|
Name |
Accession |
Description |
Interval |
E-value |
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
8-398 |
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: 762.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 8 EDPATSLFREYLNIRTVQPDPDYDKGIQFLIRVAEEIGLESKTLELHPGRVILILTWKGTDPQLRSVILNSHTDVVPVFE 87
Cdd:cd05646 1 EDPAVTRFREYLRINTVHPNPDYDACVEFLKRQADELGLPVRVIEVVPGKPVVVLTWEGSNPELPSILLNSHTDVVPVFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 88 EFWTYPPFSAHKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHKGMELFVQHPDFHALN 167
Cdd:cd05646 81 EKWTHDPFSAHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGHDGMEKFVKTEEFKKLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 168 PGITLDEGLANPSEEFSVFYGEKCPWWITVHCGGDPGHGSRFIENTAAAKLHSVISRFLEFREKEKNRLLSDPNLTLGDV 247
Cdd:cd05646 161 VGFALDEGLASPTEEYRVFYGERSPWWVVITAPGTPGHGSKLLENTAGEKLRKVIESIMEFRESQKQRLKSNPNLTLGDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 248 TTVNLTRVSGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCREAGDNITWEYHQKCMNERVTTPDDSNPWWKAFS 327
Cdd:cd05646 241 TTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGRGVTYEFEQKSPEKDPTSLDDSNPWWAAFK 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50417585 328 TPCKEMGLKLKPEIFPAATDSRYIRTAGYSALGFSPMNNTPILLHDHNEYLNEDVFLRGIQIYTKIIASLA 398
Cdd:cd05646 321 KAVKEMGLKLKPEIFPAATDSRYIRALGIPALGFSPMNNTPILLHDHNEFLNEDVFLRGIEIYEKIIPALA 391
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
1-400 |
0e+00 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 616.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 1 MDLATATEDPATSLFREYLNIRTVQPDPDYDKGIQFLIRVAEEIGLESKTLELHPGRVILILTWKGTDPQLRSVILNSHT 80
Cdd:TIGR01880 1 MSSSKWEEDIAVTRFREYLRINTVQPNPDYAACVDFLIKQADELGLARKTIEFVPGKPVVVLTWPGSNPELPSILLNSHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 81 DVVPVFEEFWTYPPFSAHKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHKGMELFVQH 160
Cdd:TIGR01880 81 DVVPVFREHWTHPPFSAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEKFAKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 161 PDFHALNPGITLDEGLANPSEEFSVFYGEKCPWWITVHCGGDPGHGSRFIENTAAAKLHSVISRFLEFREKEKNRLLSDP 240
Cdd:TIGR01880 161 DEFKALNLGFALDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKLMENTAMEKLEKSVESIRRFRESQFQLLQSNP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 241 NLTLGDVTTVNLTRVSGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCREAGDNITWEYHQKCMNERVTTPDDSN 320
Cdd:TIGR01880 241 DLAIGDVTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAGEGVTYEFSQHSGKPLVTPHDDSN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 321 PWWKAFSTPCKEMGLKLKPEIFPAATDSRYIRTAGYSALGFSPMNNTPILLHDHNEYLNEDVFLRGIQIYTKIIASLASV 400
Cdd:TIGR01880 321 PWWVAFKDAVKEMGCTFKPEILPGSTDSRYIRAAGVPALGFSPMNNTPVLLHDHNEFLNEAVFLRGIEIYQTLISALASV 400
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
1-398 |
2.36e-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: 223.61 E-value: 2.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 1 MDLATATEDPATSLFREYLNIRTVqpDPDYDKGIQFLIRVAEEIGLESKTLELHPGRVILILTWKGTDPQlRSVILNSHT 80
Cdd:COG0624 4 LAAIDAHLDEALELLRELVRIPSV--SGEEAAAAELLAELLEALGFEVERLEVPPGRPNLVARRPGDGGG-PTLLLYGHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 81 DVVPV-FEEFWTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHkGMELFVQ 159
Cdd:COG0624 81 DVVPPgDLELWTSDPFEP-TIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSP-GARALVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 160 HpdfhaLNPGITLDEGL-ANPSEEFSVFYGEKCPWWITVHCGGDPGHGSRF--IENtAAAKLHSVISRFLEFREKEKnrl 236
Cdd:COG0624 159 E-----LAEGLKADAAIvGEPTGVPTIVTGHKGSLRFELTVRGKAAHSSRPelGVN-AIEALARALAALRDLEFDGR--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 237 lSDPNLtlgDVTTVNLTRVSGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCREAGDNITWEYHQKCMNERVTTP 316
Cdd:COG0624 230 -ADPLF---GRTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEVEVLGDGRPPFET 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 317 DDSNPWWKAFSTPCKE-MGLKLKPEIFPAATDSRYI-RTAGYSALGFSPMNNTpiLLHDHNEYLNEDVFLRGIQIYTKII 394
Cdd:COG0624 306 PPDSPLVAAARAAIREvTGKEPVLSGVGGGTDARFFaEALGIPTVVFGPGDGA--GAHAPDEYVELDDLEKGARVLARLL 383
|
....
gi 50417585 395 ASLA 398
Cdd:COG0624 384 ERLA 387
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
75-394 |
1.16e-52 |
|
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: 178.31 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 75 ILNSHTDVVPVfEEFWTYPpFSAhkDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRfPRTIHLTLVPDEEiGGHKGM 154
Cdd:pfam01546 1 LLRGHMDVVPD-EETWGWP-FKS--TEDGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEE-GGMGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 155 ELFVQHPDFHALNP----GITLDEG-LANPSEEFSVFYGEKCPWWITVHCGGDPGHGSRF-IENTAAAKLHSVISRFLEF 228
Cdd:pfam01546 75 RALIEDGLLEREKVdavfGLHIGEPtLLEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPhLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 229 REKEKNRLLSDPnltlgdVTTVNLTRVSGGvsFNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCREAGD--NITWEYHQ 306
Cdd:pfam01546 155 VSRNVDPLDPAV------VTVGNITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAayGVKVEVEY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 307 KCMNERVTTPDDsnPWWKAFSTPCKEM-GLKLKPEIFP--AATDSRYIRTA-GYSALGFSPMNNTpilLHDHNEYLNEDV 382
Cdd:pfam01546 227 VEGGAPPLVNDS--PLVAALREAAKELfGLKVELIVSGsmGGTDAAFFLLGvPPTVVFFGPGSGL---AHSPNEYVDLDD 301
|
330
....*....|..
gi 50417585 383 FLRGIQIYTKII 394
Cdd:pfam01546 302 LEKGAKVLARLL 313
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
13-394 |
5.02e-50 |
|
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: 174.47 E-value: 5.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 13 SLFREYLNIRTVQPDPDYDK---GIQFLIRVAEEIGL--ESKTLELHPGRVILILTWKGTDPQLRSVILNSHTDVVPVFE 87
Cdd:cd05675 2 DLLQELIRIDTTNSGDGTGSetrAAEVLAARLAEAGIqtEIFVVESHPGRANLVARIGGTDPSAGPLLLLGHIDVVPADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 88 EFWTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHKGMELFVQ-HPDF--- 163
Cdd:cd05675 82 SDWSVDPFSG-EIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDnHPELfdg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 164 --HALNP--GITLDEGlaNPSEEFSVFYGEKCPWWITVHCGGDPGHGSR-FIENtAAAKLHSVISR-------------- 224
Cdd:cd05675 161 atFALNEggGGSLPVG--KGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRpTDDN-AITRLAEALRRlgahnfpvrltdet 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 225 -----FLEFREKEKNRLLSDPNLTLGDV----------------TTVNLTRVSGGVSFNVVPSEMTATFDLRIPPTVNLK 283
Cdd:cd05675 238 ayfaqMAELAGGEGGALMLTAVPVLDPAlaklgpsapllnamlrNTASPTMLDAGYATNVLPGRATAEVDCRILPGQSEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 284 EFERQLEgwcREAGD---NITWEYHQKCMnerVTTPDdsNPWWKAFSTPCKEM--GLKLKPEIFPAATDSRYIRTAGYSA 358
Cdd:cd05675 318 EVLDTLD---KLLGDpdvSVEAVHLEPAT---ESPLD--SPLVDAMEAAVQAVdpGAPVVPYMSPGGTDAKYFRRLGIPG 389
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 50417585 359 LGFSPMNNTPIL-----LHDHNEYLNEDVFLRGIQIYTKII 394
Cdd:cd05675 390 YGFAPLFLPPELdytglFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
13-394 |
1.82e-42 |
|
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: 152.45 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 13 SLFREYLNIRTVQPDpdyDKGIQ-FLIRVAEEIGLESKTlELHPGRVILILTwKGTDPQlRSVILNSHTDVVPV-FEEFW 90
Cdd:cd08659 1 SLLQDLVQIPSVNPP---EAEVAeYLAELLAKRGYGIES-TIVEGRGNLVAT-VGGGDG-PVLLLNGHIDTVPPgDGDKW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 91 TYPPFSAHkDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGhKGMELFVQHPDFHALNPGI 170
Cdd:cd08659 75 SFPPFSGR-IRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGS-DGARALLEAGYADRLDALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 171 TldeglANPSEeFSVFYGEKCPWWITVHCGGDPGHGSR-FIENTAAAKLHSVISRFLEFR-EKEKNRLLSDPnltlgdvt 248
Cdd:cd08659 153 V-----GEPTG-LDVVYAHKGSLWLRVTVHGKAAHSSMpELGVNAIYALADFLAELRTLFeELPAHPLLGPP-------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 249 TVNLTRVSGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCREAGDNITWEYHQKCMNERVTTPDdsNPWWKAFST 328
Cdd:cd08659 219 TLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPPFFTDPD--HPLVQALQA 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50417585 329 PCKEMGLKLKPEIFPAATDSRYI-RTAGYSALGFSPMNntPILLHDHNEYLNEDVFLRGIQIYTKII 394
Cdd:cd08659 297 AARALGGDPVVRPFTGTTDASYFaKDLGFPVVVYGPGD--LALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
14-391 |
1.55e-38 |
|
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: 141.76 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 14 LFREYLNIRTVQPDPDYDKGIQFLIR-VAEEIGLESKTLELHPGRVILILTWKGTDPQLRsVILNSHTDVVPVFE-EFWT 91
Cdd:cd08011 3 LLQELVQIPSPNPPGDNTSAIAAYIKlLLEDLGYPVELHEPPEEIYGVVSNIVGGRKGKR-LLFNGHYDVVPAGDgEGWT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 92 YPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHKGMELFVQHPDFHalnPGIT 171
Cdd:cd08011 82 VDPYSG-KIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYLLEKVRIK---PNDV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 172 LdegLANPSEEFSVFYGEKCPWWITVHCGGDPGHGSRFIENTAAAKLHSVISRFLEFREKeknrllsdpnltlgdvtTVN 251
Cdd:cd08011 158 L---IGEPSGSDNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELEK-----------------TVN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 252 LTRVSGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQLEGwCREAGDNITWEYHQkcmNERVTTPDDSNPWWKAFSTPCK 331
Cdd:cd08011 218 PGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIID-HLDSIEEVSFEIKS---FYSPTVSNPDSEIVKKTEEAIT 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50417585 332 EM-GLKLKPEIFPAATDSRYIRTAGYSALGFSPmnNTPILLHDHNEYLNEDVFLRGIQIYT 391
Cdd:cd08011 294 EVlGIRPKEVISVGASDARFYRNAGIPAIVYGP--GRLGQMHAPNEYVEIDELIKVIKVHA 352
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
48-394 |
7.73e-38 |
|
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: 142.39 E-value: 7.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 48 SKTLEL-HPGRVILILTWKGTDPQLRSVILNSHTDVVPVFEEF---WTYPPFSAHKDkDGNIYARGAQDMKCVTIQYLEA 123
Cdd:cd05674 45 HKTLKVeVVNEYGLLYTWEGSDPSLKPLLLMAHQDVVPVNPETedqWTHPPFSGHYD-GGYIWGRGALDDKNSLIGILEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 124 VCRLKSEGRRFPRTIHLTLVPDEEIGGHKGMELFVQHPDFHALNPGI--TLDEGLAN-PSEEFSVFY-----GEK--CPW 193
Cdd:cd05674 124 VELLLKRGFKPRRTIILAFGHDEEVGGERGAGAIAELLLERYGVDGLaaILDEGGAVlEGVFLGVPFalpgvAEKgyMDV 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 194 WITVHcgGDPGHGS----------------RFIENTAAAKLH---------------------SVISRFLEFREKEKNRL 236
Cdd:cd05674 204 EITVH--TPGGHSSvppkhtgigilseavaALEANPFPPKLTpgnpyygmlqclaehsplpprSLKSNLWLASPLLKALL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 237 LSDPNLTLGDV-----TTVNLTRVSGGVSFNVVPSEMTATFDLRIPPTVNLKE----FERQLE-------------GWCR 294
Cdd:cd05674 282 ASELLSTSPLTrallrTTQAVDIINGGVKINALPETATATVNHRIAPGSSVEEvlehVKNLIAdiavkyglglsafGGDV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 295 EAGDNITWEYHQKCMNERVTTPDDSNPWWKAFSTPCKEM------GLKLKPEIFPAATDSRYirtagYSALG-----FSP 363
Cdd:cd05674 362 IYSTNGTKLLTSLLSPEPSPVSSTSSPVWQLLAGTIRQVfeqfgeDLVVAPGIMTGNTDTRH-----YWNLTkniyrFTP 436
|
410 420 430
....*....|....*....|....*....|....
gi 50417585 364 MNNTPILL---HDHNEYLNEDVFLRGIQIYTKII 394
Cdd:cd05674 437 IRLNPEDLgriHGVNERISIDDYLETVAFYYQLI 470
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
59-390 |
4.23e-37 |
|
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: 133.70 E-value: 4.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 59 ILILTWKGTDPqLRSVILNSHTDVVPVFEEFWTYPPFSAHKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTI 138
Cdd:cd03873 1 NLIARLGGGEG-GKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 139 HLTLVPDEEIGGHKGMELFVqhpdfhalnpgitlDEGLANPSEEFSVFYGEKCPWWItvhcgGDPGHGSRfientaaakl 218
Cdd:cd03873 80 VVAFTADEEVGSGGGKGLLS--------------KFLLAEDLKVDAAFVIDATAGPI-----LQKGVVIR---------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 219 hsvisrflefrekeknrllsdpnltlgdvttvnltrvsggvsfnvvpsemtatfdlripptvnlkeferqlegwcreagd 298
Cdd:cd03873 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 299 nitweyhqkcmnervttpddsNPWWKAFSTPCKEMGLKLKPEI-FPAATDSRYIRTAGYSALGFSPMnnTPILLHDHNEY 377
Cdd:cd03873 131 ---------------------NPLVDALRKAAREVGGKPQRASvIGGGTDGRLFAELGIPGVTLGPP--GDKGAHSPNEF 187
|
330
....*....|...
gi 50417585 378 LNEDVFLRGIQIY 390
Cdd:cd03873 188 LNLDDLEKATKVY 200
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
8-399 |
7.25e-37 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 140.08 E-value: 7.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 8 EDPATSLFREYLNIRTV--QPDPDYDKG--IQFLIRVAEEIGLESKTLELHP-GRVILILTWKGTDPQLRSVILNSHTDV 82
Cdd:PRK08262 43 EDAAAERLSEAIRFRTIsnRDRAEDDAAafDALHAHLEESYPAVHAALEREVvGGHSLLYTWKGSDPSLKPIVLMAHQDV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 83 VPV---FEEFWTYPPFSAHKdKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGH---KGMEL 156
Cdd:PRK08262 123 VPVapgTEGDWTHPPFSGVI-ADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVGGLgarAIAEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 157 FVQ---HPDFhalnpgiTLDEGLA-------NPSEEFSVF-YGEKCPWWITVHCGGDPGHGSRFIENTAAAKLHSVISRF 225
Cdd:PRK08262 202 LKErgvRLAF-------VLDEGGAitegvlpGVKKPVALIgVAEKGYATLELTARATGGHSSMPPRQTAIGRLARALTRL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 226 ------LEFREKEK-------------NR-LLSDPNLTLGDV---------------TTVNLTRVSGGVSFNVVPSEMTA 270
Cdd:PRK08262 275 ednplpMRLRGPVAemfdtlapemsfaQRvVLANLWLFEPLLlrvlakspetaamlrTTTAPTMLKGSPKDNVLPQRATA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 271 TFDLRIPP--TVNlKEFERqlegwCREA--GDNITWEYHQKCMNERVTTPDDSnPWWKAFSTPCKEM--GLKLKPEIFPA 344
Cdd:PRK08262 355 TVNFRILPgdSVE-SVLAH-----VRRAvaDDRVEIEVLGGNSEPSPVSSTDS-AAYKLLAATIREVfpDVVVAPYLVVG 427
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 50417585 345 ATDSRYIRTAGYSALGFSPMNNTP---ILLHDHNEYLNEDVFLRGIQIYTKIIASLAS 399
Cdd:PRK08262 428 ATDSRHYSGISDNVYRFSPLRLSPedlARFHGTNERISVANYARMIRFYYRLIENAAG 485
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
6-399 |
3.34e-36 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 136.27 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 6 ATEDPAtSLFREYLNIRTVQPDP-DYDKGIQFLIRVAEEIGLESKTLE--------LHPGRVILILtWKGTDPqlRSVIL 76
Cdd:PRK08651 4 MMFDIV-EFLKDLIKIPTVNPPGeNYEEIAEFLRDTLEELGFSTEIIEvpneyvkkHDGPRPNLIA-RRGSGN--PHLHF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 77 NSHTDVVPVFEEFWTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRfprTIHLTLVPDEEIGGHKGMEL 156
Cdd:PRK08651 80 NGHYDVVPPGEGWSVNVPFEP-KVKDGKVYGRGASDMKGGIAALLAAFERLDPAGDG---NIELAIVPDEETGGTGTGYL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 157 fvqhpdfhALNPGITLDEGL-ANPSEEFSVFYGEKCPWWITVHCGGDPGHGSR-FIENTAAAKLHSVISRFLE-FREKEK 233
Cdd:PRK08651 156 --------VEEGKVTPDYVIvGEPSGLDNICIGHRGLVWGVVKVYGKQAHASTpWLGINAFEAAAKIAERLKSsLSTIKS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 234 NRLLSDPnltLGDVTTVNLTR--VSGGVSFNVVPSEMTATFDLRIPPTVNL----KEFERQLEGWCREAGDNITWEYHQK 307
Cdd:PRK08651 228 KYEYDDE---RGAKPTVTLGGptVEGGTKTNIVPGYCAFSIDRRLIPEETAeevrDELEALLDEVAPELGIEVEFEITPF 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 308 cMNERVTTPDdsNPWWKAFSTPCKE-MGLKLKPEIFPAATDSRYIRTAGYSALGFSPMNntPILLHDHNEYLNEDVFLRG 386
Cdd:PRK08651 305 -SEAFVTDPD--SELVKALREAIREvLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGE--LELAHAPDEYVEVKDVEKA 379
|
410
....*....|...
gi 50417585 387 IQIYTKIIASLAS 399
Cdd:PRK08651 380 AKVYEEVLKRLAK 392
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
13-378 |
2.36e-35 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 133.68 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 13 SLFREYLNIRTVQPDPDYDKGIQ-FLIRVAEEIGLESKTLELHPGR---VILILTWKGTDPQLRSVILNSHTDVVPVFE- 87
Cdd:TIGR01910 2 ELLKDLISIPSVNPPGGNEETIAnYIKDLLREFGFSTDVIEITDDRlkvLGKVVVKEPGNGNEKSLIFNGHYDVVPAGDl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 88 EFWTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHKGMELFVQhpdfhaln 167
Cdd:TIGR01910 82 ELWKTDPFKP-VEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLLQR-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 168 pGITLDEGL---ANPSEEFSVFYGEKCPWWITVHCGGDPGHGSR--FIENtAAAKLHSVISRFLEFrEKEKNRLLSDPNL 242
Cdd:TIGR01910 153 -GYFKDADGvliPEPSGGDNIVIGHKGSIWFKLRVKGKQAHASFpqFGVN-AIMKLAKLITELNEL-EEHIYARNSYGFI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 243 TLGdvTTVNLTRVSGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCREAGDNITWEYH---QKCMNERVTTPDDs 319
Cdd:TIGR01910 230 PGP--ITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYEnepVVKWSGPNETPPD- 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 320 NPWWKAFSTPCKEM-GLKLKPEIFPAATDSRYIRTAGYSALGFSPMNNTpiLLHDHNEYL 378
Cdd:TIGR01910 307 SRLVKALEAIIKKVrGIEPEVLVSTGGTDARFLRKAGIPSIVYGPGDLE--TAHQVNEYI 364
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
40-307 |
3.78e-34 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 131.51 E-value: 3.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 40 VAE---EIGLESKTLELHPGRVILILTWKGTDPQLRSVILNSHTDVVPVFEEFWTYPPFSAhKDKDGNIYARGAQDMKCV 116
Cdd:PRK07906 31 VAEklaEVGLEPTYLESAPGRANVVARLPGADPSRPALLVHGHLDVVPAEAADWSVHPFSG-EIRDGYVWGRGAVDMKDM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 117 TIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHKGMELFVQ-HPDFHAlnpGITldEGLanpSEE--FSV-------F 186
Cdd:PRK07906 110 DAMMLAVVRHLARTGRRPPRDLVFAFVADEEAGGTYGAHWLVDnHPELFE---GVT--EAI---SEVggFSLtvpgrdrL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 187 Y----GEKCPWWITVHCGGDPGHGSRFIENTAAAKLHSVISRF-------------------------LEFREkeknrll 237
Cdd:PRK07906 182 YlietAEKGLAWMRLTARGRAGHGSMVNDDNAVTRLAEAVARIgrhrwplvltptvrafldgvaeltgLEFDP------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 238 SDPNLT---LGDV---------TTVNLTRVSGGVSFNVVPSEMTATFDLRIPPTvNLKEFERQLEgwcREAGDNITWEYH 305
Cdd:PRK07906 255 DDPDALlakLGPAarmvgatlrNTANPTMLKAGYKVNVIPGTAEAVVDGRFLPG-REEEFLATVD---ELLGPDVEREWV 330
|
..
gi 50417585 306 QK 307
Cdd:PRK07906 331 HR 332
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
59-390 |
1.45e-33 |
|
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: 124.08 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 59 ILILTWKGTdPQLRSVILNSHTDVVPVFEEFWTYPPFSAHKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTI 138
Cdd:cd18669 1 NVIARYGGG-GGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 139 HLTLVPDEEIGGHKGMELFVqhpdfhalnpgitlDEGLANPSEEFSVFYGEKCPWWitvhcggDPGHGSRfientaaakl 218
Cdd:cd18669 80 VVAFTPDEEVGSGAGKGLLS--------------KDALEEDLKVDYLFVGDATPAP-------QKGVGIR---------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 219 hsvisrflefrekeknrllsdpnltlgdvttvnltrvsggvsfnvvpsemtatfdlripptvnlkeferqlegwcreagd 298
Cdd:cd18669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 299 nitweyhqkcmnervttpddsNPWWKAFSTPCKEMGLKLKPEI-FPAATDSRYIRTAGYSALGFSPMnnTPILLHDHNEY 377
Cdd:cd18669 129 ---------------------TPLVDALSEAARKVFGKPQHAEgTGGGTDGRYLQELGIPGVTLGAG--GGKGAHSPNER 185
|
330
....*....|...
gi 50417585 378 LNEDVFLRGIQIY 390
Cdd:cd18669 186 VNLEDLESALAVL 198
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
74-297 |
2.68e-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: 111.53 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 74 VILNSHTDVVPVFEEFWTYPPFSAHkDKDGNIYARGAQDMK----CVtiqyLEAVCRLKSEGRRFPrtIHLTLVPDEEIG 149
Cdd:cd03894 60 LLLSGHTDVVPVDGQKWSSDPFTLT-ERDGRLYGRGTCDMKgflaAV----LAAVPRLLAAKLRKP--LHLAFSYDEEVG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 150 --GHKGMelfvqhpdfhalnpgitLDEGLANPSEEFSVFYGE------------KCPWWITVHcgGDPGHGSR------F 209
Cdd:cd03894 133 clGVRHL-----------------IAALAARGGRPDAAIVGEptslqpvvahkgIASYRIRVR--GRAAHSSLpplgvnA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 210 IEntAAAKLhsvISRFLEFREKEKNRLLSDPnLTLGdVTTVNLTRVSGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQL 289
Cdd:cd03894 194 IE--AAARL---IGKLRELADRLAPGLRDPP-FDPP-YPTLNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARL 266
|
....*...
gi 50417585 290 EGWCREAG 297
Cdd:cd03894 267 RDYAEALL 274
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
54-395 |
2.14e-25 |
|
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: 106.62 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 54 HPGRVILILTWKGTDPQLRSVILNSHTDVVPVFE-EFWTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGR 132
Cdd:cd03895 57 YAGAPNVVGTHRPRGETGRSLILNGHIDVVPEGPvELWTRPPFEA-TIVDGWMYGRGAGDMKAGLAANLFALDALRAAGL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 133 RFPRTIHLTLVPDEEIGGHKGMElfvqhpdfhALNPGITLDEGLANPSEEFSVFYGEKCPWWITVHCGGDPGHGSRF--- 209
Cdd:cd03895 136 QPAADVHFQSVVEEECTGNGALA---------ALMRGYRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEAseg 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 210 ---IEntAAAKLHSVIsRFLEFR---EKEKNRLLSD---PNltlgdvtTVNLTRVSGGVSFNVVPSEmtATFDLRIP--P 278
Cdd:cd03895 207 vnaIE--KAMHLIQAL-QELEREwnaRKKSHPHFSDhphPI-------NFNIGKIEGGDWPSSVPAW--CVLDCRIGiyP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 279 TVNLKEFERQLEGWCREAGDNITWEYHQK-------CMNERVTTPDDSnPWWKAFSTPCKEM-GLKLKPEIFPAATDSR- 349
Cdd:cd03895 275 GESPEEARREIEECVADAAATDPWLSNHPpevewngFQAEGYVLEPGS-DAEQVLAAAHQAVfGTPPVQSAMTATTDGRf 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 50417585 350 YIRTAGYSALGFSPMNNTPillHDHNEYLNedvfLRGIQIYTKIIA 395
Cdd:cd03895 354 FVLYGDIPALCYGPGSRDA---HGFDESVD----LESLRKITKTIA 392
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
5-398 |
2.27e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 92.76 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 5 TATEDPATSLFREYLNIRTVqpdpdydKGIQFLIRVAEEIGLESKT----------LELHPGRVILILTWKGTDPQlRSV 74
Cdd:PRK09133 33 TADQQAARDLYKELIEINTT-------ASTGSTTPAAEAMAARLKAagfadadievTGPYPRKGNLVARLRGTDPK-KPI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 75 ILNSHTDVVPVFEEFWTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHKGM 154
Cdd:PRK09133 105 LLLAHMDVVEAKREDWTRDPFKL-VEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEGTPMNGV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 155 E-LFVQHPDFH----ALNPG--ITLDE-GLANPseeFSVFYGEKCPWWITVHCGGDPGHGSRFIENTAAAKLHSVISRFL 226
Cdd:PRK09133 184 AwLAENHRDLIdaefALNEGggGTLDEdGKPVL---LTVQAGEKTYADFRLEVTNPGGHSSRPTKDNAIYRLAAALSRLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 227 EFR-------------------------------------EKEKNRLLSDP--NLTLGdvTTVNLTRVSGGVSFNVVPSE 267
Cdd:PRK09133 261 AYRfpvmlndvtrayfkqsaaietgplaaamrafaanpadEAAIALLSADPsyNAMLR--TTCVATMLEGGHAENALPQR 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 268 MTATFDLRIPPTVNLKEFERQLEgwcrEAGDN--ITWEYhqkcMNERVTTPddSNPW----WKAFSTPCKEM--GLKLKP 339
Cdd:PRK09133 339 ATANVNCRIFPGDTIEAVRATLK----QVVADpaIKITR----IGDPSPSP--ASPLrpdiMKAVEKLTAAMwpGVPVIP 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50417585 340 EIFPAATDSRYIRTAGYSALGFSPMNNTPILLHDH--NEYLNEDVFLRGIQIYTKIIASLA 398
Cdd:PRK09133 409 SMSTGATDGRYLRAAGIPTYGVSGLFGDPDDTFAHglNERIPVASFYEGRDFLYELVKDLA 469
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
35-394 |
1.76e-18 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 86.09 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 35 QFLIRVAEEIGLESKTLELHPGRVILILTWKGTDPQLRsviLNSHTDVVPVF-EEFWTYPPFSAHKdKDGNIYARGAQDM 113
Cdd:PRK08588 26 NYLQDLFAKHGIESKIVKVNDGRANLVAEIGSGSPVLA---LSGHMDVVAAGdVDKWTYDPFELTE-KDGKLYGRGATDM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 114 KCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHkGMELFVQHpdfhalnpGITLD-EGL--ANPSEEFsVFYGEK 190
Cdd:PRK08588 102 KSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGEL-GAKQLTEK--------GYADDlDALiiGEPSGHG-IVYAHK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 191 CPWWITVHCGGDPGHGSR-FIENTAaaklhsvISRFLEF--REKEKNRLLSDPNLTLGDVTTVNlTRVSGGVSFNVVPSE 267
Cdd:PRK08588 172 GSMDYKVTSTGKAAHSSMpELGVNA-------IDPLLEFynEQKEYFDSIKKHNPYLGGLTHVV-TIINGGEQVNSVPDE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 268 MTATFDLRIPPTVNLKEFERQLEGWCRE----AGDNITWEYHqkcMNER-VTTPDDSnpwwkAFSTPCKEMGLK-LKPEI 341
Cdd:PRK08588 244 AELEFNIRTIPEYDNDQVISLLQEIINEvnqnGAAQLSLDIY---SNHRpVASDKDS-----KLVQLAKDVAKSyVGQDI 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 342 F----PAATDSRYIRTAG--YSALGFSP-MNNTPillHDHNEYLNEDVFLRGIQIYTKII 394
Cdd:PRK08588 316 PlsaiPGATDASSFLKKKpdFPVIIFGPgNNLTA---HQVDEYVEKDMYLKFIDIYKEII 372
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
54-395 |
6.45e-18 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 85.05 E-value: 6.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 54 HPGRVILILTWKGTDPQLRSVILNSHTDVVPVF-EEFWTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGR 132
Cdd:PRK06837 80 YSGAPNVVGTYRPAGKTGRSLILQGHIDVVPEGpLDLWSRPPFDP-VIVDGWMYGRGAADMKAGLAAMLFALDALRAAGL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 133 RFPRTIHLTLVPDEEIGGHKGMElfvqhpdfhALNPGITLDEGLANPSEEFSVFYGEKCPWWITVHCGGDPGHgSRFIEN 212
Cdd:PRK06837 159 APAARVHFQSVIEEESTGNGALS---------TLQRGYRADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVH-VREAGT 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 213 TAAA--KLHSVISRFLEFREKEKNRLLSDPNL-TLGDVTTVNLTRVSGGVSFNVVPSEmtATFDLRIP--PTVNLKEFER 287
Cdd:PRK06837 229 GANAidAAYHLIQALRELEAEWNARKASDPHFeDVPHPINFNVGIIKGGDWASSVPAW--CDLDCRIAiyPGVTAADAQA 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 288 QLEGWCREAGDNITWEYHqkcmnervttpddsNP---WWKAFS------TPCKEM------------GLKLKPEIFPAAT 346
Cdd:PRK06837 307 EIEACLAAAARDDRFLSN--------------NPpevVWSGFLaegyvlEPGSEAeaalarahaavfGGPLRSFVTTAYT 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 50417585 347 DSR-YIRTAGYSALGFSPMNNTPillHDHNEYLNEDVfLRGIqiyTKIIA 395
Cdd:PRK06837 373 DTRfYGLYYGIPALCYGPSGEGI---HGFDERVDLES-VRKV---TKTIA 415
|
|
| PRK06915 |
PRK06915 |
peptidase; |
8-302 |
1.14e-17 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 84.36 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 8 EDPATSLFREYLNIRTVQPDpdyDKGIQflIRVAE---EIGLE-------SKTLELHP----------GRVILILTWKGT 67
Cdd:PRK06915 16 EEEAVKLLKRLIQEKSVSGD---ESGAQ--AIVIEklrELGLDldiwepsFKKLKDHPyfvsprtsfsDSPNIVATLKGS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 68 DPQlRSVILNSHTDVVPVFE-EFWTYPPFSAHKdKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDE 146
Cdd:PRK06915 91 GGG-KSMILNGHIDVVPEGDvNQWDHHPYSGEV-IGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 147 EIGGHKGMElfvqhpdfhALNPGITLDEGLANPSEEFSVFYGEKCPWWITVHCGGDPGH-GSRFIENTAAAKLHSVISRF 225
Cdd:PRK06915 169 ESGGAGTLA---------AILRGYKADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHgGTRYEGVSAIEKSMFVIDHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 226 LEFrEKEKNRLLSDP---NLTLGdvTTVNLTRVSGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCREAGDNITW 302
Cdd:PRK06915 240 RKL-EEKRNDRITDPlykGIPIP--IPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAELNDVDEW 316
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
36-397 |
1.23e-16 |
|
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: 80.47 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 36 FLIRVAEEIGLESKTLELhpGRVILiltwkGTDPQLRSVILNSHTDVVPVFeefwtYPPfsahKDKDGNIYARGAQDMKC 115
Cdd:cd05653 26 FLEEIMKELGLEAWVDEA--GNAVG-----GAGSGPPDVLLLGHIDTVPGE-----IPV----RVEGGVLYGRGAVDAKG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 116 VTIQYLEAVCRLKSEGRRfprTIHLTLVPDEEIGGHKGMELFVQHPDFHAlnpgITLDEglanPSEEFSVFYGEKCPWWI 195
Cdd:cd05653 90 PLAAMILAASALNEELGA---RVVVAGLVDEEGSSKGARELVRRGPRPDY----IIIGE----PSGWDGITLGYRGSLLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 196 TVHCGGDPGHGSRFIENTAaaklHSVISRFLEFRekeknRLLSDPNLTLGDVTTVNLTRVSGGVSFNVVPSEMTATFDLR 275
Cdd:cd05653 159 KIRCEGRSGHSSSPERNAA----EDLIKKWLEVK-----KWAEGYNVGGRDFDSVVPTLIKGGESSNGLPQRAEATIDLR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 276 IPPTVNLKEFERQLEGWCREAgdniTWEYHQKCmnERVTTPDDsNPWWKAFSTPCKEMGlkLKPEIFPAATDSR---YIR 352
Cdd:cd05653 230 LPPRLSPEEAIALATALLPTC----ELEFIDDT--EPVKVSKN-NPLARAFRRAIRKQG--GKPRLKRKTGTSDmnvLAP 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 50417585 353 TAGYSALGFSPMNNTpiLLHDHNEYLNEDVFLRGIQIYTKIIASL 397
Cdd:cd05653 301 LWTVPIVAYGPGDST--LDHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
74-295 |
2.25e-16 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 79.85 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 74 VILNSHTDVVPVFEEFWTYPPFSAhKDKDGNIYARGAQDMK----CVtiqyLEAVCRLKSEGRRFPrtIHLTLVPDEEIG 149
Cdd:PRK07522 67 IVLSGHTDVVPVDGQAWTSDPFRL-TERDGRLYGRGTCDMKgfiaAA----LAAVPELAAAPLRRP--LHLAFSYDEEVG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 150 --GhkgmelfVQH--PDFHALNP---GITLDEglanPSeEFSVFYGEKCPWWITVHCGGDPGHGSRF------IEntAAA 216
Cdd:PRK07522 140 clG-------VPSmiARLPERGVkpaGCIVGE----PT-SMRPVVGHKGKAAYRCTVRGRAAHSSLApqgvnaIE--YAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 217 KLhsvISRFLEFREKEKNRLLSDPnltLGDV--TTVNLTRVSGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCR 294
Cdd:PRK07522 206 RL---IAHLRDLADRLAAPGPFDA---LFDPpySTLQTGTIQGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAE 279
|
.
gi 50417585 295 E 295
Cdd:PRK07522 280 A 280
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
11-397 |
3.23e-16 |
|
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: 79.38 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 11 ATSLFREYLNIRTVQPDpdyDKG-IQFLIRVAEEIGLESKtlELHPGRVILILTWKGTDPQLrsVILNSHTDVVPV-FEE 88
Cdd:TIGR01246 1 VTELAKELISRPSVTPN---DAGcQDIIAERLEKLGFEIE--WMHFGDTKNLWATRGTGEPV--LAFAGHTDVVPAgPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 89 FWTYPPFSAHKdKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEE---IGGHKGMELFVQH----P 161
Cdd:TIGR01246 74 QWSSPPFEPVE-RDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEgtaIDGTKKVVETLMArdelI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 162 DFHAlnpgitldegLANPSEEF----SVFYGEKCPWWITVHCGGDPGH-GSRFIENTAAAKLHSVISRFLEFREKEKNRL 236
Cdd:TIGR01246 153 DYCI----------VGEPSSVKklgdVIKNGRRGSITGNLTIKGIQGHvAYPHLANNPIHKAAPALAELTAIKWDEGNEF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 237 LSDPNLTLGDVttvnltRVSGGVSfNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCREAGDNITWEYHqkCMNERVTTP 316
Cdd:TIGR01246 223 FPPTSLQITNI------HAGTGAN-NVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWS--LSGEPFLTN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 317 DdsNPWWKAFSTPCKEMgLKLKPEIFPAA--TDSRYIRTAGYSALGFSPMNNTpilLHDHNEYLNEDVFLRGIQIYTKII 394
Cdd:TIGR01246 294 D--GKLIDKAREAIEET-NGIKPELSTGGgtSDGRFIALMGAEVVEFGPVNAT---IHKVNECVSIEDLEKLSDVYQDLL 367
|
...
gi 50417585 395 ASL 397
Cdd:TIGR01246 368 ENL 370
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
13-147 |
1.76e-15 |
|
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: 77.16 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 13 SLFREYLNIRTVQPDpdyDKGIQ-FLIRVAEEIGLESKTLELhpGRVI-LILTWKGTDPQLrsvILNSHTDVVPV-FEEF 89
Cdd:cd03891 2 ELAKELIRRPSVTPD---DAGAQdLIAERLKALGFTCERLEF--GGVKnLWARRGTGGPHL---CFAGHTDVVPPgDLEG 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 50417585 90 WTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEE 147
Cdd:cd03891 74 WSSDPFSP-TIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEE 130
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
68-294 |
2.54e-15 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349902 [Multi-domain] Cd Length: 341 Bit Score: 76.58 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 68 DPQLRSVILNSHTDVV-PVfeEFWTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRfPRTIHLTLVPDE 146
Cdd:cd05651 52 DEGKPTLLLNSHHDTVkPN--AGWTKDPFEP-VEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGPL-NYNLIYAASAEE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 147 EIGGHKGMElfvqhpdfhALNPGI-TLDEGLANPSEEFSVFYGEKCPWWITVHCGGDPGHGSRFIENTAAAKLHSVISRF 225
Cdd:cd05651 128 EISGKNGIE---------SLLPHLpPLDLAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAARNEGDNAIYKALDDIQWL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50417585 226 LEFREKEKNRLLSDPNLTlgdVTTVNltrvsGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCR 294
Cdd:cd05651 199 RDFRFDKVSPLLGPVKMT---VTQIN-----AGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLK 259
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
16-190 |
5.99e-15 |
|
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: 76.26 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 16 REYLNIRTVQPDPDYDKGIQF----------LIRVAEEIGLESKTLELHPGRVILiltwkGTDPQLRSVIlnSHTDVVPV 85
Cdd:TIGR01887 9 KELIAIDSVEDLEKAKEGAPFgegprkaldkFLEIAKRDGFTTENVDNYAGYIEY-----GQGEEVLGIL--GHLDVVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 86 FEEfWTYPPFSAHKdKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEiGGHKGMELFVQH---PD 162
Cdd:TIGR01887 82 GDG-WTSPPFEPTI-KDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEE-SGWKCIDYYFEHeemPD 158
|
170 180
....*....|....*....|....*...
gi 50417585 163 FhalnpGITldeglanPSEEFSVFYGEK 190
Cdd:TIGR01887 159 I-----GFT-------PDAEFPIIYGEK 174
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
78-377 |
7.81e-15 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 75.57 E-value: 7.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 78 SHTDVVPVFE-EFWTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHKGMEL 156
Cdd:cd05650 76 SHLDTVPPGDlSLWETDPWEP-VVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEYGIQY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 157 FVQHPD-FHALNPGITLDEGlaNPSEEFsVFYGEKCPWWITVHCGGDPGHGSRFIEN----TAAAKLHSVISRFLEFREK 231
Cdd:cd05650 155 LLNKFDlFKKDDLIIVPDFG--TEDGEF-IEIAEKSILWIKVNVKGKQCHASTPENGinafVAASNFALELDELLHEKFD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 232 EKNRLLSDPnltlgdVTTVNLTRVSGGV-SFNVVPSEMTATFDLRIPPTVN----LKEFERQLEGWCREAGDNITWEYHQ 306
Cdd:cd05650 232 EKDDLFNPP------YSTFEPTKKEANVpNVNTIPGYDVFYFDCRVLPTYKldevLKFVNKIISDFENSYGAGITYEIVQ 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50417585 307 KcMNERVTTPDDSNPWWKAFSTPCKEMGLKLKPEIFPAATDSRYIRTAGYSALGFSPMNNTPillHDHNEY 377
Cdd:cd05650 306 K-EQAPPATPEDSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETA---HQPNEY 372
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
35-395 |
5.28e-14 |
|
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.
Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 72.62 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 35 QFLIRVAEEIGLeskTLELHPGRVI---LILTWKGTDPqlRSVILNSHTDVVpvfeefwtYP-------PFSAhkdKDGN 104
Cdd:cd03885 26 ELLAEELEALGF---TVERRPLGEFgdhLIATFKGTGG--KRVLLIGHMDTV--------FPegtlafrPFTV---DGDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 105 IYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHKGMELFVQHPDFH--ALNPGITLDEGlanpsee 182
Cdd:cd03885 90 AYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRELIEEEAKGAdyVLVFEPARADG------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 183 fSVFYGEK--CPWWITVHcgGDPGH-GSRFIE----NTAAAklHSVisrfLEFREkeknrlLSDPnlTLGdvTTVNLTRV 255
Cdd:cd03885 163 -NLVTARKgiGRFRLTVK--GRAAHaGNAPEKgrsaIYELA--HQV----LALHA------LTDP--EKG--TTVNVGVI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 256 SGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCREA-GDNITWEYHQKcmnerVTTP-----DDSNPWWKAFSTP 329
Cdd:cd03885 224 SGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTlVPGTSVELTGG-----LNRPpmeetPASRRLLARAQEI 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50417585 330 CKEMGLKLKPEIFPAATDSRYIRTAGYSAL-GFSPMNNTPillHDHNEYLNEDVFLRGIQIYTKIIA 395
Cdd:cd03885 299 AAELGLTLDWEATGGGSDANFTAALGVPTLdGLGPVGGGA---HTEDEYLELDSLVPRIKLLARLLM 362
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
2-272 |
5.69e-14 |
|
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: 73.05 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 2 DLATATEDPATSLFREYLNIRTV--QPDPDYDKGIQF------LIRVAEEIGLESKTLELHPGRVililTWKGTDPQLrs 73
Cdd:cd03888 1 EEIDKYKDEILEDLKELVAIPSVrdEATEGAPFGEGPrkaldkFLDLAKRLGFKTKNIDNYAGYA----EYGEGEEVL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 74 VILNsHTDVVPVFEEfWTYPPFSAHKdKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGhKG 153
Cdd:cd03888 75 GILG-HLDVVPAGEG-WTTDPFKPVI-KDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGW-KC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 154 MELFVQH---PDFhalnpGITLDeglanpsEEFSVFYGEKcpwWITvhcggdpghgsrfientaAAKLHSVISrflefre 230
Cdd:cd03888 151 IEHYFEHeeyPDF-----GFTPD-------AEFPVINGEK---GIV------------------TVDLTFKID------- 190
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 50417585 231 keknrllsdpnltlgDVTTVNLTRVSGGVSFNVVPSEMTATF 272
Cdd:cd03888 191 ---------------DDKGYRLISIKGGEATNMVPDKAEAVI 217
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
16-396 |
1.38e-13 |
|
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: 71.98 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 16 REYLNIRTVQPDPDYDKGIQfliRVAEEIGlesKTLELHPGRVILILTWKGT---------DPQLRSVILNSHTDVVPVF 86
Cdd:cd03893 5 AELVAIPSVSAQPDRREELR---RAAEWLA---DLLRRLGFTVEIVDTSNGApvvfaefpgAPGAPTVLLYGHYDVQPAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 87 EEF-WTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHKGMELFVQHPDFHA 165
Cdd:cd03893 79 DEDgWDSDPFEL-TERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEESGSPSLDQLVEAHRDLLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 166 LNPGITLDeGLANPSEEFSVFYGEK--CPWWITVHCGGDPGHGSRF--IENTAAAKLHSVISRF---------------- 225
Cdd:cd03893 158 ADAIVISD-STWVGQEQPTLTYGLRgnANFDVEVKGLDHDLHSGLYggVVPDPMTALAQLLASLrdetgrilvpglydav 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 226 LEFREKEKN---------------------RLLSDPNLTlgdVTTVNLTRVSGGvSFNVVPSEMTATFDLRIPPTVNLKE 284
Cdd:cd03893 237 RELPEEEFRldagvleeveiiggttgsvaeRLWTRPALT---VLGIDGGFPGEG-SKTVIPPRARAKISIRLVPGQDPEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 285 FERQLEGWCREAGdnitweYHQKCMNerVTTPDDSNPWWKAFSTPCKEMGLKLKPEIFPAATDsrYIRTAG----YSALG 360
Cdd:cd03893 313 ASRLLEAHLEKHA------PSGAKVT--VSYVEGGMPWRSDPSDPAYQAAKDALRTAYGVEPP--LTREGGsipfISVLQ 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 50417585 361 FSPmnNTPILL----------HDHNEYLNEDVFLRGIQIYTKIIAS 396
Cdd:cd03893 383 EFP--QAPVLLigvgdpddnaHSPNESLRLGNYKEGTQAEAALLYS 426
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
42-149 |
1.80e-13 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 71.61 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 42 EEIGLESKTLELHPGRVILILTWKGTDPQ-LRSVILNSHTDVVPVFE-EFWTYPPFSAHKdKDGNIYARGAQDMKCVTIQ 119
Cdd:PRK08596 47 RKLGFSVDKWDVYPNDPNVVGVKKGTESDaYKSLIINGHMDVAEVSAdEAWETNPFEPTI-KDGWLYGRGAADMKGGLAG 125
|
90 100 110
....*....|....*....|....*....|
gi 50417585 120 YLEAVCRLKSEGRRFPRTIHLTLVPDEEIG 149
Cdd:PRK08596 126 ALFAIQLLHEAGIELPGDLIFQSVIGEEVG 155
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
8-295 |
4.16e-13 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 70.26 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 8 EDPATSLFREYLNIRTVQPDPD----YDKGiQFLIRVAEEIGLES-KTLELHPGRVI------LILTWKGTDPQLRSVIL 76
Cdd:PRK13983 4 RDEMIELLSELIAIPAVNPDFGgegeKEKA-EYLESLLKEYGFDEvERYDAPDPRVIegvrpnIVAKIPGGDGKRTLWII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 77 nSHTDVVPVFE-EFWTYPPFSAHKdKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHKGME 155
Cdd:PRK13983 83 -SHMDVVPPGDlSLWETDPFKPVV-KDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYGIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 156 -LFVQHPD-FHALNPGITLDEGlaNPSEEFsVFYGEKCPWWITVHCGGDPGHGSR----FIENTAAAKLHSVISRFLEFR 229
Cdd:PRK13983 161 yLLKKHPElFKKDDLILVPDAG--NPDGSF-IEIAEKSILWLKFTVKGKQCHASTpengINAHRAAADFALELDEALHEK 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50417585 230 EKEKNRLLSDPnltlgdVTTVNLTRVSGGV-SFNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCRE 295
Cdd:PRK13983 238 FNAKDPLFDPP------YSTFEPTKKEANVdNINTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIADE 298
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-304 |
4.63e-13 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal, and have been inferred by similarity as being related to both ArgE and DapE.
Pssm-ID: 349903 [Multi-domain] Cd Length: 340 Bit Score: 69.61 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 13 SLFREYLNIRTVQPDpDYDKGiQFLIRVAEEIGLESKTLELHPGRVILILTWKGTDPQLRsVILNSHTDVVPvfeefwTY 92
Cdd:cd05652 3 SLHKSLVEIPSISGN-EAAVG-DFLAEYLESLGFTVEKQPVENKDRFNVYAYPGSSRQPR-VLLTSHIDTVP------PF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 93 PPFSAHkDKDGNIYARGAQDMK-CVTIQYLeAVCRLKSEGRRFPRTIHLTLVPDEEIGGHkGMELFVqhpdfhalnpgit 171
Cdd:cd05652 74 IPYSIS-DGGDTIYGRGSVDAKgSVAAQII-AVEELLAEGEVPEGDLGLLFVVGEETGGD-GMKAFN------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 172 lDEGLANPSeefSVFYGE----------KCPWWITVHCGGDPGH------GSRFIENTAAAkLHSVISRflefrekeknR 235
Cdd:cd05652 138 -DLGLNTWD---AVIFGEptelklasghKGMLGFKLTAKGKAGHsgypwlGISAIEILVEA-LVKLIDA----------D 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50417585 236 LLSDPnlTLGDvTTVNLTRVSGGVSFNVVPSEMTATFDLRI---PPTVN--LKEFERQLEGWCREAGDNITWEY 304
Cdd:cd05652 203 LPSSE--LLGP-TTLNIGRISGGVAANVVPAAAEASVAIRLaagPPEVKdiVKEAVAGILTDTEDIEVTFTSGY 273
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
10-147 |
9.12e-13 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 68.96 E-value: 9.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 10 PATSLFREYLNIRTVQPDpdyDKGIQ-FLIRVAEEIGLESKTLELhpGRVI-LILTWKGTDPQLrsvILNSHTDVVPV-F 86
Cdd:PRK13009 3 DVLELAQDLIRRPSVTPD---DAGCQdLLAERLEALGFTCERMDF--GDVKnLWARRGTEGPHL---CFAGHTDVVPPgD 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50417585 87 EEFWTYPPFSAHKdKDGNIYARGAQDMK----CvtiqYLEAVCRLKSEGRRFPRTIHLTLVPDEE 147
Cdd:PRK13009 75 LEAWTSPPFEPTI-RDGMLYGRGAADMKgslaA----FVVAAERFVAAHPDHKGSIAFLITSDEE 134
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
11-304 |
5.01e-12 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 66.71 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 11 ATSLFREYLNIRTvqPDPDYDKGIQFLIRVaeeigLESKTLELHP---GRVILILTWKGTDpqlrsVILNSHTDVVPVFE 87
Cdd:PRK08652 4 AKELLKQLVKIPS--PSGQEDEIALHIMEF-----LESLGYDVHIesdGEVINIVVNSKAE-----LFVEVHYDTVPVRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 88 EFWTyppfsahkdkDGNI-YARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIhlTLVPDEEIGGhKGMELFVQhpdfhAL 166
Cdd:PRK08652 72 EFFV----------DGVYvYGTGACDAKGGVAAILLALEELGKEFEDLNVGI--AFVSDEEEGG-RGSALFAE-----RY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 167 NPGITL-----DEGLANPSeefsvfYG--EkcpwwITVHCGGDPGHGSrFIENTAAAklhsvISRFLEFREKEKNRLlsd 239
Cdd:PRK08652 134 RPKMAIvleptDLKVAIAH------YGnlE-----AYVEVKGKPSHGA-CPESGVNA-----IEKAFEMLEKLKELL--- 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50417585 240 PNLTLGDVTTVNLTRVSGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCreagDNITWEY 304
Cdd:PRK08652 194 KALGKYFDPHIGIQEIIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPIL----DEYTVKY 254
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
6-225 |
6.60e-12 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 66.71 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 6 ATEDPATSLFREYLNIRTVQPDPD-YDKGIQFLIRVAEEIGLESKTLELH--PG------RVILILTWKGTDPQlRSVIL 76
Cdd:PRK13013 11 ARRDDLVALTQDLIRIPTLNPPGRaYREICEFLAARLAPRGFEVELIRAEgaPGdsetypRWNLVARRQGARDG-DCVHF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 77 NSHTDVVPVFEEfWTYPPFSAHKdKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGHKGMEL 156
Cdd:PRK13013 90 NSHHDVVEVGHG-WTRDPFGGEV-KDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGGVAY 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50417585 157 FVQHPDF------HALNPgitldeglaNPSEEFSVFYGEKCPWWITVHCGGDPGHGSR-FIENTAAAKLHSVISRF 225
Cdd:PRK13013 168 LAEQGRFspdrvqHVIIP---------EPLNKDRICLGHRGVWWAEVETRGRIAHGSMpFLGDSAIRHMGAVLAEI 234
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
193-301 |
1.03e-11 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 61.21 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 193 WWITVHcgGDPGHGSRFIENTAAAKLhsvISRFL-EFREKEKNRLLSDPNltlgdvTTVNLTRVSGGVSFNVVPSEMTAT 271
Cdd:pfam07687 9 GHLTVK--GKAGHSGAPGKGVNAIKL---LARLLaELPAEYGDIGFDFPR------TTLNITGIEGGTATNVIPAEAEAK 77
|
90 100 110
....*....|....*....|....*....|
gi 50417585 272 FDLRIPPTVNLKEFERQLEGWCREAGDNIT 301
Cdd:pfam07687 78 FDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
72-395 |
2.08e-11 |
|
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: 64.88 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 72 RSVILNSHTDVVPVFEEfWTYPPFSAHKDkDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGH 151
Cdd:cd02697 74 RTVALNAHGDVVPPGDG-WTRDPYGAVVE-DGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 152 KGmelfvqhpdfhalnPGITLDEGLANP--------SEEFSVFYGEKCPWWITVHcgGDPGHGSrfIENT-------AAA 216
Cdd:cd02697 152 LG--------------PGWLLRQGLTKPdlliaagfSYEVVTAHNGCLQMEVTVH--GKQAHAA--IPDTgvdalqgAVA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 217 KLHSVISRFLEFREKEKN-RLLSDPNLTLGdvttvnltRVSGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQLEGWCRE 295
Cdd:cd02697 214 ILNALYALNAQYRQVSSQvEGITHPYLNVG--------RIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIAD 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 296 AGDN---ITWEYHQKCMNERVTTPDDSNPWWKAFSTPCKEM-GLKLKPEIFPAATDSRYIRTAGYSALGFSPMNNTpiLL 371
Cdd:cd02697 286 AAASmpgISVDIRRLLLANSMRPLPGNAPLVEAIQTHGEAVfGEPVPAMGTPLYTDVRLYAEAGIPGVIYGAGPRT--VL 363
|
330 340
....*....|....*....|....
gi 50417585 372 HDHNEYLNEDVFLRGIQIYTKIIA 395
Cdd:cd02697 364 ESHAKRADERLQLEDLRRATKVIA 387
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
17-149 |
1.14e-10 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 62.71 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 17 EYLNIRTVQPDPDYDKGIQ----FLIRVAEEIGLEskTLELHP--GRVILILTWKGtDPQLRSVILNSHTDVVPVF-EEF 89
Cdd:cd05680 6 ELLRIPSVSADPAHKGDVRraaeWLADKLTEAGFE--HTEVLPtgGHPLVYAEWLG-APGAPTVLVYGHYDVQPPDpLEL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 90 WTYPPFSAHKdKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIG 149
Cdd:cd05680 83 WTSPPFEPVV-RDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIG 141
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
79-307 |
1.18e-10 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 62.94 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 79 HTDVVPVFEEfWTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEiGGHKGMELFV 158
Cdd:PRK07318 87 HLDVVPAGDG-WDTDPYEP-VIKDGKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRFIVGTDEE-SGWKCMDYYF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 159 QH---PDFhalnpGITldeglanPSEEFSVFYGEKcpwwitvhcggdpghgsrfientaaaklhSVISRFLEFREKEKNr 235
Cdd:PRK07318 164 EHeeaPDF-----GFS-------PDAEFPIINGEK-----------------------------GITTFDLVHFEGENE- 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50417585 236 llsdpnltlGDVTtvnLTRVSGGVSFNVVPSEMTATFDLRIPPTV--NLKEF--ERQLEGWCREAGDNITWEYHQK 307
Cdd:PRK07318 202 ---------GDYV---LVSFKSGLRENMVPDSAEAVITGDDLDDLiaAFEAFlaENGLKGELEEEGGKLVLTVIGK 265
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
16-190 |
4.31e-10 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 61.20 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 16 REYLNIRTVQPdpdYDKGIQ----FLIRVAEEIGLESKTLElHPGRVILILTWKGTDPQlrSVILNSHTDVVPV--FEEf 89
Cdd:cd05681 6 RDLLKIPSVSA---QGRGIPetadFLKEFLRRLGAEVEIFE-TDGNPIVYAEFNSGDAK--TLLFYNHYDVQPAepLEL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 90 WTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEIGGhKGMELFV-QHPDFHALNp 168
Cdd:cd05681 79 WTSDPFEL-TIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGS-PNLEKFVaEHADLLKAD- 155
|
170 180
....*....|....*....|..
gi 50417585 169 GITLDEGLANPSEEFSVFYGEK 190
Cdd:cd05681 156 GCIWEGGGKNPKGRPQISLGVK 177
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
69-376 |
4.15e-09 |
|
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: 57.84 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 69 PQLRSVILNSHTDVVPVFEEFwtyPPfsaHKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFprtiHLTLV--PDE 146
Cdd:cd05647 51 GLASRVILAGHLDTVPVAGNL---PS---RVEEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKH----DLTLIfyDCE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 147 EIGGHK-GME-LFVQHPDFHALNPGITLD------EGLANPSEEFsvfygekcpwWITVHcgGDPGHGSR-FIENTAAAK 217
Cdd:cd05647 121 EVAAELnGLGrLAEEHPEWLAADFAVLGEptdgtiEGGCQGTLRF----------KVTTH--GVRAHSARsWLGENAIHK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 218 LHSVISRFLEFREKEKNRllsdPNLTLGDVttVNLTRVSGGVSFNVVPSEMTATFDLRIPPTVNLKEFERQLegwcREAG 297
Cdd:cd05647 189 LAPILARLAAYEPRTVNI----DGLTYREG--LNAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHV----REVF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 298 D--NITWEYHQKCMNERvttPDDSNPWWKAFSTPCKEmglklKPEIFPAATDSRYIRTAGYSALGFSPMNntPILLHDHN 375
Cdd:cd05647 259 EglGYEIEVTDLSPGAL---PGLDHPVARDLIEAVGG-----KVRAKYGWTDVARFSALGIPAVNFGPGD--PLLAHKRD 328
|
.
gi 50417585 376 E 376
Cdd:cd05647 329 E 329
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
45-278 |
7.53e-09 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349935 [Multi-domain] Cd Length: 379 Bit Score: 57.10 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 45 GLESKTLELHPGRVILILTWKGTDPQlRSVILNSHTDVVPVFeefwTYP--PFSAHKdKDGNIYARGAQDMKCVTIQYLE 122
Cdd:cd08013 43 GIEAHRIEGTPGRPSVVGVVRGTGGG-KSLMLNGHIDTVTLD----GYDgdPLSGEI-ADGRVYGRGTLDMKGGLAACMA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 123 AVCRLKSEGRRfpRTIHLTLVPDEEiGGHKGMElfvqhpdfHALNPGITLDEGLANPSEEFSVFYGEKCPWWITVHCGGD 202
Cdd:cd08013 117 ALADAKEAGLR--GDVILAAVADEE-DASLGTQ--------EVLAAGWRADAAIVTEPTNLQIIHAHKGFVWFEVDIHGR 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50417585 203 PGHGSRfIENTAAAKLHSviSRFLEFREKEKNRLLSDPNLTLGDVTTVNLTRVSGGVSFNVVPSEMTATFDLRIPP 278
Cdd:cd08013 186 AAHGSR-PDLGVDAILKA--GYFLVALEEYQQELPERPVDPLLGRASVHASLIKGGEEPSSYPARCTLTIERRTIP 258
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
78-148 |
5.74e-08 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 54.18 E-value: 5.74e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50417585 78 SHTDVVPVF-EEFWTYPPFSAHKDkDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFPRTIHLTLVPDEEI 148
Cdd:PRK13004 76 AHIDTVGIGdIKNWDFDPFEGEED-DGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEED 146
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
31-159 |
9.79e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 53.60 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 31 DKGIQFLIRVAEEIGLESKtLELHPGR-VILILTWKGTDpqlRSVILNSHTDVVPV--FEEfWTYPPFSAhKDKDGNIYA 107
Cdd:PRK06446 25 EETANYLKDTMEKLGIKAN-IERTKGHpVVYGEINVGAK---KTLLIYNHYDVQPVdpLSE-WKRDPFSA-TIENGRIYA 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 50417585 108 RGAQDMKCVTIQYLEAVCRLKSEGrRFPRTIHLTLVPDEEIGGhKGMELFVQ 159
Cdd:PRK06446 99 RGASDNKGTLMARLFAIKHLIDKH-KLNVNVKFLYEGEEEIGS-PNLEDFIE 148
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
34-290 |
1.61e-07 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 52.75 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 34 IQFLIRVAEEIGLESKTLELHpgrvILILTWKGT-DPQLRSVILNSHTDVVPVFEefwtyppfsahKD------KDGNIY 106
Cdd:COG2195 26 ADYLVEELKELGLEVEEDEAG----NVIATLPATpGYNVPTIGLQAHMDTVPQFP-----------GDgikpqiDGGLIT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 107 AR-----GAQDmK--CVTIqyLEAVCRLKSEGRRFPrTIHLTLVPDEEIGGHkGMELFvqhpDFHALNP--GITLDegla 177
Cdd:COG2195 91 ADgtttlGADD-KagVAAI--LAALEYLKEPEIPHG-PIEVLFTPDEEIGLR-GAKAL----DVSKLGAdfAYTLD---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 178 npSEEFSVFYGEkCP----WWITVH-CGGDPG--HGSRFIENTAAAKLhsvISRFLEFREKEKnrllsdpnltlgdvTTV 250
Cdd:COG2195 158 --GGEEGELEYE-CAgaadAKITIKgKGGHSGdaKEKMINAIKLAARF---LAALPLGRIPEE--------------TEG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 50417585 251 NLTRVSGGVSFNVVPSEMTATFDLRippTVNLKEFERQLE 290
Cdd:COG2195 218 NEGFIHGGSATNAIPREAEAVYIIR---DHDREKLEARKA 254
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
29-149 |
4.79e-06 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 48.59 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 29 DYDKGIQFLIRVAEEIGLESKTLELHPGRVILILTWKGTdPQLRSVILNSHTDVVPVFE-EFWTYPPFSAhKDKDGNIYA 107
Cdd:PRK08201 38 DVRKAAEWLAGALEKAGLEHVEIMETAGHPIVYADWLHA-PGKPTVLIYGHYDVQPVDPlNLWETPPFEP-TIRDGKLYA 115
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 50417585 108 RGAQDMKCVTIQYLEAV-CRLKSEGrRFPRTIHLTLVPDEEIG 149
Cdd:PRK08201 116 RGASDDKGQVFMHLKAVeALLKVEG-TLPVNVKFCIEGEEEIG 157
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
21-165 |
5.12e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 48.36 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 21 IRTVQPDP----DYDKGIQFLIRVAEEIGLESKTLELHPGRVILILTWKGtDPQLRSVILNSHTDVVPVF-EEFWTYPPF 95
Cdd:PRK07907 30 IPSVAADPfrreEVARSAEWVADLLREAGFDDVRVVSADGAPAVIGTRPA-PPGAPTVLLYAHHDVQPPGdPDAWDSPPF 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50417585 96 SAhKDKDGNIYARGAQDMKCVTIQYLEAvcrLKSEGRRFPrtIHLTLVPD--EEIGGhKGMELFV-QHPD-FHA 165
Cdd:PRK07907 109 EL-TERDGRLYGRGAADDKGGIAMHLAA---LRALGGDLP--VGVTVFVEgeEEMGS-PSLERLLaEHPDlLAA 175
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
39-397 |
6.75e-06 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 47.80 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 39 RVAEEIGLESKTL---ELHPGRVILILTWKGTDPQLrsVILNSHTDVVPVFEEF-WTYPPFSAhKDKDGNIYARGAQDMK 114
Cdd:cd05649 19 GVVERIEEEMEKLgfdEVEIDPMGNVIGYIGGGKKK--ILFDGHIDTVGIGNIDnWKFDPYEG-YETDGKIYGRGTSDQK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 115 CVTIQYLEAVCRLKSEGRR-FPRTIHLTLVPDEEI-GGHKGMELFVQH---PDFhalnpgITLDEglanPSeEFSVFYGE 189
Cdd:cd05649 96 GGLASMVYAAKIMKDLGLRdFAYTILVAGTVQEEDcDGVCWQYISKADkikPDF------VVSGE----PT-DGNIYRGQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 190 KCPWWITVHCGGDPGHGS---RfiENTAAAKLHSVISRFLEFREK-EKNRLLSDPNLTLGDVttvnltrVSGGVSFNVVP 265
Cdd:cd05649 165 RGRMEIRVDTKGVSCHGSapeR--GDNAVYKMADIIQDIRQLNPNfPEAPFLGRGTLTVTDI-------FSTSPSRCAVP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 266 SEMTATFDLRIppTVN------LKEFeRQLEGwCREAGDNIT---WEYHQKCMNERVTTPDDSNPWW---------KAFS 327
Cdd:cd05649 236 DSCRISIDRRL--TVGetwegcLEEI-RALPA-VKKYGDDVAvsmYNYDRPSYTGEVYESERYFPTWllpedhelvKALL 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50417585 328 TPCKEMGLKlKPEI--FPAATD-SRYIRTAGYSALGFSPmnNTPILLHDHNEYLNEDVFLRGIQIYTKIIASL 397
Cdd:cd05649 312 EAYKALFGA-RPLIdkWTFSTNgVSIMGRAGIPCIGFGP--GAENQAHAPNEYTWKEDLVRCAAGYAAIPTSY 381
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
66-135 |
9.35e-06 |
|
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: 47.60 E-value: 9.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50417585 66 GTDPQLRSVILNSHTDVVPV-FEEFWTYPPFSAHkDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRFP 135
Cdd:cd05676 80 GSDPSKKTVLIYGHLDVQPAkLEDGWDTDPFELT-EKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELP 149
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
11-397 |
3.85e-05 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 45.54 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 11 ATSLFREYLNIRTvqPDPDYDKGIQFLIRVAEEIGLeskTLELHPGRVILILTwkgtDPQlrsVILNSHTDVVPVFeefw 90
Cdd:PRK00466 12 AKELLLDLLSIYT--PSGNETNATKFFEKISNELNL---KLEILPDSNSFILG----EGD---ILLASHVDTVPGY---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 91 tYPPfsahKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRfprtIHLTLVPDEEiGGHKGM-ELfvqhpdfhaLNPG 169
Cdd:PRK00466 76 -IEP----KIEGEVIYGRGAVDAKGPLISMIIAAWLLNEKGIK----VMVSGLADEE-STSIGAkEL---------VSKG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 170 ITLDEGL-ANPSEEFSVFYGEKCPWWITVHCGGDPGHGSRFIENTAAaklhSVISRFLEFREKEKNrlLSDPNLTLgdvt 248
Cdd:PRK00466 137 FNFKHIIvGEPSNGTDIVVEYRGSIQLDIMCEGTPEHSSSAKSNLIV----DISKKIIEVYKQPEN--YDKPSIVP---- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 249 tvnlTRVSGGVSFNVVPSEMTATFDLRIPptvnlkefERQLEGwcrEAGDNITWEYHQKCMNERVTTP----DDSNPWWK 324
Cdd:PRK00466 207 ----TIIRAGESYNVTPAKLYLHFDVRYA--------INNKRD---DLISEIKDKFQECGLKIVDETPpvkvSINNPVVK 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50417585 325 AFSTPCKEMGlkLKPEIFPAA--TDSRYIRTAGYSALGFSPMNntPILLHDHNEYLNEDVFLRGIQIYTKIIASL 397
Cdd:PRK00466 272 ALMRALLKQN--IKPRLVRKAgtSDMNILQKITTSIATYGPGN--SMLEHTNQEKITLDEIYIAVKTYMLAIEEL 342
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
3-159 |
5.70e-05 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 44.89 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 3 LATATEDPATSLFR--EYLNIRTVQPDPDY----DKGIQFLIRVAEEIGLESKTLELhPGRVILILTWKGTDPQLRSVIL 76
Cdd:PRK09104 9 LDHIDANLDASLERlfALLRIPSISTDPAYaadcRKAADWLVADLASLGFEASVRDT-PGHPMVVAHHEGPTGDAPHVLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 77 NSHTDVVPVF-EEFWTYPPFS----AHKDKDGNIYARGAQDMKCVTIQYLEAvCR-LKSEGRRFPrtIHLT-LVPDEEIG 149
Cdd:PRK09104 88 YGHYDVQPVDpLDLWESPPFEprikETPDGRKVIVARGASDDKGQLMTFVEA-CRaWKAVTGSLP--VRVTiLFEGEEES 164
|
170
....*....|
gi 50417585 150 GHKGMELFVQ 159
Cdd:PRK09104 165 GSPSLVPFLE 174
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
13-156 |
1.30e-04 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 43.99 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 13 SLFREYLNIRTVQpDPDydKGI-------QFLIRVAEEIGLESKTLElHPGRVILILTWKGTDPQLrsvILNSHTDVVPV 85
Cdd:PRK08554 5 ELLSSLVSFETVN-DPS--KGIkpskecpKFIKDTLESWGIESELIE-KDGYYAVYGEIGEGKPKL---LFMAHFDVVPV 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50417585 86 FEEFWTYPPFSAhKDKDGNIYARGAQDMKCVTIQYLEAVCRLKSEGRRfpRTIHLTLVPDEEIGGHKGMEL 156
Cdd:PRK08554 78 NPEEWNTEPFKL-TVKGDKAYGRGSADDKGNVASVMLALKELSKEPLN--GKVIFAFTGDEEIGGAMAMHI 145
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
45-112 |
1.78e-04 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 43.60 E-value: 1.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50417585 45 GLESKTLELHPGRVILILTWKGTDPQLRSVILNSHTDVVPVFEEFWTYPPFSAHKDKDgNIYARGAQD 112
Cdd:cd08012 52 PLVIDHVSYVKGRGNIIVEYPGTVDGKTVSFVGSHMDVVTANPETWEFDPFSLSIDGD-KLYGRGTTD 118
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
195-306 |
1.82e-04 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 43.36 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50417585 195 ITVHcgGDPGHGSRfIENT-----AAA----KLHSVISRFLefrekeknrllsDPnltlGDVTTVNLTRVSGGVSFNVVP 265
Cdd:cd03886 176 ITVK--GKGGHGAS-PHLGvdpivAAAqivlALQTVVSREL------------DP----LEPAVVTVGKFHAGTAFNVIP 236
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 50417585 266 SE--MTAT---FDLRIPPTVnLKEFERQLEGWCREAGDNITWEYHQ 306
Cdd:cd03886 237 DTavLEGTirtFDPEVREAL-EARIKRLAEGIAAAYGATVELEYGY 281
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
76-114 |
7.38e-03 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 38.27 E-value: 7.38e-03
10 20 30
....*....|....*....|....*....|....*....
gi 50417585 76 LNSHTDVVPVFEEFWTYPPFSAhKDKDGNIYARGAQDMK 114
Cdd:PRK05111 76 LAGHTDTVPFDEGRWTRDPFTL-TEHDGKLYGLGTADMK 113
|
|
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