|
Name |
Accession |
Description |
Interval |
E-value |
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
53-488 |
0e+00 |
|
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: 564.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 53 EALKGAIQIPTVSFSH-----EESNTTALAEFGEYIRKAFPTVFhsSLVQHEVVAKYSHLFTIQGSDPSLQPYMLMAHID 127
Cdd:cd05674 2 ERLSGAVQIPTVSFDDmppidEDERWDAFYKFHDYLEKTFPLVH--KTLKVEVVNEYGLLYTWEGSDPSLKPLLLMAHQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 128 VVPAPEE---GWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGEKGAQKISA 204
Cdd:cd05674 80 VVPVNPEtedQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTIILAFGHDEEVGGERGAGAIAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 205 LLQAR-GVQ-LAFLVDEGSFILEGFIpnLEKPVAMISVTEKGALDLMLQVNMTPGHSSAPPKETSIGILSAAVSRLEQTP 282
Cdd:cd05674 160 LLLERyGVDgLAAILDEGGAVLEGVF--LGVPFALPGVAEKGYMDVEITVHTPGGHSSVPPKHTGIGILSEAVAALEANP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 283 MPNMFGGG-PLKKTMKLLANEFSFPINIVLRNLWLFHPI-----VSRIMERNPITNALVRTTTALTMFNAGIKVNVIPPL 356
Cdd:cd05674 238 FPPKLTPGnPYYGMLQCLAEHSPLPPRSLKSNLWLASPLlkallASELLSTSPLTRALLRTTQAVDIINGGVKINALPET 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 357 AQATINCRIHPSQTVHEVLELVKNTVADDRVQLHV-------------------LRSFEPLPISPSDDQAMGYQLLQETI 417
Cdd:cd05674 318 ATATVNHRIAPGSSVEEVLEHVKNLIADIAVKYGLglsafggdviystngtkllTSLLSPEPSPVSSTSSPVWQLLAGTI 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227908835 418 RSVF---PEVDIVVPGICIANTDTRHYANITNGMYRFNPLPLNPQDFSGVHGINEKVSVQNYQNQVKFIFEFIQ 488
Cdd:cd05674 398 RQVFeqfGEDLVVAPGIMTGNTDTRHYWNLTKNIYRFTPIRLNPEDLGRIHGVNERISIDDYLETVAFYYQLIQ 471
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
4-491 |
2.04e-179 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 512.57 E-value: 2.04e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 4 LLASLPAWAAVLLLFFATVsgstgpRSRENRGASRIPSQFSEEERVaikEALKGAIQIPTVS-FSHEESNTTALAEFGEY 82
Cdd:PRK08262 8 LLALLLLLAAVLAVRTFRF------KSRQIDVPAVAPVAVDEDAAA---ERLSEAIRFRTISnRDRAEDDAAAFDALHAH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 83 IRKAFPTVfHSSLvQHEVVAKYSHLFTIQGSDPSLQPYMLMAHIDVVPAP---EEGWEVPPFSGLERNGFIYGRGALDNK 159
Cdd:PRK08262 79 LEESYPAV-HAAL-EREVVGGHSLLYTWKGSDPSLKPIVLMAHQDVVPVApgtEGDWTHPPFSGVIADGYVWGRGALDDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 160 NSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGEkGAQKISALLQARGVQLAFLVDEGSFILEGFIPNLEKPVAMIS 239
Cdd:PRK08262 157 GSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVGGL-GARAIAELLKERGVRLAFVLDEGGAITEGVLPGVKKPVALIG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 240 VTEKGALDLMLQVNMTPGHSSAPPKETSIGILSAAVSRLEQTPMPNMFGGgPLKKTMKLLANEFSFPINIVLRNLWLFHP 319
Cdd:PRK08262 236 VAEKGYATLELTARATGGHSSMPPRQTAIGRLARALTRLEDNPLPMRLRG-PVAEMFDTLAPEMSFAQRVVLANLWLFEP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 320 IVSRIMERNPITNALVRTTTALTMFNAGIKVNVIPPLAQATINCRIHPSQTVHEVLELVKNTVADDRVQLHVLRS-FEPL 398
Cdd:PRK08262 315 LLLRVLAKSPETAAMLRTTTAPTMLKGSPKDNVLPQRATATVNFRILPGDSVESVLAHVRRAVADDRVEIEVLGGnSEPS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 399 PISPSDDQamGYQLLQETIRSVFPEVdIVVPGICIANTDTRHYANITNGMYRFNPLPLNPQDFSGVHGINEKVSVQNYQN 478
Cdd:PRK08262 395 PVSSTDSA--AYKLLAATIREVFPDV-VVAPYLVVGATDSRHYSGISDNVYRFSPLRLSPEDLARFHGTNERISVANYAR 471
|
490
....*....|...
gi 227908835 479 QVKFIFEFIQNAD 491
Cdd:PRK08262 472 MIRFYYRLIENAA 484
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
59-488 |
6.59e-68 |
|
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: 224.16 E-value: 6.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 59 IQIPTVSFSHEESNTTALAEF-GEYIRKA-FPTVFH---SSLVQHEVVAkyshlfTIQGSDPSLQPYMLMAHIDVVPAPE 133
Cdd:cd05675 8 IRIDTTNSGDGTGSETRAAEVlAARLAEAgIQTEIFvveSHPGRANLVA------RIGGTDPSAGPLLLLGHIDVVPADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 134 EGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGEKGAQKISALLQARGVQL 213
Cdd:cd05675 82 SDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDNHPELFDGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 214 AFLVDEGSfileGF-IPNLEKPVAM-ISVTEKGALDLMLQVNMTPGHSSAPPKETSIGILSAAVSRLEQTPMPNMFggGP 291
Cdd:cd05675 162 TFALNEGG----GGsLPVGKGRRLYpIQVAEKGIAWMKLTVRGRAGHGSRPTDDNAITRLAEALRRLGAHNFPVRL--TD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 292 LKKTMKLLAnEFSFPINIVL--RNLWLFHPIVSRIMERNPITNALVRTTTALTMFNAGIKVNVIPPLAQATINCRIHPSQ 369
Cdd:cd05675 236 ETAYFAQMA-ELAGGEGGALmlTAVPVLDPALAKLGPSAPLLNAMLRNTASPTMLDAGYATNVLPGRATAEVDCRILPGQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 370 TVHEVLELVKNTVADDRVQLHvLRSFEPLPISPSDDQAmgYQLLQETIRSVFPEVdIVVPGICIANTDTRHYANITNGMY 449
Cdd:cd05675 315 SEEEVLDTLDKLLGDPDVSVE-AVHLEPATESPLDSPL--VDAMEAAVQAVDPGA-PVVPYMSPGGTDAKYFRRLGIPGY 390
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 227908835 450 RFNPLPLNPQ--DFSGVHGINEKVSVQNYQNQVKFIFEFIQ 488
Cdd:cd05675 391 GFAPLFLPPEldYTGLFHGVDERVPVESLYFGVRFLDRLVK 431
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
9-488 |
2.16e-60 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 205.62 E-value: 2.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 9 PAWAAVLLLFFATVSGSTGPRSrenrgasriPSQFSEEERVAIKEALKGAIQIPTVsfsHEESNTTALAE-FGEYIRKA- 86
Cdd:PRK09133 6 RALALALALLAAAAATGAAAAA---------APAAPTADQQAARDLYKELIEINTT---ASTGSTTPAAEaMAARLKAAg 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 87 FP----TVFHSSLVQHEVVAkyshlfTIQGSDPSlQPYMLMAHIDVVPAPEEGWEVPPFSGLERNGFIYGRGALDNKNSV 162
Cdd:PRK09133 74 FAdadiEVTGPYPRKGNLVA------RLRGTDPK-KPILLLAHMDVVEAKREDWTRDPFKLVEENGYFYGRGTSDDKADA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 163 MAILHALELLLIRNYSPKRSFFIALGHDEEVSGEKG----AQKISALLQArgvqlAFLVDEGSfilEGFIPNLEKPVAM- 237
Cdd:PRK09133 147 AIWVATLIRLKREGFKPKRDIILALTGDEEGTPMNGvawlAENHRDLIDA-----EFALNEGG---GGTLDEDGKPVLLt 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 238 ISVTEKGALDLMLQVNMTPGHSSAPPKETSIGILSAAVSRLEQTPMPNMFG--------------GGPLKKTMKLLANEF 303
Cdd:PRK09133 219 VQAGEKTYADFRLEVTNPGGHSSRPTKDNAIYRLAAALSRLAAYRFPVMLNdvtrayfkqsaaieTGPLAAAMRAFAANP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 304 SFPINIvlrnlwlfhpivsRIMERNPITNALVRTTTALTMFNAGIKVNVIPPLAQATINCRIHPSQTVHEVLELVKNTVA 383
Cdd:PRK09133 299 ADEAAI-------------ALLSADPSYNAMLRTTCVATMLEGGHAENALPQRATANVNCRIFPGDTIEAVRATLKQVVA 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 384 DDRVQLHVLRSFEPLPISPSDDQAMGyqllqeTIRSV----FPEVdIVVPGICIANTDTRHYANITNGMYRFNPLPLNPQ 459
Cdd:PRK09133 366 DPAIKITRIGDPSPSPASPLRPDIMK------AVEKLtaamWPGV-PVIPSMSTGATDGRYLRAAGIPTYGVSGLFGDPD 438
|
490 500
....*....|....*....|....*....
gi 227908835 460 DfSGVHGINEKVSVQNYQNQVKFIFEFIQ 488
Cdd:PRK09133 439 D-TFAHGLNERIPVASFYEGRDFLYELVK 466
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
45-489 |
2.35e-53 |
|
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: 184.70 E-value: 2.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 45 EEERVAIKEALKGAIQIPTVSFSHEEsnttALAEFGEYIRKA-FPTVfhsslVQHEVVAKYSHLFTIQGSDPSlQPYMLM 123
Cdd:COG0624 8 DAHLDEALELLRELVRIPSVSGEEAA----AAELLAELLEALgFEVE-----RLEVPPGRPNLVARRPGDGGG-PTLLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 124 AHIDVVPA-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVsGEKGAQKI 202
Cdd:COG0624 78 GHLDVVPPgDLELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEV-GSPGARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 203 SALLQARGVQLAFLVDEGSfilegfipnlekPVAMISVTEKGALDLMLQVNMTPGHSSAPPKETS-IGILSAAVSRLEQT 281
Cdd:COG0624 157 VEELAEGLKADAAIVGEPT------------GVPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNaIEALARALAALRDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 282 PMPNmfgggplkktmkllanefsfpinivlrnlwlfhpivsrimERNPitnALVRTTTALTMFNAGIKVNVIPPLAQATI 361
Cdd:COG0624 225 EFDG----------------------------------------RADP---LFGRTTLNVTGIEGGTAVNVIPDEAEAKV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 362 NCRIHPSQTVHEVLELVKNTVA----DDRVQLHVL-RSFEPLPISPSDDqamGYQLLQETIRSVFPEVdiVVPGICIANT 436
Cdd:COG0624 262 DIRLLPGEDPEEVLAALRALLAaaapGVEVEVEVLgDGRPPFETPPDSP---LVAAARAAIREVTGKE--PVLSGVGGGT 336
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 227908835 437 DTRHYANITNG-MYRFNPLplnpqDFSGVHGINEKVSVQNYQNQVKFIFEFIQN 489
Cdd:COG0624 337 DARFFAEALGIpTVVFGPG-----DGAGAHAPDEYVELDDLEKGARVLARLLER 385
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
121-489 |
3.82e-40 |
|
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: 147.11 E-value: 3.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 121 MLMAHIDVVPaPEEGWEVPpFSgLERNGFIYGRGALDNKNSVMAILHALELLLiRNYSPKRSFFIALGHDEEvSGEKGAQ 200
Cdd:pfam01546 1 LLRGHMDVVP-DEETWGWP-FK-STEDGKLYGRGHDDMKGGLLAALEALRALK-EEGLKKGTVKLLFQPDEE-GGMGGAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 201 KISALLQARGVQLAFLVdeGSFILEGFIPNlEKPVAMISVTEKGALDLMLQVNMTPGHSSAPPK-ETSIGILSAAVSRLE 279
Cdd:pfam01546 76 ALIEDGLLEREKVDAVF--GLHIGEPTLLE-GGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLgVNAIVAAARLILALQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 280 QtpmpnmfgggplkktmkllanefsfpinIVLRNLWLFHPivsrimernpitnaLVRTTTALTMFNAGikVNVIPPLAQA 359
Cdd:pfam01546 153 D----------------------------IVSRNVDPLDP--------------AVVTVGNITGIPGG--VNVIPGEAEL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 360 TINCRIHPSQTVHEVLELVKN---TVADDRVQLHVLRSFEPLPISPSDDQAMgYQLLQETIRSVFPEVDIVVPGICIANT 436
Cdd:pfam01546 189 KGDIRLLPGEDLEELEERIREileAIAAAYGVKVEVEYVEGGAPPLVNDSPL-VAALREAAKELFGLKVELIVSGSMGGT 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 227908835 437 DTRHYAN-ITNGMYRFNPlplnpqDFSGVHGINEKVSVQNYQNQVKFIFEFIQN 489
Cdd:pfam01546 268 DAAFFLLgVPPTVVFFGP------GSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
88-473 |
6.07e-37 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 141.14 E-value: 6.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 88 PTVFHSSLVQHEVVAKyshlftIQGSDPSLQPYMLMAHIDVVPAPEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILH 167
Cdd:PRK07906 42 PTYLESAPGRANVVAR------LPGADPSRPALLVHGHLDVVPAEAADWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 168 ALELLLIRNYSPKRSFFIALGHDEEVSGEKGAQkisallqargvqlaFLVDE---------------GSFILEgfIPNlE 232
Cdd:PRK07906 116 VVRHLARTGRRPPRDLVFAFVADEEAGGTYGAH--------------WLVDNhpelfegvteaisevGGFSLT--VPG-R 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 233 KPVAMISVTEKGALDLMLQVNMTPGHSSAPPKETSIGILSAAVSRLEQ-------TPMPNMFgggpLKKTMKLLANEFSf 305
Cdd:PRK07906 179 DRLYLIETAEKGLAWMRLTARGRAGHGSMVNDDNAVTRLAEAVARIGRhrwplvlTPTVRAF----LDGVAELTGLEFD- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 306 PINIvlrnlwlfHPIVSRIMERNPITNALVRTTTALTMFNAGIKVNVIPPLAQATINCRIHPSQTvHEVLELVKNTVADD 385
Cdd:PRK07906 254 PDDP--------DALLAKLGPAARMVGATLRNTANPTMLKAGYKVNVIPGTAEAVVDGRFLPGRE-EEFLATVDELLGPD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 386 --RVQLHVLRSFEpLPISPSDDQAMGYQLLQETirsvfPEVdIVVPGICIANTDTRHYA--NITNgmYRFNPLPLNPQ-D 460
Cdd:PRK07906 325 veREWVHRDPALE-TPFDGPLVDAMNAALLAED-----PGA-RVVPYMLSGGTDAKAFSrlGIRC--YGFAPLRLPPDlD 395
|
410
....*....|....
gi 227908835 461 FSG-VHGINEKVSV 473
Cdd:PRK07906 396 FAAlFHGVDERVPV 409
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
53-481 |
7.33e-32 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 125.97 E-value: 7.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 53 EALKGAIQIPTVSFSHEESNTTA------LAEFGEYIRKAFPTVFHSSLVQHEVVAKYSHlftiqGSDPSLqpyMLMAHI 126
Cdd:TIGR01910 2 ELLKDLISIPSVNPPGGNEETIAnyikdlLREFGFSTDVIEITDDRLKVLGKVVVKEPGN-----GNEKSL---IFNGHY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 127 DVVPA-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEvSGEKGAQKisaL 205
Cdd:TIGR01910 74 DVVPAgDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEE-SGEAGTLY---L 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 206 LQARGVQLA--FLVDEGSFILEGFIpnlekpvamisvTEKGALDLMLQVNMTPGHSSappketsigilsaavsrleqtpM 283
Cdd:TIGR01910 150 LQRGYFKDAdgVLIPEPSGGDNIVI------------GHKGSIWFKLRVKGKQAHAS----------------------F 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 284 PNmFGGGPLKKTMKLLA--NEFsfpinivlrnlwlfhpiVSRIMERNPITNALVRTTTALTMFNAGIKVNVIPPLAQATI 361
Cdd:TIGR01910 196 PQ-FGVNAIMKLAKLITelNEL-----------------EEHIYARNSYGFIPGPITFNPGVIKGGDWVNSVPDYCEFSI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 362 NCRIHPSQTVHEVLELVKNTVADDRVQLHVLRSFEP-LPIS---PSDDQAMGYQLLQETIRSVFPE--VDIVVPGIcian 435
Cdd:TIGR01910 258 DVRIIPEENLDEVKQIIEDVVKALSKSDGWLYENEPvVKWSgpnETPPDSRLVKALEAIIKKVRGIepEVLVSTGG---- 333
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 227908835 436 TDTRHYANitNGmyrFNPLPLNPQDFSGVHGINEKVSVQNYQNQVK 481
Cdd:TIGR01910 334 TDARFLRK--AG---IPSIVYGPGDLETAHQVNEYISIKNLVESTK 374
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
55-487 |
5.32e-28 |
|
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: 114.70 E-value: 5.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 55 LKGAIQIPTVSfSHEESNTTALAEFGEYIRKAFPTVFHSSLVQheVVAkyshlfTIQGSDPSlqPYMLMAHIDVVPA-PE 133
Cdd:cd08659 3 LQDLVQIPSVN-PPEAEVAEYLAELLAKRGYGIESTIVEGRGN--LVA------TVGGGDGP--VLLLNGHIDTVPPgDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 134 EGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVsGEKGAQKISALLQARGVqL 213
Cdd:cd08659 72 DKWSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEV-GSDGARALLEAGYADRL-D 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 214 AFLVDEgsfilegfiPNLEKPVamisVTEKGALDLMLQVNMTPGHSSAPPKETS-IGILSAAVSRLEqtpmpnmfgggpl 292
Cdd:cd08659 150 ALIVGE---------PTGLDVV----YAHKGSLWLRVTVHGKAAHSSMPELGVNaIYALADFLAELR------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 293 kktmkllanEFSFPInivlrnlwlfhpivsrimERNPItnaLVRTTTALTMFNAGIKVNVIPPLAQATINCRIHPSQTVH 372
Cdd:cd08659 204 ---------TLFEEL------------------PAHPL---LGPPTLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 373 EVLELVKNTVADDRVQLHVLRSFEPLPISPSDDQAMGYQLLQETIRSVFPEVDIVVPGiciANTDTRHYAnitnGMYRFN 452
Cdd:cd08659 254 GVIARLEAILEEHEAKLTVEVSLDGDPPFFTDPDHPLVQALQAAARALGGDPVVRPFT---GTTDASYFA----KDLGFP 326
|
410 420 430
....*....|....*....|....*....|....*
gi 227908835 453 PLPLNPQDFSGVHGINEKVSVQNYQNQVKFIFEFI 487
Cdd:cd08659 327 VVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
98-439 |
9.99e-28 |
|
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: 114.29 E-value: 9.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 98 HEVV-AKYSHLFTIQGSDPSLQPYMLMAHIDVVPAPEEGWEVPPFSG-LERNGFIYGRGALDNKNSVMAILHALELLLIR 175
Cdd:cd05646 44 IEVVpGKPVVVLTWEGSNPELPSILLNSHTDVVPVFEEKWTHDPFSAhKDEDGNIYARGAQDMKCVGIQYLEAIRRLKAS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 176 NYSPKRSFFIALGHDEEVSGEKGAQKISALLQARGVQLAFLVDEGsfilegfIPNlEKPVAMISVTEKGALDLMLQVNMT 255
Cdd:cd05646 124 GFKPKRTIHLSFVPDEEIGGHDGMEKFVKTEEFKKLNVGFALDEG-------LAS-PTEEYRVFYGERSPWWVVITAPGT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 256 PGHSSAPPKETsigilsaAVSRLEQTpmpnmfgggpLKKTMKLLANEFSFpinivlrnlwlfhpivsriMERNP-ITNAL 334
Cdd:cd05646 196 PGHGSKLLENT-------AGEKLRKV----------IESIMEFRESQKQR-------------------LKSNPnLTLGD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 335 VrTTTALTMFNAGIKVNVIPPLAQATINCRIHPSQTVHEVLELVKNTVAD--DRVQLHVLRSFEPLPISPSDDQAMGYQL 412
Cdd:cd05646 240 V-TTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEagRGVTYEFEQKSPEKDPTSLDDSNPWWAA 318
|
330 340
....*....|....*....|....*...
gi 227908835 413 LQETIRsvfpEVDI-VVPGICIANTDTR 439
Cdd:cd05646 319 FKKAVK----EMGLkLKPEIFPAATDSR 342
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
44-488 |
3.17e-23 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 101.61 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 44 SEEERVAIKEALKGAIQIPTVSFSHEEsnttaLAEFGEYIRKAFPTV-FHSSLVQ---HEVVAKYSHLFTIQGSDPSLQP 119
Cdd:PRK08651 1 VEAMMFDIVEFLKDLIKIPTVNPPGEN-----YEEIAEFLRDTLEELgFSTEIIEvpnEYVKKHDGPRPNLIARRGSGNP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 120 Y-MLMAHIDVVPaPEEGWEV-PPFSGLERNGFIYGRGALDNKNSVMAILHALELL-LIRNYSPKrsffIALGHDEEVsGE 196
Cdd:PRK08651 76 HlHFNGHYDVVP-PGEGWSVnVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLdPAGDGNIE----LAIVPDEET-GG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 197 KGAqkisallqargvqlAFLVDEGSFILEGFIPNLEKPVAMISVTEKGALDLMLQVNMTPGHSSAPpketSIGI-----L 271
Cdd:PRK08651 150 TGT--------------GYLVEEGKVTPDYVIVGEPSGLDNICIGHRGLVWGVVKVYGKQAHASTP----WLGInafeaA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 272 SAAVSRLEQtpmpnmfgggplKKTMKLLANEFSFPINivlrnlwlfhPIVSRIMERNPItnalvrtttaltmfNAGIKVN 351
Cdd:PRK08651 212 AKIAERLKS------------SLSTIKSKYEYDDERG----------AKPTVTLGGPTV--------------EGGTKTN 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 352 VIPPLAQATINCRIHPSQTVHEVLELVKNTVADDRVQLHVLRSFEPLPISP---SDDQAMGYQLLQETIRSVFPEVDIVV 428
Cdd:PRK08651 256 IVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFEITPFSEafvTDPDSELVKALREAIREVLGVEPKKT 335
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227908835 429 pgICIANTDTRHYANITNGMYRFNPLPLnpqdfsGV-HGINEKVSVQNYQNQVKFIFEFIQ 488
Cdd:PRK08651 336 --ISLGGTDARFFGAKGIPTVVYGPGEL------ELaHAPDEYVEVKDVEKAAKVYEEVLK 388
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
107-368 |
1.03e-22 |
|
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: 99.87 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 107 LFTIQGSDPSLQPYMLMAHIDVVPAPEEGWEVPPFSG-LERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFI 185
Cdd:TIGR01880 61 VLTWPGSNPELPSILLNSHTDVVPVFREHWTHPPFSAfKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 186 ALGHDEEVSGEKGAQKISALLQARGVQLAFLVDEGsfilegfIPNlekPVAMISV--TEKGALDLMLQVNMTPGHSSapp 263
Cdd:TIGR01880 141 SFVPDEEIGGHDGMEKFAKTDEFKALNLGFALDEG-------LAS---PDDVYRVfyAERVPWWVVVTAPGNPGHGS--- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 264 ketsigilsaavSRLEQTPMPNMFGGgpLKKTMKLLANEFSFpinivlrnlwlfhpivsriMERNP-ITNALVrTTTALT 342
Cdd:TIGR01880 208 ------------KLMENTAMEKLEKS--VESIRRFRESQFQL-------------------LQSNPdLAIGDV-TSVNLT 253
|
250 260
....*....|....*....|....*.
gi 227908835 343 MFNAGIKVNVIPPLAQATINCRIHPS 368
Cdd:TIGR01880 254 KLKGGVQSNVIPSEAEAGFDIRLAPS 279
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
107-291 |
4.35e-21 |
|
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: 90.95 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 107 LFTIQGSDPSLQPYMLMAHIDVVPAPEEGWEVPPFSGL-ERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFI 185
Cdd:cd18669 2 VIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDtVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 186 ALGHDEEVSGEKGAQKISALLQAR--GVQLAFLVDEGSFILEGFIPNLEKPVAMISVTEKgaldlmlqVNMTPGHSSAPP 263
Cdd:cd18669 82 AFTPDEEVGSGAGKGLLSKDALEEdlKVDYLFVGDATPAPQKGVGIRTPLVDALSEAARK--------VFGKPQHAEGTG 153
|
170 180
....*....|....*....|....*...
gi 227908835 264 KETSIGILSAAvsrleQTPMPNMFGGGP 291
Cdd:cd18669 154 GGTDGRYLQEL-----GIPGVTLGAGGG 176
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
53-489 |
4.99e-21 |
|
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: 95.48 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 53 EALKGAIQIPTVSFSHEESNTTALAeFGEYIRKAFPTV--FHSSlvQHEVVakYSHLFTiqGSDPSLQPYmlmAHIDVVP 130
Cdd:cd05681 3 EDLRDLLKIPSVSAQGRGIPETADF-LKEFLRRLGAEVeiFETD--GNPIV--YAEFNS--GDAKTLLFY---NHYDVQP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 131 A-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALE-LLLIRNYSPKRSFFIALGhDEEVSG---EKGAQKISAL 205
Cdd:cd05681 73 AePLELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRaLLQHLGELPVNIKFLVEG-EEEVGSpnlEKFVAEHADL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 206 LQARGVqlaflvdegsfILE-GFIPNLEKPvaMISVTEKGALDLMLQVNMTPG--HSS-APPKETSIGILSAAVSRL--- 278
Cdd:cd05681 152 LKADGC-----------IWEgGGKNPKGRP--QISLGVKGIVYVELRVKTADFdlHSSyGAIVENPAWRLVQALNSLrde 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 279 -EQTPMPNMFGG-GPLKKTMKLLANEFSFPINIVLRNLWLFHPIVSRIMERnpitnaLVRTTTALTM----FNAG----I 348
Cdd:cd05681 219 dGRVLIPGFYDDvRPLSEAERALIDTYDFDPEELRKTYGLKRPLQVEGKDP------LRALFTEPTCningIYSGytgeG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 349 KVNVIPPLAQATINCRIHPSQTVHEVLELVKNTVAD---DRVQLHVLRSFEPLPISPSDDQAmgyQLLQETIRSVFPEVD 425
Cdd:cd05681 293 SKTILPSEAFAKLDFRLVPDQDPAKILSLLRKHLDKngfDDIEIHDLLGEKPFRTDPDAPFV---QAVIESAKEVYGQDP 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 227908835 426 IVVPGicIANTDTRHYanitngMYRFNPLPLNP----QDFSGVHGINEKVSVQNYQNQVKFIFEFIQN 489
Cdd:cd05681 370 IVLPN--SAGTGPMYP------FYDALEVPVVAigvgNAGSNAHAPNENIRIADYYKGIEHTEELLRN 429
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
54-481 |
1.32e-20 |
|
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: 93.22 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 54 ALKGAIQIPTVSFSHeeSNTTALAEFGEYIRKA--FPTVFHSSlvQHEVVAKYSHLFTIQGSdPSLqpyMLMAHIDVVPA 131
Cdd:cd08011 3 LLQELVQIPSPNPPG--DNTSAIAAYIKLLLEDlgYPVELHEP--PEEIYGVVSNIVGGRKG-KRL---LFNGHYDVVPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 132 PE-EGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGEKGAQkisallqarg 210
Cdd:cd08011 75 GDgEGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTK---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 211 vqlaFLVDEGSFILEGFIPNLEKPVAMISVTEKGALDLMLQVNMTPGHSSAPPK-ETSIGILSAAVSRLeqtpmpnmfgg 289
Cdd:cd08011 145 ----YLLEKVRIKPNDVLIGEPSGSDNIRIGEKGLVWVIIEITGKPAHGSLPHRgESAVKAAMKLIERL----------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 290 GPLKKTMkllanefsfpinivlrnlwlfhpivsrimerNPITNalvrtttaltmfNAGIKVNVIPPLAQATINCRIHPSQ 369
Cdd:cd08011 210 YELEKTV-------------------------------NPGVI------------KGGVKVNLVPDYCEFSVDIRLPPGI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 370 TVHEVLELVKNTVAD-DRVQLHVLRSFEPLPISPsdDQAMgYQLLQETIRSVFPEVDIVVpgICIANTDTRHY--ANITN 446
Cdd:cd08011 247 STDEVLSRIIDHLDSiEEVSFEIKSFYSPTVSNP--DSEI-VKKTEEAITEVLGIRPKEV--ISVGASDARFYrnAGIPA 321
|
410 420 430
....*....|....*....|....*....|....*
gi 227908835 447 GMYrfnplplNPQDFSGVHGINEKVSVQNYQNQVK 481
Cdd:cd08011 322 IVY-------GPGRLGQMHAPNEYVEIDELIKVIK 349
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
111-243 |
7.00e-20 |
|
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: 87.48 E-value: 7.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 111 QGSDPSLQPYMLMAHIDVVPAPEEGWEVPPFSGL-ERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGH 189
Cdd:cd03873 6 LGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDtEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTA 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 227908835 190 DEEVSGEKGAQKISALLQAR--GVQLAFLVDEGSFILEGFIPNLEKPV--AMISVTEK 243
Cdd:cd03873 86 DEEVGSGGGKGLLSKFLLAEdlKVDAAFVIDATAGPILQKGVVIRNPLvdALRKAARE 143
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
52-489 |
1.09e-18 |
|
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: 88.15 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 52 KEALKGAIQIPTVSfsheesnttALAEFGEYIRKAfptvfhsslvqHEVVAKY--SHLFTIQGSDPSLQPYMLMA----- 124
Cdd:cd03893 1 LQTLAELVAIPSVS---------AQPDRREELRRA-----------AEWLADLlrRLGFTVEIVDTSNGAPVVFAefpga 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 125 ----------HIDVVPA-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKR--SFFIalghde 191
Cdd:cd03893 61 pgaptvllygHYDVQPAgDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVnvKFII------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 192 EVSGEKGAQKISALLQAR--GVQLAFLVdegsfILEGFIPNLEKPVamISVTEKGALDLMLQVNMT--PGHSS--APPKE 265
Cdd:cd03893 135 EGEEESGSPSLDQLVEAHrdLLAADAIV-----ISDSTWVGQEQPT--LTYGLRGNANFDVEVKGLdhDLHSGlyGGVVP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 266 TSIGILSAAVSRLE----QTPMPNMF--GGGPLKKTMKLLA---NEFSFPINIVLrnlwlfhPIVSRIMERNPITnalvr 336
Cdd:cd03893 208 DPMTALAQLLASLRdetgRILVPGLYdaVRELPEEEFRLDAgvlEEVEIIGGTTG-------SVAERLWTRPALT----- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 337 TTTALTMFNAGIKVNVIPPLAQATINCRIHPSQTVHEVLELV-----KNTVADDRVQLHVLRSFEPLPISPSDDQamgYQ 411
Cdd:cd03893 276 VLGIDGGFPGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLeahleKHAPSGAKVTVSYVEGGMPWRSDPSDPA---YQ 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 227908835 412 LLQETIRSVFP-EVDIVVPGICIANTDTrhYANITNGMYRFNPLpLNPQDfsGVHGINEKVSVQNYQNQVKFIFEFIQN 489
Cdd:cd03893 353 AAKDALRTAYGvEPPLTREGGSIPFISV--LQEFPQAPVLLIGV-GDPDD--NAHSPNESLRLGNYKEGTQAEAALLYS 426
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
53-405 |
1.31e-18 |
|
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: 87.26 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 53 EALKGAIQIPTVSFsheESNttalAEFGEYIRKAFPTV-FHSSLVQHEVVAKYSHLFTIqgsDPSLQP-YMLMAHIDVVP 130
Cdd:cd03894 1 ELLARLVAFDTVSR---NSN----LALIEYVADYLAALgVKSRRVPVPEGGKANLLATL---GPGGEGgLLLSGHTDVVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 131 APEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNysPKRSFFIALGHDEEVsGEKGAQKISALLQARG 210
Cdd:cd03894 71 VDGQKWSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAK--LRKPLHLAFSYDEEV-GCLGVRHLIAALAARG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 211 VQlaflvDEGSFILEgfiPNLEKPVamisVTEKGALDLMLQVNMTPGHSSAPPKETS-IGILSAAVSRLEQtpmpnmfgg 289
Cdd:cd03894 148 GR-----PDAAIVGE---PTSLQPV----VAHKGIASYRIRVRGRAAHSSLPPLGVNaIEAAARLIGKLRE--------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 290 gplkktmklLANEFsfpinivlrnlwlfhpivsRIMERNP---ITNalvrTTTALTMFNAGIKVNVIPPLAQATINCRIH 366
Cdd:cd03894 207 ---------LADRL-------------------APGLRDPpfdPPY----PTLNVGLIHGGNAVNIVPAECEFEFEFRPL 254
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 227908835 367 PSQT---VHEVLE-LVKNTVADDRVQLHVLRSFEPLPISPSDD 405
Cdd:cd03894 255 PGEDpeaIDARLRdYAEALLEFPEAGIEVEPLFEVPGLETDED 297
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
50-261 |
1.52e-18 |
|
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: 87.82 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 50 AIKEALKGAIQIPTVsfsHEESNTTALAEFGEYIRKA---FPTVFHSSLVQHEVVAKYSHLFTIQGSDPSLQpymLMAHI 126
Cdd:TIGR01887 3 EILEDLKELIAIDSV---EDLEKAKEGAPFGEGPRKAldkFLEIAKRDGFTTENVDNYAGYIEYGQGEEVLG---ILGHL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 127 DVVPApEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEvSGekgaqkisall 206
Cdd:TIGR01887 77 DVVPA-GDGWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEE-SG----------- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227908835 207 qARGVQLAFLVDEGSFIleGFIPNLEKPVAM---------ISVTEKGALDLMLQV-------NMTPGHSSA 261
Cdd:TIGR01887 144 -WKCIDYYFEHEEMPDI--GFTPDAEFPIIYgekgittleIKFKDDTEGDVVLESfkageayNMVPDHATA 211
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
122-420 |
4.40e-18 |
|
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: 85.97 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 122 LMAHIDVVPAPEEG-WEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGEKGaq 200
Cdd:cd05650 74 IISHLDTVPPGDLSlWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEYG-- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 201 kISALLQARGVqlafLVDEGSFIlegfIPNLEKPV-AMISVTEKGALDLMLQVNMTPGHSSAPpkETSIGILSAA---VS 276
Cdd:cd05650 152 -IQYLLNKFDL----FKKDDLII----VPDFGTEDgEFIEIAEKSILWIKVNVKGKQCHASTP--ENGINAFVAAsnfAL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 277 RLEQtpmpnmfgggplkktmkLLANEFSFPINIVLRNLWLFHPIvsrIMERNpITNalvrtttaltmfnagikVNVIPPL 356
Cdd:cd05650 221 ELDE-----------------LLHEKFDEKDDLFNPPYSTFEPT---KKEAN-VPN-----------------VNTIPGY 262
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 357 AQATINCRIHPSQTVHEVLELVKNTVADD------RVQLHVLRSFEPLPISPSDDQAMgyQLLQETIRSV 420
Cdd:cd05650 263 DVFYFDCRVLPTYKLDEVLKFVNKIISDFensygaGITYEIVQKEQAPPATPEDSEIV--VRLSKAIKKV 330
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
124-196 |
7.86e-18 |
|
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: 85.76 E-value: 7.86e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227908835 124 AHIDVVPApEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGE 196
Cdd:cd03888 78 GHLDVVPA-GEGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGWK 149
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
125-384 |
1.09e-17 |
|
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349886 [Multi-domain] Cd Length: 366 Bit Score: 84.48 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 125 HIDVVPA-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGEKGAQKIS 203
Cdd:cd03891 62 HTDVVPPgDLEGWSSDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 204 ALLQARGVQLAF-LVDEGSfilegfipNLEKPVAMISVTEKGALDLMLQVNMTPGHSSAPPK-ETSIGILSAAVSRLEQT 281
Cdd:cd03891 142 EWLKARGEKIDYcIVGEPT--------SEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLaDNPIHLLAPILAELTAT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 282 PMPNmfgggplkktmkllANEFsfpinivlrnlwlFHPivsrimernpitnalvrTTTALTMFNAGIKV-NVIPPLAQAT 360
Cdd:cd03891 214 VLDE--------------GNEF-------------FPP-----------------SSLQITNIDVGNGAtNVIPGELKAK 249
|
250 260
....*....|....*....|....
gi 227908835 361 INCRIHPSQTVHEVLELVKNTVAD 384
Cdd:cd03891 250 FNIRFNDEHTGESLKARIEAILDK 273
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
125-477 |
1.02e-15 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 78.61 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 125 HIDVVPA-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGEKGAQKIS 203
Cdd:TIGR01246 63 HTDVVPAgPEEQWSSPPFEPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 204 ALLQARGVQLAF-LVDEgsfilegfiPNLEKPVA-MISVTEKGALDLMLQVNMTPGHSSAPPKETSigilsaavsrleqt 281
Cdd:TIGR01246 143 ETLMARDELIDYcIVGE---------PSSVKKLGdVIKNGRRGSITGNLTIKGIQGHVAYPHLANN-------------- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 282 pmpnmfgggPLKKTMKLLA----------NEFSFPINIVLRNLwlfhpivsrimernpitnalvrtttaltmfNAGIKV- 350
Cdd:TIGR01246 200 ---------PIHKAAPALAeltaikwdegNEFFPPTSLQITNI------------------------------HAGTGAn 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 351 NVIPPLAQATINCRIHPSQTVHEVLELVKNTVADDRVQ--LHVLRSFEPLPISPSDdqamgyqlLQETIRSVFPEVDIVV 428
Cdd:TIGR01246 241 NVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDydLEWSLSGEPFLTNDGK--------LIDKAREAIEETNGIK 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 227908835 429 PgicIANT-----DTRHYANITNGMYRFNPLPlnpqdfSGVHGINEKVSVQNYQ 477
Cdd:TIGR01246 313 P---ELSTgggtsDGRFIALMGAEVVEFGPVN------ATIHKVNECVSIEDLE 357
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
53-382 |
3.67e-15 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349902 [Multi-domain] Cd Length: 341 Bit Score: 76.58 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 53 EALKGAIQIPtvSFSHEESNTTALAEfgEYIRKAfptVFHSSLVQHEVVAKYSHLftiqgsDPSLQPYMLMAHIDVVPaP 132
Cdd:cd05651 4 ELLKSLIATP--SFSREEHKTADLIE--NYLEQK---GIPFKRKGNNVWAENGHF------DEGKPTLLLNSHHDTVK-P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 133 EEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALeLLLIRNYSPKRSFFIALGHDEEVSGEKGaqkISALLQARG-V 211
Cdd:cd05651 70 NAGWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATF-LHLYSEGPLNYNLIYAASAEEEISGKNG---IESLLPHLPpL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 212 QLAfLVDEgsfilegfiPNLEKPvamiSVTEKGALDLMLQVNMTPGHSSAPPKETSIGILSAAVSRLEqtpmpnmfgggp 291
Cdd:cd05651 146 DLA-IVGE---------PTEMQP----AIAEKGLLVLDCTARGKAGHAARNEGDNAIYKALDDIQWLR------------ 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 292 lkktmkllanEFSFPinivlrnlwlfhpivsrimernPITNALVRTTTALTMFNAGIKVNVIPPLAQATINCRIHPSQTV 371
Cdd:cd05651 200 ----------DFRFD----------------------KVSPLLGPVKMTVTQINAGTQHNVVPDSCTFVVDIRTTEAYTN 247
|
330
....*....|.
gi 227908835 372 HEVLELVKNTV 382
Cdd:cd05651 248 EEIFEIIRGNL 258
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
100-487 |
1.84e-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 have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 75.04 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 100 VVAKYshlftiQGSDPSLQPYMLMAHIDVVPA-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLlirnys 178
Cdd:cd03895 63 VVGTH------RPRGETGRSLILNGHIDVVPEgPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDAL------ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 179 pkRSFFIALGHD-------EEVSGEKGAqkISALLQARGVQLAflvdegsfilegFIPNLEKPvaMISVTEKGALDLMLQ 251
Cdd:cd03895 131 --RAAGLQPAADvhfqsvvEEECTGNGA--LAALMRGYRADAA------------LIPEPTEL--KLVRAQVGVIWFRVK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 252 VNMTPGHssappketsigilsaaVSRLEqtpmpnmFGGGPLKKTMKLLAnefsfpiniVLRNL---W----LFHPIVSRI 324
Cdd:cd03895 193 VRGTPAH----------------VAEAS-------EGVNAIEKAMHLIQ---------ALQELereWnarkKSHPHFSDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 325 meRNPITnalvrtttaltmFNAG-IK----VNVIPplAQATINCRIH--PSQTVHEVLELVKNTVADDRVQLHVLR---- 393
Cdd:cd03895 241 --PHPIN------------FNIGkIEggdwPSSVP--AWCVLDCRIGiyPGESPEEARREIEECVADAAATDPWLSnhpp 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 394 -------SFEPLPISPSDDqAMgyQLLQETIRSVF--PEVDIVVPgiciANTDTR---HYANITNGMYrfNPLPLNPqdf 461
Cdd:cd03895 305 evewngfQAEGYVLEPGSD-AE--QVLAAAHQAVFgtPPVQSAMT----ATTDGRffvLYGDIPALCY--GPGSRDA--- 372
|
410 420
....*....|....*....|....*.
gi 227908835 462 sgvHGINEKVSVQNYQNQVKFIFEFI 487
Cdd:cd03895 373 ---HGFDESVDLESLRKITKTIALFI 395
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
122-420 |
2.64e-14 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 74.50 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 122 LMAHIDVVPAPEEG-WEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGEKGaq 200
Cdd:PRK13983 81 IISHMDVVPPGDLSlWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYG-- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 201 kISALLQARgVQL-----AFLV-DEGSFilEGfipnlekpvAMISVTEKGALDLMLQVNMTPGHSSAPpkETSIGILSAA 274
Cdd:PRK13983 159 -IQYLLKKH-PELfkkddLILVpDAGNP--DG---------SFIEIAEKSILWLKFTVKGKQCHASTP--ENGINAHRAA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 275 vsrleqtpmpNMFGggplKKTMKLLANEFSfpinivLRNLwLFHPIVSrimernpitnalvrtTTALTMFNAGIK-VNVI 353
Cdd:PRK13983 224 ----------ADFA----LELDEALHEKFN------AKDP-LFDPPYS---------------TFEPTKKEANVDnINTI 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227908835 354 PPLAQATINCRIHPSQTVHEVLELVKNTVADD------RVQLHVLRSFEPLPISPSDDQAMgyQLLQETIRSV 420
Cdd:PRK13983 268 PGRDVFYFDCRVLPDYDLDEVLKDIKEIADEFeeeygvKIEVEIVQREQAPPPTPPDSEIV--KKLKRAIKEV 338
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
125-210 |
4.94e-14 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 73.58 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 125 HIDVVPA-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGEKGAQKIS 203
Cdd:PRK13009 66 HTDVVPPgDLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVL 145
|
....*..
gi 227908835 204 ALLQARG 210
Cdd:PRK13009 146 EWLKARG 152
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
120-264 |
5.51e-14 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 73.30 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 120 YMLMAHIDVVPAPEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNysPKRSFFIALGHDEEVsGEKGA 199
Cdd:PRK07522 67 IVLSGHTDVVPVDGQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAP--LRRPLHLAFSYDEEV-GCLGV 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227908835 200 QKISALLQARGVQ-LAFLVDEgsfilegfiPNLEKPVamisVTEKGALDLMLQVNMTPGHSSAPPK 264
Cdd:PRK07522 144 PSMIARLPERGVKpAGCIVGE---------PTSMRPV----VGHKGKAAYRCTVRGRAAHSSLAPQ 196
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
41-192 |
3.70e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 71.26 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 41 SQFSEEERVAIKEALKGAIQIPTVSFSHEESnttalAEFGEYIRKAFPTV--------FHSSLvqhEVVAKYSHLFTIQG 112
Cdd:PRK07205 3 SYITEKVQDACVAAIKTLVSYPSVLNEGENG-----TPFGQAIQDVLEATldlcqglgFKTYL---DPKGYYGYAEIGQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 113 SdpslQPYMLMAHIDVVPAPEEG-WEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYS-PKRSFFIaLGHD 190
Cdd:PRK07205 75 E----ELLAILCHLDVVPEGDLSdWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQfNKRIRFI-FGTD 149
|
..
gi 227908835 191 EE 192
Cdd:PRK07205 150 EE 151
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
45-198 |
2.41e-12 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 68.71 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 45 EEERVAIKEALKGAIQIPTVSfshEESNTTALAEFGEYIRKA------------FPTVFHSSLVQH-------EVVAkys 105
Cdd:PRK07318 10 EKRKDDLIEDLQELLRINSVR---DDSKAKEGAPFGPGPVKAlekfleiaerdgFKTKNVDNYAGHieygegeEVLG--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 106 hlftiqgsdpslqpymLMAHIDVVPAPEeGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFI 185
Cdd:PRK07318 84 ----------------ILGHLDVVPAGD-GWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRF 146
|
170
....*....|...
gi 227908835 186 ALGHDEEvSGEKG 198
Cdd:PRK07318 147 IVGTDEE-SGWKC 158
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
112-488 |
1.94e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 65.93 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 112 GSDPSLQPYmlmAHIDVVPA-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHD 190
Cdd:PRK06446 60 GAKKTLLIY---NHYDVQPVdPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKHKLNVNVKFLYEGEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 191 E--EVSGEKGAQKISALLQARGVQLaflvdEGSfileGFIPNlEKPvaMISVTEKGALDLMLQVNMTPG--HSS-AP--- 262
Cdd:PRK06446 137 EigSPNLEDFIEKNKNKLKADSVIM-----EGA----GLDPK-GRP--QIVLGVKGLLYVELVLRTGTKdlHSSnAPivr 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 263 -PKETSIGILSAAVSRLEQTPMPNMFGG-GPLKKTMKLLANEFSFPINIVLRNLWLFHPivsRIMERNPITNALVRTTTa 340
Cdd:PRK06446 205 nPAWDLVKLLSTLVDGEGRVLIPGFYDDvRELTEEERELLKKYDIDVEELRKALGFKEL---KYSDREKIAEALLTEPT- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 341 ltmFN-AGIKV--------NVIPPLAQATINCRIHPSQTVHEVLELVKNTV--ADDRVQLHVLRSFEPLPISPSDDQAMG 409
Cdd:PRK06446 281 ---CNiDGFYSgytgkgskTIVPSRAFAKLDFRLVPNQDPYKIFELLKKHLqkVGFNGEIIVHGFEYPVRTSVNSKVVKA 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 410 YQLLQETIRSVFPEVDIVVPGICIANTDTRHYAN--ITNGMYRFNPlplnpqdFSGVHGINEKVSVQNYQNQVKFIFEFI 487
Cdd:PRK06446 358 MIESAKRVYGTEPVVIPNSAGTQPMGLFVYKLGIrdIVSAIGVGGY-------YSNAHAPNENIRIDDYYKAIKHTEEFL 430
|
.
gi 227908835 488 Q 488
Cdd:PRK06446 431 K 431
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
125-495 |
1.83e-10 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 62.59 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 125 HIDVVPAP-EEGWEVPPFSGLERNGFIYGRGALDNKNSVMAI------LHALELLL---IRnyspkrsfFIALGhDEEVs 194
Cdd:PRK08588 67 HMDVVAAGdVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALviamieLKEQGQLLngtIR--------LLATA-GEEV- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 195 GEKGAQkisaLLQARGV--QL-AFLVDEGSFilegfipnlekpvAMISVTEKGALDLMLQVNMTPGHSSappketsigil 271
Cdd:PRK08588 137 GELGAK----QLTEKGYadDLdALIIGEPSG-------------HGIVYAHKGSMDYKVTSTGKAAHSS----------- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 272 saavsrleqtpMPNmFGGGPLKKTMKLLANEFSFpinivlrnlwlfhpiVSRIMERNPITNALVRTTtalTMFNAGIKVN 351
Cdd:PRK08588 189 -----------MPE-LGVNAIDPLLEFYNEQKEY---------------FDSIKKHNPYLGGLTHVV---TIINGGEQVN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 352 VIPPLAQATINCRIHPSQTVHEVLELVKNTVA------DDRVQLHVLRSFEPLPISPSDDqamgyqlLQETIRSVFPEV- 424
Cdd:PRK08588 239 SVPDEAELEFNIRTIPEYDNDQVISLLQEIINevnqngAAQLSLDIYSNHRPVASDKDSK-------LVQLAKDVAKSYv 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227908835 425 --DIVVPGIcIANTDTRHYA-NITNgmyrFNPLPLNPQDFSGVHGINEKVSVQNYqnqVKFIfefiqnaDTYKE 495
Cdd:PRK08588 312 gqDIPLSAI-PGATDASSFLkKKPD----FPVIIFGPGNNLTAHQVDEYVEKDMY---LKFI-------DIYKE 370
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
112-170 |
1.99e-10 |
|
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: 63.00 E-value: 1.99e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 112 GSDPSLQPYMLMAHIDVVPA-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALE 170
Cdd:cd05676 80 GSDPSKKTVLIYGHLDVQPAkLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIE 139
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
45-169 |
5.55e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 61.46 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 45 EEERVAIKEALKGAIQIPTVS---FSHEESNTTAlaefgEYIRKAF------PTVFHSSLVQHEVVAKYshlftiQGSD- 114
Cdd:PRK07907 14 AELLPRVRADLEELVRIPSVAadpFRREEVARSA-----EWVADLLreagfdDVRVVSADGAPAVIGTR------PAPPg 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 227908835 115 -PSLqpyMLMAHIDVVPAP-EEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHAL 169
Cdd:PRK07907 83 aPTV---LLYAHHDVQPPGdPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAAL 136
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
124-173 |
5.80e-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: 61.17 E-value: 5.80e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 227908835 124 AHIDVVPA-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLL 173
Cdd:cd05680 70 GHYDVQPPdPLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWL 120
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
122-280 |
8.03e-10 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 60.79 E-value: 8.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 122 LMAHIDVVPA-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGeKGAq 200
Cdd:PRK06837 102 LQGHIDVVPEgPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEESTG-NGA- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 201 kISALLqaRGVQlAFLVdegsfilegFIPNLEKPVAMISVTekGALDLMLQVNMTPGHssapPKETSIG---ILSA---- 273
Cdd:PRK06837 180 -LSTLQ--RGYR-ADAC---------LIPEPTGEKLVRAQV--GVIWFRLRVRGAPVH----VREAGTGanaIDAAyhli 240
|
....*...
gi 227908835 274 -AVSRLEQ 280
Cdd:PRK06837 241 qALRELEA 248
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
109-198 |
1.42e-09 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 60.05 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 109 TIQGSDP-SLQPYMLMAHIDVVPA-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIA 186
Cdd:PRK08596 68 VKKGTESdAYKSLIINGHMDVAEVsADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQ 147
|
90
....*....|..
gi 227908835 187 LGHDEEVsGEKG 198
Cdd:PRK08596 148 SVIGEEV-GEAG 158
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
121-218 |
2.83e-09 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 59.02 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 121 MLMAHIDVVPAPEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKrsFFIALGHDEEVSGEKGAq 200
Cdd:PRK08554 67 LFMAHFDVVPVNPEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLNGK--VIFAFTGDEEIGGAMAM- 143
|
90
....*....|....*...
gi 227908835 201 KISALLQARGVQLAFLVD 218
Cdd:PRK08554 144 HIAEKLREEGKLPKYMIN 161
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
125-489 |
4.50e-09 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 58.23 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 125 HIDVVPApeegwEVPPFsglERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKrsFFIALGHDEEVSGeKGaqkiSA 204
Cdd:PRK08652 63 HYDTVPV-----RAEFF---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLN--VGIAFVSDEEEGG-RG----SA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 205 LLQAR-GVQLAFLvdegsfilegfipnLEKPVAMISVTEKGALDLMLQVNMTPGHSSAPpkETSIGILSAAVSRLEQtpm 283
Cdd:PRK08652 128 LFAERyRPKMAIV--------------LEPTDLKVAIAHYGNLEAYVEVKGKPSHGACP--ESGVNAIEKAFEMLEK--- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 284 pnmfgggpLKKTMKLLANEFSFPINIvlrnlwlfhpivSRIMERNPitnalvrtttaltmfnagikVNVIPPLAQATINC 363
Cdd:PRK08652 189 --------LKELLKALGKYFDPHIGI------------QEIIGGSP--------------------EYSIPALCRLRLDA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 364 RIHPSQTVHEVLELVKNTVADDRVQLHVLRSFEPLPISPSDDQAmgyQLLQETIRSVFPEVDIVVpgiciantdTRHYAN 443
Cdd:PRK08652 229 RIPPEVEVEDVLDEIDPILDEYTVKYEYTEIWDGFELDEDEEIV---QLLEKAMKEVGLEPEFTV---------MRSWTD 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 227908835 444 ITNGMYR-FNPLPLNPQDFSGVHGINEKVSVQNYQNQVKFI---FEFIQN 489
Cdd:PRK08652 297 AINFRYNgTKTVVWGPGELDLCHTKFERIDVREVEKAKEFLkalNEILLE 346
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
124-168 |
9.68e-09 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 57.26 E-value: 9.68e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 227908835 124 AHIDVVPAP-EEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHA 168
Cdd:PRK13004 76 AHIDTVGIGdIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYA 121
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
45-173 |
1.05e-08 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 57.45 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 45 EEERVAIKEALKGAIQIPTVSfsheesnttALAEFGEYIRKA---FPTVFHSSLVQH-EVVAKYSH-LFTIQGSDPSLQP 119
Cdd:PRK08201 10 RERREAHLEELKEFLRIPSIS---------ALSEHKEDVRKAaewLAGALEKAGLEHvEIMETAGHpIVYADWLHAPGKP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 227908835 120 YMLM-AHIDVVPA-PEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLL 173
Cdd:PRK08201 81 TVLIyGHYDVQPVdPLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALL 136
|
|
| PRK06915 |
PRK06915 |
peptidase; |
121-172 |
2.43e-08 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 56.24 E-value: 2.43e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 227908835 121 MLMAHIDVVPAPE-EGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELL 172
Cdd:PRK06915 97 ILNGHIDVVPEGDvNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEAL 149
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
240-384 |
2.67e-08 |
|
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: 51.96 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 240 VTEKGALDLMLQVNMTPGHSSAPPKETS-IGILSAAVSRLEQtpmpnmfgggplkktmkllanefsfpinivlrnlwlfh 318
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNaIKLLARLLAELPA-------------------------------------- 42
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227908835 319 pivsrimERNPITNALVRTTTALTMFNAGIKVNVIPPLAQATINCRIHPSQTVHEVLELVKNTVAD 384
Cdd:pfam07687 43 -------EYGDIGFDFPRTTLNITGIEGGTATNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEK 101
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
50-377 |
4.58e-08 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 55.05 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 50 AIKEALKGAIQIPTVSfsHEEsntTALAEFGEYIRKAFPTVFHSSLVQHEVVAKyshlftiqGSDPSLqpYMLMAHIDVV 129
Cdd:cd05653 2 DAVELLLDLLSIYSPS--GEE---ARAAKFLEEIMKELGLEAWVDEAGNAVGGA--------GSGPPD--VLLLGHIDTV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 130 PApeegwEVPPfsgLERNGFIYGRGALDNKNSVMAILHALELLlirNYSPKRSFFIALGHDEEVSGeKGAQkisallqar 209
Cdd:cd05653 67 PG-----EIPV---RVEGGVLYGRGAVDAKGPLAAMILAASAL---NEELGARVVVAGLVDEEGSS-KGAR--------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 210 gvqlaFLVDEGS---FILEGFIPNLEKpvamISVTEKGALDLMLQVNMTPGHSSApPKETSIGILSAAVSRLEQTPMPNM 286
Cdd:cd05653 126 -----ELVRRGPrpdYIIIGEPSGWDG----ITLGYRGSLLVKIRCEGRSGHSSS-PERNAAEDLIKKWLEVKKWAEGYN 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 287 FGGGPlkktmkllanefsfpinivlrnlwlFHPIVSrimernpitnalvrtttalTMFNAGIKVNVIPPLAQATINCRIH 366
Cdd:cd05653 196 VGGRD-------------------------FDSVVP-------------------TLIKGGESSNGLPQRAEATIDLRLP 231
|
330
....*....|.
gi 227908835 367 PSQTVHEVLEL 377
Cdd:cd05653 232 PRLSPEEAIAL 242
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
53-264 |
5.39e-08 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 54.73 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 53 EALKGAIQIPtvSFSHEESNTTALAEfgEYIRK-AFPTVFhsslvqhevVAKYSHLFTIQGSDPSLqpyMLM-AHIDVVP 130
Cdd:cd05649 2 RFLRDLIQIP--SESGEEKGVVERIE--EEMEKlGFDEVE---------IDPMGNVIGYIGGGKKK---ILFdGHIDTVG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 131 APEE-GWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLL-IRNYSPKRSFFIALGHDEEVSGEKGAQKISallQA 208
Cdd:cd05649 66 IGNIdNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKdLGLRDFAYTILVAGTVQEEDCDGVCWQYIS---KA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 227908835 209 RGVQLAFLV-DEGSfilEGFIPNLEKPVAMISVTEKGaldlmlqvnmTPGHSSAPPK 264
Cdd:cd05649 143 DKIKPDFVVsGEPT---DGNIYRGQRGRMEIRVDTKG----------VSCHGSAPER 186
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
72-402 |
6.36e-08 |
|
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: 54.52 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 72 NTTALAEFGEYIRKAF-PTVFHSSLVQHEVVAkySHL-FTIQGSDPslQPYMLMAHIDVVPAPEEGWEVPpFSglERNGF 149
Cdd:cd03885 17 DKEGVDRVAELLAEELeALGFTVERRPLGEFG--DHLiATFKGTGG--KRVLLIGHMDTVFPEGTLAFRP-FT--VDGDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 150 IYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVsGEKGAQkisALLQ--ARGVQLAFlvdegsfilegf 227
Cdd:cd03885 90 AYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEI-GSPGSR---ELIEeeAKGADYVL------------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 228 ipNLEKPVA--MISVTEKGALDLMLQVNMTPGHSSAPPKEtsiGIlSAAVsrleqtpmpnmfgggplkktmkllanEFSf 305
Cdd:cd03885 154 --VFEPARAdgNLVTARKGIGRFRLTVKGRAAHAGNAPEK---GR-SAIY--------------------------ELA- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 306 piNIVLRnlwlfhpivsrimernpiTNALVRTTTALTMfN-----AGIKVNVIPPLAQATINCRI---HPSQTVHEVL-E 376
Cdd:cd03885 201 --HQVLA------------------LHALTDPEKGTTV-NvgvisGGTRVNVVPDHAEAQVDVRFataEEADRVEEALrA 259
|
330 340
....*....|....*....|....*..
gi 227908835 377 LVKNT-VADDRVQLHVLRSFEPLPISP 402
Cdd:cd03885 260 IVATTlVPGTSVELTGGLNRPPMEETP 286
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
125-202 |
1.15e-07 |
|
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex.
Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 53.89 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 125 HIDVVPAPEE-GWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYspkrsffiaLGHD-------EEVSGE 196
Cdd:cd05677 79 HYDVIPAGETdGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQEGE---------LDNDvvfliegEEESGS 149
|
....*.
gi 227908835 197 KGAQKI 202
Cdd:cd05677 150 PGFKEV 155
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
124-173 |
5.21e-07 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 52.07 E-value: 5.21e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 227908835 124 AHIDVVPApEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLL 173
Cdd:PRK13013 91 SHHDVVEV-GHGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFL 139
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
122-391 |
7.82e-06 |
|
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: 47.82 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 122 LMAHIDVVPAPEEgweVPpfSGLERNGFIYGRGALDNKNSVMAILHaLELLLIRNYSPKRSFFIALGHDEEVSGEKGAQK 201
Cdd:cd05647 58 LAGHLDTVPVAGN---LP--SRVEEDGVLYGCGATDMKAGDAVQLK-LAATLAAATLKHDLTLIFYDCEEVAAELNGLGR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 202 ISA----LLQArgvQLAFLvdegsfilegfipnLEKPVAMISVTEKGALDLMLQVNMTPGHSSAP-PKETSIGILSAAVS 276
Cdd:cd05647 132 LAEehpeWLAA---DFAVL--------------GEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSwLGENAIHKLAPILA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 277 RL-EQTPMPNMFGGgplkktmkllanefsfpinivlrnlwlfhpivsriMERNPITNAlvrtttalTMFNAGIKVNVIPP 355
Cdd:cd05647 195 RLaAYEPRTVNIDG-----------------------------------LTYREGLNA--------VFISGGVAGNVIPD 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 227908835 356 LAQATINCRIHPSQTVHEVLELVKNTVADDRVQLHV 391
Cdd:cd05647 232 EARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEIEV 267
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
121-406 |
1.97e-05 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 46.93 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 121 MLMAHIDVVPAP----EEgwevpPFSglERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVsGE 196
Cdd:PRK06133 103 MLIAHMDTVYLPgmlaKQ-----PFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEET-GS 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 197 KGAQKIsallqargvqLAFLVDEGSFILegfipNLEKPVAMISVT--EKGALDLMLQVNMTPGHSSAPPKETSIGILSAA 274
Cdd:PRK06133 175 PGSREL----------IAELAAQHDVVF-----SCEPGRAKDALTlaTSGIATALLEVKGKASHAGAAPELGRNALYELA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 275 VSRLEqtpmpnmfgggplkktMKLLAnefsfpinivlrnlwlfhpivsrimerNPITNalvrTTTALTMFNAGIKVNVIP 354
Cdd:PRK06133 240 HQLLQ----------------LRDLG---------------------------DPAKG----TTLNWTVAKAGTNRNVIP 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 227908835 355 PLAQATINCRIHPSQTVHEVL----ELVKNT-VADDRVQLHVLRSFEPLPISPSDDQ 406
Cdd:PRK06133 273 ASASAQADVRYLDPAEFDRLEadlqEKVKNKlVPDTEVTLRFERGRPPLEANAASRA 329
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
121-384 |
2.89e-05 |
|
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: 46.11 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 121 MLMAHIDVVPapeegwevP--PFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGEkG 198
Cdd:cd05652 62 LLTSHIDTVP--------PfiPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGD-G 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 199 AQKISALLqargvqlaflvdegsfilegfipnLEKPVAMI---------SVTEKGALDLMLQVNMTPGHSSAPPKETS-I 268
Cdd:cd05652 133 MKAFNDLG------------------------LNTWDAVIfgeptelklASGHKGMLGFKLTAKGKAGHSGYPWLGISaI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 269 GILSAAVSRLEQTPMPNmfgggplkktmkllanefsfpinivlrnlwlfhpivsrimernpiTNALVRTTTALTMFNAGI 348
Cdd:cd05652 189 EILVEALVKLIDADLPS---------------------------------------------SELLGPTTLNIGRISGGV 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 227908835 349 KVNVIPPLAQATINCRIhpSQTVHEVLELVKNTVAD 384
Cdd:cd05652 224 AANVVPAAAEASVAIRL--AAGPPEVKDIVKEAVAG 257
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
122-279 |
4.53e-05 |
|
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: 45.62 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 122 LMAHIDVVPaPEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGEKGAqk 201
Cdd:cd02697 78 LNAHGDVVP-PGDGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGELGP-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 202 isallqargvqlAFLVDEGsfilegfipnLEKPVAMIS-------VT-EKGALDLMLQVNMTPGHSSAPpkETSIGILSA 273
Cdd:cd02697 155 ------------GWLLRQG----------LTKPDLLIAagfsyevVTaHNGCLQMEVTVHGKQAHAAIP--DTGVDALQG 210
|
....*.
gi 227908835 274 AVSRLE 279
Cdd:cd02697 211 AVAILN 216
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
121-169 |
1.63e-04 |
|
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: 44.00 E-value: 1.63e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 227908835 121 MLMAHIDVVPApeEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHAL 169
Cdd:cd08013 72 MLNGHIDTVTL--DGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAAL 118
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
121-282 |
2.86e-03 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 39.77 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 121 MLMAHIDVVPapeeGWEVPPFSGLErngfIYGRGALDNKNSVMAILHALELLLIRNYSPKrsfFIALGhDEEvSGEKGAQ 200
Cdd:PRK00466 64 LLASHVDTVP----GYIEPKIEGEV----IYGRGAVDAKGPLISMIIAAWLLNEKGIKVM---VSGLA-DEE-STSIGAK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227908835 201 KisalLQARGvqlaflvDEGSFILEGFIPNLEKpvamISVTEKGALDLMLQVNMTPGHSSApPKETSIGILSAAVSRLEQ 280
Cdd:PRK00466 131 E----LVSKG-------FNFKHIIVGEPSNGTD----IVVEYRGSIQLDIMCEGTPEHSSS-AKSNLIVDISKKIIEVYK 194
|
..
gi 227908835 281 TP 282
Cdd:PRK00466 195 QP 196
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
124-169 |
5.02e-03 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 39.57 E-value: 5.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 227908835 124 AHIDVVPAPEEGWEVP-----PFSgLERNG-FIYGRGALDNKNSVMAILHAL 169
Cdd:PRK06156 116 THADVVPANPELWVLDgtrldPFK-VTLVGdRLYGRGTEDDKGAIVTALYAM 166
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
125-157 |
7.13e-03 |
|
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: 38.98 E-value: 7.13e-03
10 20 30
....*....|....*....|....*....|....
gi 227908835 125 HIDVVPAPEEGWEVPPFSgLERNG-FIYGRGALD 157
Cdd:cd08012 86 HMDVVTANPETWEFDPFS-LSIDGdKLYGRGTTD 118
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
125-168 |
8.69e-03 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 38.73 E-value: 8.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 227908835 125 HIDVVPA-PEEGWEVPPFS-GLERNG----FIYGRGALDNKNSVMAILHA 168
Cdd:PRK09104 90 HYDVQPVdPLDLWESPPFEpRIKETPdgrkVIVARGASDDKGQLMTFVEA 139
|
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