|
Name |
Accession |
Description |
Interval |
E-value |
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
9-364 |
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: 697.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 9 EHPSVTLFRQYLRIRTVQPKPDY-----------------------------------GTNPTLSSILLNSHTDVVPVFK 53
Cdd:cd05646 1 EDPAVTRFREYLRINTVHPNPDYdacveflkrqadelglpvrvievvpgkpvvvltweGSNPELPSILLNSHTDVVPVFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 54 EHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHALR 133
Cdd:cd05646 81 EKWTHDPFSAHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGHDGMEKFVKTEEFKKLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 134 AGFALDEGIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFREKEWQRLQSNPHLKEGSV 213
Cdd:cd05646 161 VGFALDEGLASPTEEYRVFYGERSPWWVVITAPGTPGHGSKLLENTAGEKLRKVIESIMEFRESQKQRLKSNPNLTLGDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 214 TSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDSNPWWAAFS 293
Cdd:cd05646 241 TTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGRGVTYEFEQKSPEKDPTSLDDSNPWWAAFK 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312032409 294 RVCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALA 364
Cdd:cd05646 321 KAVKEMGLKLKPEIFPAATDSRYIRALGIPALGFSPMNNTPILLHDHNEFLNEDVFLRGIEIYEKIIPALA 391
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
1-366 |
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: 676.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 1 MTSKGpEEEHPSVTLFRQYLRIRTVQPKPDY-----------------------------------GTNPTLSSILLNSH 45
Cdd:TIGR01880 1 MSSSK-WEEDIAVTRFREYLRINTVQPNPDYaacvdflikqadelglarktiefvpgkpvvvltwpGSNPELPSILLNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 46 TDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQ 125
Cdd:TIGR01880 80 TDVVPVFREHWTHPPFSAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEKFAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 126 RPEFHALRAGFALDEGIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFREKEWQRLQSN 205
Cdd:TIGR01880 160 TDEFKALNLGFALDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKLMENTAMEKLEKSVESIRRFRESQFQLLQSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 206 PHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDS 285
Cdd:TIGR01880 240 PDLAIGDVTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAGEGVTYEFSQHSGKPLVTPHDDS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 286 NPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALAS 365
Cdd:TIGR01880 320 NPWWVAFKDAVKEMGCTFKPEILPGSTDSRYIRAAGVPALGFSPMNNTPVLLHDHNEFLNEAVFLRGIEIYQTLISALAS 399
|
.
gi 312032409 366 V 366
Cdd:TIGR01880 400 V 400
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
6-364 |
5.00e-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: 221.68 E-value: 5.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 6 PEEEHPSVTLFRQYLR-----IRTVQPKPDYG-------TNPTLSSILLNSHTDVVPV-FKEHWSHDPFEAfKDSEGYIY 72
Cdd:COG0624 28 SGEEAAAAELLAELLEalgfeVERLEVPPGRPnlvarrpGDGGGPTLLLYGHLDVVPPgDLELWTSDPFEP-TIEDGRLY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 73 ARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHqGMELFVQRpEFHALRAGFALdegIANPTDAFTVF 152
Cdd:COG0624 107 GRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSP-GARALVEE-LAEGLKADAAI---VGEPTGVPTIV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 153 YSERSPWWVRVTSTGRPGHASRFME-DTAAEKLHKVVNSILAFREkewqRLQSNPHLKEgsvTSVNLTKLEGGVAYNVIP 231
Cdd:COG0624 182 TGHKGSLRFELTVRGKAAHSSRPELgVNAIEALARALAALRDLEF----DGRADPLFGR---TTLNVTGIEGGTAVNVIP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 232 ATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFaqKWMHPQVTP--TDDSNPWWAAFSRVCKD-MNLTLEPEIM 308
Cdd:COG0624 255 DEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEV--EVLGDGRPPfeTPPDSPLVAAARAAIREvTGKEPVLSGV 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 312032409 309 PAATDNRYI-RAVGVPALGFSPMNRTpvLLHDHDERLHEAVFLRGVDIYTRLLPALA 364
Cdd:COG0624 333 GGGTDARFFaEALGIPTVVFGPGDGA--GAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
41-360 |
4.69e-62 |
|
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: 201.42 E-value: 4.69e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 41 LLNSHTDVVPVfkEHWSHDPFEAFKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRfPRTIHMTFVPDEEvGGHQGM 120
Cdd:pfam01546 1 LLRGHMDVVPD--EETWGWPFKSTED--GKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEE-GGMGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 121 ELFVQRPEFHALRAGFALDEGIANPTD-----AFTVFYSERSPWWVRVTSTGRPGHASRF-MEDTAAEKLHKVVNSILAF 194
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFGLHIGEPTLleggiAIGVVTGHRGSLRFRVTVKGKGGHASTPhLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 195 REKEwqrlqsNPHLKEGSVTSVNLTKLEGGVayNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFAQKW 274
Cdd:pfam01546 155 VSRN------VDPLDPAVVTVGNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 275 MHPQVTPTDDSNPWWAAFSRVCKDM---NLTLEPEIMPAATDNRYIrAVGVPA--LGFSPMNRTpvlLHDHDERLHEAVF 349
Cdd:pfam01546 227 VEGGAPPLVNDSPLVAALREAAKELfglKVELIVSGSMGGTDAAFF-LLGVPPtvVFFGPGSGL---AHSPNEYVDLDDL 302
|
330
....*....|.
gi 312032409 350 LRGVDIYTRLL 360
Cdd:pfam01546 303 EKGAKVLARLL 313
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
32-360 |
9.44e-49 |
|
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: 169.85 E-value: 9.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 32 GTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPD 111
Cdd:cd05675 60 GTDPSAGPLLLLGHIDVVPADASDWSVDPFSG-EIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVAD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 112 EEVGGHQGMELFVQ-RPEFHAlRAGFALDEG------IANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKL 184
Cdd:cd05675 139 EEAGGENGAKWLVDnHPELFD-GATFALNEGgggslpVGKGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRPTDDNAITRL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 185 HKVVNSILAF--------------------REKEWQRL---------------QSNPHLKEGSVTSVNLTKLEGGVAYNV 229
Cdd:cd05675 218 AEALRRLGAHnfpvrltdetayfaqmaelaGGEGGALMltavpvldpalaklgPSAPLLNAMLRNTASPTMLDAGYATNV 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 230 IPATMSASFDFRVAPDVDFKAFEEQLQswcQAAGE-GVTLEFAqkWMHPQVTPTDDSnPWWAAFSRVCKDM--NLTLEPE 306
Cdd:cd05675 298 LPGRATAEVDCRILPGQSEEEVLDTLD---KLLGDpDVSVEAV--HLEPATESPLDS-PLVDAMEAAVQAVdpGAPVVPY 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 312032409 307 IMPAATDNRYIRAVGVPALGFSPMNRTPVL-----LHDHDERLHEAVFLRGVDIYTRLL 360
Cdd:cd05675 372 MSPGGTDAKYFRRLGIPGYGFAPLFLPPELdytglFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
40-360 |
2.58e-45 |
|
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: 159.00 E-value: 2.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 40 ILLNSHTDVVPVFKEH-WSHDPFEAfKDSEGYIYARGAQDMK---CVSIQyleAVRRLKVEGHRFPRTIHMTFVPDEEVG 115
Cdd:cd08659 57 LLLNGHIDTVPPGDGDkWSFPPFSG-RIRDGRLYGRGACDMKgglAAMVA---ALIELKEAGALLGGRVALLATVDEEVG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 116 GhQGMELFVQRPefHALRAGFALdegIANPTDaFTVFYSERSPWWVRVTSTGRPGHASrfMEDTAAEKLHKVVNSILAFR 195
Cdd:cd08659 133 S-DGARALLEAG--YADRLDALI---VGEPTG-LDVVYAHKGSLWLRVTVHGKAAHSS--MPELGVNAIYALADFLAELR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 196 EKEWqRLQSNPHLKEgsvTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFAQKWM 275
Cdd:cd08659 204 TLFE-ELPAHPLLGP---PTLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 276 HPQVTPTDdsNPWWAAFSRVCKDMNLTLEPEIMPAATDNRYI-RAVGVPALGFSPMNrtPVLLHDHDERLHEAVFLRGVD 354
Cdd:cd08659 280 PPFFTDPD--HPLVQALQAAARALGGDPVVRPFTGTTDASYFaKDLGFPVVVYGPGD--LALAHQPDEYVSLEDLLRAAE 355
|
....*.
gi 312032409 355 IYTRLL 360
Cdd:cd08659 356 IYKEII 361
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
32-365 |
5.40e-38 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 142.39 E-value: 5.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 32 GTNPTLSSILLNSHTDVVPV---FKEHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTF 108
Cdd:PRK08262 106 GSDPSLKPIVLMAHQDVVPVapgTEGDWTHPPFSGVIA-DGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 109 VPDEEVGGH---QGMELFVQRpefhALRAGFALDEGIANPTDAFTVF--------YSERSPWWVRVTSTGRPGHASRFME 177
Cdd:PRK08262 185 GHDEEVGGLgarAIAELLKER----GVRLAFVLDEGGAITEGVLPGVkkpvaligVAEKGYATLELTARATGGHSSMPPR 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 178 DTAAEKLHKVVNSI-------------------LAFREKEWQRLQ-SNPHLKEGSV---------------TSVNLTKLE 222
Cdd:PRK08262 261 QTAIGRLARALTRLednplpmrlrgpvaemfdtLAPEMSFAQRVVlANLWLFEPLLlrvlakspetaamlrTTTAPTMLK 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 223 GGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSwcQAAGEGVTLEFAQKWMHPQ-VTPTDdsNPWWAAFSRVCKDM-- 299
Cdd:PRK08262 341 GSPKDNVLPQRATATVNFRILPGDSVESVLAHVRR--AVADDRVEIEVLGGNSEPSpVSSTD--SAAYKLLAATIREVfp 416
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312032409 300 NLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTP---VLLHDHDERLHEAVFLRGVDIYTRLLPALAS 365
Cdd:PRK08262 417 DVVVAPYLVVGATDSRHYSGISDNVYRFSPLRLSPedlARFHGTNERISVANYARMIRFYYRLIENAAG 485
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
21-329 |
3.49e-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: 132.52 E-value: 3.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 21 RIRTVQPKPDYGTNPTLssiLLNSHTDVVPV-FKEHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHR 99
Cdd:TIGR01910 51 LGKVVVKEPGNGNEKSL---IFNGHYDVVPAgDLELWKTDPFKP-VEKDGKLYGRGATDMKGGLVALLYALKAIREAGIK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 100 FPRTIHMTFVPDEEVGGhQGMELFVQRpefhalraGFALDEG---IANPTDAFTVFYSERSPWWVRVTSTGRPGHASR-- 174
Cdd:TIGR01910 127 PNGNIILQSVVDEESGE-AGTLYLLQR--------GYFKDADgvlIPEPSGGDNIVIGHKGSIWFKLRVKGKQAHASFpq 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 175 FMEDtAAEKLHKVVNSILAFrEKEWQrlQSNPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQ 254
Cdd:TIGR01910 198 FGVN-AIMKLAKLITELNEL-EEHIY--ARNSYGFIPGPITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQI 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312032409 255 LQSWCQAAG--EGVTLEFAQKWMHPQVTPTDDSNPWWAAFSRVCKDMnLTLEPEIM--PAATDNRYIRAVGVPALGFSP 329
Cdd:TIGR01910 274 IEDVVKALSksDGWLYENEPVVKWSGPNETPPDSRLVKALEAIIKKV-RGIEPEVLvsTGGTDARFLRKAGIPSIVYGP 351
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
39-360 |
2.17e-34 |
|
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: 129.81 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 39 SILLNSHTDVVPVFKEH-WSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGH 117
Cdd:cd08011 62 RLLFNGHYDVVPAGDGEgWTVDPYSG-KIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 118 QGMELFVQRPEFHalrAGFALdegIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAeklhkvVNSILAFREK 197
Cdd:cd08011 141 AGTKYLLEKVRIK---PNDVL---IGEPSGSDNIRIGEKGLVWVIIEITGKPAHGSLPHRGESA------VKAAMKLIER 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 198 ewqrlqsnphLKEgSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDfkaFEEQLQSWCQ--AAGEGVTLEFAQKwm 275
Cdd:cd08011 209 ----------LYE-LEKTVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGIS---TDEVLSRIIDhlDSIEEVSFEIKSF-- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 276 hPQVTPTDDSNPWWAAFSRVCKDM-NLTLEPEIMPAATDNRYIRAVGVPALGFSPMNrtPVLLHDHDERLHEAVFLRGVD 354
Cdd:cd08011 273 -YSPTVSNPDSEIVKKTEEAITEVlGIRPKEVISVGASDARFYRNAGIPAIVYGPGR--LGQMHAPNEYVEIDELIKVIK 349
|
....*.
gi 312032409 355 IYTRLL 360
Cdd:cd08011 350 VHALVA 355
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
32-360 |
5.58e-32 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 124.58 E-value: 5.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 32 GTNPTLSSILLNSHTDVVPVFKEHWSHDPFE-AFKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVP 110
Cdd:PRK07906 60 GADPSRPALLVHGHLDVVPAEAADWSVHPFSgEIRD--GYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 111 DEEVGGHQGMELFVQ-RPEfhalragfaLDEGIanpTDA--------FTV-----FY----SERSPWWVRVTSTGRPGHA 172
Cdd:PRK07906 138 DEEAGGTYGAHWLVDnHPE---------LFEGV---TEAisevggfsLTVpgrdrLYlietAEKGLAWMRLTARGRAGHG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 173 SRFMEDTA----AE------------KLHKVVNSILA--FREKEWQRLQSNPHL---KEGSV---------TSVNLTKLE 222
Cdd:PRK07906 206 SMVNDDNAvtrlAEavarigrhrwplVLTPTVRAFLDgvAELTGLEFDPDDPDAllaKLGPAarmvgatlrNTANPTMLK 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 223 GGVAYNVIPATMSASFDFRVAPDVDfKAFEEQLQswcQAAGEGVTLEfaqkWMHPQV---TPTDdsNPWWAAfsrvckdM 299
Cdd:PRK07906 286 AGYKVNVIPGTAEAVVDGRFLPGRE-EEFLATVD---ELLGPDVERE----WVHRDPaleTPFD--GPLVDA-------M 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312032409 300 NLTLE---------PEIMPAATDNRYIRAVGVPALGFSPMnRTPV------LLHDHDERLHEAVFLRGVDIYTRLL 360
Cdd:PRK07906 349 NAALLaedpgarvvPYMLSGGTDAKAFSRLGIRCYGFAPL-RLPPdldfaaLFHGVDERVPVDALRFGVRVLDRFL 423
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
39-365 |
2.05e-30 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 119.71 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 39 SILLNSHTDVVPVfKEHW-SHDPFEAFKDsEGYIYARGAQDMK--CVSIqyLEAVRRLKVEGhrfPRTIHMTFVPDEEVG 115
Cdd:PRK08651 76 HLHFNGHYDVVPP-GEGWsVNVPFEPKVK-DGKVYGRGASDMKggIAAL--LAAFERLDPAG---DGNIELAIVPDEETG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 116 GHQGMELfvqrpefhALRAGFALDEGI-ANPTDAFTVFYSERSPWWVRVTSTGRPGHASR-FMEDTAAEKLHKVVNSILA 193
Cdd:PRK08651 149 GTGTGYL--------VEEGKVTPDYVIvGEPSGLDNICIGHRGLVWGVVKVYGKQAHASTpWLGINAFEAAAKIAERLKS 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 194 FREKEWQRLQSNPHlkEGSVTSVNL--TKLEGGVAYNVIPATMSASFDFRVAPDVD----FKAFEEQLQSWCQAAGEGVT 267
Cdd:PRK08651 221 SLSTIKSKYEYDDE--RGAKPTVTLggPTVEGGTKTNIVPGYCAFSIDRRLIPEETaeevRDELEALLDEVAPELGIEVE 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 268 LE---FAQKWMhpqvtpTDDSNPWWAAFSR-VCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNrtPVLLHDHDER 343
Cdd:PRK08651 299 FEitpFSEAFV------TDPDSELVKALREaIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGE--LELAHAPDEY 370
|
330 340
....*....|....*....|..
gi 312032409 344 LHEAVFLRGVDIYTRLLPALAS 365
Cdd:PRK08651 371 VEVKDVEKAAKVYEEVLKRLAK 392
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
32-360 |
5.67e-30 |
|
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: 119.67 E-value: 5.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 32 GTNPTLSSILLNSHTDVVPVFKEH---WSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTF 108
Cdd:cd05674 64 GSDPSLKPLLLMAHQDVVPVNPETedqWTHPPFSGHYD-GGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTIILAF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 109 VPDEEVGGHQGMELFVQRPEFhalRAG-----FALDEGIAN-PTDAFTVFY-----SERSPWWVRVTSTGRPGHAS---- 173
Cdd:cd05674 143 GHDEEVGGERGAGAIAELLLE---RYGvdglaAILDEGGAVlEGVFLGVPFalpgvAEKGYMDVEITVHTPGGHSSvppk 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 174 ---------------------RFMEDT--------AAEKLHKVVNSILafrekeWQRLQSNPHLKEGSV----------- 213
Cdd:cd05674 220 htgigilseavaaleanpfppKLTPGNpyygmlqcLAEHSPLPPRSLK------SNLWLASPLLKALLAsellstspltr 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 214 ----TSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSwcQAAGEGVTLEFAQKWMHPQVT--------- 280
Cdd:cd05674 294 allrTTQAVDIINGGVKINALPETATATVNHRIAPGSSVEEVLEHVKN--LIADIAVKYGLGLSAFGGDVIystngtkll 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 281 ----------PTDDSNPWWAAFSRVCKDM------NLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLL---HDHD 341
Cdd:cd05674 372 tsllspepspVSSTSSPVWQLLAGTIRQVfeqfgeDLVVAPGIMTGNTDTRHYWNLTKNIYRFTPIRLNPEDLgriHGVN 451
|
410
....*....|....*....
gi 312032409 342 ERLHEAVFLRGVDIYTRLL 360
Cdd:cd05674 452 ERISIDDYLETVAFYYQLI 470
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
40-360 |
1.29e-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: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 40 ILLNSHTDVVPVFKEHWSHDPFEAfKDSEGYIYARGAQDMK----CVsiqyLEAVRRLKVEGHRFPrtIHMTFVPDEEVg 115
Cdd:cd03894 60 LLLSGHTDVVPVDGQKWSSDPFTL-TERDGRLYGRGTCDMKgflaAV----LAAVPRLLAAKLRKP--LHLAFSYDEEV- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 116 GHQGMELFVQRPEFHALRAGFALdegIANPTD-AFTVFYSERSPWWVRVtsTGRPGHASrfmeDT-----AAEKLHKVVN 189
Cdd:cd03894 132 GCLGVRHLIAALAARGGRPDAAI---VGEPTSlQPVVAHKGIASYRIRV--RGRAAHSS----LPplgvnAIEAAARLIG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 190 SILAFREkEWQRLQSNPHLKEGSVTsVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGE----G 265
Cdd:cd03894 203 KLRELAD-RLAPGLRDPPFDPPYPT-LNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEfpeaG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 266 VTLEfaqkwmHPQVTP---TDDSNPWWAAFSRVCKDMNltlePEIMPAATDNRYIRAVGVPALGFSP--MNRTpvllHDH 340
Cdd:cd03894 281 IEVE------PLFEVPgleTDEDAPLVRLAAALAGDNK----VRTVAYGTEAGLFQRAGIPTVVCGPgsIAQA----HTP 346
|
330 340
....*....|....*....|
gi 312032409 341 DERLHEAVFLRGVDIYTRLL 360
Cdd:cd03894 347 DEFVELEQLDRCEEFLRRLI 366
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
40-364 |
5.56e-27 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 111.25 E-value: 5.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 40 ILLNSHTDVVPVFKEHWSHDPFEaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQG 119
Cdd:PRK09133 104 ILLLAHMDVVEAKREDWTRDPFK-LVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEGTPMNG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 120 ME-LFVQRPEfhALRAGFALDEGIANPTD------AFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSIL 192
Cdd:PRK09133 183 VAwLAENHRD--LIDAEFALNEGGGGTLDedgkpvLLTVQAGEKTYADFRLEVTNPGGHSSRPTKDNAIYRLAAALSRLA 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 193 AFR-------------------------------------EKEWQRLQSNPHLKEGSVTSVNLTKLEGGVAYNVIPATMS 235
Cdd:PRK09133 261 AYRfpvmlndvtrayfkqsaaietgplaaamrafaanpadEAAIALLSADPSYNAMLRTTCVATMLEGGHAENALPQRAT 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 236 ASFDFRVAPDVDFKAFEEQLQswcQAAGE-GVTLEFAQKwmhPQVTPTDDSNP-WWAAFSRVCKDM--NLTLEPEIMPAA 311
Cdd:PRK09133 341 ANVNCRIFPGDTIEAVRATLK---QVVADpAIKITRIGD---PSPSPASPLRPdIMKAVEKLTAAMwpGVPVIPSMSTGA 414
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 312032409 312 TDNRYIRAVGVPALGFSPM--NRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALA 364
Cdd:PRK09133 415 TDGRYLRAAGIPTYGVSGLfgDPDDTFAHGLNERIPVASFYEGRDFLYELVKDLA 469
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
31-138 |
1.04e-26 |
|
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: 105.21 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 31 YGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVP 110
Cdd:cd18669 6 YGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTP 85
|
90 100
....*....|....*....|....*...
gi 312032409 111 DEEVGGHQGMELFVQRPEFHALRAGFAL 138
Cdd:cd18669 86 DEEVGSGAGKGLLSKDALEEDLKVDYLF 113
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
31-356 |
4.98e-26 |
|
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 103.27 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 31 YGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVP 110
Cdd:cd03873 6 LGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 111 DEEVGGHQGMELFVQRpefhALRAGFALDEgianptdaftVFYSERSPWWvrvtsTGRPGHASRfmedtaaeklhkvvns 190
Cdd:cd03873 86 DEEVGSGGGKGLLSKF----LLAEDLKVDA----------AFVIDATAGP-----ILQKGVVIR---------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 191 ilafrekewqrlqsnphlkegsvtsvnltkleggvaynvipatmsasfdfrvapdvdfkafeeqlqswcqaagegvtlef 270
Cdd:cd03873 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 271 aqkwmhpqvtptddsNPWWAAFSRVCKDMNLTLEPEIM-PAATDNRYIRAVGVPALGFSPMnrTPVLLHDHDERLHEAVF 349
Cdd:cd03873 131 ---------------NPLVDALRKAAREVGGKPQRASViGGGTDGRLFAELGIPGVTLGPP--GDKGAHSPNEFLNLDDL 193
|
....*..
gi 312032409 350 LRGVDIY 356
Cdd:cd03873 194 EKATKVY 200
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
40-330 |
4.28e-23 |
|
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: 98.82 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 40 ILLNSHTDVVpvfkehWSHD--PFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGH 117
Cdd:cd03885 63 VLLIGHMDTV------FPEGtlAFRPFTVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 118 QGMELFvqrpEFHALRAGFALDEGIANPTDAFTVFYSERSPWWVRVtsTGRPGHASRFMEDTAaeklhkvvNSILAFREK 197
Cdd:cd03885 137 GSRELI----EEEAKGADYVLVFEPARADGNLVTARKGIGRFRLTV--KGRAAHAGNAPEKGR--------SAIYELAHQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 198 eWQRLQSNPHLKEGsvTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAA-GEGVTLEFAQKWMH 276
Cdd:cd03885 203 -VLALHALTDPEKG--TTVNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTlVPGTSVELTGGLNR 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 312032409 277 PQVTPTDDSNPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVGVPAL-GFSPM 330
Cdd:cd03885 280 PPMEETPASRRLLARAQEIAAELGLTLDWEATGGGSDANFTAALGVPTLdGLGPV 334
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
32-345 |
5.66e-22 |
|
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: 96.22 E-value: 5.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 32 GTNPTLSSILLNSHTDVVPVFK-EHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVP 110
Cdd:cd03895 69 PRGETGRSLILNGHIDVVPEGPvELWTRPPFEA-TIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 111 DEEVGGHQGMELFVQrpefhALRAGFALdegIANPTDAfTVFYSERSPWWVRVTSTGRPGHASRFMEDTAA-EKLHKVVN 189
Cdd:cd03895 148 EEECTGNGALAALMR-----GYRADAAL---IPEPTEL-KLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAiEKAMHLIQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 190 SILAFrEKEW-QRLQSNPHL--KEGSVTsVNLTKLEGGVAYNVIPAtmSASFDFRVA--PDVDFKAFEEQLQSWCQAAge 264
Cdd:cd03895 219 ALQEL-EREWnARKKSHPHFsdHPHPIN-FNIGKIEGGDWPSSVPA--WCVLDCRIGiyPGESPEEARREIEECVADA-- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 265 gvtlEFAQKWM--HP-QVT---------PTDDSNPWWAAFSRVCKDM-NLTLEPEIMPAATDNR-YIRAVGVPALGFSPM 330
Cdd:cd03895 293 ----AATDPWLsnHPpEVEwngfqaegyVLEPGSDAEQVLAAAHQAVfGTPPVQSAMTATTDGRfFVLYGDIPALCYGPG 368
|
330
....*....|....*
gi 312032409 331 NRTPvllHDHDERLH 345
Cdd:cd03895 369 SRDA---HGFDESVD 380
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
11-329 |
4.34e-21 |
|
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130947 [Multi-domain] Cd Length: 364 Bit Score: 93.35 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 11 PSVTLFRQYLR---IRT-VQPKPDYGTNPTL---------SSILLNSHTDVVPVFKEHWSHDPFEaFKDSEGYIYARGAQ 77
Cdd:TIGR01892 19 DLIDWAQAYLEalgFSVeVQPFPDGAEKSNLvavigpsgaGGLALSGHTDVVPYDDAAWTRDPFR-LTEKDGRLYGRGTC 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 78 DMKCVSIQYLEAVRRLKVEGHRFPrtIHMTFVPDEEVgGHQGMELFVQRPefhALRAGFALdegIANPTDAFTVfYSERS 157
Cdd:TIGR01892 98 DMKGFLACALAAAPDLAAEQLKKP--LHLALTADEEV-GCTGAPKMIEAG---AGRPRHAI---IGEPTRLIPV-RAHKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 158 PWWVRVTSTGRPGHASRFMEDTAA-EKLHKVVNSILAFREkewqRLQSNPHLK--EGSVTSVNLTKLEGGVAYNVIPATM 234
Cdd:TIGR01892 168 YASAEVTVRGRSGHSSYPDSGVNAiFRAGRFLQRLVHLAD----TLLREDLDEgfTPPYTTLNIGVIQGGKAVNIIPGAC 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 235 SASFDFRVAPDVDFKAFEEQLQSWCQAAGEGvTLEFAQKW----MHPQVTPTDDsnpwwAAFSRVCKDMnLTLEPEIMPA 310
Cdd:TIGR01892 244 EFVFEWRPIPGMDPEELLQLLETIAQALVRD-EPGFEVQIevvsTDPGVNTEPD-----AELVAFLEEL-SGNAPEVVSY 316
|
330
....*....|....*....
gi 312032409 311 ATDNRYIRAVGVPALGFSP 329
Cdd:TIGR01892 317 GTEAPQFQELGAEAVVCGP 335
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
31-345 |
2.53e-19 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 88.91 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 31 YGTNPTLSSILLNSHTDVVPVFK-EHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFV 109
Cdd:PRK06837 91 RPAGKTGRSLILQGHIDVVPEGPlDLWSRPPFDP-VIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 110 PDEEVGGHqGMELFVQRpefhALRAGFALdegIANPTDAfTVFYSERSPWWVRVTSTGRPGHAsRFMEdTAAEKLHKVVN 189
Cdd:PRK06837 170 IEEESTGN-GALSTLQR----GYRADACL---IPEPTGE-KLVRAQVGVIWFRLRVRGAPVHV-REAG-TGANAIDAAYH 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 190 SILAFR--EKEW-QRLQSNPHLK-EGSVTSVNLTKLEGGVAYNVIPAtmSASFDFRVA--PDVDFKAFEEQLQSWCQAAg 263
Cdd:PRK06837 239 LIQALRelEAEWnARKASDPHFEdVPHPINFNVGIIKGGDWASSVPA--WCDLDCRIAiyPGVTAADAQAEIEACLAAA- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 264 egvtlEFAQKWMH---PQVTPT---------DDSNPWWAAFSRVCKDMNLT-LEPEIMPAATDNR-YIRAVGVPALGFSP 329
Cdd:PRK06837 316 -----ARDDRFLSnnpPEVVWSgflaegyvlEPGSEAEAALARAHAAVFGGpLRSFVTTAYTDTRfYGLYYGIPALCYGP 390
|
330
....*....|....*.
gi 312032409 330 MNRTPvllHDHDERLH 345
Cdd:PRK06837 391 SGEGI---HGFDERVD 403
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
9-360 |
7.94e-18 |
|
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: 83.65 E-value: 7.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 9 EHPSVTLFRQ--YLRIRTVQPKPdygtnptlSSILLNSHTDVVPVfkehwsHDPFEAFKDSEGYIYARGAQDMKCVSIQY 86
Cdd:cd05647 31 TLPHLEVIRDgnTVVARTERGLA--------SRVILAGHLDTVPV------AGNLPSRVEEDGVLYGCGATDMKAGDAVQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 87 LEAVRRLKVEGHRFPRTihMTFVPDEEVGGHQ-GME-LFVQRPEFhaLRAGFALdegIANPTDAfTVFYSERSPWWVRVT 164
Cdd:cd05647 97 LKLAATLAAATLKHDLT--LIFYDCEEVAAELnGLGrLAEEHPEW--LAADFAV---LGEPTDG-TIEGGCQGTLRFKVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 165 STGRPGHASR-FMEDTAAEKLHKVVNSILAFREKEWQrlQSNPHLKEGsvtsVNLTKLEGGVAYNVIPATMSASFDFRVA 243
Cdd:cd05647 169 THGVRAHSARsWLGENAIHKLAPILARLAAYEPRTVN--IDGLTYREG----LNAVFISGGVAGNVIPDEARVNLNYRFA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 244 PDvdfKAFEEQLQSwCQAAGEGVTLEFAQKWMHPQVTPTDDsNPWWAAFSRVCKDmnltlEPEIMPAATDNRYIRAVGVP 323
Cdd:cd05647 243 PD---KSLAEAIAH-VREVFEGLGYEIEVTDLSPGALPGLD-HPVARDLIEAVGG-----KVRAKYGWTDVARFSALGIP 312
|
330 340 350
....*....|....*....|....*....|....*..
gi 312032409 324 ALGFSPMNrtPVLLHDHDERLHEAVFLRGVDIYTRLL 360
Cdd:cd05647 313 AVNFGPGD--PLLAHKRDEQVPVEQITACAAILRRWL 347
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
31-360 |
1.07e-17 |
|
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: 83.32 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 31 YGTNPTLssILLNSHTDVVPV-FKEHWSHDPFEAfKDSEGYIYARGAQDMKCvSIQ-YLEAVRRLKVEGHRFPRTIHMTF 108
Cdd:cd03891 50 RGTGGPH--LCFAGHTDVVPPgDLEGWSSDPFSP-TIKDGMLYGRGAADMKG-GIAaFVAAAERFVAKHPNHKGSISFLI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 109 VPDEEVGGHQGMELFVQRPEFHALRAGFALdegIANPTdaftvfySE-----------RSPWWVRVTSTGRPGHASrfME 177
Cdd:cd03891 126 TSDEEGPAIDGTKKVLEWLKARGEKIDYCI---VGEPT-------SEkklgdtikigrRGSLNGKLTIKGKQGHVA--YP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 178 DTAAEKLHKVVNSILAFrekewqrlqSNPHLKEGSV----TSVNLTKLEGGV-AYNVIPATMSASFDFRVAPDVDfkafE 252
Cdd:cd03891 194 HLADNPIHLLAPILAEL---------TATVLDEGNEffppSSLQITNIDVGNgATNVIPGELKAKFNIRFNDEHT----G 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 253 EQLQSWCQAAGEGVTLEFAQKWMH---PQVTPTDD-SNPWWAAFSRVCKdmnltLEPEImpaAT-----DNRYIRAVGVP 323
Cdd:cd03891 261 ESLKARIEAILDKHGLDYDLEWKLsgePFLTKPGKlVDAVSAAIKEVTG-----ITPEL---STsggtsDARFIASYGCP 332
|
330 340 350
....*....|....*....|....*....|....*..
gi 312032409 324 ALGFSPMNRTpvlLHDHDERLHEAVFLRGVDIYTRLL 360
Cdd:cd03891 333 VVEFGLVNAT---IHKVNERVSVADLEKLTDIYERIL 366
|
|
| PRK06915 |
PRK06915 |
peptidase; |
39-329 |
6.89e-17 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 81.66 E-value: 6.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 39 SILLNSHTDVVPVFK-EHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGH 117
Cdd:PRK06915 95 SMILNGHIDVVPEGDvNQWDHHPYSG-EVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEESGGA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 118 QGMElfvqrpefhALRAGFALDEG-IANPTDaFTVFYSERSPWWVRVTSTGRPGH-ASRFMEDTAAEKLHKVVNSILAFR 195
Cdd:PRK06915 174 GTLA---------AILRGYKADGAiIPEPTN-MKFFPKQQGSMWFRLHVKGKAAHgGTRYEGVSAIEKSMFVIDHLRKLE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 196 EKEWQRLqSNPHLKEGSV-TSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGE--------GV 266
Cdd:PRK06915 244 EKRNDRI-TDPLYKGIPIpIPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAELNDvdewfvehPV 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312032409 267 TLE-FAQKWM-------HPQVTPTDDsnpwwaAFSRVCKDMnltlePEI--MPAATDNRYI-RAVGVPALGFSP 329
Cdd:PRK06915 323 EVEwFGARWVpgeleenHPLMTTLEH------NFVEIEGNK-----PIIeaSPWGTDGGLLtQIAGVPTIVFGP 385
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
40-285 |
1.61e-16 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 80.23 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 40 ILLNSHTDVVPVFKEHWSHDPFEAFKDsEGYIYARGAQDMK----CVsiqyLEAVRRLKVEGHRFPrtIHMTFVPDEEVG 115
Cdd:PRK07522 67 IVLSGHTDVVPVDGQAWTSDPFRLTER-DGRLYGRGTCDMKgfiaAA----LAAVPELAAAPLRRP--LHLAFSYDEEVG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 116 --GHQGM-ELFVQRPEfhalRAGFALdegIANPTD-----------AFtvfyserspwwvRVTSTGRPGHASRfmedtaa 181
Cdd:PRK07522 140 clGVPSMiARLPERGV----KPAGCI---VGEPTSmrpvvghkgkaAY------------RCTVRGRAAHSSL------- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 182 ekLHKVVNSI------LAFREKEWQRLQSNPHLKEG---SVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFE 252
Cdd:PRK07522 194 --APQGVNAIeyaarlIAHLRDLADRLAAPGPFDALfdpPYSTLQTGTIQGGTALNIVPAECEFDFEFRNLPGDDPEAIL 271
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 312032409 253 EQLQSWC--------QAAGEGVTLEFAQKWMHPQVTPTDDS 285
Cdd:PRK07522 272 ARIRAYAeaellpemRAVHPEAAIEFEPLSAYPGLDTAEDA 312
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
8-360 |
1.78e-16 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 79.66 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 8 EEHPSVTLFRQYLRIRTVQPK----------PDYGTNPtlSSILLNSHTDVVPVFKEhWSHDPFEAfKDSEGYIYARGAQ 77
Cdd:cd05651 18 EEHKTADLIENYLEQKGIPFKrkgnnvwaenGHFDEGK--PTLLLNSHHDTVKPNAG-WTKDPFEP-VEKGGKLYGLGSN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 78 DMKCVSIQYLEAVRRLKVEGhrfPRTIHMTFV--PDEEVGGHQGME-LFVQRPEfhalragfaLDEGI-ANPTDaFTVFY 153
Cdd:cd05651 94 DAGASVVSLLATFLHLYSEG---PLNYNLIYAasAEEEISGKNGIEsLLPHLPP---------LDLAIvGEPTE-MQPAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 154 SERSPWWVRVTSTGRPGHASRFMEDTAaekLHKVVNSILAFREKEWQRLqsNPHLKEGSVTsvnLTKLEGGVAYNVIPAT 233
Cdd:cd05651 161 AEKGLLVLDCTARGKAGHAARNEGDNA---IYKALDDIQWLRDFRFDKV--SPLLGPVKMT---VTQINAGTQHNVVPDS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 234 MSASFDFRVAPdvdfkAFEEQLqswcqaagegvTLEFAQKWMHPQVTP---------TDDSNPwwaaFSRVCKDMNLTle 304
Cdd:cd05651 233 CTFVVDIRTTE-----AYTNEE-----------IFEIIRGNLKSEIKPrsfrlnssaIPPDHP----IVQAAIAAGRT-- 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 312032409 305 PEIMPAATDNRYIravGVPA--LGFSPMNRTpvllHDHDERLHEAVFLRGVDIYTRLL 360
Cdd:cd05651 291 PFGSPTLSDQALM---PFPSvkIGPGDSSRS----HTADEFIELSEIEEGIDIYIELL 341
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
42-224 |
5.52e-16 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 78.65 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 42 LNSHTDVVPVfKEHWSHDPFEAFKDsEGYIYARGAQDMK---CVSIQYLEAVRRLKVEghrFPRTIHMTFVPDEEVGGHQ 118
Cdd:PRK13013 89 FNSHHDVVEV-GHGWTRDPFGGEVK-DGRIYGRGACDMKgglAASIIAAEAFLAVYPD---FAGSIEISGTADEESGGFG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 119 GMELFVQRPEFHALRAGFALdegIANPTDAFTVFYSERSPWWVRVTSTGRPGHASR-FMEDTAAEKLHKVVNsilAFREK 197
Cdd:PRK13013 164 GVAYLAEQGRFSPDRVQHVI---IPEPLNKDRICLGHRGVWWAEVETRGRIAHGSMpFLGDSAIRHMGAVLA---EIEER 237
|
170 180 190
....*....|....*....|....*....|..
gi 312032409 198 EWQRLQSN----PHLKEGSVTS-VNLTKLEGG 224
Cdd:PRK13013 238 LFPLLATRrtamPVVPEGARQStLNINSIHGG 269
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
45-360 |
7.57e-15 |
|
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: 75.14 E-value: 7.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 45 HTDVVPV-FKEHWSHDPFEaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELF 123
Cdd:TIGR01246 63 HTDVVPAgPEEQWSSPPFE-PVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 124 VQrpefhALRAGfalDEGI-----ANPTDAF----TVFYSERSPWWVRVTSTGRPGHASrfMEDTAAEKLHKVVNSILAF 194
Cdd:TIGR01246 142 VE-----TLMAR---DELIdycivGEPSSVKklgdVIKNGRRGSITGNLTIKGIQGHVA--YPHLANNPIHKAAPALAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 195 rekewqrlqSNPHLKEGSV----TSVNLTKLEGGV-AYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLE 269
Cdd:TIGR01246 212 ---------TAIKWDEGNEffppTSLQITNIHAGTgANNVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLE 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 270 FAQKwMHPQVTPTDD-SNPWWAAFSRVCKdmnltLEPEIMPAA--TDNRYIRAVGVPALGFSPMNRTpvlLHDHDERLHE 346
Cdd:TIGR01246 283 WSLS-GEPFLTNDGKlIDKAREAIEETNG-----IKPELSTGGgtSDGRFIALMGAEVVEFGPVNAT---IHKVNECVSI 353
|
330
....*....|....
gi 312032409 347 AVFLRGVDIYTRLL 360
Cdd:TIGR01246 354 EDLEKLSDVYQDLL 367
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
28-283 |
8.64e-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: 74.80 E-value: 8.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 28 KPDYGTNPTLSSIllnSHTDVVPVFK-EHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHM 106
Cdd:cd05650 63 KIPGGNDKTLWII---SHLDTVPPGDlSLWETDPWEPVVK-DGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 107 TFVPDEEVGGHQGMELFVQRPEFhalragFALDEGIANP----TDAFTVFYSERSPWWVRVTSTGRPGHASrfMEDTAAE 182
Cdd:cd05650 139 LFVADEEDGSEYGIQYLLNKFDL------FKKDDLIIVPdfgtEDGEFIEIAEKSILWIKVNVKGKQCHAS--TPENGIN 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 183 KLHKVVNSILAFREKEWQRLQSNPHLKEGSVTSVNLTKLEGGVA-YNVIPATMSASFDFRVAP--DVD--FKAFEEQLQS 257
Cdd:cd05650 211 AFVAASNFALELDELLHEKFDEKDDLFNPPYSTFEPTKKEANVPnVNTIPGYDVFYFDCRVLPtyKLDevLKFVNKIISD 290
|
250 260
....*....|....*....|....*.
gi 312032409 258 WCQAAGEGVTLEFAQKWMHPQVTPTD 283
Cdd:cd05650 291 FENSYGAGITYEIVQKEQAPPATPED 316
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
45-361 |
1.10e-14 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 74.54 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 45 HTDVVPVFKEH-WSHDPFEAfKDSEGYIYARGAQDMK----CVSIqyleAVRRLKVEGHRFPRTIHMTFVPDEEVGGHqG 119
Cdd:PRK08588 67 HMDVVAAGDVDkWTYDPFEL-TEKDGKLYGRGATDMKsglaALVI----AMIELKEQGQLLNGTIRLLATAGEEVGEL-G 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 120 MELFVQrpefhalrAGFALD-EG--IANPTDAFtVFYSERSPWWVRVTSTGRPGHASrfMedtaAEKLHKVVNSILAFRE 196
Cdd:PRK08588 141 AKQLTE--------KGYADDlDAliIGEPSGHG-IVYAHKGSMDYKVTSTGKAAHSS--M----PELGVNAIDPLLEFYN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 197 KEWQRLQS-NPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWC----QAAGEGVTLEFA 271
Cdd:PRK08588 206 EQKEYFDSiKKHNPYLGGLTHVVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIInevnQNGAAQLSLDIY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 272 QKwmHPQVTPTDDSNPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVG--VPALGFSP-MNRTPvllHDHDERLHEAV 348
Cdd:PRK08588 286 SN--HRPVASDKDSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKpdFPVIIFGPgNNLTA---HQVDEYVEKDM 360
|
330
....*....|...
gi 312032409 349 FLRGVDIYTRLLP 361
Cdd:PRK08588 361 YLKFIDIYKEIII 373
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
31-344 |
3.23e-14 |
|
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.
Pssm-ID: 349869 [Multi-domain] Cd Length: 394 Bit Score: 73.36 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 31 YGTNPtlSSILLNSHTDVVPVfKEHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVP 110
Cdd:cd02697 69 YGDGG--RTVALNAHGDVVPP-GDGWTRDPYGAVVE-DGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 111 DEEVGGHQGMELFVQ----RPEFhALRAGFAldegianptdaFTVFYSERSPWWVRVTSTGRPGHASRfmEDTAAEKLH- 185
Cdd:cd02697 145 DEEFGGELGPGWLLRqgltKPDL-LIAAGFS-----------YEVVTAHNGCLQMEVTVHGKQAHAAI--PDTGVDALQg 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 186 --KVVNSILAFREKEWQRLQSNPHLkegSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAG 263
Cdd:cd02697 211 avAILNALYALNAQYRQVSSQVEGI---THPYLNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 264 E---GVTLEFAQKWMHPQVTPTDDSNPWWAAFSRVCKDMNLTLEPEI-MPAATDNRYIRAVGVPALGFSPMNRTPVLLHD 339
Cdd:cd02697 288 AsmpGISVDIRRLLLANSMRPLPGNAPLVEAIQTHGEAVFGEPVPAMgTPLYTDVRLYAEAGIPGVIYGAGPRTVLESHA 367
|
....*..
gi 312032409 340 H--DERL 344
Cdd:cd02697 368 KraDERL 374
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
44-324 |
3.41e-14 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 73.34 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 44 SHTDVVPVFKEH-WSHDPFEA-FKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGME 121
Cdd:PRK13983 83 SHMDVVPPGDLSlWETDPFKPvVKD--GKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYGIQ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 122 -LFVQRPEfhalraGFALDEGI-----ANPTDAFtVFYSERSPWWVRVTSTGRPGHASrfMEDTA----------AEKLH 185
Cdd:PRK13983 161 yLLKKHPE------LFKKDDLIlvpdaGNPDGSF-IEIAEKSILWLKFTVKGKQCHAS--TPENGinahraaadfALELD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 186 KVVNSilAFREKewqrlqsNPhLKEGSVTSVNLTKLEGGV-AYNVIPATMSASFDFRVAPDVD----FKAFEEQLQSWCQ 260
Cdd:PRK13983 232 EALHE--KFNAK-------DP-LFDPPYSTFEPTKKEANVdNINTIPGRDVFYFDCRVLPDYDldevLKDIKEIADEFEE 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312032409 261 AAGEGVTLEFAQKWMHPQVTPTDdsNPWWAAFSRVCKDMnLTLEPEI--MPAATDNRYIRAVGVPA 324
Cdd:PRK13983 302 EYGVKIEVEIVQREQAPPPTPPD--SEIVKKLKRAIKEV-RGIEPKVggIGGGTVAAFLRKKGYPA 364
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
38-247 |
5.16e-14 |
|
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: 72.31 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 38 SSILLNSHTDVVPvfkehwSHDPFEAfKDSEGYIYARGAQDMK-CVSIQYLeAVRRLKVEGHRFPRTIHMTFVPDEEVGG 116
Cdd:cd05652 59 PRVLLTSHIDTVP------PFIPYSI-SDGGDTIYGRGSVDAKgSVAAQII-AVEELLAEGEVPEGDLGLLFVVGEETGG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 117 HqGMELF--VQRPEFHALRAGfaldegiaNPTD--------AFTVFyserspwwvRVTSTGRPGHaSRFME--DTAAEKL 184
Cdd:cd05652 131 D-GMKAFndLGLNTWDAVIFG--------EPTElklasghkGMLGF---------KLTAKGKAGH-SGYPWlgISAIEIL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312032409 185 HKVVNSILAfrekewQRLQSNPHLKEgsvTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVD 247
Cdd:cd05652 192 VEALVKLID------ADLPSSELLGP---TTLNIGRISGGVAANVVPAAAEASVAIRLAAGPP 245
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
153-267 |
1.76e-13 |
|
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: 66.22 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 153 YSERSPWWVRVTSTGRPGHASRFmedtaaeklHKVVNSI-------LAFREKEWQRLQSNPHlkegsvTSVNLTKLEGGV 225
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAP---------GKGVNAIkllarllAELPAEYGDIGFDFPR------TTLNITGIEGGT 65
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 312032409 226 AYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVT 267
Cdd:pfam07687 66 ATNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
25-331 |
4.42e-12 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 66.32 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 25 VQPKPDygtnptlssILLNSHTDVVPVFKEhwshdPFEafkdSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTI 104
Cdd:PRK08652 52 VNSKAE---------LFVEVHYDTVPVRAE-----FFV----DGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 105 hmTFVPDEEVGGhQGMELFVQRpefhaLRAGFALdegIANPTDaFTVFYSERSPWWVRVTSTGRPGHASrFMEdtaaekl 184
Cdd:PRK08652 114 --AFVSDEEEGG-RGSALFAER-----YRPKMAI---VLEPTD-LKVAIAHYGNLEAYVEVKGKPSHGA-CPE------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 185 hKVVNSIL-AFreKEWQRLQS-NPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWcqAA 262
Cdd:PRK08652 174 -SGVNAIEkAF--EMLEKLKElLKALGKYFDPHIGIQEIIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPI--LD 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312032409 263 GEGVTLEFAQKWmhpQVTPTDDSNPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMN 331
Cdd:PRK08652 249 EYTVKYEYTEIW---DGFELDEDEEIVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTKTVVWGPGE 314
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
40-360 |
5.46e-12 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 66.38 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 40 ILLNSHTDVVPVfKEHWSHDPFeAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHrfprtihMTFVPDEEVGGHQG 119
Cdd:PRK08737 66 YLFNVHLDTVPD-SPHWSADPH-VMRRTDDRVIGLGVCDIKGAAAALLAAANAGDGDAA-------FLFSSDEEANDPRC 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 120 MELFVQR-PEFHALRagfaldegIANPTDAFTVFySERSPWWVRVTSTGRPGHASRfMEDTAAEKLHKVVNSILAFREKE 198
Cdd:PRK08737 137 VAAFLARgIPYEAVL--------VAEPTMSEAVL-AHRGISSVLMRFAGRAGHASG-KQDPSASALHQAMRWGGQALDHV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 199 WQRLQSNPHLKEGsvTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFaqkwMHPQ 278
Cdd:PRK08737 207 ESLAHARFGGLTG--LRFNIGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFAGFAEPAAATFEETF----RGPS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 279 VTPTDDSNpwwAAFSRV-CKDMNLTLEPEIMPAA---TDNRYIRAVGVPALGFSPMNRTPVllHDHDERLHEAVFLRGVD 354
Cdd:PRK08737 281 LPSGDIAR---AEERRLaARDVADALDLPIGNAVdfwTEASLFSAAGYTALVYGPGDIAQA--HTADEFVTLDQLQRYAE 355
|
....*.
gi 312032409 355 IYTRLL 360
Cdd:PRK08737 356 SVHRII 361
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
40-363 |
5.51e-11 |
|
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: 63.14 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 40 ILLNSHTDVVPVFKEhwshdpfeaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRfprTIHMTFVPDEEVGGHQG 119
Cdd:cd05653 57 VLLLGHIDTVPGEIP---------VRVEGGVLYGRGAVDAKGPLAAMILAASALNEELGA---RVVVAGLVDEEGSSKGA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 120 MELFVQRPEFHALRAGfaldegiaNPTDAFTVFYSERSPWWVRVTSTGRPGHASRfMEDTAAEKLHKVVNSILafrekew 199
Cdd:cd05653 125 RELVRRGPRPDYIIIG--------EPSGWDGITLGYRGSLLVKIRCEGRSGHSSS-PERNAAEDLIKKWLEVK------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 200 qRLQSNPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCqaagEGVTLEFAQKwMHPQV 279
Cdd:cd05653 189 -KWAEGYNVGGRDFDSVVPTLIKGGESSNGLPQRAEATIDLRLPPRLSPEEAIALATALL----PTCELEFIDD-TEPVK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 280 TPTDdsNPWWAAFSRVCKDMNLtlEPEIMPAA--TD-NRYIRAVGVPALGFSPMNrtPVLLHDHDERLHEAVFLRGVDIY 356
Cdd:cd05653 263 VSKN--NPLARAFRRAIRKQGG--KPRLKRKTgtSDmNVLAPLWTVPIVAYGPGD--STLDHTPNEHIELAEIERAAAVL 336
|
....*..
gi 312032409 357 TRLLPAL 363
Cdd:cd05653 337 KGALEEL 343
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
45-360 |
6.26e-11 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 63.18 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 45 HTDVVPV-FKEHWSHDPFEAfKDSEGYIYARGAQDMK----CvsiqYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQG 119
Cdd:PRK13009 66 HTDVVPPgDLEAWTSPPFEP-TIRDGMLYGRGAADMKgslaA----FVVAAERFVAAHPDHKGSIAFLITSDEEGPAING 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 120 ----MELFVQRPEfhalRAGFALdegIANPT------DA------------FTVfyserspwwvrvtsTGRPGHAS---R 174
Cdd:PRK13009 141 tvkvLEWLKARGE----KIDYCI---VGEPTsterlgDVikngrrgsltgkLTV--------------KGVQGHVAyphL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 175 fmedtAAEKLHKVVnSILAfrekewqRLqSNPHLKEGSV----TSVNLTKLEGGV-AYNVIPATMSASFDFRVAPDVDfk 249
Cdd:PRK13009 200 -----ADNPIHLAA-PALA-------EL-AATEWDEGNEffppTSLQITNIDAGTgATNVIPGELEAQFNFRFSTEHT-- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 250 afEEQLQSWCQAAGEGVTLEFAQKWM---HPQVTPTDDSNpwwAAFSRVCKDMNlTLEPEImpaAT-----DNRYIRAVG 321
Cdd:PRK13009 264 --AESLKARVEAILDKHGLDYTLEWTlsgEPFLTPPGKLV---DAVVAAIEAVT-GITPEL---STsggtsDARFIADYG 334
|
330 340 350
....*....|....*....|....*....|....*....
gi 312032409 322 VPALGFSPMNRTpvlLHDHDERLHEAVFLRGVDIYTRLL 360
Cdd:PRK13009 335 AQVVEFGPVNAT---IHKVNECVSVADLEKLTRIYERIL 370
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
40-325 |
1.87e-10 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 61.76 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 40 ILLNSHTDVVPvFKEH-WSHDPF---EAfkdsEGYIYARGAQDMKCVSIQYLEAVRRLKVegHRFPRTIHMTFVPDEEVG 115
Cdd:PRK05111 74 LLLAGHTDTVP-FDEGrWTRDPFtltEH----DGKLYGLGTADMKGFFAFILEALRDIDL--TKLKKPLYILATADEETS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 116 GHqGMELFVQRpefHALRAGFALdegIANPTDAFTVF-----YSERspwwVRVtsTGRPGHASrfmeD-----TAAEKLH 185
Cdd:PRK05111 147 MA-GARAFAEA---TAIRPDCAI---IGEPTSLKPVRahkghMSEA----IRI--TGQSGHSS----DpalgvNAIELMH 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 186 KVVNSILAFREkEWQRLQSNPHLKEGSVTsVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGE- 264
Cdd:PRK05111 210 DVIGELLQLRD-ELQERYHNPAFTVPYPT-LNLGHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSEr 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312032409 265 -GVTLEFAQkwMHPQV----TPTDdsnpwwAAFSRVCKdmNLT-LEPEIMPAATDNRYIRAVGVPAL 325
Cdd:PRK05111 288 wPGRITVAP--LHPPIpgyeCPAD------HQLVRVVE--KLLgHKAEVVNYCTEAPFIQQLGCPTL 344
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
30-115 |
2.55e-10 |
|
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: 61.63 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 30 DYGTNPTLSSILlnSHTDVVPVfKEHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFV 109
Cdd:TIGR01887 62 EYGQGEEVLGIL--GHLDVVPA-GDGWTSPPFEPTIK-DGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFG 137
|
....*.
gi 312032409 110 PDEEVG 115
Cdd:TIGR01887 138 TDEESG 143
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
32-115 |
2.00e-09 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 58.90 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 32 GTNPT-LSSILLNSHTDVVPVFK-EHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFV 109
Cdd:PRK08596 71 GTESDaYKSLIINGHMDVAEVSAdEAWETNPFEPTIK-DGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSV 149
|
....*.
gi 312032409 110 PDEEVG 115
Cdd:PRK08596 150 IGEEVG 155
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
32-241 |
2.73e-09 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 58.20 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 32 GTNPTLssILLNSHTDVVPVF-KEHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHR-FPRTIHMTFV 109
Cdd:cd05649 49 GGGKKK--ILFDGHIDTVGIGnIDNWKFDPYEG-YETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLRdFAYTILVAGT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 110 PDEEV-GGHQGMELFVQ---RPEFHAlragfaldegIANPTDAfTVFYSERSPWWVRVTSTGRPGHASrfmedtAAEK-- 183
Cdd:cd05649 126 VQEEDcDGVCWQYISKAdkiKPDFVV----------SGEPTDG-NIYRGQRGRMEIRVDTKGVSCHGS------APERgd 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 184 --LHKVVNSILAFREKEwQRLQSNPHLKEGSVTSVNLTKLEGGVayNVIPATMSASFDFR 241
Cdd:cd05649 189 naVYKMADIIQDIRQLN-PNFPEAPFLGRGTLTVTDIFSTSPSR--CAVPDSCRISIDRR 245
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
32-214 |
2.96e-09 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 58.03 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 32 GTNPTLssILLNSHTDVVPVF-KEHWSHDPFEAFKDsEGYIYARGAQDMK--CVSIQYleAVRRLKVEGHRFPRTIHMT- 107
Cdd:PRK13004 66 GHGKKL--IAFDAHIDTVGIGdIKNWDFDPFEGEED-DGRIYGRGTSDQKggMASMVY--AAKIIKDLGLDDEYTLYVTg 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 108 FVPDEEVGGHQGMELFVQ---RPEFHAlragfaldegIANPTDaFTVFYSERSPWWVRVTSTGRPGHAS---RfmEDTAA 181
Cdd:PRK13004 141 TVQEEDCDGLCWRYIIEEdkiKPDFVV----------ITEPTD-LNIYRGQRGRMEIRVETKGVSCHGSapeR--GDNAI 207
|
170 180 190
....*....|....*....|....*....|...
gi 312032409 182 EKLHKVVNSILAFREKewqrLQSNPHLKEGSVT 214
Cdd:PRK13004 208 YKMAPILNELEELNPN----LKEDPFLGKGTLT 236
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
45-236 |
4.64e-09 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 57.64 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 45 HTDVVPVfKEHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQGMELFV 124
Cdd:cd03888 79 HLDVVPA-GEGWTTDPFKPVIK-DGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGW-KCIEHYF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 125 QR---PEFhalraGFALDegiANptdaFTVFYSERSPWWVRVTSTGRPGhasrfmedtaaeklhkvvnsilafrekewqr 201
Cdd:cd03888 156 EHeeyPDF-----GFTPD---AE----FPVINGEKGIVTVDLTFKIDDD------------------------------- 192
|
170 180 190
....*....|....*....|....*....|....*
gi 312032409 202 lqsnphlkegsvTSVNLTKLEGGVAYNVIPATMSA 236
Cdd:cd03888 193 ------------KGYRLISIKGGEATNMVPDKAEA 215
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
30-113 |
8.58e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 56.63 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 30 DYGTNPTLSSILlnSHTDVVPVFKEH-WSHDPFEA-FKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMT 107
Cdd:PRK07205 70 EIGQGEELLAIL--CHLDVVPEGDLSdWQTPPFEAvEKD--GCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFI 145
|
....*.
gi 312032409 108 FVPDEE 113
Cdd:PRK07205 146 FGTDEE 151
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
30-141 |
1.87e-08 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 55.81 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 30 DYGTNPTLssiLLNSHTDVVPVFK-EHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTF 108
Cdd:cd05681 55 NSGDAKTL---LFYNHYDVQPAEPlELWTSDPFEL-TIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLV 130
|
90 100 110
....*....|....*....|....*....|....*
gi 312032409 109 VPDEEVGGhQGMELFVQRpefHA--LRAGFALDEG 141
Cdd:cd05681 131 EGEEEVGS-PNLEKFVAE---HAdlLKADGCIWEG 161
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
39-244 |
4.05e-08 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 54.41 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 39 SILLNSHTDVVPVfkEHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRfpRTIHMTFVPDEEVGGhQ 118
Cdd:cd08013 70 SLMLNGHIDTVTL--DGYDGDPLSG-EIADGRVYGRGTLDMKGGLAACMAALADAKEAGLR--GDVILAAVADEEDAS-L 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 119 GMElfvqrpefHALRAGFALDEGI-ANPTDaFTVFYSERSPWWVRVTSTGRPGHASRfmEDTAAEKLHKVVNSILAFREK 197
Cdd:cd08013 144 GTQ--------EVLAAGWRADAAIvTEPTN-LQIIHAHKGFVWFEVDIHGRAAHGSR--PDLGVDAILKAGYFLVALEEY 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 312032409 198 EwQRLQSNPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAP 244
Cdd:cd08013 213 Q-QELPERPVDPLLGRASVHASLIKGGEEPSSYPARCTLTIERRTIP 258
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
40-360 |
4.51e-08 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 54.29 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 40 ILLNSHTDVVPVFkehwSHDPFEAFKDsEGYIYAR-----GAQDmK--CVSIqyLEAVRRLKVEG--HRfprTIHMTFVP 110
Cdd:COG2195 63 IGLQAHMDTVPQF----PGDGIKPQID-GGLITADgtttlGADD-KagVAAI--LAALEYLKEPEipHG---PIEVLFTP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 111 DEEVGGHqGMELFvqrpEFHALRAGFAL-----DEG---IANPTDAFtvfyserspwwVRVTSTGRPGHASrfmedTAAE 182
Cdd:COG2195 132 DEEIGLR-GAKAL----DVSKLGADFAYtldggEEGeleYECAGAAD-----------AKITIKGKGGHSG-----DAKE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 183 KLhkvVNSI-LAFrekewqRLQSnpHLKEGSV---TSVNLTKLEGGVAYNVIPATMSASFdfrVAPDVDFKAFEEQLQSW 258
Cdd:COG2195 191 KM---INAIkLAA------RFLA--ALPLGRIpeeTEGNEGFIHGGSATNAIPREAEAVY---IIRDHDREKLEARKAEL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 259 CQAA-------GEGVtLEFAQKWMHPQVTPTDDSNPwWAAFSRVCKDMNltLEPEIMP--AATDNRYIRAVGVPALGFSP 329
Cdd:COG2195 257 EEAFeeenakyGVGV-VEVEIEDQYPNWKPEPDSPI-VDLAKEAYEELG--IEPKIKPirGGLDGGILSFKGLPTPNLGP 332
|
330 340 350
....*....|....*....|....*....|...
gi 312032409 330 --MNrtpvlLHDHDERLHEAVFLRGVDIYTRLL 360
Cdd:COG2195 333 ggHN-----FHSPDERVSIESMEKAWELLVEIL 360
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
5-115 |
7.82e-08 |
|
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.
Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 53.76 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 5 GPEEEHPSVTLFRqylrirtvqpkpdYGTNPTLSSILLNSHTDVVPVFKE-HWSHDPFEaFKDSEGYIYARGAQDMKCVS 83
Cdd:cd05676 66 GEELPLPPVLLGR-------------LGSDPSKKTVLIYGHLDVQPAKLEdGWDTDPFE-LTEKDGKLYGRGSTDDKGPV 131
|
90 100 110
....*....|....*....|....*....|..
gi 312032409 84 IQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVG 115
Cdd:cd05676 132 LGWLNAIEAYQKLGQELPVNLKFCFEGMEESG 163
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
35-363 |
4.71e-07 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 51.54 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 35 PTlssILLNSHTDVVPVFKEH-WSHDPFE-AFKDseGYIYARGAQDMKCVSIQYLEAVRR-LKVEGhRFPRTIHMTFVPD 111
Cdd:cd05680 64 PT---VLVYGHYDVQPPDPLElWTSPPFEpVVRD--GRLYARGASDDKGQVFIHIKAVEAwLAVEG-ALPVNVKFLIEGE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 112 EEVGGhQGMELFVqrpEFHA--LRAGFAL--DEGIANPtDAFTVFYSER--SPWWVRVTSTGRPGHASRF--MEDTAAEK 183
Cdd:cd05680 138 EEIGS-PSLPAFL---EENAerLAADVVLvsDTSMWSP-DTPTITYGLRglAYLEISVTGPNRDLHSGSYggAVPNPANA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 184 LHKVVNSI------------------LAFREKE-WQRLqsnPHLKEGSVTSVNLTKLEGGVAYN---------------- 228
Cdd:cd05680 213 LARLLASLhdedgrvaipgfyddvrpLTDAEREaWAAL---PFDEAAFKASLGVPALGGEAGYTtlerlwarptldvngi 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 229 -----------VIPATMSASFDFRVAPDVDFKAFEEQLQSWCQA-AGEGVTLEFaqKWMH---PQVTPTDDsnPWWAAFS 293
Cdd:cd05680 290 wggyqgegsktVIPSKAHAKISMRLVPGQDPDAIADLLEAHLRAhAPPGVTLSV--KPLHggrPYLVPTDH--PALQAAE 365
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312032409 294 RVC-----KDMNLTLEPEIMPAATDNRyiRAVGVPAL--GFS-PMNRtpvlLHDHDERLHEAVFLRGVDIYTRLLPAL 363
Cdd:cd05680 366 RALeeafgKPPVFVREGGSIPIVALFE--KVLGIPTVlmGFGlPDDA----IHAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
30-257 |
2.33e-06 |
|
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: 49.25 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 30 DYGTNPTLSSILLNSHTDVVPVFKEH-WSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMtF 108
Cdd:cd03893 56 EFPGAPGAPTVLLYGHYDVQPAGDEDgWDSDPFEL-TERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKF-I 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 109 VPDEEVGGHQGMELFV-QRPEFHALRAGFALDeGIANPTDAFTVFYSERSPWWVRVTSTGR--PGHASRF--MEDTAAEK 183
Cdd:cd03893 134 IEGEEESGSPSLDQLVeAHRDLLAADAIVISD-STWVGQEQPTLTYGLRGNANFDVEVKGLdhDLHSGLYggVVPDPMTA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 184 LHKVVNSILAFR----------------EKEWQRLQ------SNPHLKEGSVT-------SVNLTKLEGGV----AYNVI 230
Cdd:cd03893 213 LAQLLASLRDETgrilvpglydavrelpEEEFRLDAgvleevEIIGGTTGSVAerlwtrpALTVLGIDGGFpgegSKTVI 292
|
250 260
....*....|....*....|....*..
gi 312032409 231 PATMSASFDFRVAPDVDFKAFEEQLQS 257
Cdd:cd03893 293 PPRARAKISIRLVPGQDPEEASRLLEA 319
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
40-122 |
4.12e-06 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 48.62 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 40 ILLNSHTDVVPVFKEHWSHDPFEaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRfpRTIHMTFVPDEEVGGHQG 119
Cdd:PRK08554 66 LLFMAHFDVVPVNPEEWNTEPFK-LTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLN--GKVIFAFTGDEEIGGAMA 142
|
...
gi 312032409 120 MEL 122
Cdd:PRK08554 143 MHI 145
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
32-258 |
6.24e-06 |
|
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: 47.84 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 32 GTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGyIYARGAQDmkCVSIQYL--EAVRRLKVEGHRFPRTIHMTFV 109
Cdd:cd08012 73 GTVDGKTVSFVGSHMDVVTANPETWEFDPFSLSIDGDK-LYGRGTTD--CLGHVALvtELFRQLATEKPALKRTVVAVFI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 110 PDEEVGG--HQGMELFVQRPEFHALRAG--FALDEGIANPtdafTVFYSERSPWwvRVTSTGRPGHASRfmedtaaekLH 185
Cdd:cd08012 150 ANEENSEipGVGVDALVKSGLLDNLKSGplYWVDSADSQP----CIGTGGMVTW--KLTATGKLFHSGL---------PH 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 186 KVVNSILAFRE--KEWQR---LQSNPHLKEG-------SVTSVNLTKLEGGvAYNVIPATMSASFDFRVAPDVDFKAFEE 253
Cdd:cd08012 215 KAINALELVMEalAEIQKrfyIDFPPHPKEEvygfatpSTMKPTQWSYPGG-SINQIPGECTICGDCRLTPFYDVKEVRE 293
|
....*
gi 312032409 254 QLQSW 258
Cdd:cd08012 294 KLEEY 298
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
39-141 |
6.76e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 47.83 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 39 SILLNSHTDVVPVFK-EHWSHDPFEA-FKDseGYIYARGAQDMKCVSIQYLEAVRRLkVEGHRFPRTIHMTFVPDEEVGG 116
Cdd:PRK06446 64 TLLIYNHYDVQPVDPlSEWKRDPFSAtIEN--GRIYARGASDNKGTLMARLFAIKHL-IDKHKLNVNVKFLYEGEEEIGS 140
|
90 100
....*....|....*....|....*
gi 312032409 117 hQGMELFVQRPEfHALRAGFALDEG 141
Cdd:PRK06446 141 -PNLEDFIEKNK-NKLKADSVIMEG 163
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
32-120 |
1.35e-05 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 46.95 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 32 GTNPTLSSILLNSHTDVVPV-------------------FKEHWSHDPFEAFKD--SEGYIYARGAQDMKCVSIQYLEAV 90
Cdd:cd05654 66 GKKPSKRTIILISHFDTVGIedygelkdiafdpdeltkaFSEYVEELDEEVREDllSGEWLFGRGTMDMKSGLAVHLALL 145
|
90 100 110
....*....|....*....|....*....|
gi 312032409 91 RRLKVEGHrFPRTIHMTFVPDEEVgGHQGM 120
Cdd:cd05654 146 EQASEDED-FDGNLLLMAVPDEEV-NSRGM 173
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
166-359 |
1.56e-05 |
|
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1L2 family contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.
Pssm-ID: 349945 [Multi-domain] Cd Length: 366 Bit Score: 46.46 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 166 TGRPGHASrfMEDTAAEKLHKVVNSILAFRekewQRLQSNPHLKEGSVTSVnlTKLEGGVAYNVIPATMSASFDFRVAPD 245
Cdd:cd08660 178 KGKGGHAS--IPNNSIDPIAAAGQIISGLQ----SVVSRNISSLQNAVVSI--TRVQGGTAWNVIPDQAE*EGTVRAFTK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 246 VDFKAFEEQLQSWC--QAAGEGVTLEFaqKWMHPQVTPTDDSNPWWAAFSRVCKDM-NLTLEPEIMPAATDNRYIRAVgV 322
Cdd:cd08660 250 EARQAVPEH*RRVAegIAAGYGCQAEF--KWFPNGPSEVQNDGTLLNAFSKAAARLgYATVHAEQSPGSEDFALYQEK-I 326
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 312032409 323 PalGFSP---MNRTPVLLHDHDERLHEAVFLRGVDIYTRL 359
Cdd:cd08660 327 P--GFFVw*gTNGRTEEWHHPAFRLDEEALTVGAQIFAEL 364
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
87-349 |
1.67e-05 |
|
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273857 [Multi-domain] Cd Length: 363 Bit Score: 46.18 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 87 LEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQ----------------GMELFVQRPEFH-ALRAGFaldegIANPTDAF 149
Cdd:TIGR01891 99 LGTAKLLKKLADLLEGTVRLIFQPAEEGGGGAtkmiedgvlddvdailGLHPDPSIPAGTvGLRPGT-----IMAAADKF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 150 TVFYserspwwvrvtsTGRPGHASRfmedtaaekLHKVVNSILAFREKeWQRLQ-----SNPHLKEGSVTsvnLTKLEGG 224
Cdd:TIGR01891 174 EVTI------------HGKGAHAAR---------PHLGRDALDAAAQL-VVALQqivsrNVDPSRPAVVS---VGIIEAG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 225 VAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGE--GVTLEFaqKWMH--PQVTPTDDSNPWWAAFSR-VCKDM 299
Cdd:TIGR01891 229 GAPNVIPDKASMSGTVRSLDPEVRDQIIDRIERIVEGAAAmyGAKVEL--NYDRglPAVTNDPALTQILKEVARhVVGPE 306
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 312032409 300 NLTLEPEIMPAATDNRYIRAVgVP-ALGFSP-MNRTPVLLHDHderlHEAVF 349
Cdd:TIGR01891 307 NVAEDPEVTMGSEDFAYYSQK-VPgAFFFLGiGNEGTGLSHPL----HHPRF 353
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
45-115 |
1.78e-05 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 46.37 E-value: 1.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312032409 45 HTDVVPVfKEHWSHDPFEA-FKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVG 115
Cdd:PRK07318 87 HLDVVPA-GDGWDTDPYEPvIKD--GKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRFIVGTDEESG 155
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
161-359 |
2.41e-05 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 45.67 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 161 VRVTSTGRPGHASRfmedtaaekLHKVVNSILAFREKeWQRLQSNPHLKEGSVTS--VNLTKLEGGVAYNVIP--ATMSA 236
Cdd:cd03886 174 FEITVKGKGGHGAS---------PHLGVDPIVAAAQI-VLALQTVVSRELDPLEPavVTVGKFHAGTAFNVIPdtAVLEG 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 237 ---SFDFRVAPDVdFKAFEEQLQSWCQAAGEGVTLEfaqkwMHPQVTPTDDSNPWWAAFSRVCKDM---NLTLEPEIMPA 310
Cdd:cd03886 244 tirTFDPEVREAL-EARIKRLAEGIAAAYGATVELE-----YGYGYPAVINDPELTELVREAAKELlgeEAVVEPEPVMG 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 312032409 311 ATDNRYIrAVGVPA----LGFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRL 359
Cdd:cd03886 318 SEDFAYY-LEKVPGaffwLGAGEPDGENPGLHSPTFDFDEDALPIGAALLAEL 369
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
38-256 |
3.51e-05 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 45.39 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 38 SSILLNSHTDVVpvFKEHWSHDpfEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGH 117
Cdd:PRK06133 100 RRIMLIAHMDTV--YLPGMLAK--QPFRIDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGSP 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 118 QGMELFVQRPEFHalRAGFALDEGiaNPTDAFTVFYSERSPWWVRVTstGRPGHASrfmedtAAEKLHkvVNSILafrEK 197
Cdd:PRK06133 176 GSRELIAELAAQH--DVVFSCEPG--RAKDALTLATSGIATALLEVK--GKASHAG------AAPELG--RNALY---EL 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 312032409 198 EWQRLQSNPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQ 256
Cdd:PRK06133 239 AHQLLQLRDLGDPAKGTTLNWTVAKAGTNRNVIPASASAQADVRYLDPAEFDRLEADLQ 297
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
40-243 |
1.15e-04 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 43.62 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 40 ILLNSHTDVVPVFKEhwshdPFEafkdsEGY-IYARGAQDMKCVSIQYLEAVRRLKVEGHRfprtIHMTFVPDEEVGGHQ 118
Cdd:PRK00466 63 ILLASHVDTVPGYIE-----PKI-----EGEvIYGRGAVDAKGPLISMIIAAWLLNEKGIK----VMVSGLADEESTSIG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 119 GMELfvqrpefhaLRAGFALDEGI-ANPTDAFTVFYSERSPWWVRVTSTGRPGHASRfMEDTAAEKLHKVVNSILafrek 197
Cdd:PRK00466 129 AKEL---------VSKGFNFKHIIvGEPSNGTDIVVEYRGSIQLDIMCEGTPEHSSS-AKSNLIVDISKKIIEVY----- 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 312032409 198 ewqRLQSNPhlkegSVTSVNLTKLEGGVAYNVIPATMSASFDFRVA 243
Cdd:PRK00466 194 ---KQPENY-----DKPSIVPTIIRAGESYNVTPAKLYLHFDVRYA 231
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
22-172 |
1.30e-04 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 43.62 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 22 IRTVQPKPDYGTnptlSSILLNSHTDVV-PVfkehwshDPFE--AFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGH 98
Cdd:PRK07473 64 VRARFPHPRQGE----PGILIAGHMDTVhPV-------GTLEklPWRREGNKCYGPGILDMKGGNYLALEAIRQLARAGI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 99 RFPRTIHMTFVPDEEVGGHQGMELFvqrpEFHALRAGFAL-------DEGIANPTDAFTVFyserspwwvRVTSTGRPGH 171
Cdd:PRK07473 133 TTPLPITVLFTPDEEVGTPSTRDLI----EAEAARNKYVLvpepgrpDNGVVTGRYAIARF---------NLEATGRPSH 199
|
.
gi 312032409 172 A 172
Cdd:PRK07473 200 A 200
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
30-126 |
1.80e-04 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 43.20 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 30 DYGTNPTLSSILLNSHTDVVPVFKEH-WSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRR-LKVEGhRFPRTIHMT 107
Cdd:PRK08201 72 DWLHAPGKPTVLIYGHYDVQPVDPLNlWETPPFEP-TIRDGKLYARGASDDKGQVFMHLKAVEAlLKVEG-TLPVNVKFC 149
|
90
....*....|....*....
gi 312032409 108 FVPDEEVGGhQGMELFVQR 126
Cdd:PRK08201 150 IEGEEEIGS-PNLDSFVEE 167
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
45-151 |
6.22e-04 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 41.43 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 45 HTDVVPVFK-EHWSHDPFE-AFKDSEG---YIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQG 119
Cdd:PRK09104 90 HYDVQPVDPlDLWESPPFEpRIKETPDgrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEESGS-PS 168
|
90 100 110
....*....|....*....|....*....|....*..
gi 312032409 120 MELFVQRpefHA--LRAGFAL--DEGIANP-TDAFTV 151
Cdd:PRK09104 169 LVPFLEA---NAeeLKADVALvcDTGMWDReTPAITT 202
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
32-265 |
8.95e-04 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 40.93 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 32 GTNPtlsSILLNSHTDVVpvFKEHwshDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMT-FVP 110
Cdd:cd03896 52 GGGP---ALLFSAHLDTV--FPGD---TPATVRHE-GGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAaNVG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 111 DEEVGGHQGMELFVQRpefHALRAGFALdegIANPTDaFTVFYSERSPWWVRVTSTGRPGHasRFMEDTAAEKLHKVVNS 190
Cdd:cd03896 123 EEGLGDLRGARYLLSA---HGARLDYFV---VAEGTD-GVPHTGAVGSKRFRITTVGPGGH--SYGAFGSPSAIVAMAKL 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312032409 191 ILAFreKEWQrLQSNPHlkegsvTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEG 265
Cdd:cd03896 194 VEAL--YEWA-APYVPK------TTFAAIRGGGGTSVNRIANLCSMYLDIRSNPDAELADVQREVEAVVSKLAAK 259
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
35-131 |
8.98e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 41.04 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 35 PTlssILLNSHTDVVPVFKE-HWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLkveGHRFPRTIHMtFVPDEE 113
Cdd:PRK07907 84 PT---VLLYAHHDVQPPGDPdAWDSPPFEL-TERDGRLYGRGAADDKGGIAMHLAALRAL---GGDLPVGVTV-FVEGEE 155
|
90 100
....*....|....*....|
gi 312032409 114 VGGHQGMELFV--QRPEFHA 131
Cdd:PRK07907 156 EMGSPSLERLLaeHPDLLAA 175
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
158-280 |
1.80e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 40.14 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312032409 158 PWWVRVTSTGRPGHA-SRFMED------TAAEklhkvvnSILAFREKEWQrlqsnphLKEGSVTSV-NLTKLEGGVayNV 229
Cdd:PRK09290 215 QRRYRVTFTGEANHAgTTPMALrrdallAAAE-------IILAVERIAAA-------HGPDLVATVgRLEVKPNSV--NV 278
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 312032409 230 IPATMSASFDFRvAPDVDF-KAFEEQLQSWCQ--AAGEGVTLEFAQKWMHPQVT 280
Cdd:PRK09290 279 IPGEVTFTLDIR-HPDDAVlDALVAELRAAAEaiAARRGVEVEIELISRRPPVP 331
|
|
| |
