGEE------FDHI---- 139
Cdd:PRK13983 87 VVPPgdlslwetdPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEEtgskygIQYLlkkh 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17551016 140 -GMIEANKLEILPEYllvGEPTelkfGTI----QKGALKVKLTVTGQAGHSGYPNSG 191
Cdd:PRK13983 167 pELFKKDDLILVPDA---GNPD----GSFieiaEKSILWLKFTVKGKQCHASTPENG 216
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
8-220 |
1.48e-05 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 46.57 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 8 EVEKRLLEYMSHSSTTGN--EAAFADVVA---KDL---EENGWTVyKQSIPNSD--RYNIYATFRNSDPKHVKVLLNTHL 77
Cdd:cd05654 2 RLEQLLKSLVSWPSVTGTegERSFADFLKeilKELpyfKENPSHV-WQLLPPDDlgRRNVTALVKGKKPSKRTIILISHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 78 DTVP-------------------------PYFPP--TQD---EQNIYGNGSNDAKGQLA---AMVTAATIisktDEDVAR 124
Cdd:cd05654 81 DTVGiedygelkdiafdpdeltkafseyvEELDEevREDllsGEWLFGRGTMDMKSGLAvhlALLEQASE----DEDFDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 125 ALGLLFVVGEEFDHIGMIEA-NKLEILP-----EYLLV--GEPTELKF----------GTIQK---GALkvkltVTGQAG 183
Cdd:cd05654 157 NLLLMAVPDEEVNSRGMRAAvPALLELKkkhdlEYKLAinSEPIFPQYdgdqtryiytGSIGKilpGFL-----CYGKET 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 17551016 184 HSGYPNSGSSAIHKMIEVLHDVQLAKWPCDATNGATT 220
Cdd:cd05654 232 HVGEPFAGINANLMASEITARLELNADLCEKVEGEIT 268
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
106-280 |
1.53e-05 |
|
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: 46.44 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 106 AAMVTAATIISKTDEDVARALGLLFVVGEEfdhIG-----MIEANKLE-----------ILPeYLLVGEpTELKFGTIQK 169
Cdd:cd03886 95 AMLLGAAKLLAERRDPLKGTVRFIFQPAEE---GPggakaMIEEGVLEnpgvdaafglhVWP-GLPVGT-VGVRSGALMA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 170 GALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQ-------LAKWPCdatngatTYNIGKISGGQALNAWAANCE-- 240
Cdd:cd03886 170 SADEFEITVKGKGGHGASPHLGVDPIVAAAQIVLALQtvvsrelDPLEPA-------VVTVGKFHAGTAFNVIPDTAVle 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 17551016 241 -------ADIFFRVVTSVKDIQNQLLALVNGRAEVSLLSFNDPVILD 280
Cdd:cd03886 243 gtirtfdPEVREALEARIKRLAEGIAAAYGATVELEYGYGYPAVIND 289
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
56-136 |
1.18e-04 |
|
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: 42.41 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 56 NIYATFRNSDPKHVkVLLNTHLDTVP---------PYFPPTQDEQNIYGNGSNDAKGQLAAMVTAATIISKTDEDVARAL 126
Cdd:cd03873 1 NLIARLGGGEGGKS-VALGAHLDVVPagegdnrdpPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTI 79
|
90
....*....|
gi 17551016 127 GLLFVVGEEF 136
Cdd:cd03873 80 VVAFTADEEV 89
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
54-193 |
1.98e-04 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 43.01 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 54 RYNIYATFRNSDPKHVKVLLNTHLDTVPP--------YFPP---TQDEQNIYGNGSNDAKGQLAAMVTAA---------- 112
Cdd:cd05674 55 EYGLLYTWEGSDPSLKPLLLMAHQDVVPVnpetedqwTHPPfsgHYDGGYIWGRGALDDKNSLIGILEAVelllkrgfkp 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 113 --TII--SKTDEDV-----ARAL-----------GLLFVVGEefdhiGMIeankleILpEYLLVGEPTELkFGTIQKGAL 172
Cdd:cd05674 135 rrTIIlaFGHDEEVggergAGAIaelllerygvdGLAAILDE-----GGA------VL-EGVFLGVPFAL-PGVAEKGYM 201
|
170 180
....*....|....*....|.
gi 17551016 173 KVKLTVTGQAGHSGYPNSGSS 193
Cdd:cd05674 202 DVEITVHTPGGHSSVPPKHTG 222
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
13-111 |
4.17e-04 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 41.94 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 13 LLEYMSHSSTTGNEAAF---ADVVAKDLEENGWTVykQSIPNSDRYNIYATFRNSDPKhvKVLLNTHLDTVP-------- 81
Cdd:cd05681 5 LRDLLKIPSVSAQGRGIpetADFLKEFLRRLGAEV--EIFETDGNPIVYAEFNSGDAK--TLLFYNHYDVQPaeplelwt 80
|
90 100 110
....*....|....*....|....*....|.
gi 17551016 82 -PYFPPTQDEQNIYGNGSNDAKGQLAAMVTA 111
Cdd:cd05681 81 sDPFELTIRNGKLYARGVADDKGELMARLAA 111
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
103-280 |
1.93e-03 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 39.63 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 103 GQLAAMVTAATIISKTDEDVARALGLLFVVGEEFDHiG---MIEANKLE------------ILPEYLLVGEPtelkfGTI 167
Cdd:cd08019 91 GHTAMLLGAAKILNEIKDTIKGTVKLIFQPAEEVGE-GakqMIEEGVLEdvdavfgihlwsDVPAGKISVEA-----GPR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 168 QKGALKVKLTVTGQAGHSGYPNSGSSAIHKMIEVLHDVQ--LAKwPCDATNGAtTYNIGKISGGQALNAWAANCEADIFF 245
Cdd:cd08019 165 MASADIFKIEVKGKGGHGSMPHQGIDAVLAAASIVMNLQsiVSR-EIDPLEPV-VVTVGKLNSGTRFNVIADEAKIEGTL 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17551016 246 R---------VVTSVKDIQNQLLALVNGRAEVSLLSFNDPVILD 280
Cdd:cd08019 243 RtfnpetrekTPEIIERIAKHTAASYGAEAELTYGAATPPVIND 286
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
42-163 |
2.17e-03 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 39.76 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 42 WTVYKQSIPNSDRYNIYATFRNSDPKhvkVLLNTHLDTVPPY--------FPPTQDEQNIYGNGSNDAKGQLAAMVTAAT 113
Cdd:PRK08554 40 WGIESELIEKDGYYAVYGEIGEGKPK---LLFMAHFDVVPVNpeewntepFKLTVKGDKAYGRGSADDKGNVASVMLALK 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 17551016 114 IISKtdEDVARALGLLFVVGEEF-DHIGMIEANKLE---ILPEYLLVGEPTELK 163
Cdd:PRK08554 117 ELSK--EPLNGKVIFAFTGDEEIgGAMAMHIAEKLReegKLPKYMINADGIGMK 168
|
|
| M28 |
cd02690 |
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ... |
55-148 |
5.51e-03 |
|
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; 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. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases.
Pssm-ID: 349868 [Multi-domain] Cd Length: 202 Bit Score: 37.71 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 55 YNIYATFRNSD-PKHVkVLLNTHLDTVPPyfpptqdeqniyGNGSNDAKGQLAAMVTAATIISKTDEDVARALGLLFVVG 133
Cdd:cd02690 2 YNVIATIKGSDkPDEV-ILIGAHYDSVPL------------SPGANDNASGVAVLLELARVLSKLQLKPKRSIRFAFWDA 68
|
90
....*....|....*.
gi 17551016 134 EEFDHIGMIE-ANKLE 148
Cdd:cd02690 69 EELGLLGSKYyAEQLL 84
|
|
| Iap |
COG2234 |
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ... |
55-140 |
6.99e-03 |
|
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];
Pssm-ID: 441835 [Multi-domain] Cd Length: 257 Bit Score: 37.80 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 55 YNIYATFRNSDPKHVKVLLNTHLDTVPPYFPptqdeqniygnGSND-AKGqLAAMVTAATIISKTDEDVARALGLLFVVG 133
Cdd:COG2234 47 RNVIAEIPGTDPPDEVVVLGAHYDSVGSIGP-----------GADDnASG-VAALLELARALAALGPKPKRTIRFVAFGA 114
|
....*..
gi 17551016 134 EEFDHIG 140
Cdd:COG2234 115 EEQGLLG 121
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
54-206 |
7.36e-03 |
|
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: 38.21 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 54 RYNIYATFRNSDPKHVKVLLNTHLDTVP---------PyFPPTQDEQNIYGNGSNDAKGQLAaMVTAATI-ISKTDEDVA 123
Cdd:cd08012 64 RGNIIVEYPGTVDGKTVSFVGSHMDVVTanpetwefdP-FSLSIDGDKLYGRGTTDCLGHVA-LVTELFRqLATEKPALK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 124 RALGLLFVVGEEFDHIGMI---------EANKLEILPEYLLVGEPTELKFGTIqkGALKVKLTVTGQAGHSGYPNSGSSA 194
Cdd:cd08012 142 RTVVAVFIANEENSEIPGVgvdalvksgLLDNLKSGPLYWVDSADSQPCIGTG--GMVTWKLTATGKLFHSGLPHKAINA 219
|
170
....*....|..
gi 17551016 195 IHKMIEVLHDVQ 206
Cdd:cd08012 220 LELVMEALAEIQ 231
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
102-337 |
8.90e-03 |
|
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: 37.61 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 102 KGQLAAMVTAATIISKTDEDVAralgllFVVGEEFDHI-GMIEANKLEILPEYLLVGEPTELKFGTIQKGAlKVKLTVTG 180
Cdd:cd03888 178 KGIVTVDLTFKIDDDKGYRLIS------IKGGEATNMVpDKAEAVIPGKDKEELALSAATDLKGNIEIDDG-GVELTVTG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 181 QAGHSGYPNSGSSAIHKMIEVLHDVQ-----------LAKWPCDATN-------------GATTYNIGKISggqaLNAWA 236
Cdd:cd03888 251 KSAHASAPEKGVNAITLLAKFLAELNkdgndkdfikfLAKNLHEDYNgkklginfedevmGELTLNPGIIT----LDDGK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551016 237 ANCEADIFFRVVTSVKDIQNQLLALVnGRAEVSLLSFNDPVILDVPPieaelDHVSFNTDI-AYFDARDKVKAKYLFGGG 315
Cdd:cd03888 327 LELGLNVRYPVGTSAEDIIKQIEEAL-EKYGVEVEGHKHQKPLYVPK-----DSPLVKTLLkVYEEQTGKEGEPVAIGGG 400
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 17551016 316 S----IKN--------------AHSKNEFIPKDELHKCTA 337
Cdd:cd03888 401 TyareLPNgvafgpefpgqkdtMHQANEFIPIDDLIKALA 440
|
|
| |
