|
Name |
Accession |
Description |
Interval |
E-value |
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
3-394 |
0e+00 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 710.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 3 EDIGVTRFREYLRVNTEQPKPDYEACRDFLFKYADELGIERRSVETAPGTYFVIMTIPGSKPDLPSIMLYSHTDVVPTFR 82
Cdd:cd05646 1 EDPAVTRFREYLRINTVHPNPDYDACVEFLKRQADELGLPVRVIEVVPGKPVVVLTWEGSNPELPSILLNSHTDVVPVFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 83 EYWTHDPYSAFKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVKqWTRTIHIVWGPDEEIGHINGMKGFAVTEEFKKL 162
Cdd:cd05646 81 EKWTHDPFSAHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFK-PKRTIHLSFVPDEEIGGHDGMEKFVKTEEFKKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 163 NIDFALDEGIATEDDVYKIFYAERIPWWVKVTLPGHPGHGSKFIEKTAIEKLHKLIASVDEFRNEQKSLLAEHPEWTVGD 242
Cdd:cd05646 160 NVGFALDEGLASPTEEYRVFYGERSPWWVVITAPGTPGHGSKLLENTAGEKLRKVIESIMEFRESQKQRLKSNPNLTLGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 243 VTTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAGEGVTYEFMQFSNFKLISPNTREDPFWAAI 322
Cdd:cd05646 240 VTTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGRGVTYEFEQKSPEKDPTSLDDSNPWWAAF 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71982082 323 DDALQKEGCKYKKEIFIGATDSRFVRAQGIRAIGFSPIINTPSLLHDHNEFLNEKTFLRGVEIYETLINKLA 394
Cdd:cd05646 320 KKAVKEMGLKLKPEIFPAATDSRYIRALGIPALGFSPMNNTPILLHDHNEFLNEDVFLRGIEIYEKIIPALA 391
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
3-396 |
0e+00 |
|
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: 616.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 3 EDIGVTRFREYLRVNTEQPKPDYEACRDFLFKYADELGIERRSVETAPGTYFVIMTIPGSKPDLPSIMLYSHTDVVPTFR 82
Cdd:TIGR01880 8 EDIAVTRFREYLRINTVQPNPDYAACVDFLIKQADELGLARKTIEFVPGKPVVVLTWPGSNPELPSILLNSHTDVVPVFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 83 EYWTHDPYSAFKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGvKQWTRTIHIVWGPDEEIGHINGMKGFAVTEEFKKL 162
Cdd:TIGR01880 88 EHWTHPPFSAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASG-FKFKRTIHISFVPDEEIGGHDGMEKFAKTDEFKAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 163 NIDFALDEGIATEDDVYKIFYAERIPWWVKVTLPGHPGHGSKFIEKTAIEKLHKLIASVDEFRNEQKSLLAEHPEWTVGD 242
Cdd:TIGR01880 167 NLGFALDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKLMENTAMEKLEKSVESIRRFRESQFQLLQSNPDLAIGD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 243 VTTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAGEGVTYEFMQFSNFKLISPNTREDPFWAAI 322
Cdd:TIGR01880 247 VTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAGEGVTYEFSQHSGKPLVTPHDDSNPWWVAF 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71982082 323 DDALQKEGCKYKKEIFIGATDSRFVRAQGIRAIGFSPIINTPSLLHDHNEFLNEKTFLRGVEIYETLINKLANV 396
Cdd:TIGR01880 327 KDAVKEMGCTFKPEILPGSTDSRYIRAAGVPALGFSPMNNTPVLLHDHNEFLNEAVFLRGIEIYQTLISALASV 400
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
7-394 |
9.52e-65 |
|
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: 211.67 E-value: 9.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 7 VTRFREYLRVNTEQPkpDYEACRDFLFKYADELGIERRSVETAPGTYFVIMTIPGSKPDlPSIMLYSHTDVVPT-FREYW 85
Cdd:COG0624 15 LELLRELVRIPSVSG--EEAAAAELLAELLEALGFEVERLEVPPGRPNLVARRPGDGGG-PTLLLYGHLDVVPPgDLELW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 86 THDPYSAfKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVKQwTRTIHIVWGPDEEIGHiNGMKGFaVTEEFKKLNID 165
Cdd:COG0624 92 TSDPFEP-TIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRL-PGNVTLLFTGDEEVGS-PGARAL-VEELAEGLKAD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 166 FALD-EGiateDDVYKIFYAERIPWWVKVTLPGHPGHGSKFIE-KTAIEKLHKLIASVDEFRNEqkslLAEHPEWtvgDV 243
Cdd:COG0624 168 AAIVgEP----TGVPTIVTGHKGSLRFELTVRGKAAHSSRPELgVNAIEALARALAALRDLEFD----GRADPLF---GR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 244 TTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAGEGVTYEFMQFSNFkLISPNTRED-PFWAAI 322
Cdd:COG0624 237 TTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEVEVLGDG-RPPFETPPDsPLVAAA 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71982082 323 DDALQKE-GCKYKKEIFIGATDSRFVRAQ-GIRAIGFSPIinTPSLLHDHNEFLNEKTFLRGVEIYETLINKLA 394
Cdd:COG0624 316 RAAIREVtGKEPVLSGVGGGTDARFFAEAlGIPTVVFGPG--DGAGAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
70-392 |
3.60e-60 |
|
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 197.57 E-value: 3.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 70 MLYSHTDVVPTfrEYWTHDPYSAfkDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVKQwtRTIHIVWGPDEEIGHiNG 149
Cdd:pfam01546 1 LLRGHMDVVPD--EETWGWPFKS--TEDGKLYGRGHDDMKGGLLAALEALRALKEEGLKK--GTVKLLFQPDEEGGM-GG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 150 MKGFAVTEEFKKLNIDFAL-----DEGIATEDDVYKIFYAERIPWWVKVTLPGHPGHGSKF-IEKTAIEKLHKLIASVDE 223
Cdd:pfam01546 74 ARALIEDGLLEREKVDAVFglhigEPTLLEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPhLGVNAIVAAARLILALQD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 224 FRNEQKSLLAEHPewtvgdVTTSNITIINGGVqvNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAGE--GVTYEFM 301
Cdd:pfam01546 154 IVSRNVDPLDPAV------VTVGNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAayGVKVEVE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 302 QFSNFKliSPNTREDPFWAAIDDALQKE-GCKYKKEI--FIGATDSRFVrAQGIRAIGFSpIINTPSLLHDHNEFLNEKT 378
Cdd:pfam01546 226 YVEGGA--PPLVNDSPLVAALREAAKELfGLKVELIVsgSMGGTDAAFF-LLGVPPTVVF-FGPGSGLAHSPNEYVDLDD 301
|
330
....*....|....
gi 71982082 379 FLRGVEIYETLINK 392
Cdd:pfam01546 302 LEKGAKVLARLLLK 315
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
7-390 |
2.63e-46 |
|
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: 164.07 E-value: 2.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 7 VTRFREYLRVNTEQPKPDYEACR---DFLFKYADELGIERRS--VETAPGTYFVIMTIPGSKPDLPSIMLYSHTDVVPTF 81
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTGSETraaEVLAARLAEAGIQTEIfvVESHPGRANLVARIGGTDPSAGPLLLLGHIDVVPAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 82 REYWTHDPYSAfKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVKQwTRTIHIVWGPDEEIGHINGMKgFAVtEEFKK 161
Cdd:cd05675 81 ASDWSVDPFSG-EIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKP-KRDLVFAFVADEEAGGENGAK-WLV-DNHPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 162 L--NIDFALDE-GIATEDDV-----YKIFYAERIPWWVKVTLPGHPGHGS-------------------KFIEKTAIEKL 214
Cdd:cd05675 157 LfdGATFALNEgGGGSLPVGkgrrlYPIQVAEKGIAWMKLTVRGRAGHGSrptddnaitrlaealrrlgAHNFPVRLTDE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 215 HKLIASVDEFRNEQKSLLAEHPEWTVGDV----------------TTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDL 278
Cdd:cd05675 237 TAYFAQMAELAGGEGGALMLTAVPVLDPAlaklgpsapllnamlrNTASPTMLDAGYATNVLPGRATAEVDCRILPGQSE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 279 DAVLARVDqwaKEAGE-GVTYEFmQFSNFKLISPNTreDPFWAAIDDALQKE--GCKYKKEIFIGATDSRFVRAQGIRAI 355
Cdd:cd05675 317 EEVLDTLD---KLLGDpDVSVEA-VHLEPATESPLD--SPLVDAMEAAVQAVdpGAPVVPYMSPGGTDAKYFRRLGIPGY 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 71982082 356 GFSPIINTP-----SLLHDHNEFLNEKTFLRGVEIYETLI 390
Cdd:cd05675 391 GFAPLFLPPeldytGLFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
11-385 |
1.54e-45 |
|
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: 160.64 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 11 REYLRVNTEQP-KPDYEACRDFLFKYADELGIERRSVETAPG----TYFVIMTIPGSKPDlPSIMLYSHTDVVPT-FREY 84
Cdd:TIGR01910 5 KDLISIPSVNPpGGNEETIANYIKDLLREFGFSTDVIEITDDrlkvLGKVVVKEPGNGNE-KSLIFNGHYDVVPAgDLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 85 WTHDPYSAfKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVKQwTRTIHIVWGPDEEIGhinGMKGFAVTEEFKKLNI 164
Cdd:TIGR01910 84 WKTDPFKP-VEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKP-NGNIILQSVVDEESG---EAGTLYLLQRGYFKDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 165 DFALdegIATEDDVYKIFYAERIPWWVKVTLPGHPGHGSkFIEKT--AIEKLHKLIASVDEFrneQKSLLAEHPEWTVGD 242
Cdd:TIGR01910 159 DGVL---IPEPSGGDNIVIGHKGSIWFKLRVKGKQAHAS-FPQFGvnAIMKLAKLITELNEL---EEHIYARNSYGFIPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 243 VTTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAG--EGVTYEFMQFSNFKLISPNTREDPFWA 320
Cdd:TIGR01910 232 PITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSksDGWLYENEPVVKWSGPNETPPDSRLVK 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71982082 321 AIDDALQK-EGCKYKKEIFIGATDSRFVRAQGIRAIGFSPIINtpSLLHDHNEFLNEKTFLRGVEI 385
Cdd:TIGR01910 312 ALEAIIKKvRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPGDL--ETAHQVNEYISIKNLVESTKV 375
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-390 |
7.30e-44 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 156.01 E-value: 7.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 7 VTRFREYLRVNTEQPKPD-YEACRDFLFKYADELGIERRSVETAPGTYFVIMTIPGSKPDlPSIMLYSHTDVVPTFR-EY 84
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDnTSAIAAYIKLLLEDLGYPVELHEPPEEIYGVVSNIVGGRKG-KRLLFNGHYDVVPAGDgEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 85 WTHDPYSAfKDEDGNIFARGAQDMKCVGVQYMEALRnWFAKGVKQWTRTIHIVWGPDEEIGHINGMKgfAVTEefkklNI 164
Cdd:cd08011 80 WTVDPYSG-KIKDGKLYGRGSSDMKGGIAASIIAVA-RLADAKAPWDLPVVLTFVPDEETGGRAGTK--YLLE-----KV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 165 DFALDEGIATEDD-VYKIFYAERIPWWVKVTLPGHPGHGSKF-IEKTAIEKLHKLIasvDEFRNEQKSLlaehpewtvgd 242
Cdd:cd08011 151 RIKPNDVLIGEPSgSDNIRIGEKGLVWVIIEITGKPAHGSLPhRGESAVKAAMKLI---ERLYELEKTV----------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 243 vttsNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQwAKEAGEGVTYEFMQFSNFKLISPNtreDPFWAAI 322
Cdd:cd08011 217 ----NPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIID-HLDSIEEVSFEIKSFYSPTVSNPD---SEIVKKT 288
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71982082 323 DDALQK-EGCKYKKEIFIGATDSRFVRAQGIRAIGFSPiiNTPSLLHDHNEFLNEKTFLRGVEIYETLI 390
Cdd:cd08011 289 EEAITEvLGIRPKEVISVGASDARFYRNAGIPAIVYGP--GRLGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
23-390 |
4.49e-41 |
|
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: 148.60 E-value: 4.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 23 PDYEACRDFLFKYADELG--IERRSVEtapGTYFVIMTIPGSKPdlPSIMLYSHTDVVPTFREY-WTHDPYSAfKDEDGN 99
Cdd:cd08659 14 PPEAEVAEYLAELLAKRGygIESTIVE---GRGNLVATVGGGDG--PVLLLNGHIDTVPPGDGDkWSFPPFSG-RIRDGR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 100 IFARGAQDMK---CVGVQYMEALRnwfAKGVKQwTRTIHIVWGPDEEIGHiNGMKgfAVTEEFKKLNIDFALDeGIATED 176
Cdd:cd08659 88 LYGRGACDMKgglAAMVAALIELK---EAGALL-GGRVALLATVDEEVGS-DGAR--ALLEAGYADRLDALIV-GEPTGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 177 DVYkifYAERIPWWVKVTLPGHPGHGS-KFIEKTAIEKLHKLIASVDEFRNEqkslLAEHPEwtVGDvTTSNITIINGGV 255
Cdd:cd08659 160 DVV---YAHKGSLWLRVTVHGKAAHSSmPELGVNAIYALADFLAELRTLFEE----LPAHPL--LGP-PTLNVGVINGGT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 256 QVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAGEGVTYEF-MQFSNFKLISPNtreDPFWAAIDDALQKEGCKYK 334
Cdd:cd08659 230 QVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVsLDGDPPFFTDPD---HPLVQALQAAARALGGDPV 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 71982082 335 KEIFIGATDSR-FVRAQGIRAIGFSPiiNTPSLLHDHNEFLNEKTFLRGVEIYETLI 390
Cdd:cd08659 307 VRPFTGTTDASyFAKDLGFPVVVYGP--GDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
51-394 |
4.25e-38 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 143.16 E-value: 4.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 51 GTYFVIMTIPGSKPDLPSIMLYSHTDVVP---TFREYWTHDPYSAfKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGV 127
Cdd:PRK08262 96 GGHSLLYTWKGSDPSLKPIVLMAHQDVVPvapGTEGDWTHPPFSG-VIADGYVWGRGALDDKGSLVAILEAAEALLAQGF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 128 kQWTRTIHIVWGPDEEIGhinGMKGFAVTEEFKKLNI--DFALDEGIATEDDVYK--------IFYAERIPWWVKVTLPG 197
Cdd:PRK08262 175 -QPRRTIYLAFGHDEEVG---GLGARAIAELLKERGVrlAFVLDEGGAITEGVLPgvkkpvalIGVAEKGYATLELTARA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 198 HPGHGSKFIEKTAIEKLHKLIASVD---------------------EFRNEQKSLLAEhpEWTVGDV------------- 243
Cdd:PRK08262 251 TGGHSSMPPRQTAIGRLARALTRLEdnplpmrlrgpvaemfdtlapEMSFAQRVVLAN--LWLFEPLllrvlakspetaa 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 244 ---TTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAkeAGEGVTYE-FMQFSNFKLISPntREDPFW 319
Cdd:PRK08262 329 mlrTTTAPTMLKGSPKDNVLPQRATATVNFRILPGDSVESVLAHVRRAV--ADDRVEIEvLGGNSEPSPVSS--TDSAAY 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 320 AAIDDALqkegckykKEIF----------IGATDSRFvrAQGI--RAIGFSPIINTP---SLLHDHNEFLNEKTFLRGVE 384
Cdd:PRK08262 405 KLLAATI--------REVFpdvvvapylvVGATDSRH--YSGIsdNVYRFSPLRLSPedlARFHGTNERISVANYARMIR 474
|
410
....*....|
gi 71982082 385 IYETLINKLA 394
Cdd:PRK08262 475 FYYRLIENAA 484
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
1-394 |
5.33e-37 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 138.20 E-value: 5.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 1 MSEDIgVTRFREYLRVNTEQPKP-DYEACRDFLFKYADELGIERRSVEtAPGTY------FVIMTIPGSKPDLPSIMLYS 73
Cdd:PRK08651 4 MMFDI-VEFLKDLIKIPTVNPPGeNYEEIAEFLRDTLEELGFSTEIIE-VPNEYvkkhdgPRPNLIARRGSGNPHLHFNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 74 HTDVVPTFREYWTHDPYSAFKDeDGNIFARGAQDMKCVGVQYMEALRNWFAKGVKQWTRTIhivwGPDEEIGhinGMKGF 153
Cdd:PRK08651 82 HYDVVPPGEGWSVNVPFEPKVK-DGKVYGRGASDMKGGIAALLAAFERLDPAGDGNIELAI----VPDEETG---GTGTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 154 AVTEEfkklnIDFALDEGIATED-DVYKIFYAERIPWWVKVTLPGHPGHGSK-FIEKTAIEKLHKLIASVDEFRNEQKSL 231
Cdd:PRK08651 154 YLVEE-----GKVTPDYVIVGEPsGLDNICIGHRGLVWGVVKVYGKQAHASTpWLGINAFEAAAKIAERLKSSLSTIKSK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 232 L------AEHPEWTVGDVTtsnitiINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLAR----VDQWAKEAGEGVTYEFM 301
Cdd:PRK08651 229 YeydderGAKPTVTLGGPT------VEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDElealLDEVAPELGIEVEFEIT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 302 QFSNFKLISPNtreDPFWAAIDDAL-QKEGCKYKKEIFIGATDSRFVRAQGIRAIGFSPIinTPSLLHDHNEFLNEKTFL 380
Cdd:PRK08651 303 PFSEAFVTDPD---SELVKALREAIrEVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPG--ELELAHAPDEYVEVKDVE 377
|
410
....*....|....
gi 71982082 381 RGVEIYETLINKLA 394
Cdd:PRK08651 378 KAAKVYEEVLKRLA 391
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
51-391 |
1.81e-34 |
|
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: 132.76 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 51 GTYFVIMTIPGSKPDLPSIMLYSHTDVVP---TFREYWTHDPYSAFKDeDGNIFARGAQDMKCVGVQYMEALRNWFAKGV 127
Cdd:cd05674 54 NEYGLLYTWEGSDPSLKPLLLMAHQDVVPvnpETEDQWTHPPFSGHYD-GGYIWGRGALDDKNSLIGILEAVELLLKRGF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 128 KQwTRTIHIVWGPDEEIGHINGmKGFAVTEEFKKLNID---FALDEGIATEDDVYKIFY------AER--IPWWVKVTLP 196
Cdd:cd05674 133 KP-RRTIILAFGHDEEVGGERG-AGAIAELLLERYGVDglaAILDEGGAVLEGVFLGVPfalpgvAEKgyMDVEITVHTP 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 197 GhpGHGSKFIEKTAIEKLHKLIASVDE--------FRNEQKSLL---AEHP------------------------EWTVG 241
Cdd:cd05674 211 G--GHSSVPPKHTGIGILSEAVAALEAnpfppkltPGNPYYGMLqclAEHSplpprslksnlwlaspllkallasELLST 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 242 DV-------TTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARV----DQWAKEAGEGVTYE----------- 299
Cdd:cd05674 289 SPltrallrTTQAVDIINGGVKINALPETATATVNHRIAPGSSVEEVLEHVknliADIAVKYGLGLSAFggdviystngt 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 300 --FMQFSNFKLISPNTREDPFWAAIDDALQKEGCKYKKE------IFIGATDSRFVRA--QGI-RaigFSPIINTPSLL- 367
Cdd:cd05674 369 klLTSLLSPEPSPVSSTSSPVWQLLAGTIRQVFEQFGEDlvvapgIMTGNTDTRHYWNltKNIyR---FTPIRLNPEDLg 445
|
410 420
....*....|....*....|....*.
gi 71982082 368 --HDHNEFLNEKTFLRGVEIYETLIN 391
Cdd:cd05674 446 riHGVNERISIDDYLETVAFYYQLIQ 471
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
37-359 |
3.10e-31 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 123.04 E-value: 3.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 37 DELGIERRSVETAPGTYFVIMTIPGSKPDLPSIMLYSHTDVVPTFREYWTHDPYSAfKDEDGNIFARGAQDMKCVGVQYM 116
Cdd:PRK07906 36 AEVGLEPTYLESAPGRANVVARLPGADPSRPALLVHGHLDVVPAEAADWSVHPFSG-EIRDGYVWGRGAVDMKDMDAMML 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 117 EALRNWFAKGVKQwTRTIHIVWGPDEEIGhinGMKG-----------FA-VTEefkklnidfALDEG------IATEDDV 178
Cdd:PRK07906 115 AVVRHLARTGRRP-PRDLVFAFVADEEAG---GTYGahwlvdnhpelFEgVTE---------AISEVggfsltVPGRDRL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 179 YKIFYAERIPWWVKVTLPGHPGHGSKFIEKTAIEKL---------HK----LIASVDEFRNEQKSLL-----AEHPEWTV 240
Cdd:PRK07906 182 YLIETAEKGLAWMRLTARGRAGHGSMVNDDNAVTRLaeavarigrHRwplvLTPTVRAFLDGVAELTglefdPDDPDALL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 241 ---GDV---------TTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDlDAVLARVDQWakeAGEGVTYEFMQfsnfKL 308
Cdd:PRK07906 262 aklGPAarmvgatlrNTANPTMLKAGYKVNVIPGTAEAVVDGRFLPGRE-EEFLATVDEL---LGPDVEREWVH----RD 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 71982082 309 ISPNTRED-PFWAAIDDALQKE--GCKYKKEIFIGATDSRFVRAQGIRAIGFSP 359
Cdd:PRK07906 334 PALETPFDgPLVDAMNAALLAEdpGARVVPYMLSGGTDAKAFSRLGIRCYGFAP 387
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
30-391 |
1.04e-26 |
|
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: 109.60 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 30 DFLFKYADELGIERRSVETAPGTYF-VIMTIPGSkpDLPSIMLYSHTDVVPTFREYWTHDPYSAfKDEDGNIFARGAQDM 108
Cdd:cd03894 22 EYVADYLAALGVKSRRVPVPEGGKAnLLATLGPG--GEGGLLLSGHTDVVPVDGQKWSSDPFTL-TERDGRLYGRGTCDM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 109 K----CVgvqyMEALRNWFAKGVKqwtRTIHIVWGPDEEIGHInGMKGFAVTEEFKKLNIDFALdegIA--TEDDVY--- 179
Cdd:cd03894 99 KgflaAV----LAAVPRLLAAKLR---KPLHLAFSYDEEVGCL-GVRHLIAALAARGGRPDAAI---VGepTSLQPVvah 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 180 KIFYAeripWWVKVTlpGHPGHGS-KFIEKTAIEKLHKLIASVDEFRNEQKSLLAEHPeWTVGdVTTSNITIINGGVQVN 258
Cdd:cd03894 168 KGIAS----YRIRVR--GRAAHSSlPPLGVNAIEAAARLIGKLRELADRLAPGLRDPP-FDPP-YPTLNVGLIHGGNAVN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 259 VVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAGEgvtyefmQFSNFKLISPNTREDPFWAAIDDALQKEGCK----YK 334
Cdd:cd03894 240 IVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLE-------FPEAGIEVEPLFEVPGLETDEDAPLVRLAAAlagdNK 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 71982082 335 KEIFIGATDSRFVRAQGIRAIGFSPiintPSLLHDH--NEFLNEKTFLRGVEIYETLIN 391
Cdd:cd03894 313 VRTVAYGTEAGLFQRAGIPTVVCGP----GSIAQAHtpDEFVELEQLDRCEEFLRRLIA 367
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
50-395 |
2.18e-21 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 95.45 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 50 PGTYFVIMTIPGSKPDLPsIMLYSHTDVVPTFREYWTHDPYSaFKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVKQ 129
Cdd:PRK09133 86 PRKGNLVARLRGTDPKKP-ILLLAHMDVVEAKREDWTRDPFK-LVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 130 wTRTIHIVWGPDEEIGHINGmkGFAVTEEFKKL-NIDFALDEGIA--TEDDVYKIFY----AERIP--WWVKVTLPGhpG 200
Cdd:PRK09133 164 -KRDIILALTGDEEGTPMNG--VAWLAENHRDLiDAEFALNEGGGgtLDEDGKPVLLtvqaGEKTYadFRLEVTNPG--G 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 201 HGSKFIEKTAIEKL---------HKLIASVDE-----FRNEQK-----------------------SLLAEHPEWtVGDV 243
Cdd:PRK09133 239 HSSRPTKDNAIYRLaaalsrlaaYRFPVMLNDvtrayFKQSAAietgplaaamrafaanpadeaaiALLSADPSY-NAML 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 244 -TTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAGEGVTYEfmqfsNFKLISPNTREDP-FWAA 321
Cdd:PRK09133 318 rTTCVATMLEGGHAENALPQRATANVNCRIFPGDTIEAVRATLKQVVADPAIKITRI-----GDPSPSPASPLRPdIMKA 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 322 IDDALQKegcKYKKEIFI-----GATDSRFVRAQGIRAIGFSPIINTPSLLHDHNefLNEKT----FLRGVEIYETLINK 392
Cdd:PRK09133 393 VEKLTAA---MWPGVPVIpsmstGATDGRYLRAAGIPTYGVSGLFGDPDDTFAHG--LNERIpvasFYEGRDFLYELVKD 467
|
...
gi 71982082 393 LAN 395
Cdd:PRK09133 468 LAG 470
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
37-373 |
1.04e-17 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 84.05 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 37 DELGIERRSVetapgtyfvIMTIPGSKPDLPSIMlySHTDVVPTFR-EYWTHDPYSAfKDEDGNIFARGAQDMKCVGVQY 115
Cdd:cd05650 51 DERGIIRPNI---------VAKIPGGNDKTLWII--SHLDTVPPGDlSLWETDPWEP-VVKDGKIYGRGVEDNQQGIVSS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 116 MEALRNWFAKGVKQwTRTIHIVWGPDEEIGHINGMKGFAVTEE-FKKLNIDFALDEGiaTEDDVYkIFYAERIPWWVKVT 194
Cdd:cd05650 119 LLALKAIIKNGITP-KYNFGLLFVADEEDGSEYGIQYLLNKFDlFKKDDLIIVPDFG--TEDGEF-IEIAEKSILWIKVN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 195 LPGHPGHGSKFIE-KTAIEKLHKLIASVDEFRNEQKSLLAE--HPEWTVGDVTTSNITIINggvqVNVVPEKFEAYIDIR 271
Cdd:cd05650 195 VKGKQCHASTPENgINAFVAASNFALELDELLHEKFDEKDDlfNPPYSTFEPTKKEANVPN----VNTIPGYDVFYFDCR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 272 VTPLQDLDAVLARVDQWAKEA----GEGVTYEFMQFSNfklISPNTREDP-FWAAIDDALQKEGCKYKKEIFI-GATDSR 345
Cdd:cd05650 271 VLPTYKLDEVLKFVNKIISDFensyGAGITYEIVQKEQ---APPATPEDSeIVVRLSKAIKKVRGREAKLIGIgGGTVAA 347
|
330 340
....*....|....*....|....*...
gi 71982082 346 FVRAQGIRAIGFSPIINTPsllHDHNEF 373
Cdd:cd05650 348 FLRKKGYPAVVWSTLDETA---HQPNEY 372
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
40-390 |
2.63e-17 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 82.62 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 40 GIERRSVETAPGTYFVIMTIPGSKPDLPsimLYSHTDVV-PTFREYWTHDPYSAfKDEDGNIFARGAQDMKCvGVQYME- 117
Cdd:PRK08588 36 GIESKIVKVNDGRANLVAEIGSGSPVLA---LSGHMDVVaAGDVDKWTYDPFEL-TEKDGKLYGRGATDMKS-GLAALVi 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 118 ALRNWFAKGVKQwTRTIHIVWGPDEEIGHInGMKGFAvteefkklnidfalDEGIAteDDV----------YKIFYAERI 187
Cdd:PRK08588 111 AMIELKEQGQLL-NGTIRLLATAGEEVGEL-GAKQLT--------------EKGYA--DDLdaliigepsgHGIVYAHKG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 188 PWWVKVTLPGHPGHGS-KFIEKTAIEKLHKLIasvdefrNEQKSLLAEHPEWT--VGDvTTSNITIINGGVQVNVVPEKF 264
Cdd:PRK08588 173 SMDYKVTSTGKAAHSSmPELGVNAIDPLLEFY-------NEQKEYFDSIKKHNpyLGG-LTHVVTIINGGEQVNSVPDEA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 265 EAYIDIRVTPLQDLDAVLARVDQWAKE--AGEGVTYEFMQFSNFKLISpNTREDPFWAAIDDALQKE-GCKYKKEIFIGA 341
Cdd:PRK08588 245 ELEFNIRTIPEYDNDQVISLLQEIINEvnQNGAAQLSLDIYSNHRPVA-SDKDSKLVQLAKDVAKSYvGQDIPLSAIPGA 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 71982082 342 TD-SRFVRA-QGIRAIGFSPIINTPSllHDHNEFLNEKTFLRGVEIYETLI 390
Cdd:PRK08588 324 TDaSSFLKKkPDFPVIIFGPGNNLTA--HQVDEYVEKDMYLKFIDIYKEII 372
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
61-182 |
6.99e-17 |
|
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: 78.24 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 61 GSKPDLPSIMLYSHTDVVPTFREYWTHDPYSAFKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVKQwTRTIHIVWGP 140
Cdd:cd18669 7 GGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKL-KGTVVVAFTP 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 71982082 141 DEEIGHINGMKGFAVTEEFKKLNIDFAL--------DEGIATEDDVYKIF 182
Cdd:cd18669 86 DEEVGSGAGKGLLSKDALEEDLKVDYLFvgdatpapQKGVGIRTPLVDAL 135
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
189-297 |
8.22e-17 |
|
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: 75.46 E-value: 8.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 189 WWVKVTLPGHPGHGS-KFIEKTAIEKLHKLIASVDEFRNEQKSLLAEhpewtvgdvTTSNITIINGGVQVNVVPEKFEAY 267
Cdd:pfam07687 7 AGGHLTVKGKAGHSGaPGKGVNAIKLLARLLAELPAEYGDIGFDFPR---------TTLNITGIEGGTATNVIPAEAEAK 77
|
90 100 110
....*....|....*....|....*....|
gi 71982082 268 IDIRVTPLQDLDAVLARVDQWAKEAGEGVT 297
Cdd:pfam07687 78 FDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
55-190 |
8.72e-17 |
|
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: 78.24 E-value: 8.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 55 VIMTIPGSkPDLPSIMLYSHTDVVPTFREYWTHDPYSAFKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVKQwTRTI 134
Cdd:cd03873 2 LIARLGGG-EGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKP-KGTI 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 71982082 135 HIVWGPDEEIGHINGMKGFAVTEEFKKLNIDFALdEGIATEDDVYKIFYAERIPWW 190
Cdd:cd03873 80 VVAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAF-VIDATAGPILQKGVVIRNPLV 134
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
9-308 |
3.07e-16 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 79.32 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 9 RFREYLRVNT---EQpkpdyEACRDFLFKYADELGIERRSVETApgtyFVIMTIPGSKP-DLPSIMLYSHTDVVPTFrey 84
Cdd:COG2195 8 RFLEYVKIPTpsdHE-----EALADYLVEELKELGLEVEEDEAG----NVIATLPATPGyNVPTIGLQAHMDTVPQF--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 85 wTHDPYSAFKDeDGNIFAR-----GAQDMkcVGVQY-MEALRNWFAKGVKqwTRTIHIVWGPDEEIGhINGMKGFavteE 158
Cdd:COG2195 76 -PGDGIKPQID-GGLITADgtttlGADDK--AGVAAiLAALEYLKEPEIP--HGPIEVLFTPDEEIG-LRGAKAL----D 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 159 FKKLNIDFA--LDegiaTEDD---VYKIFYAERIpwwvKVTL---PGHPGhgskfiekTAIEKL---HKLIAsvdEFrne 227
Cdd:COG2195 145 VSKLGADFAytLD----GGEEgelEYECAGAADA----KITIkgkGGHSG--------DAKEKMinaIKLAA---RF--- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 228 qkslLAEHPEWTVGDVTTSNITIINGGVQVNVVPEKFEAYIDIRvtpLQDLDAVLARVDQW-------AKEAGEG-VTYE 299
Cdd:COG2195 203 ----LAALPLGRIPEETEGNEGFIHGGSATNAIPREAEAVYIIR---DHDREKLEARKAELeeafeeeNAKYGVGvVEVE 275
|
330
....*....|
gi 71982082 300 F-MQFSNFKL 308
Cdd:COG2195 276 IeDQYPNWKP 285
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
68-375 |
9.52e-16 |
|
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: 78.12 E-value: 9.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 68 SIMLYSHTDVVPT-FREYWTHDPYSAfKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVkQWTRTIHIVWGPDEEIGH 146
Cdd:cd03895 76 SLILNGHIDVVPEgPVELWTRPPFEA-TIVDGWMYGRGAGDMKAGLAANLFALDALRAAGL-QPAADVHFQSVVEEECTG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 147 iNG-----MKGFAVteefkklnidfalDEGIATEDDVYKIFYAERIPWWVKVTLPGHPGHGSKFIEKT-AIEKLHKLIAS 220
Cdd:cd03895 154 -NGalaalMRGYRA-------------DAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVnAIEKAMHLIQA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 221 VDEFRNEQKSLLAEHPEWtvGDVTTS---NITIINGGVQVNVVPEkfEAYIDIRVT--PLQDLDAVLARVDQWAKEA--- 292
Cdd:cd03895 220 LQELEREWNARKKSHPHF--SDHPHPinfNIGKIEGGDWPSSVPA--WCVLDCRIGiyPGESPEEARREIEECVADAaat 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 293 -----GEGVTYEFMQFSnfklISPNTRED--PFWAAIDDALQK-EGCKYKKEIFIGATDSR-FVRAQGIRAIGFSPIINT 363
Cdd:cd03895 296 dpwlsNHPPEVEWNGFQ----AEGYVLEPgsDAEQVLAAAHQAvFGTPPVQSAMTATTDGRfFVLYGDIPALCYGPGSRD 371
|
330
....*....|..
gi 71982082 364 PsllHDHNEFLN 375
Cdd:cd03895 372 A---HGFDESVD 380
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
64-275 |
4.03e-15 |
|
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: 75.81 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 64 PDLPSIMLYSHTDVVPTFREyWTHDPYSAfKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVKQWTrtIHIVWGPDEE 143
Cdd:cd05651 53 EGKPTLLLNSHHDTVKPNAG-WTKDPFEP-VEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGPLNYN--LIYAASAEEE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 144 IGHINGMKgfAVTEEFKKlnIDFAldegIATEDDVYKIFYAERIPWWVKVTLPGHPGHGSKFIEKTAIEKLHKLIASVDE 223
Cdd:cd05651 129 ISGKNGIE--SLLPHLPP--LDLA----IVGEPTEMQPAIAEKGLLVLDCTARGKAGHAARNEGDNAIYKALDDIQWLRD 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 71982082 224 FRNEQKSLLaehpewtVGDVTTSnITIINGGVQVNVVPEKFEAYIDIRVTPL 275
Cdd:cd05651 201 FRFDKVSPL-------LGPVKMT-VTQINAGTQHNVVPDSCTFVVDIRTTEA 244
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
74-390 |
2.70e-14 |
|
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: 73.69 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 74 HTDVVPT-FREYWTHDPYSAfKDEDGNIFARGAQDMKCvGVQYMEALRNWFAKGVKQWTRTIHIVWGPDEEIGHINGMKg 152
Cdd:cd03891 62 HTDVVPPgDLEGWSSDPFSP-TIKDGMLYGRGAADMKG-GIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTK- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 153 fAVTEEFKKLN--IDFAL-DEGIATED--DVYKIfyAERIPWWVKVTLPGHPGHgSKFIEKtAIEKLHKLIASVDEFRNE 227
Cdd:cd03891 139 -KVLEWLKARGekIDYCIvGEPTSEKKlgDTIKI--GRRGSLNGKLTIKGKQGH-VAYPHL-ADNPIHLLAPILAELTAT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 228 QksllaehpeWTVGDV----TTSNITIINGGVQV-NVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAGEGVTYEFMQ 302
Cdd:cd03891 214 V---------LDEGNEffppSSLQITNIDVGNGAtNVIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 303 FSNFKLispnTREDPFWAAIDDALQKEgCKYKKEIFI--GATDSRFVRAQGIRAIGFSPIINTpslLHDhnefLNEKTFL 380
Cdd:cd03891 285 SGEPFL----TKPGKLVDAVSAAIKEV-TGITPELSTsgGTSDARFIASYGCPVVEFGLVNAT---IHK----VNERVSV 352
|
330
....*....|....
gi 71982082 381 RGVE----IYETLI 390
Cdd:cd03891 353 ADLEkltdIYERIL 366
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
38-352 |
3.68e-14 |
|
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: 73.01 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 38 ELGI--ERRSVETAPGTyfVIMTIPGskPDLPSIMLYSHTDVVptfreyWTHD--PYSAFKDEDGNIFARGAQDMKCVGV 113
Cdd:cd03885 34 ALGFtvERRPLGEFGDH--LIATFKG--TGGKRVLLIGHMDTV------FPEGtlAFRPFTVDGDRAYGPGVADMKGGLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 114 QYMEALRNWFAKGVKQwTRTIHIVWGPDEEIGHINGMkgfAVTEEFKK-----LNIDFALDE--------GIATeddvyk 180
Cdd:cd03885 104 VILHALKALKAAGGRD-YLPITVLLNSDEEIGSPGSR---ELIEEEAKgadyvLVFEPARADgnlvtarkGIGR------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 181 ifyaeripWWVKVTlpGHPGH-GSKFIE-KTAIEKL-HKLIASVDEFRNEQKsllaehpewtvgdvTTSNITIINGGVQV 257
Cdd:cd03885 174 --------FRLTVK--GRAAHaGNAPEKgRSAIYELaHQVLALHALTDPEKG--------------TTVNVGVISGGTRV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 258 NVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEA-GEGVTYEFmqfsNFKLISPNTREDP----FWAAIDDALQKEGCK 332
Cdd:cd03885 230 NVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTlVPGTSVEL----TGGLNRPPMEETPasrrLLARAQEIAAELGLT 305
|
330 340
....*....|....*....|
gi 71982082 333 YKKEIFIGATDSRFVRAQGI 352
Cdd:cd03885 306 LDWEATGGGSDANFTAALGV 325
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
67-393 |
5.25e-14 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 72.83 E-value: 5.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 67 PSIMLYSHTDVVPT-FREYWTHDPYsAFKDEDGNIFARGAQDMKCvGVQYMEALRNWFAKGVKQWTRTIHIVWGPDEEIG 145
Cdd:TIGR01246 56 PVLAFAGHTDVVPAgPEEQWSSPPF-EPVERDGKLYGRGAADMKG-SLAAFIVAAERFVKKNPDHKGSISLLITSDEEGT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 146 HINGMKGFAVTEEFKKLNIDFAL-DEGIATED--DVYKIfyAERIPWWVKVTLPGHPGHGSkFIEKtAIEKLHKLIASVD 222
Cdd:TIGR01246 134 AIDGTKKVVETLMARDELIDYCIvGEPSSVKKlgDVIKN--GRRGSITGNLTIKGIQGHVA-YPHL-ANNPIHKAAPALA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 223 EFRNEQksllaehpeWTVGDV----TTSNITIINGGVQV-NVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAGEGVT 297
Cdd:TIGR01246 210 ELTAIK---------WDEGNEffppTSLQITNIHAGTGAnNVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 298 YEFMQFSNFKLISPNTREDPFWAAIDdalqkEGCKYKKEIFI--GATDSRFVRAQGIRAIGFSPIINTpslLHDHNEFLN 375
Cdd:TIGR01246 281 LEWSLSGEPFLTNDGKLIDKAREAIE-----ETNGIKPELSTggGTSDGRFIALMGAEVVEFGPVNAT---IHKVNECVS 352
|
330
....*....|....*...
gi 71982082 376 EKTFLRGVEIYETLINKL 393
Cdd:TIGR01246 353 IEDLEKLSDVYQDLLENL 370
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
26-291 |
1.01e-13 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 71.76 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 26 EACRDFLfkyaDELGIERRSVETAPGTYFVIM-TIPGSkpDLPSIMLYSHTDVVPTFREYWTHDPYSAfKDEDGNIFARG 104
Cdd:PRK07522 29 EWVRDYL----AAHGVESELIPDPEGDKANLFaTIGPA--DRGGIVLSGHTDVVPVDGQAWTSDPFRL-TERDGRLYGRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 105 AQDMK----CVgvqyMEALRNWFAKGVKqwtRTIHIVWGPDEEIG-----HIngmkgfavTEEFKKLNIDFAL------- 168
Cdd:PRK07522 102 TCDMKgfiaAA----LAAVPELAAAPLR---RPLHLAFSYDEEVGclgvpSM--------IARLPERGVKPAGcivgept 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 169 -------DEGIATeddvykifyaeripwwVKVTLPGHPGHGS---KFIekTAIEKLHKLIASVdefRNEQKSLLAEHPEW 238
Cdd:PRK07522 167 smrpvvgHKGKAA----------------YRCTVRGRAAHSSlapQGV--NAIEYAARLIAHL---RDLADRLAAPGPFD 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 71982082 239 TVGDV--TTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKE 291
Cdd:PRK07522 226 ALFDPpySTLQTGTIQGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEA 280
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
55-373 |
1.11e-13 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 71.80 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 55 VIMTIPGSKPDLpSIMLYSHTDVVPTF-REYWTHDPYSAfKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVKQwTRT 133
Cdd:PRK13983 66 IVAKIPGGDGKR-TLWIISHMDVVPPGdLSLWETDPFKP-VVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRP-KYN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 134 IHIVWGPDEEIGHINGMKgFAVTEE---FKK--LNI--DFALDEGIATEddvykifYAERIPWWVKVTLPGHPGHGSkfI 206
Cdd:PRK13983 143 LGLAFVSDEETGSKYGIQ-YLLKKHpelFKKddLILvpDAGNPDGSFIE-------IAEKSILWLKFTVKGKQCHAS--T 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 207 EKTAIEKLH---KLIASVDEFRNE---QKSLLAEHPewtvgdVTTSNITIINGGVQ-VNVVPEKFEAYIDIRVTPLQDLD 279
Cdd:PRK13983 213 PENGINAHRaaaDFALELDEALHEkfnAKDPLFDPP------YSTFEPTKKEANVDnINTIPGRDVFYFDCRVLPDYDLD 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 280 AVLARVDQWAK----EAGEGVTYEFMQFSNfklISPNTRED-PFWAAIDDALQKegcKYKKEIFI----GATDSRFVRAQ 350
Cdd:PRK13983 287 EVLKDIKEIADefeeEYGVKIEVEIVQREQ---APPPTPPDsEIVKKLKRAIKE---VRGIEPKVggigGGTVAAFLRKK 360
|
330 340
....*....|....*....|...
gi 71982082 351 GIRAIGFSPIINTPsllHDHNEF 373
Cdd:PRK13983 361 GYPAVVWSTLDETA---HQPNEY 380
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
27-287 |
1.63e-13 |
|
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: 71.15 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 27 ACRDFLFKYADELGI--ERRSVEtaPGTYFVIMTIPGSKPDlPSIMLYSHTDVVPTFReywthdPYSAfKDEDGNIFARG 104
Cdd:cd05652 20 AVGDFLAEYLESLGFtvEKQPVE--NKDRFNVYAYPGSSRQ-PRVLLTSHIDTVPPFI------PYSI-SDGGDTIYGRG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 105 AQDMK-CVGVQyMEALRNWFAKGVKQwTRTIHIVWGPDEEIGHInGMKGFAvteefKKLNIDFalDEGIATEDDVYKIFY 183
Cdd:cd05652 90 SVDAKgSVAAQ-IIAVEELLAEGEVP-EGDLGLLFVVGEETGGD-GMKAFN-----DLGLNTW--DAVIFGEPTELKLAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 184 AERIPWWVKVTLPGHPGH-GSKFIEKTAIEKLHKLIASVDefrneqKSLLAEHPEWtvGDvTTSNITIINGGVQVNVVPE 262
Cdd:cd05652 160 GHKGMLGFKLTAKGKAGHsGYPWLGISAIEILVEALVKLI------DADLPSSELL--GP-TTLNIGRISGGVAANVVPA 230
|
250 260
....*....|....*....|....*..
gi 71982082 263 KFEAYIDIRVT--PLQDLDAVLARVDQ 287
Cdd:cd05652 231 AAEASVAIRLAagPPEVKDIVKEAVAG 257
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
11-299 |
7.42e-12 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 66.32 E-value: 7.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 11 REYLRVNTEQPKPD-YEACRDFLFKYADELG--IERRSVETAPG---TY---FVIMTIPGSKPDlPSIMLYSHTDVVPTf 81
Cdd:PRK13013 21 QDLIRIPTLNPPGRaYREICEFLAARLAPRGfeVELIRAEGAPGdseTYprwNLVARRQGARDG-DCVHFNSHHDVVEV- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 82 REYWTHDPYSAfKDEDGNIFARGAQDMK---CVGVQYMEALRnwfAKGVkQWTRTIHIVWGPDEEIGHINGMKGFAVTEE 158
Cdd:PRK13013 99 GHGWTRDPFGG-EVKDGRIYGRGACDMKgglAASIIAAEAFL---AVYP-DFAGSIEISGTADEESGGFGGVAYLAEQGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 159 FKKLNIDFALdegIATEDDVYKIFYAERIPWWVKVTLPGHPGHGS-KFIEKTAIEKLHkliASVDEFRNEQKSLLAEH-- 235
Cdd:PRK13013 174 FSPDRVQHVI---IPEPLNKDRICLGHRGVWWAEVETRGRIAHGSmPFLGDSAIRHMG---AVLAEIEERLFPLLATRrt 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 236 -----PEWtvGDVTTSNITIING----------GVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVD---QWAKEAGEGVT 297
Cdd:PRK13013 248 ampvvPEG--ARQSTLNINSIHGgepeqdpdytGLPAPCVADRCRIVIDRRFLIEEDLDEVKAEITallERLKRARPGFA 325
|
..
gi 71982082 298 YE 299
Cdd:PRK13013 326 YE 327
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
30-359 |
1.35e-11 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 65.58 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 30 DFLFKYADELGIERRSVETAPGTYFVIMTIPGSKPDlPSIMLYSHTDVVPTfrEYWTHDPYSAfKDEDGNIFARGAQDMK 109
Cdd:cd08013 33 TYVAAWLAHRGIEAHRIEGTPGRPSVVGVVRGTGGG-KSLMLNGHIDTVTL--DGYDGDPLSG-EIADGRVYGRGTLDMK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 110 CVGVQYMEALrnwfAKGVKQWTRTIHIVWG-PDEEIGHINgmkgfavTEEFkkLNIDFALDEGIATEDDVYKIFYAERIP 188
Cdd:cd08013 109 GGLAACMAAL----ADAKEAGLRGDVILAAvADEEDASLG-------TQEV--LAAGWRADAAIVTEPTNLQIIHAHKGF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 189 WWVKVTLPGHPGHGSKFIEKT-AIEKLHKLIASVDEFRNEqkslLAEHPEWTVGDVTTSNITIINGGVQVNVVPEKFEAY 267
Cdd:cd08013 176 VWFEVDIHGRAAHGSRPDLGVdAILKAGYFLVALEEYQQE----LPERPVDPLLGRASVHASLIKGGEEPSSYPARCTLT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 268 IDIRVTPLQDLDAVLARVdqwaKEAGEGVTYEFMQFSnFKLISPNTREDPFWAAIDDALQK-----------EGCKYKKE 336
Cdd:cd08013 252 IERRTIPGETDESVLAEL----TAILGELAQTVPNFS-YREPRITLSRPPFEVPKEHPFVQlvaahaakvlgEAPQIRSE 326
|
330 340
....*....|....*....|...
gi 71982082 337 IFigATDSRFVRAQGIRAIGFSP 359
Cdd:cd08013 327 TF--WTDAALLAEAGIPSVVFGP 347
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
27-360 |
3.06e-11 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 64.64 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 27 ACRDFLFKYADELG-------IERRSVETAPG----------TYFVIMTIPGSKPDLPSIMLYSHTDVVPTF-REYWTHD 88
Cdd:PRK06837 41 PCQDFLARAFRERGyevdrwsIDPDDLKSHPGagpveidysgAPNVVGTYRPAGKTGRSLILQGHIDVVPEGpLDLWSRP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 89 PYSAfKDEDGNIFARGAQDMKC--VGVQY-MEALRnwfAKGVkQWTRTIHIVWGPDEE-IGhiNG-----MKGFAVteef 159
Cdd:PRK06837 121 PFDP-VIVDGWMYGRGAADMKAglAAMLFaLDALR---AAGL-APAARVHFQSVIEEEsTG--NGalstlQRGYRA---- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 160 kklniDFAL----DEGIATEDDVYKIfyaeripwWVKVTLPGHPGH----GSKFiekTAIEKLHKLIASVDEFR---NEQ 228
Cdd:PRK06837 190 -----DACLipepTGEKLVRAQVGVI--------WFRLRVRGAPVHvreaGTGA---NAIDAAYHLIQALRELEaewNAR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 229 KsllAEHPEW-TVGDVTTSNITIINGGVQVNVVPEkfEAYIDIRVT--PLQDLDAVLARVDQWAKEAGEgvTYEFM---- 301
Cdd:PRK06837 254 K---ASDPHFeDVPHPINFNVGIIKGGDWASSVPA--WCDLDCRIAiyPGVTAADAQAEIEACLAAAAR--DDRFLsnnp 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982082 302 ---QFSNFK----LISPNtrEDPFwAAIDDALQKE-GCKYKKEIFIGATDSRF-VRAQGIRAIGFSPI 360
Cdd:PRK06837 327 pevVWSGFLaegyVLEPG--SEAE-AALARAHAAVfGGPLRSFVTTAYTDTRFyGLYYGIPALCYGPS 391
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
11-285 |
3.58e-11 |
|
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation.
Pssm-ID: 349888 [Multi-domain] Cd Length: 426 Bit Score: 64.27 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 11 REYLRVNTEQPKPD----YEACRDFLFKYADELGIERRSVETAPGTYFVIMTIPGSkPDLPSIMLYSHTDVVPTFREY-W 85
Cdd:cd03893 5 AELVAIPSVSAQPDrreeLRRAAEWLADLLRRLGFTVEIVDTSNGAPVVFAEFPGA-PGAPTVLLYGHYDVQPAGDEDgW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 86 THDPYSAfKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVKQWTRTIHIVWGpDEEIGHiNGMKGFAVTE-EFKKLNI 164
Cdd:cd03893 84 DSDPFEL-TERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEG-EEESGS-PSLDQLVEAHrDLLAADA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 165 DFALDeGIATEDDVYKIFYAER--IPWWVKVTLPGHPGHGSKF--IEKTAIEKLHKLIAS---------VD--------- 222
Cdd:cd03893 161 IVISD-STWVGQEQPTLTYGLRgnANFDVEVKGLDHDLHSGLYggVVPDPMTALAQLLASlrdetgrilVPglydavrel 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982082 223 ---EFRNEQKSL-LAEHPEWTVGDVT-------TSNITIINGGVQV----NVVPEKFEAYIDIRVTPLQDLDAVLARV 285
Cdd:cd03893 240 peeEFRLDAGVLeEVEIIGGTTGSVAerlwtrpALTVLGIDGGFPGegskTVIPPRARAKISIRLVPGQDPEEASRLL 317
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
56-386 |
4.07e-10 |
|
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: 60.90 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 56 IMTIPGSKPdlPSIMLYSHTDVVP-TFREYWTHDPYSAfKDEDGNIFARGAQDMK------CVGVQYMEALRNWFAKGvk 128
Cdd:cd05649 44 VIGYIGGGK--KKILFDGHIDTVGiGNIDNWKFDPYEG-YETDGKIYGRGTSDQKgglasmVYAAKIMKDLGLRDFAY-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 129 qwtrTIHIVWGPDEEIghingMKGFAVTEEFKKLNI--DFAldegIATEDDVYKIFYAERIPWWVKVTLPGHPGHGSKfI 206
Cdd:cd05649 119 ----TILVAGTVQEED-----CDGVCWQYISKADKIkpDFV----VSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSA-P 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 207 EK--TAIEKLHKLIASVDEFRNEQKsllaEHPEWTVGDVTTSNITIINGGvqVNVVPEKFEAYIDIRVTPLQDLDAVLAR 284
Cdd:cd05649 185 ERgdNAVYKMADIIQDIRQLNPNFP----EAPFLGRGTLTVTDIFSTSPS--RCAVPDSCRISIDRRLTVGETWEGCLEE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 285 VDQWA--KEAGEGVT---YEFMQFSNFKLISPNTREDPFWAAIDDA-LQKEGCKYKKEIFIGAT----------DSRFVR 348
Cdd:cd05649 259 IRALPavKKYGDDVAvsmYNYDRPSYTGEVYESERYFPTWLLPEDHeLVKALLEAYKALFGARPlidkwtfstnGVSIMG 338
|
330 340 350
....*....|....*....|....*....|....*...
gi 71982082 349 AQGIRAIGFSPiiNTPSLLHDHNEFLNEKTFLRGVEIY 386
Cdd:cd05649 339 RAGIPCIGFGP--GAENQAHAPNEYTWKEDLVRCAAGY 374
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
74-386 |
2.51e-09 |
|
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: 58.80 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 74 HTDVVPTFrEYWTHDPYSAFKdEDGNIFARGAQDMKCVGVQYMEALrnwfaKGVK----QWTRTIHIVWGPDEEIG---- 145
Cdd:cd03888 79 HLDVVPAG-EGWTTDPFKPVI-KDGKLYGRGTIDDKGPTIAALYAL-----KILKdlglPLKKKIRLIFGTDEETGwkci 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 146 -H--------------------INGMKG-FAVTEEFKKLNIDFALDEGI-------------------------ATEDDV 178
Cdd:cd03888 152 eHyfeheeypdfgftpdaefpvINGEKGiVTVDLTFKIDDDKGYRLISIkggeatnmvpdkaeavipgkdkeelALSAAT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 179 YKIFYAERIPWWVKVTLPGHPGHGS-------------KFIEK-TAIEKLHKLIASVDEFRNEQ---KSL-LAEHPEWTv 240
Cdd:cd03888 232 DLKGNIEIDDGGVELTVTGKSAHASapekgvnaitllaKFLAElNKDGNDKDFIKFLAKNLHEDyngKKLgINFEDEVM- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 241 GDVTTsNITIINggvqvnVVPEKFEAYIDIRVTPLQDLDAVLARVDqwAKEAGEGVTYEFMQFSNFKLISPNtreDPFWA 320
Cdd:cd03888 311 GELTL-NPGIIT------LDDGKLELGLNVRYPVGTSAEDIIKQIE--EALEKYGVEVEGHKHQKPLYVPKD---SPLVK 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71982082 321 AIDDALQKEGCKYKKEIFI-GATDSRFVRaqgiRAIGFSPII-NTPSLLHDHNEFLNEKTFLRGVEIY 386
Cdd:cd03888 379 TLLKVYEEQTGKEGEPVAIgGGTYARELP----NGVAFGPEFpGQKDTMHQANEFIPIDDLIKALAIY 442
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
11-393 |
8.28e-09 |
|
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: 56.59 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 11 REYLRVNTeqPKPDYEACRDFLFKYADELGIERRSVETapGTYFVimtipGSKPDLPSIMLYSHTDVVPTFREywthdpy 90
Cdd:cd05653 8 LDLLSIYS--PSGEEARAAKFLEEIMKELGLEAWVDEA--GNAVG-----GAGSGPPDVLLLGHIDTVPGEIP------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 91 saFKDEDGNIFARGAQDMKCVGVQYMEAlrnwFAKGVKQWTRTIHIVWGPDEEighiNGMKG--FAVTEefkKLNIDFAL 168
Cdd:cd05653 72 --VRVEGGVLYGRGAVDAKGPLAAMILA----ASALNEELGARVVVAGLVDEE----GSSKGarELVRR---GPRPDYII 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 169 ------DEGIATEddvykifYAERIPwwVKVTLPGHPGHGSKfIEKTAIEKLHKLIASVDEfrneqkslLAEHPEWTVGD 242
Cdd:cd05653 139 igepsgWDGITLG-------YRGSLL--VKIRCEGRSGHSSS-PERNAAEDLIKKWLEVKK--------WAEGYNVGGRD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 243 VTTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAgegvTYEFMQFSNFKLISPNTredPFWAAI 322
Cdd:cd05653 201 FDSVVPTLIKGGESSNGLPQRAEATIDLRLPPRLSPEEAIALATALLPTC----ELEFIDDTEPVKVSKNN---PLARAF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 323 DDALQKEGCKykkeifigatdSRFVRAQG-----IRAIGFSPIINT-----PSLLHDHNEFLNEKTFLRGVEIYETLINK 392
Cdd:cd05653 274 RRAIRKQGGK-----------PRLKRKTGtsdmnVLAPLWTVPIVAygpgdSTLDHTPNEHIELAEIERAAAVLKGALEE 342
|
.
gi 71982082 393 L 393
Cdd:cd05653 343 L 343
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
68-330 |
1.65e-08 |
|
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.
Pssm-ID: 349869 [Multi-domain] Cd Length: 394 Bit Score: 56.02 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 68 SIMLYSHTDVVPTfREYWTHDPYSAfKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVK-QWTRTIHIVWgpDEEIGH 146
Cdd:cd02697 75 TVALNAHGDVVPP-GDGWTRDPYGA-VVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPlRGAVELHFTY--DEEFGG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 147 INGmKGFAVTEEFKKlnIDFALDEGIAteddvYKIFYAERIPWWVKVTLPGHPGHGSkfIEKTAIEKLH---KLIASVDE 223
Cdd:cd02697 151 ELG-PGWLLRQGLTK--PDLLIAAGFS-----YEVVTAHNGCLQMEVTVHGKQAHAA--IPDTGVDALQgavAILNALYA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 224 FRNEQKSLLAE-----HPEWTVGdvttsnitIINGGVQVNVVPEKFEAYIDIRVTPLQD---LDAVLARVDQWAKEAGEG 295
Cdd:cd02697 221 LNAQYRQVSSQvegitHPYLNVG--------RIEGGTNTNVVPGKVTFKLDRRMIPEENpveVEAEIRRVIADAAASMPG 292
|
250 260 270
....*....|....*....|....*....|....*
gi 71982082 296 VTYEFMQFsnfkLISPNTREDPFWAAIDDALQKEG 330
Cdd:cd02697 293 ISVDIRRL----LLANSMRPLPGNAPLVEAIQTHG 323
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
74-109 |
2.50e-08 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 55.48 E-value: 2.50e-08
10 20 30
....*....|....*....|....*....|....*..
gi 71982082 74 HTDVVPT-FREYWTHDPYSAfKDEDGNIFARGAQDMK 109
Cdd:PRK13009 66 HTDVVPPgDLEAWTSPPFEP-TIRDGMLYGRGAADMK 101
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
7-384 |
7.68e-08 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 53.85 E-value: 7.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 7 VTRFREYLR---VNTeQP--KPDYEACRDFLFKYADELGIERRSVETAPGTYFVIMTIPGSkPDLPSIMLYSHTDVVPTF 81
Cdd:cd05680 1 LEELFELLRipsVSA-DPahKGDVRRAAEWLADKLTEAGFEHTEVLPTGGHPLVYAEWLGA-PGAPTVLVYGHYDVQPPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 82 R-EYWTHDPYSAFKdEDGNIFARGAQDMKCVGVQYMEALRNWFAKG------VKqwtrtiHIVWGpDEEIGHINgMKGFa 154
Cdd:cd05680 79 PlELWTSPPFEPVV-RDGRLYARGASDDKGQVFIHIKAVEAWLAVEgalpvnVK------FLIEG-EEEIGSPS-LPAF- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 155 VTEEFKKLNIDFAL--DEGIATEdDVYKIFYAER--IPWWVKVTLPGHPGHGSKF--IEKTAIEKLHKLIASV------- 221
Cdd:cd05680 149 LEENAERLAADVVLvsDTSMWSP-DTPTITYGLRglAYLEISVTGPNRDLHSGSYggAVPNPANALARLLASLhdedgrv 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 222 -------------DEFRNEQKSLLAEHPEWT----VGDV---------------TTSNITIINGGVQ----VNVVPEKFE 265
Cdd:cd05680 228 aipgfyddvrpltDAEREAWAALPFDEAAFKaslgVPALggeagyttlerlwarPTLDVNGIWGGYQgegsKTVIPSKAH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 266 AYIDIRVTPLQDLDAVLARVDQWAKE-AGEGVTYEFmqfsnfkliSPNTREDPFWAAIDDALQKEGCKYKKEIFigATDS 344
Cdd:cd05680 308 AKISMRLVPGQDPDAIADLLEAHLRAhAPPGVTLSV---------KPLHGGRPYLVPTDHPALQAAERALEEAF--GKPP 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 71982082 345 RFVRAQG-IRAIG-FSPIINTPSLL----------HDHNEFLNEKTFLRGVE 384
Cdd:cd05680 377 VFVREGGsIPIVAlFEKVLGIPTVLmgfglpddaiHAPNEKFRLECFHKGIE 428
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
31-171 |
8.76e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 53.99 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 31 FLFKYADELGIERRSVETaPGTYFVIMTIP-GSKPDLpsiMLYSHTDVVPTFR-EYWTHDPYSAfKDEDGNIFARGAQDM 108
Cdd:PRK06446 30 YLKDTMEKLGIKANIERT-KGHPVVYGEINvGAKKTL---LIYNHYDVQPVDPlSEWKRDPFSA-TIENGRIYARGASDN 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71982082 109 KCVGVQYMEALRNWFAKGvkQWTRTIHIVWGPDEEIGHINgMKGFaVTEEFKKLNIDFALDEG 171
Cdd:PRK06446 105 KGTLMARLFAIKHLIDKH--KLNVNVKFLYEGEEEIGSPN-LEDF-IEKNKNKLKADSVIMEG 163
|
|
| PRK06915 |
PRK06915 |
peptidase; |
68-294 |
9.07e-08 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 53.93 E-value: 9.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 68 SIMLYSHTDVVPTF-REYWTHDPYSAfKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVkQWTRTIHIVWGPDEEIGH 146
Cdd:PRK06915 95 SMILNGHIDVVPEGdVNQWDHHPYSG-EVIGGRIYGRGTTDMKGGNVALLLAMEALIESGI-ELKGDVIFQSVIEEESGG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 147 INGMKgfAVTEEFKKlnidfalDEGIATEDDVYKIFYAERIPWWVKVTLPGHPGHGSKFIEK-TAIEKLHKLIASVDEFR 225
Cdd:PRK06915 173 AGTLA--AILRGYKA-------DGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGvSAIEKSMFVIDHLRKLE 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71982082 226 NEQKSLLAEHPEWTVGDVTTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAGE 294
Cdd:PRK06915 244 EKRNDRITDPLYKGIPIPIPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAELND 312
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
69-385 |
1.74e-07 |
|
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: 52.44 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 69 IMLYSHTDVVPTfreywtHDPYSAFKDEDGNIFARGAQDMKCvGVQYMEALrnwFAKGVKQWTRT--IHIVWGPDEEIGH 146
Cdd:cd05647 56 VILAGHLDTVPV------AGNLPSRVEEDGVLYGCGATDMKA-GDAVQLKL---AATLAAATLKHdlTLIFYDCEEVAAE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 147 INGMKgfAVTEEFKK-LNIDFAL-----DEGI-ATEDDVYKIFyaeripwwvkVTLPGHPGHGSK-FIEKTAIEKLHKLI 218
Cdd:cd05647 126 LNGLG--RLAEEHPEwLAADFAVlgeptDGTIeGGCQGTLRFK----------VTTHGVRAHSARsWLGENAIHKLAPIL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 219 ASVDEFRNEqksllaehpEWTVGDVTTS---NITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVdqwaKEAGEG 295
Cdd:cd05647 194 ARLAAYEPR---------TVNIDGLTYReglNAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHV----REVFEG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 296 VTYEFmqfsNFKLISPNTR---EDPFWAAIDDAL-QKEGCKYkkeifiGATD-SRFvRAQGIRAIGFSPiiNTPSLLHDH 370
Cdd:cd05647 261 LGYEI----EVTDLSPGALpglDHPVARDLIEAVgGKVRAKY------GWTDvARF-SALGIPAVNFGP--GDPLLAHKR 327
|
330
....*....|....*
gi 71982082 371 NEFLNEKTFLRGVEI 385
Cdd:cd05647 328 DEQVPVEQITACAAI 342
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
26-171 |
2.16e-07 |
|
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: 52.73 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 26 EACRDFLFKYADELGIERRSVETaPGTYFVIMTIPGSKPdlPSIMLYSHTDVVPTFR-EYWTHDPYSAfKDEDGNIFARG 104
Cdd:cd05681 22 PETADFLKEFLRRLGAEVEIFET-DGNPIVYAEFNSGDA--KTLLFYNHYDVQPAEPlELWTSDPFEL-TIRNGKLYARG 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71982082 105 AQDMKCVGVQYMEALRNWFAKGVKQWTRTIHIVWGpDEEIGHINgMKGFaVTEEFKKLNIDFALDEG 171
Cdd:cd05681 98 VADDKGELMARLAALRALLQHLGELPVNIKFLVEG-EEEVGSPN-LEKF-VAEHADLLKADGCIWEG 161
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
67-298 |
2.21e-07 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 52.63 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 67 PSIMLYSHTDVVP-TFREYWTHDPYSAFKDeDGNIFARGAQDMK------CVGVQYMEALRNWFAkgvkqwtRTIHIVWG 139
Cdd:PRK13004 70 KLIAFDAHIDTVGiGDIKNWDFDPFEGEED-DGRIYGRGTSDQKggmasmVYAAKIIKDLGLDDE-------YTLYVTGT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 140 PDEEIghingMKGFAVTEEFKKLNI--DFAldegIATEDDVYKIFYAERIPWWVKVTLPGHPGHGSKfIEK--TAIEKLH 215
Cdd:PRK13004 142 VQEED-----CDGLCWRYIIEEDKIkpDFV----VITEPTDLNIYRGQRGRMEIRVETKGVSCHGSA-PERgdNAIYKMA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 216 KLIASVDEFRNEqkslLAEHPEWTVGDVTTSNITIINGGvqVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWA--KEAG 293
Cdd:PRK13004 212 PILNELEELNPN----LKEDPFLGKGTLTVSDIFSTSPS--RCAVPDSCAISIDRRLTVGETWESVLAEIRALPavKKAN 285
|
....*
gi 71982082 294 EGVTY 298
Cdd:PRK13004 286 AKVSM 290
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
38-120 |
1.61e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 49.90 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 38 ELGIERRSVETAPGTYFVIMTIPGSkPDLPSIMLYSHTDVVPTF-REYWTHDPYSAfKDEDGNIFARGAQDMKCVGVQYM 116
Cdd:PRK07907 56 EAGFDDVRVVSADGAPAVIGTRPAP-PGAPTVLLYAHHDVQPPGdPDAWDSPPFEL-TERDGRLYGRGAADDKGGIAMHL 133
|
....
gi 71982082 117 EALR 120
Cdd:PRK07907 134 AALR 137
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
22-393 |
8.19e-06 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 47.46 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 22 KPDYEaCRDFLFKYADELGIERRSVETApGTYFVIMTIPGSKPdlpSIMLYSHTDVVPTFREYWTHDPysaFKD--EDGN 99
Cdd:PRK08554 24 KPSKE-CPKFIKDTLESWGIESELIEKD-GYYAVYGEIGEGKP---KLLFMAHFDVVPVNPEEWNTEP---FKLtvKGDK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 100 IFARGAQDMKCVGVQYMEALRNWFAKGVKQwtrTIHIVWGPDEEIGHINGMKgfaVTEEFKKLNI--DFALD-EGIATED 176
Cdd:PRK08554 96 AYGRGSADDKGNVASVMLALKELSKEPLNG---KVIFAFTGDEEIGGAMAMH---IAEKLREEGKlpKYMINaDGIGMKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 177 DV--YKIFYAE-RIP------------WWVKVTLPGHPG-HGSKFIEKTaieKLHKLIASVDEFRNEQKSLLAEHPEWTV 240
Cdd:PRK08554 170 IIrrRKGFGVTiRVPsekvkvkgklreQTFEIRTPVVETrHAAYFLPGV---DTHPLIAASHFLRESNVLAVSLEGKFLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 241 GDVTTSNITI----INGGVQVNV----------------VPEKFEAYID--IRVTP----LQDLDAVLaRVDQWA----K 290
Cdd:PRK08554 247 GNVVPGEVTLtylePGEGEEVEVdlgltrllkaivplvrAPIKAEKYSDygVSITPnvysFAEGKHVL-KLDIRAmsysK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 291 EAGEGVTYEFMQFS--------------NFKLISPntrEDPFWAAIDDALQKEGCKYKKEIFIGATDSRFVRAQGIRAIG 356
Cdd:PRK08554 326 EDIERTLKEVLEFNlpeaeveirtnekaGYLFTPP---DEEIVKVALRVLKELGEDAEPVEGPGASDSRYFTPYGVKAID 402
|
410 420 430
....*....|....*....|....*....|....*..
gi 71982082 357 FSPIINTpslLHDHNEFLNEKTFLRGVEIYETLINKL 393
Cdd:PRK08554 403 FGPKGGN---IHGPNEYVEIDSLKKMPEVYKRIALRL 436
|
|
| PRK12893 |
PRK12893 |
Zn-dependent hydrolase; |
22-334 |
1.18e-05 |
|
Zn-dependent hydrolase;
Pssm-ID: 237250 [Multi-domain] Cd Length: 412 Bit Score: 47.18 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 22 KPDYEAcRDFLFKYADELGIERRsvETAPGTyfVIMTIPGSKPDLPSIMLYSHTDVVPT---F----------------- 81
Cdd:PRK12893 37 DEDREA-RDLLAQWMEEAGLTVS--VDAIGN--LFGRRAGTDPDAPPVLIGSHLDTQPTggrFdgalgvlaalevvrtln 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 82 -REYWTHDPYS--AFKDEDGNIFARGaqdmkcvgvqyMEALRNWFAKGVKQWTRTIHIVWGPD--EEIGHIngmkGFAVT 156
Cdd:PRK12893 112 dAGIRTRRPIEvvSWTNEEGARFAPA-----------MLGSGVFTGALPLDDALARRDADGITlgEALARI----GYRGT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 157 EEFKKLNID-F---------ALDE-----GIATedDVYKIfyaeripWWVKVTLPGHPGH-GSK--FIEKTAIEKLHKLI 218
Cdd:PRK12893 177 ARVGRRAVDaYlelhieqgpVLEAeglpiGVVT--GIQGI-------RWLEVTVEGQAAHaGTTpmAMRRDALVAAARII 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 219 ASVdefrNEQKSLLAEHPEWTVGDVTTSNitiiNGgvqVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKE--AGEGV 296
Cdd:PRK12893 248 LAV----ERIAAALAPDGVATVGRLRVEP----NS---RNVIPGKVVFTVDIRHPDDARLDAMEAALRAACAKiaAARGV 316
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 71982082 297 TYEFMQFSNFklisPNTREDPfW--AAIDDALQKEGCKYK 334
Cdd:PRK12893 317 QVTVETVWDF----PPVPFDP-AlvALVEAAAEALGLSHM 351
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
61-109 |
4.74e-05 |
|
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.
Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 45.29 E-value: 4.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 71982082 61 GSKPDLPSIMLYSHTDVVPT-FREYWTHDPYSaFKDEDGNIFARGAQDMK 109
Cdd:cd05676 80 GSDPSKKTVLIYGHLDVQPAkLEDGWDTDPFE-LTEKDGKLYGRGSTDDK 128
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
15-109 |
1.53e-04 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 43.49 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 15 RVNTEQPkP--DYEACRDFLFKYADELGIERRSVETAPGTYFVIMTIPGSKPDLP-SIMLYSHTDVVPTFR-EYWTHDPY 90
Cdd:PRK08596 24 RFETPAP-ParNTNEAQEFIAEFLRKLGFSVDKWDVYPNDPNVVGVKKGTESDAYkSLIINGHMDVAEVSAdEAWETNPF 102
|
90
....*....|....*....
gi 71982082 91 SAFKdEDGNIFARGAQDMK 109
Cdd:PRK08596 103 EPTI-KDGWLYGRGAADMK 120
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
27-334 |
1.54e-04 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 43.61 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 27 ACRDFLFKYADELGIErrsVET-APGTyfVIMTIPGSKPDLPSIMLYSHTDVVP-------------------TFRE-YW 85
Cdd:PRK09290 38 QARDLFAEWMEAAGLT---VRVdAVGN--LFGRLEGRDPDAPAVLTGSHLDTVPnggrfdgplgvlagleavrTLNErGI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 86 THdPYS----AFKDEDGNIF------------------ARGAQDMKcvGVQYMEALRNWFAKG--VKQWTRT-------- 133
Cdd:PRK09290 113 RP-RRPievvAFTNEEGSRFgpamlgsrvftgaltpedALALRDAD--GVSFAEALAAIGYDGdeAVGAARArrdikafv 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 134 -IHIVWGPdeeighingmkgfaVTEEfkkLNIDFALDEGIATeddvykifyaeriPWWVKVTLPGHPGH----------- 201
Cdd:PRK09290 190 eLHIEQGP--------------VLEA---EGLPIGVVTGIVG-------------QRRYRVTFTGEANHagttpmalrrd 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 202 ----GSKFIekTAIEKLhkliasvdefrneqkslLAEHPEWTVGdvTTSNITIINGGVqvNVVPEKFEAYIDIRVTPLQD 277
Cdd:PRK09290 240 allaAAEII--LAVERI-----------------AAAHGPDLVA--TVGRLEVKPNSV--NVIPGEVTFTLDIRHPDDAV 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 278 LDAVLARVDQWAKE--AGEGVTYEFMQFSNFklisPNTREDPFW-AAIDDALQKEGCKYK 334
Cdd:PRK09290 297 LDALVAELRAAAEAiaARRGVEVEIELISRR----PPVPFDPGLvAALEEAAERLGLSYR 352
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
48-152 |
2.08e-04 |
|
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: 43.49 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 48 TAPGTYFVIMTIPGSKPDLPSIMLYSHTDVVPT-------------------FREYWTHDPYSAFKDEDGN--IFARGAQ 106
Cdd:cd05654 53 DDLGRRNVTALVKGKKPSKRTIILISHFDTVGIedygelkdiafdpdeltkaFSEYVEELDEEVREDLLSGewLFGRGTM 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 71982082 107 DMKCVGVQYMEALRnwFAKGVKQWTRTIHIVWGPDEEIGHiNGMKG 152
Cdd:cd05654 133 DMKSGLAVHLALLE--QASEDEDFDGNLLLMAVPDEEVNS-RGMRA 175
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
62-386 |
5.23e-04 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 41.67 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 62 SKPDLpsiMLYSHTDVVPTFREYWthdpysafkdEDGNI-FARGAQDMKCVGVQYMEALrnwfAKGVKQWTR-TIHIVWG 139
Cdd:PRK08652 54 SKAEL---FVEVHYDTVPVRAEFF----------VDGVYvYGTGACDAKGGVAAILLAL----EELGKEFEDlNVGIAFV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 140 PDEEIGHiNGMKGFAvtEEFKKlnidfalDEGIATEDDVYKIFYAERIPWWVKVTLPGHPGHGSkFIE--KTAIEKLHKL 217
Cdd:PRK08652 117 SDEEEGG-RGSALFA--ERYRP-------KMAIVLEPTDLKVAIAHYGNLEAYVEVKGKPSHGA-CPEsgVNAIEKAFEM 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 218 IasvdefrNEQKSLLaehPEWTVGDVTTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAgeGVT 297
Cdd:PRK08652 186 L-------EKLKELL---KALGKYFDPHIGIQEIIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEY--TVK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 298 YEFMQF-SNFKLispnTREDPFWAAIDDALQKEGCKYKKEIFIGATDSRFVRAQGIRAIGFSP----IINTPSLLHDHNE 372
Cdd:PRK08652 254 YEYTEIwDGFEL----DEDEEIVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTKTVVWGPgeldLCHTKFERIDVRE 329
|
330
....*....|....*
gi 71982082 373 FLNEKTFLRGV-EIY 386
Cdd:PRK08652 330 VEKAKEFLKALnEIL 344
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
2-355 |
5.70e-04 |
|
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: 41.67 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 2 SEDIGVTRFREYLRVNTEQPKPDyEACRdFLFKYADELG---IERRSVETAP-GTYFVIMTIPGSKPDLPSIMLYSHTDV 77
Cdd:cd05683 1 NEDRLINTFLELVQIDSETLHEK-EISK-VLKKKFENLGlsvIEDDAGKTTGgGAGNLICTLKADKEEVPKILFTSHMDT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 78 VPTFREYWTHDPYSAFKDEDGNIFArGAQDMKCVGVqYMEALRnwFAKGVKQWTRTIHIVWGPDEEIGHInGMKgfAVTE 157
Cdd:cd05683 79 VTPGINVKPPQIADGYIYSDGTTIL-GADDKAGIAA-ILEAIR--VIKEKNIPHGQIQFVITVGEESGLV-GAK--ALDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 158 EFKKLNIDFALDegiaTEDDVYKIFYAERIPWWVKVTLPGHPGHGSKFIEK--TAIEKLHKLIASVDEFRneqksllaeh 235
Cdd:cd05683 152 ELIDADYGYALD----SEGDVGTIIVGAPTQDKINAKIYGKTAHAGTSPEKgiSAINIAAKAISNMKLGR---------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 236 pewtVGDVTTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLAR-VDQWAKEAGE-GVTYEFMQFSNFKLISPNT 313
Cdd:cd05683 218 ----IDEETTANIGKFQGGTATNIVTDEVNIEAEARSLDEEKLDAQVKHmKETFETTAKEkGAHAEVEVETSYPGFKINE 293
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 71982082 314 REDPFWAAiDDALQKEGCKYKKEIFIGATDSRFVRAQGIRAI 355
Cdd:cd05683 294 DEEVVKLA-KRAANNLGLEINTTYSGGGSDANIINGLGIPTV 334
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
12-291 |
9.28e-04 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 41.29 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 12 EYLRVNTEQ--PKPDyEACR---DFLFKYADELG--IERRSVETAPGTYFVIMTIPGSKPDLPSIMLYSHTDVVPTFREY 84
Cdd:cd08012 18 KYLQNNPPQlvPKED-NAGRhvlEALTPYSTENGgpLVIDHVSYVKGRGNIIVEYPGTVDGKTVSFVGSHMDVVTANPET 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 85 WTHDPYSAFKDEDgNIFARGAQDmkCVG-VQYMEALRNWFAKGVKQWTRTIHIVWGPDEEIGHINGMKGFAVTEEFKKLN 163
Cdd:cd08012 97 WEFDPFSLSIDGD-KLYGRGTTD--CLGhVALVTELFRQLATEKPALKRTVVAVFIANEENSEIPGVGVDALVKSGLLDN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 164 IDFALDEGIATEDDVYKIFYAERIPWwvKVTLPG---HPGHGSKFIekTAIEKLHKLIASVDE-FRNEQKSllaeHPEWT 239
Cdd:cd08012 174 LKSGPLYWVDSADSQPCIGTGGMVTW--KLTATGklfHSGLPHKAI--NALELVMEALAEIQKrFYIDFPP----HPKEE 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 240 VGDVTTSN------ITIINGGvqVNVVPEkfEAYI--DIRVTPLQDLDAVLARVDQWAKE 291
Cdd:cd08012 246 VYGFATPStmkptqWSYPGGS--INQIPG--ECTIcgDCRLTPFYDVKEVREKLEEYVDD 301
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
16-145 |
4.52e-03 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 39.00 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 16 VNTEQPKPDYEACRDFLFKYADELGIERRSVETAPGTY----FVIMTIPGSKPDLPSIMLYSHTDVV-P--TFREYwthd 88
Cdd:PRK07473 21 VECESPTWDAAAVNRMLDLAARDMAIMGATIERIPGRQgfgdCVRARFPHPRQGEPGILIAGHMDTVhPvgTLEKL---- 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 71982082 89 pysAFKDEDGNIFARGAQDMKCVGVQYMEALRNWFAKGVKQwTRTIHIVWGPDEEIG 145
Cdd:PRK07473 97 ---PWRREGNKCYGPGILDMKGGNYLALEAIRQLARAGITT-PLPITVLFTPDEEVG 149
|
|
| M20_ACY1L2-like |
cd05672 |
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 ... |
249-305 |
5.06e-03 |
|
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. This subfamily includes Staphylococcus aureus antibiotic resistance factor HmrA that has been shown to participate in methicillin resistance mechanisms in vivo in the presence of beta-lactams. Aminoacylase 1 (ACY1) proteins 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 the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. 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: 349921 [Multi-domain] Cd Length: 360 Bit Score: 38.70 E-value: 5.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 71982082 249 TIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAGE--GVTYEFMQFSN 305
Cdd:cd05672 209 IITEGGKAPNIIPDYAEARFYVRAPTRKELEELRERVIACFEGAALatGCTVEIEEDEP 267
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
248-370 |
7.55e-03 |
|
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273857 [Multi-domain] Cd Length: 363 Bit Score: 38.09 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71982082 248 ITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAGE--GVTYEFmqfsNFKLISPNTREDPFWAAIDDA 325
Cdd:TIGR01891 222 VGIIEAGGAPNVIPDKASMSGTVRSLDPEVRDQIIDRIERIVEGAAAmyGAKVEL----NYDRGLPAVTNDPALTQILKE 297
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 71982082 326 LQKEGcKYKKEIFI------GATDSRFV--RAQGirAIGFSPIIN-TPSLLHDH 370
Cdd:TIGR01891 298 VARHV-VGPENVAEdpevtmGSEDFAYYsqKVPG--AFFFLGIGNeGTGLSHPL 348
|
|
| M20_Acy1L2 |
cd03887 |
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
249-305 |
8.28e-03 |
|
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, Aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase) subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins 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 the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. 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: 349883 [Multi-domain] Cd Length: 360 Bit Score: 37.94 E-value: 8.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 71982082 249 TIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLARVDQWAKEAGE--GVTYEFMQFSN 305
Cdd:cd03887 209 IITEGGKAPNIIPDYAEAEFYVRAPTLKELEELTERVIACFEGAALatGCEVEIEELEG 267
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
244-283 |
8.60e-03 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 38.07 E-value: 8.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 71982082 244 TTSNITIINGGVQVNVVPEKFEAYIDIRVTPLQDLDAVLA 283
Cdd:PRK06133 255 TTLNWTVAKAGTNRNVIPASASAQADVRYLDPAEFDRLEA 294
|
|
| |
