|
Name |
Accession |
Description |
Interval |
E-value |
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
99-489 |
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: 773.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 99 EHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFK 178
Cdd:cd05646 1 EDPAVTRFREYLRINTVHPNPDYDACVEFLKRQADELGLPVRVIEVVPGKPVVVLTWEGSNPELPSILLNSHTDVVPVFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 179 EHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHALR 258
Cdd:cd05646 81 EKWTHDPFSAHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGHDGMEKFVKTEEFKKLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 259 AGFALDEGIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFREKEWQRLQSNPHLKEGSV 338
Cdd:cd05646 161 VGFALDEGLASPTEEYRVFYGERSPWWVVITAPGTPGHGSKLLENTAGEKLRKVIESIMEFRESQKQRLKSNPNLTLGDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 339 TSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDSNPWWAAFS 418
Cdd:cd05646 241 TTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGRGVTYEFEQKSPEKDPTSLDDSNPWWAAFK 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 938318566 419 RVCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALA 489
Cdd:cd05646 321 KAVKEMGLKLKPEIFPAATDSRYIRALGIPALGFSPMNNTPILLHDHNEFLNEDVFLRGIEIYEKIIPALA 391
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
91-491 |
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: 753.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 91 MTSKGpEEEHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSH 170
Cdd:TIGR01880 1 MSSSK-WEEDIAVTRFREYLRINTVQPNPDYAACVDFLIKQADELGLARKTIEFVPGKPVVVLTWPGSNPELPSILLNSH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 171 TDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQ 250
Cdd:TIGR01880 80 TDVVPVFREHWTHPPFSAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEKFAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 251 RPEFHALRAGFALDEGIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFREKEWQRLQSN 330
Cdd:TIGR01880 160 TDEFKALNLGFALDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKLMENTAMEKLEKSVESIRRFRESQFQLLQSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 331 PHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDDS 410
Cdd:TIGR01880 240 PDLAIGDVTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAGEGVTYEFSQHSGKPLVTPHDDS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 411 NPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALAS 490
Cdd:TIGR01880 320 NPWWVAFKDAVKEMGCTFKPEILPGSTDSRYIRAAGVPALGFSPMNNTPVLLHDHNEFLNEAVFLRGIEIYQTLISALAS 399
|
.
gi 938318566 491 V 491
Cdd:TIGR01880 400 V 400
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
89-489 |
3.91e-78 |
|
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: 249.42 E-value: 3.91e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 89 SAMTSKGPEEEHPSVTLFRQYLRIRTVQPkpDYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTlSSILLN 168
Cdd:COG0624 1 AAVLAAIDAHLDEALELLRELVRIPSVSG--EEAAAAELLAELLEALGFEVERLEVPPGRPNLVARRPGDGGG-PTLLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 169 SHTDVVPV-FKEHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHqGMEL 247
Cdd:COG0624 78 GHLDVVPPgDLELWTSDPFEP-TIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSP-GARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 248 FVQRpEFHALRAGFALdegIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFME-DTAAEKLHKVVNSILAFREkewqR 326
Cdd:COG0624 156 LVEE-LAEGLKADAAI---VGEPTGVPTIVTGHKGSLRFELTVRGKAAHSSRPELgVNAIEALARALAALRDLEF----D 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 327 LQSNPHLKEgsvTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFaqKWMHPQVTP 406
Cdd:COG0624 228 GRADPLFGR---TTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEV--EVLGDGRPP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 407 --TDDSNPWWAAFSRVCKD-MNLTLEPEIMPAATDNRYI-RAVGVPALGFSPMNRTpvLLHDHDERLHEAVFLRGVDIYT 482
Cdd:COG0624 303 feTPPDSPLVAAARAAIREvTGKEPVLSGVGGGTDARFFaEALGIPTVVFGPGDGA--GAHAPDEYVELDDLEKGARVLA 380
|
....*..
gi 938318566 483 RLLPALA 489
Cdd:COG0624 381 RLLERLA 387
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
166-485 |
4.05e-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: 205.27 E-value: 4.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 166 LLNSHTDVVPVfkEHWSHDPFEAFKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRfPRTIHMTFVPDEEvGGHQGM 245
Cdd:pfam01546 1 LLRGHMDVVPD--EETWGWPFKSTED--GKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEE-GGMGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 246 ELFVQRPEFHALRAGFALDEGIANPTD-----AFTVFYSERSPWWVRVTSTGRPGHASRF-MEDTAAEKLHKVVNSILAF 319
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFGLHIGEPTLleggiAIGVVTGHRGSLRFRVTVKGKGGHASTPhLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 320 REKEwqrlqsNPHLKEGSVTSVNLTKLEGGVayNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFAQKW 399
Cdd:pfam01546 155 VSRN------VDPLDPAVVTVGNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 400 MHPQVTPTDDSNPWWAAFSRVCKDM---NLTLEPEIMPAATDNRYIRAvGVPA--LGFSPMNRTpvlLHDHDERLHEAVF 474
Cdd:pfam01546 227 VEGGAPPLVNDSPLVAALREAAKELfglKVELIVSGSMGGTDAAFFLL-GVPPtvVFFGPGSGL---AHSPNEYVDLDDL 302
|
330
....*....|.
gi 938318566 475 LRGVDIYTRLL 485
Cdd:pfam01546 303 EKGAKVLARLL 313
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
103-485 |
9.03e-55 |
|
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: 189.49 E-value: 9.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 103 VTLFRQYLRIRTVQPKPDYG-------AAVAFFEETArqLGLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVP 175
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTGsetraaeVLAARLAEAG--IQTEIFVVESHPGRANLVARIGGTDPSAGPLLLLGHIDVVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 176 VFKEHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQ-RPEF 254
Cdd:cd05675 79 ADASDWSVDPFSG-EIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDnHPEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 255 HAlRAGFALDEG------IANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAF--------- 319
Cdd:cd05675 158 FD-GATFALNEGgggslpVGKGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRPTDDNAITRLAEALRRLGAHnfpvrltde 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 320 -----------REKEWQRL---------------QSNPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDF 373
Cdd:cd05675 237 tayfaqmaelaGGEGGALMltavpvldpalaklgPSAPLLNAMLRNTASPTMLDAGYATNVLPGRATAEVDCRILPGQSE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 374 KAFEEQLQswcQAAGE-GVTLEFAqkWMHPQVTPTDDSnPWWAAFSRVCKDM--NLTLEPEIMPAATDNRYIRAVGVPAL 450
Cdd:cd05675 317 EEVLDTLD---KLLGDpDVSVEAV--HLEPATESPLDS-PLVDAMEAAVQAVdpGAPVVPYMSPGGTDAKYFRRLGIPGY 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 938318566 451 GFSPMNRTPVL-----LHDHDERLHEAVFLRGVDIYTRLL 485
Cdd:cd05675 391 GFAPLFLPPELdytglFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
105-485 |
3.07e-48 |
|
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: 170.17 E-value: 3.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 105 LFRQYLRIRTVQPkpDYGAAVAFFEET--ARQLGLGCQKVEVAPGYVVTVLTwpGTNPTLssiLLNSHTDVVPVFKEH-W 181
Cdd:cd08659 2 LLQDLVQIPSVNP--PEAEVAEYLAELlaKRGYGIESTIVEGRGNLVATVGG--GDGPVL---LLNGHIDTVPPGDGDkW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 182 SHDPFEAfKDSEGYIYARGAQDMK---CVSIQyleAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQGMELFVQRPefHALR 258
Cdd:cd08659 75 SFPPFSG-RIRDGRLYGRGACDMKgglAAMVA---ALIELKEAGALLGGRVALLATVDEEVGS-DGARALLEAG--YADR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 259 AGFALdegIANPTDaFTVFYSERSPWWVRVTSTGRPGHASrfMEDTAAEKLHKVVNSILAFREKEWqRLQSNPHLKEgsv 338
Cdd:cd08659 148 LDALI---VGEPTG-LDVVYAHKGSLWLRVTVHGKAAHSS--MPELGVNAIYALADFLAELRTLFE-ELPAHPLLGP--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 339 TSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFAQKWMHPQVTPTDdsNPWWAAFS 418
Cdd:cd08659 218 PTLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPPFFTDPD--HPLVQALQ 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 938318566 419 RVCKDMNLTLEPEIMPAATDNRYI-RAVGVPALGFSPMNrtPVLLHDHDERLHEAVFLRGVDIYTRLL 485
Cdd:cd08659 296 AAARALGGDPVVRPFTGTTDASYFaKDLGFPVVVYGPGD--LALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
81-490 |
3.58e-42 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 156.64 E-value: 3.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 81 LTFQLTTRSAMTSKGPEEEHPSVTL------FRQYLRIRTV--QPKPDYGAA-----VAFFEETARQLGLGCQKVEVAPg 147
Cdd:PRK08262 19 LAVRTFRFKSRQIDVPAVAPVAVDEdaaaerLSEAIRFRTIsnRDRAEDDAAafdalHAHLEESYPAVHAALEREVVGG- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 148 yvVTVL-TWPGTNPTLSSILLNSHTDVVPV---FKEHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGH 223
Cdd:PRK08262 98 --HSLLyTWKGSDPSLKPIVLMAHQDVVPVapgTEGDWTHPPFSGVIA-DGYVWGRGALDDKGSLVAILEAAEALLAQGF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 224 RFPRTIHMTFVPDEEVGGH---QGMELFVQRpefhALRAGFALDEGIANPTDAFTVF--------YSERSPWWVRVTSTG 292
Cdd:PRK08262 175 QPRRTIYLAFGHDEEVGGLgarAIAELLKER----GVRLAFVLDEGGAITEGVLPGVkkpvaligVAEKGYATLELTARA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 293 RPGHASRFMEDTAAEKLHKVVNSI-------------------LAFREKEWQRLQ-SNPHLKEGSV-------------- 338
Cdd:PRK08262 251 TGGHSSMPPRQTAIGRLARALTRLednplpmrlrgpvaemfdtLAPEMSFAQRVVlANLWLFEPLLlrvlakspetaaml 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 339 -TSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSwcQAAGEGVTLEFAQKWMHPQ-VTPTDdsNPWWAA 416
Cdd:PRK08262 331 rTTTAPTMLKGSPKDNVLPQRATATVNFRILPGDSVESVLAHVRR--AVADDRVEIEVLGGNSEPSpVSSTD--SAAYKL 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 938318566 417 FSRVCKDM--NLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTP---VLLHDHDERLHEAVFLRGVDIYTRLLPALAS 490
Cdd:PRK08262 407 LAATIREVfpDVVVAPYLVVGATDSRHYSGISDNVYRFSPLRLSPedlARFHGTNERISVANYARMIRFYYRLIENAAG 485
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
103-454 |
3.08e-38 |
|
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: 143.31 E-value: 3.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 103 VTLFRQYLRIRTVQP-KPDYGAAVAFFEETARQLGLGCQKVEVAPGYV----VTVLTWPGTNPTlSSILLNSHTDVVPV- 176
Cdd:TIGR01910 1 VELLKDLISIPSVNPpGGNEETIANYIKDLLREFGFSTDVIEITDDRLkvlgKVVVKEPGNGNE-KSLIFNGHYDVVPAg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 177 FKEHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQGMELFVQRpefha 256
Cdd:TIGR01910 80 DLELWKTDPFKP-VEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGE-AGTLYLLQR----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 257 lraGFALDEG---IANPTDAFTVFYSERSPWWVRVTSTGRPGHASR--FMEDtAAEKLHKVVNSILAFrEKEWQrlQSNP 331
Cdd:TIGR01910 153 ---GYFKDADgvlIPEPSGGDNIVIGHKGSIWFKLRVKGKQAHASFpqFGVN-AIMKLAKLITELNEL-EEHIY--ARNS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 332 HLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAG--EGVTLEFAQKWMHPQVTPTDD 409
Cdd:TIGR01910 226 YGFIPGPITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSksDGWLYENEPVVKWSGPNETPP 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 938318566 410 SNPWWAAFSRVCKDMnLTLEPEIM--PAATDNRYIRAVGVPALGFSP 454
Cdd:TIGR01910 306 DSRLVKALEAIIKKV-RGIEPEVLvsTGGTDARFLRKAGIPSIVYGP 351
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
102-490 |
4.01e-37 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 140.90 E-value: 4.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 102 SVTLFRQYLRIRTVQPKP-DYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTW-----PGTNPTLSSILLNSHTDVVP 175
Cdd:PRK08651 8 IVEFLKDLIKIPTVNPPGeNYEEIAEFLRDTLEELGFSTEIIEVPNEYVKKHDGPrpnliARRGSGNPHLHFNGHYDVVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 176 VfKEHW-SHDPFEAFKDsEGYIYARGAQDMK--CVSIqyLEAVRRLKVEGhrfPRTIHMTFVPDEEVGGHQGMELfvqrp 252
Cdd:PRK08651 88 P-GEGWsVNVPFEPKVK-DGKVYGRGASDMKggIAAL--LAAFERLDPAG---DGNIELAIVPDEETGGTGTGYL----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 253 efhALRAGFALDEGI-ANPTDAFTVFYSERSPWWVRVTSTGRPGHASR-FMEDTAAEKLHKVVNSILAFREKEWQRLQSN 330
Cdd:PRK08651 156 ---VEEGKVTPDYVIvGEPSGLDNICIGHRGLVWGVVKVYGKQAHASTpWLGINAFEAAAKIAERLKSSLSTIKSKYEYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 331 PHlkEGSVTSVNL--TKLEGGVAYNVIPATMSASFDFRVAPDVD----FKAFEEQLQSWCQAAGEGVTLE---FAQKWMh 401
Cdd:PRK08651 233 DE--RGAKPTVTLggPTVEGGTKTNIVPGYCAFSIDRRLIPEETaeevRDELEALLDEVAPELGIEVEFEitpFSEAFV- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 402 pqvtpTDDSNPWWAAFSR-VCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMNrtPVLLHDHDERLHEAVFLRGVDI 480
Cdd:PRK08651 310 -----TDPDSELVKALREaIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGE--LELAHAPDEYVEVKDVEKAAKV 382
|
410
....*....|
gi 938318566 481 YTRLLPALAS 490
Cdd:PRK08651 383 YEEVLKRLAK 392
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
103-485 |
4.52e-37 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 141.53 E-value: 4.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 103 VTLFRQYLRIRTVQP-----KPDYGAAvaffEETARQL---GLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVV 174
Cdd:PRK07906 2 VDLCSELIRIDTTNTgdgtgKGEREAA----EYVAEKLaevGLEPTYLESAPGRANVVARLPGADPSRPALLVHGHLDVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 175 PVFKEHWSHDPFE-AFKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQ-RP 252
Cdd:PRK07906 78 PAEAADWSVHPFSgEIRD--GYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEAGGTYGAHWLVDnHP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 253 EfhalragfaLDEGIanpTDA--------FTV-----FY----SERSPWWVRVTSTGRPGHASRFMEDTA----AE---- 307
Cdd:PRK07906 156 E---------LFEGV---TEAisevggfsLTVpgrdrLYlietAEKGLAWMRLTARGRAGHGSMVNDDNAvtrlAEavar 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 308 --------KLHKVVNSILA--FREKEWQRLQSNPHL---KEGSV---------TSVNLTKLEGGVAYNVIPATMSASFDF 365
Cdd:PRK07906 224 igrhrwplVLTPTVRAFLDgvAELTGLEFDPDDPDAllaKLGPAarmvgatlrNTANPTMLKAGYKVNVIPGTAEAVVDG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 366 RVAPDVDfKAFEEQLQswcQAAGEGVTLEfaqkWMHPQV---TPTDdsNPWWAAfsrvckdMNLTLE---------PEIM 433
Cdd:PRK07906 304 RFLPGRE-EEFLATVD---ELLGPDVERE----WVHRDPaleTPFD--GPLVDA-------MNAALLaedpgarvvPYML 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 938318566 434 PAATDNRYIRAVGVPALGFSPMnRTPV------LLHDHDERLHEAVFLRGVDIYTRLL 485
Cdd:PRK07906 367 SGGTDAKAFSRLGIRCYGFAPL-RLPPdldfaaLFHGVDERVPVDALRFGVRVLDRFL 423
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
103-485 |
8.51e-37 |
|
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: 139.06 E-value: 8.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 103 VTLFRQYLRIRTVQPKPD-YGAAVAFFEETARQLGLGCQKVEVAPG--YVVTVLTWPGTNPTLssiLLNSHTDVVPVFKE 179
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDnTSAIAAYIKLLLEDLGYPVELHEPPEEiyGVVSNIVGGRKGKRL---LFNGHYDVVPAGDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 180 H-WSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHalr 258
Cdd:cd08011 78 EgWTVDPYSG-KIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYLLEKVRIK--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 259 AGFALdegIANPTDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAeklhkvVNSILAFREKewqrlqsnphLKEgSV 338
Cdd:cd08011 154 PNDVL---IGEPSGSDNIRIGEKGLVWVIIEITGKPAHGSLPHRGESA------VKAAMKLIER----------LYE-LE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 339 TSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDfkaFEEQLQSWCQ--AAGEGVTLEFAQKwmhPQVTPTDDSNPWWAA 416
Cdd:cd08011 214 KTVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGIS---TDEVLSRIIDhlDSIEEVSFEIKSF---YSPTVSNPDSEIVKK 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 417 FSRVCKDM-NLTLEPEIMPAATDNRYIRAVGVPALGFSPMNrtPVLLHDHDERLHEAVFLRGVDIYTRLL 485
Cdd:cd08011 288 TEEAITEVlGIRPKEVISVGASDARFYRNAGIPAIVYGPGR--LGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
152-485 |
4.46e-33 |
|
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: 130.84 E-value: 4.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 152 VLTWPGTNPTLSSILLNSHTDVVPVFKEH---WSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRT 228
Cdd:cd05674 59 LYTWEGSDPSLKPLLLMAHQDVVPVNPETedqWTHPPFSGHYD-GGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 229 IHMTFVPDEEVGGHQGMELFVQRPEFhalRAG-----FALDEGIAN-PTDAFTVFY-----SERSPWWVRVTSTGRPGHA 297
Cdd:cd05674 138 IILAFGHDEEVGGERGAGAIAELLLE---RYGvdglaAILDEGGAVlEGVFLGVPFalpgvAEKGYMDVEITVHTPGGHS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 298 S-------------------------RFMEDT--------AAEKLHKVVNSILafrekeWQRLQSNPHLKEGSV------ 338
Cdd:cd05674 215 SvppkhtgigilseavaaleanpfppKLTPGNpyygmlqcLAEHSPLPPRSLK------SNLWLASPLLKALLAsellst 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 339 ---------TSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSwcQAAGEGVTLEFAQKWMHPQVT---- 405
Cdd:cd05674 289 spltrallrTTQAVDIINGGVKINALPETATATVNHRIAPGSSVEEVLEHVKN--LIADIAVKYGLGLSAFGGDVIystn 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 406 ---------------PTDDSNPWWAAFSRVCKDM------NLTLEPEIMPAATDNRYIRAVGVPALGFSPMNRTPVLL-- 462
Cdd:cd05674 367 gtklltsllspepspVSSTSSPVWQLLAGTIRQVfeqfgeDLVVAPGIMTGNTDTRHYWNLTKNIYRFTPIRLNPEDLgr 446
|
410 420
....*....|....*....|....
gi 938318566 463 -HDHDERLHEAVFLRGVDIYTRLL 485
Cdd:cd05674 447 iHGVNERISIDDYLETVAFYYQLI 470
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
105-489 |
3.60e-30 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 122.80 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 105 LFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVVT---VLTWPGTNPTlSSILLNSHTDVVPVFKEHW 181
Cdd:PRK09133 42 LYKELIEINTTASTGSTTPAAEAMAARLKAAGFADADIEVTGPYPRKgnlVARLRGTDPK-KPILLLAHMDVVEAKREDW 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 182 SHDPFEaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGME-LFVQRPEfhALRAG 260
Cdd:PRK09133 121 TRDPFK-LVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEGTPMNGVAwLAENHRD--LIDAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 261 FALDEGIANPTD------AFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFR-------------- 320
Cdd:PRK09133 198 FALNEGGGGTLDedgkpvLLTVQAGEKTYADFRLEVTNPGGHSSRPTKDNAIYRLAAALSRLAAYRfpvmlndvtrayfk 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 321 -----------------------EKEWQRLQSNPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFE 377
Cdd:PRK09133 278 qsaaietgplaaamrafaanpadEAAIALLSADPSYNAMLRTTCVATMLEGGHAENALPQRATANVNCRIFPGDTIEAVR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 378 EQLQswcQAAGE-GVTLEFAQKwmhPQVTPTDDSNP-WWAAFSRVCKDM--NLTLEPEIMPAATDNRYIRAVGVPALGFS 453
Cdd:PRK09133 358 ATLK---QVVADpAIKITRIGD---PSPSPASPLRPdIMKAVEKLTAAMwpGVPVIPSMSTGATDGRYLRAAGIPTYGVS 431
|
410 420 430
....*....|....*....|....*....|....*...
gi 938318566 454 PM--NRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALA 489
Cdd:PRK09133 432 GLfgDPDDTFAHGLNERIPVASFYEGRDFLYELVKDLA 469
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
165-485 |
8.40e-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: 111.15 E-value: 8.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 165 ILLNSHTDVVPVFKEHWSHDPFEAfKDSEGYIYARGAQDMK----CVsiqyLEAVRRLKVEGHRFPrtIHMTFVPDEEVg 240
Cdd:cd03894 60 LLLSGHTDVVPVDGQKWSSDPFTL-TERDGRLYGRGTCDMKgflaAV----LAAVPRLLAAKLRKP--LHLAFSYDEEV- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 241 GHQGMELFVQRPEFHALRAGFALdegIANPTD-AFTVFYSERSPWWVRVtsTGRPGHASrfmeDT-----AAEKLHKVVN 314
Cdd:cd03894 132 GCLGVRHLIAALAARGGRPDAAI---VGEPTSlQPVVAHKGIASYRIRV--RGRAAHSS----LPplgvnAIEAAARLIG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 315 SILAFREkEWQRLQSNPHLKEGSVTsVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGE--GVT 392
Cdd:cd03894 203 KLRELAD-RLAPGLRDPPFDPPYPT-LNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEfpEAG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 393 LEFAQKWMHPQVtPTDDSNPWWAAFSRVCKDMNltlePEIMPAATDNRYIRAVGVPALGFSP--MNRTpvllHDHDERLH 470
Cdd:cd03894 281 IEVEPLFEVPGL-ETDEDAPLVRLAAALAGDNK----VRTVAYGTEAGLFQRAGIPTVVCGPgsIAQA----HTPDEFVE 351
|
330
....*....|....*
gi 938318566 471 EAVFLRGVDIYTRLL 485
Cdd:cd03894 352 LEQLDRCEEFLRRLI 366
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
152-263 |
1.51e-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: 106.36 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 152 VLTWPGTnPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHM 231
Cdd:cd18669 3 IARYGGG-GGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVV 81
|
90 100 110
....*....|....*....|....*....|..
gi 938318566 232 TFVPDEEVGGHQGMELFVQRPEFHALRAGFAL 263
Cdd:cd18669 82 AFTPDEEVGSGAGKGLLSKDALEEDLKVDYLF 113
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
152-481 |
2.89e-26 |
|
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 105.59 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 152 VLTWPGTnPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHM 231
Cdd:cd03873 3 IARLGGG-EGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 232 TFVPDEEVGGHQGMELFVQRpefhALRAGFALDEgianptdaftVFYSERSPWWvrvtsTGRPGHASRfmedtaaeklhk 311
Cdd:cd03873 82 AFTADEEVGSGGGKGLLSKF----LLAEDLKVDA----------AFVIDATAGP-----ILQKGVVIR------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 312 vvnsilafrekewqrlqsnphlkegsvtsvnltkleggvaynvipatmsasfdfrvapdvdfkafeeqlqswcqaagegv 391
Cdd:cd03873 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 392 tlefaqkwmhpqvtptddsNPWWAAFSRVCKDMNLTLEPEIM-PAATDNRYIRAVGVPALGFSPMnrTPVLLHDHDERLH 470
Cdd:cd03873 131 -------------------NPLVDALRKAAREVGGKPQRASViGGGTDGRLFAELGIPGVTLGPP--GDKGAHSPNEFLN 189
|
330
....*....|.
gi 938318566 471 EAVFLRGVDIY 481
Cdd:cd03873 190 LDDLEKATKVY 200
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
123-455 |
4.55e-25 |
|
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: 106.14 E-value: 4.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 123 AAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPtlSSILLNSHTDVVpvfkehWSHD--PFEAFKDSEGYIYARG 200
Cdd:cd03885 23 RVAELLAEELEALGFTVERRPLGEFGDHLIATFKGTGG--KRVLLIGHMDTV------FPEGtlAFRPFTVDGDRAYGPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 201 AQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFvqrpEFHALRAGFALDEGIANPTDAFTVFYSE 280
Cdd:cd03885 95 VADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRELI----EEEAKGADYVLVFEPARADGNLVTARKG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 281 RSPWWVRVtsTGRPGHASRFMEDTAaeklhkvvNSILAFREKeWQRLQSNPHLKEGsvTSVNLTKLEGGVAYNVIPATMS 360
Cdd:cd03885 171 IGRFRLTV--KGRAAHAGNAPEKGR--------SAIYELAHQ-VLALHALTDPEKG--TTVNVGVISGGTRVNVVPDHAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 361 ASFDFRVAPDVDFKAFEEQLQSWCQAA-GEGVTLEFAQKWMHPQVTPTDDSNPWWAAFSRVCKDMNLTLEPEIMPAATDN 439
Cdd:cd03885 238 AQVDVRFATAEEADRVEEALRAIVATTlVPGTSVELTGGLNRPPMEETPASRRLLARAQEIAAELGLTLDWEATGGGSDA 317
|
330
....*....|....*..
gi 938318566 440 RYIRAVGVPAL-GFSPM 455
Cdd:cd03885 318 NFTAALGVPTLdGLGPV 334
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
98-470 |
3.30e-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: 98.53 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 98 EEHPSVTLFRQYLRIRtvqpkpdyGAAVAFFEETARQLG--LGCQKVEV----APGyVVTVLTwpGTNPTLSSILLNSHT 171
Cdd:cd03895 15 EEAAAQDLVAAALRSR--------GYTVDRWEIDVEKLKhhPGFSPVAVdyagAPN-VVGTHR--PRGETGRSLILNGHI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 172 DVVPVFK-EHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQ 250
Cdd:cd03895 84 DVVPEGPvELWTRPPFEA-TIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNGALAALMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 251 rpefhALRAGFALdegIANPTDAfTVFYSERSPWWVRVTSTGRPGHASRFMEDTAA-EKLHKVVNSILAFrEKEW-QRLQ 328
Cdd:cd03895 163 -----GYRADAAL---IPEPTEL-KLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAiEKAMHLIQALQEL-EREWnARKK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 329 SNPHL--KEGSVTsVNLTKLEGGVAYNVIPAtmSASFDFRVA--PDVDFKAFEEQLQSWCQAAgegvtlEFAQKWM--HP 402
Cdd:cd03895 233 SHPHFsdHPHPIN-FNIGKIEGGDWPSSVPA--WCVLDCRIGiyPGESPEEARREIEECVADA------AATDPWLsnHP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 403 -QVT---------PTDDSNPWWAAFSRVCKDM-NLTLEPEIMPAATDNR-YIRAVGVPALGFSPMNRTPvllHDHDERLH 470
Cdd:cd03895 304 pEVEwngfqaegyVLEPGSDAEQVLAAAHQAVfGTPPVQSAMTATTDGRfFVLYGDIPALCYGPGSRDA---HGFDESVD 380
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
165-454 |
7.08e-20 |
|
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: 91.04 E-value: 7.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 165 ILLNSHTDVVPVFKEHWSHDPFEaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPrtIHMTFVPDEEVgGHQG 244
Cdd:TIGR01892 61 LALSGHTDVVPYDDAAWTRDPFR-LTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKP--LHLALTADEEV-GCTG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 245 MELFVQRPefhALRAGFALdegIANPTDAFTVfYSERSPWWVRVTSTGRPGHASRFMEDTAA-EKLHKVVNSILAFREke 323
Cdd:TIGR01892 137 APKMIEAG---AGRPRHAI---IGEPTRLIPV-RAHKGYASAEVTVRGRSGHSSYPDSGVNAiFRAGRFLQRLVHLAD-- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 324 wqRLQSNPHLK--EGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGvTLEFAQKW-- 399
Cdd:TIGR01892 208 --TLLREDLDEgfTPPYTTLNIGVIQGGKAVNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRD-EPGFEVQIev 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 938318566 400 --MHPQVTPTDDsnpwwAAFSRVCKDMnLTLEPEIMPAATDNRYIRAVGVPALGFSP 454
Cdd:TIGR01892 285 vsTDPGVNTEPD-----AELVAFLEEL-SGNAPEVVSYGTEAPQFQELGAEAVVCGP 335
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
152-470 |
4.30e-19 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 89.29 E-value: 4.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 152 VLTWPGTNPTLSSILLNSHTDVVPVFK-EHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIH 230
Cdd:PRK06837 87 VGTYRPAGKTGRSLILQGHIDVVPEGPlDLWSRPPFDP-VIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVH 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 231 MTFVPDEEVGGHqGMELFVQRpefhALRAGFALdegIANPTDAfTVFYSERSPWWVRVTSTGRPGHAsRFMEdTAAEKLH 310
Cdd:PRK06837 166 FQSVIEEESTGN-GALSTLQR----GYRADACL---IPEPTGE-KLVRAQVGVIWFRLRVRGAPVHV-REAG-TGANAID 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 311 KVVNSILAFR--EKEW-QRLQSNPHLK-EGSVTSVNLTKLEGGVAYNVIPAtmSASFDFRVA--PDVDFKAFEEQLQSWC 384
Cdd:PRK06837 235 AAYHLIQALRelEAEWnARKASDPHFEdVPHPINFNVGIIKGGDWASSVPA--WCDLDCRIAiyPGVTAADAQAEIEACL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 385 QAAgegvtlEFAQKWMH---PQVTPT---------DDSNPWWAAFSRVCKDMNLT-LEPEIMPAATDNR-YIRAVGVPAL 450
Cdd:PRK06837 313 AAA------ARDDRFLSnnpPEVVWSgflaegyvlEPGSEAEAALARAHAAVFGGpLRSFVTTAYTDTRfYGLYYGIPAL 386
|
330 340
....*....|....*....|
gi 938318566 451 GFSPMNRTPvllHDHDERLH 470
Cdd:PRK06837 387 CYGPSGEGI---HGFDERVD 403
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
103-485 |
5.21e-19 |
|
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: 88.33 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 103 VTLFRQYLRIRTVQPKpDYGAaVAFFEETARQLGLGCQKVEVapGYVVTVLTWPGTNPTLssILLNSHTDVVPV-FKEHW 181
Cdd:cd03891 1 LELAKELIRRPSVTPD-DAGA-QDLIAERLKALGFTCERLEF--GGVKNLWARRGTGGPH--LCFAGHTDVVPPgDLEGW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 182 SHDPFEAfKDSEGYIYARGAQDMKCvSIQ-YLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHALRAG 260
Cdd:cd03891 75 SSDPFSP-TIKDGMLYGRGAADMKG-GIAaFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 261 FALdegIANPTdaftvfySE-----------RSPWWVRVTSTGRPGHASrfMEDTAAEKLHKVVNSILAFrekewqrlqS 329
Cdd:cd03891 153 YCI---VGEPT-------SEkklgdtikigrRGSLNGKLTIKGKQGHVA--YPHLADNPIHLLAPILAEL---------T 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 330 NPHLKEGSV----TSVNLTKLEGGV-AYNVIPATMSASFDFRVAPDVDfkafEEQLQSWCQAAGEGVTLEFAQKWMH--- 401
Cdd:cd03891 212 ATVLDEGNEffppSSLQITNIDVGNgATNVIPGELKAKFNIRFNDEHT----GESLKARIEAILDKHGLDYDLEWKLsge 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 402 PQVTPTDD-SNPWWAAFSRVCKdmnltLEPEImpaAT-----DNRYIRAVGVPALGFSPMNRTpvlLHDHDERLHEAVFL 475
Cdd:cd03891 288 PFLTKPGKlVDAVSAAIKEVTG-----ITPEL---STsggtsDARFIASYGCPVVEFGLVNAT---IHKVNERVSVADLE 356
|
410
....*....|
gi 938318566 476 RGVDIYTRLL 485
Cdd:cd03891 357 KLTDIYERIL 366
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
151-485 |
2.69e-17 |
|
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: 83.26 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 151 TVLTWPGTNPtLSSILLNSHTDVVPVfkehwsHDPFEAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTih 230
Cdd:cd05647 43 TVVARTERGL-ASRVILAGHLDTVPV------AGNLPSRVEEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLT-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 231 MTFVPDEEVGGHQ-GME-LFVQRPEFhaLRAGFALdegIANPTDAfTVFYSERSPWWVRVTSTGRPGHASR-FMEDTAAE 307
Cdd:cd05647 114 LIFYDCEEVAAELnGLGrLAEEHPEW--LAADFAV---LGEPTDG-TIEGGCQGTLRFKVTTHGVRAHSARsWLGENAIH 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 308 KLHKVVNSILAFREKEWQrlQSNPHLKEGsvtsVNLTKLEGGVAYNVIPATMSASFDFRVAPDvdfKAFEEQLQSwCQAA 387
Cdd:cd05647 188 KLAPILARLAAYEPRTVN--IDGLTYREG----LNAVFISGGVAGNVIPDEARVNLNYRFAPD---KSLAEAIAH-VREV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 388 GEGVTLEFAQKWMHPQVTPTDDsNPWWAAFSRVCKDmnltlEPEIMPAATDNRYIRAVGVPALGFSPMNrtPVLLHDHDE 467
Cdd:cd05647 258 FEGLGYEIEVTDLSPGALPGLD-HPVARDLIEAVGG-----KVRAKYGWTDVARFSALGIPAVNFGPGD--PLLAHKRDE 329
|
330
....*....|....*...
gi 938318566 468 RLHEAVFLRGVDIYTRLL 485
Cdd:cd05647 330 QVPVEQITACAAILRRWL 347
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
123-372 |
8.44e-17 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 81.55 E-value: 8.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 123 AAVA-FFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPTlSSILLNSHTDVVPvfkehwSHDPFEAfKDSEGYIYARGA 201
Cdd:cd05652 19 AAVGdFLAEYLESLGFTVEKQPVENKDRFNVYAYPGSSRQ-PRVLLTSHIDTVP------PFIPYSI-SDGGDTIYGRGS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 202 QDMK-CVSIQYLeAVRRLKVEGHRFPRTIHMTFVPDEEVGGHqGMELF--VQRPEFHALRAGfaldegiaNPTD------ 272
Cdd:cd05652 91 VDAKgSVAAQII-AVEELLAEGEVPEGDLGLLFVVGEETGGD-GMKAFndLGLNTWDAVIFG--------EPTElklasg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 273 --AFTVFyserspwwvRVTSTGRPGHaSRFME--DTAAEKLHKVVNSILAfrekewQRLQSNPHLKEgsvTSVNLTKLEG 348
Cdd:cd05652 161 hkGMLGF---------KLTAKGKAGH-SGYPWlgISAIEILVEALVKLID------ADLPSSELLGP---TTLNIGRISG 221
|
250 260
....*....|....*....|....
gi 938318566 349 GVAYNVIPATMSASFDFRVAPDVD 372
Cdd:cd05652 222 GVAANVVPAAAEASVAIRLAAGPP 245
|
|
| PRK06915 |
PRK06915 |
peptidase; |
164-454 |
1.22e-16 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 82.05 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 164 SILLNSHTDVVPVFK-EHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGH 242
Cdd:PRK06915 95 SMILNGHIDVVPEGDvNQWDHHPYSG-EVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEESGGA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 243 QGMElfvqrpefhALRAGFALDEG-IANPTDaFTVFYSERSPWWVRVTSTGRPGH-ASRFMEDTAAEKLHKVVNSILAFR 320
Cdd:PRK06915 174 GTLA---------AILRGYKADGAiIPEPTN-MKFFPKQQGSMWFRLHVKGKAAHgGTRYEGVSAIEKSMFVIDHLRKLE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 321 EKEWQRLqSNPHLKEGSV-TSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGE--------GV 391
Cdd:PRK06915 244 EKRNDRI-TDPLYKGIPIpIPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAELNDvdewfvehPV 322
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 938318566 392 TLE-FAQKWM-------HPQVTPTDDsnpwwaAFSRVCKDMnltlePEI--MPAATDNRYI-RAVGVPALGFSP 454
Cdd:PRK06915 323 EVEwFGARWVpgeleenHPLMTTLEH------NFVEIEGNK-----PIIeaSPWGTDGGLLtQIAGVPTIVFGP 385
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
103-349 |
1.86e-16 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 81.34 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 103 VTLFRQYLRIRTVQPKPD-YGAAVAFFEETARQLGLGCQKVeVAPGYVVTVLTWPGTN--------PTLSSILLNSHTDV 173
Cdd:PRK13013 17 VALTQDLIRIPTLNPPGRaYREICEFLAARLAPRGFEVELI-RAEGAPGDSETYPRWNlvarrqgaRDGDCVHFNSHHDV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 174 VPVfKEHWSHDPFEAFKDsEGYIYARGAQDMK---CVSIQYLEAVRRLKVEghrFPRTIHMTFVPDEEVGGHQGMELFVQ 250
Cdd:PRK13013 96 VEV-GHGWTRDPFGGEVK-DGRIYGRGACDMKgglAASIIAAEAFLAVYPD---FAGSIEISGTADEESGGFGGVAYLAE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 251 RPEFHALRAGFALdegIANPTDAFTVFYSERSPWWVRVTSTGRPGHASR-FMEDTAAEKLHKVVNsilAFREKEWQRLQS 329
Cdd:PRK13013 171 QGRFSPDRVQHVI---IPEPLNKDRICLGHRGVWWAEVETRGRIAHGSMpFLGDSAIRHMGAVLA---EIEERLFPLLAT 244
|
250 260
....*....|....*....|....*
gi 938318566 330 N----PHLKEGSVTS-VNLTKLEGG 349
Cdd:PRK13013 245 RrtamPVVPEGARQStLNINSIHGG 269
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
165-410 |
5.16e-16 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 79.46 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 165 ILLNSHTDVVPVFKEHWSHDPFEAFKDsEGYIYARGAQDMK----CVsiqyLEAVRRLKVEGHRFPrtIHMTFVPDEEVG 240
Cdd:PRK07522 67 IVLSGHTDVVPVDGQAWTSDPFRLTER-DGRLYGRGTCDMKgfiaAA----LAAVPELAAAPLRRP--LHLAFSYDEEVG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 241 --GHQGM-ELFVQRPEfhalRAGFALdegIANPTD-----------AFtvfyserspwwvRVTSTGRPGHASRfmedtaa 306
Cdd:PRK07522 140 clGVPSMiARLPERGV----KPAGCI---VGEPTSmrpvvghkgkaAY------------RCTVRGRAAHSSL------- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 307 ekLHKVVNSI------LAFREKEWQRLQSNPHLKEG---SVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFE 377
Cdd:PRK07522 194 --APQGVNAIeyaarlIAHLRDLADRLAAPGPFDALfdpPYSTLQTGTIQGGTALNIVPAECEFDFEFRNLPGDDPEAIL 271
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 938318566 378 EQLQSWC--------QAAGEGVTLEFAQKWMHPQVTPTDDS 410
Cdd:PRK07522 272 ARIRAYAeaellpemRAVHPEAAIEFEPLSAYPGLDTAEDA 312
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
164-485 |
9.08e-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: 78.50 E-value: 9.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 164 SILLNSHTDVVPVFKEhWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGhrfPRTIHMTFV--PDEEVGG 241
Cdd:cd05651 57 TLLLNSHHDTVKPNAG-WTKDPFEP-VEKGGKLYGLGSNDAGASVVSLLATFLHLYSEG---PLNYNLIYAasAEEEISG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 242 HQGME-LFVQRPEfhalragfaLDEGI-ANPTDaFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAaekLHKVVNSILAF 319
Cdd:cd05651 132 KNGIEsLLPHLPP---------LDLAIvGEPTE-MQPAIAEKGLLVLDCTARGKAGHAARNEGDNA---IYKALDDIQWL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 320 REKEWQRLqsNPHLKEGSVTsvnLTKLEGGVAYNVIPATMSASFDFRVAPdvdfkAFEEQLqswcqaagegvTLEFAQKW 399
Cdd:cd05651 199 RDFRFDKV--SPLLGPVKMT---VTQINAGTQHNVVPDSCTFVVDIRTTE-----AYTNEE-----------IFEIIRGN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 400 MHPQVTP---------TDDSNPwwaaFSRVCKDMNLTlePEIMPAATDNRYIravGVPA--LGFSPMNRTpvllHDHDER 468
Cdd:cd05651 258 LKSEIKPrsfrlnssaIPPDHP----IVQAAIAAGRT--PFGSPTLSDQALM---PFPSvkIGPGDSSRS----HTADEF 324
|
330
....*....|....*..
gi 938318566 469 LHEAVFLRGVDIYTRLL 485
Cdd:cd05651 325 IELSEIEEGIDIYIELL 341
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
102-485 |
1.45e-14 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 75.14 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 102 SVTLFRQYLRIRTVQPKpDYGAaVAFFEETARQLGLGCQKVEVapGYVVTVLTWPGTNPTLssILLNSHTDVVPV-FKEH 180
Cdd:TIGR01246 1 VTELAKELISRPSVTPN-DAGC-QDIIAERLEKLGFEIEWMHF--GDTKNLWATRGTGEPV--LAFAGHTDVVPAgPEEQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 181 WSHDPFEaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQrpefhALRAG 260
Cdd:TIGR01246 75 WSSPPFE-PVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVE-----TLMAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 261 falDEGI-----ANPTDAF----TVFYSERSPWWVRVTSTGRPGHASrfMEDTAAEKLHKVVNSILAFrekewqrlqSNP 331
Cdd:TIGR01246 149 ---DELIdycivGEPSSVKklgdVIKNGRRGSITGNLTIKGIQGHVA--YPHLANNPIHKAAPALAEL---------TAI 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 332 HLKEGSV----TSVNLTKLEGGV-AYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFAQKwMHPQVTP 406
Cdd:TIGR01246 215 KWDEGNEffppTSLQITNIHAGTgANNVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLS-GEPFLTN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 407 TDD-SNPWWAAFSRVCKdmnltLEPEIMPAA--TDNRYIRAVGVPALGFSPMNRTpvlLHDHDERLHEAVFLRGVDIYTR 483
Cdd:TIGR01246 294 DGKlIDKAREAIEETNG-----IKPELSTGGgtSDGRFIALMGAEVVEFGPVNAT---IHKVNECVSIEDLEKLSDVYQD 365
|
..
gi 938318566 484 LL 485
Cdd:TIGR01246 366 LL 367
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
169-408 |
2.21e-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 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: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 169 SHTDVVPVFK-EHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMEL 247
Cdd:cd05650 76 SHLDTVPPGDlSLWETDPWEPVVK-DGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEYGIQY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 248 FVQRPEFhalragFALDEGIANP----TDAFTVFYSERSPWWVRVTSTGRPGHASrfMEDTAAEKLHKVVNSILAFREKE 323
Cdd:cd05650 155 LLNKFDL------FKKDDLIIVPdfgtEDGEFIEIAEKSILWIKVNVKGKQCHAS--TPENGINAFVAASNFALELDELL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 324 WQRLQSNPHLKEGSVTSVNLTKLEGGVA-YNVIPATMSASFDFRVAP--DVD--FKAFEEQLQSWCQAAGEGVTLEFAQK 398
Cdd:cd05650 227 HEKFDEKDDLFNPPYSTFEPTKKEANVPnVNTIPGYDVFYFDCRVLPtyKLDevLKFVNKIISDFENSYGAGITYEIVQK 306
|
250
....*....|
gi 938318566 399 WMHPQVTPTD 408
Cdd:cd05650 307 EQAPPATPED 316
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
170-486 |
2.29e-14 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 74.54 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 170 HTDVVPVFKEH-WSHDPFEAfKDSEGYIYARGAQDMK----CVSIqyleAVRRLKVEGHRFPRTIHMTFVPDEEVGGHqG 244
Cdd:PRK08588 67 HMDVVAAGDVDkWTYDPFEL-TEKDGKLYGRGATDMKsglaALVI----AMIELKEQGQLLNGTIRLLATAGEEVGEL-G 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 245 MELFVQrpefhalrAGFALD-EG--IANPTDAFtVFYSERSPWWVRVTSTGRPGHASrfMedtaAEKLHKVVNSILAFRE 321
Cdd:PRK08588 141 AKQLTE--------KGYADDlDAliIGEPSGHG-IVYAHKGSMDYKVTSTGKAAHSS--M----PELGVNAIDPLLEFYN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 322 KEWQRLQS-NPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWC----QAAGEGVTLEFA 396
Cdd:PRK08588 206 EQKEYFDSiKKHNPYLGGLTHVVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIInevnQNGAAQLSLDIY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 397 QKwmHPQVTPTDDSNPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVG--VPALGFSP-MNRTPvllHDHDERLHEAV 473
Cdd:PRK08588 286 SN--HRPVASDKDSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKpdFPVIIFGPgNNLTA---HQVDEYVEKDM 360
|
330
....*....|...
gi 938318566 474 FLRGVDIYTRLLP 486
Cdd:PRK08588 361 YLKFIDIYKEIII 373
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
169-449 |
5.91e-14 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 73.34 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 169 SHTDVVPVFKEH-WSHDPFEA-FKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGME 246
Cdd:PRK13983 83 SHMDVVPPGDLSlWETDPFKPvVKD--GKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYGIQ 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 247 -LFVQRPEfhalraGFALDEGI-----ANPTDAFtVFYSERSPWWVRVTSTGRPGHASrfMEDTA----------AEKLH 310
Cdd:PRK13983 161 yLLKKHPE------LFKKDDLIlvpdaGNPDGSF-IEIAEKSILWLKFTVKGKQCHAS--TPENGinahraaadfALELD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 311 KVVNSilAFREKewqrlqsNPhLKEGSVTSVNLTKLEGGV-AYNVIPATMSASFDFRVAPDVD----FKAFEEQLQSWCQ 385
Cdd:PRK13983 232 EALHE--KFNAK-------DP-LFDPPYSTFEPTKKEANVdNINTIPGRDVFYFDCRVLPDYDldevLKDIKEIADEFEE 301
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938318566 386 AAGEGVTLEFAQKWMHPQVTPTDdsNPWWAAFSRVCKDMnLTLEPEI--MPAATDNRYIRAVGVPA 449
Cdd:PRK13983 302 EYGVKIEVEIVQREQAPPPTPPD--SEIVKKLKRAIKEV-RGIEPKVggIGGGTVAAFLRKKGYPA 364
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
164-469 |
5.95e-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: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 164 SILLNSHTDVVPVfKEHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQ 243
Cdd:cd02697 75 TVALNAHGDVVPP-GDGWTRDPYGAVVE-DGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 244 GMELFVQ----RPEFhALRAGFAldegianptdaFTVFYSERSPWWVRVTSTGRPGHASRfmEDTAAEKLH---KVVNSI 316
Cdd:cd02697 153 GPGWLLRqgltKPDL-LIAAGFS-----------YEVVTAHNGCLQMEVTVHGKQAHAAI--PDTGVDALQgavAILNAL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 317 LAFREKEWQRLQSNPHLkegSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGE---GVTL 393
Cdd:cd02697 219 YALNAQYRQVSSQVEGI---THPYLNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAAsmpGISV 295
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 938318566 394 EFAQKWMHPQVTPTDDSNPWWAAFSRVCKDMNLTLEPEI-MPAATDNRYIRAVGVPALGFSPMNRTPVLLHDH--DERL 469
Cdd:cd02697 296 DIRRLLLANSMRPLPGNAPLVEAIQTHGEAVFGEPVPAMgTPLYTDVRLYAEAGIPGVIYGAGPRTVLESHAKraDERL 374
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
103-488 |
7.03e-14 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 72.77 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 103 VTLFRQYLRIRTvqPKPDYGAAVAFFEETARQLGLGCQKVEVapGYVVTVLtwpGTNPTLssILLNSHTDVVPVFKEhws 182
Cdd:cd05653 4 VELLLDLLSIYS--PSGEEARAAKFLEEIMKELGLEAWVDEA--GNAVGGA---GSGPPD--VLLLGHIDTVPGEIP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 183 hdpfeaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRfprTIHMTFVPDEEVGGHQGMELFVQRPEFHALRAGfa 262
Cdd:cd05653 72 ------VRVEGGVLYGRGAVDAKGPLAAMILAASALNEELGA---RVVVAGLVDEEGSSKGARELVRRGPRPDYIIIG-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 263 ldegiaNPTDAFTVFYSERSPWWVRVTSTGRPGHASRfMEDTAAEKLHKVVNSILafrekewqRLQSNPHLKEGSVTSVN 342
Cdd:cd05653 141 ------EPSGWDGITLGYRGSLLVKIRCEGRSGHSSS-PERNAAEDLIKKWLEVK--------KWAEGYNVGGRDFDSVV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 343 LTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCqaagEGVTLEFAQKwMHPQVTPTDdsNPWWAAFSRVCK 422
Cdd:cd05653 206 PTLIKGGESSNGLPQRAEATIDLRLPPRLSPEEAIALATALL----PTCELEFIDD-TEPVKVSKN--NPLARAFRRAIR 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 938318566 423 DMNLtlEPEIMPAA--TD-NRYIRAVGVPALGFSPMNrtPVLLHDHDERLHEAVFLRGVDIYTRLLPAL 488
Cdd:cd05653 279 KQGG--KPRLKRKTgtSDmNVLAPLWTVPIVAYGPGD--STLDHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
278-392 |
2.63e-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: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 278 YSERSPWWVRVTSTGRPGHASRFmedtaaeklHKVVNSI-------LAFREKEWQRLQSNPHlkegsvTSVNLTKLEGGV 350
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAP---------GKGVNAIkllarllAELPAEYGDIGFDFPR------TTLNITGIEGGT 65
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 938318566 351 AYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVT 392
Cdd:pfam07687 66 ATNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
165-456 |
7.26e-12 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 66.71 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 165 ILLNS--------HTDVVPVFKEhwshdPFEafkdSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIhmTFVPD 236
Cdd:PRK08652 50 IVVNSkaelfvevHYDTVPVRAE-----FFV----DGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGI--AFVSD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 237 EEVGGhQGMELFVQRpefhaLRAGFALdegIANPTDaFTVFYSERSPWWVRVTSTGRPGHASrFMEdtaaeklhKVVNSI 316
Cdd:PRK08652 119 EEEGG-RGSALFAER-----YRPKMAI---VLEPTD-LKVAIAHYGNLEAYVEVKGKPSHGA-CPE--------SGVNAI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 317 L-AFreKEWQRLQS-NPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWcqAAGEGVTLE 394
Cdd:PRK08652 180 EkAF--EMLEKLKElLKALGKYFDPHIGIQEIIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPI--LDEYTVKYE 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 938318566 395 FAQKWmhpQVTPTDDSNPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVGVPALGFSPMN 456
Cdd:PRK08652 256 YTEIW---DGFELDEDEEIVQLLEKAMKEVGLEPEFTVMRSWTDAINFRYNGTKTVVWGPGE 314
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
127-240 |
8.21e-12 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 66.99 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 127 FFEETARQLGLGCQKVEVAPGYVVTVLTWPGTNPT-LSSILLNSHTDVVPVFK-EHWSHDPFEAFKDsEGYIYARGAQDM 204
Cdd:PRK08596 41 FIAEFLRKLGFSVDKWDVYPNDPNVVGVKKGTESDaYKSLIINGHMDVAEVSAdEAWETNPFEPTIK-DGWLYGRGAADM 119
|
90 100 110
....*....|....*....|....*....|....*.
gi 938318566 205 KCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVG 240
Cdd:PRK08596 120 KGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEVG 155
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
165-485 |
1.11e-11 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 66.38 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 165 ILLNSHTDVVPVfKEHWSHDPFeAFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHrfprtihMTFVPDEEVGGHQG 244
Cdd:PRK08737 66 YLFNVHLDTVPD-SPHWSADPH-VMRRTDDRVIGLGVCDIKGAAAALLAAANAGDGDAA-------FLFSSDEEANDPRC 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 245 MELFVQR-PEFHALRagfaldegIANPTDAFTVFySERSPWWVRVTSTGRPGHASRfMEDTAAEKLHKVVNSILAFREKE 323
Cdd:PRK08737 137 VAAFLARgIPYEAVL--------VAEPTMSEAVL-AHRGISSVLMRFAGRAGHASG-KQDPSASALHQAMRWGGQALDHV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 324 WQRLQSNPHLKEGsvTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEGVTLEFaqkwMHPQ 403
Cdd:PRK08737 207 ESLAHARFGGLTG--LRFNIGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFAGFAEPAAATFEETF----RGPS 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 404 VTPTDDSNpwwAAFSRV-CKDMNLTLEPEIMPAA---TDNRYIRAVGVPALGFSPMNRTPVllHDHDERLHEAVFLRGVD 479
Cdd:PRK08737 281 LPSGDIAR---AEERRLaARDVADALDLPIGNAVdfwTEASLFSAAGYTALVYGPGDIAQA--HTADEFVTLDQLQRYAE 355
|
....*.
gi 938318566 480 IYTRLL 485
Cdd:PRK08737 356 SVHRII 361
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
100-485 |
3.29e-11 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 64.72 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 100 HPSVTLFRQYLRIRTVQPKpDYGAaVAFFEETARQLGLGCQKVEVAPgyvVTVL--TWPGTNPTLssiLLNSHTDVVPV- 176
Cdd:PRK13009 2 SDVLELAQDLIRRPSVTPD-DAGC-QDLLAERLEALGFTCERMDFGD---VKNLwaRRGTEGPHL---CFAGHTDVVPPg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 177 FKEHWSHDPFEAfKDSEGYIYARGAQDMK----CvsiqYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQG----MELF 248
Cdd:PRK13009 74 DLEAWTSPPFEP-TIRDGMLYGRGAADMKgslaA----FVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGtvkvLEWL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 249 VQRPEfhalRAGFALdegIANPT------DA------------FTVfyserspwwvrvtsTGRPGHAS---RfmedtAAE 307
Cdd:PRK13009 149 KARGE----KIDYCI---VGEPTsterlgDVikngrrgsltgkLTV--------------KGVQGHVAyphL-----ADN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 308 KLHKVVnSILAfrekewqRLqSNPHLKEGSV----TSVNLTKLEGGV-AYNVIPATMSASFDFRVAPDVDfkafEEQLQS 382
Cdd:PRK13009 203 PIHLAA-PALA-------EL-AATEWDEGNEffppTSLQITNIDAGTgATNVIPGELEAQFNFRFSTEHT----AESLKA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 383 WCQAAGEGVTLEFAQKWM---HPQVTPTDDSNpwwAAFSRVCKDMNlTLEPEImpaAT-----DNRYIRAVGVPALGFSP 454
Cdd:PRK13009 270 RVEAILDKHGLDYTLEWTlsgEPFLTPPGKLV---DAVVAAIEAVT-GITPEL---STsggtsDARFIADYGAQVVEFGP 342
|
410 420 430
....*....|....*....|....*....|.
gi 938318566 455 MNRTpvlLHDHDERLHEAVFLRGVDIYTRLL 485
Cdd:PRK13009 343 VNAT---IHKVNECVSVADLEKLTRIYERIL 370
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
110-240 |
2.27e-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: 62.40 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 110 LRIRTVQ----PKPDY------GAAVAFFEETARQLGLGCQKVEVAPGYVVTvltwpGTNPTLSSILlnSHTDVVPVfKE 179
Cdd:TIGR01887 12 IAIDSVEdlekAKEGApfgegpRKALDKFLEIAKRDGFTTENVDNYAGYIEY-----GQGEEVLGIL--GHLDVVPA-GD 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 938318566 180 HWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVG 240
Cdd:TIGR01887 84 GWTSPPFEPTIK-DGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEESG 143
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
137-339 |
2.32e-10 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 62.26 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 137 LGCQKVEVAP-----GYVvtvltwpGTNPTLssILLNSHTDVVPVF-KEHWSHDPFEAFKDsEGYIYARGAQDMK--CVS 208
Cdd:PRK13004 48 VGFDKVEIDPmgnvlGYI-------GHGKKL--IAFDAHIDTVGIGdIKNWDFDPFEGEED-DGRIYGRGTSDQKggMAS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 209 IQYleAVRRLKVEGHRFPRTIHMT-FVPDEEVGGHQGMELFVQ---RPEFHAlragfaldegIANPTDaFTVFYSERSPW 284
Cdd:PRK13004 118 MVY--AAKIIKDLGLDDEYTLYVTgTVQEEDCDGLCWRYIIEEdkiKPDFVV----------ITEPTD-LNIYRGQRGRM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 938318566 285 WVRVTSTGRPGHAS---RfmEDTAAEKLHKVVNSILAFREKewqrLQSNPHLKEGSVT 339
Cdd:PRK13004 185 EIRVETKGVSCHGSapeR--GDNAIYKMAPILNELEELNPN----LKEDPFLGKGTLT 236
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
165-450 |
3.17e-10 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 61.76 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 165 ILLNSHTDVVPvFKEH-WSHDPF---EAfkdsEGYIYARGAQDMKCVSIQYLEAVRRLKVegHRFPRTIHMTFVPDEEVG 240
Cdd:PRK05111 74 LLLAGHTDTVP-FDEGrWTRDPFtltEH----DGKLYGLGTADMKGFFAFILEALRDIDL--TKLKKPLYILATADEETS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 241 GHqGMELFVQRpefHALRAGFALdegIANPTDAFTVF-----YSERspwwVRVtsTGRPGHASrfmeD-----TAAEKLH 310
Cdd:PRK05111 147 MA-GARAFAEA---TAIRPDCAI---IGEPTSLKPVRahkghMSEA----IRI--TGQSGHSS----DpalgvNAIELMH 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 311 KVVNSILAFREkEWQRLQSNPHLKEGSVTsVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGE- 389
Cdd:PRK05111 210 DVIGELLQLRD-ELQERYHNPAFTVPYPT-LNLGHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSEr 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938318566 390 -GVTLEFAQkwMHPQV----TPTDdsnpwwAAFSRVCKdmNLT-LEPEIMPAATDNRYIRAVGVPAL 450
Cdd:PRK05111 288 wPGRITVAP--LHPPIpgyeCPAD------HQLVRVVE--KLLgHKAEVVNYCTEAPFIQQLGCPTL 344
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
110-488 |
3.35e-10 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 61.94 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 110 LRIRTVQPKPDYGAAVAFFEE-TARQL-GLGCQKVEV--APGYVVTVLTWPGTnPTLSSILLNSHTDVVPVFKEH-WSHD 184
Cdd:cd05680 8 LRIPSVSADPAHKGDVRRAAEwLADKLtEAGFEHTEVlpTGGHPLVYAEWLGA-PGAPTVLVYGHYDVQPPDPLElWTSP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 185 PFE-AFKDseGYIYARGAQDMKCVSIQYLEAVRR-LKVEGhRFPRTIHMTFVPDEEVGGhQGMELFVqrpEFHA--LRAG 260
Cdd:cd05680 87 PFEpVVRD--GRLYARGASDDKGQVFIHIKAVEAwLAVEG-ALPVNVKFLIEGEEEIGS-PSLPAFL---EENAerLAAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 261 FAL--DEGIANPtDAFTVFYSER--SPWWVRVTSTGRPGHASRF--MEDTAAEKLHKVVNSI------------------ 316
Cdd:cd05680 160 VVLvsDTSMWSP-DTPTITYGLRglAYLEISVTGPNRDLHSGSYggAVPNPANALARLLASLhdedgrvaipgfyddvrp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 317 LAFREKE-WQRLqsnPHLKEGSVTSVNLTKLEGGVAYN---------------------------VIPATMSASFDFRVA 368
Cdd:cd05680 239 LTDAEREaWAAL---PFDEAAFKASLGVPALGGEAGYTtlerlwarptldvngiwggyqgegsktVIPSKAHAKISMRLV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 369 PDVDFKAFEEQLQSWCQA-AGEGVTLEFaqKWMH---PQVTPTDDsnPWWAAFSRVC-----KDMNLTLEPEIMPAATDN 439
Cdd:cd05680 316 PGQDPDAIADLLEAHLRAhAPPGVTLSV--KPLHggrPYLVPTDH--PALQAAERALeeafgKPPVFVREGGSIPIVALF 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 938318566 440 RyiRAVGVPAL--GFS-PMNRtpvlLHDHDERLHEAVFLRGVDIYTRLLPAL 488
Cdd:cd05680 392 E--KVLGIPTVlmGFGlPDDA----IHAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
103-366 |
3.36e-10 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 61.67 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 103 VTLFRQYLRIRTvqPKPDYGAAVAFFEETARQLGLgcQKVEVAPgyVVTVLTWPGTNPTLssILLNSHTDVVPVF-KEHW 181
Cdd:cd05649 1 TRFLRDLIQIPS--ESGEEKGVVERIEEEMEKLGF--DEVEIDP--MGNVIGYIGGGKKK--ILFDGHIDTVGIGnIDNW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 182 SHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHR-FPRTIHMTFVPDEEV-GGHQGMELFVQ---RPEFHA 256
Cdd:cd05649 73 KFDPYEG-YETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLRdFAYTILVAGTVQEEDcDGVCWQYISKAdkiKPDFVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 257 lragfaldegIANPTDAfTVFYSERSPWWVRVTSTGRPGHASrfmedtAAEK----LHKVVNSILAFREKEwQRLQSNPH 332
Cdd:cd05649 152 ----------SGEPTDG-NIYRGQRGRMEIRVDTKGVSCHGS------APERgdnaVYKMADIIQDIRQLN-PNFPEAPF 213
|
250 260 270
....*....|....*....|....*....|....
gi 938318566 333 LKEGSVTSVNLTKLEGGVayNVIPATMSASFDFR 366
Cdd:cd05649 214 LGRGTLTVTDIFSTSPSR--CAVPDSCRISIDRR 245
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
107-361 |
6.35e-10 |
|
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: 61.11 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 107 RQYLRIRTV--QPKPDY--G----AAVAFFEETARQLGLgcqKVEVAPGYVVTVLTwpGTNPTLSSILlnSHTDVVPVfK 178
Cdd:cd03888 15 KELVAIPSVrdEATEGApfGegprKALDKFLDLAKRLGF---KTKNIDNYAGYAEY--GEGEEVLGIL--GHLDVVPA-G 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 179 EHWSHDPFEAFKDsEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQGMELFVQR---PEFh 255
Cdd:cd03888 87 EGWTTDPFKPVIK-DGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGW-KCIEHYFEHeeyPDF- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 256 alraGFALDegiANptdaFTVFYSERSPWWVRVTSTGRPGhasrfmedtaaeklhkvvnsilafrekewqrlqsnphlke 335
Cdd:cd03888 164 ----GFTPD---AE----FPVINGEKGIVTVDLTFKIDDD---------------------------------------- 192
|
250 260
....*....|....*....|....*.
gi 938318566 336 gsvTSVNLTKLEGGVAYNVIPATMSA 361
Cdd:cd03888 193 ---KGYRLISIKGGEATNMVPDKAEA 215
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
129-485 |
1.31e-09 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 59.68 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 129 EETARQLGLGCQKVEVapGYVVtvLTWPGT-NPTLSSILLNSHTDVVPVFkehwSHDPFEAFKDsEGYIYAR-----GAQ 202
Cdd:COG2195 30 VEELKELGLEVEEDEA--GNVI--ATLPATpGYNVPTIGLQAHMDTVPQF----PGDGIKPQID-GGLITADgtttlGAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 203 DmK--CVSIqyLEAVRRLKVEG--HRfprTIHMTFVPDEEVGGHqGMELFvqrpEFHALRAGFAL-----DEG---IANP 270
Cdd:COG2195 101 D-KagVAAI--LAALEYLKEPEipHG---PIEVLFTPDEEIGLR-GAKAL----DVSKLGADFAYtldggEEGeleYECA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 271 TDAFtvfyserspwwVRVTSTGRPGHASrfmedTAAEKLhkvVNSI-LAFrekewqRLQSnpHLKEGSV---TSVNLTKL 346
Cdd:COG2195 170 GAAD-----------AKITIKGKGGHSG-----DAKEKM---INAIkLAA------RFLA--ALPLGRIpeeTEGNEGFI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 347 EGGVAYNVIPATMSASFdfrVAPDVDFKAFEEQLQSWCQAA-------GEGVtLEFAQKWMHPQVTPTDDSNPwWAAFSR 419
Cdd:COG2195 223 HGGSATNAIPREAEAVY---IIRDHDREKLEARKAELEEAFeeenakyGVGV-VEVEIEDQYPNWKPEPDSPI-VDLAKE 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 420 VCKDMNltLEPEIMP--AATDNRYIRAVGVPALGFSP--MNrtpvlLHDHDERLHEAVFLRGVDIYTRLL 485
Cdd:COG2195 298 AYEELG--IEPKIKPirGGLDGGILSFKGLPTPNLGPggHN-----FHSPDERVSIESMEKAWELLVEIL 360
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
170-238 |
1.82e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 56.63 E-value: 1.82e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 938318566 170 HTDVVPVFKEH-WSHDPFEA-FKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEE 238
Cdd:PRK07205 83 HLDVVPEGDLSdWQTPPFEAvEKD--GCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGTDEE 151
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
136-383 |
3.20e-08 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 55.54 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 136 GLGCQKVEVAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGyIYARGAQDmkCVSIQYL--E 213
Cdd:cd08012 52 PLVIDHVSYVKGRGNIIVEYPGTVDGKTVSFVGSHMDVVTANPETWEFDPFSLSIDGDK-LYGRGTTD--CLGHVALvtE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 214 AVRRLKVEGHRFPRTIHMTFVPDEEVGG--HQGMELFVQRPEFHALRAG--FALDEGIANPtdafTVFYSERSPWwvRVT 289
Cdd:cd08012 129 LFRQLATEKPALKRTVVAVFIANEENSEipGVGVDALVKSGLLDNLKSGplYWVDSADSQP----CIGTGGMVTW--KLT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 290 STGRPGHASRfmedtaaekLHKVVNSILAFRE--KEWQR---LQSNPHLKEG-------SVTSVNLTKLEGGvAYNVIPA 357
Cdd:cd08012 203 ATGKLFHSGL---------PHKAINALELVMEalAEIQKrfyIDFPPHPKEEvygfatpSTMKPTQWSYPGG-SINQIPG 272
|
250 260
....*....|....*....|....*.
gi 938318566 358 TMSASFDFRVAPDVDFKAFEEQLQSW 383
Cdd:cd08012 273 ECTICGDCRLTPFYDVKEVREKLEEY 298
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
107-266 |
3.92e-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: 55.42 E-value: 3.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 107 RQYLRIRTVQPKPDYGAAVA-FFEETARQLGLGCQKVEvAPGYVVTVLTWP-GTNPTLssiLLNSHTDVVPVFK-EHWSH 183
Cdd:cd05681 6 RDLLKIPSVSAQGRGIPETAdFLKEFLRRLGAEVEIFE-TDGNPIVYAEFNsGDAKTL---LFYNHYDVQPAEPlELWTS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 184 DPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQGMELFVQRpefHA--LRAGF 261
Cdd:cd05681 82 DPFEL-TIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGS-PNLEKFVAE---HAdlLKADG 156
|
....*
gi 938318566 262 ALDEG 266
Cdd:cd05681 157 CIWEG 161
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
136-369 |
4.03e-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: 55.18 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 136 GLGCQKVEVAPGY--VVTVLTWPGTNPTLssiLLNSHTDVVPVfkEHWSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLE 213
Cdd:cd08013 43 GIEAHRIEGTPGRpsVVGVVRGTGGGKSL---MLNGHIDTVTL--DGYDGDPLSG-EIADGRVYGRGTLDMKGGLAACMA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 214 AVRRLKVEGHRfpRTIHMTFVPDEEVGGhQGMElfvqrpefHALRAGFALDEGI-ANPTDaFTVFYSERSPWWVRVTSTG 292
Cdd:cd08013 117 ALADAKEAGLR--GDVILAAVADEEDAS-LGTQ--------EVLAAGWRADAAIvTEPTN-LQIIHAHKGFVWFEVDIHG 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938318566 293 RPGHASRfmEDTAAEKLHKVVNSILAFREKEwQRLQSNPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAP 369
Cdd:cd08013 185 RAAHGSR--PDLGVDAILKAGYFLVALEEYQ-QELPERPVDPLLGRASVHASLIKGGEEPSSYPARCTLTIERRTIP 258
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
107-485 |
2.67e-07 |
|
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: 52.72 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 107 RQYLRIRTVQPKPD----YGAAVAFFEETARQLGLGCQKVEVAPG--YVVTVLTWPGTNPTlssILLNSHTDVVPVFKEH 180
Cdd:cd03893 5 AELVAIPSVSAQPDrreeLRRAAEWLADLLRRLGFTVEIVDTSNGapVVFAEFPGAPGAPT---VLLYGHYDVQPAGDED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 181 -WSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMtFVPDEEVGGHQGMELFV-QRPEFHALR 258
Cdd:cd03893 82 gWDSDPFEL-TERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKF-IIEGEEESGSPSLDQLVeAHRDLLAAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 259 AGFALDeGIANPTDAFTVFYSERSPWWVRVTSTGR--PGHASRF--MEDTAAEKLHKVVNSILAFR-------------- 320
Cdd:cd03893 160 AIVISD-STWVGQEQPTLTYGLRGNANFDVEVKGLdhDLHSGLYggVVPDPMTALAQLLASLRDETgrilvpglydavre 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 321 --EKEWQRLQ------SNPHLKEGSVT-------SVNLTKLEGGV----AYNVIPATMSASFDFRVAPDVDFKAFEEQLQ 381
Cdd:cd03893 239 lpEEEFRLDAgvleevEIIGGTTGSVAerlwtrpALTVLGIDGGFpgegSKTVIPPRARAKISIRLVPGQDPEEASRLLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 382 SWCQA---AGEGVTLEFAQKWMhPQVTPTDDsnPWWAAFSRVCKDMNLTLEPEIMPAAT---DNRYIRAVGVPALgfspm 455
Cdd:cd03893 319 AHLEKhapSGAKVTVSYVEGGM-PWRSDPSD--PAYQAAKDALRTAYGVEPPLTREGGSipfISVLQEFPQAPVL----- 390
|
410 420 430
....*....|....*....|....*....|....*
gi 938318566 456 nRTPVLL-----HDHDERLHEAVFLRGVDIYTRLL 485
Cdd:cd03893 391 -LIGVGDpddnaHSPNESLRLGNYKEGTQAEAALL 424
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
105-368 |
3.22e-07 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 52.09 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 105 LFRQYLRIRTvqPKPDYGAAVAFFEETARQLGLGCQkvevapgyvvtvlTWPGTNPTLSS---ILLNSHTDVVPVFKEhw 181
Cdd:PRK00466 15 LLLDLLSIYT--PSGNETNATKFFEKISNELNLKLE-------------ILPDSNSFILGegdILLASHVDTVPGYIE-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 182 shdPFEafkdsEGY-IYARGAQDMKCVSIQYLEAVRRLKVEGHRfprtIHMTFVPDEEVGGHQGMELfvqrpefhaLRAG 260
Cdd:PRK00466 78 ---PKI-----EGEvIYGRGAVDAKGPLISMIIAAWLLNEKGIK----VMVSGLADEESTSIGAKEL---------VSKG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 261 FALDEGI-ANPTDAFTVFYSERSPWWVRVTSTGRPGHASRfMEDTAAEKLHKVVNSILafrekewqRLQSNPhlkegSVT 339
Cdd:PRK00466 137 FNFKHIIvGEPSNGTDIVVEYRGSIQLDIMCEGTPEHSSS-AKSNLIVDISKKIIEVY--------KQPENY-----DKP 202
|
250 260
....*....|....*....|....*....
gi 938318566 340 SVNLTKLEGGVAYNVIPATMSASFDFRVA 368
Cdd:PRK00466 203 SIVPTIIRAGESYNVTPAKLYLHFDVRYA 231
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
111-256 |
7.12e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 51.44 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 111 RIRTVQPKP----DYGAAVAFFEETARQLGLGCQKVEVAPGYVVTVLTWPGTN--PTlssILLNSHTDVVPVFKE-HWSH 183
Cdd:PRK07907 29 RIPSVAADPfrreEVARSAEWVADLLREAGFDDVRVVSADGAPAVIGTRPAPPgaPT---VLLYAHHDVQPPGDPdAWDS 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 938318566 184 DPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRRLkveGHRFPRTIHMtFVPDEEVGGHQGMELFV--QRPEFHA 256
Cdd:PRK07907 106 PPFEL-TERDGRLYGRGAADDKGGIAMHLAALRAL---GGDLPVGVTV-FVEGEEEMGSPSLERLLaeHPDLLAA 175
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
117-390 |
1.07e-06 |
|
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: 50.56 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 117 PKP---DYGAAVAFFEETARqlgLGCQKVEV-APGYVVTVLTWPGTNPtlsSILLNSHTDVVpvFKEHwshDPFEAFKDs 192
Cdd:cd03896 11 PAPtfrEGARADLVAEWMAD---LGLGDVERdGRGNVVGRLRGTGGGP---ALLFSAHLDTV--FPGD---TPATVRHE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 193 EGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMT-FVPDEEVGGHQGMELFVQRpefHALRAGFALdegIANPT 271
Cdd:cd03896 79 GGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAaNVGEEGLGDLRGARYLLSA---HGARLDYFV---VAEGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 272 DaFTVFYSERSPWWVRVTSTGRPGHasRFMEDTAAEKLHKVVNSILAFreKEWQrLQSNPHlkegsvTSVNLTKLEGGVA 351
Cdd:cd03896 153 D-GVPHTGAVGSKRFRITTVGPGGH--SYGAFGSPSAIVAMAKLVEAL--YEWA-APYVPK------TTFAAIRGGGGTS 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 938318566 352 YNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEG 390
Cdd:cd03896 221 VNRIANLCSMYLDIRSNPDAELADVQREVEAVVSKLAAK 259
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
157-240 |
1.84e-06 |
|
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.
Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 50.29 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 157 GTNPTLSSILLNSHTDVVPVFKE-HWSHDPFEaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVP 235
Cdd:cd05676 80 GSDPSKKTVLIYGHLDVQPAKLEdGWDTDPFE-LTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEG 158
|
....*
gi 938318566 236 DEEVG 240
Cdd:cd05676 159 MEESG 163
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
107-251 |
2.61e-06 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 49.74 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 107 RQYLRIRTV----QPKPDYGAAVAFFEETARQLGLgcQKVEV--APGYVVTVLTW---PGtNPTlssILLNSHTDVVPVF 177
Cdd:PRK08201 21 KEFLRIPSIsalsEHKEDVRKAAEWLAGALEKAGL--EHVEImeTAGHPIVYADWlhaPG-KPT---VLIYGHYDVQPVD 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 938318566 178 KEH-WSHDPFEAfKDSEGYIYARGAQDMKCVSIQYLEAVRR-LKVEGhRFPRTIHMTFVPDEEVGGhQGMELFVQR 251
Cdd:PRK08201 95 PLNlWETPPFEP-TIRDGKLYARGASDDKGQVFMHLKAVEAlLKVEG-TLPVNVKFCIEGEEEIGS-PNLDSFVEE 167
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
165-247 |
5.27e-06 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 48.62 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 165 ILLNSHTDVVPVFKEHWSHDPFEaFKDSEGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRfpRTIHMTFVPDEEVGGHQG 244
Cdd:PRK08554 66 LLFMAHFDVVPVNPEEWNTEPFK-LTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLN--GKVIFAFTGDEEIGGAMA 142
|
...
gi 938318566 245 MEL 247
Cdd:PRK08554 143 MHI 145
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
212-474 |
8.32e-06 |
|
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: 48.11 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 212 LEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQ----------------GMELFVQRPEFH-ALRAGFaldegIANPTDAF 274
Cdd:TIGR01891 99 LGTAKLLKKLADLLEGTVRLIFQPAEEGGGGAtkmiedgvlddvdailGLHPDPSIPAGTvGLRPGT-----IMAAADKF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 275 TVFYserspwwvrvtsTGRPGHASRfmedtaaekLHKVVNSILAFREKeWQRLQ-----SNPHLKEGSVTsvnLTKLEGG 349
Cdd:TIGR01891 174 EVTI------------HGKGAHAAR---------PHLGRDALDAAAQL-VVALQqivsrNVDPSRPAVVS---VGIIEAG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 350 VAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGE--GVTLEFaqKWMH--PQVTPTDDSNPWWAAFSR-VCKDM 424
Cdd:TIGR01891 229 GAPNVIPDKASMSGTVRSLDPEVRDQIIDRIERIVEGAAAmyGAKVEL--NYDRglPAVTNDPALTQILKEVARhVVGPE 306
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 938318566 425 NLTLEPEIMPAATDNRYIRAVgVP-ALGFSP-MNRTPVLLHDHderlHEAVF 474
Cdd:TIGR01891 307 NVAEDPEVTMGSEDFAYYSQK-VPgAFFFLGiGNEGTGLSHPL----HHPRF 353
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
105-276 |
1.02e-05 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 47.97 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 105 LFrQYLRIRTVQPKPDYGA----AVAFFEETARQLGLGCQKVEvAPGYVVTVLTWPGTNPTLSSILLNSHTDVVPVFK-E 179
Cdd:PRK09104 23 LF-ALLRIPSISTDPAYAAdcrkAADWLVADLASLGFEASVRD-TPGHPMVVAHHEGPTGDAPHVLFYGHYDVQPVDPlD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 180 HWSHDPFE-AFKDSEG---YIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQGMELFVQRpefH 255
Cdd:PRK09104 101 LWESPPFEpRIKETPDgrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEESGS-PSLVPFLEA---N 176
|
170 180
....*....|....*....|....*.
gi 938318566 256 A--LRAGFAL--DEGIANP-TDAFTV 276
Cdd:PRK09104 177 AeeLKADVALvcDTGMWDReTPAITT 202
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
126-381 |
1.07e-05 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 47.70 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 126 AFFEETARQLGLGCQKVEVAPGYVVTVL-TWPGTNPtlSSILLNSHTDVVpvFKEHWSHDpfEAFKDSEGYIYARGAQDM 204
Cdd:PRK06133 64 ALLAERLKALGAKVERAPTPPSAGDMVVaTFKGTGK--RRIMLIAHMDTV--YLPGMLAK--QPFRIDGDRAYGPGIADD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 205 KCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHalRAGFALDEGiaNPTDAFTVFYSERSPW 284
Cdd:PRK06133 138 KGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGSPGSRELIAELAAQH--DVVFSCEPG--RAKDALTLATSGIATA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 285 WVRVTstGRPGHASrfmedtAAEKLHkvVNSILafrEKEWQRLQSNPHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFD 364
Cdd:PRK06133 214 LLEVK--GKASHAG------AAPELG--RNALY---ELAHQLLQLRDLGDPAKGTTLNWTVAKAGTNRNVIPASASAQAD 280
|
250
....*....|....*..
gi 938318566 365 FRVAPDVDFKAFEEQLQ 381
Cdd:PRK06133 281 VRYLDPAEFDRLEADLQ 297
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
164-266 |
1.10e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 47.83 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 164 SILLNSHTDVVPVFK-EHWSHDPFEA-FKDseGYIYARGAQDMKCVSIQYLEAVRRLkVEGHRFPRTIHMTFVPDEEVGG 241
Cdd:PRK06446 64 TLLIYNHYDVQPVDPlSEWKRDPFSAtIEN--GRIYARGASDNKGTLMARLFAIKHL-IDKHKLNVNVKFLYEGEEEIGS 140
|
90 100
....*....|....*....|....*
gi 938318566 242 hQGMELFVQRPEfHALRAGFALDEG 266
Cdd:PRK06446 141 -PNLEDFIEKNK-NKLKADSVIMEG 163
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
291-484 |
1.30e-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: 47.23 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 291 TGRPGHASrfMEDTAAEKLHKVVNSILAFRekewQRLQSNPHLKEGSVTSVnlTKLEGGVAYNVIPATMSASFDFRVAPD 370
Cdd:cd08660 178 KGKGGHAS--IPNNSIDPIAAAGQIISGLQ----SVVSRNISSLQNAVVSI--TRVQGGTAWNVIPDQAE*EGTVRAFTK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 371 VDFKAFEEQLQSWC--QAAGEGVTLEFaqKWMHPQVTPTDDSNPWWAAFSRVCKDM-NLTLEPEIMPAATDNRYIRAVgV 447
Cdd:cd08660 250 EARQAVPEH*RRVAegIAAGYGCQAEF--KWFPNGPSEVQNDGTLLNAFSKAAARLgYATVHAEQSPGSEDFALYQEK-I 326
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 938318566 448 PalGFSP---MNRTPVLLHDHDERLHEAVFLRGVDIYTRL 484
Cdd:cd08660 327 P--GFFVw*gTNGRTEEWHHPAFRLDEEALTVGAQIFAEL 364
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
157-245 |
1.80e-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: 47.34 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 157 GTNPTLSSILLNSHTDVVPV-------------------FKEHWSHDPFEAFKD--SEGYIYARGAQDMKCVSIQYLEAV 215
Cdd:cd05654 66 GKKPSKRTIILISHFDTVGIedygelkdiafdpdeltkaFSEYVEELDEEVREDllSGEWLFGRGTMDMKSGLAVHLALL 145
|
90 100 110
....*....|....*....|....*....|
gi 938318566 216 RRLKVEGHrFPRTIHMTFVPDEEVgGHQGM 245
Cdd:cd05654 146 EQASEDED-FDGNLLLMAVPDEEV-NSRGM 173
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
286-484 |
2.42e-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: 46.44 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 286 VRVTSTGRPGHASRfmedtaaekLHKVVNSILAFREKeWQRLQSNPHLKEGSVTS--VNLTKLEGGVAYNVIP--ATMSA 361
Cdd:cd03886 174 FEITVKGKGGHGAS---------PHLGVDPIVAAAQI-VLALQTVVSRELDPLEPavVTVGKFHAGTAFNVIPdtAVLEG 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 362 ---SFDFRVAPDVdFKAFEEQLQSWCQAAGEGVTLEfaqkwMHPQVTPTDDSNPWWAAFSRVCKDM---NLTLEPEIMPA 435
Cdd:cd03886 244 tirTFDPEVREAL-EARIKRLAEGIAAAYGATVELE-----YGYGYPAVINDPELTELVREAAKELlgeEAVVEPEPVMG 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 938318566 436 ATDNRYIrAVGVPA----LGFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRL 484
Cdd:cd03886 318 SEDFAYY-LEKVPGaffwLGAGEPDGENPGLHSPTFDFDEDALPIGAALLAEL 369
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
170-240 |
2.88e-05 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 46.37 E-value: 2.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 938318566 170 HTDVVPVfKEHWSHDPFEA-FKDseGYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVG 240
Cdd:PRK07318 87 HLDVVPA-GDGWDTDPYEPvIKD--GKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRFIVGTDEESG 155
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
132-297 |
7.02e-04 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 42.08 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 132 ARQLGLGCQKVEVAPGYV----VTVLTWPGTNPTLSSILLNSHTDVV-PVfkehwshDPFE--AFKDSEGYIYARGAQDM 204
Cdd:PRK07473 41 ARDMAIMGATIERIPGRQgfgdCVRARFPHPRQGEPGILIAGHMDTVhPV-------GTLEklPWRREGNKCYGPGILDM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 205 KCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFvqrpEFHALRAGFAL-------DEGIANPTDAFTVF 277
Cdd:PRK07473 114 KGGNYLALEAIRQLARAGITTPLPITVLFTPDEEVGTPSTRDLI----EAEAARNKYVLvpepgrpDNGVVTGRYAIARF 189
|
170 180
....*....|....*....|
gi 938318566 278 yserspwwvRVTSTGRPGHA 297
Cdd:PRK07473 190 ---------NLEATGRPSHA 200
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
107-251 |
1.45e-03 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 41.11 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 107 RQYLRIRTV----QPKPDYGAAVAF---FEETARQLGLGCQKVevapGYVVTVLTWPGTNPTLSSILlnSHTDVVPVFKE 179
Cdd:PRK06156 53 RELVAFPTVrvegVPQHENPEFIGFkklLKSLARDFGLDYRNV----DNRVLEIGLGGSGSDKVGIL--THADVVPANPE 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 938318566 180 HW-----SHDPFEAFKDSEgYIYARGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGhQGMELFVQR 251
Cdd:PRK06156 127 LWvldgtRLDPFKVTLVGD-RLYGRGTEDDKGAIVTALYAMKAIKDSGLPLARRIELLVYTTEETDG-DPLKYYLER 201
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
283-405 |
2.77e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 40.14 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 283 PWWVRVTSTGRPGHA-SRFMED------TAAEklhkvvnSILAFREKEWQrlqsnphLKEGSVTSV-NLTKLEGGVayNV 354
Cdd:PRK09290 215 QRRYRVTFTGEANHAgTTPMALrrdallAAAE-------IILAVERIAAA-------HGPDLVATVgRLEVKPNSV--NV 278
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 938318566 355 IPATMSASFDFRvAPDVDF-KAFEEQLQSWCQ--AAGEGVTLEFAQKWMHPQVT 405
Cdd:PRK09290 279 IPGEVTFTLDIR-HPDDAVlDALVAELRAAAEaiAARRGVEVEIELISRRPPVP 331
|
|
| PRK12890 |
PRK12890 |
allantoate amidohydrolase; Reviewed |
119-416 |
4.34e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 237248 [Multi-domain] Cd Length: 414 Bit Score: 39.50 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 119 PDYGAAVAFFEETARQLGLgcqKVEV-APGYVVtvLTWPGTNPTLSSILLNSHTDVVPvfkehwshdpfeafkdsEGyiy 197
Cdd:PRK12890 35 DEERAARALLAAWMRAAGL---EVRRdAAGNLF--GRLPGRDPDLPPLMTGSHLDTVP-----------------NG--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 198 arGAQDMKCVSIQYLEAVRRLKVEGHRFPRTIHMTFVPDEEV--------------GG--HQGMeLFVQRPEFHAL---- 257
Cdd:PRK12890 90 --GRYDGILGVLAGLEVVAALREAGIRPPHPLEVIAFTNEEGvrfgpsmigsralaGTldVEAV-LATRDDDGTTLaeal 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 258 -RAGFALD-----EGIANPTDAFTVFYSERSP------------------WWVRVTSTGRPGHAS--------------- 298
Cdd:PRK12890 167 rRIGGDPDalpgaLRPPGAVAAFLELHIEQGPvleaeglpigvvtaiqgiRRQAVTVEGEANHAGttpmdlrrdalvaaa 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 938318566 299 ---RFMEDTAAEKLHKVVNSIlafrekewQRLQSNPHlkegsvtsvnltkleggvAYNVIPATMSASFDFRvAPDVD-FK 374
Cdd:PRK12890 247 elvTAMERRARALLHDLVATV--------GRLDVEPN------------------AINVVPGRVVFTLDLR-SPDDAvLE 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 938318566 375 AFEEQLQSWCQ--AAGEGVTLEFAQKWmhpqVTPTDDSNPWWAA 416
Cdd:PRK12890 300 AAEAALLAELEaiAAARGVRIELERLS----RSEPVPCDPALVD 339
|
|
| |
