|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
6-405 |
0e+00 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 626.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 6 EKEKIQLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVNEHRANFVAEIGSGSPILALSGHMDVVDAGNQDNWT 85
Cdd:PRK08588 1 EEEKIQILADIVKINSVNDNEIEVANYLQDLFAKHGIESKIVKVNDGRANLVAEIGSGSPVLALSGHMDVVAAGDVDKWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 86 YPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLADKGYLDDVDGLMIAE 165
Cdd:PRK08588 81 YDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGELGAKQLTEKGYADDLDALIIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 166 PTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYAELKKNDtkheldvapmfksligkdisee 245
Cdd:PRK08588 161 PSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYFDSIKKHN---------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 246 daNYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNVDSN---KLSLDIPSNHRPVTSDKN 322
Cdd:PRK08588 219 --PYLGGLTHVVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNQNgaaQLSLDIYSNHRPVASDKD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 323 SKLITTIKDVASSYVDKdDIFVSALVGATDASSFLgDNKDNVDLAIFGPGNPLMAHQIDEYIEKDMYLKYIDIFKEASIQ 402
Cdd:PRK08588 297 SKLVQLAKDVAKSYVGQ-DIPLSAIPGATDASSFL-KKKPDFPVIIFGPGNNLTAHQVDEYVEKDMYLKFIDIYKEIIIQ 374
|
...
gi 612905143 403 YLK 405
Cdd:PRK08588 375 YLK 377
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
11-399 |
2.22e-132 |
|
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: 384.34 E-value: 2.22e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 11 QLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVnEHRANFVAEIGSGS-PILALSGHMDVVDAGNQDNWTYPPF 89
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIV-EGRGNLVATVGGGDgPVLLLNGHIDTVPPGDGDKWSFPPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 90 QLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLADKGYLDDVDGLMIAEPTGS 169
Cdd:cd08659 80 SGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLEAGYADRLDALIVGEPTGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 170 GIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYAELKKNDtkheldvapmfksLIGkdiseedany 249
Cdd:cd08659 160 DVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPAHP-------------LLG---------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 250 asGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDND-FIESFFQniINNVDSNKLSLDIPSNHRPVT-SDKNSKLIT 327
Cdd:cd08659 217 --PPTLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEgVIARLEA--ILEEHEAKLTVEVSLDGDPPFfTDPDHPLVQ 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612905143 328 TIKDVASSYVDKDDIFVSAlvGATDASSFLGDNkdNVDLAIFGPGNPLMAHQIDEYIEKDMYLKYIDIFKEA 399
Cdd:cd08659 293 ALQAAARALGGDPVVRPFT--GTTDASYFAKDL--GFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEI 360
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
10-395 |
1.17e-91 |
|
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: 280.82 E-value: 1.17e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 10 IQLLADIVELQTENN---NEIDVCNYLKDLFDKYDIKSEILKVNEHRAN-----FVAEIGSGS-PILALSGHMDVVDAGN 80
Cdd:TIGR01910 1 VELLKDLISIPSVNPpggNEETIANYIKDLLREFGFSTDVIEITDDRLKvlgkvVVKEPGNGNeKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 81 QDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLADKGYLDDVDG 160
Cdd:TIGR01910 81 LELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLLQRGYFKDADG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 161 LMIAEPTGS-GIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEkyAELKKNDTKHELDvapmfkslIG 239
Cdd:TIGR01910 161 VLIPEPSGGdNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNE--LEEHIYARNSYGF--------IP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 240 KDISEEDAnyasgltavcsIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNVDSNK---LSLDIPSN-HR 315
Cdd:TIGR01910 231 GPITFNPG-----------VIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSDgwlYENEPVVKwSG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 316 PVTSDKNSKLITTIKDVASSYVdKDDIFVSALVGATDAsSFLGDNKdnVDLAIFGPGNPLMAHQIDEYIEKDMYLKYIDI 395
Cdd:TIGR01910 300 PNETPPDSRLVKALEAIIKKVR-GIEPEVLVSTGGTDA-RFLRKAG--IPSIVYGPGDLETAHQVNEYISIKNLVESTKV 375
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
10-396 |
1.30e-91 |
|
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: 281.00 E-value: 1.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 10 IQLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVNEHRANFVAEI--GSGSPILALSGHMDVVDAGNQDNWTYP 87
Cdd:COG0624 15 LELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPPGRPNLVARRpgDGGGPTLLLYGHLDVVPPGDLELWTSD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 88 PFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQEGAK-LLADKGYLDDVDGLMIAEP 166
Cdd:COG0624 95 PFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSPGARaLVEELAEGLKADAAIVGEP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 167 TGSG-IYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKekyaelkknDTKHELDVAPMFKSLigkdisee 245
Cdd:COG0624 175 TGVPtIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALR---------DLEFDGRADPLFGRT-------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 246 danyasglTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNVDSN-KLSLDIPSNHR-PVTSDKNS 323
Cdd:COG0624 238 --------TLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGvEVEVEVLGDGRpPFETPPDS 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612905143 324 KLITTIKDVASSyVDKDDIFVSALVGATDASSFLGDNkdNVDLAIFGPGNPLMAHQIDEYIEKDMYLKYIDIF 396
Cdd:COG0624 310 PLVAAARAAIRE-VTGKEPVLSGVGGGTDARFFAEAL--GIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVL 379
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
68-399 |
7.62e-63 |
|
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: 204.50 E-value: 7.62e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 68 ALSGHMDVVDAGNQDNWtypPFQLTEkDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPqGTIRLLATAGEEKEQEGAK 147
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLKK-GTVKLLFQPDEEGGMGGAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 148 LLADKGYLDD-----VDGLMIAEPT------GSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQfkeky 216
Cdd:pfam01546 76 ALIEDGLLERekvdaVFGLHIGEPTlleggiAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILA----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 217 aelkkndtkheldvapmfkslIGKDISEEDANYASGLTAVCSI--INGGkqFNSVPDEASLEFNVRPVPEYDNDFIESFF 294
Cdd:pfam01546 151 ---------------------LQDIVSRNVDPLDPAVVTVGNItgIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 295 QNIINNV---DSNKLSLDIPSNHRPVTSDkNSKLITTIKDVASSYVDKD-DIFVSALVGATDASSFLGDNKDNVDlaIFG 370
Cdd:pfam01546 208 REILEAIaaaYGVKVEVEYVEGGAPPLVN-DSPLVAALREAAKELFGLKvELIVSGSMGGTDAAFFLLGVPPTVV--FFG 284
|
330 340
....*....|....*....|....*....
gi 612905143 371 PGNPLmAHQIDEYIEKDMYLKYIDIFKEA 399
Cdd:pfam01546 285 PGSGL-AHSPNEYVDLDDLEKGAKVLARL 312
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
10-399 |
1.55e-61 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 203.68 E-value: 1.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 10 IQLLADIVELQTENNNEIDV---CNYLKDLFDKYDIKSEIL--------KVNEHRANFVAEIGSGSPILALSGHMDVVDA 78
Cdd:PRK08651 9 VEFLKDLIKIPTVNPPGENYeeiAEFLRDTLEELGFSTEIIevpneyvkKHDGPRPNLIARRGSGNPHLHFNGHYDVVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 79 GnqDNW-TYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEqnqLPQGTIRLLATAGEEKEQEGAKLLADKGYlDD 157
Cdd:PRK08651 89 G--EGWsVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDP---AGDGNIELAIVPDEETGGTGTGYLVEEGK-VT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 158 VDGLMIAEPTGSG-IYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYAELKKNdtkheldvapmfks 236
Cdd:PRK08651 163 PDYVIVGEPSGLDnICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSK-------------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 237 ligKDISEEDANYASgLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNV---DSNKLSLDIPSN 313
Cdd:PRK08651 229 ---YEYDDERGAKPT-VTLGGPTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVapeLGIEVEFEITPF 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 314 HRPVTSDKNSKLITTIKDVASSYVDKDDIFVSAlVGATDASSFLgdnKDNVDLAIFGPGNPLMAHQIDEYIEKDMYLKYI 393
Cdd:PRK08651 305 SEAFVTDPDSELVKALREAIREVLGVEPKKTIS-LGGTDARFFG---AKGIPTVVYGPGELELAHAPDEYVEVKDVEKAA 380
|
....*.
gi 612905143 394 DIFKEA 399
Cdd:PRK08651 381 KVYEEV 386
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
10-399 |
4.64e-60 |
|
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: 198.77 E-value: 4.64e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 10 IQLLADIVELQTEN---NNEIDVCNYLKDLFDKYDIKSEILKVNEHRANFVAEI--GSGSPILALSGHMDVVDAGNQDNW 84
Cdd:cd08011 1 VKLLQELVQIPSPNppgDNTSAIAAYIKLLLEDLGYPVELHEPPEEIYGVVSNIvgGRKGKRLLFNGHYDVVPAGDGEGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 85 TYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEK-EQEGAKLLADKgYLDDVDGLMI 163
Cdd:cd08011 81 TVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETgGRAGTKYLLEK-VRIKPNDVLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 164 AEPTGS-GIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLefynqfkekyaelkkndtkheldvapmfkSLIGKdI 242
Cdd:cd08011 160 GEPSGSdNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAM-----------------------------KLIER-L 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 243 SEEDANYASGltavcsIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESffqNIINNVDS-NKLSLDIPSNHRPVTSDK 321
Cdd:cd08011 210 YELEKTVNPG------VIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLS---RIIDHLDSiEEVSFEIKSFYSPTVSNP 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612905143 322 NSKLITTIKDVASSYVDKDDIFVSAlVGATDASSFlgdNKDNVDLAIFGPGNPLMAHQIDEYIEKDMYLKYIDIFKEA 399
Cdd:cd08011 281 DSEIVKKTEEAITEVLGIRPKEVIS-VGASDARFY---RNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVHALV 354
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
11-385 |
1.12e-54 |
|
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: 185.10 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 11 QLLADIVELQTEN-NNEIDVCNYLKDLFDKYDIKSEILKVNEH-RANFVAEIGSGS-PILALSGHMDVVDAGNQDnWTYP 87
Cdd:cd03894 1 ELLARLVAFDTVSrNSNLALIEYVADYLAALGVKSRRVPVPEGgKANLLATLGPGGeGGLLLSGHTDVVPVDGQK-WSSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 88 PFQLTEKDDKLYGRGTTDMKGGLmALVIALI-ELKEQNQlpQGTIRLLATAGEEKEQEGAKLLADKGYLDDV--DGLMIA 164
Cdd:cd03894 80 PFTLTERDGRLYGRGTCDMKGFL-AAVLAAVpRLLAAKL--RKPLHLAFSYDEEVGCLGVRHLIAALAARGGrpDAAIVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 165 EPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYAELKKNDTKHELDVaPmfksligkdise 244
Cdd:cd03894 157 EPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPFDP-P------------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 245 edanyasGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINN--------VDSNKLSLDIPSNhrp 316
Cdd:cd03894 224 -------YPTLNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEAllefpeagIEVEPLFEVPGLE--- 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612905143 317 vtSDKNSKLITTIKDVASSYVdkddifVSALVGATDASSF--LGdnkdnVDLAIFGPGNPLMAHQIDEYIE 385
Cdd:cd03894 294 --TDEDAPLVRLAAALAGDNK------VRTVAYGTEAGLFqrAG-----IPTVVCGPGSIAQAHTPDEFVE 351
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
11-356 |
5.39e-43 |
|
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: 155.60 E-value: 5.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 11 QLLADIVELQTENN-----NEIDVCNYLKDLFDKYDIKSEILKVNEH--RANFVAEIGSGSPI---LALSGHMDVVDAgN 80
Cdd:cd05675 2 DLLQELIRIDTTNSgdgtgSETRAAEVLAARLAEAGIQTEIFVVESHpgRANLVARIGGTDPSagpLLLLGHIDVVPA-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 81 QDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQE-GAKLLADK------G 153
Cdd:cd05675 81 ASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGEnGAKWLVDNhpelfdG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 154 Y---LDDVDGLMIAEPTGSGIYY---AHKGSMSCKVTATGKAVHSSVPFIgDNAIDTLLEFYNQFKEKYAELKKNDTK-- 225
Cdd:cd05675 161 AtfaLNEGGGGSLPVGKGRRLYPiqvAEKGIAWMKLTVRGRAGHGSRPTD-DNAITRLAEALRRLGAHNFPVRLTDETay 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 226 ----HELDVAP----MFKSLIGKDI-------SEEDANYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFI 290
Cdd:cd05675 240 faqmAELAGGEggalMLTAVPVLDPalaklgpSAPLLNAMLRNTASPTMLDAGYATNVLPGRATAEVDCRILPGQSEEEV 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612905143 291 ESFFQNIINNVD-SNKLSLDIPSNHRPVTsdknSKLITTIKDVASSyVDKDDIFVSALV-GATDASSF 356
Cdd:cd05675 320 LDTLDKLLGDPDvSVEAVHLEPATESPLD----SPLVDAMEAAVQA-VDPGAPVVPYMSpGGTDAKYF 382
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
28-387 |
5.88e-42 |
|
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130947 [Multi-domain] Cd Length: 364 Bit Score: 151.13 E-value: 5.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 28 DVCNYLKDLFDKYDIKSEILKVNE--HRANFVAEIG-SGSPILALSGHMDVVDAGNQdNWTYPPFQLTEKDDKLYGRGTT 104
Cdd:TIGR01892 19 DLIDWAQAYLEALGFSVEVQPFPDgaEKSNLVAVIGpSGAGGLALSGHTDVVPYDDA-AWTRDPFRLTEKDGRLYGRGTC 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 105 DMKGGLMALVIALIELkEQNQLpQGTIRLLATAGEEKEQEGAKLLADKGYLDDvDGLMIAEPTGSGIYYAHKGSMSCKVT 184
Cdd:TIGR01892 98 DMKGFLACALAAAPDL-AAEQL-KKPLHLALTADEEVGCTGAPKMIEAGAGRP-RHAIIGEPTRLIPVRAHKGYASAEVT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 185 ATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYAELKKNDtkHELDVAPMFKSL-IGkdiseedanyasgltavcsIINGG 263
Cdd:TIGR01892 175 VRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLRED--LDEGFTPPYTTLnIG-------------------VIQGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 264 KQFNSVPDEASLEFNVRPVPeydndfiesffqniinNVDSNKLSLDIPSNHRPVTSDKNS-----KLITTIKDVASSYVD 338
Cdd:TIGR01892 234 KAVNIIPGACEFVFEWRPIP----------------GMDPEELLQLLETIAQALVRDEPGfevqiEVVSTDPGVNTEPDA 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 612905143 339 KDDIFVSALVG--------ATDASSFLGDNKDNVdlaIFGPGNPLMAHQIDEYIEKD 387
Cdd:TIGR01892 298 ELVAFLEELSGnapevvsyGTEAPQFQELGAEAV---VCGPGDIRQAHQPDEYVEIE 351
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
29-394 |
8.18e-40 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 146.12 E-value: 8.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 29 VCNYLKDLFDKYDIKSEILKVNEHR--ANFVAEIGSGSPILALSGHMDVV--DAGNqdnWTYPPFQLTEKDDKLYGRGTT 104
Cdd:PRK05111 34 VIDLLAGWFEDLGFNVEIQPVPGTRgkFNLLASLGSGEGGLLLAGHTDTVpfDEGR---WTRDPFTLTEHDGKLYGLGTA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 105 DMKgGLMALVI-ALIELKEQNQlpQGTIRLLATAGEEKEQEGAKLLADKGYLDDvDGLMIAEPTGSGIYYAHKGSMSCKV 183
Cdd:PRK05111 111 DMK-GFFAFILeALRDIDLTKL--KKPLYILATADEETSMAGARAFAEATAIRP-DCAIIGEPTSLKPVRAHKGHMSEAI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 184 TATGKAVHSSVPFIGDNAIDT-------LLEFYNQFKEKYAElkkndtkheldvaPMFksligkDISEEDANYASgltav 256
Cdd:PRK05111 187 RITGQSGHSSDPALGVNAIELmhdvigeLLQLRDELQERYHN-------------PAF------TVPYPTLNLGH----- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 257 csiINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNV-DSNKLSLDIPSNHRPVTS---DKNSKLITTIKDV 332
Cdd:PRK05111 243 ---IHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVsERWPGRITVAPLHPPIPGyecPADHQLVRVVEKL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612905143 333 ------ASSYvdkddifvsalvgATDAsSFLgdNKDNVDLAIFGPGNPLMAHQIDEYIEkdmyLKYID 394
Cdd:PRK05111 320 lghkaeVVNY-------------CTEA-PFI--QQLGCPTLVLGPGSIEQAHQPDEYLE----LSFIK 367
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
31-385 |
7.03e-38 |
|
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: 140.33 E-value: 7.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 31 NYLKDLFDKYDIKSEILKVNEHRaNFVAEIGSGSPILALSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGL 110
Cdd:cd03891 22 DLIAERLKALGFTCERLEFGGVK-NLWARRGTGGPHLCFAGHTDVVPPGDLEGWSSDPFSPTIKDGMLYGRGAADMKGGI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 111 MALVIALIELKEQNQLPQGTIRLLATAGEEKEQE-GAKL----LADKGYLddVDGLMIAEPT-----GSGIYYAHKGSMS 180
Cdd:cd03891 101 AAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIdGTKKvlewLKARGEK--IDYCIVGEPTsekklGDTIKIGRRGSLN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 181 CKVTATGKAVHSSVPFIGDNAIDTLlefynqfkekyaelkkndtkheldvAPMFKSLIGKDISEEDANYASGLTAVCSII 260
Cdd:cd03891 179 GKLTIKGKQGHVAYPHLADNPIHLL-------------------------APILAELTATVLDEGNEFFPPSSLQITNID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 261 NGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNVDSNkLSLDIPSNHRP-VTsdKNSKLITTIKDVASSYVDK 339
Cdd:cd03891 234 VGNGATNVIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLD-YDLEWKLSGEPfLT--KPGKLVDAVSAAIKEVTGI 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 612905143 340 DDIFvSALVGATDAsSFLGDNKDNVdlAIFGPGNpLMAHQIDEYIE 385
Cdd:cd03891 311 TPEL-STSGGTSDA-RFIASYGCPV--VEFGLVN-ATIHKVNERVS 351
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
6-407 |
2.62e-36 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 136.99 E-value: 2.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 6 EKEKIQLLADIVELQTENNNEIDVCNYLKDLFDK--YDiKSEIlkvnEHRANFVAEIGSGSPILALSGHMDVVDAGNQDN 83
Cdd:PRK13004 14 KADMTRFLRDLIRIPSESGDEKRVVKRIKEEMEKvgFD-KVEI----DPMGNVLGYIGHGKKLIAFDAHIDTVGIGDIKN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 84 WTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEkEQEGaklLADKgYLDDVDGL-- 161
Cdd:PRK13004 89 WDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEE-DCDG---LCWR-YIIEEDKIkp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 162 ---MIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKekyaELKKNDTKHEldvapmfksLI 238
Cdd:PRK13004 164 dfvVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELE----ELNPNLKEDP---------FL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 239 GKdiseedanyasGLTAVCSIINGGKQFNSVPDEASLEFNVR-PVPEYDNDFIESffqniINNVDSNKlsldipsNHRPV 317
Cdd:PRK13004 231 GK-----------GTLTVSDIFSTSPSRCAVPDSCAISIDRRlTVGETWESVLAE-----IRALPAVK-------KANAK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 318 TS--DKNSKLITTIKDVASSY-----VDKDDIFVSALVGA-----------------TDASSFLGDNKdnvdlaI----F 369
Cdd:PRK13004 288 VSmyNYDRPSYTGLVYPTECYfptwlYPEDHEFVKAAVEAykglfgkapevdkwtfsTNGVSIAGRAG------IptigF 361
|
410 420 430
....*....|....*....|....*....|....*...
gi 612905143 370 GPGNPLMAHQIDEYIEKDMYLKYIDIFKEASIQYLKEK 407
Cdd:PRK13004 362 GPGKEPLAHAPNEYTWKEQLVKAAAMYAAIPKSLLKKK 399
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
10-286 |
6.01e-36 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 135.70 E-value: 6.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 10 IQLLADIVELQT---ENNNE-IDvcnYLKDLFDKYDIKSEILKVNE-HRANFVAEIG-SGSPILALSGHMDVVDAGNQDn 83
Cdd:PRK07522 7 LDILERLVAFDTvsrDSNLAlIE---WVRDYLAAHGVESELIPDPEgDKANLFATIGpADRGGIVLSGHTDVVPVDGQA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 84 WTYPPFQLTEKDDKLYGRGTTDMKGGLmALVIALI-ELKEQN-QLPqgtIRLLATAGEEKEQEGAKLLAD--KGYLDDVD 159
Cdd:PRK07522 83 WTSDPFRLTERDGRLYGRGTCDMKGFI-AAALAAVpELAAAPlRRP---LHLAFSYDEEVGCLGVPSMIArlPERGVKPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 160 GLMIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYAELKKNDtkhelDVAPMFkslig 239
Cdd:PRK07522 159 GCIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLAAPG-----PFDALF----- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 612905143 240 kdiseeDANYASGLTAVcsiINGGKQFNSVPDEASLEFNVRPVPEYD 286
Cdd:PRK07522 229 ------DPPYSTLQTGT---IQGGTALNIVPAECEFDFEFRNLPGDD 266
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
12-393 |
1.13e-35 |
|
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: 134.46 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 12 LLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVNEhRANFVAEIGSGSPILALSGHMDVVDAGNQDNWTYPPFQL 91
Cdd:TIGR01246 4 LAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGD-TKNLWATRGTGEPVLAFAGHTDVVPAGPEEQWSSPPFEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 92 TEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKE-----QEGAKLLADKGYLddVDGLMIAEP 166
Cdd:TIGR01246 83 VERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTaidgtKKVVETLMARDEL--IDYCIVGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 167 T-----GSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLlefynqfkekyaelkkndtkheldvAPMFKSLIGKD 241
Cdd:TIGR01246 161 SsvkklGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKA-------------------------APALAELTAIK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 242 ISEEDAnYASGLTAVCSIINGGKQFNSV-PDEASLEFNVRPVPEYDNDFIESFFQNIInnvDSNKLSLDIP--SNHRPVT 318
Cdd:TIGR01246 216 WDEGNE-FFPPTSLQITNIHAGTGANNViPGELYVQFNLRFSTEVSDEILKQRVEAIL---DQHGLDYDLEwsLSGEPFL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 319 SDKNsKLITTIKDVASSYVDKDDIFVSAlvGATDASSFLGDNkdNVDLAIFGPGNPlMAHQIDEY-----IEK--DMYLK 391
Cdd:TIGR01246 292 TNDG-KLIDKAREAIEETNGIKPELSTG--GGTSDGRFIALM--GAEVVEFGPVNA-TIHKVNECvsiedLEKlsDVYQD 365
|
..
gi 612905143 392 YI 393
Cdd:TIGR01246 366 LL 367
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
8-399 |
1.35e-34 |
|
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: 130.93 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 8 EKIQLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVNehraNFVAEIGSGSPILALSGHMDVVdagnqdnwtYP 87
Cdd:cd05653 2 DAVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEAG----NAVGGAGSGPPDVLLLGHIDTV---------PG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 88 PFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQnqlPQGTIRLLATAGEEKEQEGAKLLADKGYldDVDGLMIAEPT 167
Cdd:cd05653 69 EIPVRVEGGVLYGRGAVDAKGPLAAMILAASALNEE---LGARVVVAGLVDEEGSSKGARELVRRGP--RPDYIIIGEPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 168 G-SGIYYAHKGSMSCKVTATGKAVHSSVPfiGDNAIDTLLefynqfkEKYAELKKNDTKHELDVAPMFksligkdiseed 246
Cdd:cd05653 144 GwDGITLGYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLI-------KKWLEVKKWAEGYNVGGRDFD------------ 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 247 anyasglTAVCSIINGGKQFNSVPDEASLEFNVR-PVPEYDNDFIEsffqnIINNVDSNkLSLDIPSNHRPVTSDKNSKL 325
Cdd:cd05653 203 -------SVVPTLIKGGESSNGLPQRAEATIDLRlPPRLSPEEAIA-----LATALLPT-CELEFIDDTEPVKVSKNNPL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 326 ittikdvassyvdkddifVSALVGA-------------TDASSF--LGDNKDnVDLAIFGPGNPLMAHQIDEYIEKDMYL 390
Cdd:cd05653 270 ------------------ARAFRRAirkqggkprlkrkTGTSDMnvLAPLWT-VPIVAYGPGDSTLDHTPNEHIELAEIE 330
|
....*....
gi 612905143 391 KYIDIFKEA 399
Cdd:cd05653 331 RAAAVLKGA 339
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
10-387 |
3.53e-33 |
|
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: 127.01 E-value: 3.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 10 IQLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKV-NEHRANFVAEIGSG-SPILALSGHMDVVdagnqdnwtyP 87
Cdd:cd05652 2 LSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKQPVeNKDRFNVYAYPGSSrQPRVLLTSHIDTV----------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 88 PF---QLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLADKGyLDDVDGLMIA 164
Cdd:cd05652 72 PFipySISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGDGMKAFNDLG-LNTWDAVIFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 165 EPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEkyAELKKNDTKHELDVApmfkslIGKdise 244
Cdd:cd05652 151 EPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLID--ADLPSSELLGPTTLN------IGR---- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 245 edanyasgltavcsiINGGKQFNSVPDEASLEFNVRPV--PEYDNDFIESFFQNIINNVDSnkLSLDIPSNHRPVTSDKN 322
Cdd:cd05652 219 ---------------ISGGVAANVVPAAAEASVAIRLAagPPEVKDIVKEAVAGILTDTED--IEVTFTSGYGPVDLDCD 281
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612905143 323 sklittikdvassyVDKDDIFVSALvgATDASSFLGDNKDnvdlAIFGPGNPLMAHQIDEYIEKD 387
Cdd:cd05652 282 --------------VDGFETDVVAY--GTDIPYLKGDHKR----YLYGPGSILVAHGPDEAITVS 326
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
10-387 |
2.12e-32 |
|
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: 126.00 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 10 IQLLADIVELQTENNNEIDVCNYLKDLFDK--YDiKSEIlkvnEHRANFVAEIGSGSPILALSGHMDVVDAGNQDNWTYP 87
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKlgFD-EVEI----DPMGNVIGYIGGGKKKILFDGHIDTVGIGNIDNWKFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 88 PFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQEG--AKLLADKGYLdDVDGLMIAE 165
Cdd:cd05649 76 PYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLRDFAYTILVAGTVQEEDCDGvcWQYISKADKI-KPDFVVSGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 166 PTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYnqfkEKYAELKKNDTKHEldvapmfksLIGKDISE- 244
Cdd:cd05649 155 PTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADII----QDIRQLNPNFPEAP---------FLGRGTLTv 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 245 EDANYAS-GLTAV---CSI-----INGGKQFNSVPDEASlefNVRPVPEYDNDF------------------IESFFQNI 297
Cdd:cd05649 222 TDIFSTSpSRCAVpdsCRIsidrrLTVGETWEGCLEEIR---ALPAVKKYGDDVavsmynydrpsytgevyeSERYFPTW 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 298 InnvdsnklsldIPSNHRPVtsdknSKLITTIKDV--ASSYVDKddifvsaLVGATDASSFLGDNKdnVDLAIFGPGNPL 375
Cdd:cd05649 299 L-----------LPEDHELV-----KALLEAYKALfgARPLIDK-------WTFSTNGVSIMGRAG--IPCIGFGPGAEN 353
|
410
....*....|..
gi 612905143 376 MAHQIDEYIEKD 387
Cdd:cd05649 354 QAHAPNEYTWKE 365
|
|
| PRK06915 |
PRK06915 |
peptidase; |
61-401 |
9.06e-32 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 124.80 E-value: 9.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 61 GSGSPILaLSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIrLLATAGEE 140
Cdd:PRK06915 91 GGGKSMI-LNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDV-IFQSVIEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 141 kEQEGAKLLAD--KGYldDVDGLMIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEkyAE 218
Cdd:PRK06915 169 -ESGGAGTLAAilRGY--KADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRK--LE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 219 LKKNDTKHEldvaPMFKSL-------IGKdiseedanyasgltavcsiINGGKQFNSVPDEASLEFNVRPVPEYDNDFIE 291
Cdd:PRK06915 244 EKRNDRITD----PLYKGIpipipinIGK-------------------IEGGSWPSSVPDSVILEGRCGIAPNETIEAAK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 292 SFFQNIINNVDSNklslDIPSNHRPVTS------------DKNSKLITTIKdvaSSY--VDKDDIFVSALVGATDASSFl 357
Cdd:PRK06915 301 EEFENWIAELNDV----DEWFVEHPVEVewfgarwvpgelEENHPLMTTLE---HNFveIEGNKPIIEASPWGTDGGLL- 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 612905143 358 gDNKDNVDLAIFGPGNPLMAHQIDEYIEKDmylkyiDIFKEASI 401
Cdd:PRK06915 373 -TQIAGVPTIVFGPGETKVAHYPNEYIEVD------KMIAAAKI 409
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
58-399 |
2.95e-29 |
|
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: 118.12 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 58 AEIGSGSPILALSGHMDVVDAGnqDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATA 137
Cdd:cd03888 65 AEYGEGEEVLGILGHLDVVPAG--EGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 138 GEE----------KEQEGAKLL-----------ADKGYL--------------------------------------DDV 158
Cdd:cd03888 143 DEEtgwkciehyfEHEEYPDFGftpdaefpvinGEKGIVtvdltfkidddkgyrlisikggeatnmvpdkaeavipgKDK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 159 DGLMIAEPTGSGIYYAHKGSMScKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYAElkKNDTKHELDVAPM--FKS 236
Cdd:cd03888 223 EELALSAATDLKGNIEIDDGGV-ELTVTGKSAHASAPEKGVNAITLLAKFLAELNKDGND--KDFIKFLAKNLHEdyNGK 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 237 LIGKDISEEDanyaSG-LTAVCSIINggkqFNsvPDEASLEFNVR-PVPEYDNDFIESffqnIINNVDSNKLSLDIPSNH 314
Cdd:cd03888 300 KLGINFEDEV----MGeLTLNPGIIT----LD--DGKLELGLNVRyPVGTSAEDIIKQ----IEEALEKYGVEVEGHKHQ 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 315 RPVTSDKNSKLITTIKDVASSYVDKDDIFVsALVGATDASSFlgdnKDNVdlaIFG---PGNPLMAHQIDEYIEKDMYLK 391
Cdd:cd03888 366 KPLYVPKDSPLVKTLLKVYEEQTGKEGEPV-AIGGGTYAREL----PNGV---AFGpefPGQKDTMHQANEFIPIDDLIK 437
|
....*...
gi 612905143 392 YIDIFKEA 399
Cdd:cd03888 438 ALAIYAEA 445
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
55-310 |
3.73e-29 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 116.72 E-value: 3.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 55 NFVAEIGSGSPILALSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLL 134
Cdd:PRK13009 49 NLWARRGTEGPHLCFAGHTDVVPPGDLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 135 ATAGEE-KEQEGAK----LLADKGYLddVDGLMIAEPT-----GSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDT 204
Cdd:PRK13009 129 ITSDEEgPAINGTVkvleWLKARGEK--IDYCIVGEPTsterlGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 205 LLEFynqfkekYAELkkndTKHELDvapmfksligkdisEEDANY-ASGLtaVCSIINGGKQFNSV-PDEASLEFNVRPV 282
Cdd:PRK13009 207 AAPA-------LAEL----AATEWD--------------EGNEFFpPTSL--QITNIDAGTGATNViPGELEAQFNFRFS 259
|
250 260
....*....|....*....|....*...
gi 612905143 283 PEYDNDFIESFFQNIInnvDSNKLSLDI 310
Cdd:PRK13009 260 TEHTAESLKARVEAIL---DKHGLDYTL 284
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
10-385 |
4.43e-29 |
|
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: 116.00 E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 10 IQLLADIVELQTENNNEIDVCNYLKDLFDKydikSEILKVNEHRANFVAEIGSGSPI-LALSGHMDVVD-AGNqdnwtYP 87
Cdd:cd05647 2 IELTAALVDIPSVSGNEKPIADEIEAALRT----LPHLEVIRDGNTVVARTERGLASrVILAGHLDTVPvAGN-----LP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 88 PfqLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNqlPQGTIRLLATAGEE--KEQEGAKLLADK-GYLDDVDGLMIA 164
Cdd:cd05647 73 S--RVEEDGVLYGCGATDMKAGDAVQLKLAATLAAAT--LKHDLTLIFYDCEEvaAELNGLGRLAEEhPEWLAADFAVLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 165 EPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTL---LEFYNQFKEKYAELkkndtkheldvapmfksligkd 241
Cdd:cd05647 149 EPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLapiLARLAAYEPRTVNI---------------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 242 iseEDANYASGLTAVcsIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNVDSNKLSLDIPSNHRPVTSdk 321
Cdd:cd05647 207 ---DGLTYREGLNAV--FISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEIEVTDLSPGALPGLD-- 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612905143 322 nsklittiKDVASSYVDKDDIFVSALVGATDASSFLGDNKDNVDlaiFGPGNPLMAHQIDEYIE 385
Cdd:cd05647 280 --------HPVARDLIEAVGGKVRAKYGWTDVARFSALGIPAVN---FGPGDPLLAHKRDEQVP 332
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
12-385 |
3.43e-28 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 114.33 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 12 LLADIVELQTENNNEIDVCNYLKDLF-------DKYDIKSEILKVN----------EHRANFVA---EIGSGSPILALSG 71
Cdd:cd03895 2 FLQDLVRFPSLRGEEAAAQDLVAAALrsrgytvDRWEIDVEKLKHHpgfspvavdyAGAPNVVGthrPRGETGRSLILNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 72 HMDVVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLAD 151
Cdd:cd03895 82 HIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNGALAALM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 152 KGYldDVDGLMIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDT---LLEFYNQFKEKYAELKKNDtKHEL 228
Cdd:cd03895 162 RGY--RADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKamhLIQALQELEREWNARKKSH-PHFS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 229 DVAPMFKSLIGKdiseedanyasgltavcsiINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNVDSNKLSL 308
Cdd:cd03895 239 DHPHPINFNIGK-------------------IEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVADAAATDPWL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 309 dipSNHRP-----------VTSDKNSKLITTIKDVASSYVDKDDIFVSALVGaTDASSFLGDNkdNVDLAIFGPGNpLMA 377
Cdd:cd03895 300 ---SNHPPevewngfqaegYVLEPGSDAEQVLAAAHQAVFGTPPVQSAMTAT-TDGRFFVLYG--DIPALCYGPGS-RDA 372
|
....*...
gi 612905143 378 HQIDEYIE 385
Cdd:cd03895 373 HGFDESVD 380
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
10-387 |
5.17e-28 |
|
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: 113.45 E-value: 5.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 10 IQLLADIVELQ--TENNNEID-VCNYLKDLFDKYDIKSEILKVNEHRANFVAEI-GSGSPILALSGHMDVVdagnqdnwt 85
Cdd:cd03885 2 LDLLERLVNIEsgTYDKEGVDrVAELLAEELEALGFTVERRPLGEFGDHLIATFkGTGGKRVLLIGHMDTV--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 86 YP----PFQ-LTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQEGAK-LLADKGYLDDVd 159
Cdd:cd03885 73 FPegtlAFRpFTVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSReLIEEEAKGADY- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 160 gLMIAEPTGSG--IYYAHKGSMSCKVTATGKAVHSSVPFI-GDNAIDTLLEFYNQFkekyaelkkndtkHELdvapmfks 236
Cdd:cd03885 152 -VLVFEPARADgnLVTARKGIGRFRLTVKGRAAHAGNAPEkGRSAIYELAHQVLAL-------------HAL-------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 237 ligkdiseedANYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNVDSNKLSLDI-PSNHR 315
Cdd:cd03885 210 ----------TDPEKGTTVNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTLVPGTSVELtGGLNR 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612905143 316 PV--TSDKNSKLITTIKDVASSyVDKDDIFVSAlVGATDASSFLGDNKDNVD-LAIFGPGnplmAHQIDEYIEKD 387
Cdd:cd03885 280 PPmeETPASRRLLARAQEIAAE-LGLTLDWEAT-GGGSDANFTAALGVPTLDgLGPVGGG----AHTEDEYLELD 348
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
41-300 |
1.28e-27 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 113.94 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 41 DIksEILKVNEHRANFVAEI---GSGSPILaLSGHMDVVDAGNQDnWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIAL 117
Cdd:PRK09133 78 DI--EVTGPYPRKGNLVARLrgtDPKKPIL-LLAHMDVVEAKRED-WTRDPFKLVEENGYFYGRGTSDDKADAAIWVATL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 118 IELKEQNQLPQGTIRLLATAGEEKEQ-EGAKLLADK-------GY-LDDVDGLMIAEpTGSGIYYAHKGS----MSCKVT 184
Cdd:PRK09133 154 IRLKREGFKPKRDIILALTGDEEGTPmNGVAWLAENhrdlidaEFaLNEGGGGTLDE-DGKPVLLTVQAGektyADFRLE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 185 ATGKAVHSSVPfIGDNAIDTL------LEFYnQFKEKYAELKKNDTKHELDVAP------MfkSLIGKDISEE------- 245
Cdd:PRK09133 233 VTNPGGHSSRP-TKDNAIYRLaaalsrLAAY-RFPVMLNDVTRAYFKQSAAIETgplaaaM--RAFAANPADEaaialls 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 612905143 246 -DANYASGL--TAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINN 300
Cdd:PRK09133 309 aDPSYNAMLrtTCVATMLEGGHAENALPQRATANVNCRIFPGDTIEAVRATLKQVVAD 366
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
6-157 |
1.79e-27 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 112.82 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 6 EKEKIQLLADIVELQTE-----NNNEI--DVCNYLKDLfdKYDIKSEILKVNEhrANFVAEI-GSGSP---ILALSGHMD 74
Cdd:PRK08596 12 KDELLELLKTLVRFETPapparNTNEAqeFIAEFLRKL--GFSVDKWDVYPND--PNVVGVKkGTESDaykSLIINGHMD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 75 VVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLADKGY 154
Cdd:PRK08596 88 VAEVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEVGEAGTLQCCERGY 167
|
...
gi 612905143 155 LDD 157
Cdd:PRK08596 168 DAD 170
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
31-398 |
2.35e-27 |
|
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: 113.12 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 31 NYLKDLFDKYDIKSEILKVNEHRANFVAEiGSGS---PILaLSGHMDVVDA--GNQDNWTYPPFQLTEKDDKLYGRGTTD 105
Cdd:cd05674 35 DYLEKTFPLVHKTLKVEVVNEYGLLYTWE-GSDPslkPLL-LMAHQDVVPVnpETEDQWTHPPFSGHYDGGYIWGRGALD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 106 MKGGLMALVIALIELKEQNQLPQGTIrLLATAGEEKE--QEGAKLLAD---KGYLDD-----VD-GLMIAEPTGSGIYYA 174
Cdd:cd05674 113 DKNSLIGILEAVELLLKRGFKPRRTI-ILAFGHDEEVggERGAGAIAElllERYGVDglaaiLDeGGAVLEGVFLGVPFA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 175 H-----KGSMSCKVTATGKAVHSSVPFIGDN------AIDTLLEfyNQFKEKYAELKKNDT------KHELDVAPMFKSL 237
Cdd:cd05674 192 LpgvaeKGYMDVEITVHTPGGHSSVPPKHTGigilseAVAALEA--NPFPPKLTPGNPYYGmlqclaEHSPLPPRSLKSN 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 238 IGKDISEEDANYASGL--------------TAVcSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNVDs 303
Cdd:cd05674 270 LWLASPLLKALLASELlstspltrallrttQAV-DIINGGVKINALPETATATVNHRIAPGSSVEEVLEHVKNLIADIA- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 304 NKLSL--------DIPSNHR-------------PVTSDKNS--KLIT-TIKDVASSYvdKDDIFV--SALVGATDaSSFL 357
Cdd:cd05674 348 VKYGLglsafggdVIYSTNGtklltsllspepsPVSSTSSPvwQLLAgTIRQVFEQF--GEDLVVapGIMTGNTD-TRHY 424
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 612905143 358 GDNKDNV---DLAIFGPGNPLMAHQIDEYIEKDMYLKYIDIFKE 398
Cdd:cd05674 425 WNLTKNIyrfTPIRLNPEDLGRIHGVNERISIDDYLETVAFYYQ 468
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
32-384 |
3.53e-27 |
|
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: 111.40 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 32 YLKDL----FDKYDIKSEILKvneHRANFVAEIGSGSP-ILALSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDM 106
Cdd:cd05650 35 KLREYgfytLERYDAPDERGI---IRPNIVAKIPGGNDkTLWIISHLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 107 KGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQE-GAKLLADKGYLDDVDGLMI----AEPTGSGIYYAHKGSMSC 181
Cdd:cd05650 112 QQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEyGIQYLLNKFDLFKKDDLIIvpdfGTEDGEFIEIAEKSILWI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 182 KVTATGKAVHSSVPFIGDNAI----DTLLEFYNQFKEKYAElkKND-----------TKHELDVapmfksligkdiseed 246
Cdd:cd05650 192 KVNVKGKQCHASTPENGINAFvaasNFALELDELLHEKFDE--KDDlfnppystfepTKKEANV---------------- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 247 anyasgltavcsiinggKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNVDSN-----KLSLDIPSNHRPVTsDK 321
Cdd:cd05650 254 -----------------PNVNTIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDFENSygagiTYEIVQKEQAPPAT-PE 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612905143 322 NSKLITTIKDVASSYVDKDDIFVSalVGATDASSFLgdNKDNVDLAIFGPGNPlMAHQIDEYI 384
Cdd:cd05650 316 DSEIVVRLSKAIKKVRGREAKLIG--IGGGTVAAFL--RKKGYPAVVWSTLDE-TAHQPNEYI 373
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
8-398 |
2.05e-26 |
|
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: 108.55 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 8 EKIQLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVNEHRANfvAEIGSGSPILALSGHMDVVDAGNqdNWTYP 87
Cdd:cd05651 1 EAIELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRKGNNVWAEN--GHFDEGKPTLLLNSHHDTVKPNA--GWTKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 88 PFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIrLLATAGEEKE-QEGAKLLADkgYLDDVDGLMIAEP 166
Cdd:cd05651 77 PFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGPLNYNLI-YAASAEEEISgKNGIESLLP--HLPPLDLAIVGEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 167 TGSGIYYAHKGSMSCKVTATGKAVHSSVPfIGDNAIdtllefynqfkekYAELKkndtkhelDVApMFKSLIGKDISEed 246
Cdd:cd05651 154 TEMQPAIAEKGLLVLDCTARGKAGHAARN-EGDNAI-------------YKALD--------DIQ-WLRDFRFDKVSP-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 247 anYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNdfiESFFQNIINNVdsnklsldipsnhrpvtsdkNSKLI 326
Cdd:cd05651 209 --LLGPVKMTVTQINAGTQHNVVPDSCTFVVDIRTTEAYTN---EEIFEIIRGNL--------------------KSEIK 263
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612905143 327 TTIKDVASSYVDKDDIFVSALVGA---TDASSFLGD----NKDNVDLaifGPGNPLMAHQIDEYIEKDMYLKYIDIFKE 398
Cdd:cd05651 264 PRSFRLNSSAIPPDHPIVQAAIAAgrtPFGSPTLSDqalmPFPSVKI---GPGDSSRSHTADEFIELSEIEEGIDIYIE 339
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
53-202 |
9.03e-26 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 107.92 E-value: 9.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 53 RANFVAEIGSGSP--ILALSGHMDVVDAGNqdNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGT 130
Cdd:PRK13013 71 RWNLVARRQGARDgdCVHFNSHHDVVEVGH--GWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGS 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612905143 131 IRLLATAGEEKEQ-EGAKLLADKGYL--DDVDGLMIAEPTGSG-IYYAHKGSMSCKVTATGKAVHSSVPFIGDNAI 202
Cdd:PRK13013 149 IEISGTADEESGGfGGVAYLAEQGRFspDRVQHVIIPEPLNKDrICLGHRGVWWAEVETRGRIAHGSMPFLGDSAI 224
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
65-398 |
3.56e-23 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 101.17 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 65 PILaLSGHMDVV--DAGNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKE 142
Cdd:PRK08262 113 PIV-LMAHQDVVpvAPGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 143 QEGAKLLADkgYLDD--------VD-GLMIAE--------PTGS-GIyyAHKGSMSCKVTATGKAVHSSVPFiGDNAIDT 204
Cdd:PRK08262 192 GLGARAIAE--LLKErgvrlafvLDeGGAITEgvlpgvkkPVALiGV--AEKGYATLELTARATGGHSSMPP-RQTAIGR 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 205 LLEFynqfkekYAELKKNDTKHELD--VAPMFKSLiGKDISEEDANYASGL------------------------TAVcS 258
Cdd:PRK08262 267 LARA-------LTRLEDNPLPMRLRgpVAEMFDTL-APEMSFAQRVVLANLwlfeplllrvlakspetaamlrttTAP-T 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 259 IINGGKQFNSVPDEASLEFNVRPVPeydNDFIESFFQNIINNVDSNKLS---LDIPSNHRPVTSDKN---SKLITTIKDv 332
Cdd:PRK08262 338 MLKGSPKDNVLPQRATATVNFRILP---GDSVESVLAHVRRAVADDRVEievLGGNSEPSPVSSTDSaayKLLAATIRE- 413
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612905143 333 assyVDKDDIFVSALV-GATDASSFLGDNkDNV-----------DLAIFgpgnplmaHQIDEYIEKDMYLKYIDIFKE 398
Cdd:PRK08262 414 ----VFPDVVVAPYLVvGATDSRHYSGIS-DNVyrfsplrlspeDLARF--------HGTNERISVANYARMIRFYYR 478
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
26-298 |
5.85e-23 |
|
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: 99.47 E-value: 5.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 26 EIDVCNYLKDLFDKYDIKSEILKVNEHRANFVAEI-GSGS-PILALSGHMDVVdagNQDNWTYPPFQLTEKDDKLYGRGT 103
Cdd:cd08013 28 EAEIATYVAAWLAHRGIEAHRIEGTPGRPSVVGVVrGTGGgKSLMLNGHIDTV---TLDGYDGDPLSGEIADGRVYGRGT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 104 TDMKGGLMALVIALIELKEQNqlPQGTIRLLATAGEEKEQEGAKLLADKGYldDVDGLMIAEPTGSGIYYAHKGSMSCKV 183
Cdd:cd08013 105 LDMKGGLAACMAALADAKEAG--LRGDVILAAVADEEDASLGTQEVLAAGW--RADAAIVTEPTNLQIIHAHKGFVWFEV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 184 TATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYAELKKndtkheldvapmfksligkdiSEEDANYASGlTAVCSIINGG 263
Cdd:cd08013 181 DIHGRAAHGSRPDLGVDAILKAGYFLVALEEYQQELPE---------------------RPVDPLLGRA-SVHASLIKGG 238
|
250 260 270
....*....|....*....|....*....|....*
gi 612905143 264 KQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNII 298
Cdd:cd08013 239 EEPSSYPARCTLTIERRTIPGETDESVLAELTAIL 273
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
29-384 |
8.23e-23 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 99.15 E-value: 8.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 29 VCNYLKDLFDK----YDIKSEILKvNEHRANFVAEI--GSGSPILALSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRG 102
Cdd:PRK13983 36 LESLLKEYGFDeverYDAPDPRVI-EGVRPNIVAKIpgGDGKRTLWIISHMDVVPPGDLSLWETDPFKPVVKDGKIYGRG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 103 TTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEkeqEGAK-----LLADKGYLDDVDGLMI----AEPTGSGIYY 173
Cdd:PRK13983 115 SEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEE---TGSKygiqyLLKKHPELFKKDDLILvpdaGNPDGSFIEI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 174 AHKGSMSCKVTATGKAVHSSVPFIGDNA----IDTLLEFYNQFKEKYAElkKND-----------TKHEldvapmfksli 238
Cdd:PRK13983 192 AEKSILWLKFTVKGKQCHASTPENGINAhraaADFALELDEALHEKFNA--KDPlfdppystfepTKKE----------- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 239 gkdiseedANyasgltaVCSIinggkqfNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNVDSN---KLSLDI--PSN 313
Cdd:PRK13983 259 --------AN-------VDNI-------NTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIADEFEEEygvKIEVEIvqREQ 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612905143 314 HRPVTsDKNSKLITTIKDVASSyVDKDDIFVSALVGATDASSFlgdNKDNVDLAIFGPGNPlMAHQIDEYI 384
Cdd:PRK13983 317 APPPT-PPDSEIVKKLKRAIKE-VRGIEPKVGGIGGGTVAAFL---RKKGYPAVVWSTLDE-TAHQPNEYA 381
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
58-399 |
5.92e-22 |
|
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: 97.06 E-value: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 58 AEIGSGSPILALSGHMDVVDAGnqDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATA 137
Cdd:TIGR01887 61 IEYGQGEEVLGILGHLDVVPAG--DGWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGT 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 138 GEEKEQEGAKL------LADKGYLDDVDGLMIaeptgsgiyYAHKGSMSCKVTATGKAVHSSV--PFIGDNAIDTL---- 205
Cdd:TIGR01887 139 DEESGWKCIDYyfeheeMPDIGFTPDAEFPII---------YGEKGITTLEIKFKDDTEGDVVleSFKAGEAYNMVpdha 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 206 ------LEFYNQFKEKYAELKKNDTKHELDVAPMFKSLIGKDISEEDANYASGLTAVCSIINGGKQFNsvpdeaslefnv 279
Cdd:TIGR01887 210 tavisgKKLTEVEQLKFVFFIAKELEGDFEVNDGTLTITLEGKSAHGSAPEKGINAATYLALFLAQLN------------ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 280 rpVPEYDNDFIESFFQNIINNVDSNKLSLD-------------------------IPSNHR-PVTSDKNSKL------IT 327
Cdd:TIGR01887 278 --LAGGAKAFLQFLAEYLHEDHYGEKLGIKfhddvsgdltmnvgvidyenaeaglIGLNVRyPVGNDPDTMLknelakES 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 328 TIKDV------ASSYVDKDDIFVSALV-----------------GATDASSFlgdnKDNVDL-AIFgPGNPLMAHQIDEY 383
Cdd:TIGR01887 356 GVVEVtlngylKPLYVPKDDPLVQTLMkvyekqtgdegepvaigGGTYARLM----PNGVAFgALF-PGEEDTMHQANEY 430
|
410
....*....|....*.
gi 612905143 384 IEKDMYLKYIDIFKEA 399
Cdd:TIGR01887 431 IMIDDLLLATAIYAEA 446
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
2-399 |
7.28e-22 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 95.79 E-value: 7.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 2 TTFSEKEKIQLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVnehrANFVAEIGSGSPILALSGHMDVVdAGnq 81
Cdd:PRK04443 1 MTISALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREAWVDEA----GNARGPAGDGPPLVLLLGHIDTV-PG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 82 dnwtYPPFQLteKDDKLYGRGTTDMKGGLMALVIALIELKeqnQLPQGTIRLLATAGEE-KEQEGAKLLADKGYLDDVdg 160
Cdd:PRK04443 74 ----DIPVRV--EDGVLWGRGSVDAKGPLAAFAAAAARLE---ALVRARVSFVGAVEEEaPSSGGARLVADRERPDAV-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 161 lMIAEPTG-SGIYYAHKGSMSCKVTATGKAVHSSVPfiGDNAIDTLLEFYNQFKEkYAELKKNDTkheldvaPMFKSLIG 239
Cdd:PRK04443 143 -IIGEPSGwDGITLGYKGRLLVTYVATSESFHSAGP--EPNAAEDAIEWWLAVEA-WFEANDGRE-------RVFDQVTP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 240 K--DI-SEEDanyasGLTavcsiinggkqfnsvpDEASLEFNVRPVPEYDNDFIESFFQNIINNVDSNkLSLDIPsnhrP 316
Cdd:PRK04443 212 KlvDFdSSSD-----GLT----------------VEAEMTVGLRLPPGLSPEEAREILDALLPTGTVT-FTGAVP----A 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 317 VTSDKNSKLITTikdvassyvdkddiFVSALVGATDASSFL---GDNKDNV-------DLAIFGPGNPLMAHQIDEYIEK 386
Cdd:PRK04443 266 YMVSKRTPLARA--------------FRVAIREAGGTPRLKrktGTSDMNVvapawgcPMVAYGPGDSDLDHTPDEHLPL 331
|
410
....*....|...
gi 612905143 387 DMYLKYIDIFKEA 399
Cdd:PRK04443 332 AEYLRAIAVLTDV 344
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
55-167 |
5.21e-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: 90.18 E-value: 5.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 55 NFVAEIGSGS--PILALSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIR 132
Cdd:cd18669 1 NVIARYGGGGggKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 612905143 133 LLATAGEEKEQEGAKLLADKGYL---DDVDGLMIAEPT 167
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLSKDALeedLKVDYLFVGDAT 118
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
11-286 |
8.59e-21 |
|
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: 93.55 E-value: 8.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 11 QLLADIVELQTENNNEID------VCNYLKDLFDKYDIKSEILKvNEHRANFV-AEIGS--GSPILALSGHMDVVDAGNQ 81
Cdd:cd03893 2 QTLAELVAIPSVSAQPDRreelrrAAEWLADLLRRLGFTVEIVD-TSNGAPVVfAEFPGapGAPTVLLYGHYDVQPAGDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 82 DNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQEG-AKLLADKGYLDDVDG 160
Cdd:cd03893 81 DGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEESGSPSlDQLVEAHRDLLAADA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 161 LMIAEPTGSG-----IYYAHKGSMSCKVTATG--KAVHSSVpFIG--DNAI---------------DTLLEFYNQFKEKY 216
Cdd:cd03893 161 IVISDSTWVGqeqptLTYGLRGNANFDVEVKGldHDLHSGL-YGGvvPDPMtalaqllaslrdetgRILVPGLYDAVREL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 217 AELKKNDTKHELDVAPMFKSLIGKDISEEDANYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYD 286
Cdd:cd03893 240 PEEEFRLDAGVLEEVEIIGGTTGSVAERLWTRPALTVLGIDGGFPGEGSKTVIPPRARAKISIRLVPGQD 309
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
24-398 |
9.56e-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: 93.56 E-value: 9.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 24 NNEIDVC-NYLKDLFDKYDIKSEILKVNEHRANFvAEIGSGS-PILALSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGR 101
Cdd:cd05681 18 GRGIPETaDFLKEFLRRLGAEVEIFETDGNPIVY-AEFNSGDaKTLLFYNHYDVQPAEPLELWTSDPFELTIRNGKLYAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 102 GTTDMKGGLMALVIALIELKEQ-NQLPQgTIRLLATAGEEK---------EQEGAKLLAD-----KGYLDDVDGLMIAEP 166
Cdd:cd05681 97 GVADDKGELMARLAALRALLQHlGELPV-NIKFLVEGEEEVgspnlekfvAEHADLLKADgciweGGGKNPKGRPQISLG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 167 TGSGIYYahkgSMSCKVTAtgKAVHSSVPFIGDN-------AIDTLLE---------FYNQFKEKYAELKKNDTKHELDV 230
Cdd:cd05681 176 VKGIVYV----ELRVKTAD--FDLHSSYGAIVENpawrlvqALNSLRDedgrvlipgFYDDVRPLSEAERALIDTYDFDP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 231 APMFKSLIGKD-ISEEDANYASGLTA--VCSI--INGGKQFNS----VPDEASLEFNVRPVPEYDNDFIESFFQNIINNV 301
Cdd:cd05681 250 EELRKTYGLKRpLQVEGKDPLRALFTepTCNIngIYSGYTGEGsktiLPSEAFAKLDFRLVPDQDPAKILSLLRKHLDKN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 302 DSNKLSLDIPSNHRPVTSDKNSKLITTIKDVASSYVDKDDIFVSALVGATDASSFLGDNKDNVDLaiFGPGNP-LMAHQI 380
Cdd:cd05681 330 GFDDIEIHDLLGEKPFRTDPDAPFVQAVIESAKEVYGQDPIVLPNSAGTGPMYPFYDALEVPVVA--IGVGNAgSNAHAP 407
|
410
....*....|....*...
gi 612905143 381 DEYIEKDMYLKYIDIFKE 398
Cdd:cd05681 408 NENIRIADYYKGIEHTEE 425
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
67-280 |
4.01e-20 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 91.60 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 67 LALSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQEGA 146
Cdd:PRK06837 100 LILQGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEESTGNGA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 147 KLLADKGYldDVDGLMIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYAELKKNDTKH 226
Cdd:PRK06837 180 LSTLQRGY--RADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRELEAEWNARKASD 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 612905143 227 eldvaPMFKSLigkdisEEDANYASGltavcsIINGGKQFNSVPdeASLEFNVR 280
Cdd:PRK06837 258 -----PHFEDV------PHPINFNVG------IIKGGDWASSVP--AWCDLDCR 292
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
8-398 |
4.06e-20 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 90.59 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 8 EKIQLLADIVELQTENNNEIDVCNYLKDLFDK--YDIKSEilkVNEHRANFVAeigSGSPILALSGHMDVVDAgnqdnwT 85
Cdd:PRK08652 3 RAKELLKQLVKIPSPSGQEDEIALHIMEFLESlgYDVHIE---SDGEVINIVV---NSKAELFVEVHYDTVPV------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 86 YPPFqltEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATagEEKEQEGAKLLADK---GYLddvdglM 162
Cdd:PRK08652 71 AEFF---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSD--EEEGGRGSALFAERyrpKMA------I 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 163 IAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEkyaelkkndtkHELDVAPMFKSLIGkdi 242
Cdd:PRK08652 140 VLEPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKE-----------LLKALGKYFDPHIG--- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 243 seedanyasgltavCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNVDSNKLSLDIPSNHRpvtSDKN 322
Cdd:PRK08652 206 --------------IQEIIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEYTEIWDGFE---LDED 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 323 SKLITTIKDvASSYVDKDDIFVsALVGATDASSFlgdnKDN-VDLAIFGPGNPLMAHQIDEYIE-------KDMYLKYID 394
Cdd:PRK08652 269 EEIVQLLEK-AMKEVGLEPEFT-VMRSWTDAINF----RYNgTKTVVWGPGELDLCHTKFERIDvrevekaKEFLKALNE 342
|
....
gi 612905143 395 IFKE 398
Cdd:PRK08652 343 ILLE 346
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
55-157 |
4.91e-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: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 55 NFVAEIGSGS--PILALSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIR 132
Cdd:cd03873 1 NLIARLGGGEggKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
|
90 100
....*....|....*....|....*
gi 612905143 133 LLATAGEEKEQEGAKLLADKGYLDD 157
Cdd:cd03873 81 VAFTADEEVGSGGGKGLLSKFLLAE 105
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
173-301 |
8.13e-20 |
|
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: 83.93 E-value: 8.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 173 YAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYaelkkndtkheldvapmfksligkdisEEDANYASG 252
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEY---------------------------GDIGFDFPR 53
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 612905143 253 LTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNV 301
Cdd:pfam07687 54 TTLNITGIEGGTATNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEKE 102
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
65-398 |
3.02e-19 |
|
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: 88.48 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 65 PILALSGHMDVVDAgNQDNWTYPPFQlTEKDDK--LYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEE-K 141
Cdd:cd05646 65 PSILLNSHTDVVPV-FEEKWTHDPFS-AHKDEDgnIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEiG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 142 EQEGAKLLADKGY---------LDdvDGLmiAEPTGS-GIYYAHKGSMSCKVTATGKAVHSSVpFIGDNAIDTLLEFYNQ 211
Cdd:cd05646 143 GHDGMEKFVKTEEfkklnvgfaLD--EGL--ASPTEEyRVFYGERSPWWVVITAPGTPGHGSK-LLENTAGEKLRKVIES 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 212 F----KEKYAELKKNDTKHELDVapmfksligkdiseedanyasglTAV-CSIINGGKQFNSVPDEASLEFNVRPVPEYD 286
Cdd:cd05646 218 ImefrESQKQRLKSNPNLTLGDV-----------------------TTVnLTMLKGGVQMNVVPSEAEAGFDLRIPPTVD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 287 -NDF---IESFFQNIINNVdsnKLSLDIPSNHRPVTS--DKN---SKLITTIKDVASSYvdKDDIFvsalVGATDaSSFL 357
Cdd:cd05646 275 lEEFekqIDEWCAEAGRGV---TYEFEQKSPEKDPTSldDSNpwwAAFKKAVKEMGLKL--KPEIF----PAATD-SRYI 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 612905143 358 gdnkDNVDLAIFG--PGN--PLMAHQIDEYIEKDMYLKYIDIFKE 398
Cdd:cd05646 345 ----RALGIPALGfsPMNntPILLHDHNEFLNEDVFLRGIEIYEK 385
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
58-399 |
5.11e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 88.60 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 58 AEIGSGSPILALSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATA 137
Cdd:PRK07205 69 AEIGQGEELLAILCHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 138 GEE---------KEQEGaklLADKGYLDDVDGLMIaeptgsgiyYAHKGSMSCKVTATGK------------AVHSSVPF 196
Cdd:PRK07205 149 DEEtlwrcmnryNEVEE---QATMGFAPDSSFPLT---------YAEKGLLQAKLVGPGSdqlelevgqafnVVPAKASY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 197 IGDnaidtllefynqfkeKYAELKKNDTKHELDVAPMFKSL--IGKDISEEDAnyASGLTAvcsIINGGKQFNSVPDEAS 274
Cdd:PRK07205 217 QGP---------------KLEAVKKELDKLGFEYVVKENEVtvLGKSVHAKDA--PQGINA---VIRLAKALVVLEPHPA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 275 LEFNVRPVPEYDNDFiesffqNIINNVD---SNKLS-----LDIPSNHR--------PVTSDKNsKLITTIKDVASS--- 335
Cdd:PRK07205 277 LDFLANVIGEDATGL------NIFGDIEdepSGKLSfniagLTITKEKSeiridiriPVLADKE-KLVQQLSQKAQEygl 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 336 -----------YVDKDDIFVSALV-----------------GATDASSFlgdnkDN-VDL-AIFgPGNPLMAHQIDEYIE 385
Cdd:PRK07205 350 tyeefdylaplYVPLDSELVSTLMsvyqektgddspaqssgGATFARTM-----PNcVAFgALF-PGAPQTEHQANEHIV 423
|
410
....*....|....*
gi 612905143 386 -KDMYlKYIDIFKEA 399
Cdd:PRK07205 424 lEDLY-RAMDIYAEA 437
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
10-164 |
3.04e-18 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 85.98 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 10 IQLLADIVELQTENNNEI------DVCNYLKDLFDKYDIKSEILKVNEHRAnFVAEIGSGSPILALSGHMDVVDAgNQDN 83
Cdd:PRK08554 4 LELLSSLVSFETVNDPSKgikpskECPKFIKDTLESWGIESELIEKDGYYA-VYGEIGEGKPKLLFMAHFDVVPV-NPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 84 WTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQlpQGTIRLLATAGEEKEQEGAKLLADK--------GYL 155
Cdd:PRK08554 82 WNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPL--NGKVIFAFTGDEEIGGAMAMHIAEKlreegklpKYM 159
|
....*....
gi 612905143 156 DDVDGLMIA 164
Cdd:PRK08554 160 INADGIGMK 168
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
65-396 |
3.37e-17 |
|
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: 82.53 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 65 PILALSGHMDVVDAgNQDNWTYPPFQ-LTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEE-KE 142
Cdd:TIGR01880 72 PSILLNSHTDVVPV-FREHWTHPPFSaFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEiGG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 143 QEGAKLLADK--------GYLDDvDGLmiAEPTGS-GIYYAHKGSMSCKVTATGKAVHSSVpFIGDNAIDTLLEFYN--- 210
Cdd:TIGR01880 151 HDGMEKFAKTdefkalnlGFALD-EGL--ASPDDVyRVFYAERVPWWVVVTAPGNPGHGSK-LMENTAMEKLEKSVEsir 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 211 QFKEKYAELKKNdtkheldvapmfksliGKDISEEDAnyasgLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFI 290
Cdd:TIGR01880 227 RFRESQFQLLQS----------------NPDLAIGDV-----TSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEM 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 291 E----SFFQNIINNVDsnkLSLDIPSNHRPVT--SDKN---SKLITTIKDVASSYvdKDDIFvsalVGATDASSFlgdNK 361
Cdd:TIGR01880 286 EnrldEWCADAGEGVT---YEFSQHSGKPLVTphDDSNpwwVAFKDAVKEMGCTF--KPEIL----PGSTDSRYI---RA 353
|
330 340 350
....*....|....*....|....*....|....*..
gi 612905143 362 DNVDLAIFGPGN--PLMAHQIDEYIEKDMYLKYIDIF 396
Cdd:TIGR01880 354 AGVPALGFSPMNntPVLLHDHNEFLNEAVFLRGIEIY 390
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
53-391 |
1.78e-16 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 80.22 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 53 RANFVAEI-GSGS-PILALSGHMDVVDAGnQDNWTyppfqLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGT 130
Cdd:cd03896 41 RGNVVGRLrGTGGgPALLFSAHLDTVFPG-DTPAT-----VRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 131 IRLLATAGEEKEQE--GAK-LLADKGYLddVDGLMIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLle 207
Cdd:cd03896 115 VVFAANVGEEGLGDlrGARyLLSAHGAR--LDYFVVAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAM-- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 208 fynqfkekyaelkkndtkheldvapmfkSLIGKDISEEDANYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDN 287
Cdd:cd03896 191 ----------------------------AKLVEALYEWAAPYVPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPDAEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 288 DFIESFFQNIINNVDSNKLSLDI---PSNHRPVTSDKNSKLITTIKDVASSYVDKDDIFVSALVGATDASSfLGdnkdnV 364
Cdd:cd03896 243 ADVQREVEAVVSKLAAKHLRVKArvkPVGDRPGGEAQGTEPLVNAAVAAHREVGGDPRPGSSSTDANPANS-LG-----I 316
|
330 340
....*....|....*....|....*..
gi 612905143 365 DLAIFGPGNPLMAHQIDEYIEKDMYLK 391
Cdd:cd03896 317 PAVTYGLGRGGNAHRGDEYVLKDDMLK 343
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
31-398 |
2.23e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 80.57 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 31 NYLKDLFDKYDIKSEILKvneHRANFV--AEIGSGS-PILALSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDMK 107
Cdd:PRK06446 29 NYLKDTMEKLGIKANIER---TKGHPVvyGEINVGAkKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 108 GGLMALVIALIELKEQNQLPQgTIRLLAtagEEKEQEGAKLLADkgYLDDVDGLMIAEPT---GSG--------IYYAHK 176
Cdd:PRK06446 106 GTLMARLFAIKHLIDKHKLNV-NVKFLY---EGEEEIGSPNLED--FIEKNKNKLKADSVimeGAGldpkgrpqIVLGVK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 177 GSMSCKVTA-TG-KAVHSS-VPFIGDNAID---------------TLLEFYNQFKEKYAELKKNDTKHELDVAPMFKSLI 238
Cdd:PRK06446 180 GLLYVELVLrTGtKDLHSSnAPIVRNPAWDlvkllstlvdgegrvLIPGFYDDVRELTEEERELLKKYDIDVEELRKALG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 239 GKDIS-EEDANYASGLTA--VCSI------INGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNVDSNkLSLD 309
Cdd:PRK06446 260 FKELKySDREKIAEALLTepTCNIdgfysgYTGKGSKTIVPSRAFAKLDFRLVPNQDPYKIFELLKKHLQKVGFN-GEII 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 310 IPSNHRPVTSDKNSKLITTIKDVASSYVDKDDIFVSALVGATDASSFLGDNKDNVDLAIFGPGNPLM-AHQIDEYIEKDM 388
Cdd:PRK06446 339 VHGFEYPVRTSVNSKVVKAMIESAKRVYGTEPVVIPNSAGTQPMGLFVYKLGIRDIVSAIGVGGYYSnAHAPNENIRIDD 418
|
410
....*....|
gi 612905143 389 YLKYIDIFKE 398
Cdd:PRK06446 419 YYKAIKHTEE 428
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
58-401 |
2.32e-16 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 80.66 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 58 AEIGSGSPILALSGHMDVVDAGnqDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATA 137
Cdd:PRK07318 73 IEYGEGEEVLGILGHLDVVPAG--DGWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRFIVGT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 138 GEEK---------EQEGAKLL------------ADKG----YLDDVDGlmiaEPTG--------SGIYY----------- 173
Cdd:PRK07318 151 DEESgwkcmdyyfEHEEAPDFgfspdaefpiinGEKGittfDLVHFEG----ENEGdyvlvsfkSGLREnmvpdsaeavi 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 174 ------------------------AHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKekyaelKKNDTKHELD 229
Cdd:PRK07318 227 tgddlddliaafeaflaenglkgeLEEEGGKLVLTVIGKSAHGSTPEKGVNAATYLAKFLNQLN------LDGDAKAFLD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 230 VAP--MFKSLIGK--DISEEDAnyASG-LTAVCSIINGGKQfnsvpDEASLEFNVR-PVpEYDNDFIESFFQNIINNVDs 303
Cdd:PRK07318 301 FAAeyLHEDTRGEklGIAYEDD--VMGdLTMNVGVFSFDEE-----KGGTLGLNFRyPV-GTDFEKIKAKLEKLIGVTG- 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 304 nkLSLDIPSNHRPVTSDKNSKLITTIKDVassYVDKDDIFVSALV--GATDASSFlgdnKDNVDL-AIFgPGNPLMAHQI 380
Cdd:PRK07318 372 --VELSEHEHQKPHYVPKDDPLVKTLLKV---YEKQTGLKGEEQVigGGTYARLL----KRGVAFgAMF-PGSEDTMHQA 441
|
410 420
....*....|....*....|.
gi 612905143 381 DEYIEKDmylkyiDIFKEASI 401
Cdd:PRK07318 442 NEYIEID------DLIKAAAI 456
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
53-304 |
2.48e-16 |
|
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: 80.20 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 53 RANFVAEIGSGSP--ILALSG-HMDVVDAgNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLmALVIAL-IELKEQNQLPQ 128
Cdd:cd08012 64 RGNIIVEYPGTVDgkTVSFVGsHMDVVTA-NPETWEFDPFSLSIDGDKLYGRGTTDCLGHV-ALVTELfRQLATEKPALK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 129 GTIRLLATAGEEKEQ---EGAKLLADKGYLDDV-DGLMI------AEPT-GSGiyyahkGSMSCKVTATGKAVHSSVPFI 197
Cdd:cd08012 142 RTVVAVFIANEENSEipgVGVDALVKSGLLDNLkSGPLYwvdsadSQPCiGTG------GMVTWKLTATGKLFHSGLPHK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 198 GDNAIDTLLE--------FYNQFKekyaelkkndtKHEldvapmfksligkdiSEEDANYASGLT---AVCSIINGGkqF 266
Cdd:cd08012 216 AINALELVMEalaeiqkrFYIDFP-----------PHP---------------KEEVYGFATPSTmkpTQWSYPGGS--I 267
|
250 260 270
....*....|....*....|....*....|....*...
gi 612905143 267 NSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNVDSN 304
Cdd:cd08012 268 NQIPGECTICGDCRLTPFYDVKEVREKLEEYVDDINAN 305
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
4-401 |
5.54e-15 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 75.59 E-value: 5.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 4 FSEKEKI-----QLLADIVELQTENNNEidvcNYLKDLFDKydIKSEI---LKVNEHRANFVaeigSGSPILALSGHMDV 75
Cdd:PRK00466 2 QQEKELVkqkakELLLDLLSIYTPSGNE----TNATKFFEK--ISNELnlkLEILPDSNSFI----LGEGDILLASHVDT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 76 VdagnqdnwtyPPF-QLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQlpqgTIRLLATAGEEKEQEGAKLLADKGy 154
Cdd:PRK00466 72 V----------PGYiEPKIEGEVIYGRGAVDAKGPLISMIIAAWLLNEKGI----KVMVSGLADEESTSIGAKELVSKG- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 155 lDDVDGLMIAEPT-GSGIYYAHKGSMSCKVTATGKAVHSSVPfiGDNAIDTLLefynqfkekyaelkkndtkheldvapm 233
Cdd:PRK00466 137 -FNFKHIIVGEPSnGTDIVVEYRGSIQLDIMCEGTPEHSSSA--KSNLIVDIS--------------------------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 234 fKSLIgkDISEEDANYASgLTAVCSIINGGKQFNSVPDEASLEFNVR-PVPEYDNDFI----ESFFQNIINNVDsnklsl 308
Cdd:PRK00466 187 -KKII--EVYKQPENYDK-PSIVPTIIRAGESYNVTPAKLYLHFDVRyAINNKRDDLIseikDKFQECGLKIVD------ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 309 DIPsnhrPVTSDKNSkliTTIKDVASSYVD---KDDIFVSAlvGATDAsSFLGDNKDNVdlAIFGPGNPLMAHQIDEYIE 385
Cdd:PRK00466 257 ETP----PVKVSINN---PVVKALMRALLKqniKPRLVRKA--GTSDM-NILQKITTSI--ATYGPGNSMLEHTNQEKIT 324
|
410
....*....|....*.
gi 612905143 386 KDmylkyiDIFKEASI 401
Cdd:PRK00466 325 LD------EIYIAVKT 334
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
5-390 |
1.38e-14 |
|
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349932 [Multi-domain] Cd Length: 368 Bit Score: 74.41 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 5 SEKEKIQLLADIVELQTENNNEIDVCNYLKDLFDKYDikseiLKVNEHRANFVAEIGSGS------------PILALSGH 72
Cdd:cd05683 1 NEDRLINTFLELVQIDSETLHEKEISKVLKKKFENLG-----LSVIEDDAGKTTGGGAGNlictlkadkeevPKILFTSH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 73 MDVVDAGNQDnwtyPPFQltEKDDKLYGRGTT----DMKGGLMALVIALIELKEQNqLPQGTIRLLATAGEEKEQEGAKL 148
Cdd:cd05683 76 MDTVTPGINV----KPPQ--IADGYIYSDGTTilgaDDKAGIAAILEAIRVIKEKN-IPHGQIQFVITVGEESGLVGAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 149 L------ADKGYLDDVDG----LMIAEPTGSGIYyahkgsmsckVTATGKAVHSSV-PFIGDNAIDTLLEFYNQFKekya 217
Cdd:cd05683 149 LdpelidADYGYALDSEGdvgtIIVGAPTQDKIN----------AKIYGKTAHAGTsPEKGISAINIAAKAISNMK---- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 218 elkkndtkheldvapmfkslIGKdISEEDanyasglTAVCSIINGGKQFNSVPDEASLEFNVRpvpEYDNDFIES----F 293
Cdd:cd05683 215 --------------------LGR-IDEET-------TANIGKFQGGTATNIVTDEVNIEAEAR---SLDEEKLDAqvkhM 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 294 FQNIINNVDSNKLSLDIPSN--HRPVTSDKNSKLITTIKDVASSYVDKDDIFVSAlvGATDASSFLGDNKDNVDLAIfGP 371
Cdd:cd05683 264 KETFETTAKEKGAHAEVEVEtsYPGFKINEDEEVVKLAKRAANNLGLEINTTYSG--GGSDANIINGLGIPTVNLGI-GY 340
|
410 420
....*....|....*....|
gi 612905143 372 GNplmAHQIDEYIE-KDMYL 390
Cdd:cd05683 341 EN---IHTTNERIPiEDLYD 357
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
63-192 |
1.70e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 74.56 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 63 GSPILALSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEqnQLPQGtIRLLAtAGEEkE 142
Cdd:PRK07907 82 GAPTVLLYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRALGG--DLPVG-VTVFV-EGEE-E 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612905143 143 QEGA---KLLADKGYLDDVDGLMIA--------EPTgsgIYYAHKGSMSCKVTAT--GKAVHS 192
Cdd:PRK07907 157 MGSPsleRLLAEHPDLLAADVIVIAdsgnwsvgVPA---LTTSLRGNADVVVTVRtlEHAVHS 216
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
32-207 |
4.07e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 73.35 E-value: 4.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 32 YLKDLFDKYDIKSEILKVNEHRANFVAEIG---SGSPILALSGHMDVVDAgNQDNWTYPPFQLTEKDDKLYGRGTTDMKg 108
Cdd:PRK07906 30 YVAEKLAEVGLEPTYLESAPGRANVVARLPgadPSRPALLVHGHLDVVPA-EAADWSVHPFSGEIRDGYVWGRGAVDMK- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 109 GLMALVIALI-ELKEQNQLPQGTIRLLATAGEEKEQE-GAKLLADK--GYLDDVD-------GLMIAEPTGSGIYY---A 174
Cdd:PRK07906 108 DMDAMMLAVVrHLARTGRRPPRDLVFAFVADEEAGGTyGAHWLVDNhpELFEGVTeaisevgGFSLTVPGRDRLYLietA 187
|
170 180 190
....*....|....*....|....*....|...
gi 612905143 175 HKGSMSCKVTATGKAVHSSVPfIGDNAIDTLLE 207
Cdd:PRK07906 188 EKGLAWMRLTARGRAGHGSMV-NDDNAVTRLAE 219
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
59-300 |
6.33e-14 |
|
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.
Pssm-ID: 349869 [Multi-domain] Cd Length: 394 Bit Score: 72.59 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 59 EIGSGSPILALSGHMDVVDAGnqDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAG 138
Cdd:cd02697 68 RYGDGGRTVALNAHGDVVPPG--DGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 139 EEKEQE-GAKLLADKGyLDDVDgLMIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYA 217
Cdd:cd02697 146 EEFGGElGPGWLLRQG-LTKPD-LLIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 218 ELKKNDTKHELDVAPMFKslIGKdiseedanyasgltavcsiINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNI 297
Cdd:cd02697 224 QYRQVSSQVEGITHPYLN--VGR-------------------IEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRV 282
|
...
gi 612905143 298 INN 300
Cdd:cd02697 283 IAD 285
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
71-165 |
3.65e-13 |
|
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: 70.71 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 71 GHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALvIALIE--LKEQNQLPQgTIRLLATAGEEKEQEG-AK 147
Cdd:cd05676 92 GHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGW-LNAIEayQKLGQELPV-NLKFCFEGMEESGSEGlDE 169
|
90 100
....*....|....*....|
gi 612905143 148 LLADKG--YLDDVDGLMIAE 165
Cdd:cd05676 170 LIEARKdtFFSDVDYVCISD 189
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
69-333 |
4.69e-13 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 69.99 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 69 LSGHMDVVdagnqdnwtYP---PFQLTE--KDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKEQ 143
Cdd:PRK07338 97 LTGHMDTV---------FPadhPFQTLSwlDDGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLGYDVLINPDEEIGS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 144 EG-AKLLAD--KGYlddvDGLMIAEP-----TGSGiyyAHKGSMSCKVTATGKAVHSS-VPFIGDNAIDTLLEFynqfke 214
Cdd:PRK07338 168 PAsAPLLAElaRGK----HAALTYEPalpdgTLAG---ARKGSGNFTIVVTGRAAHAGrAFDEGRNAIVAAAEL------ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 215 kyaelkkndtkheldvAPMFKSLIGKdiseedanyASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFF 294
Cdd:PRK07338 235 ----------------ALALHALNGQ---------RDGVTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAEL 289
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 612905143 295 QNIINNVDSNK-LSLDIPSN-HRPVT--SDKNSKLITTIKDVA 333
Cdd:PRK07338 290 KKLIAQVNQRHgVSLHLHGGfGRPPKpiDAAQQRLFEAVQACG 332
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
63-394 |
2.56e-12 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 67.53 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 63 GSPILALSGHMDVVDAgnQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALielkeqnQLPQGTIRLLATAGEEKE 142
Cdd:PRK08737 62 GTPKYLFNVHLDTVPD--SPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAA-------NAGDGDAAFLFSSDEEAN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 143 QEgaklLADKGYLD---DVDGLMIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPF-IGDNAIDTLLEFYNQFKEkYAE 218
Cdd:PRK08737 133 DP----RCVAAFLArgiPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKQdPSASALHQAMRWGGQALD-HVE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 219 lkkndtkheldvapmfksligkdiSEEDANYAsGLTAVC---SIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQ 295
Cdd:PRK08737 208 ------------------------SLAHARFG-GLTGLRfniGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 296 NIinnvDSNKLSLDIPSNHRPVTSDKNSKLITTIKDVASSYVDKDDIFVSALVGA-TDASSFlgdNKDNVDLAIFGPGNP 374
Cdd:PRK08737 263 GF----AEPAAATFEETFRGPSLPSGDIARAEERRLAARDVADALDLPIGNAVDFwTEASLF---SAAGYTALVYGPGDI 335
|
330 340
....*....|....*....|
gi 612905143 375 LMAHQIDEYIEKDMYLKYID 394
Cdd:PRK08737 336 AQAHTADEFVTLDQLQRYAE 355
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
56-357 |
5.10e-12 |
|
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273857 [Multi-domain] Cd Length: 363 Bit Score: 66.60 E-value: 5.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 56 FVAEIGSGSP--ILALSGHMDVVDAGNQDNWtypPFQLTeKDDKLYGRGttdmKGGLMA-LVIALIELKEQNQLPQGTIR 132
Cdd:TIGR01891 46 VVATIGGGKPgpVVALRADMDALPIQEQTDL---PYKST-NPGVMHACG----HDLHTAiLLGTAKLLKKLADLLEGTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 133 LLATAGEEKEQEGAKLLADkGYLDDVDGLMIAEP----------TGSGIYYAhkGSMSCKVTATGKAVHSSVPFIGDNAI 202
Cdd:TIGR01891 118 LIFQPAEEGGGGATKMIED-GVLDDVDAILGLHPdpsipagtvgLRPGTIMA--AADKFEVTIHGKGAHAARPHLGRDAL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 203 DTLLEFYNQFKEkyaelkkndtkheldvapmfksligkdISEEDANYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPV 282
Cdd:TIGR01891 195 DAAAQLVVALQQ---------------------------IVSRNVDPSRPAVVSVGIIEAGGAPNVIPDKASMSGTVRSL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 283 PEYDNDFIESFFQNIINNVDSN---KLSLDIPSNHRPVTSDK--NSKLITTIKDVASSYVDKDDIFVSAlvGATDASSFL 357
Cdd:TIGR01891 248 DPEVRDQIIDRIERIVEGAAAMygaKVELNYDRGLPAVTNDPalTQILKEVARHVVGPENVAEDPEVTM--GSEDFAYYS 325
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
31-164 |
8.36e-12 |
|
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: 66.60 E-value: 8.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 31 NYLKDLFDKYDIKSEILKVNEHRAN---FVAEIGSGSP-----ILaLSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRG 102
Cdd:cd05677 31 IFLRQLFKKLGATNCLLLPSGPGTNpivLATFSGNSSDakrkrIL-FYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRG 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612905143 103 TTDMKGGLMALVIALIELKEQNQLPQGTIRLLatagEEKEQEGAKLLAD-----KGYLDDVDGLMIA 164
Cdd:cd05677 110 VSDNKGPLLAAIYAVAELFQEGELDNDVVFLI----EGEEESGSPGFKEvlrknKELIGDIDWILLS 172
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
11-230 |
4.58e-11 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 64.29 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 11 QLLADIVELQTENNNEID------VCNYLKDL--FDKY--DIKSEILKVNEHRANFVAEI---GSGSPILALSGHMDVV- 76
Cdd:cd05654 5 QLLKSLVSWPSVTGTEGErsfadfLKEILKELpyFKENpsHVWQLLPPDDLGRRNVTALVkgkKPSKRTIILISHFDTVg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 77 --DAGNQDNWTYPPFQLTEK------------------DDKLYGRGTTDMKGGLmALVIALIE-LKEQNQLPqGTIRLLA 135
Cdd:cd05654 85 ieDYGELKDIAFDPDELTKAfseyveeldeevredllsGEWLFGRGTMDMKSGL-AVHLALLEqASEDEDFD-GNLLLMA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 136 TAGEEKEQEGA--------KLLADKGYldDVDGLMIAEPT-----GSGIYYAHKGSMScKVTAT----GKAVHSSVPFIG 198
Cdd:cd05654 163 VPDEEVNSRGMraavpallELKKKHDL--EYKLAINSEPIfpqydGDQTRYIYTGSIG-KILPGflcyGKETHVGEPFAG 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 612905143 199 DNA------IDTLLEFYNQFKEKY--------AELKKNDTKHELDV 230
Cdd:cd05654 240 INAnlmaseITARLELNADLCEKVegeitpppVCLKQKDLKESYSV 285
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
63-406 |
4.87e-11 |
|
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: 63.87 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 63 GSPILALSGHMDVVDAGNQDNWTYPPFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRLLaTAGEEK- 141
Cdd:cd05680 62 GAPTVLVYGHYDVQPPDPLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFL-IEGEEEi 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 142 ---------EQEGAKLLADKGYLddVDGLMIAEPTGSgIYYAHKGSMSCKVTATG--KAVHSSVpFIG--DNAIDTLLE- 207
Cdd:cd05680 141 gspslpaflEENAERLAADVVLV--SDTSMWSPDTPT-ITYGLRGLAYLEISVTGpnRDLHSGS-YGGavPNPANALARl 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 208 ---------------FYNQF-------KEKYAELKKNDTKheldvapmFKSLIGKDISEEDANYAS----GLTAVCSI-- 259
Cdd:cd05680 217 laslhdedgrvaipgFYDDVrpltdaeREAWAALPFDEAA--------FKASLGVPALGGEAGYTTlerlWARPTLDVng 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 260 INGGKQFNS----VPDEASLEFNVRPVPEYDNDFIESFFQNIINNV--DSNKLSLDIPSNHRPVTSDKNSKLITTIKDVA 333
Cdd:cd05680 289 IWGGYQGEGsktvIPSKAHAKISMRLVPGQDPDAIADLLEAHLRAHapPGVTLSVKPLHGGRPYLVPTDHPALQAAERAL 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612905143 334 SSYVDKDDIFV---SALVGATDASSFLGdnkdnVDLAIFGPGNPLMA-HQIDEYIEKDMYLKYIdifkEASIQYLKE 406
Cdd:cd05680 369 EEAFGKPPVFVregGSIPIVALFEKVLG-----IPTVLMGFGLPDDAiHAPNEKFRLECFHKGI----EAIAHLLAR 436
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
61-387 |
8.82e-11 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 63.11 E-value: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 61 GSGSPILALSGHMDVVdagnqdnwtYP-------PFQltEKDDKLYGRGTTDMKGGLMALVIALIELKEQNQLPQGTIRL 133
Cdd:PRK06133 96 GTGKRRIMLIAHMDTV---------YLpgmlakqPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 134 LATAGEEKEQEGAK-LLADKGylDDVDGLMIAEPTGS--GIYYAHKGSMSCKVTATGKAVHS-SVPFIGDNAidtLLEFY 209
Cdd:PRK06133 165 LFNPDEETGSPGSReLIAELA--AQHDVVFSCEPGRAkdALTLATSGIATALLEVKGKASHAgAAPELGRNA---LYELA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 210 NQFkekyaelkkndtkheldvapmfksLIGKDISEEdanyASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDF 289
Cdd:PRK06133 240 HQL------------------------LQLRDLGDP----AKGTTLNWTVAKAGTNRNVIPASASAQADVRYLDPAEFDR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 290 IESFFQNIINN--VDSNKLSLDIPSNhRP--VTSDKNSKLITTIKDVASSYVDKDDIFVSALVGATDASSFLGDNKDNV- 364
Cdd:PRK06133 292 LEADLQEKVKNklVPDTEVTLRFERG-RPplEANAASRALAEHAQGIYGELGRRLEPIDMGTGGGTDAAFAAGSGKAAVl 370
|
330 340
....*....|....*....|....
gi 612905143 365 -DLAIFGPGnplmAHQIDEYIEKD 387
Cdd:PRK06133 371 eGFGLVGFG----AHSNDEYIELN 390
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
56-203 |
1.75e-10 |
|
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349939 [Multi-domain] Cd Length: 365 Bit Score: 61.91 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 56 FVAEIGSGS--PILALSGHMDVVdaGNQDNWTYPPFQLTEKDdklygrgttdmkgGLMALVIALI-ELKEQNQLPQGTIR 132
Cdd:cd08018 50 VVAEIGSGKpgPVVALRADMDAL--WQEVDGEFKANHSCGHD-------------AHMTMVLGAAeLLKKIGLVKKGKLK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 133 LLATAGEEKEQeGAKLLADKGYLDDVDGLM------IAE-PTG---SGIYyaHKGSMSCKVTATGKAVHSSVPFIGDNAI 202
Cdd:cd08018 115 FLFQPAEEKGT-GALKMIEDGVLDDVDYLFgvhlrpIQElPFGtaaPAIY--HGASTFLEGTIKGKQAHGARPHLGINAI 191
|
.
gi 612905143 203 D 203
Cdd:cd08018 192 E 192
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
10-280 |
1.76e-10 |
|
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1L2 family contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.
Pssm-ID: 349945 [Multi-domain] Cd Length: 366 Bit Score: 61.87 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 10 IQLLADIVELQTENNNEIDVCNYLKDLFDKYDIksEILKVNEHRANFVAEIGSG--SPILALSGHMDVVDAGNQDNWTYP 87
Cdd:cd08660 2 INIRRDIHEHPELGFEEVETSKKIRRWLEEEQI--EILDVPQLKTGVIAEIKGGedGPVIAIRADIDALPIQEQTNLPFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 88 pfqlTEKDDKLYGRGttdMKGGLMALVIALIELKEQNQLPQGTIRLLATAGEEKeQEGAKLLADKGYLDDVDGLMIAEPT 167
Cdd:cd08660 80 ----SKVDGT*HACG---HDFHTTSIIGTA*LLNQRRAELKGTVVFIFQPAEEG-AAGARKVLEAGVLNGVSAIFGIHNK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 168 GS---GIYYAHKGSMSCKVTA-----TGKAVHSSVPFIGD---NAIDTLLEFYNQFKEKYAELKKNDTKHeldvapmfks 236
Cdd:cd08660 152 PDlpvGTIGVKEGPL*ASVDVfeiviKGKGGHASIPNNSIdpiAAAGQIISGLQSVVSRNISSLQNAVVS---------- 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 612905143 237 ligkdiseedanyasgltavCSIINGGKQFNSVPDEASLEFNVR 280
Cdd:cd08660 222 --------------------ITRVQGGTAWNVIPDQAE*EGTVR 245
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
1-230 |
2.61e-10 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 62.18 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 1 MTTFSEKEKI-QLLADIVELQTENN--NEIDVCNYLKDLFDK-------------YDIKSEILKvnehRANFVAEI---G 61
Cdd:COG4187 1 MKKWQTKEQLeELLCELVSIPSVTGteGEKEVAEFIYEKLSElpyfqenpehlglHPLPDDPLG----RKNVTALVkgkG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 62 SGSPILALSGHMDVVDA---GNQDNWTYPPFQLTEK----------------DDKLYGRGTTDMKGGLmALVIALIELKE 122
Cdd:COG4187 77 ESKKTVILISHFDVVDVedyGSLKPLAFDPEELTEAlkeiklpedvrkdlesGEWLFGRGTMDMKAGL-ALHLALLEEAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 123 QNQLPQGTIRLLATAGEEKEQEG--------AKLLADKG--YLddvdgLMI-AEPT-----GSGIYYAHKGS----MSCk 182
Cdd:COG4187 156 ENEEFPGNLLLLAVPDEEVNSAGmraavpllAELKEKYGleYK-----LAInSEPSfpkypGDETRYIYTGSigklMPG- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612905143 183 VTATGKAVHSSVPFIGDNA------IDTLLEFYNQFKEKYAE--------LKKNDTKHELDV 230
Cdd:COG4187 230 FYCYGKETHVGEPFSGLNAnllaseLTRELELNPDFCEEVGGevtpppvsLKQKDLKEEYSV 291
|
|
| M20_Acy1L2 |
cd03887 |
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
115-280 |
8.56e-10 |
|
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, Aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase) subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349883 [Multi-domain] Cd Length: 360 Bit Score: 59.90 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 115 IALIELKEQNQLPqGTIRLLATAGEekEQEGAK-LLADKGYLDDVDGLMIAEPTGSGIYYAHkgSMSC---KVTATGKAV 190
Cdd:cd03887 96 LALKAALKALGLP-GTVVVLGTPAE--EGGGGKiDLIKAGAFDDVDIALMVHPGPKDVAGPK--SLAVsklRVEFHGKAA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 191 H-SSVPFIGDNAIDTLLEFYN------QFkekyaeLKKNDTKHeldvapmfksligkdiseedanyasgltavcSII-NG 262
Cdd:cd03887 171 HaAAAPWEGINALDAAVLAYNnisalrQQ------LKPTVRVH-------------------------------GIItEG 213
|
170
....*....|....*...
gi 612905143 263 GKQFNSVPDEASLEFNVR 280
Cdd:cd03887 214 GKAPNIIPDYAEAEFYVR 231
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
55-211 |
6.56e-09 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 57.67 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 55 NFVAEI---GSGSPILALSGHMDVVDAgNQDNWTYP-----PFQLTEKDDKLYGRGTTDMKGGLMALVIALIELKEqNQL 126
Cdd:PRK06156 97 NRVLEIglgGSGSDKVGILTHADVVPA-NPELWVLDgtrldPFKVTLVGDRLYGRGTEDDKGAIVTALYAMKAIKD-SGL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 127 P-QGTIRLLATAGEEKEQEGAK---------------------LLADKGY------------------LDDVDGLMIA-- 164
Cdd:PRK06156 175 PlARRIELLVYTTEETDGDPLKyylerytppdynitldaeypvVTAEKGWgtimatfpkraadgkgaeIVAMTGGAFAnq 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 612905143 165 ---------------------EPTGSGIYYAHKGSMS---------CKVTATGKAVHSSVPFIGDNAIDTLLEFYNQ 211
Cdd:PRK06156 255 ipqtavatlsggdpaalaaalQAAAAAQVKRHGGGFSidfkrdgkdVTITVTGKSAHSSTPESGVNPVTRLALFLQS 331
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
110-280 |
9.70e-09 |
|
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 56.66 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 110 LMALVIALIELKEQnqlPQGTIRLLATAGEEKEQeGAKLLADKGYLD--DVD---GL--MIAEPTGSgIYYaHKGSMSC- 181
Cdd:COG1473 109 LLGAAKALAELRDE---LKGTVRLIFQPAEEGGG-GAKAMIEDGLLDrpDVDaifGLhvWPGLPVGT-IGV-RPGPIMAa 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 182 ----KVTATGKAVHSSVPFIGDNAIDTLLEFYNQfkekyaelkkndtkheldvapmFKSLIGKDISEEDAnyasgltAVC 257
Cdd:COG1473 183 adsfEITIKGKGGHAAAPHLGIDPIVAAAQIVTA----------------------LQTIVSRNVDPLDP-------AVV 233
|
170 180
....*....|....*....|....*
gi 612905143 258 SI--INGGKQFNSVPDEASLEFNVR 280
Cdd:COG1473 234 TVgiIHGGTAPNVIPDEAELEGTVR 258
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
63-234 |
6.86e-08 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 54.37 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 63 GSPILALSGHMDV--VDAGNQdnWTYPPFQLTEKDDKLYGRGTTDMKGGLMaLVIALIE--LKEQNQLPQgTIRLLaTAG 138
Cdd:PRK08201 78 GKPTVLIYGHYDVqpVDPLNL--WETPPFEPTIRDGKLYARGASDDKGQVF-MHLKAVEalLKVEGTLPV-NVKFC-IEG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 139 EEK----------EQEGAKLLADKGYLDDVDGLmiaEPTGSGIYYAHKGSMSCKVTATGKA--VHS-----SVPfigdNA 201
Cdd:PRK08201 153 EEEigspnldsfvEEEKDKLAADVVLISDTTLL---GPGKPAICYGLRGLAALEIDVRGAKgdLHSglyggAVP----NA 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 612905143 202 IDTLLE----------------FYNQF-------KEKYAELKKND--TKHELDVAPMF 234
Cdd:PRK08201 226 LHALVQllaslhdehgtvavegFYDGVrpltpeeREEFAALGFDEekLKRELGVDELF 283
|
|
| M20_Acy1L2_AbgB |
cd05673 |
M20 Peptidase Aminoacylase 1-like protein 2 aminobenzoyl-glutamate utilization protein B ... |
56-280 |
2.22e-07 |
|
M20 Peptidase Aminoacylase 1-like protein 2 aminobenzoyl-glutamate utilization protein B subfamily; Peptidase M20 family, ACY1L2 aminobenzoyl-glutamate utilization protein B (AbgB) subfamily. This group contains mostly bacterial amidohydrolases, including gene products of abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate is a natural end product of folate catabolism, and its utilization is initiated by the abg region gene product, AbgT, by enabling uptake of its into the cell in a concentration-dependent, saturable manner. It is subsequently cleaved by AbgA and AbgB (sometimes referred to as AbgAB).
Pssm-ID: 349922 [Multi-domain] Cd Length: 437 Bit Score: 52.69 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 56 FVAEIGSGSPILALSGHMDVVDAGNQDNWTYPPfqlTEKDDKLYGRGTTDMKGGLMAL--VIALIELKEQNQLPqGTIRL 133
Cdd:cd05673 54 FVASYGSGGPVIAILGEYDALPGLSQEAGVAER---KPVEPGANGHGCGHNLLGTGSLgaAIAVKDYMEENNLA-GTVRF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 134 LATAGEekEQEGAK-LLADKGYLDDVDGLMIAEPTG-SGIYYAHKGS-MSCKVTATGKAVH-SSVPFIGDNAIDTlLEFY 209
Cdd:cd05673 130 YGCPAE--EGGSGKtFMVRDGVFDDVDAAISWHPASfNGVWSTSSLAnISVKFKFKGISAHaAAAPHLGRSALDA-VELM 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612905143 210 NqFKEKYaeLKKNdtkheldvapMfksligkdISEEDANYAsgltavcsIIN-GGKQFNSVPDEASLEFNVR 280
Cdd:cd05673 207 N-VGVNY--LREH----------M--------IPEARVHYA--------ITNgGGAAPNVVPAFAEVWYYIR 249
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
111-301 |
3.90e-07 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 51.89 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 111 MALVIALIeLKEQNQLPQGTIRLLATAGEEKEQEGAKLLADKGYLDDVDG-----LMIAEPTGSgIYYAHKGSMSC---- 181
Cdd:cd08021 107 MLLGAAKV-LAENKDEIKGTVRFIFQPAEEVPPGGAKPMIEAGVLEGVDAvfglhLWSTLPTGT-IAVRPGAIMAApdef 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 182 KVTATGKAVHSSVPFIGDNAIDTLLEFYNQfkekyaelkkndtkheldvapmFKSLIGKDISEEDanyasglTAVCSI-- 259
Cdd:cd08021 185 DITIKGKGGHGSMPHETVDPIVIAAQIVTA----------------------LQTIVSRRVDPLD-------PAVVTIgt 235
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 612905143 260 INGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNV 301
Cdd:cd08021 236 FQGGTSFNVIPDTVELKGTVRTFDEEVREQVPKRIERIVKGI 277
|
|
| M20_IAA_Hyd |
cd08017 |
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ... |
57-280 |
5.24e-07 |
|
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349938 [Multi-domain] Cd Length: 376 Bit Score: 51.17 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 57 VAEIGSGS-PILALSGHMDVVDAGNQDNWTYPpfqlTEKDDKLYGRG----TTdmkgglMALVIALIeLKEQNQLPQGTI 131
Cdd:cd08017 46 VATIGSGSpPVVALRADMDALPIQELVEWEHK----SKVDGKMHACGhdahVA------MLLGAAKL-LKARKHLLKGTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 132 RLLATAGEEKeQEGAKLLADKGYLDDVDG-----LMIAEPTG-----SGIYYAhkGSMSCKVTATGKAVHSSVPFigdNA 201
Cdd:cd08017 115 RLLFQPAEEG-GAGAKEMIKEGALDDVEAifgmhVSPALPTGtiasrPGPFLA--GAGRFEVVIRGKGGHAAMPH---HT 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 612905143 202 IDTLLefynqfkekyaelkkndtkheldVAPMFKSLIGKDISEEDANYASGLTAVcSIINGGKQFNSVPDEASLEFNVR 280
Cdd:cd08017 189 VDPVV-----------------------AASSAVLALQQLVSRETDPLDSQVVSV-TRFNGGHAFNVIPDSVTFGGTLR 243
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
110-280 |
9.45e-07 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 50.41 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 110 LMALVIALIELKEQnqlPQGTIRLLATAGEEKeQEGAKLLADKGYLDDVDGLM---IAEPTGSGIYYAHKGSM--SC--- 181
Cdd:cd08019 96 LLGAAKILNEIKDT---IKGTVKLIFQPAEEV-GEGAKQMIEEGVLEDVDAVFgihLWSDVPAGKISVEAGPRmaSAdif 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 182 KVTATGKAVHSSVPFIGDNAIDTLLEFYNQfkekyaelkkndtkheldvapmFKSLIGKDISEEDanyasglTAVCSI-- 259
Cdd:cd08019 172 KIEVKGKGGHGSMPHQGIDAVLAAASIVMN----------------------LQSIVSREIDPLE-------PVVVTVgk 222
|
170 180
....*....|....*....|.
gi 612905143 260 INGGKQFNSVPDEASLEFNVR 280
Cdd:cd08019 223 LNSGTRFNVIADEAKIEGTLR 243
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
71-113 |
1.53e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 49.91 E-value: 1.53e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 612905143 71 GHMDVVDaGNQDNWTYP--PFQLTEKDDKLYGRGTTDMKG----GLMAL 113
Cdd:PRK07079 92 GHGDVVR-GYDEQWREGlsPWTLTEEGDRWYGRGTADNKGqhtiNLAAL 139
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
111-301 |
1.02e-05 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 47.21 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 111 MALVIALIeLKEQNQLPQGTIRLLATAGEEKEqEGAKLLADKGYL--DDVD---GLMIAEPTGSGIYYAHKGSMSC---- 181
Cdd:cd03886 96 MLLGAAKL-LAERRDPLKGTVRFIFQPAEEGP-GGAKAMIEEGVLenPGVDaafGLHVWPGLPVGTVGVRSGALMAsade 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 182 -KVTATGKAVHSSVPFIGDNAIDTLLEFYNQfkekyaelkkndtkheldvapmFKSLIGKDISEEDAnyasgltAVCSI- 259
Cdd:cd03886 174 fEITVKGKGGHGASPHLGVDPIVAAAQIVLA----------------------LQTVVSRELDPLEP-------AVVTVg 224
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 612905143 260 -INGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINNV 301
Cdd:cd03886 225 kFHAGTAFNVIPDTAVLEGTIRTFDPEVREALEARIKRLAEGI 267
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
53-108 |
1.20e-03 |
|
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: 349928 [Multi-domain] Cd Length: 448 Bit Score: 40.95 E-value: 1.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612905143 53 RANF-VAE-IGSGS-PILALSGHMDVVDaGNQDNWT--YPPFQLTEKDDKLYGRGTTDMKG 108
Cdd:cd05679 58 RAPFlIAErIEDPSlPTLLIYGHGDVVP-GYEGRWRdgRDPWTVTVWGERWYGRGTADNKG 117
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
71-151 |
4.41e-03 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 39.11 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 71 GHMDV--VDAgnQDNWTYPPF--QLTEKDDK---LYGRGTTDMKGGLMALVIALIELKEQN-QLPQGTIRLLatAGEEK- 141
Cdd:PRK09104 89 GHYDVqpVDP--LDLWESPPFepRIKETPDGrkvIVARGASDDKGQLMTFVEACRAWKAVTgSLPVRVTILF--EGEEEs 164
|
90
....*....|....*....
gi 612905143 142 ---------EQEGAKLLAD 151
Cdd:PRK09104 165 gspslvpflEANAEELKAD 183
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
64-155 |
4.76e-03 |
|
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.
Pssm-ID: 349885 [Multi-domain] Cd Length: 474 Bit Score: 39.04 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612905143 64 SPILALSGHMDVV---DAGNQDNWTYPPFQLTEKDDKLYGRGTT---DmKGGLMALVIALIELKEqnqLPQGTIRLLATA 137
Cdd:cd03890 60 APPVILQGHMDMVcekNADSEHDFEKDPIKLRIDGDWLKATGTTlgaD-NGIGVAYALAILEDKD---IEHPPLEVLFTV 135
|
90
....*....|....*...
gi 612905143 138 GEEKEQEGAKLLaDKGYL 155
Cdd:cd03890 136 DEETGMTGALGL-DPSLL 152
|
|
| |
