|
Name |
Accession |
Description |
Interval |
E-value |
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
4-383 |
1.15e-85 |
|
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: 265.21 E-value: 1.15e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 4 DTLEQRAVLWTQALVRVPSVSGSpaCLQVLETARDLIESTGVEADIRILFPEAPNpVLLARTGRGKAGVteLMLSGHVDV 83
Cdd:COG0624 8 DAHLDEALELLRELVRIPSVSGE--EAAAAELLAELLEALGFEVERLEVPPGRPN-LVARRPGDGGGPT--LLLYGHLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 84 VPPAGME----DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVD--GVLWLILSTDEETAAQGVVRAL-SCSD 156
Cdd:COG0624 83 VPPGDLElwtsDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRlpGNVTLLFTGDEEVGSPGARALVeELAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 157 APRPQLCVICEPTGLC-VRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAkKRLPELLAGNAAAGPASSSI 235
Cdd:COG0624 163 GLKADAAIVGEPTGVPtIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAAL-RDLEFDGRADPLFGRTTLNV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 236 DLVSGGAAENVVPASASVTIDFRY-QGVESAQVQcDRIEKILSEVRTDPDfppVSTSLtVTGDWTALSTDMTQPLAQAAV 314
Cdd:COG0624 242 TGIEGGTAVNVIPDEAEAKVDIRLlPGEDPEEVL-AALRALLAAAAPGVE---VEVEV-LGDGRPPFETPPDSPLVAAAR 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 315 AALGESLGHIPETTEMTGWGEGGSMQK-FGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKALFHLVDRL 383
Cdd:COG0624 317 AAIREVTGKEPVLSGVGGGTDARFFAEaLGIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERL 386
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
14-376 |
2.96e-71 |
|
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: 227.18 E-value: 2.96e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 14 TQALVRVPSVSgsPACLQVLETARDLIESTGVEADiRILFPEAPNPVLLARTGRGKagvtELMLSGHVDVVPPAGME--- 90
Cdd:cd08659 3 LQDLVQIPSVN--PPEAEVAEYLAELLAKRGYGIE-STIVEGRGNLVATVGGGDGP----VLLLNGHIDTVPPGDGDkws 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 91 -DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGV--DGVLWLILSTDEETAAQGVVRALSCSDAPRPQLCVICE 167
Cdd:cd08659 76 fPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGAllGGRVALLATVDEEVGSDGARALLEAGYADRLDALIVGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 168 PTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAkKRLPELLAGNAAAGPASSSIDLVSGGAAENVV 247
Cdd:cd08659 156 PTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAEL-RTLFEELPAHPLLGPPTLNVGVINGGTQVNSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 248 PASASVTIDFRYQGVESAQVQCDRIEKILSEVrtdpdfpPVSTSLTVTGDWTALS-TDMTQPLAQAAVAALGEsLGHIPE 326
Cdd:cd08659 235 PDEATLRVDIRLVPGETNEGVIARLEAILEEH-------EAKLTVEVSLDGDPPFfTDPDHPLVQALQAAARA-LGGDPV 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1821508169 327 TTEMTGWGEGGSMQKF-GIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKAL 376
Cdd:cd08659 307 VRPFTGTTDASYFAKDlGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIY 357
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
13-381 |
3.26e-64 |
|
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: 209.37 E-value: 3.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 13 WTQALVRVPSVSGSPAcLQVLETARDLIESTGVEADiRILFPEAPNPVLLARTGRGKAGVteLMLSGHVDVVPPAGME-- 90
Cdd:cd03894 2 LLARLVAFDTVSRNSN-LALIEYVADYLAALGVKSR-RVPVPEGGKANLLATLGPGGEGG--LLLSGHTDVVPVDGQKws 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 91 -DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVDGVLWLILSTDEETAAQGV---VRALScSDAPRPQLCVIC 166
Cdd:cd03894 78 sDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVrhlIAALA-ARGGRPDAAIVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 167 EPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAKKRLPELLAGNAAAG---PASS-SIDLVSGGA 242
Cdd:cd03894 157 EPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGLRDPPfdpPYPTlNVGLIHGGN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 243 AENVVPASASVTIDFRY-QGVESAQVQcdriEKILSEVRTDPDFPPVSTSLTVTGDWTALSTDMTQPLAQAAVAALGEsl 321
Cdd:cd03894 237 AVNIVPAECEFEFEFRPlPGEDPEAID----ARLRDYAEALLEFPEAGIEVEPLFEVPGLETDEDAPLVRLAAALAGD-- 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 322 gHIPETTemTGWGEGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKALFHLVD 381
Cdd:cd03894 311 -NKVRTV--AYGTEAGLFQRAGIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
17-386 |
5.05e-58 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 194.05 E-value: 5.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 17 LVRVPSVSgsPACLQVLETA---RDLIESTGVEADIrILFPE-------APNPVLLARTGRGKagvTELMLSGHVDVVPP 86
Cdd:PRK08651 15 LIKIPTVN--PPGENYEEIAeflRDTLEELGFSTEI-IEVPNeyvkkhdGPRPNLIARRGSGN---PHLHFNGHYDVVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 87 AGME---DPWSARIEGDRMHGRGTTDMKSGAACALTTFcEAARQGVDGVLWLILSTDEETAAQGVvRALSCSDAPRPQLC 163
Cdd:PRK08651 89 GEGWsvnVPFEPKVKDGKVYGRGASDMKGGIAALLAAF-ERLDPAGDGNIELAIVPDEETGGTGT-GYLVEEGKVTPDYV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 164 VICEPTGL---CVrsAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAA---ALFIVHAKKRLPELLAGNAAAGpASSSIDL 237
Cdd:PRK08651 167 IVGEPSGLdniCI--GHRGLVWGVVKVYGKQAHASTPWLGINAFEAAakiAERLKSSLSTIKSKYEYDDERG-AKPTVTL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 238 ----VSGGAAENVVPASASVTIDFRYQGVESAQVQCDRIEKILSEVRtdPDFPpVSTSLTVTGDWTALSTDMTQPLAQAA 313
Cdd:PRK08651 244 ggptVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVA--PELG-IEVEFEITPFSEAFVTDPDSELVKAL 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821508169 314 VAALGESLGHIPETTEMTGWGEGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKALFHLVDRLVVH 386
Cdd:PRK08651 321 REAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVLKRLAKG 393
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
13-369 |
1.06e-56 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 190.02 E-value: 1.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 13 WTQALVRVPSVSGSPAcLQVLETARDLIESTGVEADiRILFPEAPNPVLLARTG-RGKAGVtelMLSGHVDVVPPAGME- 90
Cdd:PRK07522 9 ILERLVAFDTVSRDSN-LALIEWVRDYLAAHGVESE-LIPDPEGDKANLFATIGpADRGGI---VLSGHTDVVPVDGQAw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 91 --DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVDGVLWLILSTDEETAAQGV------VRALscsdAPRPQL 162
Cdd:PRK07522 84 tsDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVpsmiarLPER----GVKPAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 163 CVICEPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAkKRLPELLAGNAAAGPA------SSSID 236
Cdd:PRK07522 160 CIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHL-RDLADRLAAPGPFDALfdppysTLQTG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 237 LVSGGAAENVVPASASVTIDFRY-QGVESAQVQcDRIEK-----ILSEVRTdpDFPPVSTSLTVTGDWTALSTDMTQPLA 310
Cdd:PRK07522 239 TIQGGTALNIVPAECEFDFEFRNlPGDDPEAIL-ARIRAyaeaeLLPEMRA--VHPEAAIEFEPLSAYPGLDTAEDAAAA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 311 QAAVAALG-ESLGHIPETTemtgwgEGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEI 369
Cdd:PRK07522 316 RLVRALTGdNDLRKVAYGT------EAGLFQRAGIPTVVCGPGSIEQAHKPDEFVELAQL 369
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
16-370 |
1.33e-51 |
|
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: 176.16 E-value: 1.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 16 ALVRVPSVSGSPAcLQVLETARDLIESTGVEADiRILFPEAPNPVLLARTgRGKAGVTELMLSGHVDVVPPAG---MEDP 92
Cdd:TIGR01892 5 KLVAFDSTSFRPN-VDLIDWAQAYLEALGFSVE-VQPFPDGAEKSNLVAV-IGPSGAGGLALSGHTDVVPYDDaawTRDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 93 WSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVDGVLWLILSTDEETAAQGVvRALSCSDAPRPQLCVICEPTGLC 172
Cdd:TIGR01892 82 FRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGA-PKMIEAGAGRPRHAIIGEPTRLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 173 VRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAKKRLPELLAG--NAAAGPASSSIDL--VSGGAAENVVP 248
Cdd:TIGR01892 161 PVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREdlDEGFTPPYTTLNIgvIQGGKAVNIIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 249 ASASVTIDFR-YQGVESAQVQCDrIEKILSEV-RTDPDFPPVstsltvtgdWTALSTD---MTQPLAQaAVAALGESLGH 323
Cdd:TIGR01892 241 GACEFVFEWRpIPGMDPEELLQL-LETIAQALvRDEPGFEVQ---------IEVVSTDpgvNTEPDAE-LVAFLEELSGN 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1821508169 324 IPETTEMTgwGEGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEIK 370
Cdd:TIGR01892 310 APEVVSYG--TEAPQFQELGAEAVVCGPGDIRQAHQPDEYVEIEDLV 354
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
76-382 |
1.35e-51 |
|
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: 174.84 E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 76 MLSGHVDVVPPAGMED-PWSARIEGdRMHGRGTTDMKSGAACALTTFCEAARQGVD-GVLWLILSTDEETAAQGV--VRA 151
Cdd:pfam01546 1 LLRGHMDVVPDEETWGwPFKSTEDG-KLYGRGHDDMKGGLLAALEALRALKEEGLKkGTVKLLFQPDEEGGMGGAraLIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 152 LSCSDAPRPQLCV---ICEPTGL------CVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAKKRLPELL 222
Cdd:pfam01546 80 DGLLEREKVDAVFglhIGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSRNV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 223 AGNAAAGPASSSIDLVSGGAaeNVVPASASVTIDFRYQGVESAQVQCDRIEKILSEVrTDPDFPPVSTSLTVTGDWTALS 302
Cdd:pfam01546 160 DPLDPAVVTVGNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAI-AAAYGVKVEVEYVEGGAPPLVN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 303 TDmtqPLAQAAVAALGESLG--HIPETTEMTGWGEGGSMQKfGIPA--FYFGPGDGpLAHTPKESVSVSEIKTAVKALFH 378
Cdd:pfam01546 237 DS---PLVAALREAAKELFGlkVELIVSGSMGGTDAAFFLL-GVPPtvVFFGPGSG-LAHSPNEYVDLDDLEKGAKVLAR 311
|
....
gi 1821508169 379 LVDR 382
Cdd:pfam01546 312 LLLK 315
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
14-380 |
4.86e-46 |
|
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: 161.88 E-value: 4.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 14 TQALVRV----PSVSGSPAC--LQVLETARDLIESTGVEADIRILFPEAPNPVLLAR-TGRGKAgvteLMLSGHVDVVPP 86
Cdd:cd08013 7 TQTLVRInssnPSLSATGGAgeAEIATYVAAWLAHRGIEAHRIEGTPGRPSVVGVVRgTGGGKS----LMLNGHIDTVTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 87 AGME-DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVDGVLWLILSTDEETAAQG---VVRALSCSDAprpql 162
Cdd:cd08013 83 DGYDgDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGLRGDVILAAVADEEDASLGtqeVLAAGWRADA----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 163 CVICEPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAK---KRLPElLAGNAAAGPASSSIDLVS 239
Cdd:cd08013 158 AIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALEeyqQELPE-RPVDPLLGRASVHASLIK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 240 GGAAENVVPASASVTIDFRYQGVESAQVQCDRIEKILSEV-RTDPDFPPVSTSLTVTGDWTALSTDmtQPLAQAAVAALG 318
Cdd:cd08013 237 GGEEPSSYPARCTLTIERRTIPGETDESVLAELTAILGELaQTVPNFSYREPRITLSRPPFEVPKE--HPFVQLVAAHAA 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821508169 319 ESLGHIPETTEMTGWGEGGSMQKFGIPAFYFGPgDGPLAHTPKESVSVSEIKTAVKALFHLV 380
Cdd:cd08013 315 KVLGEAPQIRSETFWTDAALLAEAGIPSVVFGP-SGAGLHAKEEWVDVESIRQLREVLSAVV 375
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
15-374 |
1.88e-44 |
|
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: 157.16 E-value: 1.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 15 QALVRVPSV----SGSPACLQVLetaRDLIESTGVEADIRILFPEAPNPVLLARTGRGKagvTELMLSGHVDVVPPAGME 90
Cdd:cd08011 5 QELVQIPSPnppgDNTSAIAAYI---KLLLEDLGYPVELHEPPEEIYGVVSNIVGGRKG---KRLLFNGHYDVVPAGDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 91 ----DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGV--DGVLWLILSTDEETAAQGVVRALSCSDAPRPQLCV 164
Cdd:cd08011 79 gwtvDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKApwDLPVVLTFVPDEETGGRAGTKYLLEKVRIKPNDVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 165 ICEPTGL-CVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAKKRLPELLAGNaaagpasssidlVSGGAA 243
Cdd:cd08011 159 IGEPSGSdNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELEKTVNPGV------------IKGGVK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 244 ENVVPASASVTIDFRYQGVESAQVQCDRIEKILsevrtdPDFPPVSTSLTVTGDWTALSTDmtQPLAQAAVAALGESLGH 323
Cdd:cd08011 227 VNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHL------DSIEEVSFEIKSFYSPTVSNPD--SEIVKKTEEAITEVLGI 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1821508169 324 IPETTEMTGWGEGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVK 374
Cdd:cd08011 299 RPKEVISVGASDARFYRNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIK 349
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
17-375 |
5.87e-43 |
|
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: 153.71 E-value: 5.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 17 LVRVPSVS-GSPACLQVLETARDLIESTGVEADIRILFPEAPNP---VLLARTGRGKAGVteLMLSGHVDVVPPAGME-- 90
Cdd:TIGR01910 7 LISIPSVNpPGGNEETIANYIKDLLREFGFSTDVIEITDDRLKVlgkVVVKEPGNGNEKS--LIFNGHYDVVPAGDLElw 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 91 --DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGV--DGVLWLILSTDEETAAQGVVRALSCSDAPRPQLCVIC 166
Cdd:TIGR01910 85 ktDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIkpNGNIILQSVVDEESGEAGTLYLLQRGYFKDADGVLIP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 167 EPTG---LCVrsAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAKKRLPELLAGNAAA---GPASSSIDLVSG 240
Cdd:TIGR01910 165 EPSGgdnIVI--GHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEEHIYARNSYGfipGPITFNPGVIKG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 241 GAAENVVPASASVTIDFR-YQGVESAQVQcDRIEKILSEV----RTDPDFPPVStsltvtgDWTA-LSTDMTQPLAQAAV 314
Cdd:TIGR01910 243 GDWVNSVPDYCEFSIDVRiIPEENLDEVK-QIIEDVVKALsksdGWLYENEPVV-------KWSGpNETPPDSRLVKALE 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821508169 315 AALGESLGHIPETTEMTGWGEGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKA 375
Cdd:TIGR01910 315 AIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPGDLETAHQVNEYISIKNLVESTKV 375
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
14-376 |
1.07e-39 |
|
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: 144.51 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 14 TQALVRVPSVSGSPACL-QVLETARDLIESTGVEADirilfpeapNPVLLARTGRGKAgvTELMLSGHVDVVPPAGMEDp 92
Cdd:cd05647 5 TAALVDIPSVSGNEKPIaDEIEAALRTLPHLEVIRD---------GNTVVARTERGLA--SRVILAGHLDTVPVAGNLP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 93 wSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVDGVLWLILSTDEETAA-----QGVVRALScsDAPRPQLCVICE 167
Cdd:cd05647 73 -SRVEEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLTLIFYDCEEVAAelnglGRLAEEHP--EWLAADFAVLGE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 168 PTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAAlfivhakkrlpELLAGNAAAGPASSSID----------- 236
Cdd:cd05647 150 PTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLA-----------PILARLAAYEPRTVNIDgltyreglnav 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 237 LVSGGAAENVVPASASVTIDFRYQGVESaqvqcdrIEKILSEVRTDPDFppVSTSLTVTGDWTALSTDMTQPLAQAAVAA 316
Cdd:cd05647 219 FISGGVAGNVIPDEARVNLNYRFAPDKS-------LAEAIAHVREVFEG--LGYEIEVTDLSPGALPGLDHPVARDLIEA 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 317 LGEslghipETTEMTGWGEGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKAL 376
Cdd:cd05647 290 VGG------KVRAKYGWTDVARFSALGIPAVNFGPGDPLLAHKRDEQVPVEQITACAAIL 343
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
14-377 |
8.06e-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. 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: 140.52 E-value: 8.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 14 TQALVRVPSVSGSPACLQVL---------------ETARDLIESTGVEADIRILFPEAPNPVLLARtGRGKAGVTeLMLS 78
Cdd:cd03895 3 LQDLVRFPSLRGEEAAAQDLvaaalrsrgytvdrwEIDVEKLKHHPGFSPVAVDYAGAPNVVGTHR-PRGETGRS-LILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 79 GHVDVVPPAGME----DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGV--DGVLWLILSTDEETAAQGvvrAL 152
Cdd:cd03895 81 GHIDVVPEGPVElwtrPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLqpAADVHFQSVVEEECTGNG---AL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 153 SC------SDAprpqlCVICEPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAAlFIVHAKKRLPELLAGNA 226
Cdd:cd03895 158 AAlmrgyrADA-----ALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAM-HLIQALQELEREWNARK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 227 AAGPASSSID--------LVSGGAAENVVPasASVTIDFR---YQGVESAQVQCDrIEKILSEV-RTDPDFPPVSTSLTV 294
Cdd:cd03895 232 KSHPHFSDHPhpinfnigKIEGGDWPSSVP--AWCVLDCRigiYPGESPEEARRE-IEECVADAaATDPWLSNHPPEVEW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 295 TG-DWTALSTDMTQPLAQAAVAALGESLGHIPETTEMTGWGEGGSMQK-FGIPAFYFGPGDGPlAHTPKESVSVSEIKTA 372
Cdd:cd03895 309 NGfQAEGYVLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLyGDIPALCYGPGSRD-AHGFDESVDLESLRKI 387
|
....*..
gi 1821508169 373 VK--ALF 377
Cdd:cd03895 388 TKtiALF 394
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
9-383 |
2.65e-36 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 135.27 E-value: 2.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 9 RAVLWTQALVRVPSVSGSPA--CLQVLETARDL-----IESTGVEADIrILFPEApnpvllartgrgkagvtELMLSGHV 81
Cdd:PRK08652 3 RAKELLKQLVKIPSPSGQEDeiALHIMEFLESLgydvhIESDGEVINI-VVNSKA-----------------ELFVEVHY 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 82 DVVPPAGMEDpwsarIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVDGVLWLILSTDEETAAQG---VVRALscsdap 158
Cdd:PRK08652 65 DTVPVRAEFF-----VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSDEEEGGRGsalFAERY------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 159 RPQLCVICEPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIvhakKRLPELLAGNAAAGPASSSIDLV 238
Cdd:PRK08652 134 RPKMAIVLEPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEML----EKLKELLKALGKYFDPHIGIQEI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 239 SGGAAENVVPASASVTIDFRYQGVESAQVQCDRIEKILSEvrtdpdfppVSTSLTVTGDWTALSTDMTQPLAQAAVAALg 318
Cdd:PRK08652 210 IGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDE---------YTVKYEYTEIWDGFELDEDEEIVQLLEKAM- 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821508169 319 ESLGHIPETTEMTGWGEGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKALFHLVDRL 383
Cdd:PRK08652 280 KEVGLEPEFTVMRSWTDAINFRYNGTKTVVWGPGELDLCHTKFERIDVREVEKAKEFLKALNEIL 344
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
15-365 |
4.23e-35 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 132.70 E-value: 4.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 15 QALVRVPSVSGSPacLQVLETARDLIESTGVEADIRILFPEAPNpvLLARTGRGKAgVteLMLSGHVDVVPPAGME---- 90
Cdd:PRK08588 9 ADIVKINSVNDNE--IEVANYLQDLFAKHGIESKIVKVNDGRAN--LVAEIGSGSP-V--LALSGHMDVVAAGDVDkwty 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 91 DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGV--DGVLWLILSTDEET--------AAQGV---VRALscsda 157
Cdd:PRK08588 82 DPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQllNGTIRLLATAGEEVgelgakqlTEKGYaddLDAL----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 158 prpqlcVICEPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAKKRLPELLAGNAAAGPASSSIDL 237
Cdd:PRK08588 157 ------IIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYFDSIKKHNPYLGGLTHVVTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 238 VSGGAAENVVPASASVTIDFR-YQGVESAQVQcDRIEKILSEVRTDPDfppVSTSLTVTGDWTALSTDMTQPLAQAAVAA 316
Cdd:PRK08588 231 INGGEQVNSVPDEAELEFNIRtIPEYDNDQVI-SLLQEIINEVNQNGA---AQLSLDIYSNHRPVASDKDSKLVQLAKDV 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1821508169 317 LGESLGHIPETTEMTGWGEGGSMQKFG--IPAFYFGPGDGPLAHTPKESVS 365
Cdd:PRK08588 307 AKSYVGQDIPLSAIPGATDASSFLKKKpdFPVIIFGPGNNLTAHQVDEYVE 357
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
14-373 |
4.95e-35 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 132.76 E-value: 4.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 14 TQALVRVPSVSGSPAclQVLETARDLIESTG---VEADirilfpeaPNPVLLARTGRGKagvTELMLSGHVDVVPPAGME 90
Cdd:PRK13004 21 LRDLIRIPSESGDEK--RVVKRIKEEMEKVGfdkVEID--------PMGNVLGYIGHGK---KLIAFDAHIDTVGIGDIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 91 ----DPWSARIEGDRMHGRGTTDMKSGAA---CALTTFCEAARQGvDGVLWLILSTDEE----TAAQGVVRALSCsdapR 159
Cdd:PRK13004 88 nwdfDPFEGEEDDGRIYGRGTSDQKGGMAsmvYAAKIIKDLGLDD-EYTLYVTGTVQEEdcdgLCWRYIIEEDKI----K 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 160 PQLCVICEPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALfIVHAKKRLPELLAGNAAAGPASSSI-DLV 238
Cdd:PRK13004 163 PDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAP-ILNELEELNPNLKEDPFLGKGTLTVsDIF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 239 SGGAAENVVPASASVTIDFRYQGVESAqvqcdriEKILSEVRTDPDFPP----VSTSLTVTGDWTALS-----------T 303
Cdd:PRK13004 242 STSPSRCAVPDSCAISIDRRLTVGETW-------ESVLAEIRALPAVKKanakVSMYNYDRPSYTGLVyptecyfptwlY 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821508169 304 DMTQPLAQAAVAALGESLGHIPETTEMTGWGEGGS-MQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAV 373
Cdd:PRK13004 315 PEDHEFVKAAVEAYKGLFGKAPEVDKWTFSTNGVSiAGRAGIPTIGFGPGKEPLAHAPNEYTWKEQLVKAA 385
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
14-371 |
9.17e-34 |
|
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: 128.78 E-value: 9.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 14 TQALVRVPSVSgsPA---CLQVLEtarDLIESTGVEAdIRILFPEAPNpvLLARtgRGKAGVTeLMLSGHVDVVPPAGME 90
Cdd:cd03891 4 AKELIRRPSVT--PDdagAQDLIA---ERLKALGFTC-ERLEFGGVKN--LWAR--RGTGGPH-LCFAGHTDVVPPGDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 91 ----DPWSARIEGDRMHGRGTTDMKSGAACALTTFCE--AARQGVDGVLWLILSTDEETAA----QGVVRALSCSDApRP 160
Cdd:cd03891 73 gwssDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERfvAKHPNHKGSISFLITSDEEGPAidgtKKVLEWLKARGE-KI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 161 QLCVICEPT-----GLCVRSAHRG--DCWIRVdfTGKSAHSSRPHLGINAIEAAAlfivhakKRLPELLA-----GNAAA 228
Cdd:cd03891 152 DYCIVGEPTsekklGDTIKIGRRGslNGKLTI--KGKQGHVAYPHLADNPIHLLA-------PILAELTAtvldeGNEFF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 229 GPAS---SSIDlvSGGAAENVVPASASVTIDFRY---QGVESAQvqcDRIEKILSEVRTDPDFppvstsltvtgDWTaLS 302
Cdd:cd03891 223 PPSSlqiTNID--VGNGATNVIPGELKAKFNIRFndeHTGESLK---ARIEAILDKHGLDYDL-----------EWK-LS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 303 TDM--TQP--LAQAAVAALGESLGHIPE--TTemtgwgeGGS-----MQKFGIPAFYFGP-GDgpLAHTPKESVSVSEIK 370
Cdd:cd03891 286 GEPflTKPgkLVDAVSAAIKEVTGITPElsTS-------GGTsdarfIASYGCPVVEFGLvNA--TIHKVNERVSVADLE 356
|
.
gi 1821508169 371 T 371
Cdd:cd03891 357 K 357
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
15-380 |
5.51e-33 |
|
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: 126.55 E-value: 5.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 15 QALVRVPSVSGSPACL-QVLETARDLIESTGVEADIRILFPEAPNpvLLAR-TGRGKAGVtelMLSGHVDVVPPAGMEDP 92
Cdd:cd03885 6 ERLVNIESGTYDKEGVdRVAELLAEELEALGFTVERRPLGEFGDH--LIATfKGTGGKRV---LLIGHMDTVFPEGTLAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 93 WSARIEGDRMHGRGTTDMKSGAAC---ALTTFCEAARQGVDGVLWLiLSTDEETAAQGvVRALSCSDAPRPQLCVICEPT 169
Cdd:cd03885 81 RPFTVDGDRAYGPGVADMKGGLVVilhALKALKAAGGRDYLPITVL-LNSDEEIGSPG-SRELIEEEAKGADYVLVFEPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 170 GL--CVRSAHRGDCWIRVDFTGKSAHSSR-PHLGINAIEAAALFIvhakkrlpelLAGNAAAGPASS---SIDLVSGGAA 243
Cdd:cd03885 159 RAdgNLVTARKGIGRFRLTVKGRAAHAGNaPEKGRSAIYELAHQV----------LALHALTDPEKGttvNVGVISGGTR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 244 ENVVPASASVTIDFRYQGVESAqvqcDRIEKILSEVRTDPDFPpvSTSLTVTGDWTAL---STDMTQPLAqAAVAALGES 320
Cdd:cd03885 229 VNVVPDHAEAQVDVRFATAEEA----DRVEEALRAIVATTLVP--GTSVELTGGLNRPpmeETPASRRLL-ARAQEIAAE 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821508169 321 LGhIPETTEMTGWG-EGGSMQKFGIPAF-YFGP-GDGplAHTPKESVSVSEIKTAVKALFHLV 380
Cdd:cd03885 302 LG-LTLDWEATGGGsDANFTAALGVPTLdGLGPvGGG--AHTEDEYLELDSLVPRIKLLARLL 361
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
15-380 |
1.50e-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 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: 125.08 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 15 QALVRVPSVSGSP-ACLQVLEtarDLIESTG--VEadiRILFPEAPNPVLLARTGRGKAgvTELMLSGHVDVVPPAgmeD 91
Cdd:cd05652 6 KSLVEIPSISGNEaAVGDFLA---EYLESLGftVE---KQPVENKDRFNVYAYPGSSRQ--PRVLLTSHIDTVPPF---I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 92 PWSARIEGDRMHGRGTTDMKSGAACALTTFCE--AARQGVDGVLWLILSTDEETAAQGVvRALSCSDAPRPQLCVICEPT 169
Cdd:cd05652 75 PYSISDGGDTIYGRGSVDAKGSVAAQIIAVEEllAEGEVPEGDLGLLFVVGEETGGDGM-KAFNDLGLNTWDAVIFGEPT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 170 GLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEA--AALFIVHAKKrLP--ELLagnaaaGPASSSIDLVSGGAAEN 245
Cdd:cd05652 154 ELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEIlvEALVKLIDAD-LPssELL------GPTTLNIGRISGGVAAN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 246 VVPASASVTIDFRY-QGVESAQvqcDRIEKILSEVRTDPDfppvSTSLTVTGDWTALSTDMTQPLAQAAVAALGESLGHI 324
Cdd:cd05652 227 VVPAAAEASVAIRLaAGPPEVK---DIVKEAVAGILTDTE----DIEVTFTSGYGPVDLDCDVDGFETDVVAYGTDIPYL 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1821508169 325 PettemtgwgegGSMQKfgipaFYFGPGDGPLAHTPKESVSVSEIKTAVKALFHLV 380
Cdd:cd05652 300 K-----------GDHKR-----YLYGPGSILVAHGPDEAITVSELEEAVEGYKKLI 339
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
14-377 |
5.10e-32 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 125.11 E-value: 5.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 14 TQALVRVPSVSGSPACLQVL---------------ETARDLIESTGVEADIRILFPEAPNPVLLARtGRGKAGVTeLMLS 78
Cdd:PRK06837 26 TQDLVRFPSTRGAEAPCQDFlarafrergyevdrwSIDPDDLKSHPGAGPVEIDYSGAPNVVGTYR-PAGKTGRS-LILQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 79 GHVDVVP--PAGM--EDPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGV--DGVLWLILSTDEETAAQGvvrAL 152
Cdd:PRK06837 104 GHIDVVPegPLDLwsRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLapAARVHFQSVIEEESTGNG---AL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 153 SC------SDAprpqlCVICEPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEaAALFIVHAKKRLPELLAGNA 226
Cdd:PRK06837 181 STlqrgyrADA-----CLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAID-AAYHLIQALRELEAEWNARK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 227 AAGPASSSID--------LVSGGAAENVVPASAsvTIDFR---YQGVESAQVQcDRIEKILSEVRTDPDF----PPVSTs 291
Cdd:PRK06837 255 ASDPHFEDVPhpinfnvgIIKGGDWASSVPAWC--DLDCRiaiYPGVTAADAQ-AEIEACLAAAARDDRFlsnnPPEVV- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 292 ltvtgdWTAL---------STDMTQPLAQAAVAALGESLGH--IPETTEMTGWGeggsmQKFGIPAFYFGP-GDGPlaHT 359
Cdd:PRK06837 331 ------WSGFlaegyvlepGSEAEAALARAHAAVFGGPLRSfvTTAYTDTRFYG-----LYYGIPALCYGPsGEGI--HG 397
|
410 420
....*....|....*....|
gi 1821508169 360 PKESVSVSEIK--TAVKALF 377
Cdd:PRK06837 398 FDERVDLESVRkvTKTIALF 417
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
15-372 |
3.16e-30 |
|
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: 119.45 E-value: 3.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 15 QALVRVPSVSGSPAclQVLETARDLIESTGVEaDIRIlfpeAPNPVLLARTGRGKagvTELMLSGHVDVVPPAGME---- 90
Cdd:cd05649 5 RDLIQIPSESGEEK--GVVERIEEEMEKLGFD-EVEI----DPMGNVIGYIGGGK---KKILFDGHIDTVGIGNIDnwkf 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 91 DPWSARIEGDRMHGRGTTDMKSGAAC---ALTTFCEAARQGVDGVLWLILSTDEE----TAAQGVVRAlscsDAPRPQLC 163
Cdd:cd05649 75 DPYEGYETDGKIYGRGTSDQKGGLASmvyAAKIMKDLGLRDFAYTILVAGTVQEEdcdgVCWQYISKA----DKIKPDFV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 164 VICEPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALfIVHAKKRLPELLAGNAAAGPASSSI-DLVSGGA 242
Cdd:cd05649 151 VSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMAD-IIQDIRQLNPNFPEAPFLGRGTLTVtDIFSTSP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 243 AENVVPASASVTIDFRYQGVESAQVQCDRIEKILSEvrtdPDFPPVSTSLTVTGD---WTALS-----------TDMTQP 308
Cdd:cd05649 230 SRCAVPDSCRISIDRRLTVGETWEGCLEEIRALPAV----KKYGDDVAVSMYNYDrpsYTGEVyeseryfptwlLPEDHE 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821508169 309 LAQAAVAALGESLGHIPETTEMTGWGEGGS-MQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTA 372
Cdd:cd05649 306 LVKALLEAYKALFGARPLIDKWTFSTNGVSiMGRAGIPCIGFGPGAENQAHAPNEYTWKEDLVRC 370
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
14-371 |
5.72e-30 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 118.65 E-value: 5.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 14 TQALVRVPSVSgsPA---CLQVLEtarDLIESTGVEADiRILFPEAPNpvLLARtgRGKAGVTeLMLSGHVDVVPPAGME 90
Cdd:PRK13009 8 AQDLIRRPSVT--PDdagCQDLLA---ERLEALGFTCE-RMDFGDVKN--LWAR--RGTEGPH-LCFAGHTDVVPPGDLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 91 ----DPWSARIEGDRMHGRGTTDMKSGAACALTTFCE--AARQGVDGVLWLILSTDEETAA-QGVVRALscsDA-----P 158
Cdd:PRK13009 77 awtsPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERfvAAHPDHKGSIAFLITSDEEGPAiNGTVKVL---EWlkargE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 159 RPQLCVICEPTglcvrSAHR-GDC-----------WIRVDftGKSAHSSRPHLGINAIEAAAlfivhakKRLPELLA--- 223
Cdd:PRK13009 154 KIDYCIVGEPT-----STERlGDVikngrrgsltgKLTVK--GVQGHVAYPHLADNPIHLAA-------PALAELAAtew 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 224 --GNAAAGPAS---SSIDlvSGGAAENVVPASASVTIDFRY---QGVESAQvqcDRIEKILSEVRTDPDFppvstsltvt 295
Cdd:PRK13009 220 deGNEFFPPTSlqiTNID--AGTGATNVIPGELEAQFNFRFsteHTAESLK---ARVEAILDKHGLDYTL---------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 296 gDWTaLSTD--MTQP--LAQAAVAALGESLGHIPE--TTemtgwgeGGS-----MQKFGIPAFYFGP-GDgpLAHTPKES 363
Cdd:PRK13009 285 -EWT-LSGEpfLTPPgkLVDAVVAAIEAVTGITPElsTS-------GGTsdarfIADYGAQVVEFGPvNA--TIHKVNEC 353
|
....*...
gi 1821508169 364 VSVSEIKT 371
Cdd:PRK13009 354 VSVADLEK 361
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
15-374 |
5.75e-30 |
|
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: 117.80 E-value: 5.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 15 QALVRVPSVSGSPAclqvlETArDLIESTGVEADIRilfPEAPNPVLLARTGRGKAGVTELMLSGHVDVVPP-AGME-DP 92
Cdd:cd05651 7 KSLIATPSFSREEH-----KTA-DLIENYLEQKGIP---FKRKGNNVWAENGHFDEGKPTLLLNSHHDTVKPnAGWTkDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 93 WSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGV-DGVLWLILSTDEETAAQGVVRALSCsDAPRPQLCVICEPTGL 171
Cdd:cd05651 78 FEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGPlNYNLIYAASAEEEISGKNGIESLLP-HLPPLDLAIVGEPTEM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 172 CVRSAHRGDCWIRVDFTGKSAHSSRPHlGINAIEAAALFIVHAK----KRLPELLagnaaaGPASSSIDLVSGGAAENVV 247
Cdd:cd05651 157 QPAIAEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDIQWLRdfrfDKVSPLL------GPVKMTVTQINAGTQHNVV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 248 PASASVTIDFRyqgVESAQVQCDRIEKILSEVRTdpDFPPVSTSLtvtgdwTALSTDMTQPLAQAAVAALGESLGHiPET 327
Cdd:cd05651 230 PDSCTFVVDIR---TTEAYTNEEIFEIIRGNLKS--EIKPRSFRL------NSSAIPPDHPIVQAAIAAGRTPFGS-PTL 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1821508169 328 temtgwgeggSMQKF-GIPAFYFGPGDGPLAHTPKESVSVSEIKTAVK 374
Cdd:cd05651 298 ----------SDQALmPFPSVKIGPGDSSRSHTADEFIELSEIEEGID 335
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
16-383 |
3.00e-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: 115.91 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 16 ALVRVPSVSGSPAclQVLETARDLIESTGVEADIrilfPEAPNpvllARTGRGKAGVTeLMLSGHVDVVPpagmeDPWSA 95
Cdd:cd05653 9 DLLSIYSPSGEEA--RAAKFLEEIMKELGLEAWV----DEAGN----AVGGAGSGPPD-VLLLGHIDTVP-----GEIPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 96 RIEGDRMHGRGTTDMKsGAACALTTFCEAARQGVDGVLWLILSTDEETAAQGVvRALScSDAPRPQLCVICEPTGLC-VR 174
Cdd:cd05653 73 RVEGGVLYGRGAVDAK-GPLAAMILAASALNEELGARVVVAGLVDEEGSSKGA-RELV-RRGPRPDYIIIGEPSGWDgIT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 175 SAHRGDCWIRVDFTGKSAHSSRPhlGINAIEAAALFIVHAKKRLPELLAGNAAAGPASSSIdlVSGGAAENVVPASASVT 254
Cdd:cd05653 150 LGYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLIKKWLEVKKWAEGYNVGGRDFDSVVPTL--IKGGESSNGLPQRAEAT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 255 IDFRYQGVESAqvqCDRIEKILSEVRTDpdfppvstSLTVTGDWTALSTDMTQPLAQAAVAALGEsLGHIPE------TT 328
Cdd:cd05653 226 IDLRLPPRLSP---EEAIALATALLPTC--------ELEFIDDTEPVKVSKNNPLARAFRRAIRK-QGGKPRlkrktgTS 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1821508169 329 EMTGWGEggsmqKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKALFHLVDRL 383
Cdd:cd05653 294 DMNVLAP-----LWTVPIVAYGPGDSTLDHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
15-206 |
5.19e-27 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 110.68 E-value: 5.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 15 QALVRVPSVSGSPACL-----QVLETARDLIESTGVEADIRILfPEAPNPV-LLARTGRGKAGvteLMLSGHVDVVP-PA 87
Cdd:PRK05111 12 RALIATPSISATDPALdqsnrAVIDLLAGWFEDLGFNVEIQPV-PGTRGKFnLLASLGSGEGG---LLLAGHTDTVPfDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 88 GM--EDPWSARIEGDRMHGRGTTDMKSGAACALttfcEAARQgvdgVLW-------LILST-DEETAAQGVvRALSCSDA 157
Cdd:PRK05111 88 GRwtRDPFTLTEHDGKLYGLGTADMKGFFAFIL----EALRD----IDLtklkkplYILATaDEETSMAGA-RAFAEATA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1821508169 158 PRPQLCVICEPTGLC-VRsAHRGDCWIRVDFTGKSAHSSRPHLGINAIEA 206
Cdd:PRK05111 159 IRPDCAIIGEPTSLKpVR-AHKGHMSEAIRITGQSGHSSDPALGVNAIEL 207
|
|
| PRK06915 |
PRK06915 |
peptidase; |
7-377 |
1.40e-26 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 109.78 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 7 EQRAVLWTQALVRVPSVSGSPACLQ--VLETARDLiestGVEADI-----------------RILFPEAPNpvlLARTGR 67
Cdd:PRK06915 16 EEEAVKLLKRLIQEKSVSGDESGAQaiVIEKLREL----GLDLDIwepsfkklkdhpyfvspRTSFSDSPN---IVATLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 68 GKAGVTELMLSGHVDVVPPAGM----EDPWSARIEGDRMHGRGTTDMKSGAACALttFCEAARQGVDGVLW--LILST-- 139
Cdd:PRK06915 89 GSGGGKSMILNGHIDVVPEGDVnqwdHHPYSGEVIGGRIYGRGTTDMKGGNVALL--LAMEALIESGIELKgdVIFQSvi 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 140 DEETAAQGVVRAL---SCSDAprpqlCVICEPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAKK 216
Cdd:PRK06915 167 EEESGGAGTLAAIlrgYKADG-----AIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 217 -------RLPELLAGNAAAgPASSSIDLVSGGAAENVVPASasVTIDFRY-----QGVESAQVQCDRIEKILSEVrtDPD 284
Cdd:PRK06915 242 leekrndRITDPLYKGIPI-PIPINIGKIEGGSWPSSVPDS--VILEGRCgiapnETIEAAKEEFENWIAELNDV--DEW 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 285 FPPVSTSLTVTG-DWTALSTDMTQPLAQAAVAALGESLGHIPETtEMTGWGEGGSM--QKFGIPAFYFGPGDGPLAHTPK 361
Cdd:PRK06915 317 FVEHPVEVEWFGaRWVPGELEENHPLMTTLEHNFVEIEGNKPII-EASPWGTDGGLltQIAGVPTIVFGPGETKVAHYPN 395
|
410
....*....|....*...
gi 1821508169 362 ESVSVSEIKTAVK--ALF 377
Cdd:PRK06915 396 EYIEVDKMIAAAKiiALT 413
|
|
| dapE-lys-deAc |
TIGR01902 |
N-acetyl-ornithine/N-acetyl-lysine deacetylase; This clade of mainly archaeal and related ... |
17-376 |
2.69e-24 |
|
N-acetyl-ornithine/N-acetyl-lysine deacetylase; This clade of mainly archaeal and related bacterial species contains two characterized enzymes, an deacetylase with specificity for both N-acetyl-ornithine and N-acetyl-lysine from Thermus, which is found within a lysine biosynthesis operon, and a fusion protein with acetyl-glutamate kinase (an enzyme of ornithine biosynthesis) from Lactobacillus. It is possible that all of the sequences within this clade have dual specificity, or that a mix of specificities have evolved within this clade.
Pssm-ID: 130957 [Multi-domain] Cd Length: 336 Bit Score: 102.24 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 17 LVRVPSVSGSPAclQVLETARDLIESTGVEADIrilfPEAPNPVLlartGRGKAGVtELMLSGHVDVVPpagmeDPWSAR 96
Cdd:TIGR01902 6 LLEIYSPSGKEA--NAAKFLEEISKDLGLKLII----DDAGNFIL----GKGDGHK-KILLAGHVDTVP-----GYIPVK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 97 IEGDRMHGRGTTDMKSgaacALTTFCEAARQGVDGVLWLILS--TDEETAAQGVVRALscsDAPRPQLCVICEPTGLC-V 173
Cdd:TIGR01902 70 IEGGLLYGRGAVDAKG----PLIAMIFATWLLNEKGIKVIVSglVDEESSSKGAREVI---DKNYPFYVIVGEPSGAEgI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 174 RSAHRGDCWIRVDFTGKSAHSSrphLGINAIEAaalfIVHAKKRLPELLAGNAAAGPASSSIDLVSGGAAENVVPASASV 253
Cdd:TIGR01902 143 TLGYKGSLQLKIMCEGTPFHSS---SAGNAAEL----LIDYSKKIIEVYKQPENYDKPSIVPTIIRFGESYNDTPAKLEL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 254 TIDFRYQgVESAQVqcDRIEKIlsevrtDPDFPpvsTSLTVTGDWTALSTDMTQPLAQAAVAALGEsLGHIPETTEMTGW 333
Cdd:TIGR01902 216 HFDLRYP-PNNKPE--EAIKEI------TDKFP---ICLEIVDETPPYKVSRNNPLVRAFVRAIRK-QGMKPRLKKKTGT 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1821508169 334 GEGGSMQ-KFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKAL 376
Cdd:TIGR01902 283 SDMNILApIWTVPMVAYGPGDSTLDHTPQEKISLAEYLIGIKTL 326
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
1-383 |
4.15e-21 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 93.10 E-value: 4.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 1 MPQDTLEQRAVLwtQALVRVPSVSGSPAclQVLETARDLIESTGVEADIrilfPEAPNpvllARTGRGKAGVTeLMLSGH 80
Cdd:PRK04443 1 MTISALEARELL--KGLVEIPSPSGEEA--AAAEFLVEFMESHGREAWV----DEAGN----ARGPAGDGPPL-VLLLGH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 81 VDVVP---PAgmedpwsaRIEGDRMHGRGTTDMKsGAACALttFCEAARQGVDGVLWLIL--STDEETAAQGVVRALscS 155
Cdd:PRK04443 68 IDTVPgdiPV--------RVEDGVLWGRGSVDAK-GPLAAF--AAAAARLEALVRARVSFvgAVEEEAPSSGGARLV--A 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 156 DAPRPQLCVICEPTGL-CVRSAHRGDCWIRVDFTGKSAHSSRPhlGINAIEAAALFIVhakkRLPELLAGNAAAGPA--S 232
Cdd:PRK04443 135 DRERPDAVIIGEPSGWdGITLGYKGRLLVTYVATSESFHSAGP--EPNAAEDAIEWWL----AVEAWFEANDGRERVfdQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 233 SSIDLVSGGAAENVVPASASVTIDFRYqgveSAQVQCDRIEKILsevrtdpDFPPVSTSLTVTGDWTALSTDMTQPLAQA 312
Cdd:PRK04443 209 VTPKLVDFDSSSDGLTVEAEMTVGLRL----PPGLSPEEAREIL-------DALLPTGTVTFTGAVPAYMVSKRTPLARA 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821508169 313 AVAALGESlGHIPE------TTEMTGWGEggsmqKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKALFHLVDRL 383
Cdd:PRK04443 278 FRVAIREA-GGTPRlkrktgTSDMNVVAP-----AWGCPMVAYGPGDSDLDHTPDEHLPLAEYLRAIAVLTDVLERL 348
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
67-380 |
1.43e-20 |
|
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: 91.77 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 67 RGKAGVTELMLSGHVDVVPPAgmEDPWSARIEGDRMHGRGTTDMKSGAACaLTTFCEAARQG---VDGVLWLILSTDEET 143
Cdd:cd03896 49 RGTGGGPALLFSAHLDTVFPG--DTPATVRHEGGRIYGPGIGDNKGSLAC-LLAMARAMKEAgaaLKGDVVFAANVGEEG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 144 AAQGV-VRALSCSDAPRPQLCVICEPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVhakkrlpELL 222
Cdd:cd03896 126 LGDLRgARYLLSAHGARLDYFVVAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVE-------ALY 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 223 AGNAAAGPASS-SIDLVSGGAAENVVPASASVTIDFRYQG-VESAQVQcDRIEKILSEVRTdpDFPPVSTSLTVTGDWTA 300
Cdd:cd03896 199 EWAAPYVPKTTfAAIRGGGGTSVNRIANLCSMYLDIRSNPdAELADVQ-REVEAVVSKLAA--KHLRVKARVKPVGDRPG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 301 LSTDMTQPLAQAAVAALGESLGHiPETTEMtgWGEGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKALFHLV 380
Cdd:cd03896 276 GEAQGTEPLVNAAVAAHREVGGD-PRPGSS--STDANPANSLGIPAVTYGLGRGGNAHRGDEYVLKDDMLKGAKAYLMLA 352
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
75-380 |
3.06e-20 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 90.88 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 75 LMLSGHVDVVP--PAgmeDPWSARIEGDRMHGRGTT----DMKSGAACALTtfceAARQGVD-----GVLWLILSTDEET 143
Cdd:COG2195 63 IGLQAHMDTVPqfPG---DGIKPQIDGGLITADGTTtlgaDDKAGVAAILA----ALEYLKEpeiphGPIEVLFTPDEEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 144 AAQGV----VRALSCSDAprpqLCVICEPTG-LCVRSAhrGDCWIRVDFTGKSAHS-SRPHLGINAIEAAALFIVHAKK- 216
Cdd:COG2195 136 GLRGAkaldVSKLGADFA----YTLDGGEEGeLEYECA--GAADAKITIKGKGGHSgDAKEKMINAIKLAARFLAALPLg 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 217 RLPELLAGNaaagpasssIDLVSGGAAENVVPASASVTIDFRYQGVESAQVQCDRIEKILSEVRTdpDFPPVSTSLTVTG 296
Cdd:COG2195 210 RIPEETEGN---------EGFIHGGSATNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENA--KYGVGVVEVEIED 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 297 DWTALSTDMTQPLAQAAVAALgESLGHIPETTEMTGwG-EGGSMQKFGIPAFYFGPGdGPLAHTPKESVSVSEIKTAVKA 375
Cdd:COG2195 279 QYPNWKPEPDSPIVDLAKEAY-EELGIEPKIKPIRG-GlDGGILSFKGLPTPNLGPG-GHNFHSPDERVSIESMEKAWEL 355
|
....*
gi 1821508169 376 LFHLV 380
Cdd:COG2195 356 LVEIL 360
|
|
| selenium_YgeY |
TIGR03526 |
putative selenium metabolism hydrolase; SelD, selenophosphate synthase, is the selenium donor ... |
17-380 |
3.52e-20 |
|
putative selenium metabolism hydrolase; SelD, selenophosphate synthase, is the selenium donor protein for both selenocysteine and selenouridine biosynthesis systems, but it occurs also in a few prokaryotes that have neither of those pathways. The method of partial phylogenetic profiling, starting from such orphan-selD genomes, identifies this protein as one of those most strongly correlated to SelD occurrence. Its distribution is also well correlated with that of family TIGR03309, a putative accessory protein of labile selenium (non-selenocysteine) enzyme maturation. This family includes the uncharacterized YgeY of Escherichia coli, and belongs to a larger family of metalloenzymes in which some are known peptidases, others enzymes of different types.
Pssm-ID: 132565 [Multi-domain] Cd Length: 395 Bit Score: 91.40 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 17 LVRVPSVSGSPAclQVLETARDLIESTG---VEADirilfpeaPNPVLLARTGRGKagvTELMLSGHVDVVPPAGME--- 90
Cdd:TIGR03526 22 LVAIPSESGDEG--RVALRIKQEMEKLGfdkVEID--------PMGNVLGYIGHGP---KLIAMDAHIDTVGIGDMDqwq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 91 -DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGV-DGVLWLILSTDEETAAQGVV-RALSCSDAPRPQLCVICE 167
Cdd:TIGR03526 89 fDPYEGYEDEEIIYGRGASDQEGGIASMVYAGKIIKDLGLlDDYTLLVTGTVQEEDCDGLCwQYIIEEDKIKPEFVVITE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 168 PTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALfIVHAKKRLPELLAGNAAAGPASSSIDLVSGGA-AENV 246
Cdd:TIGR03526 169 PTDMNIYRGQRGRMEIKVTVKGVSCHGSAPERGDNAIYKMAP-ILKELSQLNANLVEDPFLGKGTLTVSEIFFSSpSRCA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 247 VPASASVTIDFRYQGVESAQVQCDRIEKiLSEVRTDP------DFP-PVSTSLTVTGD--WTALSTDMTQPLAQAAVAAL 317
Cdd:TIGR03526 248 VADGCTISIDRRLTWGETWEYALEQIRN-LPAVQGAEaevemyEYDrPSYTGLVYPTEcyFPTWVLPEDHLITKAALETY 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821508169 318 GESLGHIPETTEMTGWGEGGS-MQKFGIPAFYFGPGDGPLAHTPKESVSVSEI--KTAVKALFHLV 380
Cdd:TIGR03526 327 KRLFGKEPGVDKWTFSTNGVSiMGRHGIPVIGFGPGDEDQAHAPNEKTWKEDLvkAAAMYAAIPTV 392
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
71-380 |
3.21e-19 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 87.95 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 71 GVTELMLSGHVDVVP--PAGMEDPWSARIEGDRMHGRGTTDMKSGAACALttfceAARQGVDGVLWLILSTDEETAAQGV 148
Cdd:PRK08737 62 GTPKYLFNVHLDTVPdsPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALL-----AAANAGDGDAAFLFSSDEEANDPRC 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 149 VRALsCSDAPRPQLCVICEPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPH-LGINAIEAAALFIVHAKKRLPELL-AGNA 226
Cdd:PRK08737 137 VAAF-LARGIPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKQdPSASALHQAMRWGGQALDHVESLAhARFG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 227 AAGPASSSIDLVSGGAAENVVPASASVTIDFRyqgvesaQVQCDRIEKILSEVRTDPDFPPVSTSLTVTGD---WTALST 303
Cdd:PRK08737 216 GLTGLRFNIGRVEGGIKANMIAPAAELRFGFR-------PLPSMDVDGLLATFAGFAEPAAATFEETFRGPslpSGDIAR 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821508169 304 DMTQPLAQAAVA-ALgeslgHIPETTEMTGWGEGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKALFHLV 380
Cdd:PRK08737 289 AEERRLAARDVAdAL-----DLPIGNAVDFWTEASLFSAAGYTALVYGPGDIAQAHTADEFVTLDQLQRYAESVHRII 361
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
11-376 |
1.62e-18 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 86.74 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 11 VLWTQALVRVPSVSgSP-----ACLQVLET-------ARDLIESTGVEADIrilfPEAPNPVLLARTGRGKAGVTeLMLS 78
Cdd:PRK13013 17 VALTQDLIRIPTLN-PPgrayrEICEFLAArlaprgfEVELIRAEGAPGDS----ETYPRWNLVARRQGARDGDC-VHFN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 79 GHVDVVPpAG---MEDPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVD--GVLWLILSTDEETAAQGVVRALS 153
Cdd:PRK13013 91 SHHDVVE-VGhgwTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDfaGSIEISGTADEESGGFGGVAYLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 154 CS---DAPRPQLCVICEPTG---LCVrsAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAKKRLPELLAGNAA 227
Cdd:PRK13013 170 EQgrfSPDRVQHVIIPEPLNkdrICL--GHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEIEERLFPLLATRRT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 228 AGP--------ASSSIDLVSGGAAEN----------VVPASASVTIDFRYQGVESAQVQCDRIEKILSEV-RTDPDFppv 288
Cdd:PRK13013 248 AMPvvpegarqSTLNINSIHGGEPEQdpdytglpapCVADRCRIVIDRRFLIEEDLDEVKAEITALLERLkRARPGF--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 289 STSLTVTGDWTALSTDMTQPLAQAAVAALGESLGHIPETTEMTGWGEGGSMQKFG-IP-AFYFGPGDGPLAHTPKESVSV 366
Cdd:PRK13013 325 AYEIRDLFEVLPTMTDRDAPVVRSVAAAIERVLGRQADYVVSPGTYDQKHIDRIGkLKnCIAYGPGILDLAHQPDEWVGI 404
|
410
....*....|
gi 1821508169 367 SEIKTAVKAL 376
Cdd:PRK13013 405 ADMVDSAKVM 414
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
176-279 |
2.42e-18 |
|
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: 79.70 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 176 AHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVhakkRLPELLAGNAAAGPASS-SIDLVSGGAAENVVPASASVT 254
Cdd:pfam07687 2 GHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLA----ELPAEYGDIGFDFPRTTlNITGIEGGTATNVIPAEAEAK 77
|
90 100
....*....|....*....|....*
gi 1821508169 255 IDFRYQGVESAQVQCDRIEKILSEV 279
Cdd:pfam07687 78 FDIRLLPGEDLEELLEEIEAILEKE 102
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
14-381 |
4.09e-18 |
|
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: 85.49 E-value: 4.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 14 TQALVRVPSV---SGSPACLQVLETARDLIESTGVEADIrILFPEAPNPV-LLARTGRGKAGVTELMLSGHVDVVP--PA 87
Cdd:cd05675 4 LQELIRIDTTnsgDGTGSETRAAEVLAARLAEAGIQTEI-FVVESHPGRAnLVARIGGTDPSAGPLLLLGHIDVVPadAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 88 GM-EDPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGV--DGVLWLILSTDEETAAQGVVRALscsDAPRPQLC- 163
Cdd:cd05675 83 DWsVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFkpKRDLVFAFVADEEAGGENGAKWL---VDNHPELFd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 164 ----VICEPTG-----------LCVRSAHRGDCWIRVDFTGKSAHSSRPHLGiNAIE--AAALFIVHA------------ 214
Cdd:cd05675 160 gatfALNEGGGgslpvgkgrrlYPIQVAEKGIAWMKLTVRGRAGHGSRPTDD-NAITrlAEALRRLGAhnfpvrltdeta 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 215 --------------------KKRLPELLAGNAAAGP-------ASSSIDLVSGGAAENVVPASASVTIDFRYQGVESAQV 267
Cdd:cd05675 239 yfaqmaelaggeggalmltaVPVLDPALAKLGPSAPllnamlrNTASPTMLDAGYATNVLPGRATAEVDCRILPGQSEEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 268 QCDRIEKILSevrtDPDfppvstsltVTGDWTALSTDMTQPLAQAAVAALGESLGH-IPET----TEMTGWGEGGSMQKF 342
Cdd:cd05675 319 VLDTLDKLLG----DPD---------VSVEAVHLEPATESPLDSPLVDAMEAAVQAvDPGApvvpYMSPGGTDAKYFRRL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1821508169 343 GIPAFYFGP-------GDGPLAHTPKESVSVSEIKTAVKALFHLVD 381
Cdd:cd05675 386 GIPGYGFAPlflppelDYTGLFHGVDERVPVESLYFGVRFLDRLVK 431
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
17-369 |
4.11e-18 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349901 [Multi-domain] Cd Length: 389 Bit Score: 85.20 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 17 LVRVPSV---SGSPA----CLQVLETARDLIESTGVEADIRILF-PEAPNPVLLARTGRGKAgvteLMLSGHVDVVPPAG 88
Cdd:cd05650 10 LIRIPAVnpeSGGEGekekADYLEKKLREYGFYTLERYDAPDERgIIRPNIVAKIPGGNDKT----LWIISHLDTVPPGD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 89 M----EDPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGV--DGVLWLILSTDEETAAQ-GVVRALSCSDAPRPQ 161
Cdd:cd05650 86 LslweTDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGItpKYNFGLLFVADEEDGSEyGIQYLLNKFDLFKKD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 162 LCVIC----EPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVhakkRLPELLAGNAAA------GPA 231
Cdd:cd05650 166 DLIIVpdfgTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFAL----ELDELLHEKFDEkddlfnPPY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 232 SSSIDLVSGGAAENV--VPASASVTIDFRYqgvesaqVQCDRIEKILSEVRTDPDFPPVSTSLTVTgdwtaLSTDMTQPL 309
Cdd:cd05650 242 STFEPTKKEANVPNVntIPGYDVFYFDCRV-------LPTYKLDEVLKFVNKIISDFENSYGAGIT-----YEIVQKEQA 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 310 AQAA------VAALGESL----GHIPETTEMTGWGEGGSMQKFGIPAFYFGPGDgPLAHTPKESVSVSEI 369
Cdd:cd05650 310 PPATpedseiVVRLSKAIkkvrGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLD-ETAHQPNEYIRISHI 378
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
3-374 |
5.67e-17 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 81.37 E-value: 5.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 3 QDTLEQRAVLWTQALVRVPSVSGSPaclqvlETARDLIESTGVEADIRILFPEAPNPVLLartgrgkaGVTELMLSGHVD 82
Cdd:PRK00466 5 KELVKQKAKELLLDLLSIYTPSGNE------TNATKFFEKISNELNLKLEILPDSNSFIL--------GEGDILLASHVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 83 VVPpaGMEDPwsaRIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVDgVLWLILStDEETAAQGVVRALSCSDapRPQL 162
Cdd:PRK00466 71 TVP--GYIEP---KIEGEVIYGRGAVDAKGPLISMIIAAWLLNEKGIK-VMVSGLA-DEESTSIGAKELVSKGF--NFKH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 163 CVICEPT-GLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGInaieaaalfIVHAKKRLPELLAGNAAAGPASSSIDLVSGG 241
Cdd:PRK00466 142 IIVGEPSnGTDIVVEYRGSIQLDIMCEGTPEHSSSAKSNL---------IVDISKKIIEVYKQPENYDKPSIVPTIIRAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 242 AAENVVPASASVTIDFRYQGVESAqvqcdriEKILSEVRTDpdFPpvSTSLTVTGDWTALSTDMTQPLAQAAVAALGESl 321
Cdd:PRK00466 213 ESYNVTPAKLYLHFDVRYAINNKR-------DDLISEIKDK--FQ--ECGLKIVDETPPVKVSINNPVVKALMRALLKQ- 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1821508169 322 GHIPETTEMTGWGEGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVK 374
Cdd:PRK00466 281 NIKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLEHTNQEKITLDEIYIAVK 333
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
7-369 |
2.01e-15 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 77.36 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 7 EQRAVLWT-QALVRVPSVSGSPACL-QVLETARDLIESTGVEADiRILFPEAPNPVLLAR-TGRGKAgvtELMLSGHVDV 83
Cdd:PRK06133 35 EQPAYLDTlKELVSIESGSGDAEGLkQVAALLAERLKALGAKVE-RAPTPPSAGDMVVATfKGTGKR---RIMLIAHMDT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 84 VPPAGMEDPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVD--GVLWLILSTDEETAAQGvVRALSCSDAPRPQ 161
Cdd:PRK06133 111 VYLPGMLAKQPFRIDGDRAYGPGIADDKGGVAVILHALKILQQLGFKdyGTLTVLFNPDEETGSPG-SRELIAELAAQHD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 162 LCVICEPTGLC--VRSAHRGDCWIRVDFTGKSAHS-SRPHLGINA-IEAAalfivHAKKRLPELlaGNAAAGpASSSIDL 237
Cdd:PRK06133 190 VVFSCEPGRAKdaLTLATSGIATALLEVKGKASHAgAAPELGRNAlYELA-----HQLLQLRDL--GDPAKG-TTLNWTV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 238 VSGGAAENVVPASASVTIDFRYQGVESAqvqcDRIEKILSEVRTDPDFPPVSTSLTVTGDWTAL-STDMTQPLAQAAVAA 316
Cdd:PRK06133 262 AKAGTNRNVIPASASAQADVRYLDPAEF----DRLEADLQEKVKNKLVPDTEVTLRFERGRPPLeANAASRALAEHAQGI 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821508169 317 LGEsLGHIPETTEM-TGWGEGGS----------MQKFGIPAFYfgpgdgplAHTPKESVSVSEI 369
Cdd:PRK06133 338 YGE-LGRRLEPIDMgTGGGTDAAfaagsgkaavLEGFGLVGFG--------AHSNDEYIELNSI 392
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
75-325 |
2.32e-15 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 76.93 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 75 LMLSGHVDVVPPAGMEDPWSARIEGDRMHGRGTTDMKSGAAC---ALTTF--CE-AARQGVDgvlwLILSTDEET---AA 145
Cdd:PRK07338 95 VLLTGHMDTVFPADHPFQTLSWLDDGTLNGPGVADMKGGIVVmlaALLAFerSPlADKLGYD----VLINPDEEIgspAS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 146 QGVVRALscsdAPRPQLCVICEPT---GLCVrSAHRGDCWIRVDFTGKSAHSSR-PHLGINAIEAAALFIVhAKKRLPEL 221
Cdd:PRK07338 171 APLLAEL----ARGKHAALTYEPAlpdGTLA-GARKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAELAL-ALHALNGQ 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 222 LAG---NAAAgpasssidlVSGGAAENVVPASASVTIDFRYQGVESAQVQCDRIEKILSEVRTDPDFppvstSLTVTGDW 298
Cdd:PRK07338 245 RDGvtvNVAK---------IDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHGV-----SLHLHGGF 310
|
250 260 270
....*....|....*....|....*....|...
gi 1821508169 299 T--ALSTDMTQP----LAQAAVAALGESLGHIP 325
Cdd:PRK07338 311 GrpPKPIDAAQQrlfeAVQACGAALGLTIDWKD 343
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
15-382 |
5.87e-14 |
|
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: 72.75 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 15 QALVRVPSVSGSPA----CLQVLETARDLIESTGveADIRILFPEAPNPVLLARTGRGKAGVTeLMLSGHVDVVPPAGME 90
Cdd:cd03893 5 AELVAIPSVSAQPDrreeLRRAAEWLADLLRRLG--FTVEIVDTSNGAPVVFAEFPGAPGAPT-VLLYGHYDVQPAGDED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 91 ----DPWSARIEGDRMHGRGTTDMKSGAACALTTFcEAARQGVDGV---LWLILSTDEETAAQGVVR------------A 151
Cdd:cd03893 82 gwdsDPFELTERDGRLYGRGAADDKGPILAHLAAL-RALMQQGGDLpvnVKFIIEGEEESGSPSLDQlveahrdllaadA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 152 LSCSDAPRPQLCVICEPTGLcvrsahRG--DCWIRVDFTGKSAHSSrpHLGINAIEAAALFI-----VHAKK-------- 216
Cdd:cd03893 161 IVISDSTWVGQEQPTLTYGL------RGnaNFDVEVKGLDHDLHSG--LYGGVVPDPMTALAqllasLRDETgrilvpgl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 217 -----RLPE--------LLAGNAAAG-------------PASSSIDLVSGGAAE---NVVPASASVTIDFRY---QGVES 264
Cdd:cd03893 233 ydavrELPEeefrldagVLEEVEIIGgttgsvaerlwtrPALTVLGIDGGFPGEgskTVIPPRARAKISIRLvpgQDPEE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 265 AQVQcdrIEKILSEVRtdpdFPPVSTSLTVTGDWTALSTDMTQPLAQAAVAALGESLGHIPETTEMtgwgeGGSM----- 339
Cdd:cd03893 313 ASRL---LEAHLEKHA----PSGAKVTVSYVEGGMPWRSDPSDPAYQAAKDALRTAYGVEPPLTRE-----GGSIpfisv 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1821508169 340 --QKFGIPAFYFGPGD-GPLAHTPKESVSVSEIKTAVKALFHLVDR 382
Cdd:cd03893 381 lqEFPQAPVLLIGVGDpDDNAHSPNESLRLGNYKEGTQAEAALLYS 426
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
11-258 |
1.11e-13 |
|
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: 71.82 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 11 VLWTQALVRVPSVSGSPACLQVLETARDLIESTGVEADiRILFPEAPNPV--------LLARTGRGKAGVTeLMLSGHVD 82
Cdd:cd02697 6 VRFLQKLVRVPTDTPPGNNAPHAERTAALLQGFGFEAE-RHPVPEAEVRAygmesitnLIVRRRYGDGGRT-VALNAHGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 83 VVPPAG--MEDPWSARIEGDRMHGRGTTDMKSGAAC------ALTTFCEAARQGVDgvlwLILSTDEETAAQGVVRALSC 154
Cdd:cd02697 84 VVPPGDgwTRDPYGAVVEDGVMYGRAAAVSKSDFASftfavrALESLGAPLRGAVE----LHFTYDEEFGGELGPGWLLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 155 SDAPRPQLcVICEPTGLCVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAAlfivhakKRLPELLAGNAAAGPASSS 234
Cdd:cd02697 160 QGLTKPDL-LIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAV-------AILNALYALNAQYRQVSSQ 231
|
250 260 270
....*....|....*....|....*....|....
gi 1821508169 235 ID----------LVSGGAAENVVPASASVTIDFR 258
Cdd:cd02697 232 VEgithpylnvgRIEGGTNTNVVPGKVTFKLDRR 265
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
17-383 |
2.12e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 71.19 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 17 LVRVPSVSGSPACLQVLETARDLIESTGV-EADIRIlFPEAPNPVLLARTGRGKAGVTELMLSGHVDVV--PPAGME-DP 92
Cdd:PRK09133 46 LIEINTTASTGSTTPAAEAMAARLKAAGFaDADIEV-TGPYPRKGNLVARLRGTDPKKPILLLAHMDVVeaKREDWTrDP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 93 WSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVDGV--LWLILSTDEETAAQGVVRALScsdAPRPQLC----VIC 166
Cdd:PRK09133 125 FKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKrdIILALTGDEEGTPMNGVAWLA---ENHRDLIdaefALN 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 167 EPTGLCVRSAHRGDCW-----------IRVDFTGKSAHSSRPHLGiNAIE--AAAL-------FIVH------------A 214
Cdd:PRK09133 202 EGGGGTLDEDGKPVLLtvqagektyadFRLEVTNPGGHSSRPTKD-NAIYrlAAALsrlaayrFPVMlndvtrayfkqsA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 215 KKRLPEL------LAGN----AAAGPASSSID------------LVSGGAAENVVPASASVTIDFR-YQGVESAQVQcDR 271
Cdd:PRK09133 281 AIETGPLaaamraFAANpadeAAIALLSADPSynamlrttcvatMLEGGHAENALPQRATANVNCRiFPGDTIEAVR-AT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 272 IEKILSE----VRTDPDFPPVSTSltvtgdwtALSTDMTQPlAQAAVAALGESLGHIPetTEMTGWGEGGSMQKFGIPAF 347
Cdd:PRK09133 360 LKQVVADpaikITRIGDPSPSPAS--------PLRPDIMKA-VEKLTAAMWPGVPVIP--SMSTGATDGRYLRAAGIPTY 428
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1821508169 348 ----YFGPGDGPLAHTPKESVSVSEIKTAVKALFHLVDRL 383
Cdd:PRK09133 429 gvsgLFGDPDDTFAHGLNERIPVASFYEGRDFLYELVKDL 468
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
57-218 |
2.75e-13 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 70.65 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 57 PNpvLLARTGrGKAGVTELMLSGHVDVVPPAGME----DPWSARIEGDRMHGRGTTD----MKSGAACALTTFCEAARQG 128
Cdd:PRK13983 64 PN--IVAKIP-GGDGKRTLWIISHMDVVPPGDLSlwetDPFKPVVKDGKIYGRGSEDngqgIVSSLLALKALMDLGIRPK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 129 VDgvLWLILSTDEETAA----QGVVRAlscsdapRPQL-----CVIC----EPTGLCVRSAHRGDCWIRVDFTGKSAHSS 195
Cdd:PRK13983 141 YN--LGLAFVSDEETGSkygiQYLLKK-------HPELfkkddLILVpdagNPDGSFIEIAEKSILWLKFTVKGKQCHAS 211
|
170 180
....*....|....*....|...
gi 1821508169 196 RPHLGINAIEAAALFIVHAKKRL 218
Cdd:PRK13983 212 TPENGINAHRAAADFALELDEAL 234
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
185-372 |
6.39e-13 |
|
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: 69.30 E-value: 6.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 185 VDFTGKSAHSSRPHLGINAIEAAALFIVhakkRLPELLAGNA-AAGPASSSIDLVSGGAAENVVPASASVTIDFRYQGVE 263
Cdd:TIGR01891 175 VTIHGKGAHAARPHLGRDALDAAAQLVV----ALQQIVSRNVdPSRPAVVSVGIIEAGGAPNVIPDKASMSGTVRSLDPE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 264 SAQVQCDRIEKILS----------EVRTDPDFPPVStsltvtgdwtaLSTDMTQPLAQAAVAALG-ESLGHIPETTeMTG 332
Cdd:TIGR01891 251 VRDQIIDRIERIVEgaaamygakvELNYDRGLPAVT-----------NDPALTQILKEVARHVVGpENVAEDPEVT-MGS 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1821508169 333 WGEGGSMQK-----FGIPAFYFGPGDGPLAHTPKESVSVSEIKTA 372
Cdd:TIGR01891 319 EDFAYYSQKvpgafFFLGIGNEGTGLSHPLHHPRFDIDEEALALG 363
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
4-374 |
4.48e-11 |
|
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: 64.19 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 4 DTLEQRAVLWTQALVRVPSVSGSP--------ACLQVLETARDLIESTGVEA-DIrilfpeaPNPVLLARTGRGKagvTE 74
Cdd:cd03888 4 DKYKDEILEDLKELVAIPSVRDEAtegapfgeGPRKALDKFLDLAKRLGFKTkNI-------DNYAGYAEYGEGE---EV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 75 LMLSGHVDVVPP-AGME-DPWSARIEGDRMHGRGTTDMKSGA-AC--ALTTFCEAarqgvdGVLW-----LILSTDEET- 143
Cdd:cd03888 74 LGILGHLDVVPAgEGWTtDPFKPVIKDGKLYGRGTIDDKGPTiAAlyALKILKDL------GLPLkkkirLIFGTDEETg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 144 ----------------------------AAQGVVRAL-----SCSDAPR-------------PQLC--VICEPTGLCVRS 175
Cdd:cd03888 148 wkciehyfeheeypdfgftpdaefpvinGEKGIVTVDltfkiDDDKGYRlisikggeatnmvPDKAeaVIPGKDKEELAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 176 AHRGDCWIRVDF---------TGKSAHSSRPHLGINAIEAAALFIV-----HAKKRLPELLAGNAA-------------- 227
Cdd:cd03888 228 SAATDLKGNIEIddggveltvTGKSAHASAPEKGVNAITLLAKFLAelnkdGNDKDFIKFLAKNLHedyngkklginfed 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 228 --AGPASSSIDLVsggaaeNVVPASASVTIDFRY-QGVESAQVQcDRIEKILSevrtdpdfppvSTSLTVTGD--WTALS 302
Cdd:cd03888 308 evMGELTLNPGII------TLDDGKLELGLNVRYpVGTSAEDII-KQIEEALE-----------KYGVEVEGHkhQKPLY 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821508169 303 TDMTQPLAQAAVAALGESLGHIPETTEMTGWGEGGSMQK---FGiPAFyfgPGDGPLAHTPKESVSVSEIKTAVK 374
Cdd:cd03888 370 VPKDSPLVKTLLKVYEEQTGKEGEPVAIGGGTYARELPNgvaFG-PEF---PGQKDTMHQANEFIPIDDLIKALA 440
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
183-380 |
4.93e-11 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 63.77 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 183 IRVDFTGKSAHSSRPHLGINAIEAAAlFIVHAkkrLPELLA-GNAAAGPASSSIDLVSGGAAENVVPASASVTIDFRYQG 261
Cdd:cd03886 174 FEITVKGKGGHGASPHLGVDPIVAAA-QIVLA---LQTVVSrELDPLEPAVVTVGKFHAGTAFNVIPDTAVLEGTIRTFD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 262 VESAQVQCDRIEKILS----------EVRTDPDFPPVstsltvtgdwtALSTDMTQPLAQAAVAALGESLGHIPettEMT 331
Cdd:cd03886 250 PEVREALEARIKRLAEgiaaaygatvELEYGYGYPAV-----------INDPELTELVREAAKELLGEEAVVEP---EPV 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821508169 332 GWGEGGS--MQKfgIPAFYF----GPGDG--PLAHTPKESVSVSEIKTAVKALFHLV 380
Cdd:cd03886 316 MGSEDFAyyLEK--VPGAFFwlgaGEPDGenPGLHSPTFDFDEDALPIGAALLAELA 370
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
37-376 |
5.57e-11 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 63.52 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 37 RDLIESTGVEADIRILFPEAPNpVLLARTGRGKAGVTELMLSGHVDVVPPAGME----DPWSARIEGDRMHGRGTTDMKS 112
Cdd:PRK08596 43 AEFLRKLGFSVDKWDVYPNDPN-VVGVKKGTESDAYKSLIINGHMDVAEVSADEawetNPFEPTIKDGWLYGRGAADMKG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 113 GAAC---ALTTFCEAARQgVDGVLWLILSTDEETAAQGVVRAlsCSDAPRPQLCVICEPTGLCVRSahRGDC---WIRVd 186
Cdd:PRK08596 122 GLAGalfAIQLLHEAGIE-LPGDLIFQSVIGEEVGEAGTLQC--CERGYDADFAVVVDTSDLHMQG--QGGVitgWITV- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 187 ftgKSA------------HSSRPHLGINAIEAAALFIVHAK---------KRLPELLAGNAAAGPAsssidLVSGGAAEN 245
Cdd:PRK08596 196 ---KSPqtfhdgtrrqmiHAGGGLFGASAIEKMMKIIQSLQelerhwavmKSYPGFPPGTNTINPA-----VIEGGRHAA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 246 VVPASASVTIDFRYQGVESAQVQCDRIEKILSEV-RTDP---DFPPVST---------------SLTVTGDWTALSTdmt 306
Cdd:PRK08596 268 FIADECRLWITVHFYPNETYEQVIKEIEEYIGKVaAADPwlrENPPQFKwggesmiedrgeifpSLEIDSEHPAVKT--- 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 307 qpLAQAAVAALGESLGHIPETTeMTgwgEGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKAL 376
Cdd:PRK08596 345 --LSSAHESVLSKNAILDMSTT-VT---DGGWFAEFGIPAVIYGPGTLEEAHSVNEKVEIEQLIEYTKVI 408
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
177-260 |
2.38e-10 |
|
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349939 [Multi-domain] Cd Length: 365 Bit Score: 61.53 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 177 HRGDCWIRVDFTGKSAHSSRPHLGINAIEAAAlFIVHAKKRL---PELlagnaaagPASSSI-DLVSGGAAENVVPASAS 252
Cdd:cd08018 164 HGASTFLEGTIKGKQAHGARPHLGINAIEAAS-AIVNAVNAIhldPNI--------PWSVKMtKLQAGGEATNIIPDKAK 234
|
....*...
gi 1821508169 253 VTIDFRYQ 260
Cdd:cd08018 235 FALDLRAQ 242
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
61-169 |
2.38e-09 |
|
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: 56.67 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 61 LLARTGRGKAGVTeLMLSGHVDVVPpAGMEDPWS-----ARIEGDRMHGRGTTDMKSGAACALTTFC--EAARQGVDGVL 133
Cdd:cd18669 2 VIARYGGGGGGKR-VLLGAHIDVVP-AGEGDPRDppffvDTVEEGRLYGRGALDDKGGVAAALEALKllKENGFKLKGTV 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1821508169 134 WLILSTDEE---TAAQGVVRALSCSDAPRPQLCVICEPT 169
Cdd:cd18669 80 VVAFTPDEEvgsGAGKGLLSKDALEEDLKVDYLFVGDAT 118
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
17-111 |
6.04e-09 |
|
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: 57.61 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 17 LVRVPSVSGSPA----CLQVLETARDLIESTGVEADIRILFPEAPN--------PVLLARTGRGKAGVTeLMLSGHVDVv 84
Cdd:cd05676 19 AVAIQSVSADPEkrpeLIRMMEWAAERLEKLGFKVELVDIGTQTLPdgeelplpPVLLGRLGSDPSKKT-VLIYGHLDV- 96
|
90 100 110
....*....|....*....|....*....|..
gi 1821508169 85 PPAGMEDPWSAR----IEGD-RMHGRGTTDMK 111
Cdd:cd05676 97 QPAKLEDGWDTDpfelTEKDgKLYGRGSTDDK 128
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
182-278 |
9.10e-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: 9.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 182 WIRVDFTGKSAHSSRPHLGINAIEAAALFIVHakkrLPELLAGNAAA-GPASSSIDLVSGGAAENVVPASASVTIDFRYQ 260
Cdd:cd08019 170 IFKIEVKGKGGHGSMPHQGIDAVLAAASIVMN----LQSIVSREIDPlEPVVVTVGKLNSGTRFNVIADEAKIEGTLRTF 245
|
90
....*....|....*...
gi 1821508169 261 GVESAQVQCDRIEKILSE 278
Cdd:cd08019 246 NPETREKTPEIIERIAKH 263
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
37-143 |
1.93e-08 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 55.94 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 37 RDLIESTGVEADIrilFPEAPNPVLLARTGRGKAgvtELMLSGHVDVVPPAGME---DPWSARIEGDRMHGRGTTDMKSG 113
Cdd:PRK08554 34 KDTLESWGIESEL---IEKDGYYAVYGEIGEGKP---KLLFMAHFDVVPVNPEEwntEPFKLTVKGDKAYGRGSADDKGN 107
|
90 100 110
....*....|....*....|....*....|
gi 1821508169 114 AACALTTFCEAARQGVDGVLWLILSTDEET 143
Cdd:PRK08554 108 VASVMLALKELSKEPLNGKVIFAFTGDEEI 137
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
16-126 |
1.43e-07 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 52.98 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 16 ALVRVPSVSGSPA----CLQVLETARDLIESTGVEADIRilfPEAPNPVLLARTGRGKAGVTELMLSGHVDVVPPAGME- 90
Cdd:PRK09104 25 ALLRIPSISTDPAyaadCRKAADWLVADLASLGFEASVR---DTPGHPMVVAHHEGPTGDAPHVLFYGHYDVQPVDPLDl 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1821508169 91 ---DPWSARIE-----GDRMHGRGTTDMKSgaacALTTFCEAAR 126
Cdd:PRK09104 102 wesPPFEPRIKetpdgRKVIVARGASDDKG----QLMTFVEACR 141
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
63-366 |
3.91e-07 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 51.71 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 63 ARTGRGKAGVTELMLSGHVDVVPPAGMEDPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVDGVL--WLILSTD 140
Cdd:PRK07473 66 ARFPHPRQGEPGILIAGHMDTVHPVGTLEKLPWRREGNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLpiTVLFTPD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 141 EETAAQGvVRALSCSDAPRPQLCVICEPtGLCVRSAHRGDCWI---RVDFTGKSAHS-SRPHLGINAIEAAAlfivhakK 216
Cdd:PRK07473 146 EEVGTPS-TRDLIEAEAARNKYVLVPEP-GRPDNGVVTGRYAIarfNLEATGRPSHAgATLSEGRSAIREMA-------R 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 217 RLPELLAGNAAagPASSSIDLVSGGAAENVVPASAsvtidfRYQGVESAQVQCDR---IEKILSEVRTDPDfppvsTSLT 293
Cdd:PRK07473 217 QILAIDAMTTE--DCTFSVGIVHGGQWVNCVATTC------TGEALSMAKRQADLdrgVARMLALSGTEDD-----VTFT 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 294 VTGD-----WTALSTDMT-QPLAQAAVAALGESLGHipettemtGWGEGGSMQKF----GIPAFyfgPGDGPL---AHTP 360
Cdd:PRK07473 284 VTRGvtrpvWEPDAGTMAlYEKARAIAGQLGLSLPH--------GSAGGGSDGNFtgamGIPTL---DGLGVRgadYHTL 352
|
....*.
gi 1821508169 361 KESVSV 366
Cdd:PRK07473 353 NEHIEV 358
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
75-380 |
4.14e-07 |
|
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: 51.87 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 75 LMLSGHVDVVP-PAGMED-----PWSARIEGDRMHGRGTTDMKS------------------------------------ 112
Cdd:cd05674 72 LLLMAHQDVVPvNPETEDqwthpPFSGHYDGGYIWGRGALDDKNsligileavelllkrgfkprrtiilafghdeevgge 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 113 -GAAcALTTFCEaARQGVDGVLWLIlstDE-----ETAAQGVVRALscsdaprpqlcviceptglcVRSAHRG--DCWIR 184
Cdd:cd05674 152 rGAG-AIAELLL-ERYGVDGLAAIL---DEggavlEGVFLGVPFAL--------------------PGVAEKGymDVEIT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 185 VDftGKSAHSSRP--HLGIN-------AIEA-------------------------------AALFIVHAKKRLPELLAG 224
Cdd:cd05674 207 VH--TPGGHSSVPpkHTGIGilseavaALEAnpfppkltpgnpyygmlqclaehsplpprslKSNLWLASPLLKALLASE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 225 NAAAGPA-------SSSIDLVSGGAAENVVPASASVTIDFRYQGVESAQVQCDRIEKILSEVR----------------- 280
Cdd:cd05674 285 LLSTSPLtrallrtTQAVDIINGGVKINALPETATATVNHRIAPGSSVEEVLEHVKNLIADIAvkyglglsafggdviys 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 281 -------TDPDFPPVSTSLTVTGD-WtalstDMTQPLAQAAVAALGESLghIPETTEMTG-------WGEGGSMQKFGip 345
Cdd:cd05674 365 tngtkllTSLLSPEPSPVSSTSSPvW-----QLLAGTIRQVFEQFGEDL--VVAPGIMTGntdtrhyWNLTKNIYRFT-- 435
|
410 420 430
....*....|....*....|....*....|....*
gi 1821508169 346 AFYFGPGDGPLAHTPKESVSVSEIKTAVKALFHLV 380
Cdd:cd05674 436 PIRLNPEDLGRIHGVNERISIDDYLETVAFYYQLI 470
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
75-381 |
1.44e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 49.85 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 75 LMLSGHVDVVPPAGME---DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGV----DGVLwlILSTDEE----- 142
Cdd:PRK07906 68 LLVHGHLDVVPAEAADwsvHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRrpprDLVF--AFVADEEaggty 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 143 ----------------TAAQGVVRALSCSDAPRPQLCVIceptglcvRSAHRGDCWIRVDFTGKSAHSSRPHlGINAIE- 205
Cdd:PRK07906 146 gahwlvdnhpelfegvTEAISEVGGFSLTVPGRDRLYLI--------ETAEKGLAWMRLTARGRAGHGSMVN-DDNAVTr 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 206 -AAAL-------FIVHAKKRLPELLAGNAAA-----------------GPASSSID----------LVSGGAAENVVPAS 250
Cdd:PRK07906 217 lAEAVarigrhrWPLVLTPTVRAFLDGVAELtglefdpddpdallaklGPAARMVGatlrntanptMLKAGYKVNVIPGT 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 251 ASVTIDFRY-QGVEsaqvqcdriEKILSEVR--TDPDfppvstsltVTGDWT----ALSTDMTQPLAQAAVAALgesLGH 323
Cdd:PRK07906 297 AEAVVDGRFlPGRE---------EEFLATVDelLGPD---------VEREWVhrdpALETPFDGPLVDAMNAAL---LAE 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821508169 324 IPETTE----MTGWGEGGSMQKFGIPAFYFGPGDGP-------LAHTPKESVSVSEIKTAVKALFHLVD 381
Cdd:PRK07906 356 DPGARVvpymLSGGTDAKAFSRLGIRCYGFAPLRLPpdldfaaLFHGVDERVPVDALRFGVRVLDRFLR 424
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
183-373 |
1.85e-06 |
|
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: 49.37 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 183 IRVDFTGKSAHSS-RPHLGINAIEAAALFIVHAK-KRLPELLAGNaaagpasssIDLVSGGAAENVVPASASVTIDFRYQ 260
Cdd:cd05683 181 INAKIYGKTAHAGtSPEKGISAINIAAKAISNMKlGRIDEETTAN---------IGKFQGGTATNIVTDEVNIEAEARSL 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 261 GVESAQVQCDRIEKIL----------SEVRTDPDFPPVSTSltvtgdwtalSTDMTQPLAQAAVAALGeslghIPETTEM 330
Cdd:cd05683 252 DEEKLDAQVKHMKETFettakekgahAEVEVETSYPGFKIN----------EDEEVVKLAKRAANNLG-----LEINTTY 316
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1821508169 331 TGWGEGGS-MQKFGIPAFYFGPGDGPlAHTPKESVSVSEI-KTAV 373
Cdd:cd05683 317 SGGGSDANiINGLGIPTVNLGIGYEN-IHTTNERIPIEDLyDTAV 360
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
183-319 |
2.30e-06 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the 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. 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 in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349914 [Multi-domain] Cd Length: 399 Bit Score: 49.26 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 183 IRVDFTGKSAHSSRPHLGINAIEAAALFIVhakkRLPELLAGNAAAG-PASSSIDLVSGGAAENVVPASASVTIDFRYQG 261
Cdd:cd05664 184 LDITIFGRGGHGSMPHLTIDPVVMAASIVT----RLQTIVSREVDPQeFAVVTVGSIQAGSAENIIPDEAELKLNVRTFD 259
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821508169 262 VESAQVQCDRIEKI------LSEVRTDPDFPPVSTSLTVTGDWTAlstdmTQPLAQAAVAALGE 319
Cdd:cd05664 260 PEVREKVLNAIKRIvraecaASGAPKPPEFTYTDSFPATVNDEDA-----TARLAAAFREYFGE 318
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
13-111 |
2.32e-06 |
|
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: 49.26 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 13 WTQALVRVPSVSGSPAclQVLETA---RDLIESTGVEADIrilFPEAPNPVLLARTGRGKAGVteLMLSGHVDVVPPAGM 89
Cdd:cd05681 4 DLRDLLKIPSVSAQGR--GIPETAdflKEFLRRLGAEVEI---FETDGNPIVYAEFNSGDAKT--LLFYNHYDVQPAEPL 76
|
90 100
....*....|....*....|....*.
gi 1821508169 90 E----DPWSARIEGDRMHGRGTTDMK 111
Cdd:cd05681 77 ElwtsDPFELTIRNGKLYARGVADDK 102
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
19-111 |
2.36e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 49.37 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 19 RVPSVSGSPACLQvlETA---RDLIESTGVEADIRilfPEAPNPVLLARTGRGkaGVTELMLSGHVDVVPPAGME----D 91
Cdd:PRK06446 13 KKPSISATGEGIE--ETAnylKDTMEKLGIKANIE---RTKGHPVVYGEINVG--AKKTLLIYNHYDVQPVDPLSewkrD 85
|
90 100
....*....|....*....|
gi 1821508169 92 PWSARIEGDRMHGRGTTDMK 111
Cdd:PRK06446 86 PFSATIENGRIYARGASDNK 105
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
75-360 |
2.46e-06 |
|
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: 49.19 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 75 LMLSGHVDVVpPAGME----DPWSARIEGD-RMHGRGTTDMKsgaaCALTTFCEAARQ-GVDGVLW-----LILSTDEET 143
Cdd:cd05646 67 ILLNSHTDVV-PVFEEkwthDPFSAHKDEDgNIYARGAQDMK----CVGIQYLEAIRRlKASGFKPkrtihLSFVPDEEI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 144 AAQGVVRALSCSDAPRpQLCV-ICEPTGLC-------VRSAHRGDCWIRVDFTGKSAHSSR---------PHLGINAIEA 206
Cdd:cd05646 142 GGHDGMEKFVKTEEFK-KLNVgFALDEGLAspteeyrVFYGERSPWWVVITAPGTPGHGSKllentagekLRKVIESIME 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 207 aalFIVHAKKRLPEllAGNAAAGPASSS-IDLVSGGAAENVVPASASVTIDFRYqgveSAQVQCDRIEKILSEVRTDP-- 283
Cdd:cd05646 221 ---FRESQKQRLKS--NPNLTLGDVTTVnLTMLKGGVQMNVVPSEAEAGFDLRI----PPTVDLEEFEKQIDEWCAEAgr 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 284 ----DFPPVSTSLTVTgdwtalSTDMTQPLAQA---AVAALGESLghIPETteMTGWGEGGSMQKFGIPAFYFgpgdGPL 356
Cdd:cd05646 292 gvtyEFEQKSPEKDPT------SLDDSNPWWAAfkkAVKEMGLKL--KPEI--FPAATDSRYIRALGIPALGF----SPM 357
|
....
gi 1821508169 357 AHTP 360
Cdd:cd05646 358 NNTP 361
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
32-217 |
2.94e-06 |
|
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: 48.99 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 32 VLETARDLIESTGVEADI-RILFPEAPNPVLLARTGRGKAGVTELMLSgHVDVVP--PAGME-DPWSARIEGDRMHGRGT 107
Cdd:cd08012 38 VLEALTPYSTENGGPLVIdHVSYVKGRGNIIVEYPGTVDGKTVSFVGS-HMDVVTanPETWEfDPFSLSIDGDKLYGRGT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 108 TDMKSGAACALTTFCEAARQ------------------------GVDGvlwLILSTDEETAAQGVVRALSCSDAprpQLC 163
Cdd:cd08012 117 TDCLGHVALVTELFRQLATEkpalkrtvvavfianeenseipgvGVDA---LVKSGLLDNLKSGPLYWVDSADS---QPC 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1821508169 164 VicePTGlcvrsahrGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAKKR 217
Cdd:cd08012 191 I---GTG--------GMVTWKLTATGKLFHSGLPHKAINALELVMEALAEIQKR 233
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
1-153 |
9.80e-06 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 47.54 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 1 MPQDTLEQRAVLWTQALVRVPSVSGSPACLQVLETARDLIESTGVeadirilFPEAPNPVLLARTG-------------R 67
Cdd:COG4187 1 MKKWQTKEQLEELLCELVSIPSVTGTEGEKEVAEFIYEKLSELPY-------FQENPEHLGLHPLPddplgrknvtalvK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 68 GKAGVTE-LMLSGHVDVVppaGMED-----------------------PWSARIE---GDRMHGRGTTDMKSGAACALTT 120
Cdd:COG4187 74 GKGESKKtVILISHFDVV---DVEDygslkplafdpeeltealkeiklPEDVRKDlesGEWLFGRGTMDMKAGLALHLAL 150
|
170 180 190
....*....|....*....|....*....|....
gi 1821508169 121 FCEAARQG-VDGVLWLILSTDEETAAQGVVRALS 153
Cdd:COG4187 151 LEEASENEeFPGNLLLLAVPDEEVNSAGMRAAVP 184
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
183-295 |
1.53e-05 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 46.50 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 183 IRVDFTGKSAHSSRPHLGINAIEAAALFIVHAK----KRLPELlagnaaaGPASSSIDLVSGGAAENVVPASASVTIDFR 258
Cdd:cd08021 184 FDITIKGKGGHGSMPHETVDPIVIAAQIVTALQtivsRRVDPL-------DPAVVTIGTFQGGTSFNVIPDTVELKGTVR 256
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1821508169 259 YQGVESAQVQCDRIEKILS----------EVRTDPDFPPVSTSLTVT 295
Cdd:cd08021 257 TFDEEVREQVPKRIERIVKgiceaygasyELEYQPGYPVVYNDPEVT 303
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
79-268 |
1.56e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 46.61 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 79 GHVDVVPPAGME----DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVD--GVLWLILSTDEETAAQGVVRAL 152
Cdd:PRK07205 82 CHLDVVPEGDLSdwqtPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQfnKRIRFIFGTDEETLWRCMNRYN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 153 SCSDAPrpqlcviceptglcvrsahrgDCWIRVDftgksahSSRPhlginaieaaalfIVHAKKRLPELlagnAAAGPAS 232
Cdd:PRK07205 162 EVEEQA---------------------TMGFAPD-------SSFP-------------LTYAEKGLLQA----KLVGPGS 196
|
170 180 190
....*....|....*....|....*....|....*.
gi 1821508169 233 SSIDLVSGGAAeNVVPASASvtidfrYQGVESAQVQ 268
Cdd:PRK07205 197 DQLELEVGQAF-NVVPAKAS------YQGPKLEAVK 225
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
60-145 |
1.88e-05 |
|
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: 45.11 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 60 VLLARTGRGKAGVteLMLSGHVDVVPpAGMEDPWS-----ARIEGDRMHGRGTTDMKSGAACALttfcEAARQGVD---- 130
Cdd:cd03873 2 LIARLGGGEGGKS--VALGAHLDVVP-AGEGDNRDppfaeDTEEEGRLYGRGALDDKGGVAAAL----EALKRLKEngfk 74
|
90
....*....|....*..
gi 1821508169 131 --GVLWLILSTDEETAA 145
Cdd:cd03873 75 pkGTIVVAFTADEEVGS 91
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
75-289 |
2.03e-05 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 46.48 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 75 LMLSGHVDVVPPA-GME-----DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGV--DGVLWLILSTDEET--- 143
Cdd:PRK08262 114 IVLMAHQDVVPVApGTEgdwthPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFqpRRTIYLAFGHDEEVggl 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 144 AAQGVVRALScSDAPRPQLCV-------------ICEPTGLcVRSAHRGDCWIRVDFTGKSAHSSRPHLGiNAIEAAALF 210
Cdd:PRK08262 194 GARAIAELLK-ERGVRLAFVLdeggaitegvlpgVKKPVAL-IGVAEKGYATLELTARATGGHSSMPPRQ-TAIGRLARA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 211 IVH-AKKRLP---------------------------------ELLAGNAAAGPASS-------SIDLVSGGAAENVVPA 249
Cdd:PRK08262 271 LTRlEDNPLPmrlrgpvaemfdtlapemsfaqrvvlanlwlfePLLLRVLAKSPETAamlrtttAPTMLKGSPKDNVLPQ 350
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1821508169 250 SASVTIDFRY---QGVESAQVQC------DRIEKILSEVRTDPdfPPVS 289
Cdd:PRK08262 351 RATATVNFRIlpgDSVESVLAHVrravadDRVEIEVLGGNSEP--SPVS 397
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
79-297 |
2.99e-05 |
|
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: 45.83 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 79 GHVDVVPPAG--MEDPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQGVD--GVLWLILSTDEET----------- 143
Cdd:TIGR01887 74 GHLDVVPAGDgwTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKlkKKIRFIFGTDEESgwkcidyyfeh 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 144 ------------------AAQGVV--------------------------------RALSCS--DAPRPQLCVICEPTGL 171
Cdd:TIGR01887 154 eempdigftpdaefpiiyGEKGITtleikfkddtegdvvlesfkageaynmvpdhaTAVISGkkLTEVEQLKFVFFIAKE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 172 CVRSAHRGDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAKkrlpelLAGNAAA----------------GPASSSI 235
Cdd:TIGR01887 234 LEGDFEVNDGTLTITLEGKSAHGSAPEKGINAATYLALFLAQLN------LAGGAKAflqflaeylhedhygeKLGIKFH 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 236 DLVSGGAAENV------VPASASVTIDFRYQGVESAQVQCDRIEKILSEVRT------------DPDFPPVSTSLTV--- 294
Cdd:TIGR01887 308 DDVSGDLTMNVgvidyeNAEAGLIGLNVRYPVGNDPDTMLKNELAKESGVVEvtlngylkplyvPKDDPLVQTLMKVyek 387
|
....
gi 1821508169 295 -TGD 297
Cdd:TIGR01887 388 qTGD 391
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
59-148 |
3.06e-05 |
|
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: 45.95 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 59 PVLLARTGRGKAGVTeLMLSGHVDVVPpaGME-------DPWSARIEGDRMHGRGTTDMKSGAACALTTFcEAARQGVDG 131
Cdd:cd05679 60 PFLIAERIEDPSLPT-LLIYGHGDVVP--GYEgrwrdgrDPWTVTVWGERWYGRGTADNKGQHSINMAAL-RQVLEARGG 135
|
90 100
....*....|....*....|.
gi 1821508169 132 VLW----LILSTDEETAAQGV 148
Cdd:cd05679 136 KLGfnvkFLIEMGEEMGSPGL 156
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
76-203 |
6.46e-05 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 45.03 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 76 MLSGHVDVVPPAGMEDPWSarieGDRMHGRGTTDMKSGAACALTTFCEAARQG-VDGVLWLILSTDEETAAQGVVRALsc 154
Cdd:cd05654 104 AFSEYVEELDEEVREDLLS----GEWLFGRGTMDMKSGLAVHLALLEQASEDEdFDGNLLLMAVPDEEVNSRGMRAAV-- 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 155 sdaprPQLCVICEPTGLCVRSAHRGDCWIR---------------------VDFTGKSAHSSRPHLGINA 203
Cdd:cd05654 178 -----PALLELKKKHDLEYKLAINSEPIFPqydgdqtryiytgsigkilpgFLCYGKETHVGEPFAGINA 242
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
79-143 |
1.55e-04 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 43.68 E-value: 1.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821508169 79 GHVDVVpPAG---MEDPWSARIEGDRMHGRGTTDMKS-GAAC--ALTTFCEAarqgvdGVLW-----LILSTDEET 143
Cdd:PRK07318 86 GHLDVV-PAGdgwDTDPYEPVIKDGKIYARGTSDDKGpTMAAyyALKIIKEL------GLPLskkvrFIVGTDEES 154
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
179-255 |
1.80e-04 |
|
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, 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: 349920 [Multi-domain] Cd Length: 367 Bit Score: 43.02 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 179 GDCWIRVDFTGKSAHSSRPHLGINAIEAAALFIVHAkkrlpELLAGNAAAGPASS--SIDLVSGGAAENVVPASASV--T 254
Cdd:cd05670 171 GTSELHIDFIGKSGHAAYPHNANDMVVAAANFVTQL-----QTIVSRNVDPIDGAvvTIGKIHAGTARNVIAGTAHLegT 245
|
.
gi 1821508169 255 I 255
Cdd:cd05670 246 I 246
|
|
| M20_Acy1L2 |
cd03887 |
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
183-276 |
2.59e-04 |
|
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: 42.56 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 183 IRVDFTGKSAH-SSRPHLGINAIEAAALFIVhakkrlpellagnaaagpassSIDL---------------VSGGAAENV 246
Cdd:cd03887 161 LRVEFHGKAAHaAAAPWEGINALDAAVLAYN---------------------NISAlrqqlkptvrvhgiiTEGGKAPNI 219
|
90 100 110
....*....|....*....|....*....|
gi 1821508169 247 VPASASVTIDFRYQGVESAQVQCDRIEKIL 276
Cdd:cd03887 220 IPDYAEAEFYVRAPTLKELEELTERVIACF 249
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
183-279 |
2.66e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349916 [Multi-domain] Cd Length: 373 Bit Score: 42.51 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 183 IRVdfTGKSAHSSRPHLGINAIEAAALFIVhakkRLPELLAGN-AAAGPASSSIDLVSGGAAENVVPASASVTIDFRYQg 261
Cdd:cd05666 177 ITI--RGKGGHAAMPHLGVDPIVAAAQLVQ----ALQTIVSRNvDPLDAAVVSVTQIHAGDAYNVIPDTAELRGTVRAF- 249
|
90
....*....|....*...
gi 1821508169 262 veSAQVQcDRIEKILSEV 279
Cdd:cd05666 250 --DPEVR-DLIEERIREI 264
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
17-147 |
2.82e-04 |
|
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: 42.72 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 17 LVRVPSVSGSPACLQVLETAR------DLIESTGveADIRILFPEAP--NPVLLAR---TGRGKAGVTeLMLSGHVDVVP 85
Cdd:cd05677 8 FIAFQTVSQSPTTENAEDSRRcaiflrQLFKKLG--ATNCLLLPSGPgtNPIVLATfsgNSSDAKRKR-ILFYGHYDVIP 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821508169 86 PAGME----DPWSARIEGDRMHGRGTTDMKSGAACALTTFCEAARQG--VDGVLWLIlSTDEETAAQG 147
Cdd:cd05677 85 AGETDgwdtDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQEGelDNDVVFLI-EGEEESGSPG 151
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
9-383 |
4.49e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 42.20 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 9 RAVLWTQALVRVPSVSGSPACLQVLETA----RDLIESTGVeADIRILfPEAPNPVLLARTgRGKAGVTELMLSGHVDVV 84
Cdd:PRK07907 19 RVRADLEELVRIPSVAADPFRREEVARSaewvADLLREAGF-DDVRVV-SADGAPAVIGTR-PAPPGAPTVLLYAHHDVQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 85 PPAGME----DPWSARIEGDRMHGRGTTDMKSGAACAL--------------TTFCEAA-RQGVDGVLWLILSTDEETAA 145
Cdd:PRK07907 96 PPGDPDawdsPPFELTERDGRLYGRGAADDKGGIAMHLaalralggdlpvgvTVFVEGEeEMGSPSLERLLAEHPDLLAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 146 QGVVRALSCSDAP-RPQLCViceptglcvrsAHRG--DCWIRVDFTGKSAHSSRphLGINAIEAAALFI----------- 211
Cdd:PRK07907 176 DVIVIADSGNWSVgVPALTT-----------SLRGnaDVVVTVRTLEHAVHSGQ--FGGAAPDALTALVrllatlhdedg 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 212 ------VHAKKR-----LPE--------LLAGNAAAGPASSS-------------IDLVSGGAAENVVPASASVTIDFRY 259
Cdd:PRK07907 243 nvavdgLDATEPwlgvdYDEerfradagVLDGVELIGTGSVAdrlwakpaitvigIDAPPVAGASNALPPSARARLSLRV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 260 Q-GVESAQVQcDRIEKILsEVRTdpdfpPVSTSLTVT--GDWTALSTDMTQPLAQAAVAALGESLGHIPETTemtgwGEG 336
Cdd:PRK07907 323 ApGQDAAEAQ-DALVAHL-EAHA-----PWGAHVTVErgDAGQPFAADASGPAYDAARAAMREAWGKDPVDM-----GMG 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821508169 337 GSmqkfgIP-------AF------YFGPGD-GPLAHTPKESVSVSEIKTAVKALFHLVDRL 383
Cdd:PRK07907 391 GS-----IPfiaelqeAFpqaeilVTGVEDpKTRAHSPNESVHLGELERAAVAEALLLARL 446
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
308-376 |
5.62e-04 |
|
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: 40.87 E-value: 5.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821508169 308 PLAQAAVAALGESLGHIPETTEMTGWGEGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKAL 376
Cdd:cd03873 132 PLVDALRKAAREVGGKPQRASVIGGGTDGRLFAELGIPGVTLGPPGDKGAHSPNEFLNLDDLEKATKVY 200
|
|
| PRK12893 |
PRK12893 |
Zn-dependent hydrolase; |
179-315 |
6.54e-04 |
|
Zn-dependent hydrolase;
Pssm-ID: 237250 [Multi-domain] Cd Length: 412 Bit Score: 41.40 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 179 GDCWIRVDFTGKSAHS-SRP-HLGINAIEAAALFIVH----AKKRLPELLA--GNAAAGPASSsidlvsggaaeNVVPAS 250
Cdd:PRK12893 213 GIRWLEVTVEGQAAHAgTTPmAMRRDALVAAARIILAveriAAALAPDGVAtvGRLRVEPNSR-----------NVIPGK 281
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821508169 251 ASVTIDFRYQGVESAQVQCDRIEKILSEVRTDpdfPPVSTSLTVTGDW--TALSTDMTQPLAQAAVA 315
Cdd:PRK12893 282 VVFTVDIRHPDDARLDAMEAALRAACAKIAAA---RGVQVTVETVWDFppVPFDPALVALVEAAAEA 345
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
92-254 |
6.84e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of uncharacterized 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: 349936 [Multi-domain] Cd Length: 371 Bit Score: 41.49 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 92 PWSARIEGdRMHGRGT---TDMKSGAACALTTFCEAARQGVDgvlwLILSTDEETAAQG---VVR--ALSCSDAprpQLC 163
Cdd:cd08014 76 PYRSTVPG-VMHACGHdahTAIALGAALVLAALEEELPGRVR----LIFQPAEETMPGGaldMIRagALDGVSA---IFA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 164 VICEPT----------GLCVRSAHRgdcwIRVDFTGKSAHSSRPHLGINAIEAAALFIVhakkRLPELLAGNA-AAGPAS 232
Cdd:cd08014 148 LHVDPRlpvgrvgvryGPITAAADS----LEIRIQGEGGHGARPHLTVDLVWAAAQVVT----DLPQAISRRIdPRSPVV 219
|
170 180
....*....|....*....|..
gi 1821508169 233 SSIDLVSGGAAENVVPASASVT 254
Cdd:cd08014 220 LTWGSIEGGRAPNVIPDSVELS 241
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
16-383 |
7.79e-04 |
|
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: 41.53 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 16 ALVRVPSVSGSPA----CLQVLETARDLIESTGVEaDIRIlFPEAPNPVLLA-RTGRGKAGVteLMLSGHVDVVPPAGME 90
Cdd:cd05680 6 ELLRIPSVSADPAhkgdVRRAAEWLADKLTEAGFE-HTEV-LPTGGHPLVYAeWLGAPGAPT--VLVYGHYDVQPPDPLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 91 ----DPWSARIEGDRMHGRGTTDMKSGAACALTTFCE--AARQGVDGVLWLILSTDEETAAQGV---VRA----LSC--- 154
Cdd:cd05680 82 lwtsPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAwlAVEGALPVNVKFLIEGEEEIGSPSLpafLEEnaerLAAdvv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 155 --SDAPR--PQLCVICepTGLcvrsahRGDCWIRVDFTGKSA--HSSRpHLGI--NAIEA-----AALFIVHAKKRLPEL 221
Cdd:cd05680 162 lvSDTSMwsPDTPTIT--YGL------RGLAYLEISVTGPNRdlHSGS-YGGAvpNPANAlarllASLHDEDGRVAIPGF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 222 LAG----------------------------NAAAGPAS----------SSIDL--VSGG----AAENVVPASASVTIDF 257
Cdd:cd05680 233 YDDvrpltdaereawaalpfdeaafkaslgvPALGGEAGyttlerlwarPTLDVngIWGGyqgeGSKTVIPSKAHAKISM 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 258 RYQGVESAQVQCDRIEKILSEVrtdpdfPPVSTSLTVTGDW--TALSTDMTQPLAQAAVAALGESLGHIPETTemtgwGE 335
Cdd:cd05680 313 RLVPGQDPDAIADLLEAHLRAH------APPGVTLSVKPLHggRPYLVPTDHPALQAAERALEEAFGKPPVFV-----RE 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821508169 336 GGSM-------QKFGIPAFYFG---PGDGPlaHTPKESVSVSEIKTAVKALFHLVDRL 383
Cdd:cd05680 382 GGSIpivalfeKVLGIPTVLMGfglPDDAI--HAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| M20_Acy1-like |
cd05667 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
183-380 |
8.20e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a 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: 349917 [Multi-domain] Cd Length: 403 Bit Score: 41.26 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 183 IRVDFTGKSAHSSRPHLGINAIEAAALFIVHAKKRLPELLagNAAAGPASSSIDLVSGGAAENVVPASASVTIDFRYQGV 262
Cdd:cd05667 198 FRITVKGKQTHGSRPWDGIDPIMASAQIIQGLQTIISRRI--DLTKEPAVISIGKINGGTRGNIIPEDAEMVGTIRTFDP 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 263 ESAQVQCDRIEKILS----------EVRTDPDFPpvstsltVTGDWTALSTDMtQPLAQAAVaalGESLGHIPETTEMTg 332
Cdd:cd05667 276 EMREDIFARLKTIAEhiakaygataEVEFANGYP-------VTYNDPALTAKM-LPTLQKAV---GKADLVVLPPTQTG- 343
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821508169 333 wGEGGSMQKFGIPAFYF---------GPGDGPLAHTPKESVSVSEIKTAVKALFHLV 380
Cdd:cd05667 344 -AEDFSFYAEQVPGMFFflggtpagqEPATAPPNHSPYFIVDESALKTGVKAHIQLV 399
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
59-111 |
8.62e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 41.44 E-value: 8.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 59 PVLLARTGRGKAGVTeLMLSGHVDVVPpaGME-------DPWSARIEGDRMHGRGTTDMK 111
Cdd:PRK07079 73 PFLIAERIEDDALPT-VLIYGHGDVVR--GYDeqwreglSPWTLTEEGDRWYGRGTADNK 129
|
|
| M20_ACY1L2-like |
cd05672 |
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 ... |
183-276 |
1.07e-03 |
|
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: 40.62 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 183 IRVDFTGKSAHSSR-PHLGINAIEAAalfivhakkrlpeLLAGNAAAG-----PASSSIDLV--SGGAAENVVPASASVT 254
Cdd:cd05672 161 LTVEFHGKSAHAAAaPWEGINALDAA-------------VLAYNAISAlrqqlKPTWRIHGIitEGGKAPNIIPDYAEAR 227
|
90 100
....*....|....*....|..
gi 1821508169 255 IDFRYQGVESAQVQCDRIEKIL 276
Cdd:cd05672 228 FYVRAPTRKELEELRERVIACF 249
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
188-227 |
1.20e-03 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 40.72 E-value: 1.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1821508169 188 TGKSAHSSRPHLGINAIEAAALFIVHAKKRLPELLAGNAA 227
Cdd:PRK06156 306 TGKSAHSSTPESGVNPVTRLALFLQSLDGDLPHNHAADAA 345
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
182-380 |
2.36e-03 |
|
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.
Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 39.81 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 182 WIRVDFTGKSAHS-----SRPHlgiNAIEAAALFIV----HAKKRLPELLA--GNAAAGPASSsidlvsggaaeNVVPAS 250
Cdd:cd03884 208 WLEVTVTGEAGHAgttpmALRR---DALLAAAELILaveeIALEHGDDLVAtvGRIEVKPNAV-----------NVIPGE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 251 ASVTIDFRY-------QGVESAQVQCDRI---EKILSEVRTDPDFPPVstsltvtgdwtALSTDMTQPLAQAAvAALGES 320
Cdd:cd03884 274 VEFTLDLRHpddavldAMVERIRAEAEAIaaeRGVEVEVERLWDSPPV-----------PFDPELVAALEAAA-EALGLS 341
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821508169 321 LGHIPettemTGWG-EGGSMQKFGIPAFYFGPGDGPLAHTPKESVSVSEIKTAVKALFHLV 380
Cdd:cd03884 342 YRRMP-----SGAGhDAMFMARICPTAMIFVPSRDGISHNPAEYTSPEDLAAGVQVLLHAL 397
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
66-118 |
2.62e-03 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 39.95 E-value: 2.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821508169 66 GRGKAGVTELMLSGHVDVVP--------PAGMEDPWSARIEGDRMHGRGTTDMKSGAACAL 118
Cdd:PRK06156 103 GLGGSGSDKVGILTHADVVPanpelwvlDGTRLDPFKVTLVGDRLYGRGTEDDKGAIVTAL 163
|
|
| M20_Acy1_IAAspH |
cd05665 |
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, ... |
164-276 |
2.74e-03 |
|
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, bacterial and archaeal aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349915 [Multi-domain] Cd Length: 415 Bit Score: 39.61 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821508169 164 VICEPTG-LCVRSahrgdcwIRVDFTGKSAHS-SRPHLGINAIEAAALFI--VHAKKRlpellagnAAAGPASSSIDLVS 239
Cdd:cd05665 206 VVCGPDNfLATTK-------LDARFTGVSAHAgAAPEDGRNALLAAATAAlnLHAIPR--------HGEGATRINVGVLG 270
|
90 100 110
....*....|....*....|....*....|....*..
gi 1821508169 240 GGAAENVVPASASVTIDFRYQGVESAQVQCDRIEKIL 276
Cdd:cd05665 271 AGEGRNVIPASAELQVETRGETTAINEYMFEQAQRVI 307
|
|
| |
