|
Name |
Accession |
Description |
Interval |
E-value |
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
21-411 |
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: 761.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 21 EDPSVTLFREYLRLKTVHPEPDYDAALKFLERMAEELALPMKKVEVCPGRVVAIISWIGSRPELKSVVLNSHTDVVPVYE 100
Cdd:cd05646 1 EDPAVTRFREYLRINTVHPNPDYDACVEFLKRQADELGLPVRVIEVVPGKPVVVLTWEGSNPELPSILLNSHTDVVPVFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 101 EHWKHHPFAAVKDADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHKGMETFVKHPEFQKLN 180
Cdd:cd05646 81 EKWTHDPFSAHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGHDGMEKFVKTEEFKKLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 181 MGFALDEGLANPTNAYTVFYGERNPWWITVRCPGSPGHGSRFVENTAAEKLRRVINSFLEFREKENQRLNTSECFTLGDV 260
Cdd:cd05646 161 VGFALDEGLASPTEEYRVFYGERSPWWVVITAPGTPGHGSKLLENTAGEKLRKVIESIMEFRESQKQRLKSNPNLTLGDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 261 TTINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIKVWCREAGEDVTYDFAQKHMDQNLTSTDENDPWWQAFS 340
Cdd:cd05646 241 TTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGRGVTYEFEQKSPEKDPTSLDDSNPWWAAFK 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42542454 341 STCKAMNMTLKKEIFPAATDSRFIREVGLPAIGFSPMNLTPILLHDHNEYLNEQVFLQGIQVYERLIPALA 411
Cdd:cd05646 321 KAVKEMGLKLKPEIFPAATDSRYIRALGIPALGFSPMNNTPILLHDHNEFLNEDVFLRGIEIYEKIIPALA 391
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
21-413 |
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: 605.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 21 EDPSVTLFREYLRLKTVHPEPDYDAALKFLERMAEELALPMKKVEVCPGRVVAIISWIGSRPELKSVVLNSHTDVVPVYE 100
Cdd:TIGR01880 8 EDIAVTRFREYLRINTVQPNPDYAACVDFLIKQADELGLARKTIEFVPGKPVVVLTWPGSNPELPSILLNSHTDVVPVFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 101 EHWKHHPFAAVKDADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHKGMETFVKHPEFQKLN 180
Cdd:TIGR01880 88 EHWTHPPFSAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEKFAKTDEFKALN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 181 MGFALDEGLANPTNAYTVFYGERNPWWITVRCPGSPGHGSRFVENTAAEKLRRVINSFLEFREKENQRLNTSECFTLGDV 260
Cdd:TIGR01880 168 LGFALDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKLMENTAMEKLEKSVESIRRFRESQFQLLQSNPDLAIGDV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 261 TTINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIKVWCREAGEDVTYDFAQKHMDQNLTSTDENDPWWQAFS 340
Cdd:TIGR01880 248 TSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAGEGVTYEFSQHSGKPLVTPHDDSNPWWVAFK 327
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42542454 341 STCKAMNMTLKKEIFPAATDSRFIREVGLPAIGFSPMNLTPILLHDHNEYLNEQVFLQGIQVYERLIPALAGV 413
Cdd:TIGR01880 328 DAVKEMGCTFKPEILPGSTDSRYIRAAGVPALGFSPMNNTPVLLHDHNEFLNEAVFLRGIEIYQTLISALASV 400
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
20-412 |
1.37e-69 |
|
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: 224.76 E-value: 1.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 20 AEDPSVTLFREYLRLKTVhpEPDYDAALKFLERMAEELALPMKKVEVCPGRVVAIISWIGSRPElKSVVLNSHTDVVPVY 99
Cdd:COG0624 10 HLDEALELLRELVRIPSV--SGEEAAAAELLAELLEALGFEVERLEVPPGRPNLVARRPGDGGG-PTLLLYGHLDVVPPG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 100 E-EHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHkGMETFVKHpEFQK 178
Cdd:COG0624 87 DlELWTSDPFEPTIE-DGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSP-GARALVEE-LAEG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 179 LNMGFALDeglANPTNAYTVFYGERNPWWITVRCPGSPGHGSRF--VENtAAEKLRRVINSFLEFREkenqRLNTSECFt 256
Cdd:COG0624 164 LKADAAIV---GEPTGVPTIVTGHKGSLRFELTVRGKAAHSSRPelGVN-AIEALARALAALRDLEF----DGRADPLF- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 257 lgDVTTINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIKVWCREAGEDVTYDFAQKHMDQNLTSTDENDPWW 336
Cdd:COG0624 235 --GRTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEVEVLGDGRPPFETPPDSPLV 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42542454 337 QAFSSTCKA-MNMTLKKEIFPAATDSRFIREV-GLPAIGFSPMNLTpiLLHDHNEYLNEQVFLQGIQVYERLIPALAG 412
Cdd:COG0624 313 AAARAAIREvTGKEPVLSGVGGGTDARFFAEAlGIPTVVFGPGDGA--GAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
88-407 |
3.94e-56 |
|
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: 187.55 E-value: 3.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 88 VLNSHTDVVPVyEEHWkHHPFAAVKDadGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRfSRTIHLTFVPDEEvGGHKGM 167
Cdd:pfam01546 1 LLRGHMDVVPD-EETW-GWPFKSTED--GKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEE-GGMGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 168 ETFVKHPEFQKLNMGFALDEGLANPTN-----AYTVFYGERNPWWITVRCPGSPGHGSRF-VENTAAEKLRRVINSFLEF 241
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFGLHIGEPTLleggiAIGVVTGHRGSLRFRVTVKGKGGHASTPhLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 242 REKENQRLNTSecftlgDVTTINMTMVKGGVayNVVPAEMDVSFDLRIPPTVNLQEFEEKIKVWCREAGEDVTYDFAQKH 321
Cdd:pfam01546 155 VSRNVDPLDPA------VVTVGNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 322 MDQNLTSTDENDPWWQAFSSTCKAM---NMTLKKEIFPAATDSRFIREvGLPAIGFSpMNLTPILLHDHNEYLNEQVFLQ 398
Cdd:pfam01546 227 VEGGAPPLVNDSPLVAALREAAKELfglKVELIVSGSMGGTDAAFFLL-GVPPTVVF-FGPGSGLAHSPNEYVDLDDLEK 304
|
....*....
gi 42542454 399 GIQVYERLI 407
Cdd:pfam01546 305 GAKVLARLL 313
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
25-407 |
1.61e-47 |
|
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: 166.02 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 25 VTLFREYLRLKTVHPEPD-YDAALKFLERMAEELALPMKKVEVCPGR--VVAIISwiGSRPElKSVVLNSHTDVVPVYEE 101
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDnTSAIAAYIKLLLEDLGYPVELHEPPEEIygVVSNIV--GGRKG-KRLLFNGHYDVVPAGDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 102 H-WKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHKG----METFVKHPef 176
Cdd:cd08011 78 EgWTVDPYSGKIK-DGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGtkylLEKVRIKP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 177 qklnmGFALdegLANPTNAYTVFYGERNPWWITVRCPGSPGHGS-----RFVENTAAEKLRRVINSflefrekenqrlnt 251
Cdd:cd08011 155 -----NDVL---IGEPSGSDNIRIGEKGLVWVIIEITGKPAHGSlphrgESAVKAAMKLIERLYEL-------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 252 secftlgdVTTINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIKVwCREAGEDVTYDFAQKHmdqNLTSTDE 331
Cdd:cd08011 213 --------EKTVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIID-HLDSIEEVSFEIKSFY---SPTVSNP 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42542454 332 NDPWWQAFSSTCKAM-NMTLKKEIFPAATDSRFIREVGLPAIGFSPMNltPILLHDHNEYLNEQVFLQGIQVYERLI 407
Cdd:cd08011 281 DSEIVKKTEEAITEVlGIRPKEVISVGASDARFYRNAGIPAIVYGPGR--LGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
25-407 |
4.15e-45 |
|
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: 161.76 E-value: 4.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 25 VTLFREYLRLKTVHPEPDYDAALKFLERMAEELA-----LPMKKVEVCPGR--VVAIISwiGSRPELKSVVLNSHTDVVP 97
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTGSETRAAEVLAARLAeagiqTEIFVVESHPGRanLVARIG--GTDPSAGPLLLLGHIDVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 98 VYEEHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHKGMETFVK-HPE- 175
Cdd:cd05675 79 ADASDWSVDPFSGEIK-DGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDnHPEl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 176 FQklNMGFALDEG------LANPTNAYTVFYGERNPWWITVRCPGSPGHGSR-FVENTA---AEKLRRV----------- 234
Cdd:cd05675 158 FD--GATFALNEGgggslpVGKGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRpTDDNAItrlAEALRRLgahnfpvrltd 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 235 INSF----LEFREKENQRLNTSECFTLGDV----------------TTINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVN 294
Cdd:cd05675 236 ETAYfaqmAELAGGEGGALMLTAVPVLDPAlaklgpsapllnamlrNTASPTMLDAGYATNVLPGRATAEVDCRILPGQS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 295 LQEFEEKIKvwcREAGEDvtyDFAQKHMDQNLTSTDENDPwwqafsSTCKAMNMTLKKEI---------FPAATDSRFIR 365
Cdd:cd05675 316 EEEVLDTLD---KLLGDP---DVSVEAVHLEPATESPLDS------PLVDAMEAAVQAVDpgapvvpymSPGGTDAKYFR 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 42542454 366 EVGLPAIGFSPMNLTPIL-----LHDHNEYLNEQVFLQGIQVYERLI 407
Cdd:cd05675 384 RLGIPGYGFAPLFLPPELdytglFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
25-402 |
1.40e-44 |
|
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: 158.72 E-value: 1.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 25 VTLFREYLRLKTVHP-EPDYDAALKFLERMAEELALPMKKVEVCPGRV----VAIISWIGSRPElKSVVLNSHTDVVPVY 99
Cdd:TIGR01910 1 VELLKDLISIPSVNPpGGNEETIANYIKDLLREFGFSTDVIEITDDRLkvlgKVVVKEPGNGNE-KSLIFNGHYDVVPAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 100 E-EHWKHHPFAAVkDADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHkGMETFVKHPEFQK 178
Cdd:TIGR01910 80 DlELWKTDPFKPV-EKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEA-GTLYLLQRGYFKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 179 LNMGFaldegLANPTNAYTVFYGERNPWWITVRCPGSPGHGSR--FVENtAAEKLRRVINSFLEFREKENQRlnTSECFT 256
Cdd:TIGR01910 158 ADGVL-----IPEPSGGDNIVIGHKGSIWFKLRVKGKQAHASFpqFGVN-AIMKLAKLITELNELEEHIYAR--NSYGFI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 257 LGDVtTINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIKVWCREAG--EDVTYDFAQKhMDQN--LTSTDEN 332
Cdd:TIGR01910 230 PGPI-TFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSksDGWLYENEPV-VKWSgpNETPPDS 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 333 DPWWQAFSSTCKAMNMTLKKEIFPAATDSRFIREVGLPAIGFSPMNLTpiLLHDHNEYLNEQVFLQGIQV 402
Cdd:TIGR01910 308 RLVKALEAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPGDLE--TAHQVNEYISIKNLVESTKV 375
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
27-407 |
6.36e-44 |
|
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: 156.69 E-value: 6.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 27 LFREYLRLKTVhpEPDYDAALKFLermAEELA--LPMKKVEVCPGRVvAIISWIGSRPElKSVVLNSHTDVVPVYEEH-W 103
Cdd:cd08659 2 LLQDLVQIPSV--NPPEAEVAEYL---AELLAkrGYGIESTIVEGRG-NLVATVGGGDG-PVLLLNGHIDTVPPGDGDkW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 104 KHHPFAAvKDADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGhKGMETFVKHPEFQKLnmGF 183
Cdd:cd08659 75 SFPPFSG-RIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGS-DGARALLEAGYADRL--DA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 184 ALDeglANPTNaYTVFYGERNPWWITVRCPGSPGHGSR-FVENTAAEKLRRVINSFLEFRekenQRLNTSEcfTLGDvTT 262
Cdd:cd08659 151 LIV---GEPTG-LDVVYAHKGSLWLRVTVHGKAAHSSMpELGVNAIYALADFLAELRTLF----EELPAHP--LLGP-PT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 263 INMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIKVWCREAGEDVTYDFAqkHMDQNLTSTDENDPWWQAFSST 342
Cdd:cd08659 220 LNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVS--LDGDPPFFTDPDHPLVQALQAA 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42542454 343 CKAMNMTLKKEIFPAATDSRFI-REVGLPAIGFSPMNLTpiLLHDHNEYLNEQVFLQGIQVYERLI 407
Cdd:cd08659 298 ARALGGDPVVRPFTGTTDASYFaKDLGFPVVVYGPGDLA--LAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
20-412 |
8.33e-42 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 152.07 E-value: 8.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 20 AEDPSVTLFREYLRLKTVHPEP-DYDAALKFLERMAEELALPMKKVEV--------CPGRVvAIISWIGSRPelKSVVLN 90
Cdd:PRK08651 4 MMFDIVEFLKDLIKIPTVNPPGeNYEEIAEFLRDTLEELGFSTEIIEVpneyvkkhDGPRP-NLIARRGSGN--PHLHFN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 91 SHTDVVPVYEEHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRfsrTIHLTFVPDEEVGGhkgmeTF 170
Cdd:PRK08651 81 GHYDVVPPGEGWSVNVPFEPKVK-DGKVYGRGASDMKGGIAALLAAFERLDPAGDG---NIELAIVPDEETGG-----TG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 171 VKHpefqklnmgfaLDEGL---------ANPTNAYTVFYGERNPWWITVRCPGSPGHGSR-FVENTAAEKLRRVINSFLE 240
Cdd:PRK08651 152 TGY-----------LVEEGkvtpdyvivGEPSGLDNICIGHRGLVWGVVKVYGKQAHASTpWLGINAFEAAAKIAERLKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 241 F------REKENQRLNTSECFTLGDVTtinmtmVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEK----IKVWCREAG 310
Cdd:PRK08651 221 SlstiksKYEYDDERGAKPTVTLGGPT------VEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDElealLDEVAPELG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 311 EDVTY---DFAQKHMdqnltsTDENDPWWQAFSSTC-KAMNMTLKKEIFPAATDSRFIREVGLPAIGFSPMNLTpiLLHD 386
Cdd:PRK08651 295 IEVEFeitPFSEAFV------TDPDSELVKALREAIrEVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGELE--LAHA 366
|
410 420
....*....|....*....|....*.
gi 42542454 387 HNEYLNEQVFLQGIQVYERLIPALAG 412
Cdd:PRK08651 367 PDEYVEVKDVEKAAKVYEEVLKRLAK 392
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
30-412 |
1.01e-34 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 134.30 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 30 EYLRLKTV----HPEPDYDAALKFLERMAEELALPMKKVEVcpgRVVA----IISWIGSRPELKSVVLNSHTDVVPV--- 98
Cdd:PRK08262 52 EAIRFRTIsnrdRAEDDAAAFDALHAHLEESYPAVHAALER---EVVGghslLYTWKGSDPSLKPIVLMAHQDVVPVapg 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 99 YEEHWKHHPFAAVKdADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHkGMETFVKHPEFQK 178
Cdd:PRK08262 129 TEGDWTHPPFSGVI-ADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVGGL-GARAIAELLKERG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 179 LNMGFALDEGLANPTNAYTVF--------YGERNPWWITVRCPGSPGHGSRFVENTAAEKLRRVI-----NSF-LEFREK 244
Cdd:PRK08262 207 VRLAFVLDEGGAITEGVLPGVkkpvaligVAEKGYATLELTARATGGHSSMPPRQTAIGRLARALtrledNPLpMRLRGP 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 245 ENQRLNT--------------SECFTLGDV---------------TTINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNL 295
Cdd:PRK08262 287 VAEMFDTlapemsfaqrvvlaNLWLFEPLLlrvlakspetaamlrTTTAPTMLKGSPKDNVLPQRATATVNFRILPGDSV 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 296 QEFEEKIkvwcREAGEDVTYDFAQKHMDQ---NLTSTDenDPWWQAFSSTCkamnmtlkKEIFP----------AATDSR 362
Cdd:PRK08262 367 ESVLAHV----RRAVADDRVEIEVLGGNSepsPVSSTD--SAAYKLLAATI--------REVFPdvvvapylvvGATDSR 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 42542454 363 FIREVGLPAIGFSPMNLTP---ILLHDHNEYLNEQVFLQGIQVYERLIPALAG 412
Cdd:PRK08262 433 HYSGISDNVYRFSPLRLSPedlARFHGTNERISVANYARMIRFYYRLIENAAG 485
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
74-407 |
2.45e-32 |
|
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: 127.37 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 74 IISWIGSRPELKSVVLNSHTDVVPV---YEEHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRT 150
Cdd:cd05674 59 LYTWEGSDPSLKPLLLMAHQDVVPVnpeTEDQWTHPPFSGHYD-GGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 151 IHLTFVPDEEVGGHKGMETFVKHPEFQKLNMGFA--LDEGLAN-PTNAYTVFY-----GERN--PWWITVRCPGspGHGS 220
Cdd:cd05674 138 IILAFGHDEEVGGERGAGAIAELLLERYGVDGLAaiLDEGGAVlEGVFLGVPFalpgvAEKGymDVEITVHTPG--GHSS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 221 -------------------------RFVE-NTAAEKLR----------RVINSFLEFREKENQRLNTSECFTLGDV---- 260
Cdd:cd05674 216 vppkhtgigilseavaaleanpfppKLTPgNPYYGMLQclaehsplppRSLKSNLWLASPLLKALLASELLSTSPLtral 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 261 --TTINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIK-VWCREA----------GEDVTYDFAQKHMDQNLT 327
Cdd:cd05674 296 lrTTQAVDIINGGVKINALPETATATVNHRIAPGSSVEEVLEHVKnLIADIAvkyglglsafGGDVIYSTNGTKLLTSLL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 328 S------TDENDPWWQAFSSTCKAMNMTLKKE------IFPAATDSRFIREVGlPAI-GFSPMNLTPILL---HDHNEYL 391
Cdd:cd05674 376 SpepspvSSTSSPVWQLLAGTIRQVFEQFGEDlvvapgIMTGNTDTRHYWNLT-KNIyRFTPIRLNPEDLgriHGVNERI 454
|
410
....*....|....*.
gi 42542454 392 NEQVFLQGIQVYERLI 407
Cdd:cd05674 455 SIDDYLETVAFYYQLI 470
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
71-392 |
5.38e-28 |
|
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: 114.33 E-value: 5.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 71 VVAIISwiGSRPELKSVVLNSHTDVVPVYE-EHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSR 149
Cdd:cd03895 63 VVGTHR--PRGETGRSLILNGHIDVVPEGPvELWTRPPFEATIV-DGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 150 TIHLTFVPDEEVGGHKGMETFVKhpefqklnmGFALDEGL-ANPTNaYTVFYGERNPWWITVRCPGSPGHGSRFVENTAA 228
Cdd:cd03895 140 DVHFQSVVEEECTGNGALAALMR---------GYRADAALiPEPTE-LKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 229 -EKLRRVINSFLEFREKENQRLNTSECFtlGDV---TTINMTMVKGGVAYNVVPAEmdVSFDLRIP--PTVNLQEFEEKI 302
Cdd:cd03895 210 iEKAMHLIQALQELEREWNARKKSHPHF--SDHphpINFNIGKIEGGDWPSSVPAW--CVLDCRIGiyPGESPEEARREI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 303 KVWCREAgedVTYDFAQKHMDQNLT---------STDENDPWWQAFSSTCKAM-NMTLKKEIFPAATDSRFIREVG-LPA 371
Cdd:cd03895 286 EECVADA---AATDPWLSNHPPEVEwngfqaegyVLEPGSDAEQVLAAAHQAVfGTPPVQSAMTATTDGRFFVLYGdIPA 362
|
330 340
....*....|....*....|.
gi 42542454 372 IGFSPMNLTPillHDHNEYLN 392
Cdd:cd03895 363 LCYGPGSRDA---HGFDESVD 380
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
78-207 |
3.57e-27 |
|
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: 107.13 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 78 IGSRPELKSVVLNSHTDVVPVYEEHWKHHPFAAVKDADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVP 157
Cdd:cd18669 6 YGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTP 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 42542454 158 DEEVGGHKGMETFVK--HPEFQKLNMGFALDeglanPTNAYTVFYGERNPWW 207
Cdd:cd18669 86 DEEVGSGAGKGLLSKdaLEEDLKVDYLFVGD-----ATPAPQKGVGIRTPLV 132
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
87-407 |
5.72e-27 |
|
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: 110.76 E-value: 5.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 87 VVLNSHTDVVPVYEEHWKHHPFAAVkDADGNIYARGAQDMKSVTIQYIEAIRRLKAAgkRFSRTIHLTFVPDEEVG--GH 164
Cdd:cd03894 60 LLLSGHTDVVPVDGQKWSSDPFTLT-ERDGRLYGRGTCDMKGFLAAVLAAVPRLLAA--KLRKPLHLAFSYDEEVGclGV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 165 KGMetfvkhpefqklnmgfaLDEGLANPTNAYTVFYGErnP--------------WWITVRcpGSPGHGS---RFVenTA 227
Cdd:cd03894 137 RHL-----------------IAALAARGGRPDAAIVGE--PtslqpvvahkgiasYRIRVR--GRAAHSSlppLGV--NA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 228 AEKLRRVINSFLEFREKENQRLnTSECFTLGdVTTINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIKVWCR 307
Cdd:cd03894 194 IEAAARLIGKLRELADRLAPGL-RDPPFDPP-YPTLNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 308 EAGE-DVTY-DFAQKHMDQNLtSTDENDPWWQAFSSTCKamnmTLKKEIFPAATDSRFIREVGLPAIGFSPMNLTPIllH 385
Cdd:cd03894 272 ALLEfPEAGiEVEPLFEVPGL-ETDEDAPLVRLAAALAG----DNKVRTVAYGTEAGLFQRAGIPTVVCGPGSIAQA--H 344
|
330 340
....*....|....*....|...
gi 42542454 386 DHNEYLnEQVFLQ-GIQVYERLI 407
Cdd:cd03894 345 TPDEFV-ELEQLDrCEEFLRRLI 366
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
73-403 |
1.33e-26 |
|
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: 105.59 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 73 AIISWIGSRPELKSVVLNSHTDVVPVYEEHWKHHPFAAVKDADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIH 152
Cdd:cd03873 1 NLIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 153 LTFVPDEEVGGHKGMETFVKhpefqklnmgFALDEGLanptNAYTVFYGERNPWWITVRCPGSPGhgsrfventaaeklr 232
Cdd:cd03873 81 VAFTADEEVGSGGGKGLLSK----------FLLAEDL----KVDAAFVIDATAGPILQKGVVIRN--------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 233 rvinsflefrekenqrlntsecftlgdvttinmtmvkggvaynvvpaemdvsfdlripptvnlqefeekikvwcreaged 312
Cdd:cd03873 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 313 vtydfaqkhmdqnltstdendPWWQAFSSTCKAMNMTLKKEI-FPAATDSRFIREVGLPAIGFSPMnlTPILLHDHNEYL 391
Cdd:cd03873 132 ---------------------PLVDALRKAAREVGGKPQRASvIGGGTDGRLFAELGIPGVTLGPP--GDKGAHSPNEFL 188
|
330
....*....|..
gi 42542454 392 NEQVFLQGIQVY 403
Cdd:cd03873 189 NLDDLEKATKVY 200
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
25-381 |
7.48e-25 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 105.70 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 25 VTLFREYLRLKTV----HPEPDYDAALKFLERMAEELALPMKKVEVCPGRVVAIISWIGSRPELKSVVLNSHTDVVPVYE 100
Cdd:PRK07906 2 VDLCSELIRIDTTntgdGTGKGEREAAEYVAEKLAEVGLEPTYLESAPGRANVVARLPGADPSRPALLVHGHLDVVPAEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 101 EHWKHHPFAAVKdADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHKGMETFV-KHPE-FQK 178
Cdd:PRK07906 82 ADWSVHPFSGEI-RDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEAGGTYGAHWLVdNHPElFEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 179 LNM------GFALDegLANPTNAYTVFYGERNPWWITVRCPGSPGHGSRFVENTA----AEKLRRV------------IN 236
Cdd:PRK07906 161 VTEaisevgGFSLT--VPGRDRLYLIETAEKGLAWMRLTARGRAGHGSMVNDDNAvtrlAEAVARIgrhrwplvltptVR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 237 SFL---------EFREKENQ----RLNTSECF---TLGDvtTINMTMVKGGVAYNVVPAEMDVSFDLRIPPTvNLQEFEE 300
Cdd:PRK07906 239 AFLdgvaeltglEFDPDDPDallaKLGPAARMvgaTLRN--TANPTMLKAGYKVNVIPGTAEAVVDGRFLPG-REEEFLA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 301 KIKvwcREAGEDVTYDFAqkHMDQNLTSTDEndpwwqafSSTCKAMNMTLKKE---------IFPAATDSRFIREVGLPA 371
Cdd:PRK07906 316 TVD---ELLGPDVEREWV--HRDPALETPFD--------GPLVDAMNAALLAEdpgarvvpyMLSGGTDAKAFSRLGIRC 382
|
410
....*....|
gi 42542454 372 IGFSPMNLTP 381
Cdd:PRK07906 383 YGFAPLRLPP 392
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
48-408 |
8.14e-21 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 93.41 E-value: 8.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 48 KFLERMAEELALPMKKVEVCPGRVvAIISWIGS-RPELksvVLNSHTDVVPVYEEH-WKHHPFAAVKDaDGNIYARGAQD 125
Cdd:PRK08588 26 NYLQDLFAKHGIESKIVKVNDGRA-NLVAEIGSgSPVL---ALSGHMDVVAAGDVDkWTYDPFELTEK-DGKLYGRGATD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 126 MKS----VTIQYIEairrLKAAGKRFSRTIHLTFVPDEEVGGHkGMETFVKHpefqklnmGFALD-EGL--ANPTNaYTV 198
Cdd:PRK08588 101 MKSglaaLVIAMIE----LKEQGQLLNGTIRLLATAGEEVGEL-GAKQLTEK--------GYADDlDALiiGEPSG-HGI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 199 FYGERNPWWITVRCPGSPGHGSRFVENTAAeklrrvINSFLEFREKENQRLNT----SECftLGDvTTINMTMVKGGVAY 274
Cdd:PRK08588 167 VYAHKGSMDYKVTSTGKAAHSSMPELGVNA------IDPLLEFYNEQKEYFDSikkhNPY--LGG-LTHVVTIINGGEQV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 275 NVVPAEMDVSFDLRIPPTVN----LQEFEEKIKVWCREAGEDVTYDFaqkHMDQNLTSTDENDPWWQ-AFSSTCKAMNMT 349
Cdd:PRK08588 238 NSVPDEAELEFNIRTIPEYDndqvISLLQEIINEVNQNGAAQLSLDI---YSNHRPVASDKDSKLVQlAKDVAKSYVGQD 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42542454 350 LKKEIFPAATD-SRFIR-EVGLPAIGFSP-MNLTPillHDHNEYLNEQVFLQGIQVYERLIP 408
Cdd:PRK08588 315 IPLSAIPGATDaSSFLKkKPDFPVIIFGPgNNLTA---HQVDEYVEKDMYLKFIDIYKEIII 373
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
85-392 |
2.84e-20 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 92.37 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 85 KSVVLNSHTDVVPVY-EEHWKHHPFAAVKdADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGG 163
Cdd:PRK06837 98 RSLILQGHIDVVPEGpLDLWSRPPFDPVI-VDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEESTG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 164 HKGMET----------FVKHPEFQKL---NMGfaldeglanptnaytvfygernPWWITVRCPGSPGHGSRFVENTAA-E 229
Cdd:PRK06837 177 NGALSTlqrgyradacLIPEPTGEKLvraQVG----------------------VIWFRLRVRGAPVHVREAGTGANAiD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 230 KLRRVINSFLEFREKENQRLNTSECF-TLGDVTTINMTMVKGGVAYNVVPAEMDvsFDLRIP--PTVNLQEFEEKIKVWC 306
Cdd:PRK06837 235 AAYHLIQALRELEAEWNARKASDPHFeDVPHPINFNVGIIKGGDWASSVPAWCD--LDCRIAiyPGVTAADAQAEIEACL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 307 REAGED-----------VTYDFAQKHMDQnltstDENDPWWQAFSSTCKAMNMT-LKKEIFPAATDSRF-IREVGLPAIG 373
Cdd:PRK06837 313 AAAARDdrflsnnppevVWSGFLAEGYVL-----EPGSEAEAALARAHAAVFGGpLRSFVTTAYTDTRFyGLYYGIPALC 387
|
330
....*....|....*....
gi 42542454 374 FSPMNLTPillHDHNEYLN 392
Cdd:PRK06837 388 YGPSGEGI---HGFDERVD 403
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
27-412 |
5.77e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 91.60 E-value: 5.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 27 LFREYLRLKTVHPEPDYDAALkflERMAEEL---ALPMKKVEVCP-----GRVVAIisWIGSRPElKSVVLNSHTDVVPV 98
Cdd:PRK09133 42 LYKELIEINTTASTGSTTPAA---EAMAARLkaaGFADADIEVTGpyprkGNLVAR--LRGTDPK-KPILLLAHMDVVEA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 99 YEEHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHKGMETFV-KHPEFq 177
Cdd:PRK09133 116 KREDWTRDPFKLVEE-NGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEGTPMNGVAWLAeNHRDL- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 178 kLNMGFALDEG----LANPTNA--YTVFYGERNP--WWITVRCPGspGHGSRFVENTA----AEKLRRvINSFlEFREKE 245
Cdd:PRK09133 194 -IDAEFALNEGgggtLDEDGKPvlLTVQAGEKTYadFRLEVTNPG--GHSSRPTKDNAiyrlAAALSR-LAAY-RFPVML 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 246 N-----------------------------------QRLNTSECF--TLGdvTTINMTMVKGGVAYNVVPAEMDVSFDLR 288
Cdd:PRK09133 269 NdvtrayfkqsaaietgplaaamrafaanpadeaaiALLSADPSYnaMLR--TTCVATMLEGGHAENALPQRATANVNCR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 289 IPPTVNLQEFEEKIKvwcrEAGEdvtydfaqkhmDQNLTSTDENDP-----------WWQAFSSTCKAMNMTLKkeIFPA 357
Cdd:PRK09133 347 IFPGDTIEAVRATLK----QVVA-----------DPAIKITRIGDPspspasplrpdIMKAVEKLTAAMWPGVP--VIPS 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42542454 358 ----ATDSRFIREVGLPAIGFSPMNLTPILLHDH--NEYLNEQVFLQGIQVYERLIPALAG 412
Cdd:PRK09133 410 mstgATDGRYLRAAGIPTYGVSGLFGDPDDTFAHglNERIPVASFYEGRDFLYELVKDLAG 470
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
22-390 |
4.20e-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 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: 88.28 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 22 DPSVTLFREYLRLKTVHPEPD-------YDAALKFLERMA----EELALPMKKVEVCPGrvvaIISWIGSRpELKSVVLN 90
Cdd:cd05650 1 EEIIELERDLIRIPAVNPESGgegekekADYLEKKLREYGfytlERYDAPDERGIIRPN----IVAKIPGG-NDKTLWII 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 91 SHTDVVPVYE-EHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHKGMET 169
Cdd:cd05650 76 SHLDTVPPGDlSLWETDPWEPVVK-DGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEYGIQY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 170 FV-KHPEFQKLNMGFALDEGlaNPTNAyTVFYGERNPWWITVRCPGSPGHGSRfvENTAAEKLRRVINSFLEFREKENQR 248
Cdd:cd05650 155 LLnKFDLFKKDDLIIVPDFG--TEDGE-FIEIAEKSILWIKVNVKGKQCHAST--PENGINAFVAASNFALELDELLHEK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 249 LNTSECFTLGDVTTINMTMVKGGVA-YNVVPAEMDVSFDLRIPPTVN----LQEFEEKIKVWCREAGEDVTYDFAQKhmD 323
Cdd:cd05650 230 FDEKDDLFNPPYSTFEPTKKEANVPnVNTIPGYDVFYFDCRVLPTYKldevLKFVNKIISDFENSYGAGITYEIVQK--E 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42542454 324 QNLTSTDENDPWWQAFSSTCKAM-NMTLKKEIFPAATDSRFIREVGLPAIGFSPMNLTPillHDHNEY 390
Cdd:cd05650 308 QAPPATPEDSEIVVRLSKAIKKVrGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETA---HQPNEY 372
|
|
| PRK06915 |
PRK06915 |
peptidase; |
85-391 |
8.19e-17 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 81.66 E-value: 8.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 85 KSVVLNSHTDVVPVYE-EHWKHHPFAAVKdADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGG 163
Cdd:PRK06915 94 KSMILNGHIDVVPEGDvNQWDHHPYSGEV-IGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEESGG 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 164 HKGMETFVKhpefqklnmGFALDEGL-ANPTNAyTVFYGERNPWWITVRCPGSPGH-GSRFVENTAAEKLRRVINSFLEF 241
Cdd:PRK06915 173 AGTLAAILR---------GYKADGAIiPEPTNM-KFFPKQQGSMWFRLHVKGKAAHgGTRYEGVSAIEKSMFVIDHLRKL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 242 REKENQRLNTSECFTLGDVTTINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIKVWCREAGE--------DV 313
Cdd:PRK06915 243 EEKRNDRITDPLYKGIPIPIPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAELNDvdewfvehPV 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 314 TYDFAQKHMDQNltSTDENDPWWQAFSSTCKAMNMTL-KKEIFPAATDSRFIREVG-LPAIGFSPMnlTPILLHDHNEYL 391
Cdd:PRK06915 323 EVEWFGARWVPG--ELEENHPLMTTLEHNFVEIEGNKpIIEASPWGTDGGLLTQIAgVPTIVFGPG--ETKVAHYPNEYI 398
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
20-238 |
1.58e-16 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 80.96 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 20 AEDPSVTLFREYLRLKTVHPEPD-YDAALKFLER--MAEELALPMKKVEVCPG--------RVVAIISwiGSRPElKSVV 88
Cdd:PRK13013 12 RRDDLVALTQDLIRIPTLNPPGRaYREICEFLAArlAPRGFEVELIRAEGAPGdsetyprwNLVARRQ--GARDG-DCVH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 89 LNSHTDVVPVyEEHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHKGME 168
Cdd:PRK13013 89 FNSHHDVVEV-GHGWTRDPFGGEVK-DGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGGVA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42542454 169 TFVKHPEFQKLNMGFALdegLANPTNAYTVFYGERNPWWITVRCPGSPGHGSR-FVENTAAEKLRRVINSF 238
Cdd:PRK13013 167 YLAEQGRFSPDRVQHVI---IPEPLNKDRICLGHRGVWWAEVETRGRIAHGSMpFLGDSAIRHMGAVLAEI 234
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
49-321 |
3.28e-16 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 79.24 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 49 FLERMAEELALPMKKVEVCPGRVVAIISWIGSRPELKsVVLNSHTDVVPvyeehwkhhPF--AAVKDADGNIYARGAQDM 126
Cdd:cd05652 24 FLAEYLESLGFTVEKQPVENKDRFNVYAYPGSSRQPR-VLLTSHIDTVP---------PFipYSISDGGDTIYGRGSVDA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 127 K-SVTIQyIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHkGMETFVkhpefqklnmgfalDEGLANPTnayTVFYGErnP 205
Cdd:cd05652 94 KgSVAAQ-IIAVEELLAEGEVPEGDLGLLFVVGEETGGD-GMKAFN--------------DLGLNTWD---AVIFGE--P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 206 ------------WWITVRCPGSPGHgSRFVE--NTAAEKLRRVINSFlefrekENQRLNTSEcfTLGDvTTINMTMVKGG 271
Cdd:cd05652 153 telklasghkgmLGFKLTAKGKAGH-SGYPWlgISAIEILVEALVKL------IDADLPSSE--LLGP-TTLNIGRISGG 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 42542454 272 VAYNVVPAEMDVSFDLRIppTVNLQEFEEKIKVWCREA---GEDVTYDFAQKH 321
Cdd:cd05652 223 VAANVVPAAAEASVAIRL--AAGPPEVKDIVKEAVAGIltdTEDIEVTFTSGY 273
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
87-308 |
7.29e-16 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 78.69 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 87 VVLNSHTDVVPVYEEHWKHHPFAAVKDaDGNIYARGAQDMKSvtiqYIEAIRRL--KAAGKRFSRTIHLTFVPDEEVG-- 162
Cdd:PRK07522 67 IVLSGHTDVVPVDGQAWTSDPFRLTER-DGRLYGRGTCDMKG----FIAAALAAvpELAAAPLRRPLHLAFSYDEEVGcl 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 163 -------------------------------GHKGMetfvkhpefqklnmgfaldeglanptNAYTVfygernpwwiTVR 211
Cdd:PRK07522 142 gvpsmiarlpergvkpagcivgeptsmrpvvGHKGK--------------------------AAYRC----------TVR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 212 cpGSPGHGS---RFVeNtAAEKLRRVINSFLEFREKENQRLNTSECFtlgDV--TTINMTMVKGGVAYNVVPAEMDVSFD 286
Cdd:PRK07522 186 --GRAAHSSlapQGV-N-AIEYAARLIAHLRDLADRLAAPGPFDALF---DPpySTLQTGTIQGGTALNIVPAECEFDFE 258
|
250 260
....*....|....*....|..
gi 42542454 287 LRIPPTVNLQEFEEKIKVWCRE 308
Cdd:PRK07522 259 FRNLPGDDPEAILARIRAYAEA 280
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
25-407 |
8.69e-16 |
|
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: 78.32 E-value: 8.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 25 VTLFREYLRLKTVHPEpdyDA-ALKFLERMAEELAlpmKKVEVCP-GRVVAIISWIGSRPELksVVLNSHTDVVPV-YEE 101
Cdd:cd03891 1 LELAKELIRRPSVTPD---DAgAQDLIAERLKALG---FTCERLEfGGVKNLWARRGTGGPH--LCFAGHTDVVPPgDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 102 HWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHKGMETFVKHPEFQKLNM 181
Cdd:cd03891 73 GWSSDPFSPTIK-DGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 182 GFALdegLANPTNAY----TVFYGER---NpWWITVRcpGSPGHgsrfVE--NTAAEKLRRVINSFLEFrekenqrlnTS 252
Cdd:cd03891 152 DYCI---VGEPTSEKklgdTIKIGRRgslN-GKLTIK--GKQGH----VAypHLADNPIHLLAPILAEL---------TA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 253 ECFTLGDV----TTINMTMVKGGV-AYNVVPAEMDVSFDLRIPPTVNlqefEEKIKVWCREAGEDVTYDFAqkhmdqnLT 327
Cdd:cd03891 213 TVLDEGNEffppSSLQITNIDVGNgATNVIPGELKAKFNIRFNDEHT----GESLKARIEAILDKHGLDYD-------LE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 328 STDENDPWWQAFSSTCKAMNMTLKKE--IFPAAT------DSRFIREVGLPAIGFSPMNLTpilLHDHNEYlneqVFLQG 399
Cdd:cd03891 282 WKLSGEPFLTKPGKLVDAVSAAIKEVtgITPELStsggtsDARFIASYGCPVVEFGLVNAT---IHKVNER----VSVAD 354
|
410
....*....|..
gi 42542454 400 IQ----VYERLI 407
Cdd:cd03891 355 LEkltdIYERIL 366
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
21-371 |
3.94e-15 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 76.43 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 21 EDPSVTLFREYLRLKTVHP----EPDYDAAlKFLERMAEELalPMKKVEV--CPGRVVA------IISWIGSRPELKSVV 88
Cdd:PRK13983 4 RDEMIELLSELIAIPAVNPdfggEGEKEKA-EYLESLLKEY--GFDEVERydAPDPRVIegvrpnIVAKIPGGDGKRTLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 89 LNSHTDVVPVYEEH-WKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHKGM 167
Cdd:PRK13983 81 IISHMDVVPPGDLSlWETDPFKPVVK-DGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 168 ETFVK-HPE-FQKLNMGFALDEGlaNPTNAyTVFYGERNPWWITVRCPGSPGHGSRfVENTaaeklrrvINSF---LEFR 242
Cdd:PRK13983 160 QYLLKkHPElFKKDDLILVPDAG--NPDGS-FIEIAEKSILWLKFTVKGKQCHAST-PENG--------INAHraaADFA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 243 EKENQRLNTSecFTLGD------VTTINMTMVKGGV-AYNVVPAEMDVSFDLRIPPTVNLQE----FEEKIKVWCREAGE 311
Cdd:PRK13983 228 LELDEALHEK--FNAKDplfdppYSTFEPTKKEANVdNINTIPGRDVFYFDCRVLPDYDLDEvlkdIKEIADEFEEEYGV 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42542454 312 DVTYDFAQKhmDQNLTSTDENDPWWQAFSSTCKAMnmtLKKEIFPA----ATDSRFIREVGLPA 371
Cdd:PRK13983 306 KIEVEIVQR--EQAPPPTPPDSEIVKKLKRAIKEV---RGIEPKVGgiggGTVAAFLRKKGYPA 364
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
85-303 |
4.06e-14 |
|
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: 73.36 E-value: 4.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 85 KSVVLNSHTDVVPVyEEHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGH 164
Cdd:cd02697 74 RTVALNAHGDVVPP-GDGWTRDPYGAVVE-DGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 165 KGmetfvkhPefqklnmGFALDEGLANPTNA------YTVFYGERNPWWITVRCPGSPGHGSRfvENTAAEKLR---RVI 235
Cdd:cd02697 152 LG-------P-------GWLLRQGLTKPDLLiaagfsYEVVTAHNGCLQMEVTVHGKQAHAAI--PDTGVDALQgavAIL 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42542454 236 NSFLEFREKENQRLNTSECFTlgdVTTINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIK 303
Cdd:cd02697 216 NALYALNAQYRQVSSQVEGIT---HPYLNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIR 280
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
81-389 |
7.66e-14 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 72.09 E-value: 7.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 81 RPELKSVVLNSHTDVVPVYEEhwkhhpFAAVKDADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTihLTFVPDEE 160
Cdd:cd05647 50 RGLASRVILAGHLDTVPVAGN------LPSRVEEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLT--LIFYDCEE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 161 VGGHK-GMETFVK-HPEFqkLNMGFALdegLANPTNAyTVFYGERNPWWITVRCPGSPGHGSR-FVENTAAEKLRRVINS 237
Cdd:cd05647 122 VAAELnGLGRLAEeHPEW--LAADFAV---LGEPTDG-TIEGGCQGTLRFKVTTHGVRAHSARsWLGENAIHKLAPILAR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 238 FLEFREKEN--QRLNTSECftlgdvttINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIkvwcREAGEDVTY 315
Cdd:cd05647 196 LAAYEPRTVniDGLTYREG--------LNAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHV----REVFEGLGY 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42542454 316 DFAQK-HMDQNLTSTDEndPWWQAFSStckamnmTLKKEIFP--AATD-SRFiREVGLPAIGFSPMNltPILLHDHNE 389
Cdd:cd05647 264 EIEVTdLSPGALPGLDH--PVARDLIE-------AVGGKVRAkyGWTDvARF-SALGIPAVNFGPGD--PLLAHKRDE 329
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
25-298 |
7.71e-14 |
|
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: 72.00 E-value: 7.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 25 VTLFREYLRLKTVHPEpDYDAAlKFLERMAEELALPMKKVEVcpGRVVAIISwigsrPELKSVVLNSHTDVVPVYEEhwk 104
Cdd:cd05653 4 VELLLDLLSIYSPSGE-EARAA-KFLEEIMKELGLEAWVDEA--GNAVGGAG-----SGPPDVLLLGHIDTVPGEIP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 105 hhpfaaVKDADGNIYARGAQDMKSVTIQYIEAIRRLKaagKRFSRTIHLTFVPDEEVGGhKGMETFV-KHPEFQKLNMGf 183
Cdd:cd05653 72 ------VRVEGGVLYGRGAVDAKGPLAAMILAASALN---EELGARVVVAGLVDEEGSS-KGARELVrRGPRPDYIIIG- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 184 aldeglaNPTNAYTVFYGERNPWWITVRCPGSPGHGSRfVENTAAEKLrrvINSFLEFRekenqRLNTSECFTLGDVTTI 263
Cdd:cd05653 141 -------EPSGWDGITLGYRGSLLVKIRCEGRSGHSSS-PERNAAEDL---IKKWLEVK-----KWAEGYNVGGRDFDSV 204
|
250 260 270
....*....|....*....|....*....|....*
gi 42542454 264 NMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEF 298
Cdd:cd05653 205 VPTLIKGGESSNGLPQRAEATIDLRLPPRLSPEEA 239
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
54-302 |
3.99e-13 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 70.17 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 54 AEELALPMKKVEVCPGRVVAIISWI-------------GSRPELKSVVLNSHTDVVpvYEEHWKHHPFAAVKDADGNI-Y 119
Cdd:PRK08652 4 AKELLKQLVKIPSPSGQEDEIALHImefleslgydvhiESDGEVINIVVNSKAELF--VEVHYDTVPVRAEFFVDGVYvY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 120 ARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIhlTFVPDEEVGGhKGMETFVkhpefQKLNMGFALdegLANPTNAYTVF 199
Cdd:PRK08652 82 GTGACDAKGGVAAILLALEELGKEFEDLNVGI--AFVSDEEEGG-RGSALFA-----ERYRPKMAI---VLEPTDLKVAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 200 --YGERNpwwITVRCPGSPGHGSrFVEN--TAAEKLRRVINSFLEFREKENQRLNTSecftlgdvttINMTMVKGGVAYN 275
Cdd:PRK08652 151 ahYGNLE---AYVEVKGKPSHGA-CPESgvNAIEKAFEMLEKLKELLKALGKYFDPH----------IGIQEIIGGSPEY 216
|
250 260
....*....|....*....|....*..
gi 42542454 276 VVPAEMDVSFDLRIPPTVNLQEFEEKI 302
Cdd:PRK08652 217 SIPALCRLRLDARIPPEVEVEDVLDEI 243
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
29-203 |
4.29e-13 |
|
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: 70.74 E-value: 4.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 29 REYLRLKTVHPEPD---------YDAALKFLErMAEELALPMKKVEvcpgRVVAIISWiGSRPELksVVLNSHTDVVPVY 99
Cdd:cd03888 15 KELVAIPSVRDEATegapfgegpRKALDKFLD-LAKRLGFKTKNID----NYAGYAEY-GEGEEV--LGILGHLDVVPAG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 100 EEhWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGhKGMETFVKHPEfqKL 179
Cdd:cd03888 87 EG-WTTDPFKPVIK-DGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGW-KCIEHYFEHEE--YP 161
|
170 180
....*....|....*....|....
gi 42542454 180 NMGFALDeglANptnaYTVFYGER 203
Cdd:cd03888 162 DFGFTPD---AE----FPVINGEK 178
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
29-203 |
1.49e-12 |
|
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: 68.94 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 29 REYLRLKTV----HPEPDY-------DAALKFLErMAEELALPMKKVEVCPGRVVaiiswIGSRPELKSVVlnSHTDVVP 97
Cdd:TIGR01887 9 KELIAIDSVedleKAKEGApfgegprKALDKFLE-IAKRDGFTTENVDNYAGYIE-----YGQGEEVLGIL--GHLDVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 98 VyEEHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGhKGMETFVKHPEFQ 177
Cdd:TIGR01887 81 A-GDGWTSPPFEPTIK-DGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEESGW-KCIDYYFEHEEMP 157
|
170 180
....*....|....*....|....*.
gi 42542454 178 klNMGFAldeglanPTNAYTVFYGER 203
Cdd:TIGR01887 158 --DIGFT-------PDAEFPIIYGEK 174
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
87-407 |
1.58e-12 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 68.59 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 87 VVLNSHTDVVPV-YEEHWKHHPFAAVKdADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHK 165
Cdd:TIGR01246 58 LAFAGHTDVVPAgPEEQWSSPPFEPVE-RDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAID 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 166 GMETFVKHPEFQKLNMGFALdegLANPTNAY----TVFYGERNPWWITVRCPGSPGH-GSRFVENTAAEKLRRVINSFLE 240
Cdd:TIGR01246 137 GTKKVVETLMARDELIDYCI---VGEPSSVKklgdVIKNGRRGSITGNLTIKGIQGHvAYPHLANNPIHKAAPALAELTA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 241 FREKENqrlntSECFTlgdVTTINMTMVKGGV-AYNVVPAEMDVSFDLRIPPTVNLQEFEEKIKVWCREAGedVTYDFAQ 319
Cdd:TIGR01246 214 IKWDEG-----NEFFP---PTSLQITNIHAGTgANNVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHG--LDYDLEW 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 320 KHMDQNLTsTDENDPWWQAFSSTCKAMNMTLKKEIFPAATDSRFIREVGLPAIGFSPMNLTpilLHDHNEYLNEQVFLQG 399
Cdd:TIGR01246 284 SLSGEPFL-TNDGKLIDKAREAIEETNGIKPELSTGGGTSDGRFIALMGAEVVEFGPVNAT---IHKVNECVSIEDLEKL 359
|
....*...
gi 42542454 400 IQVYERLI 407
Cdd:TIGR01246 360 SDVYQDLL 367
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
41-392 |
3.24e-12 |
|
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: 67.23 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 41 PDYDAALkfLERMAEELALPMK----KVEVCPGRVVA-IISWIGSRPELKSVVLNSHTDVVpvyeehWKH--HPFAAVKD 113
Cdd:cd03885 14 GTYDKEG--VDRVAELLAEELEalgfTVERRPLGEFGdHLIATFKGTGGKRVLLIGHMDTV------FPEgtLAFRPFTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 114 ADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHKGMETFVKHPEFQK--LNMGFALDEG--- 188
Cdd:cd03885 86 DGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRELIEEEAKGADyvLVFEPARADGnlv 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 189 LANPTNAYtvfygernpWWITVRcpGSPGH-GSRFVEN-TAAEKLRRVInsfLEFREKENQRLNtsecftlgdvTTINMT 266
Cdd:cd03885 166 TARKGIGR---------FRLTVK--GRAAHaGNAPEKGrSAIYELAHQV---LALHALTDPEKG----------TTVNVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 267 MVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIKVWCREA-GEDVTYDFAQKHMDQNLTSTDENDPWWQAFSSTCKA 345
Cdd:cd03885 222 VISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTlVPGTSVELTGGLNRPPMEETPASRRLLARAQEIAAE 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 42542454 346 MNMTLKKEIFPAATDSRFIREVGLPAI-GFSPMNLTPillHDHNEYLN 392
Cdd:cd03885 302 LGLTLDWEATGGGSDANFTAALGVPTLdGLGPVGGGA---HTEDEYLE 346
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
200-314 |
3.83e-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: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 200 YGERNPWWITVRCPGSPGHGSR--FVENtAAEKLRRVINSFLEFREKENQRLntsecftlgDVTTINMTMVKGGVAYNVV 277
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGApgKGVN-AIKLLARLLAELPAEYGDIGFDF---------PRTTLNITGIEGGTATNVI 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 42542454 278 PAEMDVSFDLRIPPTVNLQEFEEKIKVWCREAGEDVT 314
Cdd:pfam07687 71 PAEAEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
86-407 |
3.90e-12 |
|
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: 66.95 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 86 SVVLNSHTDVV-PVyeEHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIhLTFVPDEEVGGH 164
Cdd:cd05651 57 TLLLNSHHDTVkPN--AGWTKDPFEPVEK-GGKLYGLGSNDAGASVVSLLATFLHLYSEGPLNYNLI-YAASAEEEISGK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 165 KGMETFVkhPEFQKLNMGFaldegLANPTNaYTVFYGERNPWWITVRCPGSPGHGSRFVENTAAEKLRRVINSFLEFR-E 243
Cdd:cd05651 133 NGIESLL--PHLPPLDLAI-----VGEPTE-MQPAIAEKGLLVLDCTARGKAGHAARNEGDNAIYKALDDIQWLRDFRfD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 244 KEnqrlntSEcfTLGDVTtINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIKvwcreagEDVTYDFAQKHMD 323
Cdd:cd05651 205 KV------SP--LLGPVK-MTVTQINAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIR-------GNLKSEIKPRSFR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 324 QNLTSTDENDPwwqaFSSTCKAMNMTlkkeIF--PAATDSRFIrevGLPAIGFSPMNLTPIllHDHNEYLNEQVFLQGIQ 401
Cdd:cd05651 269 LNSSAIPPDHP----IVQAAIAAGRT----PFgsPTLSDQALM---PFPSVKIGPGDSSRS--HTADEFIELSEIEEGID 335
|
....*.
gi 42542454 402 VYERLI 407
Cdd:cd05651 336 IYIELL 341
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
29-413 |
4.53e-12 |
|
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation.
Pssm-ID: 349888 [Multi-domain] Cd Length: 426 Bit Score: 67.35 E-value: 4.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 29 REYLRLKTVHPEPDYDAALKfleRMAEELALPMKK----VEVC--PGRVVAIISWIGSRPELKSVVLNSHTDVVPVY-EE 101
Cdd:cd03893 5 AELVAIPSVSAQPDRREELR---RAAEWLADLLRRlgftVEIVdtSNGAPVVFAEFPGAPGAPTVLLYGHYDVQPAGdED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 102 HWKHHPFAAVkDADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLtFVPDEEVGGHKGMETFV-KHPEFQKLN 180
Cdd:cd03893 82 GWDSDPFELT-ERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKF-IIEGEEESGSPSLDQLVeAHRDLLAAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 181 MGFALDeGLANPTNAYTVFYGERN--PWWITVRCPGSPGHGSRF--VENTAAEKLRRVINSFLEFREK--------ENQR 248
Cdd:cd03893 160 AIVISD-STWVGQEQPTLTYGLRGnaNFDVEVKGLDHDLHSGLYggVVPDPMTALAQLLASLRDETGRilvpglydAVRE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 249 LNTSECFTLGDVT---------------------TINMTMVKGGV----AYNVVPAEMDVSFDLRIPPTVNLQEFEEKIk 303
Cdd:cd03893 239 LPEEEFRLDAGVLeeveiiggttgsvaerlwtrpALTVLGIDGGFpgegSKTVIPPRARAKISIRLVPGQDPEEASRLL- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 304 vwcREAGEDVTYDFAQKHMDQNL----TSTDENDPWWQAFSstcKAMnmtlkKEIFPAATDsrFIREVG-LPAIGFS--- 375
Cdd:cd03893 318 ---EAHLEKHAPSGAKVTVSYVEggmpWRSDPSDPAYQAAK---DAL-----RTAYGVEPP--LTREGGsIPFISVLqef 384
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 42542454 376 ---PMNLTPILLHDHNEYL-NEQVFlqgIQVYERLIPALAGV 413
Cdd:cd03893 385 pqaPVLLIGVGDPDDNAHSpNESLR---LGNYKEGTQAEAAL 423
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
23-160 |
2.15e-11 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 65.11 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 23 PSVTLFREYLRLKTVHPEpdyDA-ALKFLERMAEELALpmkKVEVCP-GRVVAIISWIGSrpELKSVVLNSHTDVVPV-Y 99
Cdd:PRK13009 3 DVLELAQDLIRRPSVTPD---DAgCQDLLAERLEALGF---TCERMDfGDVKNLWARRGT--EGPHLCFAGHTDVVPPgD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42542454 100 EEHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEE 160
Cdd:PRK13009 75 LEAWTSPPFEPTIR-DGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEE 134
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
27-162 |
3.38e-10 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 61.59 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 27 LFREYLRLKTVHPeP--DYDAALKFLERMAEELALPMKKVEVCPG--RVVAIISwiGSRPE-LKSVVLNSHTDVVPVYE- 100
Cdd:PRK08596 18 LLKTLVRFETPAP-ParNTNEAQEFIAEFLRKLGFSVDKWDVYPNdpNVVGVKK--GTESDaYKSLIINGHMDVAEVSAd 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42542454 101 EHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVG 162
Cdd:PRK08596 95 EAWETNPFEPTIK-DGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEVG 155
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
64-291 |
3.44e-10 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 61.34 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 64 VEVCPGR--VVAIISWIGSRpelKSVVLNSHTDVVPVyeEHWKHHPFAAVKdADGNIYARGAQDMKSVTIQYIEAIRRLK 141
Cdd:cd08013 49 IEGTPGRpsVVGVVRGTGGG---KSLMLNGHIDTVTL--DGYDGDPLSGEI-ADGRVYGRGTLDMKGGLAACMAALADAK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 142 AAGKRfsRTIHLTFVPDEEVGGhKGMEtfvkhpefQKLNMGFALDEGL-ANPTNaYTVFYGERNPWWITVRCPGSPGHGS 220
Cdd:cd08013 123 EAGLR--GDVILAAVADEEDAS-LGTQ--------EVLAAGWRADAAIvTEPTN-LQIIHAHKGFVWFEVDIHGRAAHGS 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42542454 221 RFVENTAAeklrrVINS--FLEFREKENQRLNTSECFTLGDVTTINMTMVKGGVAYNVVPAEMDVSFDLRIPP 291
Cdd:cd08013 191 RPDLGVDA-----ILKAgyFLVALEEYQQELPERPVDPLLGRASVHASLIKGGEEPSSYPARCTLTIERRTIP 258
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
27-290 |
8.88e-10 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 59.80 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 27 LFREYLRLKTvhPEPDYDAALKFLERMAEELALpmkKVEVCPgrvvAIISWIGSRPElksVVLNSHTDVVPVYEEhwkhh 106
Cdd:PRK00466 15 LLLDLLSIYT--PSGNETNATKFFEKISNELNL---KLEILP----DSNSFILGEGD---ILLASHVDTVPGYIE----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 107 pfaaVKDADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRfsrtIHLTFVPDEEvGGHKGMETFV-KHPEFQKLNMGfal 185
Cdd:PRK00466 78 ----PKIEGEVIYGRGAVDAKGPLISMIIAAWLLNEKGIK----VMVSGLADEE-STSIGAKELVsKGFNFKHIIVG--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 186 deglaNPTNAYTVFYGERNPWWITVRCPGSPGHGSRFVENTAAEKLRRVINSFlefREKENQrlntsecftlgDVTTINM 265
Cdd:PRK00466 146 -----EPSNGTDIVVEYRGSIQLDIMCEGTPEHSSSAKSNLIVDISKKIIEVY---KQPENY-----------DKPSIVP 206
|
250 260
....*....|....*....|....*
gi 42542454 266 TMVKGGVAYNVVPAEMDVSFDLRIP 290
Cdd:PRK00466 207 TIIRAGESYNVTPAKLYLHFDVRYA 231
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
30-186 |
4.96e-09 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 57.93 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 30 EYLRLKTV----HPEPDY------DAALKFLERMAEELALPMKKVEVCPGR--------VVAIISwigsrpelksvvlns 91
Cdd:PRK07318 22 ELLRINSVrddsKAKEGApfgpgpVKALEKFLEIAERDGFKTKNVDNYAGHieygegeeVLGILG--------------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 92 HTDVVPVyEEHWKHHPFAAVKdADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEvGGHKGMETFV 171
Cdd:PRK07318 87 HLDVVPA-GDGWDTDPYEPVI-KDGKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRFIVGTDEE-SGWKCMDYYF 163
|
170
....*....|....*...
gi 42542454 172 KH---PEFqklnmGFALD 186
Cdd:PRK07318 164 EHeeaPDF-----GFSPD 176
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
51-160 |
5.31e-09 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 57.43 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 51 ERMAEElalpMKKV---EVCPGRVVAIISWIGSRPelKSVVLNSHTDVVPVYEE-HWKHHPFAAvKDADGNIYARGAQDM 126
Cdd:cd05649 22 ERIEEE----MEKLgfdEVEIDPMGNVIGYIGGGK--KKILFDGHIDTVGIGNIdNWKFDPYEG-YETDGKIYGRGTSDQ 94
|
90 100 110
....*....|....*....|....*....|....*
gi 42542454 127 KSVTIQYIEAIRRLKAAGKR-FSRTIHLTFVPDEE 160
Cdd:cd05649 95 KGGLASMVYAAKIMKDLGLRdFAYTILVAGTVQEE 129
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
30-162 |
9.73e-09 |
|
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: 56.93 E-value: 9.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 30 EYLRLKTVHPEPDYDAALkflERMAEELA-----LPMKKVEVCP--GRVVAIISWIGSrPELKSVVLNSHTDVVPVY-EE 101
Cdd:cd05680 6 ELLRIPSVSADPAHKGDV---RRAAEWLAdklteAGFEHTEVLPtgGHPLVYAEWLGA-PGAPTVLVYGHYDVQPPDpLE 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42542454 102 HWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVG 162
Cdd:cd05680 82 LWTSPPFEPVVR-DGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIG 141
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
16-172 |
1.43e-08 |
|
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: 56.46 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 16 DGHpaEDPSVTLFREYLRLKTVHPEPDYdaaLKFLERMAEELALPMKKV-----------EVCP-GRVVA----IISWIG 79
Cdd:cd05676 6 DEH--QDEFIERLREAVAIQSVSADPEK---RPELIRMMEWAAERLEKLgfkvelvdigtQTLPdGEELPlppvLLGRLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 80 SRPELKSVVLNSHTDVVPV-YEEHWKHHPFAAVkDADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPD 158
Cdd:cd05676 81 SDPSKKTVLIYGHLDVQPAkLEDGWDTDPFELT-EKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEGM 159
|
170
....*....|....
gi 42542454 159 EEVGGhKGMETFVK 172
Cdd:cd05676 160 EESGS-EGLDELIE 172
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
51-160 |
2.49e-08 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 55.72 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 51 ERMAEELALPMKKV---EVCPGRVVAIISWIGSRPelKSVVLNSHTDVVPVY-EEHWKHHPFAAVKDaDGNIYARGAQDM 126
Cdd:PRK13004 35 KRVVKRIKEEMEKVgfdKVEIDPMGNVLGYIGHGK--KLIAFDAHIDTVGIGdIKNWDFDPFEGEED-DGRIYGRGTSDQ 111
|
90 100 110
....*....|....*....|....*....|....
gi 42542454 127 KSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEE 160
Cdd:PRK13004 112 KGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEE 145
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
59-305 |
3.70e-08 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 55.16 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 59 LPMKKVEVCPGRVVAIISWIGSRPELKSVVLNSHTDVVPVYEEHWKHHPFAAVKDADgNIYARGAQDMKSVTIQYIEAIR 138
Cdd:cd08012 53 LVIDHVSYVKGRGNIIVEYPGTVDGKTVSFVGSHMDVVTANPETWEFDPFSLSIDGD-KLYGRGTTDCLGHVALVTELFR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 139 RLKAAGKRFSRTIHLTFVPDEEVGG--HKGMETFVKHPEFQKLNMG--FALDEGLANPtnayTVFYGERNPWWITvrcpg 214
Cdd:cd08012 132 QLATEKPALKRTVVAVFIANEENSEipGVGVDALVKSGLLDNLKSGplYWVDSADSQP----CIGTGGMVTWKLT----- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 215 spGHGSRF--------------VENTAAEKLRRVINSFLEFREKENQRLNTSecftlgdvTTINMTMVK--GGvAYNVVP 278
Cdd:cd08012 203 --ATGKLFhsglphkainalelVMEALAEIQKRFYIDFPPHPKEEVYGFATP--------STMKPTQWSypGG-SINQIP 271
|
250 260
....*....|....*....|....*..
gi 42542454 279 AEMDVSFDLRIPPTVNLQEFEEKIKVW 305
Cdd:cd08012 272 GECTICGDCRLTPFYDVKEVREKLEEY 298
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
41-162 |
1.16e-06 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 50.17 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 41 PDYDAALkfLERM----AEELALPMKKVEVCPGRV----VAIISWIGSRPELKSVVLNSHTDVVpvyeehwkhHPFAAVK 112
Cdd:PRK07473 26 PTWDAAA--VNRMldlaARDMAIMGATIERIPGRQgfgdCVRARFPHPRQGEPGILIAGHMDTV---------HPVGTLE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 42542454 113 D----ADGN-IYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVG 162
Cdd:PRK07473 95 KlpwrREGNkCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFTPDEEVG 149
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
92-172 |
3.15e-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: 48.88 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 92 HTDVVPVYE-EHWKHHPFAAVKdADGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGhKGMETF 170
Cdd:cd05681 67 HYDVQPAEPlELWTSDPFELTI-RNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGS-PNLEKF 144
|
..
gi 42542454 171 VK 172
Cdd:cd05681 145 VA 146
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
30-176 |
3.74e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 48.75 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 30 EYLRLKTVHPEPdYDAAlkFLERMAEELALPMKKVEVCPGRVVA---IISWIGSRP---ELKSVVLNSHTDVVPVY-EEH 102
Cdd:PRK07907 26 ELVRIPSVAADP-FRRE--EVARSAEWVADLLREAGFDDVRVVSadgAPAVIGTRPappGAPTVLLYAHHDVQPPGdPDA 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42542454 103 WKHHPFAAVkDADGNIYARGAQDMKSVTIQYIEAIRrlkAAGKRFsrTIHLT-FVPDEEVGGHKGMETFVK-HPEF 176
Cdd:PRK07907 103 WDSPPFELT-ERDGRLYGRGAADDKGGIAMHLAALR---ALGGDL--PVGVTvFVEGEEEMGSPSLERLLAeHPDL 172
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
68-167 |
4.78e-06 |
|
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: 48.49 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 68 PGR--VVAIISwiGSRPELKSVVLNSHTDVVPVYEEH-WKHHPF------------------AAVKDADGN--IYARGAQ 124
Cdd:cd05654 55 LGRrnVTALVK--GKKPSKRTIILISHFDTVGIEDYGeLKDIAFdpdeltkafseyveeldeEVREDLLSGewLFGRGTM 132
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 42542454 125 DMKSVTIQYIEAIRRLkAAGKRFSRTIHLTFVPDEEVgGHKGM 167
Cdd:cd05654 133 DMKSGLAVHLALLEQA-SEDEDFDGNLLLMAVPDEEV-NSRGM 173
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
88-303 |
4.79e-06 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 48.28 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 88 VLNSHTDVVPVYEEHWKHHPFAAVkDADGNIYARGAQDMKSVTIQYIEAIRRLKAagKRFSRTIHLTFVPDEEVGGHkGM 167
Cdd:PRK05111 75 LLAGHTDTVPFDEGRWTRDPFTLT-EHDGKLYGLGTADMKGFFAFILEALRDIDL--TKLKKPLYILATADEETSMA-GA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 168 ETFVKHpefQKLNMGFALdegLANPTNAYTVF-----YGERnpwwitVRCPGSPGHGS---RFVenTAAEKLRRVINSFL 239
Cdd:PRK05111 151 RAFAEA---TAIRPDCAI---IGEPTSLKPVRahkghMSEA------IRITGQSGHSSdpaLGV--NAIELMHDVIGELL 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42542454 240 EFRE--KENQRlntSECFTLgDVTTINMTMVKGGVAYNVVPAEMDVSFDLRIPPTVNLQEFEEKIK 303
Cdd:PRK05111 217 QLRDelQERYH---NPAFTV-PYPTLNLGHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLR 278
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
73-167 |
1.05e-05 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 47.46 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 73 AIISWIGS-RPELksvVLNSHTDVVPVYEEHWKHHPFAAVKDADgNIYARGAQDMKSVTIQYIEAIRRLKAagKRFSRTI 151
Cdd:PRK08554 54 AVYGEIGEgKPKL---LFMAHFDVVPVNPEEWNTEPFKLTVKGD-KAYGRGSADDKGNVASVMLALKELSK--EPLNGKV 127
|
90
....*....|....*.
gi 42542454 152 HLTFVPDEEVGGHKGM 167
Cdd:PRK08554 128 IFAFTGDEEIGGAMAM 143
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
85-188 |
1.22e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 47.06 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 85 KSVVLNSHTDVVPVYE-EHWKHHPFAAVKDaDGNIYARGAQDMKSVTIQYIEAIRRLKAAGKrFSRTIHLTFVPDEEVGG 163
Cdd:PRK06446 63 KTLLIYNHYDVQPVDPlSEWKRDPFSATIE-NGRIYARGASDNKGTLMARLFAIKHLIDKHK-LNVNVKFLYEGEEEIGS 140
|
90 100
....*....|....*....|....*
gi 42542454 164 hKGMETFVKHPEfQKLNMGFALDEG 188
Cdd:PRK06446 141 -PNLEDFIEKNK-NKLKADSVIMEG 163
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
82-227 |
3.66e-05 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 45.94 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 82 PELKSVVLNSHTDVVPVYEEHW-KHHPFAAV---KDADGN------------------IYARGAQDMKSVTIQYIEAIRR 139
Cdd:cd05678 58 DARKTVLFYMHLDGQPVDPSKWdQKSPYTPVlkrKDAAGNweeinwdaifsnldpewrVFARAAADDKGPIMMMLAALDA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 140 LKAAGKRFSRTIHLTFVPDEEVGGHKGMETFVKHPEFQKLNMGFALDeGLANPTNAYTVFYGERNPWWITV-----RCPG 214
Cdd:cd05678 138 LKAGGIAPKFNVKIILDSEEEKGSPSLPKAVKEYKELLAADALIIMD-GPAHATNKPTLTFGCRGIATATLttygaKVPQ 216
|
170
....*....|...
gi 42542454 215 SPGHGSRFVENTA 227
Cdd:cd05678 217 HSGHYGNYAPNPA 229
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
29-162 |
2.27e-04 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 43.20 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 29 REYLRLKTV-----HPEPDYDAAlkflERMAEEL-ALPMKKVEV--CPGRVVAIISWIGSrPELKSVVLNSHTDVVPVYE 100
Cdd:PRK08201 21 KEFLRIPSIsalseHKEDVRKAA----EWLAGALeKAGLEHVEImeTAGHPIVYADWLHA-PGKPTVLIYGHYDVQPVDP 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42542454 101 EH-WKHHPFA-AVKDadGNIYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVG 162
Cdd:PRK08201 96 LNlWETPPFEpTIRD--GKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEEIG 157
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
21-188 |
8.81e-04 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 41.49 E-value: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 21 EDPSVTLFREYLRLKTVH----PEPDYDAALKF---LERMAEELALPMKKVevcpGRVVAIISWIGSRPELKSVVlnSHT 93
Cdd:PRK06156 45 GAAAIESLRELVAFPTVRvegvPQHENPEFIGFkklLKSLARDFGLDYRNV----DNRVLEIGLGGSGSDKVGIL--THA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 94 DVVPVYEEHW-----KHHPFAAVKDADgNIYARGAQDMKS--VTIQYieAIRRLKAAGKRFSRTIHLTFVPDEEVGGhKG 166
Cdd:PRK06156 119 DVVPANPELWvldgtRLDPFKVTLVGD-RLYGRGTEDDKGaiVTALY--AMKAIKDSGLPLARRIELLVYTTEETDG-DP 194
|
170 180
....*....|....*....|..
gi 42542454 167 METFVKHPEFQKLNMgfALDEG 188
Cdd:PRK06156 195 LKYYLERYTPPDYNI--TLDAE 214
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
27-213 |
1.18e-03 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 41.04 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 27 LFrEYLRLKTVHPEPDYDAA-LKFLERMAEELA-LPMK-KVEVCPGR--VVAIISwiGSRPELKSVVLNSHTDVVPV-YE 100
Cdd:PRK09104 23 LF-ALLRIPSISTDPAYAADcRKAADWLVADLAsLGFEaSVRDTPGHpmVVAHHE--GPTGDAPHVLFYGHYDVQPVdPL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 101 EHWKHHPFA-AVKD-ADGN--IYARGAQDMKSVTIQYIEAIRRLKAAGKRFSRTIHLTFVPDEEVGGhKGMETFVKHpEF 176
Cdd:PRK09104 100 DLWESPPFEpRIKEtPDGRkvIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEESGS-PSLVPFLEA-NA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 42542454 177 QKLNMGFAL--DEGLANP-TNAYTV-----FYGErnpwwITVRCP 213
Cdd:PRK09104 178 EELKADVALvcDTGMWDReTPAITTslrglVGEE-----VTITAA 217
|
|
| M28_like_PA |
cd05660 |
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ... |
71-204 |
1.78e-03 |
|
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.
Pssm-ID: 349910 [Multi-domain] Cd Length: 290 Bit Score: 40.04 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 71 VVAIISwiGSrpelksvvlnSHTDVVPVYEEHWKHHPFAAVKDADgNIYaRGAQDMKSVTIQYIEAIRRLKAAGKRFSRT 150
Cdd:cd05660 62 VVAILP--GS----------KLPDEYIVLSAHWDHLGIGPPIGGD-EIY-NGAVDNASGVAAVLELARVFAAQDQRPKRS 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 42542454 151 IHLTFVPDEEVGGHkGMETFVKHPEF--QKLNMGFALDE-GLANPTNAYTVF-YGERN 204
Cdd:cd05660 128 IVFLAVTAEEKGLL-GSRYYAANPIFplDKIVANLNIDMiGRIGPTKDVLLIgSGSSE 184
|
|
| Iap |
COG2234 |
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ... |
134-200 |
2.25e-03 |
|
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];
Pssm-ID: 441835 [Multi-domain] Cd Length: 257 Bit Score: 39.34 E-value: 2.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42542454 134 IEAIRRLKAAGKRFSRTIHLTFVPDEEVGGHkGMETFVKHPEFQKLNMGFALD-EGLANPTNAYTVFY 200
Cdd:COG2234 90 LELARALAALGPKPKRTIRFVAFGAEEQGLL-GSRYYAENLKAPLEKIVAVLNlDMIGRGGPRNYLYV 156
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
78-162 |
5.10e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 39.13 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42542454 78 IGSR---PELKSVVLNSHTDVVPVYEEHWKH--HPFAAVKDADgNIYARGAQDMK---SVTIQYIEAIrrLKAAGKRFSR 149
Cdd:PRK07079 76 IAERiedDALPTVLIYGHGDVVRGYDEQWREglSPWTLTEEGD-RWYGRGTADNKgqhTINLAALEQV--LAARGGRLGF 152
|
90
....*....|...
gi 42542454 150 TIHLTFVPDEEVG 162
Cdd:PRK07079 153 NVKLLIEMGEEIG 165
|
|
| |
