|
Name |
Accession |
Description |
Interval |
E-value |
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
2-312 |
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: 604.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAFKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKRPEFQALR 81
Cdd:cd05646 81 EKWTHDPFSAHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGHDGMEKFVKTEEFKKLN 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 82 AGFVLDEGLANPTDAFTVFYSERSPWWVQVTSTGKPGHASRFIEDTAAEKLHKVISSILAFREKERQRLQANPHLKEGAV 161
Cdd:cd05646 161 VGFALDEGLASPTEEYRVFYGERSPWWVVITAPGTPGHGSKLLENTAGEKLRKVIESIMEFRESQKQRLKSNPNLTLGDV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 162 TSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQEAGEGVTFEFAQKFTEPRMTPTDDSDPWWAAFS 241
Cdd:cd05646 241 TTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGRGVTYEFEQKSPEKDPTSLDDSNPWWAAFK 320
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907194533 242 GACKAMNLTLEPEIFPAATDSRFIRAVGIPALGFSPMNRTPVLLHDHNERLHEDIFLRGVDIYTGLLSALA 312
Cdd:cd05646 321 KAVKEMGLKLKPEIFPAATDSRYIRALGIPALGFSPMNNTPILLHDHNEFLNEDVFLRGIEIYEKIIPALA 391
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
2-314 |
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: 555.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAFKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKRPEFQALR 81
Cdd:TIGR01880 88 EHWTHPPFSAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEKFAKTDEFKALN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 82 AGFVLDEGLANPTDAFTVFYSERSPWWVQVTSTGKPGHASRFIEDTAAEKLHKVISSILAFREKERQRLQANPHLKEGAV 161
Cdd:TIGR01880 168 LGFALDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKLMENTAMEKLEKSVESIRRFRESQFQLLQSNPDLAIGDV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 162 TSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQEAGEGVTFEFAQKFTEPRMTPTDDSDPWWAAFS 241
Cdd:TIGR01880 248 TSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAGEGVTYEFSQHSGKPLVTPHDDSNPWWVAFK 327
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907194533 242 GACKAMNLTLEPEIFPAATDSRFIRAVGIPALGFSPMNRTPVLLHDHNERLHEDIFLRGVDIYTGLLSALASV 314
Cdd:TIGR01880 328 DAVKEMGCTFKPEILPGSTDSRYIRAAGVPALGFSPMNNTPVLLHDHNEFLNEAVFLRGIEIYQTLISALASV 400
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
2-312 |
2.32e-60 |
|
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: 197.42 E-value: 2.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHkGMELFVKRpEFQALR 81
Cdd:COG0624 89 ELWTSDPFEP-TIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSP-GARALVEE-LAEGLK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 82 AGFVLDeglANPTDAFTVFYSERSPWWVQVTSTGKPGHASRFIE-DTAAEKLHKVISSILAFREKERqrlqANPHLKEga 160
Cdd:COG0624 166 ADAAIV---GEPTGVPTIVTGHKGSLRFELTVRGKAAHSSRPELgVNAIEALARALAALRDLEFDGR----ADPLFGR-- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 161 vTSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQEAGEG--VTFEFAQKFTEPRMTPTDdsDPWWA 238
Cdd:COG0624 237 -TTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGveVEVEVLGDGRPPFETPPD--SPLVA 313
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194533 239 AFSGACKA-MNLTLEPEIFPAATDSRFI-RAVGIPALGFSPMNRTpvLLHDHNERLHEDIFLRGVDIYTGLLSALA 312
Cdd:COG0624 314 AARAAIREvTGKEPVLSGVGGGTDARFFaEALGIPTVVFGPGDGA--GAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
8-308 |
5.05e-55 |
|
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 181.78 E-value: 5.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 8 PFEAFKDseGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRfPRTIHMTFVPDEEvGGHKGMELFVKRPEFQALRAGFVLD 87
Cdd:pfam01546 18 PFKSTED--GKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEE-GGMGGARALIEDGLLEREKVDAVFG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 88 EGLANPTD-----AFTVFYSERSPWWVQVTSTGKPGHASRF-IEDTAAEKLHKVISSILAFREKERQRLqanphlkEGAV 161
Cdd:pfam01546 94 LHIGEPTLleggiAIGVVTGHRGSLRFRVTVKGKGGHASTPhLGVNAIVAAARLILALQDIVSRNVDPL-------DPAV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 162 TSV-NLTKLEGGVayNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQEAGE--GVTFEFaqKFTEPRMTPTDDSDPWWA 238
Cdd:pfam01546 167 VTVgNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAayGVKVEV--EYVEGGAPPLVNDSPLVA 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907194533 239 AFSGACKAM---NLTLEPEIFPAATDSRFIRAvGIPA--LGFSPMNRTpvlLHDHNERLHEDIFLRGVDIYTGLL 308
Cdd:pfam01546 243 ALREAAKELfglKVELIVSGSMGGTDAAFFLL-GVPPtvVFFGPGSGL---AHSPNEYVDLDDLEKGAKVLARLL 313
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
2-308 |
4.57e-38 |
|
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: 138.59 E-value: 4.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGhKGMELFVKRPefQALR 81
Cdd:cd08659 72 DKWSFPPFSG-RIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGS-DGARALLEAG--YADR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 82 AGFVLDeglANPTDaFTVFYSERSPWWVQVTSTGKPGHASRfiEDTAAEKLHKVISSILAFREkERQRLQANPHLKEgav 161
Cdd:cd08659 148 LDALIV---GEPTG-LDVVYAHKGSLWLRVTVHGKAAHSSM--PELGVNAIYALADFLAELRT-LFEELPAHPLLGP--- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 162 TSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQEAGEGVTFEFAqkFTEPRMTPTDDSDPWWAAFS 241
Cdd:cd08659 218 PTLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVS--LDGDPPFFTDPDHPLVQALQ 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194533 242 GACKAMNLTLEPEIFPAATDSRFI-RAVGIPALGFSPMNrtPVLLHDHNERLHEDIFLRGVDIYTGLL 308
Cdd:cd08659 296 AAARALGGDPVVRPFTGTTDASYFaKDLGFPVVVYGPGD--LALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
4-308 |
1.28e-37 |
|
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: 138.65 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVK-RPE-FQAlr 81
Cdd:cd05675 84 WSVDPFSG-EIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDnHPElFDG-- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 82 AGFVLDEG------LANPTDAFTVFYSERSPWWVQVTSTGKPGHASRFIEDTAAEKLHKVISSILAFREKER-------- 147
Cdd:cd05675 161 ATFALNEGgggslpVGKGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRPTDDNAITRLAEALRRLGAHNFPVRltdetayf 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 148 -----------------------QRLQA----NPHLKEGAVTSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFE 200
Cdd:cd05675 241 aqmaelaggeggalmltavpvldPALAKlgpsAPLLNAMLRNTASPTMLDAGYATNVLPGRATAEVDCRILPGQSEEEVL 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 201 KQLQRwcqEAGE-GVTFEFAQKftEPRMTPTDDSdPWWAAFSGACKAM--NLTLEPEIFPAATDSRFIRAVGIPALGFSP 277
Cdd:cd05675 321 DTLDK---LLGDpDVSVEAVHL--EPATESPLDS-PLVDAMEAAVQAVdpGAPVVPYMSPGGTDAKYFRRLGIPGYGFAP 394
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907194533 278 MNRTPVL-----LHDHNERLHEDIFLRGVDIYTGLL 308
Cdd:cd05675 395 LFLPPELdytglFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
2-290 |
5.52e-33 |
|
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: 125.20 E-value: 5.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKRpeFQALR 81
Cdd:TIGR01910 82 ELWKTDPFKP-VEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLLQRG--YFKDA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 82 AGFVLDEglanPTDAFTVFYSERSPWWVQVTSTGKPGHASR--FIEDtAAEKLHKVissILAFREKERQRLQANPHLKEG 159
Cdd:TIGR01910 159 DGVLIPE----PSGGDNIVIGHKGSIWFKLRVKGKQAHASFpqFGVN-AIMKLAKL---ITELNELEEHIYARNSYGFIP 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 160 AVTSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQEAG--EGVTFEFAQKFTEPRMTPTDDSDPWW 237
Cdd:TIGR01910 231 GPITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSksDGWLYENEPVVKWSGPNETPPDSRLV 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194533 238 AAFSGACKAMnLTLEPEI--FPAATDSRFIRAVGIPALGFSP-MNRTPvllHDHNE 290
Cdd:TIGR01910 311 KALEAIIKKV-RGIEPEVlvSTGGTDARFLRKAGIPSIVYGPgDLETA---HQVNE 362
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
2-308 |
4.03e-30 |
|
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: 117.10 E-value: 4.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKG----MELFVKRPef 77
Cdd:cd08011 78 EGWTVDPYSG-KIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGtkylLEKVRIKP-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 78 qalraGFVLdegLANPTDAFTVFYSERSPWWVQVTSTGKPGHASRFiedtaaeklHKVISSIlafrekeRQRLQANPHLK 157
Cdd:cd08011 155 -----NDVL---IGEPSGSDNIRIGEKGLVWVIIEITGKPAHGSLP---------HRGESAV-------KAAMKLIERLY 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 158 EgAVTSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRwCQEAGEGVTFEFAQkftEPRMTPTDDSDPWW 237
Cdd:cd08011 211 E-LEKTVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIID-HLDSIEEVSFEIKS---FYSPTVSNPDSEIV 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907194533 238 AAFSGACKAM-NLTLEPEIFPAATDSRFIRAVGIPALGFSPMNrtPVLLHDHNERLHEDIFLRGVDIYTGLL 308
Cdd:cd08011 286 KKTEEAITEVlGIRPKEVISVGASDARFYRNAGIPAIVYGPGR--LGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
4-313 |
6.52e-30 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 118.51 E-value: 6.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEAFKDsEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHkGMELFVKRPEFQALRAG 83
Cdd:PRK08262 133 WTHPPFSGVIA-DGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVGGL-GARAIAELLKERGVRLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 84 FVLDEGLANPTDAFTVF--------YSERSPWWVQVTSTGKPGHASRFIEDTAAEKLHKVISSI------LAFREKERQR 149
Cdd:PRK08262 211 FVLDEGGAITEGVLPGVkkpvaligVAEKGYATLELTARATGGHSSMPPRQTAIGRLARALTRLednplpMRLRGPVAEM 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 150 LQ--------------ANPHLKEGAV---------------TSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMkafE 200
Cdd:PRK08262 291 FDtlapemsfaqrvvlANLWLFEPLLlrvlakspetaamlrTTTAPTMLKGSPKDNVLPQRATATVNFRILPGDSV---E 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 201 KQLQRwCQEA--GEGVTFEFAQKFTEPRMTPTDDSDPWwaafsgacKAMNLTLEpEIFP----------AATDSRFIRAV 268
Cdd:PRK08262 368 SVLAH-VRRAvaDDRVEIEVLGGNSEPSPVSSTDSAAY--------KLLAATIR-EVFPdvvvapylvvGATDSRHYSGI 437
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1907194533 269 GIPALGFSPMNRTP---VLLHDHNERLHEDIFLRGVDIYTGLLSALAS 313
Cdd:PRK08262 438 SDNVYRFSPLRLSPedlARFHGTNERISVANYARMIRFYYRLIENAAG 485
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
6-313 |
7.56e-29 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 114.32 E-value: 7.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 6 HDPFEAFKDsEGYIYARGSQDMKS--VSIqyLEAVRRLKSEGhrfPRTIHMTFVPDEEVGGHKGMELfvkrpefqALRAG 83
Cdd:PRK08651 95 NVPFEPKVK-DGKVYGRGASDMKGgiAAL--LAAFERLDPAG---DGNIELAIVPDEETGGTGTGYL--------VEEGK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 84 FVLDEGL-ANPTDAFTVFYSERSPWWVQVTSTGKPGHASR-FIEDTAAEKLHKVISSILAFREKERQRLQANPHlkEGAV 161
Cdd:PRK08651 161 VTPDYVIvGEPSGLDNICIGHRGLVWGVVKVYGKQAHASTpWLGINAFEAAAKIAERLKSSLSTIKSKYEYDDE--RGAK 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 162 TSVNL--TKLEGGVAYNVVPATMSASFDFRVAPDVDM----KAFEKQLQRWCQEAGEGVTFEFAQkFTEPRMTPtDDSDP 235
Cdd:PRK08651 239 PTVTLggPTVEGGTKTNIVPGYCAFSIDRRLIPEETAeevrDELEALLDEVAPELGIEVEFEITP-FSEAFVTD-PDSEL 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194533 236 WWAAFSGACKAMNLTLEPEIFPAATDSRFIRAVGIPALGFSPMNrtPVLLHDHNERLHEDIFLRGVDIYTGLLSALAS 313
Cdd:PRK08651 317 VKALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGE--LELAHAPDEYVEVKDVEKAAKVYEEVLKRLAK 392
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
5-278 |
5.58e-27 |
|
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: 108.45 E-value: 5.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 5 HHD--------PFEAFKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKrpE 76
Cdd:cd03885 68 HMDtvfpegtlAFRPFTVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRELIEE--E 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 77 FQALRAGFVLDEGLANptDAFTVFYSERSPWWVQVTstGKPGHASRFIEDTAAeklhkvissilAFREKERQRLQANPHL 156
Cdd:cd03885 146 AKGADYVLVFEPARAD--GNLVTARKGIGRFRLTVK--GRAAHAGNAPEKGRS-----------AIYELAHQVLALHALT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 157 KEGAVTSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQEA-GEGVTFEFAQKFTEPRMTPTDDSDP 235
Cdd:cd03885 211 DPEKGTTVNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTlVPGTSVELTGGLNRPPMEETPASRR 290
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907194533 236 WWAAFSGACKAMNLTLEPEIFPAATDSRFIRAVGIPAL-GFSPM 278
Cdd:cd03885 291 LLARAQEIAAELGLTLDWEATGGGSDANFTAALGVPTLdGLGPV 334
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
2-312 |
1.94e-26 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 108.55 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEaFKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGME-LFVKRPEfqAL 80
Cdd:PRK09133 118 EDWTRDPFK-LVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEGTPMNGVAwLAENHRD--LI 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 81 RAGFVLDEGLANPTD------AFTVFYSERSPWWVQVTSTGKPGHASRFIEDTAAEKLHKVISSILAFR----------- 143
Cdd:PRK09133 195 DAEFALNEGGGGTLDedgkpvLLTVQAGEKTYADFRLEVTNPGGHSSRPTKDNAIYRLAAALSRLAAYRfpvmlndvtra 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 144 --------------------------EKERQRLQANPHLKEGAVTSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMK 197
Cdd:PRK09133 275 yfkqsaaietgplaaamrafaanpadEAAIALLSADPSYNAMLRTTCVATMLEGGHAENALPQRATANVNCRIFPGDTIE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 198 AFEKQLQRWCQEAGEGVTFEfaqkfTEPRMTPTDDSDP-WWAAFSGACKAM--NLTLEPEIFPAATDSRFIRAVGIPALG 274
Cdd:PRK09133 355 AVRATLKQVVADPAIKITRI-----GDPSPSPASPLRPdIMKAVEKLTAAMwpGVPVIPSMSTGATDGRYLRAAGIPTYG 429
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1907194533 275 FSPM--NRTPVLLHDHNERLHEDIFLRGVDIYTGLLSALA 312
Cdd:PRK09133 430 VSGLfgDPDDTFAHGLNERIPVASFYEGRDFLYELVKDLA 469
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
4-308 |
2.61e-23 |
|
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: 99.64 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEAFKDsEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKG----MELFVKRPEFQA 79
Cdd:cd05674 91 WTHPPFSGHYD-GGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTIILAFGHDEEVGGERGagaiAELLLERYGVDG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 80 LRagFVLDEGLAN-PTDAFTVFY-----SERSPWWVQVTSTGKPGHASRFIEDTAAEKLHKVISSILA------FREK-- 145
Cdd:cd05674 170 LA--AILDEGGAVlEGVFLGVPFalpgvAEKGYMDVEITVHTPGGHSSVPPKHTGIGILSEAVAALEAnpfppkLTPGnp 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 146 -------------------ERQRLQANPHLKEGAV---------------TSVNLTKLEGGVAYNVVPATMSASFDFRVA 191
Cdd:cd05674 248 yygmlqclaehsplpprslKSNLWLASPLLKALLAsellstspltrallrTTQAVDIINGGVKINALPETATATVNHRIA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 192 P--DVD--MKAFEKQLQRWCQEAGEGVTFE-------------FAQKFTEPRMTPTDDSDPWWAAFSGACKAM------N 248
Cdd:cd05674 328 PgsSVEevLEHVKNLIADIAVKYGLGLSAFggdviystngtklLTSLLSPEPSPVSSTSSPVWQLLAGTIRQVfeqfgeD 407
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907194533 249 LTLEPEIFPAATDSRFIRAVGIPALGFSPMNRTPVLL---HDHNERLHEDIFLRGVDIYTGLL 308
Cdd:cd05674 408 LVVAPGIMTGNTDTRHYWNLTKNIYRFTPIRLNPEDLgriHGVNERISIDDYLETVAFYYQLI 470
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
4-282 |
2.47e-21 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 93.76 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFE-AFKDseGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFV-KRPE-FQAL 80
Cdd:PRK07906 84 WSVHPFSgEIRD--GYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEAGGTYGAHWLVdNHPElFEGV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 81 RA------GFVLDegLANPTDAFTVFYSERSPWWVQVTSTGKPGHASRFIEDTAAEKLHKVISSILAFR------EKERQ 148
Cdd:PRK07906 162 TEaisevgGFSLT--VPGRDRLYLIETAEKGLAWMRLTARGRAGHGSMVNDDNAVTRLAEAVARIGRHRwplvltPTVRA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 149 RLQA------------NPHL---KEGAV---------TSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDmKAFEKQLQ 204
Cdd:PRK07906 240 FLDGvaeltglefdpdDPDAllaKLGPAarmvgatlrNTANPTMLKAGYKVNVIPGTAEAVVDGRFLPGRE-EEFLATVD 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 205 RWcqeAGEGVTFEFAQkfteprmtptdDSDPWWAAFSGA-CKAMNLTLE---------PEIFPAATDSRFIRAVGIPALG 274
Cdd:PRK07906 319 EL---LGPDVEREWVH-----------RDPALETPFDGPlVDAMNAALLaedpgarvvPYMLSGGTDAKAFSRLGIRCYG 384
|
....*...
gi 1907194533 275 FSPMnRTP 282
Cdd:PRK07906 385 FAPL-RLP 391
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
2-293 |
3.16e-19 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 87.36 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMelfvkrpefQALR 81
Cdd:cd03895 92 ELWTRPPFEA-TIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNGAL---------AALM 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 82 AGFVLDEGLANPTDAFTVFYSERSPWWVQVTSTGKPGHASRFIEDTAA-EKLHKVISSILAFREKERQRLQANPHL--KE 158
Cdd:cd03895 162 RGYRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAiEKAMHLIQALQELEREWNARKKSHPHFsdHP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 159 GAVTsVNLTKLEGGVAYNVVPAtmSASFDFRVA--PDVDMKAFEKQLQRWCQEA--------GEGVTFEFAQKFTEPRMT 228
Cdd:cd03895 242 HPIN-FNIGKIEGGDWPSSVPA--WCVLDCRIGiyPGESPEEARREIEECVADAaatdpwlsNHPPEVEWNGFQAEGYVL 318
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194533 229 PtdDSDPWWAAFSGACKAM-NLTLEPEIFPAATDSR-FIRAVGIPALGFSPMNRTPvllHDHNERLH 293
Cdd:cd03895 319 E--PGSDAEQVLAAAHQAVfGTPPVQSAMTATTDGRfFVLYGDIPALCYGPGSRDA---HGFDESVD 380
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
3-277 |
6.37e-19 |
|
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: 86.11 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 3 HWHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPrtIHMTFVPDEEVGgHKGMELFVKRPEFQALRA 82
Cdd:cd03894 75 KWSSDPFTL-TERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKP--LHLAFSYDEEVG-CLGVRHLIAALAARGGRP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 83 GFVLdegLANPTDAFTVF-----YSERspwwvqVTSTGKPGHASrfieDT-----AAEKLHKVISSILAFREKERQRLqA 152
Cdd:cd03894 151 DAAI---VGEPTSLQPVVahkgiASYR------IRVRGRAAHSS----LPplgvnAIEAAARLIGKLRELADRLAPGL-R 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 153 NPHLKEGAVTsVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQEAGE----GVTFEfaqKFTEPRMT 228
Cdd:cd03894 217 DPPFDPPYPT-LNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEfpeaGIEVE---PLFEVPGL 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907194533 229 PTDDSDPWWAAFSGACKamnlTLEPEIFPAATDSRFIRAVGIPALGFSP 277
Cdd:cd03894 293 ETDEDAPLVRLAAALAG----DNKVRTVAYGTEAGLFQRAGIPTVVCGP 337
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
4-304 |
5.16e-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: 77.85 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEAFKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKrpefQALRAG 83
Cdd:cd03873 31 NRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGSGGGKGLLSK----FLLAED 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 84 FVLDEglanptdaftVFYSERSPWWvqvtsTGKPGHASRFiedtaaeklhkvissilafrekerqrlqanphlkegavts 163
Cdd:cd03873 107 LKVDA----------AFVIDATAGP-----ILQKGVVIRN---------------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 164 vnltkleggvaynvvpatmsasfdfrvapdvdmkafekqlqrwcqeagegvtfefaqkfteprmtptddsdPWWAAFSGA 243
Cdd:cd03873 132 -----------------------------------------------------------------------PLVDALRKA 140
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907194533 244 CKAMNLTL-EPEIFPAATDSRFIRAVGIPALGFSPMnrTPVLLHDHNERLHEDIFLRGVDIY 304
Cdd:cd03873 141 AREVGGKPqRASVIGGGTDGRLFAELGIPGVTLGPP--GDKGAHSPNEFLNLDDLEKATKVY 200
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
4-86 |
1.58e-16 |
|
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: 76.70 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEAFKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKRPEFQALRAG 83
Cdd:cd18669 31 PRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEEVGSGAGKGLLSKDALEEDLKVD 110
|
...
gi 1907194533 84 FVL 86
Cdd:cd18669 111 YLF 113
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
2-298 |
5.39e-16 |
|
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: 77.98 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAFKDsEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGmelfvkrpefqalr 81
Cdd:cd02697 89 DGWTRDPYGAVVE-DGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGELG-------------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 82 AGFVLDEGLANPTDA------FTVFYSERSPWWVQVTSTGKPGHASrfIEDTAAEKLH---KVISSILAFREKERQRLQA 152
Cdd:cd02697 154 PGWLLRQGLTKPDLLiaagfsYEVVTAHNGCLQMEVTVHGKQAHAA--IPDTGVDALQgavAILNALYALNAQYRQVSSQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 153 NPHLKEgavTSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQEAGE---GVTFEFAQKFTEPRMTP 229
Cdd:cd02697 232 VEGITH---PYLNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAAsmpGISVDIRRLLLANSMRP 308
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194533 230 TDDSDPW--------WAAFSGACKAMNLtlepeifPAATDSRFIRAVGIPALGFSPMNRTpvLLHDHNERLHEDIFL 298
Cdd:cd02697 309 LPGNAPLveaiqthgEAVFGEPVPAMGT-------PLYTDVRLYAEAGIPGVIYGAGPRT--VLESHAKRADERLQL 376
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
4-308 |
1.61e-14 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 73.38 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHkGMELFVKrpefqalrAG 83
Cdd:PRK08588 79 WTYDPFEL-TEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGEL-GAKQLTE--------KG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 84 FVLD-EGL--ANPTDAFtVFYSERSPWWVQVTSTGKPGHASrfiedtAAEKLHKVISSILAFREKERQRL----QANPHL 156
Cdd:PRK08588 149 YADDlDALiiGEPSGHG-IVYAHKGSMDYKVTSTGKAAHSS------MPELGVNAIDPLLEFYNEQKEYFdsikKHNPYL 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 157 keGAVTSVNlTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQ----RWCQEAGEGVTFEFAQKFtEPRMTpTDD 232
Cdd:PRK08588 222 --GGLTHVV-TIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQeiinEVNQNGAAQLSLDIYSNH-RPVAS-DKD 296
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907194533 233 SDPWWAAFSGACKAMNLTLEPEIFPAATD-SRFIRAV-GIPALGFSP-MNRTPvllHDHNERLHEDIFLRGVDIYTGLL 308
Cdd:PRK08588 297 SKLVQLAKDVAKSYVGQDIPLSAIPGATDaSSFLKKKpDFPVIIFGPgNNLTA---HQVDEYVEKDMYLKFIDIYKEII 372
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
14-308 |
5.18e-14 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 71.70 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 14 DSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTihMTFVPDEEVGGHK-GME-LFVKRPEFQALRAGFVLDegla 91
Cdd:cd05647 76 EEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLT--LIFYDCEEVAAELnGLGrLAEEHPEWLAADFAVLGE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 92 nPTDAfTVFYSERSPWWVQVTSTGKPGHASR-FIEDTAAEKLHKVISSILAFREKE--------RQRLqanphlkegavt 162
Cdd:cd05647 150 -PTDG-TIEGGCQGTLRFKVTTHGVRAHSARsWLGENAIHKLAPILARLAAYEPRTvnidgltyREGL------------ 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 163 svNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLqrwcQEAGEGVTFEFAQKFTEPRMTPTDDSdPWWAAFSG 242
Cdd:cd05647 216 --NAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHV----REVFEGLGYEIEVTDLSPGALPGLDH-PVARDLIE 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194533 243 ACKAmnltlEPEIFPAATD-SRFiRAVGIPALGFSPMNrtPVLLHDHNERLHEDIFLRGVDIYTGLL 308
Cdd:cd05647 289 AVGG-----KVRAKYGWTDvARF-SALGIPAVNFGPGD--PLLAHKRDEQVPVEQITACAAILRRWL 347
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
4-272 |
2.08e-13 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 70.26 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEA-FKDseGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGME-LFVKRPEfqalr 81
Cdd:PRK13983 96 WETDPFKPvVKD--GKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYGIQyLLKKHPE----- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 82 aGF-------VLDEGlaNPTDAFtVFYSERSPWWVQVTSTGKPGHASRfiEDTAAEKLHKVISSILAFREKERQRLQANP 154
Cdd:PRK13983 169 -LFkkddlilVPDAG--NPDGSF-IEIAEKSILWLKFTVKGKQCHAST--PENGINAHRAAADFALELDEALHEKFNAKD 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 155 HLKEGAVTSVNLTKLEGGV-AYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWC----QEAGEGVTFEFAQKFTEPrmTP 229
Cdd:PRK13983 243 PLFDPPYSTFEPTKKEANVdNINTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIAdefeEEYGVKIEVEIVQREQAP--PP 320
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907194533 230 TDDSDPWWAAFSGACKAMnLTLEPEI--FPAATDSRFIRAVGIPA 272
Cdd:PRK13983 321 TPPDSEIVKKLKRAIKEV-RGIEPKVggIGGGTVAAFLRKKGYPA 364
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
2-308 |
3.48e-13 |
|
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349886 [Multi-domain] Cd Length: 366 Bit Score: 69.46 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAfKDSEGYIYARGSQDMKSvSIQ-YLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVkrpefQAL 80
Cdd:cd03891 72 EGWSSDPFSP-TIKDGMLYGRGAADMKG-GIAaFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVL-----EWL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 81 RA-GFVLDEGL-ANPTdaftvfySE-----------RSPWWVQVTSTGKPGHASrfIEDTAAEKLHKVISSILAFreker 147
Cdd:cd03891 145 KArGEKIDYCIvGEPT-------SEkklgdtikigrRGSLNGKLTIKGKQGHVA--YPHLADNPIHLLAPILAEL----- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 148 qrlqANPHLKEG----AVTSVNLTKLEGGV-AYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQEAGEGVTFEFAQKf 222
Cdd:cd03891 211 ----TATVLDEGneffPPSSLQITNIDVGNgATNVIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLS- 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 223 TEPRMTPTDD-SDpwwaAFSGACKAmNLTLEPEIfpaAT-----DSRFIRAVGIPALGFSPMNRTpvlLHDHNERLH-ED 295
Cdd:cd03891 286 GEPFLTKPGKlVD----AVSAAIKE-VTGITPEL---STsggtsDARFIASYGCPVVEFGLVNAT---IHKVNERVSvAD 354
|
330
....*....|...
gi 1907194533 296 IfLRGVDIYTGLL 308
Cdd:cd03891 355 L-EKLTDIYERIL 366
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
4-290 |
3.59e-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 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: 69.41 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGME-LFVKRPEFQALRA 82
Cdd:cd05650 89 WETDPWEP-VVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEYGIQyLLNKFDLFKKDDL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 83 GFVLDEGlaNPTDAFtVFYSERSPWWVQVTSTGKPGHASRfiEDTAAEKLHKVISSILAFREKERQRLQANPHLKEGAVT 162
Cdd:cd05650 168 IIVPDFG--TEDGEF-IEIAEKSILWIKVNVKGKQCHAST--PENGINAFVAASNFALELDELLHEKFDEKDDLFNPPYS 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 163 SVNLTKLEGGVA-YNVVPATMSASFDFRVAP--DVD--MKAFEKQLQRWCQEAGEGVTFEFAQKFTEPRMTPtDDSDPWW 237
Cdd:cd05650 243 TFEPTKKEANVPnVNTIPGYDVFYFDCRVLPtyKLDevLKFVNKIISDFENSYGAGITYEIVQKEQAPPATP-EDSEIVV 321
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907194533 238 AAFSGACKAMNLTLEPEIFPAATDSRFIRAVGIPALGFSPMNRTPvllHDHNE 290
Cdd:cd05650 322 RLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETA---HQPNE 371
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
4-308 |
6.62e-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 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: 68.49 E-value: 6.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGhrfPRTIHMTFV--PDEEVGGHKGMELFvkRPEFQALR 81
Cdd:cd05651 73 WTKDPFEP-VEKGGKLYGLGSNDAGASVVSLLATFLHLYSEG---PLNYNLIYAasAEEEISGKNGIESL--LPHLPPLD 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 82 AGFVLDEGLANPTDAftvfysERSPWWVQVTSTGKPGHASRFIEDTAaekLHKVISSILAFREKERQRlqANPHLkeGAV 161
Cdd:cd05651 147 LAIVGEPTEMQPAIA------EKGLLVLDCTARGKAGHAARNEGDNA---IYKALDDIQWLRDFRFDK--VSPLL--GPV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 162 TsVNLTKLEGGVAYNVVPATMSASFDFRVAPdvdmkAFEKQLqrwcqeagegvTFEFAQKFTEPRMTP---------TDD 232
Cdd:cd05651 214 K-MTVTQINAGTQHNVVPDSCTFVVDIRTTE-----AYTNEE-----------IFEIIRGNLKSEIKPrsfrlnssaIPP 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194533 233 SDPwwaaFSGACKAMNLTlePEIFPAATDSRFIravGIPA--LGFSPMNRTpvllHDHNERLHEDIFLRGVDIYTGLL 308
Cdd:cd05651 277 DHP----IVQAAIAAGRT--PFGSPTLSDQALM---PFPSvkIGPGDSSRS----HTADEFIELSEIEEGIDIYIELL 341
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
2-293 |
1.53e-12 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 67.72 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMelfvkrpefQALR 81
Cdd:PRK06837 115 DLWSRPPFDP-VIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEESTGNGAL---------STLQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 82 AGFVLDEGL-ANPTDAfTVFYSERSPWWVQVTSTGKPGHASRfiEDTAAEKLHKVISSILAFREKER---QRLQANPHLK 157
Cdd:PRK06837 185 RGYRADACLiPEPTGE-KLVRAQVGVIWFRLRVRGAPVHVRE--AGTGANAIDAAYHLIQALRELEAewnARKASDPHFE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 158 EGA-VTSVNLTKLEGGVAYNVVPAtmSASFDFRVA--PDVDMKAFEKQLQRWCQEAGEGVTF--------EFAQKFTEPR 226
Cdd:PRK06837 262 DVPhPINFNVGIIKGGDWASSVPA--WCDLDCRIAiyPGVTAADAQAEIEACLAAAARDDRFlsnnppevVWSGFLAEGY 339
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907194533 227 MtpTDDSDPWWAAFSGACKAMNLT-LEPEIFPAATDSRF-IRAVGIPALGFSPMNRTPvllHDHNERLH 293
Cdd:PRK06837 340 V--LEPGSEAEAALARAHAAVFGGpLRSFVTTAYTDTRFyGLYYGIPALCYGPSGEGI---HGFDERVD 403
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
101-215 |
3.04e-12 |
|
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: 62.36 E-value: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 101 YSERSPWWVQVTSTGKPGHASRF-IEDTAAEKLHKVISSILAFREKERQRLQAnphlkegavTSVNLTKLEGGVAYNVVP 179
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPgKGVNAIKLLARLLAELPAEYGDIGFDFPR---------TTLNITGIEGGTATNVIP 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 1907194533 180 ATMSASFDFRVAPDVDMKAFEKQLQRWCQEAGEGVT 215
Cdd:pfam07687 72 AEAEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
11-312 |
9.87e-12 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 65.19 E-value: 9.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 11 AFKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFvkrpEFQALRAGFVL---- 86
Cdd:PRK07473 97 PWRREGNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFTPDEEVGTPSTRDLI----EAEAARNKYVLvpep 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 87 ---DEGLANPTDAFTVFyserspwwvQVTSTGKPGHasrfiedtAAEKLHKVISSIlafREKERQRLQANPHLKEGAVTS 163
Cdd:PRK07473 173 grpDNGVVTGRYAIARF---------NLEATGRPSH--------AGATLSEGRSAI---REMARQILAIDAMTTEDCTFS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 164 VNLtkLEGGVAYNVVPATMSA---SFDFRVApDVDmKAFEKQLQrwCQEAGEGVTFEFAQKFTEPRMTPTDDSDPWWAAF 240
Cdd:PRK07473 233 VGI--VHGGQWVNCVATTCTGealSMAKRQA-DLD-RGVARMLA--LSGTEDDVTFTVTRGVTRPVWEPDAGTMALYEKA 306
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907194533 241 SGACKAMNLTLEPEIFPAATDSRFIRAVGIPAL-GFSPMNRTPvllHDHNERLHEDIFLRGVDIYTGLLSALA 312
Cdd:PRK07473 307 RAIAGQLGLSLPHGSAGGGSDGNFTGAMGIPTLdGLGVRGADY---HTLNEHIEVDSLAERGRLMAGLLATLE 376
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
4-172 |
7.38e-11 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 62.47 E-value: 7.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEAFKDsEGYIYARGSQDMK---SVSIQYLEAVRRlksEGHRFPRTIHMTFVPDEEVGGHKGMELFVKRPEFQAL 80
Cdd:PRK13013 102 WTRDPFGGEVK-DGRIYGRGACDMKgglAASIIAAEAFLA---VYPDFAGSIEISGTADEESGGFGGVAYLAEQGRFSPD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 81 RAGFVLdegLANPTDAFTVFYSERSPWWVQVTSTGKPGHASR-FIEDTAAEKLHKVISsilAFREKERQRLQ----ANPH 155
Cdd:PRK13013 178 RVQHVI---IPEPLNKDRICLGHRGVWWAEVETRGRIAHGSMpFLGDSAIRHMGAVLA---EIEERLFPLLAtrrtAMPV 251
|
170
....*....|....*...
gi 1907194533 156 LKEGAVTS-VNLTKLEGG 172
Cdd:PRK13013 252 VPEGARQStLNINSIHGG 269
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-195 |
1.42e-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. 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: 61.52 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 13 KDSEGYIYARGSQDMK-SVSIQYLeAVRRLKSEGHRFPRTIHMTFVPDEEVGGHkGM----ELFVKRPEfqalrAGFVld 87
Cdd:cd05652 79 SDGGDTIYGRGSVDAKgSVAAQII-AVEELLAEGEVPEGDLGLLFVVGEETGGD-GMkafnDLGLNTWD-----AVIF-- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 88 eglANPTD-----------AFTVfyserspwwvqvTSTGKPGHaSRFIE------DTAAEKLHKVISSILAFREKErqrl 150
Cdd:cd05652 150 ---GEPTElklasghkgmlGFKL------------TAKGKAGH-SGYPWlgisaiEILVEALVKLIDADLPSSELL---- 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907194533 151 qanphlkeGAvTSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVD 195
Cdd:cd05652 210 --------GP-TTLNIGRISGGVAANVVPAAAEASVAIRLAAGPP 245
|
|
| PRK06915 |
PRK06915 |
peptidase; |
4-212 |
3.62e-10 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 60.48 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMelfvkrpefQALRAG 83
Cdd:PRK06915 113 WDHHPYSG-EVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEESGGAGTL---------AAILRG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 84 FVLDEGL-ANPTDaFTVFYSERSPWWVQVTSTGKPGH-ASRFIEDTAAEKLHKVISSILAFREKERQRLqANPHLKEGAV 161
Cdd:PRK06915 183 YKADGAIiPEPTN-MKFFPKQQGSMWFRLHVKGKAAHgGTRYEGVSAIEKSMFVIDHLRKLEEKRNDRI-TDPLYKGIPI 260
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907194533 162 -TSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQEAGE 212
Cdd:PRK06915 261 pIPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAELND 312
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
2-311 |
8.73e-10 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 59.24 E-value: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFE-AFKDseGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGG---HKGMELFVKRpef 77
Cdd:cd05680 81 ELWTSPPFEpVVRD--GRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIGSpslPAFLEENAER--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 78 qaLRAGFVL--DEGLANPtDAFTVFYSERSPWWVQVTSTG--KPGHASRF--IEDTAAEKLHKVISS---------ILAF 142
Cdd:cd05680 156 --LAADVVLvsDTSMWSP-DTPTITYGLRGLAYLEISVTGpnRDLHSGSYggAVPNPANALARLLASlhdedgrvaIPGF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 143 REK-------ERQRLQANPHLKEGAVTSVNLTKLEGGVAYN---------------------------VVPATMSASFDF 188
Cdd:cd05680 233 YDDvrpltdaEREAWAALPFDEAAFKASLGVPALGGEAGYTtlerlwarptldvngiwggyqgegsktVIPSKAHAKISM 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 189 RVAPDVDMKAFEKQLQRWCQE-AGEGVTFEFAQKF-TEPRMTPTDdsDPWWAAFSGACKamnltlepEIFpaATDSRFIR 266
Cdd:cd05680 313 RLVPGQDPDAIADLLEAHLRAhAPPGVTLSVKPLHgGRPYLVPTD--HPALQAAERALE--------EAF--GKPPVFVR 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907194533 267 AVG-IPALG-FSPMNRTPVLL----------HDHNERLHEDIFLRGVDIYTGLLSAL 311
Cdd:cd05680 381 EGGsIPIVAlFEKVLGIPTVLmgfglpddaiHAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
17-292 |
5.18e-09 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 56.69 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 17 GYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIhmTFVPDEEVGGhKGMELFVKRpeFQALRAgFVLDeglanPTDa 96
Cdd:PRK08652 78 VYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGI--AFVSDEEEGG-RGSALFAER--YRPKMA-IVLE-----PTD- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 97 FTVFYSERSPWWVQVTSTGKPGHASrfIEDTAAEKLHKVISSILAFREKErqrlqanPHLKEGAVTSVNLTKLEGGVAYN 176
Cdd:PRK08652 146 LKVAIAHYGNLEAYVEVKGKPSHGA--CPESGVNAIEKAFEMLEKLKELL-------KALGKYFDPHIGIQEIIGGSPEY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 177 VVPATMSASFDFRVAPDVDMKAFEKQLQRWCQEAGEGVTF-EFAQKFTeprmtpTDDSDPWWAAFSGACKAMNLTLEPEI 255
Cdd:PRK08652 217 SIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEYtEIWDGFE------LDEDEEIVQLLEKAMKEVGLEPEFTV 290
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907194533 256 FPAATDSRFIRAVGIPALGFSPMNRTpvLLHDHNERL 292
Cdd:PRK08652 291 MRSWTDAINFRYNGTKTVVWGPGELD--LCHTKFERI 325
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
2-221 |
7.40e-09 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 56.62 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAFKDsEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGhKGMELFVKRPEFQALr 81
Cdd:TIGR01887 83 DGWTSPPFEPTIK-DGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEESGW-KCIDYYFEHEEMPDI- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 82 aGFVldeglanPTDAFTVFYSERSPWWVQVTSTGKPGHasrfiedtaaeklhkvissilafrekerqrlqanphlkegav 161
Cdd:TIGR01887 160 -GFT-------PDAEFPIIYGEKGITTLEIKFKDDTEG------------------------------------------ 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907194533 162 tSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAF----EKQLQRWCQEAGEGVTFEFAQK 221
Cdd:TIGR01887 190 -DVVLESFKAGEAYNMVPDHATAVISGKKLTEVEQLKFvffiAKELEGDFEVNDGTLTITLEGK 252
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
4-125 |
2.93e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 54.70 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEA-FKDseGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVgGHKGMELFVKRPEfqalra 82
Cdd:PRK07205 95 WQTPPFEAvEKD--GCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGTDEET-LWRCMNRYNEVEE------ 165
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1907194533 83 gfVLDEGLAnPTDAFTVFYSERSpwWVQVTSTGkPGHASRFIE 125
Cdd:PRK07205 166 --QATMGFA-PDSSFPLTYAEKG--LLQAKLVG-PGSDQLELE 202
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
13-311 |
5.41e-08 |
|
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: 53.51 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 13 KDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHrfpRTIHMTFVPDEEVGGHKGMELFVKRPEFQALRAGfvldeglaN 92
Cdd:cd05653 73 RVEGGVLYGRGAVDAKGPLAAMILAASALNEELG---ARVVVAGLVDEEGSSKGARELVRRGPRPDYIIIG--------E 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 93 PTDAFTVFYSERSPWWVQVTSTGKPGHASRfIEDTAAEKLHKVISSILafrekerqRLQANPHLKEGAVTSVNLTKLEGG 172
Cdd:cd05653 142 PSGWDGITLGYRGSLLVKIRCEGRSGHSSS-PERNAAEDLIKKWLEVK--------KWAEGYNVGGRDFDSVVPTLIKGG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 173 VAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQEAGEGVTfefaqKFTEPRMTPTDdsDPWWAAFSGACKAMNltLE 252
Cdd:cd05653 213 ESSNGLPQRAEATIDLRLPPRLSPEEAIALATALLPTCELEFI-----DDTEPVKVSKN--NPLARAFRRAIRKQG--GK 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907194533 253 PEIFPAATDSRF---IRAVGIPALGFSPMNrtPVLLHDHNERLHEDIFLRGVDIYTGLLSAL 311
Cdd:cd05653 284 PRLKRKTGTSDMnvlAPLWTVPIVAYGPGD--STLDHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
2-169 |
5.48e-08 |
|
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: 53.79 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAFKDsEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGhKGMELFVKR---PEFq 78
Cdd:cd03888 87 EGWTTDPFKPVIK-DGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGW-KCIEHYFEHeeyPDF- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 79 alraGFVLDeglANptdaFTVFYSERSPWWVQVTSTGKPGHASRFIEDTAAEKLHKV---ISSILAFREKERQRLQANPH 155
Cdd:cd03888 164 ----GFTPD---AE----FPVINGEKGIVTVDLTFKIDDDKGYRLISIKGGEATNMVpdkAEAVIPGKDKEELALSAATD 232
|
170
....*....|....
gi 1907194533 156 LKEGAVTSVNLTKL 169
Cdd:cd03888 233 LKGNIEIDDGGVEL 246
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
1-311 |
6.20e-08 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 53.58 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 1 MEHWHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHR-FPRTIHMTFVPDEEV-GGHKGMELFVK---RP 75
Cdd:cd05649 69 IDNWKFDPYEG-YETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLRdFAYTILVAGTVQEEDcDGVCWQYISKAdkiKP 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 76 EFqalragFVLDEglanPTDAfTVFYSERSPWWVQVTSTGKPGHAS---RfiEDTAAEKLHKVISSILAFREkerqRLQA 152
Cdd:cd05649 148 DF------VVSGE----PTDG-NIYRGQRGRMEIRVDTKGVSCHGSapeR--GDNAVYKMADIIQDIRQLNP----NFPE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 153 NPHLKEGAVTSVNLTKLEGGVayNVVPATMSASFDFRVAPDVDMKAFEKQLQRW--CQEAGEGVTFEFAQkFTEPRMT-- 228
Cdd:cd05649 211 APFLGRGTLTVTDIFSTSPSR--CAVPDSCRISIDRRLTVGETWEGCLEEIRALpaVKKYGDDVAVSMYN-YDRPSYTge 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 229 --PTDDSDPWWA---------AFSGACKAMNLTlEPEI--FPAATDSRFI--RAvGIPALGFSPMNRtpVLLHDHNERLH 293
Cdd:cd05649 288 vyESERYFPTWLlpedhelvkALLEAYKALFGA-RPLIdkWTFSTNGVSImgRA-GIPCIGFGPGAE--NQAHAPNEYTW 363
|
330
....*....|....*...
gi 1907194533 294 EDIFLRGVDIYTGLLSAL 311
Cdd:cd05649 364 KEDLVRCAAGYAAIPTSY 381
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
4-234 |
1.91e-07 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 52.11 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEAFKDsEGYIYARGSQDMK----SVsiqyLEAVRRLKSEGHRFPrtIHMTFVPDEEVG--GHKGM--ELfvkrP 75
Cdd:PRK07522 83 WTSDPFRLTER-DGRLYGRGTCDMKgfiaAA----LAAVPELAAAPLRRP--LHLAFSYDEEVGclGVPSMiaRL----P 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 76 EFQALRAGFVLDEglanPTD-----------AFtvfyserspwwvQVTSTGKPGHASRfiEDTAAEKLHkVISSILAFRE 144
Cdd:PRK07522 152 ERGVKPAGCIVGE----PTSmrpvvghkgkaAY------------RCTVRGRAAHSSL--APQGVNAIE-YAARLIAHLR 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 145 KERQRLQANPHLKEG---AVTSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQE--------AGEG 213
Cdd:PRK07522 213 DLADRLAAPGPFDALfdpPYSTLQTGTIQGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAellpemraVHPE 292
|
250 260
....*....|....*....|.
gi 1907194533 214 VTFEFAQKFTEPRMTPTDDSD 234
Cdd:PRK07522 293 AAIEFEPLSAYPGLDTAEDAA 313
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
35-312 |
7.59e-07 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 50.05 E-value: 7.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 35 LEAVRRLKSEG--HRfprTIHMTFVPDEEVGGHkGMELF-VKRpeFQAlRAGFVLDEGlanPTDAFTV--FYSERspwwV 109
Cdd:COG2195 109 LAALEYLKEPEipHG---PIEVLFTPDEEIGLR-GAKALdVSK--LGA-DFAYTLDGG---EEGELEYecAGAAD----A 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 110 QVTSTGKPGHASrfiedTAAEKLhkvISSI-LAFrekerqRLQAnpHLKEGAV---TSVNLTKLEGGVAYNVVPATMSAS 185
Cdd:COG2195 175 KITIKGKGGHSG-----DAKEKM---INAIkLAA------RFLA--ALPLGRIpeeTEGNEGFIHGGSATNAIPREAEAV 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 186 FdfrVAPDVDMKAFEKQLQRW-------CQEAGEG-VTFEFAQKFtePRMTPTDDSDPwwaaFSGACKAM-NLTLEPEIF 256
Cdd:COG2195 239 Y---IIRDHDREKLEARKAELeeafeeeNAKYGVGvVEVEIEDQY--PNWKPEPDSPI----VDLAKEAYeELGIEPKIK 309
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 257 P--AATDSRFIRAVGIPALGFSP--MNrtpvlLHDHNERLHEDIFLRGVDIYTGLLSALA 312
Cdd:COG2195 310 PirGGLDGGILSFKGLPTPNLGPggHN-----FHSPDERVSIESMEKAWELLVEILKLIA 364
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
2-291 |
1.00e-06 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 49.70 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAfKDSEGYIYARGSQDMKSvSIQ-YLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVkrpefQAL 80
Cdd:PRK13009 76 EAWTSPPFEP-TIRDGMLYGRGAADMKG-SLAaFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVL-----EWL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 81 RA-GFVLD-----EglanPT------DA------------FTVfyserspwwvqvtsTGKPGHAS---RfiedtAAEKLH 133
Cdd:PRK13009 149 KArGEKIDycivgE----PTsterlgDVikngrrgsltgkLTV--------------KGVQGHVAyphL-----ADNPIH 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 134 KVIsSILAfrekerqRLqANPHLKEG----AVTSVNLTKLEGGV-AYNVVPATMSASFDFRVAPDVDmkafEKQLQRWCQ 208
Cdd:PRK13009 206 LAA-PALA-------EL-AATEWDEGneffPPTSLQITNIDAGTgATNVIPGELEAQFNFRFSTEHT----AESLKARVE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 209 E--AGEGVTFEFAQKFT-EPRMTPTDD-SDpwwaAFSGACKAMNlTLEPEIfpaAT-----DSRFIRAVGIPALGFSPMN 279
Cdd:PRK13009 273 AilDKHGLDYTLEWTLSgEPFLTPPGKlVD----AVVAAIEAVT-GITPEL---STsggtsDARFIADYGAQVVEFGPVN 344
|
330
....*....|..
gi 1907194533 280 RTpvlLHDHNER 291
Cdd:PRK13009 345 AT---IHKVNEC 353
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
5-225 |
1.05e-06 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 49.96 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 5 HHD-------PFEAFKD-SEGYIYARGSQDMKSVSIQYLEAVRRLksEGHRFPRTIHMTFV--PDEEVGGHKGMELFvkr 74
Cdd:PRK07338 100 HMDtvfpadhPFQTLSWlDDGTLNGPGVADMKGGIVVMLAALLAF--ERSPLADKLGYDVLinPDEEIGSPASAPLL--- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 75 PEFQA-LRAGFVLDEGLANPTDAftvfySER--SPWWvQVTSTGKPGHASRFIEDTaaeklhkvISSILAFREKErQRLQ 151
Cdd:PRK07338 175 AELARgKHAALTYEPALPDGTLA-----GARkgSGNF-TIVVTGRAAHAGRAFDEG--------RNAIVAAAELA-LALH 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907194533 152 ANPHLKEGavTSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQE--AGEGVTFEFAQKFTEP 225
Cdd:PRK07338 240 ALNGQRDG--VTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQvnQRHGVSLHLHGGFGRP 313
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
2-89 |
1.59e-06 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 49.26 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 2 EHWHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGhKGMELFVKrpEFQA-L 80
Cdd:cd05681 77 ELWTSDPFEL-TIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGS-PNLEKFVA--EHADlL 152
|
....*....
gi 1907194533 81 RAGFVLDEG 89
Cdd:cd05681 153 KADGCIWEG 161
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
1-277 |
1.67e-06 |
|
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: 49.01 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 1 MEHWHHDPFEAfKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRfpRTIHMTFVPDEEVGGhKGMElfvkrpefQAL 80
Cdd:cd08013 82 LDGYDGDPLSG-EIADGRVYGRGTLDMKGGLAACMAALADAKEAGLR--GDVILAAVADEEDAS-LGTQ--------EVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 81 RAGFVLDEGL-ANPTDaFTVFYSERSPWWVQVTSTGKPGHASRfiEDTAAEKLHKVISSILAFREKERQRLQANPHLKEG 159
Cdd:cd08013 150 AAGWRADAAIvTEPTN-LQIIHAHKGFVWFEVDIHGRAAHGSR--PDLGVDAILKAGYFLVALEEYQQELPERPVDPLLG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 160 AvTSVNLTKLEGGVAYNVVPATMSASFDFRVAPDVDMKAFEKQLQRWCQE-AGEGVTFefaqKFTEPRMT--------PT 230
Cdd:cd08013 227 R-ASVHASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTAILGElAQTVPNF----SYREPRITlsrppfevPK 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907194533 231 DdsdpwwAAFSG--ACKAMNLTLEPEIFPAA---TDSRFIRAVGIPALGFSP 277
Cdd:cd08013 302 E------HPFVQlvAAHAAKVLGEAPQIRSEtfwTDAALLAEAGIPSVVFGP 347
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
2-63 |
1.21e-05 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 46.57 E-value: 1.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907194533 2 EHWHHDPFEAFKDsEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVG 63
Cdd:PRK08596 95 EAWETNPFEPTIK-DGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEVG 155
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
1-313 |
1.55e-05 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 46.09 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 1 MEHWHHDPFEAFKDsEGYIYARGSQDMKS--VSIQYleAVRRLKSEGHRFPRTIHMT-FVPDEEVGGHKGMELFVK---R 74
Cdd:PRK13004 86 IKNWDFDPFEGEED-DGRIYGRGTSDQKGgmASMVY--AAKIIKDLGLDDEYTLYVTgTVQEEDCDGLCWRYIIEEdkiK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 75 PEFqalragFVLDEglanPTDaFTVFYSERSPWWVQVTSTGKPGHASR-FIEDTAAEKLHKVISSIlafrEKERQRLQAN 153
Cdd:PRK13004 163 PDF------VVITE----PTD-LNIYRGQRGRMEIRVETKGVSCHGSApERGDNAIYKMAPILNEL----EELNPNLKED 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 154 PHLKEGAVTsVNLTKLEGGVAyNVVPATMSASFDFRVAPDVDMKAFEKQLQ--RWCQEAGEGVTFefaQKFTEPRMT--- 228
Cdd:PRK13004 228 PFLGKGTLT-VSDIFSTSPSR-CAVPDSCAISIDRRLTVGETWESVLAEIRalPAVKKANAKVSM---YNYDRPSYTglv 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 229 -------PT---DDSDPWWAAFSGACKAMnLTLEPEI--FPAATDSRFI--RAvGIPALGFSPMNRTpvLLHDHNERLHE 294
Cdd:PRK13004 303 yptecyfPTwlyPEDHEFVKAAVEAYKGL-FGKAPEVdkWTFSTNGVSIagRA-GIPTIGFGPGKEP--LAHAPNEYTWK 378
|
330
....*....|....*....
gi 1907194533 295 DIFLRGVDIYTGLLSALAS 313
Cdd:PRK13004 379 EQLVKAAAMYAAIPKSLLK 397
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
1-89 |
1.81e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 45.90 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 1 MEHWHHDPFEA-FKDseGYIYARGSQDMKSVSIQYLEAVRRLKSEgHRFPRTIHMTFVPDEEVGGhKGMELFVKRPEfQA 79
Cdd:PRK06446 79 LSEWKRDPFSAtIEN--GRIYARGASDNKGTLMARLFAIKHLIDK-HKLNVNVKFLYEGEEEIGS-PNLEDFIEKNK-NK 153
|
90
....*....|
gi 1907194533 80 LRAGFVLDEG 89
Cdd:PRK06446 154 LKADSVIMEG 163
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
35-218 |
8.55e-05 |
|
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: 43.87 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 35 LEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHK----------------GMELFVKRPEFQ-ALRAGFvldegLANPTDAF 97
Cdd:TIGR01891 99 LGTAKLLKKLADLLEGTVRLIFQPAEEGGGGAtkmiedgvlddvdailGLHPDPSIPAGTvGLRPGT-----IMAAADKF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 98 TVFYserspwwvqvtsTGKPGHASRFIEDTAAekLHKVISSILAFREKERQRLQANphlkEGAVTSVnlTKLEGGVAYNV 177
Cdd:TIGR01891 174 EVTI------------HGKGAHAARPHLGRDA--LDAAAQLVVALQQIVSRNVDPS----RPAVVSV--GIIEAGGAPNV 233
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907194533 178 VPATMSASFDFRVAPDVDMKAFEKQLQRWCQEAGE--GVTFEF 218
Cdd:TIGR01891 234 IPDKASMSGTVRSLDPEVRDQIIDRIERIVEGAAAmyGAKVEL 276
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
4-87 |
2.04e-04 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 42.91 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFEA-FKDseGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEvGGHKGMELFVKR---PEFqa 79
Cdd:PRK07318 97 WDTDPYEPvIKD--GKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRFIVGTDEE-SGWKCMDYYFEHeeaPDF-- 171
|
....*...
gi 1907194533 80 lraGFVLD 87
Cdd:PRK07318 172 ---GFSPD 176
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
4-99 |
2.04e-04 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 42.58 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 4 WHHDPFE-AFKDSEG---YIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGhKGMELFVKRpEFQA 79
Cdd:PRK09104 102 WESPPFEpRIKETPDgrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEESGS-PSLVPFLEA-NAEE 179
|
90 100
....*....|....*....|...
gi 1907194533 80 LRAGFVL--DEGLANP-TDAFTV 99
Cdd:PRK09104 180 LKADVALvcDTGMWDReTPAITT 202
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
14-68 |
3.95e-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: 41.94 E-value: 3.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1907194533 14 DSEGYIYARGSQDMKSVSIQYLEAVRRLkSEGHRFPRTIHMTFVPDEEVgGHKGM 68
Cdd:cd05654 121 LSGEWLFGRGTMDMKSGLAVHLALLEQA-SEDEDFDGNLLLMAVPDEEV-NSRGM 173
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
35-205 |
4.31e-04 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 41.54 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 35 LEAVRRLKSEGHRFPRTIHMTFVPDEEVGGHKGMELFVKrpefQALRAGFVLDEGLANPTDAFTVFYSERSPWWVQVTst 114
Cdd:PRK06133 145 LHALKILQQLGFKDYGTLTVLFNPDEETGSPGSRELIAE----LAAQHDVVFSCEPGRAKDALTLATSGIATALLEVK-- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 115 GKPGHASrfiedtAAEKLHKVissilAFREKERQRLQANPHLKEGAVTSVNLTKLEGGVAYNVVPATMSASFDFRVAPDV 194
Cdd:PRK06133 219 GKASHAG------AAPELGRN-----ALYELAHQLLQLRDLGDPAKGTTLNWTVAKAGTNRNVIPASASAQADVRYLDPA 287
|
170
....*....|.
gi 1907194533 195 DMKAFEKQLQR 205
Cdd:PRK06133 288 EFDRLEADLQE 298
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
16-191 |
8.79e-04 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 40.54 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 16 EGY-IYARGSQDMKSVSIQYLEAVRRLKSEGHRfprtIHMTFVPDEEVGGHKGMELFVKRPEFQALRAGfvldeglaNPT 94
Cdd:PRK00466 81 EGEvIYGRGAVDAKGPLISMIIAAWLLNEKGIK----VMVSGLADEESTSIGAKELVSKGFNFKHIIVG--------EPS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 95 DAFTVFYSERSPWWVQVTSTGKPGHASRfIEDTAAEKLHKVISSILafrekERQRLQANPhlkegavtSVNLTKLEGGVA 174
Cdd:PRK00466 149 NGTDIVVEYRGSIQLDIMCEGTPEHSSS-AKSNLIVDISKKIIEVY-----KQPENYDKP--------SIVPTIIRAGES 214
|
170
....*....|....*..
gi 1907194533 175 YNVVPATMSASFDFRVA 191
Cdd:PRK00466 215 YNVTPAKLYLHFDVRYA 231
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
35-307 |
9.19e-04 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 40.66 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 35 LEAVRRLKSEGHRFPRTIHMTFVPDEEV-GGHKGM--ELFVKRPEFQALrAGFVLDEGLANPTDAFT---VFYSERSpww 108
Cdd:cd03886 98 LGAAKLLAERRDPLKGTVRFIFQPAEEGpGGAKAMieEGVLENPGVDAA-FGLHVWPGLPVGTVGVRsgaLMASADE--- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 109 VQVTSTGKPGHASR--FIED---TAAE---KLHKVISsilafrekeRQRLQANPHLkegavtsVNLTKLEGGVAYNVVP- 179
Cdd:cd03886 174 FEITVKGKGGHGASphLGVDpivAAAQivlALQTVVS---------RELDPLEPAV-------VTVGKFHAGTAFNVIPd 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 180 -ATMSA---SFDFRVAPDVDmKAFEKQLQRWCQEAGEGVTFEFAQkftepRMTPTDDSDPWWAAFSGACKAM---NLTLE 252
Cdd:cd03886 238 tAVLEGtirTFDPEVREALE-ARIKRLAEGIAAAYGATVELEYGY-----GYPAVINDPELTELVREAAKELlgeEAVVE 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907194533 253 PEIFPAATDSRFIrAVGIPA----LGFSPMNRTPVLLHDHNERLHEDIFLRGVDIYTGL 307
Cdd:cd03886 312 PEPVMGSEDFAYY-LEKVPGaffwLGAGEPDGENPGLHSPTFDFDEDALPIGAALLAEL 369
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
110-304 |
1.40e-03 |
|
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1L2 family 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 E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.
Pssm-ID: 349945 [Multi-domain] Cd Length: 366 Bit Score: 39.92 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 110 QVTSTGKPGHASrfIEDTAAEKLHKVISSILAFRekerQRLQANPHLKEGAVTSVnlTKLEGGVAYNVVPATMSASFDFR 189
Cdd:cd08660 174 EIVIKGKGGHAS--IPNNSIDPIAAAGQIISGLQ----SVVSRNISSLQNAVVSI--TRVQGGTAWNVIPDQAE*EGTVR 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 190 VAPDVDMKAFEKQLQRWC--QEAGEGVTFEFaqKFTEPRMTPTDDSDPWWAAFSGACKAM-NLTLEPEIFPAATDSRFIR 266
Cdd:cd08660 246 AFTKEARQAVPEH*RRVAegIAAGYGCQAEF--KWFPNGPSEVQNDGTLLNAFSKAAARLgYATVHAEQSPGSEDFALYQ 323
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907194533 267 AVgIPalGFSP---MNRTPVLLHDHNERLHEDIFLRGVDIY 304
Cdd:cd08660 324 EK-IP--GFFVw*gTNGRTEEWHHPAFRLDEEALTVGAQIF 361
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
3-74 |
4.40e-03 |
|
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.
Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 38.74 E-value: 4.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907194533 3 HWHHDPFEaFKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRFPRTIHMTFVPDEEVGGhKGMELFVKR 74
Cdd:cd05676 104 GWDTDPFE-LTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEGMEESGS-EGLDELIEA 173
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
2-70 |
6.64e-03 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 37.83 E-value: 6.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907194533 2 EHWHHDPFEaFKDSEGYIYARGSQDMKSVSIQYLEAVRRLKSEGHRfpRTIHMTFVPDEEVGGHKGMEL 70
Cdd:PRK08554 80 EEWNTEPFK-LTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLN--GKVIFAFTGDEEIGGAMAMHI 145
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
106-250 |
8.78e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 37.44 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907194533 106 PWWVQVTSTGKPGHA------SRfiED---TAAEklhkvisSILAFREKERQrlqanphLKEGAVTSV-NLTKLEGGVay 175
Cdd:PRK09290 215 QRRYRVTFTGEANHAgttpmaLR--RDallAAAE-------IILAVERIAAA-------HGPDLVATVgRLEVKPNSV-- 276
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907194533 176 NVVPATMSASFDFRvAPDVD-MKAFEKQLQRWCQE--AGEGVTFEFAQKFTEPrmtPTDDSDPWWAAFSGACKAMNLT 250
Cdd:PRK09290 277 NVIPGEVTFTLDIR-HPDDAvLDALVAELRAAAEAiaARRGVEVEIELISRRP---PVPFDPGLVAALEEAAERLGLS 350
|
|
| |
