|
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: 628.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 6 EKEKIQLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVNEHRANIVAEIGNGSPILALSGHMDVVDAGNQDNWT 85
Cdd:PRK08588 1 EEEKIQILADIVKINSVNDNEIEVANYLQDLFAKHGIESKIVKVNDGRANLVAEIGSGSPVLALSGHMDVVAAGDVDKWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 86 YPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLADKGYLDDVDGLIIAE 165
Cdd:PRK08588 81 YDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGELGAKQLTEKGYADDLDALIIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 166 PTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYSELKKHDtkheldvapmfksligkeisee 245
Cdd:PRK08588 161 PSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYFDSIKKHN---------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 246 daNYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSN---KLSLDIPSNHRPVTSDKN 322
Cdd:PRK08588 219 --PYLGGLTHVVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNQNgaaQLSLDIYSNHRPVASDKD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 323 SKLITTIKDVASSYVEQDeIFVSALVGATDASSFLgDNKDNVDLAIFGPGNPLMAHQIDEYIEKDMYLKYIDIFKEASIQ 402
Cdd:PRK08588 297 SKLVQLAKDVAKSYVGQD-IPLSAIPGATDASSFL-KKKPDFPVIIFGPGNNLTAHQVDEYVEKDMYLKFIDIYKEIIIQ 374
|
...
gi 582169601 403 YLK 405
Cdd:PRK08588 375 YLK 377
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
11-399 |
8.10e-131 |
|
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: 380.11 E-value: 8.10e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 11 QLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVnEHRANIVAEIGNGS-PILALSGHMDVVDAGNQDNWTYPPF 89
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIV-EGRGNLVATVGGGDgPVLLLNGHIDTVPPGDGDKWSFPPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 90 QLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLADKGYLDDVDGLIIAEPTGS 169
Cdd:cd08659 80 SGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLEAGYADRLDALIVGEPTGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 170 GIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYSELKKHDtkheldvapmfksLIGkeiseedany 249
Cdd:cd08659 160 DVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPAHP-------------LLG---------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 250 asGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDND-FIESFFQniINDVDSNKLSLDIPSNHRPVT-SDKNSKLIT 327
Cdd:cd08659 217 --PPTLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEgVIARLEA--ILEEHEAKLTVEVSLDGDPPFfTDPDHPLVQ 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 582169601 328 TIKDVASSYVEQDEIFVSAlvGATDASSFLGDNkdNVDLAIFGPGNPLMAHQIDEYIEKDMYLKYIDIFKEA 399
Cdd:cd08659 293 ALQAAARALGGDPVVRPFT--GTTDASYFAKDL--GFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEI 360
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
10-396 |
2.24e-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: 280.62 E-value: 2.24e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 10 IQLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVNEHRANIVAEI--GNGSPILALSGHMDVVDAGNQDNWTYP 87
Cdd:COG0624 15 LELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPPGRPNLVARRpgDGGGPTLLLYGHLDVVPPGDLELWTSD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 88 PFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQEGAK-LLADKGYLDDVDGLIIAEP 166
Cdd:COG0624 95 PFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSPGARaLVEELAEGLKADAAIVGEP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 167 TGSG-IYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFkekyselkkHDTKHELDVAPMFKSligkeisee 245
Cdd:COG0624 175 TGVPtIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAAL---------RDLEFDGRADPLFGR--------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 246 danyasgLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSN-KLSLDIPSNHR-PVTSDKNS 323
Cdd:COG0624 237 -------TTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGvEVEVEVLGDGRpPFETPPDS 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 582169601 324 KLITTIKDVASSyVEQDEIFVSALVGATDASSFLGDNkdNVDLAIFGPGNPLMAHQIDEYIEKDMYLKYIDIF 396
Cdd:COG0624 310 PLVAAARAAIRE-VTGKEPVLSGVGGGTDARFFAEAL--GIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVL 379
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
10-395 |
3.30e-90 |
|
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: 276.97 E-value: 3.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 10 IQLLADIVELQTENN---NEIDVCNYLKDLFDKYDIKSEILKVNEHRAN-----IVAEIGNGS-PILALSGHMDVVDAGN 80
Cdd:TIGR01910 1 VELLKDLISIPSVNPpggNEETIANYIKDLLREFGFSTDVIEITDDRLKvlgkvVVKEPGNGNeKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 81 QDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLADKGYLDDVDG 160
Cdd:TIGR01910 81 LELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLLQRGYFKDADG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 161 LIIAEPTGS-GIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQfkekyselkkhdtkheldvapmfkslIG 239
Cdd:TIGR01910 161 VLIPEPSGGdNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITE--------------------------LN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 240 KEISEEDANYASG-----LTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSNK---LSLDIP 311
Cdd:TIGR01910 215 ELEEHIYARNSYGfipgpITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSDgwlYENEPV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 312 SN-HRPVTSDKNSKLITTIKDVASSYV-EQDEIFVSAlvGATDAsSFLGDNKdnVDLAIFGPGNPLMAHQIDEYIEKDMY 389
Cdd:TIGR01910 295 VKwSGPNETPPDSRLVKALEAIIKKVRgIEPEVLVST--GGTDA-RFLRKAG--IPSIVYGPGDLETAHQVNEYISIKNL 369
|
....*.
gi 582169601 390 LKYIDI 395
Cdd:TIGR01910 370 VESTKV 375
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
68-399 |
3.07e-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: 205.66 E-value: 3.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 68 ALSGHMDVVDAGNQDNWtypPFQLTEKaGKLYGRGTTDMKGGLMALVITLIELKEQNQLPqGTIRLLATAGEEKEQEGAK 147
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTED-GKLYGRGHDDMKGGLLAALEALRALKEEGLKK-GTVKLLFQPDEEGGMGGAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 148 LLADKGYLDD-----VDGLIIAEPT------GSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQfkeky 216
Cdd:pfam01546 76 ALIEDGLLERekvdaVFGLHIGEPTlleggiAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILA----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 217 selkkhdtkheldvapmfkslIGKEISEEDANYASGLTAVCSI--INGGkqFNSVPDEASLEFNVRPVPEYDNDFIESFF 294
Cdd:pfam01546 151 ---------------------LQDIVSRNVDPLDPAVVTVGNItgIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 295 QNI---INDVDSNKLSLDIPSNHRPVTSDkNSKLITTIKDVASSYVEQDEIF-VSALVGATDASSFLGDNKDNVDlaIFG 370
Cdd:pfam01546 208 REIleaIAAAYGVKVEVEYVEGGAPPLVN-DSPLVAALREAAKELFGLKVELiVSGSMGGTDAAFFLLGVPPTVV--FFG 284
|
330 340
....*....|....*....|....*....
gi 582169601 371 PGNPLmAHQIDEYIEKDMYLKYIDIFKEA 399
Cdd:pfam01546 285 PGSGL-AHSPNEYVDLDDLEKGAKVLARL 312
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
10-399 |
5.91e-61 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 202.14 E-value: 5.91e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 10 IQLLADIVELQTENNNEIDV---CNYLKDLFDKYDIKSEIL--------KVNEHRANIVAEIGNGSPILALSGHMDVVDA 78
Cdd:PRK08651 9 VEFLKDLIKIPTVNPPGENYeeiAEFLRDTLEELGFSTEIIevpneyvkKHDGPRPNLIARRGSGNPHLHFNGHYDVVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 79 GnqDNW-TYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEqnqLPQGTIRLLATAGEEKEQEGAKLLADKGYlDD 157
Cdd:PRK08651 89 G--EGWsVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDP---AGDGNIELAIVPDEETGGTGTGYLVEEGK-VT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 158 VDGLIIAEPTGSG-IYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYSELKKhDTKHELDVAPMFKS 236
Cdd:PRK08651 163 PDYVIVGEPSGLDnICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKS-KYEYDDERGAKPTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 237 LIGKEiseedanyasgltavcsIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDV---DSNKLSLDIPSN 313
Cdd:PRK08651 242 TLGGP-----------------TVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVapeLGIEVEFEITPF 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 314 HRPVTSDKNSKLITTIKDvASSYVEQDEIFVSALVGATDASSFLgdnKDNVDLAIFGPGNPLMAHQIDEYIEKDMYLKYI 393
Cdd:PRK08651 305 SEAFVTDPDSELVKALRE-AIREVLGVEPKKTISLGGTDARFFG---AKGIPTVVYGPGELELAHAPDEYVEVKDVEKAA 380
|
....*.
gi 582169601 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 |
1.72e-59 |
|
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: 197.22 E-value: 1.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 10 IQLLADIVELQTEN---NNEIDVCNYLKDLFDKYDIKSEILKVNEHRANIVAEI--GNGSPILALSGHMDVVDAGNQDNW 84
Cdd:cd08011 1 VKLLQELVQIPSPNppgDNTSAIAAYIKLLLEDLGYPVELHEPPEEIYGVVSNIvgGRKGKRLLFNGHYDVVPAGDGEGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 85 TYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEK-EQEGAKLLADKgYLDDVDGLII 163
Cdd:cd08011 81 TVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETgGRAGTKYLLEK-VRIKPNDVLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 164 AEPTGS-GIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLefynqfkekyselkkhdtkheldvapmfkSLIGkEI 242
Cdd:cd08011 160 GEPSGSdNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAM-----------------------------KLIE-RL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 243 SEEDANYASGltavcsIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESffqNIINDVDS-NKLSLDIPSNHRPVTSDK 321
Cdd:cd08011 210 YELEKTVNPG------VIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLS---RIIDHLDSiEEVSFEIKSFYSPTVSNP 280
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 582169601 322 NSKLITTIKDVASSYVEQDEIFVSAlVGATDASSFlgdNKDNVDLAIFGPGNPLMAHQIDEYIEKDMYLKYIDIFKEA 399
Cdd:cd08011 281 DSEIVKKTEEAITEVLGIRPKEVIS-VGASDARFY---RNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVHALV 354
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
11-385 |
4.89e-53 |
|
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: 180.48 E-value: 4.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 11 QLLADIVELQTEN-NNEIDVCNYLKDLFDKYDIKSEILKVNEH-RANIVAEIG-NGSPILALSGHMDVVDAGNQDnWTYP 87
Cdd:cd03894 1 ELLARLVAFDTVSrNSNLALIEYVADYLAALGVKSRRVPVPEGgKANLLATLGpGGEGGLLLSGHTDVVPVDGQK-WSSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 88 PFQLTEKAGKLYGRGTTDMKGGL---MALVITLIELKeqnqlPQGTIRLLATAGEEKEQEGAKLLADKGYLDDV--DGLI 162
Cdd:cd03894 80 PFTLTERDGRLYGRGTCDMKGFLaavLAAVPRLLAAK-----LRKPLHLAFSYDEEVGCLGVRHLIAALAARGGrpDAAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 163 IAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYSELKKHDTKHELDVaPmfksligkei 242
Cdd:cd03894 155 VGEPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPFDP-P---------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 243 seedanyasGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIIN--------DVDSNKLSLDIPSNh 314
Cdd:cd03894 224 ---------YPTLNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEallefpeaGIEVEPLFEVPGLE- 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 582169601 315 rpvtSDKNSKLITTIKDVASSYVeqdeifVSALVGATDASSF--LGdnkdnVDLAIFGPGNPLMAHQIDEYIE 385
Cdd:cd03894 294 ----TDEDAPLVRLAAALAGDNK------VRTVAYGTEAGLFqrAG-----IPTVVCGPGSIAQAHTPDEFVE 351
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
28-387 |
4.29e-43 |
|
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: 154.21 E-value: 4.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 28 DVCNYLKDLFDKYDIKSEILKVNE--HRANIVAEIG-NGSPILALSGHMDVVDAGNQdNWTYPPFQLTEKAGKLYGRGTT 104
Cdd:TIGR01892 19 DLIDWAQAYLEALGFSVEVQPFPDgaEKSNLVAVIGpSGAGGLALSGHTDVVPYDDA-AWTRDPFRLTEKDGRLYGRGTC 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 105 DMKgGLMALVITLIELKEQNQLpQGTIRLLATAGEEKEQEGAKLLADKGYLDDvDGLIIAEPTGSGIYYAHKGSMSCKVT 184
Cdd:TIGR01892 98 DMK-GFLACALAAAPDLAAEQL-KKPLHLALTADEEVGCTGAPKMIEAGAGRP-RHAIIGEPTRLIPVRAHKGYASAEVT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 185 ATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYSELKKHDtkHELDVAPMFKSL-IGkeiseedanyasgltavcsIINGG 263
Cdd:TIGR01892 175 VRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLRED--LDEGFTPPYTTLnIG-------------------VIQGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 264 KQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSNKLSLDIPSNHRPvtsdknsklitTIKDVASSYVEQDEIF 343
Cdd:TIGR01892 234 KAVNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRDEPGFEVQIEVVS-----------TDPGVNTEPDAELVAF 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 582169601 344 VSALVG--------ATDASSFLGDNKDNVdlaIFGPGNPLMAHQIDEYIEKD 387
Cdd:TIGR01892 303 LEELSGnapevvsyGTEAPQFQELGAEAV---VCGPGDIRQAHQPDEYVEIE 351
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
11-356 |
6.17e-41 |
|
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: 150.20 E-value: 6.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 11 QLLADIVELQTENN-----NEIDVCNYLKDLFDKYDIKSEILKVNEH--RANIVAEIGNGSPI---LALSGHMDVVDAgN 80
Cdd:cd05675 2 DLLQELIRIDTTNSgdgtgSETRAAEVLAARLAEAGIQTEIFVVESHpgRANLVARIGGTDPSagpLLLLGHIDVVPA-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 81 QDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQE-GAKLLADK------G 153
Cdd:cd05675 81 ASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGEnGAKWLVDNhpelfdG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 154 Y---LDDVDGLIIAEPTGSGIYY---AHKGSMSCKVTATGKAVHSSVPFIgDNAIDTLLEFYNQFKeKYSE-LKKHDTK- 225
Cdd:cd05675 161 AtfaLNEGGGGSLPVGKGRRLYPiqvAEKGIAWMKLTVRGRAGHGSRPTD-DNAITRLAEALRRLG-AHNFpVRLTDETa 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 226 -----HELDVAP----MFKSLIGKEI-------SEEDANYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDF 289
Cdd:cd05675 239 yfaqmAELAGGEggalMLTAVPVLDPalaklgpSAPLLNAMLRNTASPTMLDAGYATNVLPGRATAEVDCRILPGQSEEE 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 582169601 290 IESFFQNIINDVD-SNKLSLDIPSNHRPVTsdknSKLITTIKDVASSYVEQDEIFVSALVGATDASSF 356
Cdd:cd05675 319 VLDTLDKLLGDPDvSVEAVHLEPATESPLD----SPLVDAMEAAVQAVDPGAPVVPYMSPGGTDAKYF 382
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
29-394 |
7.18e-39 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 143.42 E-value: 7.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 29 VCNYLKDLFDKYDIKSEILKVNEHR--ANIVAEIGNGSPILALSGHMDVV--DAGNqdnWTYPPFQLTEKAGKLYGRGTT 104
Cdd:PRK05111 34 VIDLLAGWFEDLGFNVEIQPVPGTRgkFNLLASLGSGEGGLLLAGHTDTVpfDEGR---WTRDPFTLTEHDGKLYGLGTA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 105 DMKgGLMALVI-TLIELKEQNQlpQGTIRLLATAGEEKEQEGAKLLADKGYLDDvDGLIIAEPTGSGIYYAHKGSMSCKV 183
Cdd:PRK05111 111 DMK-GFFAFILeALRDIDLTKL--KKPLYILATADEETSMAGARAFAEATAIRP-DCAIIGEPTSLKPVRAHKGHMSEAI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 184 TATGKAVHSSVPFIGDNAIDT-------LLEFYNQFKEKYSElkkhdtkheldvaPMFksligkEISEEDANYASgltav 256
Cdd:PRK05111 187 RITGQSGHSSDPALGVNAIELmhdvigeLLQLRDELQERYHN-------------PAF------TVPYPTLNLGH----- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 257 csiINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDV-DSNKLSLDIPSNHRPVTS---DKNSKLITTIKDV 332
Cdd:PRK05111 243 ---IHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVsERWPGRITVAPLHPPIPGyecPADHQLVRVVEKL 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 582169601 333 ASSYVEqdeifvsALVGATDAsSFLgdNKDNVDLAIFGPGNPLMAHQIDEYIEkdmyLKYID 394
Cdd:PRK05111 320 LGHKAE-------VVNYCTEA-PFI--QQLGCPTLVLGPGSIEQAHQPDEYLE----LSFIK 367
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
31-385 |
4.42e-37 |
|
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: 138.02 E-value: 4.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 31 NYLKDLFDKYDIKSEILKVNEHRaNIVAEIGNGSPILALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGL 110
Cdd:cd03891 22 DLIAERLKALGFTCERLEFGGVK-NLWARRGTGGPHLCFAGHTDVVPPGDLEGWSSDPFSPTIKDGMLYGRGAADMKGGI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 111 MALVITLIELKEQNQLPQGTIRLLATAGEEKEQE-GAKL----LADKGYLddVDGLIIAEPT-----GSGIYYAHKGSMS 180
Cdd:cd03891 101 AAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIdGTKKvlewLKARGEK--IDYCIVGEPTsekklGDTIKIGRRGSLN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 181 CKVTATGKAVHSSVPFIGDNAIDTLlefynqfkekyselkkhdtkheldvAPMFKSLIGKEISEEDANYASGLTAVCSII 260
Cdd:cd03891 179 GKLTIKGKQGHVAYPHLADNPIHLL-------------------------APILAELTATVLDEGNEFFPPSSLQITNID 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 261 NGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSNkLSLDIPSNHRP-VTsdKNSKLITTIKDVASSYVEQ 339
Cdd:cd03891 234 VGNGATNVIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLD-YDLEWKLSGEPfLT--KPGKLVDAVSAAIKEVTGI 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 582169601 340 DEIFvSALVGATDAsSFLGDNKDNVdlAIFGPGNpLMAHQIDEYIE 385
Cdd:cd03891 311 TPEL-STSGGTSDA-RFIASYGCPV--VEFGLVN-ATIHKVNERVS 351
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
6-202 |
2.14e-36 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 136.99 E-value: 2.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 6 EKEKIQLLADIVELQTENNNEIDVCNYLKDLFDK--YDiKSEIlkvnEHRANIVAEIGNGSPILALSGHMDVVDAGNQDN 83
Cdd:PRK13004 14 KADMTRFLRDLIRIPSESGDEKRVVKRIKEEMEKvgFD-KVEI----DPMGNVLGYIGHGKKLIAFDAHIDTVGIGDIKN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 84 WTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEkEQEGaklLADKgYLDDVDGL-- 161
Cdd:PRK13004 89 WDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEE-DCDG---LCWR-YIIEEDKIkp 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 582169601 162 ---IIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAI 202
Cdd:PRK13004 164 dfvVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAI 207
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
10-387 |
4.95e-36 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 135.70 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 10 IQLLADIVELQT---ENNNE-IDvcnYLKDLFDKYDIKSEILKVNE-HRANIVAEIG-NGSPILALSGHMDVVDAGNQDn 83
Cdd:PRK07522 7 LDILERLVAFDTvsrDSNLAlIE---WVRDYLAAHGVESELIPDPEgDKANLFATIGpADRGGIVLSGHTDVVPVDGQA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 84 WTYPPFQLTEKAGKLYGRGTTDMKGGLmALVITLI-ELKEQN-QLPqgtIRLLATAGEEKEQEGAKLLAD--KGYLDDVD 159
Cdd:PRK07522 83 WTSDPFRLTERDGRLYGRGTCDMKGFI-AAALAAVpELAAAPlRRP---LHLAFSYDEEVGCLGVPSMIArlPERGVKPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 160 GLIIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYSELkkhdtKHELDVAPMFkslig 239
Cdd:PRK07522 159 GCIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRL-----AAPGPFDALF----- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 240 keiseeDANYASGLTAVcsiINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSNKLSLDIPSNHrpVTs 319
Cdd:PRK07522 229 ------DPPYSTLQTGT---IQGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAELLPEMRAVHPEAA--IE- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 320 dknsklITTIkdvaSSY-----VEQDEI--FVSALVG---------ATDASSF--LGdnkdnVDLAIFGPGNPLMAHQID 381
Cdd:PRK07522 297 ------FEPL----SAYpgldtAEDAAAarLVRALTGdndlrkvayGTEAGLFqrAG-----IPTVVCGPGSIEQAHKPD 361
|
....*.
gi 582169601 382 EYIEKD 387
Cdd:PRK07522 362 EFVELA 367
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
12-393 |
2.64e-34 |
|
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: 130.61 E-value: 2.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 12 LLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVNEhRANIVAEIGNGSPILALSGHMDVVDAGNQDNWTYPPFQL 91
Cdd:TIGR01246 4 LAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGD-TKNLWATRGTGEPVLAFAGHTDVVPAGPEEQWSSPPFEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 92 TEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKE-----QEGAKLLADKGYLddVDGLIIAEP 166
Cdd:TIGR01246 83 VERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTaidgtKKVVETLMARDEL--IDYCIVGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 167 T-----GSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLlefynqfkekyselkkhdtkheldvAPMFKSLIGKE 241
Cdd:TIGR01246 161 SsvkklGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKA-------------------------APALAELTAIK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 242 ISEEDAnYASGLTAVCSIINGGKQFNSV-PDEASLEFNVRPVPEYDNDFIESFFQNIIndvDSNKLSLDIP--SNHRPVT 318
Cdd:TIGR01246 216 WDEGNE-FFPPTSLQITNIHAGTGANNViPGELYVQFNLRFSTEVSDEILKQRVEAIL---DQHGLDYDLEwsLSGEPFL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 319 SDKNsKLITTIKDVASSYVEQDEIFVSAlvGATDASSFLGDNkdNVDLAIFGPGNPlMAHQIDEY-----IEK--DMYLK 391
Cdd:TIGR01246 292 TNDG-KLIDKAREAIEETNGIKPELSTG--GGTSDGRFIALM--GAEVVEFGPVNA-TIHKVNECvsiedLEKlsDVYQD 365
|
..
gi 582169601 392 YI 393
Cdd:TIGR01246 366 LL 367
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
10-387 |
1.01e-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: 128.55 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 10 IQLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKV-NEHRANIVAEIGNG-SPILALSGHMDVVdagnqdnwtyP 87
Cdd:cd05652 2 LSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKQPVeNKDRFNVYAYPGSSrQPRVLLTSHIDTV----------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 88 PF---QLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLADKGyLDDVDGLIIA 164
Cdd:cd05652 72 PFipySISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGDGMKAFNDLG-LNTWDAVIFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 165 EPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEfynqfkekyselkkhdTKHELDVAPMFKS-LIGKeis 243
Cdd:cd05652 151 EPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVE----------------ALVKLIDADLPSSeLLGP--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 244 eedanyaSGLTAvcSIINGGKQFNSVPDEASLEFNVRPV--PEYDNDFIESFFQNIINDVDSnkLSLDIPSNHRPVTSDK 321
Cdd:cd05652 212 -------TTLNI--GRISGGVAANVVPAAAEASVAIRLAagPPEVKDIVKEAVAGILTDTED--IEVTFTSGYGPVDLDC 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 582169601 322 NsklittikdvassyVEQDEIFVSALvgATDASSFLGDNKDnvdlAIFGPGNPLMAHQIDEYIEKD 387
Cdd:cd05652 281 D--------------VDGFETDVVAY--GTDIPYLKGDHKR----YLYGPGSILVAHGPDEAITVS 326
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
8-399 |
1.32e-33 |
|
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: 128.24 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 8 EKIQLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVNehraNIVAEIGNGSPILALSGHMDVVDAgnqdnwtYP 87
Cdd:cd05653 2 DAVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEAG----NAVGGAGSGPPDVLLLGHIDTVPG-------EI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 88 PFQLTEkaGKLYGRGTTDMKGGLMALVITLIELKEQnqlPQGTIRLLATAGEEKEQEGAKLLADKGYldDVDGLIIAEPT 167
Cdd:cd05653 71 PVRVEG--GVLYGRGAVDAKGPLAAMILAASALNEE---LGARVVVAGLVDEEGSSKGARELVRRGP--RPDYIIIGEPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 168 G-SGIYYAHKGSMSCKVTATGKAVHSSVPfiGDNAIDTLLefynqfkEKYSELKKHDTKHELDVAPMFksligkeiseed 246
Cdd:cd05653 144 GwDGITLGYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLI-------KKWLEVKKWAEGYNVGGRDFD------------ 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 247 anyasglTAVCSIINGGKQFNSVPDEASLEFNVR-PVPEYDNDFIEsffqniINDVDSNKLSLDIPSNHRPVTSDKNSKL 325
Cdd:cd05653 203 -------SVVPTLIKGGESSNGLPQRAEATIDLRlPPRLSPEEAIA------LATALLPTCELEFIDDTEPVKVSKNNPL 269
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 582169601 326 ittIKDVASSYVEQDeiFVSALVGATDASSF--LGDNKDnVDLAIFGPGNPLMAHQIDEYIEKDMYLKYIDIFKEA 399
Cdd:cd05653 270 ---ARAFRRAIRKQG--GKPRLKRKTGTSDMnvLAPLWT-VPIVAYGPGDSTLDHTPNEHIELAEIERAAAVLKGA 339
|
|
| PRK06915 |
PRK06915 |
peptidase; |
55-401 |
3.01e-33 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 129.04 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 55 NIVAEI---GNGSPILaLSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTI 131
Cdd:PRK06915 82 NIVATLkgsGGGKSMI-LNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 132 rLLATAGEEkEQEGAKLLAD--KGYldDVDGLIIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFY 209
Cdd:PRK06915 161 -IFQSVIEE-ESGGAGTLAAilRGY--KADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 210 NQFKekysELKKHDTKHELDvaPMFKSL-------IGKeiseedanyasgltavcsiINGGKQFNSVPDEASLEFNVRPV 282
Cdd:PRK06915 237 DHLR----KLEEKRNDRITD--PLYKGIpipipinIGK-------------------IEGGSWPSSVPDSVILEGRCGIA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 283 PEYDNDFIESFFQNIINDVDSNklslDIPSNHRPVTS------------DKNSKLITTIKdvaSSY--VEQDEIFVSALV 348
Cdd:PRK06915 292 PNETIEAAKEEFENWIAELNDV----DEWFVEHPVEVewfgarwvpgelEENHPLMTTLE---HNFveIEGNKPIIEASP 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 582169601 349 GATDASSFlgDNKDNVDLAIFGPGNPLMAHQIDEYIEKDmylkyiDIFKEASI 401
Cdd:PRK06915 365 WGTDGGLL--TQIAGVPTIVFGPGETKVAHYPNEYIEVD------KMIAAAKI 409
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
10-202 |
1.70e-31 |
|
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: 123.30 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 10 IQLLADIVELQTENNNEIDVCNYLKDLFDK--YDiKSEIlkvnEHRANIVAEIGNGSPILALSGHMDVVDAGNQDNWTYP 87
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKlgFD-EVEI----DPMGNVIGYIGGGKKKILFDGHIDTVGIGNIDNWKFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 88 PFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQEG--AKLLADKGYLdDVDGLIIAE 165
Cdd:cd05649 76 PYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLRDFAYTILVAGTVQEEDCDGvcWQYISKADKI-KPDFVVSGE 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 582169601 166 PTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAI 202
Cdd:cd05649 155 PTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAV 191
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
10-385 |
1.15e-30 |
|
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: 120.24 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 10 IQLLADIVELQTENNNEIDVCNYLKDLFDKydikSEILKVNEHRANIVAEIGNGSPI-LALSGHMDVVD-AGNqdnwtYP 87
Cdd:cd05647 2 IELTAALVDIPSVSGNEKPIADEIEAALRT----LPHLEVIRDGNTVVARTERGLASrVILAGHLDTVPvAGN-----LP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 88 PfqLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNqlPQGTIRLLATAGEE--KEQEGAKLLADK-GYLDDVDGLIIA 164
Cdd:cd05647 73 S--RVEEDGVLYGCGATDMKAGDAVQLKLAATLAAAT--LKHDLTLIFYDCEEvaAELNGLGRLAEEhPEWLAADFAVLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 165 EPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIdtllefynqfkekyselkkhdtkHELdvAPMFKSLIG---KE 241
Cdd:cd05647 149 EPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAI-----------------------HKL--APILARLAAyepRT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 242 ISEEDANYASGLTAVcsIINGGKQFNSVPDEASLEFNVRPVPeyDNDFIESffQNIINDVDSnKLSLDIpsnhrPVTSDK 321
Cdd:cd05647 204 VNIDGLTYREGLNAV--FISGGVAGNVIPDEARVNLNYRFAP--DKSLAEA--IAHVREVFE-GLGYEI-----EVTDLS 271
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 582169601 322 NSKLITTIKDVASSYVEQDEIFVSALVGATDASSFLGDNKDNVDlaiFGPGNPLMAHQIDEYIE 385
Cdd:cd05647 272 PGALPGLDHPVARDLIEAVGGKVRAKYGWTDVARFSALGIPAVN---FGPGDPLLAHKRDEQVP 332
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
12-385 |
3.66e-29 |
|
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: 117.02 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 12 LLADIVELQTENNNEIDVCNYLKDLF-------DKYDIKSEILKVN----------EHRANIVA---EIGNGSPILALSG 71
Cdd:cd03895 2 FLQDLVRFPSLRGEEAAAQDLVAAALrsrgytvDRWEIDVEKLKHHpgfspvavdyAGAPNVVGthrPRGETGRSLILNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 72 HMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLAD 151
Cdd:cd03895 82 HIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNGALAALM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 152 KGYldDVDGLIIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFK--EKYSELKKHDTKHELD 229
Cdd:cd03895 162 RGY--RADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQelEREWNARKKSHPHFSD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 230 VAPMFKSLIGKeiseedanyasgltavcsiINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSNKLSLd 309
Cdd:cd03895 240 HPHPINFNIGK-------------------IEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVADAAATDPWL- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 310 ipSNHRP-----------VTSDKNSKLITTIKDVASSYVEQDEIFVSALVGaTDASSFLGDNkdNVDLAIFGPGNpLMAH 378
Cdd:cd03895 300 --SNHPPevewngfqaegYVLEPGSDAEQVLAAAHQAVFGTPPVQSAMTAT-TDGRFFVLYG--DIPALCYGPGS-RDAH 373
|
....*..
gi 582169601 379 QIDEYIE 385
Cdd:cd03895 374 GFDESVD 380
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
41-300 |
5.61e-28 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 114.71 E-value: 5.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 41 DIksEILKVNEHRANIVAEI---GNGSPILaLSGHMDVVDAGNQDnWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITL 117
Cdd:PRK09133 78 DI--EVTGPYPRKGNLVARLrgtDPKKPIL-LLAHMDVVEAKRED-WTRDPFKLVEENGYFYGRGTSDDKADAAIWVATL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 118 IELKEQNQLPQGTIRLLATAGEEKEQ-EGAKLLADK----------------GYLDDvdgliiaepTGSGIYYAHKGS-- 178
Cdd:PRK09133 154 IRLKREGFKPKRDIILALTGDEEGTPmNGVAWLAENhrdlidaefalnegggGTLDE---------DGKPVLLTVQAGek 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 179 --MSCKVTATGKAVHSSVPfIGDNAIDTL------LEFYnQFKEKYSELKKHDTKHELDVAP-----MFKSLIGK----- 240
Cdd:PRK09133 225 tyADFRLEVTNPGGHSSRP-TKDNAIYRLaaalsrLAAY-RFPVMLNDVTRAYFKQSAAIETgplaaAMRAFAANpadea 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 582169601 241 --EISEEDANYASGL--TAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIIND 300
Cdd:PRK09133 303 aiALLSADPSYNAMLrtTCVATMLEGGHAENALPQRATANVNCRIFPGDTIEAVRATLKQVVAD 366
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
32-384 |
1.37e-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: 112.55 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 32 YLKDL----FDKYDIKSEILKvneHRANIVAEIGNGSP-ILALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDM 106
Cdd:cd05650 35 KLREYgfytLERYDAPDERGI---IRPNIVAKIPGGNDkTLWIISHLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 107 KGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQE-GAKLLADKGYLDDVDGLII----AEPTGSGIYYAHKGSMSC 181
Cdd:cd05650 112 QQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEyGIQYLLNKFDLFKKDDLIIvpdfGTEDGEFIEIAEKSILWI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 182 KVTATGKAVHSSVPFIGDNAI----DTLLEFYNQFKEKYSELKK---------HDTKHELDVapmfksligkeiseedan 248
Cdd:cd05650 192 KVNVKGKQCHASTPENGINAFvaasNFALELDELLHEKFDEKDDlfnppystfEPTKKEANV------------------ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 249 yasgltavcsiinggKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSN-----KLSLDIPSNHRPVTsDKNS 323
Cdd:cd05650 254 ---------------PNVNTIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDFENSygagiTYEIVQKEQAPPAT-PEDS 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 582169601 324 KLITTIKDVASSyVEQDEIFVSALVGATDASSFlgdNKDNVDLAIFGPGNPlMAHQIDEYI 384
Cdd:cd05650 318 EIVVRLSKAIKK-VRGREAKLIGIGGGTVAAFL---RKKGYPAVVWSTLDE-TAHQPNEYI 373
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
8-398 |
2.60e-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 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: 110.86 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 8 EKIQLLADIVELQTENNNEIDVCNYLKDLFDKYDIKseilkVNEHRANIVAEIGN---GSPILALSGHMDVVDAGNqdNW 84
Cdd:cd05651 1 EAIELLKSLIATPSFSREEHKTADLIENYLEQKGIP-----FKRKGNNVWAENGHfdeGKPTLLLNSHHDTVKPNA--GW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 85 TYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIrLLATAGEEKE-QEGAKLLADkgYLDDVDGLII 163
Cdd:cd05651 74 TKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGPLNYNLI-YAASAEEEISgKNGIESLLP--HLPPLDLAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 164 AEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPfIGDNAIdtllefynqfkekYSELKkhdtkhelDVApMFKSLIGKEIS 243
Cdd:cd05651 151 GEPTEMQPAIAEKGLLVLDCTARGKAGHAARN-EGDNAI-------------YKALD--------DIQ-WLRDFRFDKVS 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 244 EedanYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNdfiesffQNIINDVDSNKLSLDIPSNHRpvtsdkns 323
Cdd:cd05651 208 P----LLGPVKMTVTQINAGTQHNVVPDSCTFVVDIRTTEAYTN-------EEIFEIIRGNLKSEIKPRSFR-------- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 324 klittikdVASSYVEQDEIFVSALVGA---TDASSFLGD----NKDNVDLaifGPGNPLMAHQIDEYIEKDMYLKYIDIF 396
Cdd:cd05651 269 --------LNSSAIPPDHPIVQAAIAAgrtPFGSPTLSDqalmPFPSVKI---GPGDSSRSHTADEFIELSEIEEGIDIY 337
|
..
gi 582169601 397 KE 398
Cdd:cd05651 338 IE 339
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
55-310 |
3.71e-27 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 110.95 E-value: 3.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 55 NIVAEIGNGSPILALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLL 134
Cdd:PRK13009 49 NLWARRGTEGPHLCFAGHTDVVPPGDLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 135 ATAGEE-KEQEGAK----LLADKGYLddVDGLIIAEPT-----GSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDT 204
Cdd:PRK13009 129 ITSDEEgPAINGTVkvleWLKARGEK--IDYCIVGEPTsterlGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 205 LlefynqfkekyselkkhdtkheldvAPMFKSLIGKEISEEDANY-ASGLtaVCSIINGGKQFNSV-PDEASLEFNVRPV 282
Cdd:PRK13009 207 A-------------------------APALAELAATEWDEGNEFFpPTSL--QITNIDAGTGATNViPGELEAQFNFRFS 259
|
250 260
....*....|....*....|....*...
gi 582169601 283 PEYDNDFIESFFQNIIndvDSNKLSLDI 310
Cdd:PRK13009 260 TEHTAESLKARVEAIL---DKHGLDYTL 284
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
10-387 |
1.18e-26 |
|
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: 109.60 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 10 IQLLADIVELQ--TENNNEID-VCNYLKDLFDKYDIKSEILKVNEHRANIVAEI-GNGSPILALSGHMDVVdagnqdnwt 85
Cdd:cd03885 2 LDLLERLVNIEsgTYDKEGVDrVAELLAEELEALGFTVERRPLGEFGDHLIATFkGTGGKRVLLIGHMDTV--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 86 YP----PFQ-LTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQEGAK-LLADKGYLDDVd 159
Cdd:cd03885 73 FPegtlAFRpFTVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSReLIEEEAKGADY- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 160 gLIIAEPTGSG--IYYAHKGSMSCKVTATGKAVHSSVPFI-GDNAIDTLLEFYNQFkekyselkkhdtkHELdvapmfks 236
Cdd:cd03885 152 -VLVFEPARADgnLVTARKGIGRFRLTVKGRAAHAGNAPEkGRSAIYELAHQVLAL-------------HAL-------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 237 ligkeiseedANYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSNKLSLDI-PSNHR 315
Cdd:cd03885 210 ----------TDPEKGTTVNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTLVPGTSVELtGGLNR 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 582169601 316 PV--TSDKNSKLITTIKDVASsyvEQDEIFVSALV-GATDASSFLGDNKDNVD-LAIFGPGnplmAHQIDEYIEKD 387
Cdd:cd03885 280 PPmeETPASRRLLARAQEIAA---ELGLTLDWEATgGGSDANFTAALGVPTLDgLGPVGGG----AHTEDEYLELD 348
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
31-398 |
1.55e-26 |
|
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: 110.81 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 31 NYLKDLFDKYDIKSEILKVNEHraNIVAEIgNGS-----PILaLSGHMDVVDA--GNQDNWTYPPFQLTEKAGKLYGRGT 103
Cdd:cd05674 35 DYLEKTFPLVHKTLKVEVVNEY--GLLYTW-EGSdpslkPLL-LMAHQDVVPVnpETEDQWTHPPFSGHYDGGYIWGRGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 104 TDMKGGLMALVITLIELKEQNQLPQGTIrLLATAGEEKE--QEGAKLLAD---KGYLDD-----VD-GLIIAEPTGSGIY 172
Cdd:cd05674 111 LDDKNSLIGILEAVELLLKRGFKPRRTI-ILAFGHDEEVggERGAGAIAElllERYGVDglaaiLDeGGAVLEGVFLGVP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 173 YAH-----KGSMSCKVTATGKAVHSSVPF----IG----------DNAIDTLLEFYNQFKEKYSELKKHDTkhelDVAPM 233
Cdd:cd05674 190 FALpgvaeKGYMDVEITVHTPGGHSSVPPkhtgIGilseavaaleANPFPPKLTPGNPYYGMLQCLAEHSP----LPPRS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 234 FKSLIGKEISEEDANYASGL--------------TAVcSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIIN 299
Cdd:cd05674 266 LKSNLWLASPLLKALLASELlstspltrallrttQAV-DIINGGVKINALPETATATVNHRIAPGSSVEEVLEHVKNLIA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 300 DVDsNKLSL--------DIPSNHR-------------PVTSDKNS--KLIT-TIKDVASSYveQDEIFV--SALVGATDa 353
Cdd:cd05674 345 DIA-VKYGLglsafggdVIYSTNGtklltsllspepsPVSSTSSPvwQLLAgTIRQVFEQF--GEDLVVapGIMTGNTD- 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 582169601 354 SSFLGDNKDNV---DLAIFGPGNPLMAHQIDEYIEKDMYLKYIDIFKE 398
Cdd:cd05674 421 TRHYWNLTKNIyrfTPIRLNPEDLGRIHGVNERISIDDYLETVAFYYQ 468
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
6-157 |
4.71e-26 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 108.59 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 6 EKEKIQLLADIVELQTE-----NNNEI--DVCNYLKDLfdKYDIKSEILKVNEhrANIVAEI-GNGSP---ILALSGHMD 74
Cdd:PRK08596 12 KDELLELLKTLVRFETPapparNTNEAqeFIAEFLRKL--GFSVDKWDVYPND--PNVVGVKkGTESDaykSLIINGHMD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 75 VVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLADKGY 154
Cdd:PRK08596 88 VAEVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEVGEAGTLQCCERGY 167
|
...
gi 582169601 155 LDD 157
Cdd:PRK08596 168 DAD 170
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
53-388 |
8.35e-26 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 108.31 E-value: 8.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 53 RANIVAEIGNGSP--ILALSGHMDVVDAGNqdNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGT 130
Cdd:PRK13013 71 RWNLVARRQGARDgdCVHFNSHHDVVEVGH--GWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 131 IRLLATAGEEKEQ-EGAKLLADKGYL--DDVDGLIIAEPTGSG-IYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLL 206
Cdd:PRK13013 149 IEISGTADEESGGfGGVAYLAEQGRFspDRVQHVIIPEPLNKDrICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 207 EFYNQFKEK-YSELKKHDTKheLDVAP--------MFKSLIGKEiSEEDANYaSGLTAVCsiinggkqfnsVPDEASLEF 277
Cdd:PRK13013 229 AVLAEIEERlFPLLATRRTA--MPVVPegarqstlNINSIHGGE-PEQDPDY-TGLPAPC-----------VADRCRIVI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 278 NVRPVPEYDNDFIESFFQNIINDVDSNKLSLDIPSNH----RPVTSDKNSKLI-TTIKDVASSYVEQDEIFVSAlvGATD 352
Cdd:PRK13013 294 DRRFLIEEDLDEVKAEITALLERLKRARPGFAYEIRDlfevLPTMTDRDAPVVrSVAAAIERVLGRQADYVVSP--GTYD 371
|
330 340 350
....*....|....*....|....*....|....*....
gi 582169601 353 ASSF--LGDNKDNVdlaIFGPGNPLMAHQIDEYIE-KDM 388
Cdd:PRK13013 372 QKHIdrIGKLKNCI---AYGPGILDLAHQPDEWVGiADM 407
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
58-399 |
1.15e-25 |
|
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: 108.10 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 58 AEIGNGSPILALSGHMDVVDAGnqDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATA 137
Cdd:cd03888 65 AEYGEGEEVLGILGHLDVVPAG--EGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 138 GEE----------KEQEGAKLL-----------ADKGYL--------------------------------------DDV 158
Cdd:cd03888 143 DEEtgwkciehyfEHEEYPDFGftpdaefpvinGEKGIVtvdltfkidddkgyrlisikggeatnmvpdkaeavipgKDK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 159 DGLIIAEPTGSGIYYAHKGSMScKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFkekysELKKHDTKheldvapmFKSLI 238
Cdd:cd03888 223 EELALSAATDLKGNIEIDDGGV-ELTVTGKSAHASAPEKGVNAITLLAKFLAEL-----NKDGNDKD--------FIKFL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 239 GKEISEEDA------NYASGLTAVCSIINGGKQFNsvPDEASLEFNVRpVPE-YDNDFIesffQNIIND-VDSNKLSLDI 310
Cdd:cd03888 289 AKNLHEDYNgkklgiNFEDEVMGELTLNPGIITLD--DGKLELGLNVR-YPVgTSAEDI----IKQIEEaLEKYGVEVEG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 311 PSNHRPVTSDKNSKLITTIKDVASSYVEQD-EIFVSAlvGATDASSFlgdnKDNVdlaIFG---PGNPLMAHQIDEYIEK 386
Cdd:cd03888 362 HKHQKPLYVPKDSPLVKTLLKVYEEQTGKEgEPVAIG--GGTYAREL----PNGV---AFGpefPGQKDTMHQANEFIPI 432
|
410
....*....|...
gi 582169601 387 DMYLKYIDIFKEA 399
Cdd:cd03888 433 DDLIKALAIYAEA 445
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
29-384 |
1.97e-24 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 103.77 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 29 VCNYLKDLFDK----YDIKSEILKvNEHRANIVAEI--GNGSPILALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRG 102
Cdd:PRK13983 36 LESLLKEYGFDeverYDAPDPRVI-EGVRPNIVAKIpgGDGKRTLWIISHMDVVPPGDLSLWETDPFKPVVKDGKIYGRG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 103 TTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEkeqEGAK-----LLADKGYLDDVDGLII----AEPTGSGIYY 173
Cdd:PRK13983 115 SEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEE---TGSKygiqyLLKKHPELFKKDDLILvpdaGNPDGSFIEI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 174 AHKGSMSCKVTATGKAVHSSVPFIGDNA----IDTLLEFYNQFKEKYSElkkhdtKHELDVAPM--FksligkEISEEDA 247
Cdd:PRK13983 192 AEKSILWLKFTVKGKQCHASTPENGINAhraaADFALELDEALHEKFNA------KDPLFDPPYstF------EPTKKEA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 248 NyasgltaVCSIinggkqfNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSN---KLSLDI--PSNHRPVTsDKN 322
Cdd:PRK13983 260 N-------VDNI-------NTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIADEFEEEygvKIEVEIvqREQAPPPT-PPD 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 582169601 323 SKLITTIKDVASSyVEQDEIFVSALVGATDASSFlgdNKDNVDLAIFGPGNPlMAHQIDEYI 384
Cdd:PRK13983 325 SEIVKKLKRAIKE-VRGIEPKVGGIGGGTVAAFL---RKKGYPAVVWSTLDE-TAHQPNEYA 381
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
26-298 |
2.89e-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: 100.24 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 26 EIDVCNYLKDLFDKYDIKSEILKVNEHRANIVAEI---GNGSPILaLSGHMDVVdagNQDNWTYPPFQLTEKAGKLYGRG 102
Cdd:cd08013 28 EAEIATYVAAWLAHRGIEAHRIEGTPGRPSVVGVVrgtGGGKSLM-LNGHIDTV---TLDGYDGDPLSGEIADGRVYGRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 103 TTDMKGGLMALVITLIELKEQNqlPQGTIRLLATAGEEKEQEGAKLLADKGYldDVDGLIIAEPTGSGIYYAHKGSMSCK 182
Cdd:cd08013 104 TLDMKGGLAACMAALADAKEAG--LRGDVILAAVADEEDASLGTQEVLAAGW--RADAAIVTEPTNLQIIHAHKGFVWFE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 183 VTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYSELkkhdtkheldvapmfksligkEISEEDANYASGlTAVCSIING 262
Cdd:cd08013 180 VDIHGRAAHGSRPDLGVDAILKAGYFLVALEEYQQEL---------------------PERPVDPLLGRA-SVHASLIKG 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 582169601 263 GKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNII 298
Cdd:cd08013 238 GEEPSSYPARCTLTIERRTIPGETDESVLAELTAIL 273
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
65-398 |
7.40e-23 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 100.02 E-value: 7.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 65 PILaLSGHMDVV--DAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKE 142
Cdd:PRK08262 113 PIV-LMAHQDVVpvAPGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVG 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 143 QEGAKLLADkgYLDD--------VD-GLIIAE--------PTGS-GIyyAHKGSMSCKVTATGKAVHSSVPFiGDNAIDT 204
Cdd:PRK08262 192 GLGARAIAE--LLKErgvrlafvLDeGGAITEgvlpgvkkPVALiGV--AEKGYATLELTARATGGHSSMPP-RQTAIGR 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 205 L------LEfYNQFKEKYSELkkhdTKHELDV-AP--------------MFKSLIGKEISEEDANYAS--GLTAVcSIIN 261
Cdd:PRK08262 267 LaraltrLE-DNPLPMRLRGP----VAEMFDTlAPemsfaqrvvlanlwLFEPLLLRVLAKSPETAAMlrTTTAP-TMLK 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 262 GGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSNKLSLDIPSNHRPVTSDKN---SKLITTIKDVAssyve 338
Cdd:PRK08262 341 GSPKDNVLPQRATATVNFRILPGDSVESVLAHVRRAVADDRVEIEVLGGNSEPSPVSSTDSaayKLLAATIREVF----- 415
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 582169601 339 QDEIFVSALV-GATDASSFLGDNkDNV-----------DLAIFgpgnplmaHQIDEYIEKDMYLKYIDIFKE 398
Cdd:PRK08262 416 PDVVVAPYLVvGATDSRHYSGIS-DNVyrfsplrlspeDLARF--------HGTNERISVANYARMIRFYYR 478
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
8-398 |
1.17e-21 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 95.21 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 8 EKIQLLADIVELQTENNNEIDVCNYLKDLFDK--YDIKSEilkVNEHRANIVAeigNGSPILALSGHMDVVDAgnqdnwT 85
Cdd:PRK08652 3 RAKELLKQLVKIPSPSGQEDEIALHIMEFLESlgYDVHIE---SDGEVINIVV---NSKAELFVEVHYDTVPV------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 86 YPPFqltEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATagEEKEQEGAKLLADK---GYLddvdglI 162
Cdd:PRK08652 71 AEFF---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSD--EEEGGRGSALFAERyrpKMA------I 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 163 IAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNqfkekysELKKHDTKHELDVAPMFksligkei 242
Cdd:PRK08652 140 VLEPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLE-------KLKELLKALGKYFDPHI-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 243 seedanyasGLTavcsIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSNKLSLDIPSNHRpvtSDKN 322
Cdd:PRK08652 205 ---------GIQ----EIIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEYTEIWDGFE---LDED 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 323 SKLITTIKDvASSYVEQDEIFVsALVGATDASSFlgdnKDN-VDLAIFGPGNPLMAHQIDEYIE-------KDMYLKYID 394
Cdd:PRK08652 269 EEIVQLLEK-AMKEVGLEPEFT-VMRSWTDAINF----RYNgTKTVVWGPGELDLCHTKFERIDvrevekaKEFLKALNE 342
|
....
gi 582169601 395 IFKE 398
Cdd:PRK08652 343 ILLE 346
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
55-167 |
6.55e-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: 89.80 E-value: 6.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 55 NIVAEIGNGS--PILALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIR 132
Cdd:cd18669 1 NVIARYGGGGggKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 582169601 133 LLATAGEEKEQEGAKLLADKGYL---DDVDGLIIAEPT 167
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLSKDALeedLKVDYLFVGDAT 118
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
58-399 |
1.13e-20 |
|
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: 93.21 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 58 AEIGNGSPILALSGHMDVVDAGnqDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATA 137
Cdd:TIGR01887 61 IEYGQGEEVLGILGHLDVVPAG--DGWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGT 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 138 GEEKEQEGAKL------LADKGYLDDVDGLIIaeptgsgiyYAHKGSMSCKVTATGKAVHSSV--PFIGDNAIDTL---- 205
Cdd:TIGR01887 139 DEESGWKCIDYyfeheeMPDIGFTPDAEFPII---------YGEKGITTLEIKFKDDTEGDVVleSFKAGEAYNMVpdha 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 206 ------LEFYNQFKEKYSELKKHDTKHELDVAPMFKSLIGKEISEEDANYASGLTAVCSIINGGKQFNsvpdeaslefnv 279
Cdd:TIGR01887 210 tavisgKKLTEVEQLKFVFFIAKELEGDFEVNDGTLTITLEGKSAHGSAPEKGINAATYLALFLAQLN------------ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 280 rpVPEYDNDFIESFFQNIINDVDSNKLSLD-------------------------IPSNHR-PVTSDKNSKL------IT 327
Cdd:TIGR01887 278 --LAGGAKAFLQFLAEYLHEDHYGEKLGIKfhddvsgdltmnvgvidyenaeaglIGLNVRyPVGNDPDTMLknelakES 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 328 TIKDV------ASSYVEQDEIFVSALV-----------------GATDASSFlgdnKDNVDL-AIFgPGNPLMAHQIDEY 383
Cdd:TIGR01887 356 GVVEVtlngylKPLYVPKDDPLVQTLMkvyekqtgdegepvaigGGTYARLM----PNGVAFgALF-PGEEDTMHQANEY 430
|
410
....*....|....*.
gi 582169601 384 IEKDMYLKYIDIFKEA 399
Cdd:TIGR01887 431 IMIDDLLLATAIYAEA 446
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
24-398 |
1.22e-20 |
|
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: 93.17 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 24 NNEIDVC-NYLKDLFDKYDIKSEILKVNEHRAnIVAEIGNGS-PILALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGR 101
Cdd:cd05681 18 GRGIPETaDFLKEFLRRLGAEVEIFETDGNPI-VYAEFNSGDaKTLLFYNHYDVQPAEPLELWTSDPFELTIRNGKLYAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 102 GTTDMKGGLMALVITLIELKEQ-NQLPQgTIRLLATAGEEK---------EQEGAKLLAD-----KGYLDDVDGLIIAEP 166
Cdd:cd05681 97 GVADDKGELMARLAALRALLQHlGELPV-NIKFLVEGEEEVgspnlekfvAEHADLLKADgciweGGGKNPKGRPQISLG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 167 TGSGIYYahkgSMSCKVTAtgKAVHSSVPFIGDN-------AIDTLLE---------FYNQFKEKYSELKKHDTKHELDV 230
Cdd:cd05681 176 VKGIVYV----ELRVKTAD--FDLHSSYGAIVENpawrlvqALNSLRDedgrvlipgFYDDVRPLSEAERALIDTYDFDP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 231 APMFKSLIGKE-ISEEDANYASGLTA--VCSI--INGGKQFNS----VPDEASLEFNVRPVPEYDNDFIESFFQNIINDV 301
Cdd:cd05681 250 EELRKTYGLKRpLQVEGKDPLRALFTepTCNIngIYSGYTGEGsktiLPSEAFAKLDFRLVPDQDPAKILSLLRKHLDKN 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 302 DSNKLSLDIPSNHRPVTSDKNSKLITTIKDVASSYVEQDEIFVSALVGATDASSFLGDNKDNVDLaiFGPGNP-LMAHQI 380
Cdd:cd05681 330 GFDDIEIHDLLGEKPFRTDPDAPFVQAVIESAKEVYGQDPIVLPNSAGTGPMYPFYDALEVPVVA--IGVGNAgSNAHAP 407
|
410
....*....|....*...
gi 582169601 381 DEYIEKDMYLKYIDIFKE 398
Cdd:cd05681 408 NENIRIADYYKGIEHTEE 425
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
2-399 |
2.04e-20 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 91.56 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 2 TTFSEKEKIQLLADIVELQTENNNEIDVCNYLKDLFDKYDIKSEILKVnehrANIVAEIGNGSPILALSGHMDVVdAGnq 81
Cdd:PRK04443 1 MTISALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREAWVDEA----GNARGPAGDGPPLVLLLGHIDTV-PG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 82 dnwtYPPFQLteKAGKLYGRGTTDMKGGLMALVITLIELKeqnQLPQGTIRLLATAGEE-KEQEGAKLLADKGYLDDVdg 160
Cdd:PRK04443 74 ----DIPVRV--EDGVLWGRGSVDAKGPLAAFAAAAARLE---ALVRARVSFVGAVEEEaPSSGGARLVADRERPDAV-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 161 lIIAEPTG-SGIYYAHKGSMSCKVTATGKAVHSSVPfiGDNAIDTLLEFYNQFKEkYSELKKHDTkheldvaPMFKSLIG 239
Cdd:PRK04443 143 -IIGEPSGwDGITLGYKGRLLVTYVATSESFHSAGP--EPNAAEDAIEWWLAVEA-WFEANDGRE-------RVFDQVTP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 240 KEI---SEEDanyasGLTavcsiinggkqfnsvpDEASLEFNVRPVPEYDNDFIESffqniINDVDSNKLSLDIPSNHRP 316
Cdd:PRK04443 212 KLVdfdSSSD-----GLT----------------VEAEMTVGLRLPPGLSPEEARE-----ILDALLPTGTVTFTGAVPA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 317 VTSDKNSKLITTikdvassyveqdeiFVSALVGATDASSFL---GDNKDNV-------DLAIFGPGNPLMAHQIDEYIEK 386
Cdd:PRK04443 266 YMVSKRTPLARA--------------FRVAIREAGGTPRLKrktGTSDMNVvapawgcPMVAYGPGDSDLDHTPDEHLPL 331
|
410
....*....|...
gi 582169601 387 DMYLKYIDIFKEA 399
Cdd:PRK04443 332 AEYLRAIAVLTDV 344
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
55-167 |
3.41e-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: 87.87 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 55 NIVAEIGNGS--PILALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIR 132
Cdd:cd03873 1 NLIARLGGGEggKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 582169601 133 LLATAGEEKEQEGAKLLADKGYLD---DVDGLIIAEPT 167
Cdd:cd03873 81 VAFTADEEVGSGGGKGLLSKFLLAedlKVDAAFVIDAT 118
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
173-301 |
1.31e-19 |
|
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: 83.55 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 173 YAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYSelkkhdtkheldvapmfksligkeiseEDANYASG 252
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYG---------------------------DIGFDFPR 53
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 582169601 253 LTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDV 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 |
1.38e-18 |
|
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: 86.56 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 65 PILALSGHMDVVDAgNQDNWTYPPFQLTEKA-GKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEE-KE 142
Cdd:cd05646 65 PSILLNSHTDVVPV-FEEKWTHDPFSAHKDEdGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEiGG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 143 QEGAKLLADKGY---------LDDvdGLiiAEPTGS-GIYYAHKGSMSCKVTATGKAVHSSVpFIGDNAIDTLLEFYNQF 212
Cdd:cd05646 144 HDGMEKFVKTEEfkklnvgfaLDE--GL--ASPTEEyRVFYGERSPWWVVITAPGTPGHGSK-LLENTAGEKLRKVIESI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 213 ----KEKYSELKKHDTKHELDVapmfksligkeiseedanyasglTAV-CSIINGGKQFNSVPDEASLEFNVRPVPEYD- 286
Cdd:cd05646 219 mefrESQKQRLKSNPNLTLGDV-----------------------TTVnLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDl 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 287 NDF---IESFFQNIINDVdsnKLSLDIPSNHRPVTS--DKN---SKLITTIKDVASSYveQDEIFvsalVGATDaSSFLg 358
Cdd:cd05646 276 EEFekqIDEWCAEAGRGV---TYEFEQKSPEKDPTSldDSNpwwAAFKKAVKEMGLKL--KPEIF----PAATD-SRYI- 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 582169601 359 dnkDNVDLAIFG--PGN--PLMAHQIDEYIEKDMYLKYIDIFKE 398
Cdd:cd05646 345 ---RALGIPALGfsPMNntPILLHDHNEFLNEDVFLRGIEIYEK 385
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
11-286 |
2.46e-18 |
|
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation.
Pssm-ID: 349888 [Multi-domain] Cd Length: 426 Bit Score: 86.23 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 11 QLLADIVELQTENNNEID------VCNYLKDLFDKYDIKSEILKVNEHRANIVAEIGN--GSPILALSGHMDVVDAGNQD 82
Cdd:cd03893 2 QTLAELVAIPSVSAQPDRreelrrAAEWLADLLRRLGFTVEIVDTSNGAPVVFAEFPGapGAPTVLLYGHYDVQPAGDED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 83 NWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQEG-AKLLADKGYLDDVDGL 161
Cdd:cd03893 82 GWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEESGSPSlDQLVEAHRDLLAADAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 162 IIAEPTGSG-----IYYAHKGSMSCKVTATG--KAVHSSVpFIG--DNAIDTLLEFYNQFkekyselkkHDTKHELDVAP 232
Cdd:cd03893 162 VISDSTWVGqeqptLTYGLRGNANFDVEVKGldHDLHSGL-YGGvvPDPMTALAQLLASL---------RDETGRILVPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 233 MFKSLigKEISEEDANYASGLTAVCSIINGGKQ--------------------------FNSVPDEASLEFNVRPVPEYD 286
Cdd:cd03893 232 LYDAV--RELPEEEFRLDAGVLEEVEIIGGTTGsvaerlwtrpaltvlgidggfpgegsKTVIPPRARAKISIRLVPGQD 309
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
67-280 |
5.07e-18 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 85.44 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 67 LALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQEGA 146
Cdd:PRK06837 100 LILQGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEESTGNGA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 147 KLLADKGYldDVDGLIIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYSELKKHDTKH 226
Cdd:PRK06837 180 LSTLQRGY--RADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRELEAEWNARKASD 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 582169601 227 eldvaPMFKSLigkeisEEDANYASGltavcsIINGGKQFNSVPdeASLEFNVR 280
Cdd:PRK06837 258 -----PHFEDV------PHPINFNVG------IIKGGDWASSVP--AWCDLDCR 292
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
58-399 |
7.58e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 84.75 E-value: 7.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 58 AEIGNGSPILALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATA 137
Cdd:PRK07205 69 AEIGQGEELLAILCHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 138 GEE---------KEQEGaklLADKGYLDDVDGLIIaeptgsgiyYAHKGSMSCKVTATGK------------AVHSSVPF 196
Cdd:PRK07205 149 DEEtlwrcmnryNEVEE---QATMGFAPDSSFPLT---------YAEKGLLQAKLVGPGSdqlelevgqafnVVPAKASY 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 197 IGDnaidtLLEfynqfkEKYSELKKHDTKHELDVAPMfkSLIGKEISEEDAnyASGLTAvcsIINGGKQFNSVPDEASLE 276
Cdd:PRK07205 217 QGP-----KLE------AVKKELDKLGFEYVVKENEV--TVLGKSVHAKDA--PQGINA---VIRLAKALVVLEPHPALD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 277 FNVRPVPEYDNDFiesffqNIINDVD---SNKLS-----LDIPSNHR--------PVTSDKNsKLITTIKDVASS----- 335
Cdd:PRK07205 279 FLANVIGEDATGL------NIFGDIEdepSGKLSfniagLTITKEKSeiridiriPVLADKE-KLVQQLSQKAQEyglty 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 336 ---------YVEQDEIFVSALV-----------------GATDASSFlgdnkDN-VDL-AIFgPGNPLMAHQIDEYIE-K 386
Cdd:PRK07205 352 eefdylaplYVPLDSELVSTLMsvyqektgddspaqssgGATFARTM-----PNcVAFgALF-PGAPQTEHQANEHIVlE 425
|
410
....*....|...
gi 582169601 387 DMYlKYIDIFKEA 399
Cdd:PRK07205 426 DLY-RAMDIYAEA 437
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
53-391 |
1.42e-17 |
|
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: 83.30 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 53 RANIVAEI-GNGS-PILALSGHMDVVDAGnQDNWTyppfqLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGT 130
Cdd:cd03896 41 RGNVVGRLrGTGGgPALLFSAHLDTVFPG-DTPAT-----VRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 131 IRLLATAGEEKEQE--GAK-LLADKGYLddVDGLIIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLle 207
Cdd:cd03896 115 VVFAANVGEEGLGDlrGARyLLSAHGAR--LDYFVVAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAM-- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 208 fynqfkekyselkkhdtkheldvapmfkSLIGKEISEEDANYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDN 287
Cdd:cd03896 191 ----------------------------AKLVEALYEWAAPYVPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPDAEL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 288 DFIESFFQNIINDVDSNKLSLDI---PSNHRPVTSDKNSKLITTIKDVASSYVEQDEIFVSALVGATDASSfLGdnkdnV 364
Cdd:cd03896 243 ADVQREVEAVVSKLAAKHLRVKArvkPVGDRPGGEAQGTEPLVNAAVAAHREVGGDPRPGSSSTDANPANS-LG-----I 316
|
330 340
....*....|....*....|....*..
gi 582169601 365 DLAIFGPGNPLMAHQIDEYIEKDMYLK 391
Cdd:cd03896 317 PAVTYGLGRGGNAHRGDEYVLKDDMLK 343
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
31-398 |
1.82e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 83.65 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 31 NYLKDLFDKYDIKSEILKvneHRAN--IVAEIGNGS-PILALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMK 107
Cdd:PRK06446 29 NYLKDTMEKLGIKANIER---TKGHpvVYGEINVGAkKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 108 GGLMALVITLIELKEQNQLPQgTIRLLAtagEEKEQEGAKLLADkgYLDDVDGLIIAEPT---GSG--------IYYAHK 176
Cdd:PRK06446 106 GTLMARLFAIKHLIDKHKLNV-NVKFLY---EGEEEIGSPNLED--FIEKNKNKLKADSVimeGAGldpkgrpqIVLGVK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 177 GSMSCKVTA-TG-KAVHSS-VPFIGDNAID---------------TLLEFYNQFKEKYSELKKHDTKHELDVAPMFKSLI 238
Cdd:PRK06446 180 GLLYVELVLrTGtKDLHSSnAPIVRNPAWDlvkllstlvdgegrvLIPGFYDDVRELTEEERELLKKYDIDVEELRKALG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 239 GKEIS-EEDANYASGLTA--VCSI------INGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSNkLSLD 309
Cdd:PRK06446 260 FKELKySDREKIAEALLTepTCNIdgfysgYTGKGSKTIVPSRAFAKLDFRLVPNQDPYKIFELLKKHLQKVGFN-GEII 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 310 IPSNHRPVTSDKNSKLITTIKDVASSYVEQDEIFVSALVGATDASSFLGDNKDNVDLAIFGPGNPLM-AHQIDEYIEKDM 388
Cdd:PRK06446 339 VHGFEYPVRTSVNSKVVKAMIESAKRVYGTEPVVIPNSAGTQPMGLFVYKLGIRDIVSAIGVGGYYSnAHAPNENIRIDD 418
|
410
....*....|
gi 582169601 389 YLKYIDIFKE 398
Cdd:PRK06446 419 YYKAIKHTEE 428
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
65-396 |
4.28e-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: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 65 PILALSGHMDVVDAgNQDNWTYPPFQ-LTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEE-KE 142
Cdd:TIGR01880 72 PSILLNSHTDVVPV-FREHWTHPPFSaFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEiGG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 143 QEGAKLLADKGYLDDVDGLI-----IAEPTGS-GIYYAHKGSMSCKVTATGKAVHSSVpFIGDNAIDTLLEFYN---QFK 213
Cdd:TIGR01880 151 HDGMEKFAKTDEFKALNLGFaldegLASPDDVyRVFYAERVPWWVVVTAPGNPGHGSK-LMENTAMEKLEKSVEsirRFR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 214 EKYSELKKhdtkheldvapmfksligkeiSEEDANYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESF 293
Cdd:TIGR01880 230 ESQFQLLQ---------------------SNPDLAIGDVTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENR 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 294 FQNIINDVDSN-KLSLDIPSNHRPVT--SDKN---SKLITTIKDVASSYveQDEIFVsalvGATDASSFlgdNKDNVDLA 367
Cdd:TIGR01880 289 LDEWCADAGEGvTYEFSQHSGKPLVTphDDSNpwwVAFKDAVKEMGCTF--KPEILP----GSTDSRYI---RAAGVPAL 359
|
330 340 350
....*....|....*....|....*....|.
gi 582169601 368 IFGPGN--PLMAHQIDEYIEKDMYLKYIDIF 396
Cdd:TIGR01880 360 GFSPMNntPVLLHDHNEFLNEAVFLRGIEIY 390
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
10-152 |
7.13e-17 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 82.13 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 10 IQLLADIVELQTENNNEI------DVCNYLKDLFDKYDIKSEILKVNEHRAnIVAEIGNGSPILALSGHMDVVDAgNQDN 83
Cdd:PRK08554 4 LELLSSLVSFETVNDPSKgikpskECPKFIKDTLESWGIESELIEKDGYYA-VYGEIGEGKPKLLFMAHFDVVPV-NPEE 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 582169601 84 WTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQlpQGTIRLLATAGEEKEQEGAKLLADK 152
Cdd:PRK08554 82 WNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPL--NGKVIFAFTGDEEIGGAMAMHIAEK 148
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
53-304 |
8.78e-17 |
|
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: 81.74 E-value: 8.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 53 RANIVAEIGNGSP--ILALSG-HMDVVDAgNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLmALVITL-IELKEQNQLPQ 128
Cdd:cd08012 64 RGNIIVEYPGTVDgkTVSFVGsHMDVVTA-NPETWEFDPFSLSIDGDKLYGRGTTDCLGHV-ALVTELfRQLATEKPALK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 129 GTIRLLATAGEEKEQ---EGAKLLADKGYLDDV-DGLII------AEPT-GSGiyyahkGSMSCKVTATGKAVHSSVPFI 197
Cdd:cd08012 142 RTVVAVFIANEENSEipgVGVDALVKSGLLDNLkSGPLYwvdsadSQPCiGTG------GMVTWKLTATGKLFHSGLPHK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 198 GDNAIDTLLE--------FYNQFKekyselkkhdtKHEldvapmfksligkeiSEEDANYASGLT---AVCSIINGGkqF 266
Cdd:cd08012 216 AINALELVMEalaeiqkrFYIDFP-----------PHP---------------KEEVYGFATPSTmkpTQWSYPGGS--I 267
|
250 260 270
....*....|....*....|....*....|....*...
gi 582169601 267 NSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDVDSN 304
Cdd:cd08012 268 NQIPGECTICGDCRLTPFYDVKEVREKLEEYVDDINAN 305
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
58-401 |
1.46e-15 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 77.96 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 58 AEIGNGSPILALSGHMDVVDAGnqDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATA 137
Cdd:PRK07318 73 IEYGEGEEVLGILGHLDVVPAG--DGWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRFIVGT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 138 GEEK---------EQEGAKLL------------ADKG----YLDDVDGliiaEPTG--------SGIYY----------- 173
Cdd:PRK07318 151 DEESgwkcmdyyfEHEEAPDFgfspdaefpiinGEKGittfDLVHFEG----ENEGdyvlvsfkSGLREnmvpdsaeavi 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 174 ------------------------AHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFkekysELKKhDTKHELD 229
Cdd:PRK07318 227 tgddlddliaafeaflaenglkgeLEEEGGKLVLTVIGKSAHGSTPEKGVNAATYLAKFLNQL-----NLDG-DAKAFLD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 230 VAP--MFKSLIGKE--ISEEDAnyASG-LTAVCSIINGGKQfnsvpDEASLEFNVR-PVpEYDNDFIESFFQNIIndvDS 303
Cdd:PRK07318 301 FAAeyLHEDTRGEKlgIAYEDD--VMGdLTMNVGVFSFDEE-----KGGTLGLNFRyPV-GTDFEKIKAKLEKLI---GV 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 304 NKLSLDIPSNHRPVTSDKNSKLITTIKDVassYVEQDEIFVSALV--GATDASSFlgdnKDNVDL-AIFgPGNPLMAHQI 380
Cdd:PRK07318 370 TGVELSEHEHQKPHYVPKDDPLVKTLLKV---YEKQTGLKGEEQVigGGTYARLL----KRGVAFgAMF-PGSEDTMHQA 441
|
410 420
....*....|....*....|.
gi 582169601 381 DEYIEKDmylkyiDIFKEASI 401
Cdd:PRK07318 442 NEYIEID------DLIKAAAI 456
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
4-401 |
6.19e-15 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 75.20 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 4 FSEKEKI-----QLLADIVELQTENNNEidvcNYLKDLFDKydIKSEI-LKVNEHRANIVAEIGNGSPILAlsGHMDVVd 77
Cdd:PRK00466 2 QQEKELVkqkakELLLDLLSIYTPSGNE----TNATKFFEK--ISNELnLKLEILPDSNSFILGEGDILLA--SHVDTV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 78 agnqdnwtyPPF-QLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQlpqgTIRLLATAGEEKEQEGAKLLADKGylD 156
Cdd:PRK00466 73 ---------PGYiEPKIEGEVIYGRGAVDAKGPLISMIIAAWLLNEKGI----KVMVSGLADEESTSIGAKELVSKG--F 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 157 DVDGLIIAEPT-GSGIYYAHKGSMSCKVTATGKAVHSSVPfiGDNAIDTLLefynqfkekyselkkhdtkheldvapmfK 235
Cdd:PRK00466 138 NFKHIIVGEPSnGTDIVVEYRGSIQLDIMCEGTPEHSSSA--KSNLIVDIS----------------------------K 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 236 SLIgkEISEEDANYASgLTAVCSIINGGKQFNSVPDEASLEFNVR-PVPEYDNDFI----ESFFQNIINDVDsnklslDI 310
Cdd:PRK00466 188 KII--EVYKQPENYDK-PSIVPTIIRAGESYNVTPAKLYLHFDVRyAINNKRDDLIseikDKFQECGLKIVD------ET 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 311 PsnhrPVTSDKNSkliTTIKDVASSYVEQDEIFVSALVGATDASSFLGDNKDNVdlAIFGPGNPLMAHQIDEYIEKDmyl 390
Cdd:PRK00466 259 P----PVKVSINN---PVVKALMRALLKQNIKPRLVRKAGTSDMNILQKITTSI--ATYGPGNSMLEHTNQEKITLD--- 326
|
410
....*....|.
gi 582169601 391 kyiDIFKEASI 401
Cdd:PRK00466 327 ---EIYIAVKT 334
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
56-357 |
3.77e-14 |
|
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: 73.15 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 56 IVAEIGNGSP--ILALSGHMDVVDAGNQDNWtypPFQLTEKaGKLYGRGttdmKGGLMA-LVITLIELKEQNQLPQGTIR 132
Cdd:TIGR01891 46 VVATIGGGKPgpVVALRADMDALPIQEQTDL---PYKSTNP-GVMHACG----HDLHTAiLLGTAKLLKKLADLLEGTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 133 LLATAGEEKEQEGAKLLADkGYLDDVDGLIIAEP----------TGSGIYYAhkGSMSCKVTATGKAVHSSVPFIGDNAI 202
Cdd:TIGR01891 118 LIFQPAEEGGGGATKMIED-GVLDDVDAILGLHPdpsipagtvgLRPGTIMA--AADKFEVTIHGKGAHAARPHLGRDAL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 203 DTLLEFYNQFkekyselkkhdtkheldvapmfksligKEISEEDANYASGLTAVCSIINGGKQFNSVPDEASLEFNVRPV 282
Cdd:TIGR01891 195 DAAAQLVVAL---------------------------QQIVSRNVDPSRPAVVSVGIIEAGGAPNVIPDKASMSGTVRSL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 283 PEYDNDFIESFFQNIINDVDSN---KLSLDIPSNHRPVTSDK--NSKLITTIKDVASSYVEQDEIFVSAlvGATDASSFL 357
Cdd:TIGR01891 248 DPEVRDQIIDRIERIVEGAAAMygaKVELNYDRGLPAVTNDPalTQILKEVARHVVGPENVAEDPEVTM--GSEDFAYYS 325
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
62-192 |
7.35e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 72.63 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 62 NGSPILALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEqnQLPQGtIRLLAtAGEEk 141
Cdd:PRK07907 81 PGAPTVLLYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRALGG--DLPVG-VTVFV-EGEE- 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 582169601 142 EQEGA---KLLADKGYLDDVDGLIIA--------EPTgsgIYYAHKGSMSCKVTAT--GKAVHS 192
Cdd:PRK07907 156 EMGSPsleRLLAEHPDLLAADVIVIAdsgnwsvgVPA---LTTSLRGNADVVVTVRtlEHAVHS 216
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
5-390 |
1.50e-13 |
|
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: 71.33 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 5 SEKEKIQLLADIVELQTENNNEIDVCNYLKDLFDKYD---IKSEILKVNEHRA-NIV----AEIGNGSPILaLSGHMDVV 76
Cdd:cd05683 1 NEDRLINTFLELVQIDSETLHEKEISKVLKKKFENLGlsvIEDDAGKTTGGGAgNLIctlkADKEEVPKIL-FTSHMDTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 77 DAGNQDnwtyPPFQltEKAGKLYGRGTT----DMKGGLMALVITLIELKEQNqLPQGTIRLLATAGEEKEQEGAKLL--- 149
Cdd:cd05683 80 TPGINV----KPPQ--IADGYIYSDGTTilgaDDKAGIAAILEAIRVIKEKN-IPHGQIQFVITVGEESGLVGAKALdpe 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 150 ---ADKGYLDDVDG----LIIAEPTGSGIYyahkgsmsckVTATGKAVHSSV-PFIGDNAIDTLLEFYNQFKekyselkk 221
Cdd:cd05683 153 lidADYGYALDSEGdvgtIIVGAPTQDKIN----------AKIYGKTAHAGTsPEKGISAINIAAKAISNMK-------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 222 hdtkheldvapmfkslIGKeISEEDanyasglTAVCSIINGGKQFNSVPDEASLEFNVRpvpEYDNDFIES----FFQNI 297
Cdd:cd05683 215 ----------------LGR-IDEET-------TANIGKFQGGTATNIVTDEVNIEAEAR---SLDEEKLDAqvkhMKETF 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 298 INDVDSNKLSLDIPSN--HRPVTSDKNSKLITTIKDVASSYVEQDEIFVSAlvGATDASSFLGDNKDNVDLAIfGPGNpl 375
Cdd:cd05683 268 ETTAKEKGAHAEVEVEtsYPGFKINEDEEVVKLAKRAANNLGLEINTTYSG--GGSDANIINGLGIPTVNLGI-GYEN-- 342
|
410
....*....|....*.
gi 582169601 376 mAHQIDEYIE-KDMYL 390
Cdd:cd05683 343 -IHTTNERIPiEDLYD 357
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
56-165 |
2.46e-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: 71.09 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 56 IVAEIGN--GSPILALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALvITLIE--LKEQNQLPQgTI 131
Cdd:cd05676 75 LLGRLGSdpSKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGW-LNAIEayQKLGQELPV-NL 152
|
90 100 110
....*....|....*....|....*....|....*..
gi 582169601 132 RLLATAGEEKEQEG-AKLLADKG--YLDDVDGLIIAE 165
Cdd:cd05676 153 KFCFEGMEESGSEGlDELIEARKdtFFSDVDYVCISD 189
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
59-300 |
1.07e-12 |
|
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: 69.12 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 59 EIGNGSPILALSGHMDVVDAGnqDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAG 138
Cdd:cd02697 68 RYGDGGRTVALNAHGDVVPPG--DGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 139 EEKEQE-GAKLLADKGyLDDVDgLIIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPFIGDNAIDTLLEFYNQFKEKYS 217
Cdd:cd02697 146 EEFGGElGPGWLLRQG-LTKPD-LLIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 218 ELKKHDTKHELDVAPMFKslIGKeiseedanyasgltavcsiINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNI 297
Cdd:cd02697 224 QYRQVSSQVEGITHPYLN--VGR-------------------IEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRV 282
|
...
gi 582169601 298 IND 300
Cdd:cd02697 283 IAD 285
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
32-207 |
1.90e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 68.34 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 32 YLKDLFDKYDIKSEILKVNEHRANIVAEIGN---GSPILALSGHMDVVDAgNQDNWTYPPFQLTEKAGKLYGRGTTDMKg 108
Cdd:PRK07906 30 YVAEKLAEVGLEPTYLESAPGRANVVARLPGadpSRPALLVHGHLDVVPA-EAADWSVHPFSGEIRDGYVWGRGAVDMK- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 109 GLMALVITLI-ELKEQNQLPQGTIRLLATAGEEKEQE-GAKLLADK--GYLDDVD-------GLIIAEPTGSGIYY---A 174
Cdd:PRK07906 108 DMDAMMLAVVrHLARTGRRPPRDLVFAFVADEEAGGTyGAHWLVDNhpELFEGVTeaisevgGFSLTVPGRDRLYLietA 187
|
170 180 190
....*....|....*....|....*....|...
gi 582169601 175 HKGSMSCKVTATGKAVHSSVPfIGDNAIDTLLE 207
Cdd:PRK07906 188 EKGLAWMRLTARGRAGHGSMV-NDDNAVTRLAE 219
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
31-164 |
4.01e-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: 67.37 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 31 NYLKDLFDKYDIKSEILKVNEHRAN-IV--AEIGNGSP-----ILaLSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRG 102
Cdd:cd05677 31 IFLRQLFKKLGATNCLLLPSGPGTNpIVlaTFSGNSSDakrkrIL-FYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRG 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 582169601 103 TTDMKGGLMALVITLIELKEQNQLPQGTIRLLatagEEKEQEGAKLLAD-----KGYLDDVDGLIIA 164
Cdd:cd05677 110 VSDNKGPLLAAIYAVAELFQEGELDNDVVFLI----EGEEESGSPGFKEvlrknKELIGDIDWILLS 172
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
69-333 |
1.38e-11 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 65.75 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 69 LSGHMDVVdagnqdnwtYP---PFQLTE--KAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKEQ 143
Cdd:PRK07338 97 LTGHMDTV---------FPadhPFQTLSwlDDGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLGYDVLINPDEEIGS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 144 EG-AKLLADKGYLDDVdGLII--AEPTGSgIYYAHKGSMSCKVTATGKAVHSS-VPFIGDNAIDTLLEFynqfkekysel 219
Cdd:PRK07338 168 PAsAPLLAELARGKHA-ALTYepALPDGT-LAGARKGSGNFTIVVTGRAAHAGrAFDEGRNAIVAAAEL----------- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 220 kkhdtkheldvAPMFKSLIGKEiseedanyaSGLTAVCSIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIIN 299
Cdd:PRK07338 235 -----------ALALHALNGQR---------DGVTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIA 294
|
250 260 270
....*....|....*....|....*....|....*...
gi 582169601 300 DVDSNK-LSLDIPSN-HRPVT--SDKNSKLITTIKDVA 333
Cdd:PRK07338 295 QVNQRHgVSLHLHGGfGRPPKpiDAAQQRLFEAVQACG 332
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
11-230 |
2.08e-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: 65.44 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 11 QLLADIVELQTENNNEID------VCNYLKDL--FDKY--DIKSEILKVNEHRANIVAEI---GNGSPILALSGHMDVV- 76
Cdd:cd05654 5 QLLKSLVSWPSVTGTEGErsfadfLKEILKELpyFKENpsHVWQLLPPDDLGRRNVTALVkgkKPSKRTIILISHFDTVg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 77 --DAGNQDNWTYPPFQLTE-----------------KAGK-LYGRGTTDMKGGLMALVITLIELKEQNQLPqGTIRLLAT 136
Cdd:cd05654 85 ieDYGELKDIAFDPDELTKafseyveeldeevredlLSGEwLFGRGTMDMKSGLAVHLALLEQASEDEDFD-GNLLLMAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 137 AGEEKEQEGA--------KLLADKGYldDVDGLIIAEPT-----GSGIYYAHKGSMScKVTAT----GKAVHSSVPFIGD 199
Cdd:cd05654 164 PDEEVNSRGMraavpallELKKKHDL--EYKLAINSEPIfpqydGDQTRYIYTGSIG-KILPGflcyGKETHVGEPFAGI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 582169601 200 NA------IDTLLEFYNQFKEKY--------SELKKHDTKHELDV 230
Cdd:cd05654 241 NAnlmaseITARLELNADLCEKVegeitpppVCLKQKDLKESYSV 285
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
56-203 |
5.61e-11 |
|
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: 63.45 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 56 IVAEIGNGS--PILALSGHMD----VVDAgnqdnwtypPFQLTEKAGKlygrgttdmkGGLMALVITLI-ELKEQNQLPQ 128
Cdd:cd08018 50 VVAEIGSGKpgPVVALRADMDalwqEVDG---------EFKANHSCGH----------DAHMTMVLGAAeLLKKIGLVKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 129 GTIRLLATAGEEKEQeGAKLLADKGYLDDVDGLI------IAE-PTG---SGIYyaHKGSMSCKVTATGKAVHSSVPFIG 198
Cdd:cd08018 111 GKLKFLFQPAEEKGT-GALKMIEDGVLDDVDYLFgvhlrpIQElPFGtaaPAIY--HGASTFLEGTIKGKQAHGARPHLG 187
|
....*
gi 582169601 199 DNAID 203
Cdd:cd08018 188 INAIE 192
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
55-387 |
6.39e-11 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 63.50 E-value: 6.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 55 NIVAEI-GNGSPILALSGHMDVVdagnqdnwtYP-------PFQltEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQL 126
Cdd:PRK06133 89 MVVATFkGTGKRRIMLIAHMDTV---------YLpgmlakqPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 127 PQGTIRLLATAGEEKEQEGAK-LLADKGylDDVDGLIIAEPTGS--GIYYAHKGSMSCKVTATGKAVHS-SVPFIGDNAi 202
Cdd:PRK06133 158 DYGTLTVLFNPDEETGSPGSReLIAELA--AQHDVVFSCEPGRAkdALTLATSGIATALLEVKGKASHAgAAPELGRNA- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 203 dtLLEFYNQFKekysELKKhdtkheldvapmfkslIGKEiseedanyASGLTAVCSIINGGKQFNSVPDEASLEFNVRPV 282
Cdd:PRK06133 235 --LYELAHQLL----QLRD----------------LGDP--------AKGTTLNWTVAKAGTNRNVIPASASAQADVRYL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 283 PEYDNDFIESFFQNIIND--VDSNKLSLDIPSNhRP--VTSDKNSKLITTIKDVassYVEQD---EIFVSALVGATDASS 355
Cdd:PRK06133 285 DPAEFDRLEADLQEKVKNklVPDTEVTLRFERG-RPplEANAASRALAEHAQGI---YGELGrrlEPIDMGTGGGTDAAF 360
|
330 340 350
....*....|....*....|....*....|....
gi 582169601 356 FLGDNKDNV--DLAIFGPGnplmAHQIDEYIEKD 387
Cdd:PRK06133 361 AAGSGKAAVleGFGLVGFG----AHSNDEYIELN 390
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
10-280 |
3.05e-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: 61.10 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 10 IQLLADIVELQTENNNEIDVCNYLKDLFDKYDIksEILKVNEHRANIVAEIGNG--SPILALSGHMDVVDAGNQDNWTYP 87
Cdd:cd08660 2 INIRRDIHEHPELGFEEVETSKKIRRWLEEEQI--EILDVPQLKTGVIAEIKGGedGPVIAIRADIDALPIQEQTNLPFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 88 pfqlTEKAGKLYGRGttdMKGGLMALVITLIELKEQNQLPQGTIRLLATAGEEKeQEGAKLLADKGYLDDVDGLIIAEPT 167
Cdd:cd08660 80 ----SKVDGT*HACG---HDFHTTSIIGTA*LLNQRRAELKGTVVFIFQPAEEG-AAGARKVLEAGVLNGVSAIFGIHNK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 168 GS---GIYYAHKGSMSCKVTA-----TGKAVHSSVPFIGDNAIDTLLEfynqfkekyselkkhdtkheldVAPMFKSLIG 239
Cdd:cd08660 152 PDlpvGTIGVKEGPL*ASVDVfeiviKGKGGHASIPNNSIDPIAAAGQ----------------------IISGLQSVVS 209
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 582169601 240 KEISEEDANYASGltavcSIINGGKQFNSVPDEASLEFNVR 280
Cdd:cd08660 210 RNISSLQNAVVSI-----TRVQGGTAWNVIPDQAE*EGTVR 245
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
1-230 |
1.86e-09 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 59.48 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 1 MTTFSEKEKI-QLLADIVELQTENN--NEIDVCNYLKDLFDK-------------YDIKSEILKvnehRANIVAEI---G 61
Cdd:COG4187 1 MKKWQTKEQLeELLCELVSIPSVTGteGEKEVAEFIYEKLSElpyfqenpehlglHPLPDDPLG----RKNVTALVkgkG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 62 NGSPILALSGHMDVVDA---GNQDNWTYPPFQLTEKAGK----------------LYGRGTTDMKGGLmALVITLIELKE 122
Cdd:COG4187 77 ESKKTVILISHFDVVDVedyGSLKPLAFDPEELTEALKEiklpedvrkdlesgewLFGRGTMDMKAGL-ALHLALLEEAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 123 QNQLPQGTIRLLATAGEEKEQEG--------AKLLADKGYldDVDGLIIAEPT-----GSGIYYAHKGS----MSCkVTA 185
Cdd:COG4187 156 ENEEFPGNLLLLAVPDEEVNSAGmraavpllAELKEKYGL--EYKLAINSEPSfpkypGDETRYIYTGSigklMPG-FYC 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 582169601 186 TGKAVHSSVPFIGDNA------IDTLLEFYNQFKEKYSE--------LKKHDTKHELDV 230
Cdd:COG4187 233 YGKETHVGEPFSGLNAnllaseLTRELELNPDFCEEVGGevtpppvsLKQKDLKEEYSV 291
|
|
| M20_Acy1L2 |
cd03887 |
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
115-280 |
5.11e-09 |
|
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: 57.59 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 115 ITLIELKEQNQLPqGTIRLLATAGEekEQEGAK-LLADKGYLDDVDGLIIAEPTGSGIYYAHkgSMSC---KVTATGKAV 190
Cdd:cd03887 96 LALKAALKALGLP-GTVVVLGTPAE--EGGGGKiDLIKAGAFDDVDIALMVHPGPKDVAGPK--SLAVsklRVEFHGKAA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 191 H-SSVPFIGDNAIDTLLEFYN------QFkekyseLKKHDTKHeldvapmfksligkeiseedanyasgltavcSII-NG 262
Cdd:cd03887 171 HaAAAPWEGINALDAAVLAYNnisalrQQ------LKPTVRVH-------------------------------GIItEG 213
|
170
....*....|....*...
gi 582169601 263 GKQFNSVPDEASLEFNVR 280
Cdd:cd03887 214 GKAPNIIPDYAEAEFYVR 231
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
110-280 |
1.70e-08 |
|
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: 55.89 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 110 LMALVITLIELKEQnqlPQGTIRLLATAGEEKEQeGAKLLADKGYLD--DVD---GLIIAEPTGSGIYYAHKGSMSC--- 181
Cdd:COG1473 109 LLGAAKALAELRDE---LKGTVRLIFQPAEEGGG-GAKAMIEDGLLDrpDVDaifGLHVWPGLPVGTIGVRPGPIMAaad 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 182 --KVTATGKAVHSSVPFIGDNAIDTLLEFYNQfkekyselkkhdtkheldvapmFKSLIGKEISEEDAnyasgltAVCSI 259
Cdd:COG1473 185 sfEITIKGKGGHAAAPHLGIDPIVAAAQIVTA----------------------LQTIVSRNVDPLDP-------AVVTV 235
|
170 180
....*....|....*....|...
gi 582169601 260 --INGGKQFNSVPDEASLEFNVR 280
Cdd:COG1473 236 giIHGGTAPNVIPDEAELEGTVR 258
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
63-394 |
2.09e-08 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 55.59 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 63 GSPILALSGHMDVVDAgnQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLielkeqnQLPQGTIRLLATAGEEKE 142
Cdd:PRK08737 62 GTPKYLFNVHLDTVPD--SPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAA-------NAGDGDAAFLFSSDEEAN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 143 QEgaklLADKGYLD---DVDGLIIAEPTGSGIYYAHKGSMSCKVTATGKAVHSSVPF-IGDNAIDTLLEFYNQFKEkYSE 218
Cdd:PRK08737 133 DP----RCVAAFLArgiPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKQdPSASALHQAMRWGGQALD-HVE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 219 lkkhdtkheldvapmfksligkeiSEEDANYAsGLTAVC---SIINGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQ 295
Cdd:PRK08737 208 ------------------------SLAHARFG-GLTGLRfniGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 296 NIindvDSNKLSLDIPSNHRPVTSDKNSKLITTIKDVASSYVEQDEIFVSALVGA-TDASSFlgdNKDNVDLAIFGPGNP 374
Cdd:PRK08737 263 GF----AEPAAATFEETFRGPSLPSGDIARAEERRLAARDVADALDLPIGNAVDFwTEASLF---SAAGYTALVYGPGDI 335
|
330 340
....*....|....*....|
gi 582169601 375 LMAHQIDEYIEKDMYLKYID 394
Cdd:PRK08737 336 AQAHTADEFVTLDQLQRYAE 355
|
|
| M20_Acy1L2_AbgB |
cd05673 |
M20 Peptidase Aminoacylase 1-like protein 2 aminobenzoyl-glutamate utilization protein B ... |
43-280 |
1.24e-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: 53.46 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 43 KSEILKVNEHRANI----VAEIGNGSPILALSGHMDVVDAGNQDNWTYPPFQLTE-KAGKLYGR---GTtdmkGGLMAlV 114
Cdd:cd05673 37 EEEGFTVERGVAGIptafVASYGSGGPVIAILGEYDALPGLSQEAGVAERKPVEPgANGHGCGHnllGT----GSLGA-A 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 115 ITLIELKEQNQLPqGTIRLLATAGEekEQEGAK-LLADKGYLDDVDGLIIAEPTG-SGIYYAHKGS-MSCKVTATGKAVH 191
Cdd:cd05673 112 IAVKDYMEENNLA-GTVRFYGCPAE--EGGSGKtFMVRDGVFDDVDAAISWHPASfNGVWSTSSLAnISVKFKFKGISAH 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 192 -SSVPFIGDNAIDTlLEFYNqFKEKYseLKKHdtkheldvapMfksligkeISEEDANYAsgltavcsIIN-GGKQFNSV 269
Cdd:cd05673 189 aAAAPHLGRSALDA-VELMN-VGVNY--LREH----------M--------IPEARVHYA--------ITNgGGAAPNVV 238
|
250
....*....|.
gi 582169601 270 PDEASLEFNVR 280
Cdd:cd05673 239 PAFAEVWYYIR 249
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
63-406 |
1.80e-07 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 53.08 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 63 GSPILALSGHMDVVDAGNQDNWTYPPFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEQNQLPQGTIRLLaTAGEEK- 141
Cdd:cd05680 62 GAPTVLVYGHYDVQPPDPLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFL-IEGEEEi 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 142 ---------EQEGAKLLADKGYLddVDGLIIAEPTGSgIYYAHKGSMSCKVTATG--KAVHSSVpFIG--DNAIDTLLE- 207
Cdd:cd05680 141 gspslpaflEENAERLAADVVLV--SDTSMWSPDTPT-ITYGLRGLAYLEISVTGpnRDLHSGS-YGGavPNPANALARl 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 208 ---------------FYNQF-------KEKYSELKKHDTKheldvapmFKSLIGKEISEEDANYAS----GLTAVCSI-- 259
Cdd:cd05680 217 laslhdedgrvaipgFYDDVrpltdaeREAWAALPFDEAA--------FKASLGVPALGGEAGYTTlerlWARPTLDVng 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 260 INGGKQFNS----VPDEASLEFNVRPVPEYDNDFIESFFQNIINDV--DSNKLSLDIPSNHRPVTSDKNSKLITTIKDVA 333
Cdd:cd05680 289 IWGGYQGEGsktvIPSKAHAKISMRLVPGQDPDAIADLLEAHLRAHapPGVTLSVKPLHGGRPYLVPTDHPALQAAERAL 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 582169601 334 SSYVEQDEIFV---SALVGATDASSFLGdnkdnVDLAIFGPGNPLMA-HQIDEYIEKDMYLKYIdifkEASIQYLKE 406
Cdd:cd05680 369 EEAFGKPPVFVregGSIPIVALFEKVLG-----IPTVLMGFGLPDDAiHAPNEKFRLECFHKGI----EAIAHLLAR 436
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
63-215 |
2.86e-07 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 52.44 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 63 GSPILALSGHMDV--VDAGNQdnWTYPPFQLTEKAGKLYGRGTTDMKGGLMaLVITLIE--LKEQNQLPQgTIRLLaTAG 138
Cdd:PRK08201 78 GKPTVLIYGHYDVqpVDPLNL--WETPPFEPTIRDGKLYARGASDDKGQVF-MHLKAVEalLKVEGTLPV-NVKFC-IEG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 139 EEK----------EQEGAKLLADKGYLDDVdGLIiaEPTGSGIYYAHKGSMSCKVTATGKA--VHS-----SVPfigdNA 201
Cdd:PRK08201 153 EEEigspnldsfvEEEKDKLAADVVLISDT-TLL--GPGKPAICYGLRGLAALEIDVRGAKgdLHSglyggAVP----NA 225
|
170
....*....|....
gi 582169601 202 IDTLLEFYNQFKEK 215
Cdd:PRK08201 226 LHALVQLLASLHDE 239
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
55-211 |
3.76e-07 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 51.89 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 55 NIVAEI---GNGSPILALSGHMDVVDAgNQDNWTYP-----PFQLTEKAGKLYGRGTTDMKGGLMALVITLIELKEqNQL 126
Cdd:PRK06156 97 NRVLEIglgGSGSDKVGILTHADVVPA-NPELWVLDgtrldPFKVTLVGDRLYGRGTEDDKGAIVTALYAMKAIKD-SGL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 127 P-QGTIRLLATAGEEKEQEGAK---------------------LLADKGY------------------------------ 154
Cdd:PRK06156 175 PlARRIELLVYTTEETDGDPLKyylerytppdynitldaeypvVTAEKGWgtimatfpkraadgkgaeivamtggafanq 254
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 582169601 155 --------LDDVDGLIIA---EPTGSGIYYAHKGSMS---------CKVTATGKAVHSSVPFIGDNAIDTLLEFYNQ 211
Cdd:PRK06156 255 ipqtavatLSGGDPAALAaalQAAAAAQVKRHGGGFSidfkrdgkdVTITVTGKSAHSSTPESGVNPVTRLALFLQS 331
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
24-298 |
1.22e-06 |
|
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. 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 in 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.
Pssm-ID: 349919 [Multi-domain] Cd Length: 371 Bit Score: 49.99 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 24 NNEIDVCNYLKDLFDKYDIKseILKVNeHRANIVAEIGNGSPILALSGHMDVVDAGNQDNWTYPpfqlTEKAGKLYGRG- 102
Cdd:cd05669 21 NQEFETTKKIRRWLEEKGIR--ILDLP-LKTGVVAEIGGGGPIIALRADIDALPIEEETGLPYA----SQNKGVMHACGh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 103 ---TTDMKGglmalviTLIELKE-QNQLPqGTIRLLATAGEEKEQeGAKLLADKGYLDDVDGLI------------IAep 166
Cdd:cd05669 94 dfhTASLLG-------AAVLLKErEAELK-GTVRLIFQPAEETGA-GAKKVIEAGALDDVSAIFgfhnkpdlpvgtIG-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 167 TGSGIYYAhkGSMSCKVTATGKAVHSSVPfigDNAIDTLLefynqfkekyselkkhdTKHELDVApmFKSLIGKEISEED 246
Cdd:cd05669 163 LKSGALMA--AVDRFEIEIAGKGAHAAKP---ENGVDPIV-----------------AASQIINA--LQTIVSRNISPLE 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 582169601 247 AnyasgltAVCSI--INGGKQFNSVPDEASLEFNVRpvpEYDNDF---IESFFQNII 298
Cdd:cd05669 219 S-------AVVSVtrIHAGNTWNVIPDSAELEGTVR---TFDAEVrqlVKERFEQIV 265
|
|
| M20_IAA_Hyd |
cd08017 |
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ... |
56-280 |
1.26e-06 |
|
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: 50.01 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 56 IVAEIGNGS-PILALSGHMDVVDAGNQDNWTYPpfqlTEKAGKLYGRG----TTdmkgglMALVITLIeLKEQNQLPQGT 130
Cdd:cd08017 45 IVATIGSGSpPVVALRADMDALPIQELVEWEHK----SKVDGKMHACGhdahVA------MLLGAAKL-LKARKHLLKGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 131 IRLLATAGEEKeQEGAKLLADKGYLDDVDGLI-----IAEPTG-----SGIYYAhkGSMSCKVTATGKAVHSSVPFigdN 200
Cdd:cd08017 114 VRLLFQPAEEG-GAGAKEMIKEGALDDVEAIFgmhvsPALPTGtiasrPGPFLA--GAGRFEVVIRGKGGHAAMPH---H 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 201 AIDTLLefynqfkekyselkkhdtkheldVAPM----FKSLIGKEISEEDAnyasgltAVCSI--INGGKQFNSVPDEAS 274
Cdd:cd08017 188 TVDPVV-----------------------AASSavlaLQQLVSRETDPLDS-------QVVSVtrFNGGHAFNVIPDSVT 237
|
....*.
gi 582169601 275 LEFNVR 280
Cdd:cd08017 238 FGGTLR 243
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
113-357 |
1.44e-06 |
|
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: 49.96 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 113 LVITLIELKEQNQLPQGTIRLLATAGEEKEQEGAKLLADKGYLDDVDgLIIA------EPTGSgIYYAHKGSMSC----K 182
Cdd:cd08021 108 LLGAAKVLAENKDEIKGTVRFIFQPAEEVPPGGAKPMIEAGVLEGVD-AVFGlhlwstLPTGT-IAVRPGAIMAApdefD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 183 VTATGKAVHSSVPFIGDNAIDTLLEFYNQfkekyselkkhdtkheldvapmFKSLIGKEISEEDanyasglTAVCSI--I 260
Cdd:cd08021 186 ITIKGKGGHGSMPHETVDPIVIAAQIVTA----------------------LQTIVSRRVDPLD-------PAVVTIgtF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 261 NGGKQFNSVPDEASLEFNVRPVPEYDNDFIESFFQNIINDV-----DSNKLSLDIPsnhRPVTsDKNSKLITTIKDVASS 335
Cdd:cd08021 237 QGGTSFNVIPDTVELKGTVRTFDEEVREQVPKRIERIVKGIceaygASYELEYQPG---YPVV-YNDPEVTELVKKAAKE 312
|
250 260
....*....|....*....|...
gi 582169601 336 YVEQDEIFVSALV-GATDASSFL 357
Cdd:cd08021 313 VLIGVENVEPQLMmGGEDFSYYL 335
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
109-280 |
1.67e-06 |
|
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: 49.64 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 109 GLMALVITLIE-LKEQNQLPQGTIRLLATAGEEKeQEGAKLLADKGYLDDVD---GLIIAEPTGSGIYYAHKGSM--SC- 181
Cdd:cd08019 91 GHTAMLLGAAKiLNEIKDTIKGTVKLIFQPAEEV-GEGAKQMIEEGVLEDVDavfGIHLWSDVPAGKISVEAGPRmaSAd 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 182 --KVTATGKAVHSSVPFIGDNAIDTLLEFYNQfkekyselkkhdtkheldvapmFKSLIGKEISEEDanyasglTAVCSI 259
Cdd:cd08019 170 ifKIEVKGKGGHGSMPHQGIDAVLAAASIVMN----------------------LQSIVSREIDPLE-------PVVVTV 220
|
170 180
....*....|....*....|...
gi 582169601 260 --INGGKQFNSVPDEASLEFNVR 280
Cdd:cd08019 221 gkLNSGTRFNVIADEAKIEGTLR 243
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
71-113 |
1.14e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 47.22 E-value: 1.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 582169601 71 GHMDVVDaGNQDNWTYP--PFQLTEKAGKLYGRGTTDMKG----GLMAL 113
Cdd:PRK07079 92 GHGDVVR-GYDEQWREGlsPWTLTEEGDRWYGRGTADNKGqhtiNLAAL 139
|
|
| PLN02693 |
PLN02693 |
IAA-amino acid hydrolase |
56-356 |
6.81e-04 |
|
IAA-amino acid hydrolase
Pssm-ID: 178296 [Multi-domain] Cd Length: 437 Bit Score: 41.58 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 56 IVAEIGNGSP-ILALSGHMDVVDAGNQDNWTYPpfqlTEKAGKLYGRGttdMKGGLMALVITLIELKEQNQLPQGTIRLL 134
Cdd:PLN02693 93 IIGYIGTGEPpFVALRADMDALPIQEAVEWEHK----SKIPGKMHACG---HDGHVAMLLGAAKILQEHRHHLQGTVVLI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 135 ATAGEEKeQEGAKLLADKGYLDDVD---GLIIAEPTGSGIYYAHKGSMSC-----KVTATGKAVHSSVPfigDNAIDTLL 206
Cdd:PLN02693 166 FQPAEEG-LSGAKKMREEGALKNVEaifGIHLSPRTPFGKAASRAGSFMAgagvfEAVITGKGGHAAIP---QHTIDPVV 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582169601 207 EFYNqfkekyselkkhdtkheldVAPMFKSLIGKEISEEDANYASgltavCSIINGGKQFNSVPDEASLEFNVRPVPEYD 286
Cdd:PLN02693 242 AASS-------------------IVLSLQQLVSRETDPLDSKVVT-----VSKVNGGNAFNVIPDSITIGGTLRAFTGFT 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 582169601 287 NdfIESFFQNIIND---VDSNKLSLDI-PSNHRPVTSDKNSK-LITTIKDVASSYVEQdEIFVSAL--VGATDASSF 356
Cdd:PLN02693 298 Q--LQQRIKEIITKqaaVHRCNASVNLtPNGREPMPPTVNNMdLYKQFKKVVRDLLGQ-EAFVEAApeMGSEDFSYF 371
|
|
| |
