|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
6-403 |
0e+00 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 538.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 6 EEDKIKILADIVEINTENDNELEVCNYFKALLNKYDIDSKIIKVDNRRANLVAEIGEGKPKIAISGHMDVVDAGDYNEWK 85
Cdd:PRK08588 1 EEEKIQILADIVKINSVNDNEIEVANYLQDLFAKHGIESKIVKVNDGRANLVAEIGSGSPVLALSGHMDVVAAGDVDKWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 86 YDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEKEMSGAQLFKEQGYVNDLDGMIIAE 165
Cdd:PRK08588 81 YDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGELGAKQLTEKGYADDLDALIIGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 166 PSDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEKYVEIKKNEkehsldvhpyidecireqghyn 245
Cdd:PRK08588 161 PSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYFDSIKKHN---------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 246 dgdlkeDVAAGLVIVNSIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIDSE---RLSVEVTVNHPTVY 322
Cdd:PRK08588 219 ------PYLGGLTHVVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNQNgaaQLSLDIYSNHRPVA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 323 THKDNRLINTFLE-----YNHDFKVSGMVGATDAAELLgDKDEDFDLAIIGPGHITLAHQTDEYVYKSRYLDYIDMYQQV 397
Cdd:PRK08588 293 SDKDSKLVQLAKDvaksyVGQDIPLSAIPGATDASSFL-KKKPDFPVIIFGPGNNLTAHQVDEYVEKDMYLKFIDIYKEI 371
|
....*.
gi 815845711 398 ILNYLN 403
Cdd:PRK08588 372 IIQYLK 377
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
11-398 |
9.05e-123 |
|
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: 359.69 E-value: 9.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 11 KILADIVEINTENDNELEVCNYFKALLNKYD--IDSKIIKvdnRRANLVAEIGEG-KPKIAISGHMDVVDAGDYNEWKYD 87
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGygIESTIVE---GRGNLVATVGGGdGPVLLLNGHIDTVPPGDGDKWSFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 88 PFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEKEMSGAQLFKEQGYVNDLDGMIIAEPS 167
Cdd:cd08659 78 PFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLEAGYADRLDALIVGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 168 DGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEKYVEikknekehsLDVHPYIDecireqghyndg 247
Cdd:cd08659 158 GLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEE---------LPAHPLLG------------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 248 dlkedvaaGLVIVNSIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEiDSERLSVEVTVNH-PTVYTHKD 326
Cdd:cd08659 217 --------PPTLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEE-HEAKLTVEVSLDGdPPFFTDPD 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815845711 327 NRLINTFL----EYNHDFKVSGMVGATDAAELLgdKDEDFDLAIIGPGHITLAHQTDEYVYKSRYLDYIDMYQQVI 398
Cdd:cd08659 288 HPLVQALQaaarALGGDPVVRPFTGTTDASYFA--KDLGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
6-402 |
1.13e-90 |
|
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: 278.69 E-value: 1.13e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 6 EEDKIKILADIVEINTENDNELEVCNYFKALLNKYDIDSKIIKVDNRRANLVAEI--GEGKPKIAISGHMDVVDAGDYNE 83
Cdd:COG0624 11 LDEALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPPGRPNLVARRpgDGGGPTLLLYGHLDVVPPGDLEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 84 WKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEKEMSGAQ-LFKEQGYVNDLDGMI 162
Cdd:COG0624 91 WTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSPGARaLVEELAEGLKADAAI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 163 IAEPSDGFA-FYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKekyveikknEKEHSLDVHPYIDEcireq 241
Cdd:COG0624 171 VGEPTGVPTiVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALR---------DLEFDGRADPLFGR----- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 242 ghyndgdlkedvaAGLVIvnSIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIDsERLSVEVTVNH--- 318
Cdd:COG0624 237 -------------TTLNV--TGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAA-PGVEVEVEVLGdgr 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 319 PTVYTHKDNRLINTFLE-----YNHDFKVSGMVGATDA---AELLGdkdedFDLAIIGPGHITLAHQTDEYVYKSRYLDY 390
Cdd:COG0624 301 PPFETPPDSPLVAAARAairevTGKEPVLSGVGGGTDArffAEALG-----IPTVVFGPGDGAGAHAPDEYVELDDLEKG 375
|
410
....*....|..
gi 815845711 391 IDMYQQVILNYL 402
Cdd:COG0624 376 ARVLARLLERLA 387
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
10-392 |
4.98e-84 |
|
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: 261.18 E-value: 4.98e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 10 IKILADIVEINTEN---DNELEVCNYFKALLNKYDIDSKIIKVDNRRAN-----LVAEIGEGK-PKIAISGHMDVVDAGD 80
Cdd:TIGR01910 1 VELLKDLISIPSVNppgGNEETIANYIKDLLREFGFSTDVIEITDDRLKvlgkvVVKEPGNGNeKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 81 YNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEKEMSGAQLFKEQGYVNDLDG 160
Cdd:TIGR01910 81 LELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLLQRGYFKDADG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 161 MIIAEPSDG-FAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIkEKYVEIKKNEKEHSLDVHPyidecir 239
Cdd:TIGR01910 161 VLIPEPSGGdNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITEL-NELEEHIYARNSYGFIPGP------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 240 eqghyndgdlkedvaaglVIVN-SIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIDSE-----RLSVE 313
Cdd:TIGR01910 233 ------------------ITFNpGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSdgwlyENEPV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 314 VTVNHPTvYTHKDNRLINTFLE-----YNHDFKVSGMVGATDAAELlgdKDEDFDLAIIGPGHITLAHQTDEYVYKSRYL 388
Cdd:TIGR01910 295 VKWSGPN-ETPPDSRLVKALEAiikkvRGIEPEVLVSTGGTDARFL---RKAGIPSIVYGPGDLETAHQVNEYISIKNLV 370
|
....
gi 815845711 389 DYID 392
Cdd:TIGR01910 371 ESTK 374
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
12-382 |
1.15e-62 |
|
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: 205.90 E-value: 1.15e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 12 ILADIVEINTENDN-ELEVCNYFKALLNKYDIDSKIIKV-DNRRANLVAEIG-EGKPKIAISGHMDVVDAgDYNEWKYDP 88
Cdd:cd03894 2 LLARLVAFDTVSRNsNLALIEYVADYLAALGVKSRRVPVpEGGKANLLATLGpGGEGGLLLSGHTDVVPV-DGQKWSSDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 89 FKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRlqKGTIRLMATAAEEKEMSGAQLFKE--QGYVNDLDGMIIAEP 166
Cdd:cd03894 81 FTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKL--RKPLHLAFSYDEEVGCLGVRHLIAalAARGGRPDAAIVGEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 167 SDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEKYVEIKKNEKEHSLDVhPYidecireqghynd 246
Cdd:cd03894 159 TSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPFDP-PY------------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 247 gdlkedvaagLVIVNSIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVK---EIDSERLSVEVTVNHPTVYT 323
Cdd:cd03894 225 ----------PTLNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEallEFPEAGIEVEPLFEVPGLET 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815845711 324 HKDNRLINTFLEYNHDFKVSGMVGATDAAEL--LGdkdedFDLAIIGPGHITLAHQTDEYV 382
Cdd:cd03894 295 DEDAPLVRLAAALAGDNKVRTVAYGTEAGLFqrAG-----IPTVVCGPGSIAQAHTPDEFV 350
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
6-399 |
6.46e-62 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 204.45 E-value: 6.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 6 EEDKIKILADIVEINTEN---DNELEVCNYFKALLNKYDIDSKIIKVDN--------RRANLVAEIGEGKPKIAISGHMD 74
Cdd:PRK08651 5 MFDIVEFLKDLIKIPTVNppgENYEEIAEFLRDTLEELGFSTEIIEVPNeyvkkhdgPRPNLIARRGSGNPHLHFNGHYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 75 VVDAGDyNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRlqkGTIRLMATAAEEKEMSGAQLFKEQGY 154
Cdd:PRK08651 85 VVPPGE-GWSVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAGD---GNIELAIVPDEETGGTGTGYLVEEGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 155 VNdLDGMIIAEPSD-GFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEKYVEIKKNEKehsldvhpY 233
Cdd:PRK08651 161 VT-PDYVIVGEPSGlDNICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYE--------Y 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 234 IDEcireqghyndGDLKEDVAAGlvivNSIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIDSE---RL 310
Cdd:PRK08651 232 DDE----------RGAKPTVTLG----GPTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPElgiEV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 311 SVEVTVNHPTVYTHKDNRLINTFLE-----YNHDFKVSGMVGATDAAELlgdKDEDFDLAIIGPGHITLAHQTDEYVYKS 385
Cdd:PRK08651 298 EFEITPFSEAFVTDPDSELVKALREairevLGVEPKKTISLGGTDARFF---GAKGIPTVVYGPGELELAHAPDEYVEVK 374
|
410
....*....|....
gi 815845711 386 RYLDYIDMYQQVIL 399
Cdd:PRK08651 375 DVEKAAKVYEEVLK 388
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
68-400 |
3.83e-56 |
|
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: 187.17 E-value: 3.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 68 AISGHMDVVDAGDYNEWkydPFKLTEeDDKLYGRGTTDMKGGLAALIIAMIEIKESGrLQKGTIRLMATAAEEKEMSGAQ 147
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEG-LKKGTVKLLFQPDEEGGMGGAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 148 LFKEQGYVNDLD-----GMIIAEPS---DGFA---FYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKeky 216
Cdd:pfam01546 76 ALIEDGLLEREKvdavfGLHIGEPTlleGGIAigvVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQ--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 217 veikknekehsldvhpyiDECIREQGHYNDGDLKedvaaglVIVNSIIRGGeqFNTVPESAYAEFNIRTVPEYDNVAIEK 296
Cdd:pfam01546 153 ------------------DIVSRNVDPLDPAVVT-------VGNITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 297 LFKDTVKEI-DSERLSVEVTVNHPTV-YTHKDNRLINTFLE-------YNHDFKVSGMVGATDAAELLGDKDEDFDlaII 367
Cdd:pfam01546 206 RIREILEAIaAAYGVKVEVEYVEGGApPLVNDSPLVAALREaakelfgLKVELIVSGSMGGTDAAFFLLGVPPTVV--FF 283
|
330 340 350
....*....|....*....|....*....|...
gi 815845711 368 GPGhITLAHQTDEYVYKSRYLDYIDMYQQVILN 400
Cdd:pfam01546 284 GPG-SGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
10-398 |
9.61e-52 |
|
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: 176.81 E-value: 9.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 10 IKILADIVEINTEN---DNELEVCNYFKALLNKYDIDSKIIKVDNRRANLVAEI--GEGKPKIAISGHMDVVDAGDYNEW 84
Cdd:cd08011 1 VKLLQELVQIPSPNppgDNTSAIAAYIKLLLEDLGYPVELHEPPEEIYGVVSNIvgGRKGKRLLFNGHYDVVPAGDGEGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 85 KYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEK-EMSGAQLFKEQGYVNDLDgMII 163
Cdd:cd08011 81 TVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETgGRAGTKYLLEKVRIKPND-VLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 164 AEPSDGFAFY-ATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEkyvEIKKnekehsldvhpyidecireqg 242
Cdd:cd08011 160 GEPSGSDNIRiGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYE---LEKT--------------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 243 hYNDGdlkedvaaglvivnsIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIdsERLSVEVTVNHPTVY 322
Cdd:cd08011 216 -VNPG---------------VIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSI--EEVSFEIKSFYSPTV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 323 THKDNRLINTFLE-----YNHDFKVSGMVGATDAAELlgdKDEDFDLAIIGPGHITLAHQTDEYVYKSRYLDYIDMYQQV 397
Cdd:cd08011 278 SNPDSEIVKKTEEaitevLGIRPKEVISVGASDARFY---RNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVHALV 354
|
.
gi 815845711 398 I 398
Cdd:cd08011 355 A 355
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
50-382 |
9.62e-45 |
|
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: 158.83 E-value: 9.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 50 DNRRANLVAEIG-EGKPKIAISGHMDVVDAgDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESgRLQK 128
Cdd:TIGR01892 43 GAEKSNLVAVIGpSGAGGLALSGHTDVVPY-DDAAWTRDPFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAE-QLKK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 129 gTIRLMATAAEEKEMSGAQLFKEQGYVNDlDGMIIAEPSDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAF 208
Cdd:TIGR01892 121 -PLHLALTADEEVGCTGAPKMIEAGAGRP-RHAIIGEPTRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 209 IQRIKEKYVEIKKNEKEHSLDVhPYIDECIreqGHyndgdlkedvaaglvivnsiIRGGEQFNTVPESAYAEFNIRTVPE 288
Cdd:TIGR01892 199 LQRLVHLADTLLREDLDEGFTP-PYTTLNI---GV--------------------IQGGKAVNIIPGACEFVFEWRPIPG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 289 YDNVAIEKLFKDTVKEIDSERLSVEVTVN----HPTVYTHKDNRLInTFLEynhdfKVSGmvgatDAAELLGDKDE---- 360
Cdd:TIGR01892 255 MDPEELLQLLETIAQALVRDEPGFEVQIEvvstDPGVNTEPDAELV-AFLE-----ELSG-----NAPEVVSYGTEapqf 323
|
330 340
....*....|....*....|....*
gi 815845711 361 ---DFDLAIIGPGHITLAHQTDEYV 382
Cdd:TIGR01892 324 qelGAEAVVCGPGDIRQAHQPDEYV 348
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
6-405 |
4.06e-41 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 149.71 E-value: 4.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 6 EEDKIKILADIVEINTENDNELEVCNYFKALLNKYDIDSkiIKVDnRRANLVAEIGEGKPKIAISGHMDVVDAGDYNEWK 85
Cdd:PRK13004 14 KADMTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFDK--VEID-PMGNVLGYIGHGKKLIAFDAHIDTVGIGDIKNWD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 86 YDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEK-EMSGAQLFKEQGYVNDlDGMIIA 164
Cdd:PRK13004 91 FDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEEDcDGLCWRYIIEEDKIKP-DFVVIT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 165 EPSDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKekyvEIKKNEKEHSLdvhpyidecireqghy 244
Cdd:PRK13004 170 EPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELE----ELNPNLKEDPF---------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 245 ndgdlkedVAAGLVIVNSIIRGGEQFNTVPESAYAEFNIRT---------VPEYDNVAIEKLFKDTVKEIDSER-----L 310
Cdd:PRK13004 230 --------LGKGTLTVSDIFSTSPSRCAVPDSCAISIDRRLtvgetwesvLAEIRALPAVKKANAKVSMYNYDRpsytgL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 311 SVEVTVNHPTVYTHKDNRLINTFLE-YNHDFKVSGMVG----ATDAAELLGdkdeDFDLAII--GPGHITLAHQTDEYVY 383
Cdd:PRK13004 302 VYPTECYFPTWLYPEDHEFVKAAVEaYKGLFGKAPEVDkwtfSTNGVSIAG----RAGIPTIgfGPGKEPLAHAPNEYTW 377
|
410 420
....*....|....*....|..
gi 815845711 384 KSRYLDYIDMYQQVILNYLNQH 405
Cdd:PRK13004 378 KEQLVKAAAMYAAIPKSLLKKK 399
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
10-382 |
3.57e-39 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 144.18 E-value: 3.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 10 IKILADIVEINT--ENDNeLEVCNYFKALLNKYDIDSKIIK-VDNRRANLVAEIG-EGKPKIAISGHMDVVDAgDYNEWK 85
Cdd:PRK07522 7 LDILERLVAFDTvsRDSN-LALIEWVRDYLAAHGVESELIPdPEGDKANLFATIGpADRGGIVLSGHTDVVPV-DGQAWT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 86 YDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESgRLQKGtIRLMATAAEEKEMSGAQLFKEqgyvnDL------- 158
Cdd:PRK07522 85 SDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAA-PLRRP-LHLAFSYDEEVGCLGVPSMIA-----RLpergvkp 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 159 DGMIIAEPSDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAIN---SLIAFIQRIKEKyveikknekehsldvhpyid 235
Cdd:PRK07522 158 AGCIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEyaaRLIAHLRDLADR-------------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 236 ecIREQGHYNDGdlkEDVAAGLVIVNsIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKE--------IDS 307
Cdd:PRK07522 218 --LAAPGPFDAL---FDPPYSTLQTG-TIQGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAellpemraVHP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 308 E-RLSVEVTVNHPTVYTHKDNRLintfleynhdfkvsgmvgATDAAELLGDKD--------ED--FDLA-----IIGPGH 371
Cdd:PRK07522 292 EaAIEFEPLSAYPGLDTAEDAAA------------------ARLVRALTGDNDlrkvaygtEAglFQRAgiptvVCGPGS 353
|
410
....*....|.
gi 815845711 372 ITLAHQTDEYV 382
Cdd:PRK07522 354 IEQAHKPDEFV 364
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
10-214 |
1.96e-38 |
|
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: 142.17 E-value: 1.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 10 IKILADIVEINTENDNELEVCNYFKALLNKYDIDSkiIKVDnRRANLVAEIGEGKPKIAISGHMDVVDAGDYNEWKYDPF 89
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGFDE--VEID-PMGNVIGYIGGGKKKILFDGHIDTVGIGNIDNWKFDPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 90 KLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESG-RLQKGTIRLMATAAEE--KEMSGAQLFKEQGYVNDLdgMIIAEP 166
Cdd:cd05649 78 EGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGlRDFAYTILVAGTVQEEdcDGVCWQYISKADKIKPDF--VVSGEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 815845711 167 SDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKE 214
Cdd:cd05649 156 TDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQ 203
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
11-383 |
3.80e-37 |
|
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: 139.80 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 11 KILADIVEINTEND-----NELEVCNYFKALLNKYDIDSKIIKVDNR--RANLVAEIGEGKPK---IAISGHMDVVDAgD 80
Cdd:cd05675 2 DLLQELIRIDTTNSgdgtgSETRAAEVLAARLAEAGIQTEIFVVESHpgRANLVARIGGTDPSagpLLLLGHIDVVPA-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 81 YNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEKE-MSGA--------QLFKE 151
Cdd:cd05675 81 ASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGgENGAkwlvdnhpELFDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 152 QGY-VNDLDGMIIAEPsDGFAFY----ATKGSMGLKVTSKGIPAHSSLPSlGHNAINSLIAFIQRIKEKYVEIKKNE--- 223
Cdd:cd05675 161 ATFaLNEGGGGSLPVG-KGRRLYpiqvAEKGIAWMKLTVRGRAGHGSRPT-DDNAITRLAEALRRLGAHNFPVRLTDeta 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 224 -----------------KEHSLDVHPYIDECIREQGHYNdgdlkedVAAGLVIVNSIIRGGEQFNTVPESAYAEFNIRTV 286
Cdd:cd05675 239 yfaqmaelaggeggalmLTAVPVLDPALAKLGPSAPLLN-------AMLRNTASPTMLDAGYATNVLPGRATAEVDCRIL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 287 PEYDnvaiEKLFKDTV-KEIDSERLSVEVTVNHPTVYTHKDNRLINTFLEYNHDFKVSGMV------GATDAAEL--LGD 357
Cdd:cd05675 312 PGQS----EEEVLDTLdKLLGDPDVSVEAVHLEPATESPLDSPLVDAMEAAVQAVDPGAPVvpymspGGTDAKYFrrLGI 387
|
410 420
....*....|....*....|....*...
gi 815845711 358 KDEDFDLAIIGPGHI--TLAHQTDEYVY 383
Cdd:cd05675 388 PGYGFAPLFLPPELDytGLFHGVDERVP 415
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
31-392 |
5.39e-36 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 135.72 E-value: 5.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 31 NYFKALlnkyDIDSKIIKVDNRR--ANLVAEIGEGKPKIAISGHMDVVDAgDYNEWKYDPFKLTEEDDKLYGRGTTDMKG 108
Cdd:PRK05111 40 GWFEDL----GFNVEIQPVPGTRgkFNLLASLGSGEGGLLLAGHTDTVPF-DEGRWTRDPFTLTEHDGKLYGLGTADMKG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 109 GLAALIIAMIEIKESgRLQKgTIRLMATAAEEKEMSGAQLFKEQGYVNdLDGMIIAEPSDGFAFYATKGSM--GLKVTsk 186
Cdd:PRK05111 115 FFAFILEALRDIDLT-KLKK-PLYILATADEETSMAGARAFAEATAIR-PDCAIIGEPTSLKPVRAHKGHMseAIRIT-- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 187 GIPAHSSLPSLGHNAI-------NSLIAFIQRIKEKYveikkneKEHSLDV-HPYIDecireQGHyndgdlkedvaaglv 258
Cdd:PRK05111 190 GQSGHSSDPALGVNAIelmhdviGELLQLRDELQERY-------HNPAFTVpYPTLN-----LGH--------------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 259 ivnsiIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIdSERLSVEVTVN--HPTV--Ythkdnrlintfl 334
Cdd:PRK05111 243 -----IHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPV-SERWPGRITVAplHPPIpgY------------ 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815845711 335 EYNHDfkvSGMVGAtdAAELLGDKDEDFDLA--------------IIGPGHITLAHQTDEYVyksrYLDYID 392
Cdd:PRK05111 305 ECPAD---HQLVRV--VEKLLGHKAEVVNYCteapfiqqlgcptlVLGPGSIEQAHQPDEYL----ELSFIK 367
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
55-305 |
1.51e-33 |
|
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: 128.39 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 55 NLVAEIGEGKPKIAISGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLM 134
Cdd:cd03891 45 NLWARRGTGGPHLCFAGHTDVVPPGDLEGWSSDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 135 ATAAEE-------KEMsgAQLFKEQGYVndLDGMIIAEPSdgfafyATK-----------GSMGLKVTSKGIPAHSSLPS 196
Cdd:cd03891 125 ITSDEEgpaidgtKKV--LEWLKARGEK--IDYCIVGEPT------SEKklgdtikigrrGSLNGKLTIKGKQGHVAYPH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 197 LGHNAINSLIAFIQRIkekyveikkneKEHSLDvhpyidecireqghynDGDlkEDVAA-GLVIVNsiIRGG-EQFNTVP 274
Cdd:cd03891 195 LADNPIHLLAPILAEL-----------TATVLD----------------EGN--EFFPPsSLQITN--IDVGnGATNVIP 243
|
250 260 270
....*....|....*....|....*....|.
gi 815845711 275 ESAYAEFNIRTVPEYDNVAIEKLFKDTVKEI 305
Cdd:cd03891 244 GELKAKFNIRFNDEHTGESLKARIEAILDKH 274
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
10-398 |
6.89e-32 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 123.57 E-value: 6.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 10 IKILADIVEINTENDNELEVCNYFKALLNKYDIDSKiiKVDNRRANLVAEIGEGKPKIAISGHMDVVDAGdyNEWKYDPF 89
Cdd:cd05651 3 IELLKSLIATPSFSREEHKTADLIENYLEQKGIPFK--RKGNNVWAENGHFDEGKPTLLLNSHHDTVKPN--AGWTKDPF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 90 KLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLqKGTIRLMATAaeEKEMSGAQ----LFKEQGyvnDLDGMIIAE 165
Cdd:cd05651 79 EPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGPL-NYNLIYAASA--EEEISGKNgiesLLPHLP---PLDLAIVGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 166 PSDGFAFYATKGSMGLKVTSKGIPAHSSLPSlGHNAINSLIAFIQRIKEkyVEIKKnekehsldVHPYIdecireqghyn 245
Cdd:cd05651 153 PTEMQPAIAEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDIQWLRD--FRFDK--------VSPLL----------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 246 dGDLKEDVaaglvivnSIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVK---EIDSERL-SVEVTVNHPTV 321
Cdd:cd05651 211 -GPVKMTV--------TQINAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLKseiKPRSFRLnSSAIPPDHPIV 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815845711 322 YT-HKDNRliNTFleynhdfkvsGMVGATDAAeLLGdkdedFDLAIIGPGHITLAHQTDEYVYKSRYLDYIDMYQQVI 398
Cdd:cd05651 282 QAaIAAGR--TPF----------GSPTLSDQA-LMP-----FPSVKIGPGDSSRSHTADEFIELSEIEEGIDIYIELL 341
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
71-284 |
1.71e-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. 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: 123.57 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 71 GHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEKEMSGAQLFK 150
Cdd:cd03895 81 GHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNGALAAL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 151 EQGYVndLDGMIIAEPSDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEkyVEIKKNEKEHSldv 230
Cdd:cd03895 161 MRGYR--ADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQE--LEREWNARKKS--- 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 815845711 231 HPyidecireqgHYNDGDlkedvaaGLVIVN-SIIRGGEQFNTVPesAYAEFNIR 284
Cdd:cd03895 234 HP----------HFSDHP-------HPINFNiGKIEGGDWPSSVP--AWCVLDCR 269
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
10-399 |
6.98e-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. 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: 120.84 E-value: 6.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 10 IKILADIVEINTENDNELEVCNYFKALLNKYDIDSKIIKVDNR-RANLVAEIGEGK-PKIAISGHMDVVDAgdynewkYD 87
Cdd:cd05652 2 LSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKQPVENKdRFNVYAYPGSSRqPRVLLTSHIDTVPP-------FI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 88 PFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEKEMSGAQLFKEQGyVNDLDGMIIAEPS 167
Cdd:cd05652 75 PYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGDGMKAFNDLG-LNTWDAVIFGEPT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 168 DGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIkekyveikknekehsldvhpyidecireqghyNDG 247
Cdd:cd05652 154 ELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKL--------------------------------IDA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 248 DLKEDVAAGLVIVN-SIIRGGEQFNTVPESAYAEFNIRTVpeYDNVAIEKLFKDTVKEI--DSERLSVEVTVNHPTVYth 324
Cdd:cd05652 202 DLPSSELLGPTTLNiGRISGGVAANVVPAAAEASVAIRLA--AGPPEVKDIVKEAVAGIltDTEDIEVTFTSGYGPVD-- 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815845711 325 kdnrlintfLEYNHD-FKVSGMVGATDAAELLGDKDEdfdlAIIGPGHITLAHQTDEYVYKSRYLDYIDMYQQVIL 399
Cdd:cd05652 278 ---------LDCDVDgFETDVVAYGTDIPYLKGDHKR----YLYGPGSILVAHGPDEAITVSELEEAVEGYKKLIL 340
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
10-316 |
8.25e-31 |
|
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: 121.16 E-value: 8.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 10 IKILADIVEINTENDNE---LEVCNYFKALLNKYDIDSKIIKVDNRRANLVAEI-GEGKPKIAISGHMDVV-DAGDYNEW 84
Cdd:cd03885 2 LDLLERLVNIESGTYDKegvDRVAELLAEELEALGFTVERRPLGEFGDHLIATFkGTGGKRVLLIGHMDTVfPEGTLAFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 85 KYdpfklTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEK-EMSGAQLFKE----QGYVndld 159
Cdd:cd03885 82 PF-----TVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIgSPGSRELIEEeakgADYV---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 160 gmIIAEPS--DGFAFYATKGSMGLKVTSKGIPAHSSL-PSLGHNAINSLIAFIQRIkekyveikknekeHSLDvhpyide 236
Cdd:cd03885 153 --LVFEPAraDGNLVTARKGIGRFRLTVKGRAAHAGNaPEKGRSAIYELAHQVLAL-------------HALT------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 237 cireqghyndgdlkeDVAAGLVIVNSIIRGGEQFNTVPESAYAEFNIR--TVPEYDNVaieklfKDTVKEIDSERLSVEV 314
Cdd:cd03885 211 ---------------DPEKGTTVNVGVISGGTRVNVVPDHAEAQVDVRfaTAEEADRV------EEALRAIVATTLVPGT 269
|
..
gi 815845711 315 TV 316
Cdd:cd03885 270 SV 271
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
55-284 |
3.37e-30 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 119.42 E-value: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 55 NLVAEIGEGKPKIAISGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLM 134
Cdd:PRK13009 49 NLWARRGTEGPHLCFAGHTDVVPPGDLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 135 ATAAEE-------KEMsgAQLFKEQGYVndLDGMIIAEPSdgfafyATK-----------GSMGLKVTSKGIPAHSSLPS 196
Cdd:PRK13009 129 ITSDEEgpaingtVKV--LEWLKARGEK--IDYCIVGEPT------STErlgdvikngrrGSLTGKLTVKGVQGHVAYPH 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 197 LGHNAINSLIAFIQRIkekyveikkneKEHSLDvhpyidecireqghynDGDlkEDVAA-GLVIVNsiIRGG-EQFNTVP 274
Cdd:PRK13009 199 LADNPIHLAAPALAEL-----------AATEWD----------------EGN--EFFPPtSLQITN--IDAGtGATNVIP 247
|
250
....*....|
gi 815845711 275 ESAYAEFNIR 284
Cdd:PRK13009 248 GELEAQFNFR 257
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
6-382 |
1.37e-29 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 119.27 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 6 EEDKIKILADIVEINTENDNELEVC----------NYFKALLNKYDIDSKiiKVDNRRAnlVAEIGEGKPKIAISGHMDV 75
Cdd:cd03888 7 KDEILEDLKELVAIPSVRDEATEGApfgegprkalDKFLDLAKRLGFKTK--NIDNYAG--YAEYGEGEEVLGILGHLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 76 VDAGDynEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEKEMSGAQLFK----- 150
Cdd:cd03888 83 VPAGE--GWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGWKCIEHYFeheey 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 151 ----------------EQGYVN-------------------------------------DLDGMIIAEPSDGFAFYATKG 177
Cdd:cd03888 161 pdfgftpdaefpvingEKGIVTvdltfkidddkgyrlisikggeatnmvpdkaeavipgKDKEELALSAATDLKGNIEID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 178 SMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIqrikekyveikkNEKEHSLDVHPYIDECIREQGHYNDGDL----KEDV 253
Cdd:cd03888 241 DGGVELTVTGKSAHASAPEKGVNAITLLAKFL------------AELNKDGNDKDFIKFLAKNLHEDYNGKKlginFEDE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 254 AAGLVIVNSIIrggeqFNTVPESAYAEFNIRtVPEydNVAIEKLFKDTVKEIDSERLSVEVTVNHPTVYTHKDNRLINTF 333
Cdd:cd03888 309 VMGELTLNPGI-----ITLDDGKLELGLNVR-YPV--GTSAEDIIKQIEEALEKYGVEVEGHKHQKPLYVPKDSPLVKTL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 815845711 334 LE-------YNHDFKVSGmvGATDAAELlgDKDEDFDLAIigPGHITLAHQTDEYV 382
Cdd:cd03888 381 LKvyeeqtgKEGEPVAIG--GGTYAREL--PNGVAFGPEF--PGQKDTMHQANEFI 430
|
|
| PRK06915 |
PRK06915 |
peptidase; |
61-224 |
7.31e-29 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 116.71 E-value: 7.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 61 GEGKPKIaISGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEE 140
Cdd:PRK06915 91 GGGKSMI-LNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 141 KEMSGAQLFKEQGYvnDLDGMIIAEPSDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEkyVEIK 220
Cdd:PRK06915 170 SGGAGTLAAILRGY--KADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRK--LEEK 245
|
....
gi 815845711 221 KNEK 224
Cdd:PRK06915 246 RNDR 249
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
7-382 |
8.27e-29 |
|
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: 115.14 E-value: 8.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 7 EDKIKILADIVEINTENDNELEVCNYFKALLNKYDIDSKIIKVDNrranLVAEIGEGKPKIAISGHMDVVDAgdynewkY 86
Cdd:cd05653 1 QDAVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEAGN----AVGGAGSGPPDVLLLGHIDTVPG-------E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 87 DPFKLteEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRlqkGTIRLMATAAEEKEMSGAQLFKEQGYvnDLDGMIIAEP 166
Cdd:cd05653 70 IPVRV--EGGVLYGRGAVDAKGPLAAMILAASALNEELG---ARVVVAGLVDEEGSSKGARELVRRGP--RPDYIIIGEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 167 S--DGFAfYATKGSMGLKVTSKGIPAHSSLPslGHNAINSLIAFIQRIKekyveikknekehsldvhpyideciREQGHY 244
Cdd:cd05653 143 SgwDGIT-LGYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLIKKWLEVK-------------------------KWAEGY 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 245 NDGDLKEDvaaglVIVNSIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIDserlsVEVTVNHPTVYTH 324
Cdd:cd05653 195 NVGGRDFD-----SVVPTLIKGGESSNGLPQRAEATIDLRLPPRLSPEEAIALATALLPTCE-----LEFIDDTEPVKVS 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815845711 325 KDNRLINTF----LEYNHDFKVSGMVGATDaAELLGDKdEDFDLAIIGPGHITLAHQTDEYV 382
Cdd:cd05653 265 KNNPLARAFrraiRKQGGKPRLKRKTGTSD-MNVLAPL-WTVPIVAYGPGDSTLDHTPNEHI 324
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
6-215 |
1.78e-28 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 115.63 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 6 EEDKIKILADIVEINTEN---DNELEVCNYFKALLNKYDIDSKIIKVDNR--------RANLVAEIGEGKPK--IAISGH 72
Cdd:PRK13013 13 RDDLVALTQDLIRIPTLNppgRAYREICEFLAARLAPRGFEVELIRAEGApgdsetypRWNLVARRQGARDGdcVHFNSH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 73 MDVVDAGdyNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEK-EMSGAQLFKE 151
Cdd:PRK13013 93 HDVVEVG--HGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESgGFGGVAYLAE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815845711 152 QGYVND--LDGMIIAEPSDGFAFY-ATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEK 215
Cdd:PRK13013 171 QGRFSPdrVQHVIIPEPLNKDRIClGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEIEER 237
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
31-400 |
7.68e-28 |
|
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: 112.89 E-value: 7.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 31 NYFKALLNKYDIDSKIIKVdNRRANLVAEIGEGKPKIAISGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGL 110
Cdd:TIGR01246 23 DIIAERLEKLGFEIEWMHF-GDTKNLWATRGTGEPVLAFAGHTDVVPAGPEEQWSSPPFEPVERDGKLYGRGAADMKGSL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 111 AALIIAMIEIKESGRLQKGTIRLMATAAEE-------KEMsgAQLFKEQGYVndLDGMIIAEPSDGFAFYAT-----KGS 178
Cdd:TIGR01246 102 AAFIVAAERFVKKNPDHKGSISLLITSDEEgtaidgtKKV--VETLMARDEL--IDYCIVGEPSSVKKLGDVikngrRGS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 179 MGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKekyveikknekehsldvhpyidecireQGHYNDGDlKEDVAAGLV 258
Cdd:TIGR01246 178 ITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELT---------------------------AIKWDEGN-EFFPPTSLQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 259 IVNsiIRGGEQF-NTVPESAYAEFNIRTVPEydnVAIEKLFKDTVKEIDSERL--SVEVTVNHPTVYThKDNRLINTFL- 334
Cdd:TIGR01246 230 ITN--IHAGTGAnNVIPGELYVQFNLRFSTE---VSDEILKQRVEAILDQHGLdyDLEWSLSGEPFLT-NDGKLIDKARe 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815845711 335 ---EYNH---DFKVSGmvGATDAAELlgdKDEDFDLAIIGPGHITlAHQTDEYVYKSRYLDYIDMYQQVILN 400
Cdd:TIGR01246 304 aieETNGikpELSTGG--GTSDGRFI---ALMGAEVVEFGPVNAT-IHKVNECVSIEDLEKLSDVYQDLLEN 369
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-382 |
9.45e-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. 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: 109.87 E-value: 9.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 7 EDKIKILADIVEINTENDN--------ELEVCNYFKALLNKYDIDSKIIKVDNRRANLVAEI---GEGKpKIAISGHMDV 75
Cdd:cd08013 1 DDPVSLTQTLVRINSSNPSlsatggagEAEIATYVAAWLAHRGIEAHRIEGTPGRPSVVGVVrgtGGGK-SLMLNGHIDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 76 VDAGDYNEwkyDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGrlQKGTIRLMATAAEEKEMSGAQLFKEQGYv 155
Cdd:cd08013 80 VTLDGYDG---DPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAG--LRGDVILAAVADEEDASLGTQEVLAAGW- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 156 nDLDGMIIAEPSDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEKYVEIKKNEkehsldVHPYId 235
Cdd:cd08013 154 -RADAAIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALEEYQQELPERP------VDPLL- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 236 ecireqGHYNdgdlkedVAAGLvivnsiIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIDSE------- 308
Cdd:cd08013 226 ------GRAS-------VHASL------IKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTAILGELAQTvpnfsyr 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 309 -------RLSVEVTVNHPTV-YTHKDNRLIntfleYNHDFKVSGMVGATDAAELlgdKDEDFDLAIIGPgHITLAHQTDE 380
Cdd:cd08013 287 epritlsRPPFEVPKEHPFVqLVAAHAAKV-----LGEAPQIRSETFWTDAALL---AEAGIPSVVFGP-SGAGLHAKEE 357
|
..
gi 815845711 381 YV 382
Cdd:cd08013 358 WV 359
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-386 |
4.29e-26 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 108.31 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 7 EDKIKILADIVEINTEN-----DNELEVCNYFKALL--------NKYDIDSKIIKVdnrRANLVAEIGEGKPK-IAISGH 72
Cdd:cd05650 1 EEIIELERDLIRIPAVNpesggEGEKEKADYLEKKLreygfytlERYDAPDERGII---RPNIVAKIPGGNDKtLWIISH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 73 MDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEE--KEMSGAQLFK 150
Cdd:cd05650 78 LDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEdgSEYGIQYLLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 151 EQGYVNDLDGMIIAE---PSDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEKYVEiKKNEKEHS 227
Cdd:cd05650 158 KFDLFKKDDLIIVPDfgtEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFALELDELLHE-KFDEKDDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 228 LDVhPYidecireqGHYNDGDLKEDVaaglvivnsiirggEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIDS 307
Cdd:cd05650 237 FNP-PY--------STFEPTKKEANV--------------PNVNTIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDFEN 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 308 E---RLSVEVTVNHPTV-YTHKDNRLINTFLE-----YNHDFKVSGMVGATDAAELlgdKDEDFDLAIIGPGHITlAHQT 378
Cdd:cd05650 294 SygaGITYEIVQKEQAPpATPEDSEIVVRLSKaikkvRGREAKLIGIGGGTVAAFL---RKKGYPAVVWSTLDET-AHQP 369
|
....*...
gi 815845711 379 DEYVYKSR 386
Cdd:cd05650 370 NEYIRISH 377
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
10-382 |
3.12e-24 |
|
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: 102.52 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 10 IKILADIVEINTENDNELEVCNYFKALLNKYDiDSKIIKVDNrraNLVAEIGEGKP-KIAISGHMDVVD-AGDYnewkyd 87
Cdd:cd05647 2 IELTAALVDIPSVSGNEKPIADEIEAALRTLP-HLEVIRDGN---TVVARTERGLAsRVILAGHLDTVPvAGNL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 88 PFKLtEEDDKLYGRGTTDMKGGLAALIIAMIEIKEsgRLQKGTIRLMATAAEE--KEMSG-AQLFKEQGYVNDLDGMIIA 164
Cdd:cd05647 72 PSRV-EEDGVLYGCGATDMKAGDAVQLKLAATLAA--ATLKHDLTLIFYDCEEvaAELNGlGRLAEEHPEWLAADFAVLG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 165 EPSDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRI---KEKYVEIkknekehsldvhpyidecireq 241
Cdd:cd05647 149 EPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLaayEPRTVNI---------------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 242 ghynDG-DLKEdvaaGLVIVnsIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIDSErlsVEVTVNHPT 320
Cdd:cd05647 207 ----DGlTYRE----GLNAV--FISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYE---IEVTDLSPG 273
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 815845711 321 VYTHKDNRLINTFLEYNHDfKVSGMVGATDAAEL--LGDKDEDFdlaiiGPGHITLAHQTDEYV 382
Cdd:cd05647 274 ALPGLDHPVARDLIEAVGG-KVRAKYGWTDVARFsaLGIPAVNF-----GPGDPLLAHKRDEQV 331
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
6-382 |
4.91e-24 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 102.62 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 6 EEDKIKILADIVEINTEN-----DNELEVCNYFKALLNKYDIDSkiIKV----DNR-----RANLVAEI--GEGKPKIAI 69
Cdd:PRK13983 4 RDEMIELLSELIAIPAVNpdfggEGEKEKAEYLESLLKEYGFDE--VERydapDPRviegvRPNIVAKIpgGDGKRTLWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 70 SGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEE--------- 140
Cdd:PRK13983 82 ISHMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEEtgskygiqy 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 141 --KEMSGaqLFKEqgyvNDL---------DG-MI-IAEpsdgfafyatKGSMGLKVTSKGIPAHSSLPslgHNAINSLIA 207
Cdd:PRK13983 162 llKKHPE--LFKK----DDLilvpdagnpDGsFIeIAE----------KSILWLKFTVKGKQCHASTP---ENGINAHRA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 208 ---FIQRIkEKYVEIKKNEKEhSLDVHPY--IDECIREQGhyndgdlkedvaaglviVNSIirggeqfNTVPesAYAEFN 282
Cdd:PRK13983 223 aadFALEL-DEALHEKFNAKD-PLFDPPYstFEPTKKEAN-----------------VDNI-------NTIP--GRDVFY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 283 I--RTVPEYDNVAIEKLFKDTVKEIDSE-RLSVEVTV---NHPTVYTHKDNRLINTFLE-----YNHDFKVSGMVGATDA 351
Cdd:PRK13983 275 FdcRVLPDYDLDEVLKDIKEIADEFEEEyGVKIEVEIvqrEQAPPPTPPDSEIVKKLKRaikevRGIEPKVGGIGGGTVA 354
|
410 420 430
....*....|....*....|....*....|.
gi 815845711 352 AELlgdKDEDFDLAIIGPGHITlAHQTDEYV 382
Cdd:PRK13983 355 AFL---RKKGYPAVVWSTLDET-AHQPNEYA 381
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
12-212 |
5.20e-24 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 103.54 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 12 ILADIVEINT--ENDNELEVCNYFKALLNK---YDIDSKIIKVDNRRANLVAEI---GEGKPkIAISGHMDVVDAgDYNE 83
Cdd:PRK09133 42 LYKELIEINTtaSTGSTTPAAEAMAARLKAagfADADIEVTGPYPRKGNLVARLrgtDPKKP-ILLLAHMDVVEA-KRED 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 84 WKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEK-EMSGA--------QLFKEQGY 154
Cdd:PRK09133 120 WTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEGtPMNGVawlaenhrDLIDAEFA 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815845711 155 VNDLDGMIIAEpsDGFA-FYATKGS------MGLKVTSKGipAHSSLPSLGhNAINSLIAFIQRI 212
Cdd:PRK09133 200 LNEGGGGTLDE--DGKPvLLTVQAGektyadFRLEVTNPG--GHSSRPTKD-NAIYRLAAALSRL 259
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
71-284 |
2.21e-23 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 101.23 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 71 GHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEKEMSGAQLFK 150
Cdd:PRK06837 104 GHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEESTGNGALSTL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 151 EQGYvnDLDGMIIAEPSDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEkyVEIKKNEKEHSldv 230
Cdd:PRK06837 184 QRGY--RADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRE--LEAEWNARKAS--- 256
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 815845711 231 HPY---IDECIReqghYNDGdlkedvaaglvivnsIIRGGEQFNTVPesAYAEFNIR 284
Cdd:PRK06837 257 DPHfedVPHPIN----FNVG---------------IIKGGDWASSVP--AWCDLDCR 292
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
7-382 |
3.87e-23 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 99.45 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 7 EDKIKILADIVEINTENDNELEVCNYFKALLNKYDIDSKIiKVDNRRANLVAEigeGKPKIAISGHMDVVDAgdynewKY 86
Cdd:PRK08652 2 ERAKELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHI-ESDGEVINIVVN---SKAELFVEVHYDTVPV------RA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 87 DPFkltEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLmaTAAEEKEMSGAQLFKEQ---GYVndldgmII 163
Cdd:PRK08652 72 EFF---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAF--VSDEEEGGRGSALFAERyrpKMA------IV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 164 AEPSDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEkyVEIKKNEKehsLDVHPYIDEcireqgh 243
Cdd:PRK08652 141 LEPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKE--LLKALGKY---FDPHIGIQE------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 244 yndgdlkedvaaglvivnsiIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIDserLSVEVTVNHPTVYT 323
Cdd:PRK08652 209 --------------------IIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYT---VKYEYTEIWDGFEL 265
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815845711 324 HKDNRLI----NTFLEYNHDFKVSGMVGATDAAELlgdKDEDFDLAIIGPGHITLAHQTDEYV 382
Cdd:PRK08652 266 DEDEEIVqlleKAMKEVGLEPEFTVMRSWTDAINF---RYNGTKTVVWGPGELDLCHTKFERI 325
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
6-168 |
1.09e-22 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 98.96 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 6 EEDKIKILADIVEINTE-----NDNELEvcNYFKALLNKYDIDSKIIKVDNRRANLVAEIGEGKPK----IAISGHMDVV 76
Cdd:PRK08596 12 KDELLELLKTLVRFETPapparNTNEAQ--EFIAEFLRKLGFSVDKWDVYPNDPNVVGVKKGTESDayksLIINGHMDVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 77 DAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEKEMSGAQLFKEQGYVN 156
Cdd:PRK08596 90 EVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEVGEAGTLQCCERGYDA 169
|
170
....*....|..
gi 815845711 157 DLdgMIIAEPSD 168
Cdd:PRK08596 170 DF--AVVVDTSD 179
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
5-334 |
3.15e-21 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 93.87 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 5 SEEDKIKILADIVEINTENDNELEVCNYFKALLNKYDIDSKIIKVDNrranLVAEIGEGKPKIAISGHMDVVdAGDYnew 84
Cdd:PRK04443 4 SALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREAWVDEAGN----ARGPAGDGPPLVLLLGHIDTV-PGDI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 85 kydPFKLteEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLqkgTIRLMATAAEEKEMSGAQLFKEQGYVNDLdgMIIA 164
Cdd:PRK04443 76 ---PVRV--EDGVLWGRGSVDAKGPLAAFAAAAARLEALVRA---RVSFVGAVEEEAPSSGGARLVADRERPDA--VIIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 165 EPS--DGFAF-YatKGSMGLKVTSKGIPAHSSLPslGHNAINSLIAFIQRIKEkYVEIKKnekehsldvhpyidecireq 241
Cdd:PRK04443 146 EPSgwDGITLgY--KGRLLVTYVATSESFHSAGP--EPNAAEDAIEWWLAVEA-WFEAND-------------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 242 ghyNDGDLKEDVAAGLVIVNSIIRGGEQFntvpesAYAEFNIRTVPEYDNVAIEklfkdTVKEIDSERLSVEVTVNHPTV 321
Cdd:PRK04443 201 ---GRERVFDQVTPKLVDFDSSSDGLTVE------AEMTVGLRLPPGLSPEEAR-----EILDALLPTGTVTFTGAVPAY 266
|
330
....*....|...
gi 815845711 322 YTHKDNRLINTFL 334
Cdd:PRK04443 267 MVSKRTPLARAFR 279
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
8-399 |
5.24e-21 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 94.46 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 8 DKIKILADIVEINTENDNEL------EVCNYFKALLNKYDIDSKIIKVDNRRAnLVAEIGEGKPKIAISGHMDVVDAGDy 81
Cdd:PRK08554 2 DVLELLSSLVSFETVNDPSKgikpskECPKFIKDTLESWGIESELIEKDGYYA-VYGEIGEGKPKLLFMAHFDVVPVNP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 82 NEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEI-KESGRlqkGTIRLMATAAEE----KEMSGAQLFKEQGYVN 156
Cdd:PRK08554 80 EEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELsKEPLN---GKVIFAFTGDEEiggaMAMHIAEKLREEGKLP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 157 DLdgMIIAEpsdgfafyatkGSMGLKVT--SKGIPAHSSLPSLGHNAINSLiafiqRIKEKYVEIKKNEKEHS------L 228
Cdd:PRK08554 157 KY--MINAD-----------GIGMKPIIrrRKGFGVTIRVPSEKVKVKGKL-----REQTFEIRTPVVETRHAayflpgV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 229 DVHPYI--DECIREQGHYN---DGD-LKEDVAAGLVIVNSIIRGGEQFNTVPES-------------------AYAEFNI 283
Cdd:PRK08554 219 DTHPLIaaSHFLRESNVLAvslEGKfLKGNVVPGEVTLTYLEPGEGEEVEVDLGltrllkaivplvrapikaeKYSDYGV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 284 RTVPE-------------------YDNVAIEKlfkdTVKEIDSERLS---VEVTVNHPT--VYTHKDNRLINTFLEYNHD 339
Cdd:PRK08554 299 SITPNvysfaegkhvlkldiramsYSKEDIER----TLKEVLEFNLPeaeVEIRTNEKAgyLFTPPDEEIVKVALRVLKE 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815845711 340 FKVSGM----VGATDAAEL--LGDKDEDFdlaiiGP--GHItlaHQTDEYVYKSRYLDYIDMYQQVIL 399
Cdd:PRK08554 375 LGEDAEpvegPGASDSRYFtpYGVKAIDF-----GPkgGNI---HGPNEYVEIDSLKKMPEVYKRIAL 434
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
55-147 |
1.05e-20 |
|
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: 89.03 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 55 NLVAEIG--EGKPKIAISGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIR 132
Cdd:cd18669 1 NVIARYGggGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90
....*....|....*
gi 815845711 133 LMATAAEEKEMSGAQ 147
Cdd:cd18669 81 VAFTPDEEVGSGAGK 95
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
62-400 |
3.08e-20 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 92.31 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 62 EGKPKIAISGHMDVV--DAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAE 139
Cdd:PRK08262 109 PSLKPIVLMAHQDVVpvAPGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 140 EKEMSGAQ----LFKEQG----YVNDLDGMIIAEPSDG----FAF--YATKGSMGLKVTSKGIPAHSSLPSlGHNAINSL 205
Cdd:PRK08262 189 EVGGLGARaiaeLLKERGvrlaFVLDEGGAITEGVLPGvkkpVALigVAEKGYATLELTARATGGHSSMPP-RQTAIGRL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 206 IAFIQRIKEKYVEIKKNEK-EHSLDV-HPYIDECIReQGHYNDGDLKEDVAAGL------------VIVNSIIRGGEQFN 271
Cdd:PRK08262 268 ARALTRLEDNPLPMRLRGPvAEMFDTlAPEMSFAQR-VVLANLWLFEPLLLRVLakspetaamlrtTTAPTMLKGSPKDN 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 272 TVPESAYAEFNIRTVPEyDNVA--IEKlfkdtVKE-IDSERLSVEV--TVNHPTVYTHKDN---RLIN-TFLEYNHDFKV 342
Cdd:PRK08262 347 VLPQRATATVNFRILPG-DSVEsvLAH-----VRRaVADDRVEIEVlgGNSEPSPVSSTDSaayKLLAaTIREVFPDVVV 420
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815845711 343 SG--MVGATDAAELLGDKDEDFDLA--IIGPGHITLAHQTDEYVYKSRYLDYIDMYQQVILN 400
Cdd:PRK08262 421 APylVVGATDSRHYSGISDNVYRFSplRLSPEDLARFHGTNERISVANYARMIRFYYRLIEN 482
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
55-140 |
7.40e-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: 86.71 E-value: 7.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 55 NLVAEIG--EGKPKIAISGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIR 132
Cdd:cd03873 1 NLIARLGggEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
|
....*...
gi 815845711 133 LMATAAEE 140
Cdd:cd03873 81 VAFTADEE 88
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
28-297 |
8.38e-20 |
|
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: 90.46 E-value: 8.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 28 EVCNYFKALLNKYDIDSKIIKVDNRRANLVAEIG--EGKPKIAISGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTD 105
Cdd:cd03893 25 RAAEWLADLLRRLGFTVEIVDTSNGAPVVFAEFPgaPGAPTVLLYGHYDVQPAGDEDGWDSDPFELTERDGRLYGRGAAD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 106 MKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEkemSGAQLFKEqgYVNDL------DGMIIaepSDGFA-------- 171
Cdd:cd03893 105 DKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEE---SGSPSLDQ--LVEAHrdllaaDAIVI---SDSTWvgqeqptl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 172 FYATKGSMGLKVTSKGI--PAHSSLPS-LGHNAINSLIAFIQRIkekyveikKNEKEHSL------DVHPYIDECIREQG 242
Cdd:cd03893 177 TYGLRGNANFDVEVKGLdhDLHSGLYGgVVPDPMTALAQLLASL--------RDETGRILvpglydAVRELPEEEFRLDA 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815845711 243 HY-----NDGDLKEDVAAGLVIVNSI----IRGGEQ----FNTVPESAYAEFNIRTVPEYDNVAIEKL 297
Cdd:cd03893 249 GVleeveIIGGTTGSVAERLWTRPALtvlgIDGGFPgegsKTVIPPRARAKISIRLVPGQDPEEASRL 316
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
65-400 |
3.10e-19 |
|
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: 88.69 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 65 PKIAISGHMDVVDAGDYNeWKYDPFK-LTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEE--- 140
Cdd:TIGR01880 72 PSILLNSHTDVVPVFREH-WTHPPFSaFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEigg 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 141 ----KEMSGAQLFKE--QGYVNDlDGMiiAEPSDGF-AFYATKGSMGLKVTSKGIPAHSS--LPSLGHNAINSLIAFIQR 211
Cdd:TIGR01880 151 hdgmEKFAKTDEFKAlnLGFALD-EGL--ASPDDVYrVFYAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 212 IKEKYVEIKKNekehsldvhpyidecireqghyndgdlKEDVAAGLVI-VN-SIIRGGEQFNTVPESAYAEFNIRTVPEY 289
Cdd:TIGR01880 228 FRESQFQLLQS---------------------------NPDLAIGDVTsVNlTKLKGGVQSNVIPSEAEAGFDIRLAPSV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 290 DNVAIE-KLFKDTVKEIDSERLSVEVTVNHPTVYTHKDNR-----LINTFLEYNHDFKVSGMVGATDAAEL--LGDKDED 361
Cdd:TIGR01880 281 DFEEMEnRLDEWCADAGEGVTYEFSQHSGKPLVTPHDDSNpwwvaFKDAVKEMGCTFKPEILPGSTDSRYIraAGVPALG 360
|
330 340 350
....*....|....*....|....*....|....*....
gi 815845711 362 FDLAIIGPghiTLAHQTDEYVYKSRYLDYIDMYQQVILN 400
Cdd:TIGR01880 361 FSPMNNTP---VLLHDHNEFLNEAVFLRGIEIYQTLISA 396
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
12-323 |
3.07e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 86.06 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 12 ILADIVEINTEN--DN----ELEVCNYFKALLNKYDIDSKIIKVDNRRANLVAEI-GE--GKPKIAISGHMDVVDAgDYN 82
Cdd:PRK07906 4 LCSELIRIDTTNtgDGtgkgEREAAEYVAEKLAEVGLEPTYLESAPGRANVVARLpGAdpSRPALLVHGHLDVVPA-EAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 83 EWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEKEMS-GAQ--------LFkeqg 153
Cdd:PRK07906 83 DWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEAGGTyGAHwlvdnhpeLF---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 154 yvndlDGMI--IAEpSDGFAF--------Y----ATKGSMGLKVTSKGIPAHSSLPSlGHNAINSLIAFIQRIkekyvei 219
Cdd:PRK07906 159 -----EGVTeaISE-VGGFSLtvpgrdrlYlietAEKGLAWMRLTARGRAGHGSMVN-DDNAVTRLAEAVARI------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 220 kkNEKEHSLDVHPYIDECIREQGHYNDGDLKEDVAAGLV--------IVNSIIR---------GGEQFNTVPESAYAEFN 282
Cdd:PRK07906 225 --GRHRWPLVLTPTVRAFLDGVAELTGLEFDPDDPDALLaklgpaarMVGATLRntanptmlkAGYKVNVIPGTAEAVVD 302
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 815845711 283 IRTVPEYdnvaiEKLFKDTVKEIDSERLSVEVTVNHPTVYT 323
Cdd:PRK07906 303 GRFLPGR-----EEEFLATVDELLGPDVEREWVHRDPALET 338
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
58-398 |
3.44e-18 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 85.89 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 58 AEIGEGKPKIAISGHMDVVDAGDynEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATA 137
Cdd:TIGR01887 61 IEYGQGEEVLGILGHLDVVPAGD--GWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGT 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 138 AEEKEMSGAQLF---------------------KEQGYVN----------------------------DLDGMIIAEPSD 168
Cdd:TIGR01887 139 DEESGWKCIDYYfeheempdigftpdaefpiiyGEKGITTleikfkddtegdvvlesfkageaynmvpDHATAVISGKKL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 169 ------GFAFYATKGSMG--------LKVTSKGIPAHSSLPSLGHNAINSLIAFIQrikekyvEIKKNEKEHSLdVHpYI 234
Cdd:TIGR01887 219 teveqlKFVFFIAKELEGdfevndgtLTITLEGKSAHGSAPEKGINAATYLALFLA-------QLNLAGGAKAF-LQ-FL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 235 DECIREQgHYNDG---DLKEDVAAGLVIVNSIIRggeqfNTVPESAYAEFNIRTvPEYDNVAIEklfkdTVKEIDSERLS 311
Cdd:TIGR01887 290 AEYLHED-HYGEKlgiKFHDDVSGDLTMNVGVID-----YENAEAGLIGLNVRY-PVGNDPDTM-----LKNELAKESGV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 312 VEVTVN--HPTVYTHKDNRLINTFLE-Y-NHDFKVSGMV---GATDAAELlgdkDEDFDLAIIGPGHITLAHQTDEYVYK 384
Cdd:TIGR01887 358 VEVTLNgyLKPLYVPKDDPLVQTLMKvYeKQTGDEGEPVaigGGTYARLM----PNGVAFGALFPGEEDTMHQANEYIMI 433
|
410
....*....|....
gi 815845711 385 SRYLDYIDMYQQVI 398
Cdd:TIGR01887 434 DDLLLATAIYAEAI 447
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
64-399 |
1.02e-17 |
|
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: 84.61 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 64 KPkIAISGHMDVVDA--GDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIrLMATAAEEk 141
Cdd:cd05674 70 KP-LLLMAHQDVVPVnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTI-ILAFGHDE- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 142 EMSG-------AQLFKEQGYVNDLD------GMIIAEPSDG--FAFYAT--KGSMGLKVTSKGIPAHSSLPsLGHNAINS 204
Cdd:cd05674 147 EVGGergagaiAELLLERYGVDGLAaildegGAVLEGVFLGvpFALPGVaeKGYMDVEITVHTPGGHSSVP-PKHTGIGI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 205 LIAFIQRIKE---KYVEIKKNE--------KEHSLDVHPYIDECIREQGHYNDGDLKEDVAAGLVIVNS---------II 264
Cdd:cd05674 226 LSEAVAALEAnpfPPKLTPGNPyygmlqclAEHSPLPPRSLKSNLWLASPLLKALLASELLSTSPLTRAllrttqavdII 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 265 RGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIDSErLSVEVTVNHPTVYTHKDNRLI-------------- 330
Cdd:cd05674 306 NGGVKINALPETATATVNHRIAPGSSVEEVLEHVKNLIADIAVK-YGLGLSAFGGDVIYSTNGTKLltsllspepspvss 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 331 --------------NTFLEYNHDFKVSG--MVGATDAA--ELLGDKDEDFDLAIIGPGHITLAHQTDEYVYKSRYLDYID 392
Cdd:cd05674 385 tsspvwqllagtirQVFEQFGEDLVVAPgiMTGNTDTRhyWNLTKNIYRFTPIRLNPEDLGRIHGVNERISIDDYLETVA 464
|
....*..
gi 815845711 393 MYQQVIL 399
Cdd:cd05674 465 FYYQLIQ 471
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
6-401 |
2.74e-17 |
|
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: 82.71 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 6 EEDKIKILADIVEINTENDN-ELEVCNYF-KALLNKYDIDSKIIKVDNRRANLVAEIgEGK----PKIAISGHMDVVDAG 79
Cdd:cd05646 1 EDPAVTRFREYLRINTVHPNpDYDACVEFlKRQADELGLPVRVIEVVPGKPVVVLTW-EGSnpelPSILLNSHTDVVPVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 80 DyNEWKYDPFK-LTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEE-------KEMSGAQLFKE 151
Cdd:cd05646 80 E-EKWTHDPFSaHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEigghdgmEKFVKTEEFKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 152 --QGYVNDlDGmiIAEPSDGFA-FYATKGSMGLKVTSKGIPAHSSLpSLGHNAINSLiafiQRIKEKYVEIKKNEKEhsl 228
Cdd:cd05646 159 lnVGFALD-EG--LASPTEEYRvFYGERSPWWVVITAPGTPGHGSK-LLENTAGEKL----RKVIESIMEFRESQKQ--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 229 dvhpyideciREQghyNDGDLKE-DVAAglviVN-SIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKE-I 305
Cdd:cd05646 228 ----------RLK---SNPNLTLgDVTT----VNlTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEaG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 306 DSERLSVEVTVNHPTVYTHKDNR-----LINTFLEYNHDFKVSGMVGATDAAEL--LGdkdedfdLAIIG--PGHIT--L 374
Cdd:cd05646 291 RGVTYEFEQKSPEKDPTSLDDSNpwwaaFKKAVKEMGLKLKPEIFPAATDSRYIraLG-------IPALGfsPMNNTpiL 363
|
410 420
....*....|....*....|....*..
gi 815845711 375 AHQTDEYVYKSRYLDYIDMYQQVILNY 401
Cdd:cd05646 364 LHDHNEFLNEDVFLRGIEIYEKIIPAL 390
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
58-229 |
4.26e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 82.82 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 58 AEIGEGKPKIAISGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATA 137
Cdd:PRK07205 69 AEIGQGEELLAILCHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGT 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 138 AEEkemsgaQLFKEQGYVNDLDgmiiAEPSDGFA-------FYATKGSMGLKVTSKGipaHSSLPSLGHNAINSLIAFIQ 210
Cdd:PRK07205 149 DEE------TLWRCMNRYNEVE----EQATMGFApdssfplTYAEKGLLQAKLVGPG---SDQLELEVGQAFNVVPAKAS 215
|
170
....*....|....*....
gi 815845711 211 RIKEKYVEIKKNEKEHSLD 229
Cdd:PRK07205 216 YQGPKLEAVKKELDKLGFE 234
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
10-400 |
9.31e-17 |
|
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: 81.62 E-value: 9.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 10 IKILADIVEINT---ENDNELEVCNYFKALLNKYDIDSKIIKVDNRRAnLVAEIGEGKPK-IAISGHMDVVDAGDYNEWK 85
Cdd:cd05681 2 LEDLRDLLKIPSvsaQGRGIPETADFLKEFLRRLGAEVEIFETDGNPI-VYAEFNSGDAKtLLFYNHYDVQPAEPLELWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 86 YDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEE--------------KEMSGAQLFKE 151
Cdd:cd05681 81 SDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEvgspnlekfvaehaDLLKADGCIWE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 152 QGYVNDLDGMIIAepsdgfafYATKGSMGLKVTSKGIPA--HSSLPSLGHN-------AINSLIAFIQRIK-----EKYV 217
Cdd:cd05681 161 GGGKNPKGRPQIS--------LGVKGIVYVELRVKTADFdlHSSYGAIVENpawrlvqALNSLRDEDGRVLipgfyDDVR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 218 EIKKNEKEhSLDVHPYIDECIR------EQGHYNDGDLKED-VAAGLVIVNSIIRG--GEQFNTV-PESAYAEFNIRTVP 287
Cdd:cd05681 233 PLSEAERA-LIDTYDFDPEELRktyglkRPLQVEGKDPLRAlFTEPTCNINGIYSGytGEGSKTIlPSEAFAKLDFRLVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 288 EYDNvaiEKLFKDTVKEIDSERLS-VEVTVNH--PTVYTHKDNRLINTFLE-----YNHDFKVSGMVGATDAAELLGDKD 359
Cdd:cd05681 312 DQDP---AKILSLLRKHLDKNGFDdIEIHDLLgeKPFRTDPDAPFVQAVIEsakevYGQDPIVLPNSAGTGPMYPFYDAL 388
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 815845711 360 EDFDLAIIGPGHITLAHQTDEYVYKSRYLDYIDMYQQVILN 400
Cdd:cd05681 389 EVPVVAIGVGNAGSNAHAPNENIRIADYYKGIEHTEELLRN 429
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
173-308 |
1.06e-16 |
|
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: 75.46 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 173 YATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEKYVEIKKNEKEHSLDVhpyidecireqghyndgdlked 252
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGFDFPRTTLNI---------------------- 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 815845711 253 vaaglvivnSIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIDSE 308
Cdd:pfam07687 59 ---------TGIEGGTATNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEKELPE 105
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
33-140 |
4.76e-16 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 79.63 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 33 FKALLNKY--DIDSKIIKVDNRranlVAEI---GEGKPKIAISGHMDVVDAgDYNEW-----KYDPFKLTEEDDKLYGRG 102
Cdd:PRK06156 77 FKKLLKSLarDFGLDYRNVDNR----VLEIglgGSGSDKVGILTHADVVPA-NPELWvldgtRLDPFKVTLVGDRLYGRG 151
|
90 100 110
....*....|....*....|....*....|....*...
gi 815845711 103 TTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEE 140
Cdd:PRK06156 152 TEDDKGAIVTALYAMKAIKDSGLPLARRIELLVYTTEE 189
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
55-304 |
7.47e-16 |
|
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: 78.75 E-value: 7.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 55 NLVA--EIGEGKPKIAISGHMDVVDAGDynEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIR 132
Cdd:cd02697 62 NLIVrrRYGDGGRTVALNAHGDVVPPGD--GWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 133 LMATAAEE--KEMSGAQLFKeQGyVNDLDGMIIAepsdGFAF---YATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIA 207
Cdd:cd02697 140 LHFTYDEEfgGELGPGWLLR-QG-LTKPDLLIAA----GFSYevvTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 208 FIQRIKEKYVEIKKNEKEHSLDVHPYIdecireqghyNDGdlkedvaaglvivnsIIRGGEQFNTVPESAYAEFNIRTVP 287
Cdd:cd02697 214 ILNALYALNAQYRQVSSQVEGITHPYL----------NVG---------------RIEGGTNTNVVPGKVTFKLDRRMIP 268
|
250
....*....|....*..
gi 815845711 288 EYDNVAIEKLFKDTVKE 304
Cdd:cd02697 269 EENPVEVEAEIRRVIAD 285
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
53-225 |
9.61e-16 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 78.27 E-value: 9.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 53 RANLVAEI-GEGKPKIA--ISGHMDVVDAgDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKG 129
Cdd:cd08012 64 RGNIIVEYpGTVDGKTVsfVGSHMDVVTA-NPETWEFDPFSLSIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKR 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 130 TIRLMATAAEEKEM---SGAQLFKEQGYVNDL-DGMII-AEPSDGFAFYATKGSMGLKVTSKGIPAHSSLPslgHNAINS 204
Cdd:cd08012 143 TVVAVFIANEENSEipgVGVDALVKSGLLDNLkSGPLYwVDSADSQPCIGTGGMVTWKLTATGKLFHSGLP---HKAINA 219
|
170 180
....*....|....*....|....*..
gi 815845711 205 L------IAFIQriKEKYVEIKKNEKE 225
Cdd:cd08012 220 LelvmeaLAEIQ--KRFYIDFPPHPKE 244
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
63-315 |
1.43e-14 |
|
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: 74.44 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 63 GKPKIAISGHMDVVDAGDynewkyDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEK- 141
Cdd:cd03896 53 GGPALLFSAHLDTVFPGD------TPATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEGl 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 142 -EMSGAQ-LFKEQGYVndLDGMIIAEPSDGFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIKEKYVei 219
Cdd:cd03896 127 gDLRGARyLLSAHGAR--LDYFVVAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAA-- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 220 kknekehsldvhPYIDecireqghyndgdlKEDVAAGlvivnsIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFK 299
Cdd:cd03896 203 ------------PYVP--------------KTTFAAI------RGGGGTSVNRIANLCSMYLDIRSNPDAELADVQREVE 250
|
250
....*....|....*...
gi 815845711 300 DTVKEI--DSERLSVEVT 315
Cdd:cd03896 251 AVVSKLaaKHLRVKARVK 268
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
11-380 |
4.88e-14 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 72.51 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 11 KILADIVEINTENDNELEVCNYFKALLNKYDIDSKIIKVDNrranlvaEIGEGKPKIAISGHMDVVDAgdYNEWKydpfk 90
Cdd:PRK00466 14 ELLLDLLSIYTPSGNETNATKFFEKISNELNLKLEILPDSN-------SFILGEGDILLASHVDTVPG--YIEPK----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 91 ltEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRlqkgTIRLMATAAEEKEMSGAQLFKEQGYvnDLDGMIIAEPSDGF 170
Cdd:PRK00466 80 --IEGEVIYGRGAVDAKGPLISMIIAAWLLNEKGI----KVMVSGLADEESTSIGAKELVSKGF--NFKHIIVGEPSNGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 171 AFYAT-KGSMGLKVTSKGIPAHSSlpslghNAINSLIafiqrikekyveikknekehsLDVHPYIDECIREQGHYNDGDl 249
Cdd:PRK00466 152 DIVVEyRGSIQLDIMCEGTPEHSS------SAKSNLI---------------------VDISKKIIEVYKQPENYDKPS- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 250 kedvaaglvIVNSIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEID----SERLSVEVTVNHPTVYThk 325
Cdd:PRK00466 204 ---------IVPTIIRAGESYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQECGlkivDETPPVKVSINNPVVKA-- 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 815845711 326 dnrLINTFLEYNHDFKVSGMVGATDAAELlgdKDEDFDLAIIGPGHITLAHQTDE 380
Cdd:PRK00466 273 ---LMRALLKQNIKPRLVRKAGTSDMNIL---QKITTSIATYGPGNSMLEHTNQE 321
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
58-213 |
5.26e-14 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 73.34 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 58 AEIGEGKPKIAISGHMDVVDAGDynEWKYDPFKLTEEDDKLYGRGTTDMKG-GLAALiIAMIEIKESGRLQKGTIRLMAT 136
Cdd:PRK07318 73 IEYGEGEEVLGILGHLDVVPAGD--GWDTDPYEPVIKDGKIYARGTSDDKGpTMAAY-YALKIIKELGLPLSKKVRFIVG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 137 AAEEKEMSGAQ-LFK--------------------EQG----YVNDLDG------------------MI---------IA 164
Cdd:PRK07318 150 TDEESGWKCMDyYFEheeapdfgfspdaefpiingEKGittfDLVHFEGenegdyvlvsfksglrenMVpdsaeavitGD 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815845711 165 EPSD------------GFAFYATKGSMGLKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIK 213
Cdd:PRK07318 230 DLDDliaafeaflaenGLKGELEEEGGKLVLTVIGKSAHGSTPEKGVNAATYLAKFLNQLN 290
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
55-382 |
1.37e-13 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 71.59 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 55 NLVAEI-GEGKPKIAISGHMDVV-DAGDYNEwkyDPFKltEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIR 132
Cdd:PRK06133 89 MVVATFkGTGKRRIMLIAHMDTVyLPGMLAK---QPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 133 LMATAAEEKEMSG-----AQLFKEQGYVNDLDGmiiAEPSDGFAFyATKGSMGLKVTSKGIPAHS-SLPSLGHNAINSLI 206
Cdd:PRK06133 164 VLFNPDEETGSPGsreliAELAAQHDVVFSCEP---GRAKDALTL-ATSGIATALLEVKGKASHAgAAPELGRNALYELA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 207 AFIQRIKekyveikknekehsldvhpyidecireqghyndgDLKeDVAAGLVIVNSIIRGGEQFNTVPESAYAEFNIR-T 285
Cdd:PRK06133 240 HQLLQLR----------------------------------DLG-DPAKGTTLNWTVAKAGTNRNVIPASASAQADVRyL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 286 VPEydnvAIEKLFKDtVKEIDSERL--SVEVTVNH-----PTVYTHKDNRLINT----FLEYNHDFKVSGMV--GATDAA 352
Cdd:PRK06133 285 DPA----EFDRLEAD-LQEKVKNKLvpDTEVTLRFergrpPLEANAASRALAEHaqgiYGELGRRLEPIDMGtgGGTDAA 359
|
330 340 350
....*....|....*....|....*....|....*
gi 815845711 353 eLLGDKD-----EDFDLAiiGPGhitlAHQTDEYV 382
Cdd:PRK06133 360 -FAAGSGkaavlEGFGLV--GFG----AHSNDEYI 387
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
7-316 |
1.73e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 71.71 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 7 EDKIKILADIVEINT---ENDNELEVCNYFKALLNKYDIDSKIIKvdnRRANLV--AEIGEGKPK-IAISGHMDVVDAGD 80
Cdd:PRK06446 2 DEELYTLIEFLKKPSisaTGEGIEETANYLKDTMEKLGIKANIER---TKGHPVvyGEINVGAKKtLLIYNHYDVQPVDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 81 YNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLqKGTIRLMATAAEEKEMSGAQLFKEQgYVNDLDG 160
Cdd:PRK06446 79 LSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKHKL-NVNVKFLYEGEEEIGSPNLEDFIEK-NKNKLKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 161 -MIIAEPsdgfAFYATKG----SMGLK----------VTSKGIpaHSSLPSLGHN-------AINSLIAFIQRIK----- 213
Cdd:PRK06446 157 dSVIMEG----AGLDPKGrpqiVLGVKgllyvelvlrTGTKDL--HSSNAPIVRNpawdlvkLLSTLVDGEGRVLipgfy 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 214 EKYVEIKKNEKEHsLDVHPYIDECIREQ-GHYN-DGDLKEDVAAGLVI-----VNSIIRG--GEQFNT-VPESAYAEFNI 283
Cdd:PRK06446 231 DDVRELTEEEREL-LKKYDIDVEELRKAlGFKElKYSDREKIAEALLTeptcnIDGFYSGytGKGSKTiVPSRAFAKLDF 309
|
330 340 350
....*....|....*....|....*....|...
gi 815845711 284 RTVPEYDNvaiEKLFKDTVKEIDSERLSVEVTV 316
Cdd:PRK06446 310 RLVPNQDP---YKIFELLKKHLQKVGFNGEIIV 339
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
56-119 |
6.69e-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: 69.94 E-value: 6.69e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815845711 56 LVAEIGE--GKPKIAISGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAmIE 119
Cdd:cd05676 75 LLGRLGSdpSKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNA-IE 139
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
62-151 |
6.93e-13 |
|
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: 69.68 E-value: 6.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 62 EGKPK-IAISGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMataaEE 140
Cdd:cd05677 68 DAKRKrILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQEGELDNDVVFLI----EG 143
|
90
....*....|.
gi 815845711 141 KEMSGAQLFKE 151
Cdd:cd05677 144 EEESGSPGFKE 154
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
32-228 |
8.99e-13 |
|
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: 69.68 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 32 YFKAllNKYDIDSKIIKVDNRRANLVAEI---GEGKPKIAISGHMDVVDAGDYNEWK---YDPFKLTE------------ 93
Cdd:cd05654 38 YFKE--NPSHVWQLLPPDDLGRRNVTALVkgkKPSKRTIILISHFDTVGIEDYGELKdiaFDPDELTKafseyveeldee 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 94 --ED----DKLYGRGTTDMKGGLaALIIAMIEIKESGRLQKGTIRLMATAAEEKEMSGA--------QLFKEQGYvnDLD 159
Cdd:cd05654 116 vrEDllsgEWLFGRGTMDMKSGL-AVHLALLEQASEDEDFDGNLLLMAVPDEEVNSRGMraavpallELKKKHDL--EYK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 160 GMIIAEP-------SDGFAFYAtkGSMGlKVTS----KGIPAHSSLPSLGHNAiNSLIAFIQRIKEKYVEIK-KNEKEHS 227
Cdd:cd05654 193 LAINSEPifpqydgDQTRYIYT--GSIG-KILPgflcYGKETHVGEPFAGINA-NLMASEITARLELNADLCeKVEGEIT 268
|
.
gi 815845711 228 L 228
Cdd:cd05654 269 P 269
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
62-112 |
8.33e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 66.47 E-value: 8.33e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 815845711 62 EGKPKIAISGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAA 112
Cdd:PRK07907 81 PGAPTVLLYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAM 131
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
1-224 |
9.42e-12 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 66.42 E-value: 9.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 1 MSVFSEEDKIK-ILADIVEI----NTENDNELEV--------CNYFKA---LLNKYDIDSKIIKvdnrRANLVAEI-GEG 63
Cdd:COG4187 1 MKKWQTKEQLEeLLCELVSIpsvtGTEGEKEVAEfiyeklseLPYFQEnpeHLGLHPLPDDPLG----RKNVTALVkGKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 64 KPK--IAISGHMDVVDAGDYNEWK---YDPFKLTEE----------------DDKLYGRGTTDMKGGLaALIIAMIEIKE 122
Cdd:COG4187 77 ESKktVILISHFDVVDVEDYGSLKplaFDPEELTEAlkeiklpedvrkdlesGEWLFGRGTMDMKAGL-ALHLALLEEAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 123 SGRLQKGTIRLMATAAEEKEMSG--------AQLFKEQGYvnDLDGMIIAEPS-------DGFAFYatKGSMGlKVTS-- 185
Cdd:COG4187 156 ENEEFPGNLLLLAVPDEEVNSAGmraavpllAELKEKYGL--EYKLAINSEPSfpkypgdETRYIY--TGSIG-KLMPgf 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 815845711 186 --KGIPAHSSLPSLGHNAiNSLIAFIQRIKE---KYVEIKKNEK 224
Cdd:COG4187 231 ycYGKETHVGEPFSGLNA-NLLASELTRELElnpDFCEEVGGEV 273
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
63-398 |
1.47e-11 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 65.22 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 63 GKPKIAISGHMDVVDAGDYneWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEikesgrlQKGTIRLMATAAEEKE 142
Cdd:PRK08737 62 GTPKYLFNVHLDTVPDSPH--WSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANA-------GDGDAAFLFSSDEEAN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 143 MS-GAQLFKEQGYvnDLDGMIIAEPSDGFAFYATKGSMGLKVTSKGIPAHSSLP-SLGHNAINSLIAFIQRIKEkyveik 220
Cdd:PRK08737 133 DPrCVAAFLARGI--PYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKqDPSASALHQAMRWGGQALD------ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 221 knEKEHSLDVHPYIDECIReqghYNDGDlkedvaaglvivnsiIRGGEQFNTVPESAYAEFNIRTVPEYDnvaIEKLFKD 300
Cdd:PRK08737 205 --HVESLAHARFGGLTGLR----FNIGR---------------VEGGIKANMIAPAAELRFGFRPLPSMD---VDGLLAT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 301 TVKEIDSERLSVEVTVNHPTV----YTHKDNR-LINTFLEYNHDFKVSGMVGATDAAELLGDKdeDFDLAIIGPGHITLA 375
Cdd:PRK08737 261 FAGFAEPAAATFEETFRGPSLpsgdIARAEERrLAARDVADALDLPIGNAVDFWTEASLFSAA--GYTALVYGPGDIAQA 338
|
330 340
....*....|....*....|...
gi 815845711 376 HQTDEYVYKSRYLDYIDMYQQVI 398
Cdd:PRK08737 339 HTADEFVTLDQLQRYAESVHRII 361
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
5-213 |
6.86e-11 |
|
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: 63.24 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 5 SEEDKIKILADIVEINTENDNELEVCnyfKALLNKYDIDSKIIKVDNRRA-------NLVAEI---GEGKPKIAISGHMD 74
Cdd:cd05683 1 NEDRLINTFLELVQIDSETLHEKEIS---KVLKKKFENLGLSVIEDDAGKttgggagNLICTLkadKEEVPKILFTSHMD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 75 VVDAGDYNEwkydpfKLTEEDDKLYGRGTT----DMKGGLAALIIAMIEIKESgRLQKGTIRLMATAAEEKEMSGAQ--- 147
Cdd:cd05683 78 TVTPGINVK------PPQIADGYIYSDGTTilgaDDKAGIAAILEAIRVIKEK-NIPHGQIQFVITVGEESGLVGAKald 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 815845711 148 ---LFKEQGYVNDLDG----MIIAEPSdgfafyatkgSMGLKVTSKGIPAHSSL-PSLGHNAINSLIAFIQRIK 213
Cdd:cd05683 151 pelIDADYGYALDSEGdvgtIIVGAPT----------QDKINAKIYGKTAHAGTsPEKGISAINIAAKAISNMK 214
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
67-308 |
1.74e-10 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 62.29 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 67 IAISGHMDVVDAGDYnewkydPFKLTE--EDDKLYGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEE-KEM 143
Cdd:PRK07338 95 VLLTGHMDTVFPADH------PFQTLSwlDDGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLGYDVLINPDEEiGSP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 144 SGAQLFKEQGyvndlDGMIIA---EPS--DGFAFYATKGSMGLKVTSKGIPAHSSL-PSLGHNAINSLIAFIQRIkekyv 217
Cdd:PRK07338 169 ASAPLLAELA-----RGKHAAltyEPAlpDGTLAGARKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAELALAL----- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 218 eikknekeHSLDvhpyidecireqghyndgDLKEDVAaglviVN-SIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEK 296
Cdd:PRK07338 239 --------HALN------------------GQRDGVT-----VNvAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEA 287
|
250
....*....|..
gi 815845711 297 LFKDTVKEIDSE 308
Cdd:PRK07338 288 ELKKLIAQVNQR 299
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
61-318 |
1.16e-09 |
|
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: 59.63 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 61 GEGKPKIAISGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLAALIIAmIE--IKESGRLQKgTIRLMATAa 138
Cdd:cd05680 60 APGAPTVLVYGHYDVQPPDPLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKA-VEawLAVEGALPV-NVKFLIEG- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 139 eEKEMSGAQLFK---EQGYVNDLDGMIIaepSDGFAF--------YATKGSMGLKVTSKGipAHSSLPSlGH------NA 201
Cdd:cd05680 137 -EEEIGSPSLPAfleENAERLAADVVLV---SDTSMWspdtptitYGLRGLAYLEISVTG--PNRDLHS-GSyggavpNP 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 202 IN---SLIAFIQ----RIK-----EKYVEIKKNEKEhSLDVHPY----------IDECIREQGHyndGDLKEDVAAGLVI 259
Cdd:cd05680 210 ANalaRLLASLHdedgRVAipgfyDDVRPLTDAERE-AWAALPFdeaafkaslgVPALGGEAGY---TTLERLWARPTLD 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815845711 260 VNSIIRG--GEQFNTV-PESAYAEFNIRTVPEYDNVAIEKLFKDTVKEIDSERLSVEVTVNH 318
Cdd:cd05680 286 VNGIWGGyqGEGSKTViPSKAHAKISMRLVPGQDPDAIADLLEAHLRAHAPPGVTLSVKPLH 347
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
36-113 |
1.20e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 59.93 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 36 LLNKYDIDSKIikVDNRRAN----LVAEIGEGK--PKIAISGHMDVVDaGDYNEWK--YDPFKLTEEDDKLYGRGTTDMK 107
Cdd:PRK07079 53 ALAALGFTCRI--VDNPVAGggpfLIAERIEDDalPTVLIYGHGDVVR-GYDEQWRegLSPWTLTEEGDRWYGRGTADNK 129
|
90
....*....|
gi 815845711 108 G----GLAAL 113
Cdd:PRK07079 130 GqhtiNLAAL 139
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
56-316 |
1.43e-09 |
|
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: 59.22 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 56 LVAEIGEGKPK--IAISGHMDVVDAGDYNEWKydpfklteeddklyGRGTTDMKGGLAALIIAMIEIKESGRLQKGTIRL 133
Cdd:cd08018 50 VVAEIGSGKPGpvVALRADMDALWQEVDGEFK--------------ANHSCGHDAHMTMVLGAAELLKKIGLVKKGKLKF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 134 MATAAEEKeMSGAQLFKEQGYVNDLDGMI------IAEPSDGFAFYATK--GSMGLKVTSKGIPAHSSLPSLGHNAINSL 205
Cdd:cd08018 116 LFQPAEEK-GTGALKMIEDGVLDDVDYLFgvhlrpIQELPFGTAAPAIYhgASTFLEGTIKGKQAHGARPHLGINAIEAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 206 IAFIQRIKekyvEIKKN-EKEHSldvhpyidecireqghyndgdlkedvaaglVIVNSIIRGGEQFNTVPESAYAEFNIR 284
Cdd:cd08018 195 SAIVNAVN----AIHLDpNIPWS------------------------------VKMTKLQAGGEATNIIPDKAKFALDLR 240
|
250 260 270
....*....|....*....|....*....|..
gi 815845711 285 TvpeYDNVAIEKLFKDTVKEIDSERLSVEVTV 316
Cdd:cd08018 241 A---QSNEAMEELKEKVEHAIEAAAALYGASI 269
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
26-402 |
9.43e-09 |
|
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: 56.58 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 26 ELEVCNYFKALLNKYDIDskIIKVDNrrANLVAEIGEGKPK--IAISGHMDVVDAGDYNEWKYDpfklTEEDDKLYGRGt 103
Cdd:cd08019 18 EERTSKRIKEELDKLGIP--YVETGG--TGVIATIKGGKAGktVALRADIDALPVEECTDLEYK----SKNPGLMHACG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 104 tdMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEKEMsGAQLFKEQGYVNDLD-------------GMIIAEPSDGF 170
Cdd:cd08019 89 --HDGHTAMLLGAAKILNEIKDTIKGTVKLIFQPAEEVGE-GAKQMIEEGVLEDVDavfgihlwsdvpaGKISVEAGPRM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 171 AfyatkGSMGLKVTSKGIPAHSSLPSLGHNAI---NSLIAFIQRIKEKYVeikknekehsldvhpyidecireqghyndg 247
Cdd:cd08019 166 A-----SADIFKIEVKGKGGHGSMPHQGIDAVlaaASIVMNLQSIVSREI------------------------------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 248 dlkeDVAAGLVIVNSIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEI-DSERLSVEVTVNHPTVYTHKD 326
Cdd:cd08019 211 ----DPLEPVVVTVGKLNSGTRFNVIADEAKIEGTLRTFNPETREKTPEIIERIAKHTaASYGAEAELTYGAATPPVIND 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 327 NRLinTFLEYNHDFKVSGMVGATDAAELLGdkDEDFD---------LAIIGPGH----ITLAHQTDEYVYKSRYLDY-ID 392
Cdd:cd08019 287 EKL--SKIARQAAIKIFGEDSLTEFEKTTG--SEDFSyyleevpgvFAFVGSRNeekgATYPHHHEFFNIDEDALKLgAA 362
|
410
....*....|
gi 815845711 393 MYQQVILNYL 402
Cdd:cd08019 363 LYVQFALDFL 372
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
62-294 |
2.64e-08 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 55.52 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 62 EGKPKIAISGHMDVVDAGDYNEWKYDPFKLTEEDDKLYGRGTTDMKGGLaALIIAMIE--IKESGRLQKgTIRLMATAAE 139
Cdd:PRK08201 77 PGKPTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQV-FMHLKAVEalLKVEGTLPV-NVKFCIEGEE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 140 EKEMSGAQLFKEQgYVNDL--DGMIIA-----EPSDGFAFYATKGSMGLKVTSKGIPA--HSSLPSLG-HNAINSLIAFI 209
Cdd:PRK08201 155 EIGSPNLDSFVEE-EKDKLaaDVVLISdttllGPGKPAICYGLRGLAALEIDVRGAKGdlHSGLYGGAvPNALHALVQLL 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 210 QRIKEKYVEIK-KNEKEHSLDVHPYIDECIREQGHyNDGDLKEDVAAGLVI------------------VNSIIRG--GE 268
Cdd:PRK08201 234 ASLHDEHGTVAvEGFYDGVRPLTPEEREEFAALGF-DEEKLKRELGVDELFgeegytalertwarptleLNGVYGGfqGE 312
|
250 260
....*....|....*....|....*..
gi 815845711 269 QFNTV-PESAYAEFNIRTVPEYDNVAI 294
Cdd:PRK08201 313 GTKTViPAEAHAKITCRLVPDQDPQEI 339
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
56-355 |
6.92e-08 |
|
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: 53.89 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 56 LVAEIGEGKPK--IAISGHMDVVDAGDYNEWkydPFKLTEeDDKLYGRG----TTdmkgglAALIIAMIeIKESGRLQKG 129
Cdd:TIGR01891 46 VVATIGGGKPGpvVALRADMDALPIQEQTDL---PYKSTN-PGVMHACGhdlhTA------ILLGTAKL-LKKLADLLEG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 130 TIRLMATAAEEKeMSGAQLFKEQGYVNDLDGMIIAEPsdgFAFYATkGSMGL------------KVTSKGIPAHSSLPsl 197
Cdd:TIGR01891 115 TVRLIFQPAEEG-GGGATKMIEDGVLDDVDAILGLHP---DPSIPA-GTVGLrpgtimaaadkfEVTIHGKGAHAARP-- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 198 gHNAINSLIAFIQRIKEKYVEIkknekEHSLdvhpyidecireqghyndgdlkeDVAAGLVIVNSIIRGGEQFNTVPESA 277
Cdd:TIGR01891 188 -HLGRDALDAAAQLVVALQQIV-----SRNV-----------------------DPSRPAVVSVGIIEAGGAPNVIPDKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 278 YAEFNIRTVPEYDNVAIEKLFKDTVK----------EIDSERlSVEVTVNHPTVYTH--KDNRLINTFLEYNHDFKVSgm 345
Cdd:TIGR01891 239 SMSGTVRSLDPEVRDQIIDRIERIVEgaaamygakvELNYDR-GLPAVTNDPALTQIlkEVARHVVGPENVAEDPEVT-- 315
|
330
....*....|
gi 815845711 346 VGATDAAELL 355
Cdd:TIGR01891 316 MGSEDFAYYS 325
|
|
| M20_Acy1L2 |
cd03887 |
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
108-285 |
3.57e-07 |
|
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: 51.81 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 108 GGLAALIiAMIE-IKESGrlQKGTIRLMATAAEEKEmSGAQLFKEQGYVNDLDGMIIAEPSD-GFAFYATKGSMGLKVTS 185
Cdd:cd03887 90 ASVAAAL-ALKAaLKALG--LPGTVVVLGTPAEEGG-GGKIDLIKAGAFDDVDIALMVHPGPkDVAGPKSLAVSKLRVEF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 186 KGIPAHSSL-PSLGHNAINSLIAFIQRIkekyveikknekehSLdvhpyidecIREQghyndgdLKEDvaaglVIVNSII 264
Cdd:cd03887 166 HGKAAHAAAaPWEGINALDAAVLAYNNI--------------SA---------LRQQ-------LKPT-----VRVHGII 210
|
170 180
....*....|....*....|..
gi 815845711 265 R-GGEQFNTVPESAYAEFNIRT 285
Cdd:cd03887 211 TeGGKAPNIIPDYAEAEFYVRA 232
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
13-149 |
4.40e-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: 349928 [Multi-domain] Cd Length: 448 Bit Score: 51.73 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 13 LADIVEINTENDNELEVCNYFKAL-------LNKYDIDSKIIK--VDNRRANLVAEIGEGK--PKIAISGHMDVVDaGDY 81
Cdd:cd05679 10 LARRVAVPTESQEPARKPELRAYLdqemrprFERLGFTVHIHDnpVAGRAPFLIAERIEDPslPTLLIYGHGDVVP-GYE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 82 NEWK--YDPFKLTEEDDKLYGRGTTDMKGGLAALIIAMIEIKES--GRL------------QKGTIRLMATAAEEKEMSG 145
Cdd:cd05679 89 GRWRdgRDPWTVTVWGERWYGRGTADNKGQHSINMAALRQVLEArgGKLgfnvkfliemgeEMGSPGLRAFCFSHREALK 168
|
....
gi 815845711 146 AQLF 149
Cdd:cd05679 169 ADLF 172
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
111-320 |
8.50e-06 |
|
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: 47.42 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 111 AALIIAMIEIKESGRLQKGTIRLMATAAEEKeMSGAQLFKEQGYVNDLD-GMIIA------EPSDGFAF---YATKGSMG 180
Cdd:COG1473 107 AMLLGAAKALAELRDELKGTVRLIFQPAEEG-GGGAKAMIEDGLLDRPDvDAIFGlhvwpgLPVGTIGVrpgPIMAAADS 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 181 LKVTSKGIPAHSSLPSLGHNAINSLIAFIQRIkekyveikknekehsldvhPYIdeCIREQghyndgdlkeDVAAGLVIV 260
Cdd:COG1473 186 FEITIKGKGGHAAAPHLGIDPIVAAAQIVTAL-------------------QTI--VSRNV----------DPLDPAVVT 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815845711 261 NSIIRGGEQFNTVPESAYAEFNIRTVPEYDNVAIEKLFKDTVKEI-DSERLSVEV--------TVNHPT 320
Cdd:COG1473 235 VGIIHGGTAPNVIPDEAELEGTVRTFDPEVRELLEERIERIAEGIaAAYGATAEVeylrgyppTVNDPE 303
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
10-285 |
1.55e-05 |
|
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1L2 family contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.
Pssm-ID: 349945 [Multi-domain] Cd Length: 366 Bit Score: 46.46 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 10 IKILADIVEINTENDNELEVCNYFKALLNKYDIdsKIIKVDNRRANLVAEI--GEGKPKIAISGHMDVVDAGDYNEWkyd 87
Cdd:cd08660 2 INIRRDIHEHPELGFEEVETSKKIRRWLEEEQI--EILDVPQLKTGVIAEIkgGEDGPVIAIRADIDALPIQEQTNL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 88 PFKlTEEDDKLYGRGttdMKGGLAALIIAMIEIKESGRLQKGTIRLMATAAEEKeMSGAQLFKEQGYVNDLDGMIIAEPS 167
Cdd:cd08660 77 PFA-SKVDGT*HACG---HDFHTTSIIGTA*LLNQRRAELKGTVVFIFQPAEEG-AAGARKVLEAGVLNGVSAIFGIHNK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 168 DGFAF--YATKGSMG------LKVTSKGIPAHSSLPSLGHNAIN---SLIAFIQRIKEKYVEIKKNEkehsldvhpyide 236
Cdd:cd08660 152 PDLPVgtIGVKEGPL*asvdvFEIVIKGKGGHASIPNNSIDPIAaagQIISGLQSVVSRNISSLQNA------------- 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 815845711 237 cireqghyndgdlkedvaaglVIVNSIIRGGEQFNTVPESAYAEFNIRT 285
Cdd:cd08660 219 ---------------------VVSITRVQGGTAWNVIPDQAE*EGTVRA 246
|
|
| M20_ACY1L2-like |
cd05672 |
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 ... |
111-285 |
6.91e-05 |
|
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like 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. This subfamily includes Staphylococcus aureus antibiotic resistance factor HmrA that has been shown to participate in methicillin resistance mechanisms in vivo in the presence of beta-lactams. 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: 349921 [Multi-domain] Cd Length: 360 Bit Score: 44.48 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 111 AALIIAMIeIKESGrlQKGTIRLMATAAEEKEmSGAQLFKEQGYVNDLDGMIIAEPSD-GFAFYATKGSMGLKVTSKGIP 189
Cdd:cd05672 94 AALALKEA-LKALG--LPGKVVVLGTPAEEGG-GGKIDLIKAGAFDDVDAALMVHPGPrDVAGVPSLAVDKLTVEFHGKS 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 190 AHSSL-PSLGHNAINSLIAFiqrikekYVEIkknekehsldvhpyidECIREQghyndgdLKEDvaaglVIVNSIIR-GG 267
Cdd:cd05672 170 AHAAAaPWEGINALDAAVLA-------YNAI----------------SALRQQ-------LKPT-----WRIHGIITeGG 214
|
170
....*....|....*...
gi 815845711 268 EQFNTVPESAYAEFNIRT 285
Cdd:cd05672 215 KAPNIIPDYAEARFYVRA 232
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
26-333 |
1.06e-04 |
|
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: 44.21 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 26 ELEVCNYFKALLNKYDIdsKIIKVDnRRANLVAEIGEGKPKIAISGHmdvVDAGDYNEWKYDPFKlTEEDDKLYGRG--- 102
Cdd:cd05669 23 EFETTKKIRRWLEEKGI--RILDLP-LKTGVVAEIGGGGPIIALRAD---IDALPIEEETGLPYA-SQNKGVMHACGhdf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 103 -TTDMKGglAALIIAMIEikesGRLqKGTIRLMATAAEEKEmSGAQLFKEQGYVNDLDGMIiaepsdGF----------- 170
Cdd:cd05669 96 hTASLLG--AAVLLKERE----AEL-KGTVRLIFQPAEETG-AGAKKVIEAGALDDVSAIF------GFhnkpdlpvgti 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 171 -----AFYATKGSMGLKVTSKGipAHSSLPSLGHNAI---NSLIAFIQRIKekyveikknekehSLDVHPYiDECIREQG 242
Cdd:cd05669 162 glksgALMAAVDRFEIEIAGKG--AHAAKPENGVDPIvaaSQIINALQTIV-------------SRNISPL-ESAVVSVT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 243 HyndgdlkedvaaglvivnsiIRGGEQFNTVPESAYAEFNIRTvpeYDNVA---IEKLFKDTVKEIdSERLSVEVTVNhp 319
Cdd:cd05669 226 R--------------------IHAGNTWNVIPDSAELEGTVRT---FDAEVrqlVKERFEQIVEGI-AAAFGAKIEFK-- 279
|
330
....*....|....
gi 815845711 320 tvYTHKDNRLINTF 333
Cdd:cd05669 280 --WHSGPPAVINDE 291
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
62-147 |
1.18e-04 |
|
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.
Pssm-ID: 349885 [Multi-domain] Cd Length: 474 Bit Score: 44.05 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 62 EGKPKIAISGHMDVV---DAGDYNEWKYDPFKLTEEDDKLYGRGTT---DMKGGLAaliiAMIEIKESGRLQKGTIRLMA 135
Cdd:cd03890 58 ENAPPVILQGHMDMVcekNADSEHDFEKDPIKLRIDGDWLKATGTTlgaDNGIGVA----YALAILEDKDIEHPPLEVLF 133
|
90
....*....|..
gi 815845711 136 TAAEEKEMSGAQ 147
Cdd:cd03890 134 TVDEETGMTGAL 145
|
|
| M28_Pgcp_like |
cd03883 |
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate ... |
55-179 |
6.57e-04 |
|
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate carboxypeptidase (PGCP; blood plasma glutamate carboxypeptidase; EC 3.4.17.21) subfamily. PGCP is a 56kDa glutamate carboxypeptidase that is mainly produced in mammalian placenta and kidney, the majority of which is thought to be secreted into the bloodstream. Similar proteins are also found in other species, including bacteria. These proteins contain protease-associated (PA) domain inserts between the first and second strands of the central beta sheet in the protease-like domain. The PA domains may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. The exact physiological substrates of PGCP are unknown, although this enzyme may play an important role in the hydrolysis of circulating peptides. Its closest homolog encodes an important brain glutamate carboxypeptidase II (NAALADase) identical to the prostate-specific membrane antigen (PSMA), which serves as a marker for prostatic cancer metastasis. Hypermethylation of PGCP gene has been associated with human bronchial epithelial (HBE) cell immortalization and lung cancer. PGCP also provides an attractive target for serological analysis in hepatitis C virus (HCV)-induced hepatocellular carcinoma (HCC) patients.
Pssm-ID: 349879 [Multi-domain] Cd Length: 425 Bit Score: 41.53 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 55 NLVAEI-GEGKPK--IAISGHMDVVDAGDynewkydpfklteeddklygrGTTDMKGGLAALIIAMIEIKESGRLQKGTI 131
Cdd:cd03883 228 NVIAEItGSKYPDevVLVGGHLDSWDVGT---------------------GAMDDGGGVAISWEALKLIKDLGLKPKRTI 286
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 815845711 132 RLMATAAEEKEMSGAQLFKEQgYVNDLDGMIIAEPSD-------GFAFYATKGSM 179
Cdd:cd03883 287 RVVLWTGEEQGLVGAKAYAEA-HKDELENHVFAMESDigtftpyGLQFTGSDTAR 340
|
|
| M20_Acy1L2_AbgB |
cd05673 |
M20 Peptidase Aminoacylase 1-like protein 2 aminobenzoyl-glutamate utilization protein B ... |
56-205 |
7.58e-04 |
|
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: 41.52 E-value: 7.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 56 LVAEIGEGKPKIAISGHMDVVdAG---DYNEWKYDPFklteEDDKlYGRGTTDMKGGLAAL--IIAMIE-IKESGrlQKG 129
Cdd:cd05673 54 FVASYGSGGPVIAILGEYDAL-PGlsqEAGVAERKPV----EPGA-NGHGCGHNLLGTGSLgaAIAVKDyMEENN--LAG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815845711 130 TIRLMATAAEEkEMSGAQLFKEQGYVNDLDGMIIAEPsdgFAFYATKGSMGLKVTS-----KGIPAH-SSLPSLGHNAIN 203
Cdd:cd05673 126 TVRFYGCPAEE-GGSGKTFMVRDGVFDDVDAAISWHP---ASFNGVWSTSSLANISvkfkfKGISAHaAAAPHLGRSALD 201
|
..
gi 815845711 204 SL 205
Cdd:cd05673 202 AV 203
|
|
| |
