|
Name |
Accession |
Description |
Interval |
E-value |
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
19-386 |
1.11e-128 |
|
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: 373.94 E-value: 1.11e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 19 DLLQAMVRIPSVAAKEGQVADLIEAFLAPELStgLIKRERISyapGRDNLVLTIGDPNaQRWLGVDGHMDVVDAGDPNKW 98
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGY--GIESTIVE---GRGNLVATVGGGD-GPVLLLNGHIDTVPPGDGDKW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 99 QFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQI--AHEELDHGVQLMATVGEEIDNYGARQLAAAGYGDRLTGLLVA 176
Cdd:cd08659 75 SFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELkeAGALLGGRVALLATVDEEVGSDGARALLEAGYADRLDALIVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 177 EPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAALTATAPLQAkdDPILGHATHNIDIIHGGNQIN 256
Cdd:cd08659 155 EPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPA--HPLLGPPTLNVGVINGGTQVN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 257 SLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSVPKgVHLSLSIDSvLSAAAAAPDNALIQKVQQARQRIGlQRGAVAY 336
Cdd:cd08659 233 SIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAK-LTVEVSLDG-DPPFFTDPDHPLVQALQAAARALG-GDPVVRP 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 872387442 337 RTGITDAALFFHD-GLDLAIYGPGND-TSHETDEYVDLQDVFDSIKVYKDVF 386
Cdd:cd08659 310 FTGTTDASYFAKDlGFPVVVYGPGDLaLAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
14-389 |
6.56e-117 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 344.56 E-value: 6.56e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 14 EQQVTDLLQAMVRIPSVAAKEGQVADLIEAFLApelSTGlIKRERISYAPGRDNLVLTIGdpNAQRWLGVDGHMDVVDAG 93
Cdd:PRK08588 1 EEEKIQILADIVKINSVNDNEIEVANYLQDLFA---KHG-IESKIVKVNDGRANLVAEIG--SGSPVLALSGHMDVVAAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 94 DPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIaHEE--LDHG-VQLMATVGEEIDNYGARQLAAAGYGDRL 170
Cdd:PRK08588 75 DVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIEL-KEQgqLLNGtIRLLATAGEEVGELGAKQLTEKGYADDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 171 TGLLVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAALTATAPLQaKDDPILGHATHNIDIIH 250
Cdd:PRK08588 154 DALIIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYFDSIK-KHNPYLGGLTHVVTIIN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 251 GGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQA-AKTSVPKGVHLSLSIDSVLSAAAAAPDNALIQKVQQARQRIGL 329
Cdd:PRK08588 233 GGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIiNEVNQNGAAQLSLDIYSNHRPVASDKDSKLVQLAKDVAKSYVG 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872387442 330 QRGAVAYRTGITDAALFF--HDGLDLAIYGPG-NDTSHETDEYVDLQDVFDSIKVYKDVFKNY 389
Cdd:PRK08588 313 QDIPLSAIPGATDASSFLkkKPDFPVIIFGPGnNLTAHQVDEYVEKDMYLKFIDIYKEIIIQY 375
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
10-389 |
1.69e-87 |
|
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: 269.83 E-value: 1.69e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 10 LTDEEQQVTDLLQAMVRIPSVAAKEGQVADLIEAFLApelSTGlIKRERISYAPGRDNLVLTIGDPNAQRWLGVDGHMDV 89
Cdd:COG0624 7 IDAHLDEALELLRELVRIPSVSGEEAAAAELLAELLE---ALG-FEVERLEVPPGRPNLVARRPGDGGGPTLLLYGHLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 90 VDAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQI--AHEELDHGVQLMATVGEEIDNYGARQLAAAG-Y 166
Cdd:COG0624 83 VPPGDLELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALlaAGLRLPGNVTLLFTGDEEVGSPGARALVEELaE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 167 GDRLTGLLVAEPGNS-NVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFAnAALTATaPLQAKDDPILGHATHN 245
Cdd:COG0624 163 GLKADAAIVGEPTGVpTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARAL-AALRDL-EFDGRADPLFGRTTLN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 246 IDIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSVPkGVHLSLSIDSVLSAAAAAP-DNALIQKVQQAR 324
Cdd:COG0624 241 VTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAP-GVEVEVEVLGDGRPPFETPpDSPLVAAARAAI 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872387442 325 QRIGLQRGAVAYRTGITDAALFFHD-GLDLAIYGPGN-DTSHETDEYVDLQDVFDSIKVYKDVFKNY 389
Cdd:COG0624 320 REVTGKEPVLSGVGGGTDARFFAEAlGIPTVVFGPGDgAGAHAPDEYVELDDLEKGARVLARLLERL 386
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
19-381 |
7.23e-72 |
|
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: 229.21 E-value: 7.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 19 DLLQAMVRIPSVAA---KEGQVADLIEAFLApELStglIKRERISYAPGR----DNLVLTIGDPNAQRWLGVDGHMDVVD 91
Cdd:TIGR01910 2 ELLKDLISIPSVNPpggNEETIANYIKDLLR-EFG---FSTDVIEITDDRlkvlGKVVVKEPGNGNEKSLIFNGHYDVVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 92 AGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHE--ELDHGVQLMATVGEEIDNYGARQLAAAGYGDR 169
Cdd:TIGR01910 78 AGDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAgiKPNGNIILQSVVDEESGEAGTLYLLQRGYFKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 170 LTGLLVAEPGNS-NVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAA--LTATAPLQAKDDPILGHATHNI 246
Cdd:TIGR01910 158 ADGVLIPEPSGGdNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELneLEEHIYARNSYGFIPGPITFNP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 247 DIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQ-AAKTSVPKGVHLSLSIDSVLSAAAAA-PDNALIQKVQQAR 324
Cdd:TIGR01910 238 GVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDvVKALSKSDGWLYENEPVVKWSGPNETpPDSRLVKALEAII 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 872387442 325 QRIgLQRGAVAY-RTGITDAALFFHDGLDLAIYGPG-NDTSHETDEYVDLQDVFDSIKV 381
Cdd:TIGR01910 318 KKV-RGIEPEVLvSTGGTDARFLRKAGIPSIVYGPGdLETAHQVNEYISIKNLVESTKV 375
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
19-387 |
3.47e-56 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 189.05 E-value: 3.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 19 DLLQAMVRIPSVAAKEGQVADLIEaFLAPELSTGLIKRERI--------SYAPGRDNLVLTIGDPNAQrwLGVDGHMDVV 90
Cdd:PRK08651 10 EFLKDLIKIPTVNPPGENYEEIAE-FLRDTLEELGFSTEIIevpneyvkKHDGPRPNLIARRGSGNPH--LHFNGHYDVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 91 DAGDPNKwQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFkQIAHEELDHGVQLMATVGEEIDNYGARQLaAAGYGDRL 170
Cdd:PRK08651 87 PPGEGWS-VNVPFEPKVKDGKVYGRGASDMKGGIAALLAAF-ERLDPAGDGNIELAIVPDEETGGTGTGYL-VEEGKVTP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 171 TGLLVAEP-GNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAALTATAPLQAK---DDPILGHATHNI 246
Cdd:PRK08651 164 DYVIVGEPsGLDNICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKyeyDDERGAKPTVTL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 247 --DIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSVPK-GVHLSLSIDSVLSAAAAAPDNALIQKVQQA 323
Cdd:PRK08651 244 ggPTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPElGIEVEFEITPFSEAFVTDPDSELVKALREA 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872387442 324 rqrIGLQRGAVAYRT---GITDAALFFHDGLDLAIYGPGN-DTSHETDEYVDLQDVFDSIKVYKDVFK 387
Cdd:PRK08651 324 ---IREVLGVEPKKTislGGTDARFFGAKGIPTVVYGPGElELAHAPDEYVEVKDVEKAAKVYEEVLK 388
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
85-388 |
3.56e-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: 173.69 E-value: 3.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 85 GHMDVVDAGDPNKWqfpPFSAQIeDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHG-VQLMATVGEEIDNYGARQLAA 163
Cdd:pfam01546 4 GHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLKKGtVKLLFQPDEEGGMGGARALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 164 AGYGDRLT-----GLLVAEPGNSN------VDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAALTATAPLQ 232
Cdd:pfam01546 80 DGLLEREKvdavfGLHIGEPTLLEggiaigVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSRNV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 233 AKDDPILGhATHNIDIIHGGnqINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSVPKGVHlSLSIDSVLSAA-AAA 311
Cdd:pfam01546 160 DPLDPAVV-TVGNITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGV-KVEVEYVEGGApPLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 312 PDNALIQKVQQA-RQRIGLQRGAVAYRT-GITDAAlFFHDGLDLA--IYGPGNDTSHETDEYVDLQDVFDSIKVYKDVFK 387
Cdd:pfam01546 236 NDSPLVAALREAaKELFGLKVELIVSGSmGGTDAA-FFLLGVPPTvvFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLLL 314
|
.
gi 872387442 388 N 388
Cdd:pfam01546 315 K 315
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
19-372 |
6.47e-50 |
|
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: 172.01 E-value: 6.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 19 DLLQAMVRIPSV-AAKEGQVADLIEAFLApelSTGlIKRERISYA-PGRDNLVLTIGdPNAQRWLGVDGHMDVVDAGDPn 96
Cdd:cd03894 1 ELLARLVAFDTVsRNSNLALIEYVADYLA---ALG-VKSRRVPVPeGGKANLLATLG-PGGEGGLLLSGHTDVVPVDGQ- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 97 KWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHGVQLMATVGEEIDNYGARQLAAAG--YGDRLTGLL 174
Cdd:cd03894 75 KWSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALaaRGGRPDAAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 175 VAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHG---LFAFANAALTATAPLQAKDDPILGHATHNIDIIHG 251
Cdd:cd03894 155 VGEPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAaarLIGKLRELADRLAPGLRDPPFDPPYPTLNVGLIHG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 252 GNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSVPKG------VHLSLSIDSvlsaaAAAPDNALIQKVQQARQ 325
Cdd:cd03894 235 GNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPeagievEPLFEVPGL-----ETDEDAPLVRLAAALAG 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 872387442 326 RIGLQrgAVAYRtgiTDAALFFHDGLDLAIYGPGN-DTSHETDEYVDL 372
Cdd:cd03894 310 DNKVR--TVAYG---TEAGLFQRAGIPTVVCGPGSiAQAHTPDEFVEL 352
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
19-382 |
2.55e-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 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: 162.17 E-value: 2.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 19 DLLQAMVRIPSvAAKEGQVADLIEAFLAPELSTGLIKRERISYAPGRDNLVLTIGDPNAQRWLGVDGHMDVVDAGDPNKW 98
Cdd:cd08011 2 KLLQELVQIPS-PNPPGDNTSAIAAYIKLLLEDLGYPVELHEPPEEIYGVVSNIVGGRKGKRLLFNGHYDVVPAGDGEGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 99 QFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEEL-DHGVQLMATVGEE--IDNYGARQLAAAGYGdRLTGLLV 175
Cdd:cd08011 81 TVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKApWDLPVVLTFVPDEetGGRAGTKYLLEKVRI-KPNDVLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 176 AEP-GNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIhglfafaNAALTAtapLQAkddpiLG--HATHNIDIIHGG 252
Cdd:cd08011 160 GEPsGSDNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAV-------KAAMKL---IER-----LYelEKTVNPGVIKGG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 253 NQINSLPESAYLRGNVRTTMIADNDAFIAALKQAaktsVPKGVHLSLSIDSVLSAAAAAPDNALIQKVQQARQRIgLQRG 332
Cdd:cd08011 225 VKVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDH----LDSIEEVSFEIKSFYSPTVSNPDSEIVKKTEEAITEV-LGIR 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 872387442 333 AVAY-RTGITDAALFFHDGLDLAIYGPGN-DTSHETDEYVDLQDVFDSIKVY 382
Cdd:cd08011 300 PKEViSVGASDARFYRNAGIPAIVYGPGRlGQMHAPNEYVEIDELIKVIKVH 351
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
15-375 |
1.41e-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 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: 158.02 E-value: 1.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 15 QQVTDLLQAMVRIPSV--------AAKEGQVADLIEAFLAPELstglIKRERISYAPGRDNLVLTIGDPNAQRWLGVDGH 86
Cdd:cd08013 1 DDPVSLTQTLVRINSSnpslsatgGAGEAEIATYVAAWLAHRG----IEAHRIEGTPGRPSVVGVVRGTGGGKSLMLNGH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 87 MDVVDAgdpNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHGVQLMATVGEEIDNYGARQLAAAGY 166
Cdd:cd08013 77 IDTVTL---DGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGLRGDVILAAVADEEDASLGTQEVLAAGW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 167 gdRLTGLLVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAI--HGLFAFANAALTATAPlQAKDDPILGHATH 244
Cdd:cd08013 154 --RADAAIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAIlkAGYFLVALEEYQQELP-ERPVDPLLGRASV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 245 NIDIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALK---QAAKTSVPKGVHLSLSIDSVLSAAAAAPDNALIQKVQ 321
Cdd:cd08013 231 HASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTailGELAQTVPNFSYREPRITLSRPPFEVPKEHPFVQLVA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 872387442 322 QARQRIGLQRGAVAYRTGITDAALFFHDGLDLAIYGPGNDTSHETDEYVDLQDV 375
Cdd:cd08013 311 AHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGAGLHAKEEWVDVESI 364
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
14-261 |
5.02e-41 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 149.32 E-value: 5.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 14 EQQVTDLLQAMVRIPSVAAKEGQVADLIEAFLApelSTGLIKRERISYApgrdNLVLTIGdpNAQRWLGVDGHMDVVDAG 93
Cdd:PRK13004 14 KADMTRFLRDLIRIPSESGDEKRVVKRIKEEME---KVGFDKVEIDPMG----NVLGYIG--HGKKLIAFDAHIDTVGIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 94 DPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHGVQLM--ATVGEEI-DNYGARQLAAAGyGDRL 170
Cdd:PRK13004 85 DIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYvtGTVQEEDcDGLCWRYIIEED-KIKP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 171 TGLLVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAALTATAPLqaKDDPILGHATHNI-DII 249
Cdd:PRK13004 164 DFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNL--KEDPFLGKGTLTVsDIF 241
|
250
....*....|..
gi 872387442 250 HGGNQINSLPES 261
Cdd:PRK13004 242 STSPSRCAVPDS 253
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
19-375 |
2.08e-40 |
|
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: 146.89 E-value: 2.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 19 DLLQAMVRIPSVAAKEGqvADLIEaFLAPELSTGLIKRERISYAPGRD--NLVLTIGdPNAQRWLGVDGHMDVVDAgDPN 96
Cdd:TIGR01892 1 EILTKLVAFDSTSFRPN--VDLID-WAQAYLEALGFSVEVQPFPDGAEksNLVAVIG-PSGAGGLALSGHTDVVPY-DDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 97 KWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHGVQLMATVGEEIDNYGARQLAAAGYGdRLTGLLVA 176
Cdd:TIGR01892 76 AWTRDPFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIEAGAG-RPRHAIIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 177 EPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAALTATAPLQAKD-----DPilGHATHNIDIIHG 251
Cdd:TIGR01892 155 EPTRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDldegfTP--PYTTLNIGVIQG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 252 GNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSVPK--GVHLSLSIDSVLSAAAAAPDNALiqkVQQARQRIGL 329
Cdd:TIGR01892 233 GKAVNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRDepGFEVQIEVVSTDPGVNTEPDAEL---VAFLEELSGN 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 872387442 330 QRGAVAYrtgITDAALFFHDGLDLAIYGPGN-DTSHETDEYVDLQDV 375
Cdd:TIGR01892 310 APEVVSY---GTEAPQFQELGAEAVVCGPGDiRQAHQPDEYVEIEDL 353
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
19-385 |
1.83e-37 |
|
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349886 [Multi-domain] Cd Length: 366 Bit Score: 138.79 E-value: 1.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 19 DLLQAMVRIPSVAAKEGQVADLIEAFLApelSTGLiKRERISYApGRDNLVLTIGdpNAQRWLGVDGHMDVVDAGDPNKW 98
Cdd:cd03891 2 ELAKELIRRPSVTPDDAGAQDLIAERLK---ALGF-TCERLEFG-GVKNLWARRG--TGGPHLCFAGHTDVVPPGDLEGW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 99 QFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDH-G-VQLMATVGEEID-NYGARQ----LAAAgyGDRLT 171
Cdd:cd03891 75 SSDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHkGsISFLITSDEEGPaIDGTKKvlewLKAR--GEKID 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 172 GLLVAEPGNSNV--DA---AERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANaALTATaPLqakDDPILGHATHNI 246
Cdd:cd03891 153 YCIVGEPTSEKKlgDTikiGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILA-ELTAT-VL---DEGNEFFPPSSL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 247 DI--IHGGNQI-NSLPESAYLRGNVR-TTMIADND--AFIAALkqAAKTSVPKGVHLSLSIDSVLSaaaaaPDNALIQKV 320
Cdd:cd03891 228 QItnIDVGNGAtNVIPGELKAKFNIRfNDEHTGESlkARIEAI--LDKHGLDYDLEWKLSGEPFLT-----KPGKLVDAV 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872387442 321 QQARQRIglqrgavayrTGIT----------DAALFFHDGLDLAIYGPGNDTSHETDEYVDLQDVFDSIKVYKDV 385
Cdd:cd03891 301 SAAIKEV----------TGITpelstsggtsDARFIASYGCPVVEFGLVNATIHKVNERVSVADLEKLTDIYERI 365
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
20-382 |
2.20e-37 |
|
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: 139.37 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 20 LLQAMVRIPSVAAKEGQVADLIEAFLApelSTGL------IKRERISYAPG----------RDNLVLTI-GDPNAQRWLG 82
Cdd:cd03895 2 FLQDLVRFPSLRGEEAAAQDLVAAALR---SRGYtvdrweIDVEKLKHHPGfspvavdyagAPNVVGTHrPRGETGRSLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 83 VDGHMDVVDAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEeldhGVQLMATV------GEEIDNY 156
Cdd:cd03895 79 LNGHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAA----GLQPAADVhfqsvvEEECTGN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 157 GArqLAAAGYGDRLTGLLVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANA--ALTATAPLQAK 234
Cdd:cd03895 155 GA--LAALMRGYRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQAlqELEREWNARKK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 235 DDPILGHATH----NIDIIHGGNQINSLPES-------AYLRGNVRTTMIADNDAFIAALKQAAK--TSVPKGVHLS--L 299
Cdd:cd03895 233 SHPHFSDHPHpinfNIGKIEGGDWPSSVPAWcvldcriGIYPGESPEEARREIEECVADAAATDPwlSNHPPEVEWNgfQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 300 SIDSVLSaaaaaPDNALIQKVQQARQRIglqRGAVAYRTGIT---DAALFFHDGLDLAI-YGPGNDTSHETDEYVDLQDV 375
Cdd:cd03895 313 AEGYVLE-----PGSDAEQVLAAAHQAV---FGTPPVQSAMTattDGRFFVLYGDIPALcYGPGSRDAHGFDESVDLESL 384
|
....*..
gi 872387442 376 FDSIKVY 382
Cdd:cd03895 385 RKITKTI 391
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
17-388 |
1.26e-36 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 136.78 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 17 VTDLLQAMVRIPSVAAKEGQVADLIeaflAPELSTGLIKRERISYApGRDNLVLT--IGDPNaqrwLGVDGHMDVVDAGD 94
Cdd:TIGR01246 1 VTELAKELISRPSVTPNDAGCQDII----AERLEKLGFEIEWMHFG-DTKNLWATrgTGEPV----LAFAGHTDVVPAGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 95 PNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDH--GVQLMATVGEEIDN-YGARQLAAAGY--GDR 169
Cdd:TIGR01246 72 EEQWSSPPFEPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHkgSISLLITSDEEGTAiDGTKKVVETLMarDEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 170 LTGLLVAEPGNSN-----VDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHgLFAFANAALTATaplqaKDDPilGHA-- 242
Cdd:TIGR01246 152 IDYCIVGEPSSVKklgdvIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIH-KAAPALAELTAI-----KWDE--GNEff 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 243 ---THNIDIIHGGNQI-NSLPESAYLRGNVR-TTMIADND--AFIAALKQAAKtsVPKGVHLSLSIDSVLSaaaaaPDNA 315
Cdd:TIGR01246 224 pptSLQITNIHAGTGAnNVIPGELYVQFNLRfSTEVSDEIlkQRVEAILDQHG--LDYDLEWSLSGEPFLT-----NDGK 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872387442 316 LIQKVQQARQRIGLQRGAVAYRTGITDAALFFHDGLDLAIYGPGNDTSHETDEYVDLQDVFDSIKVYKDVFKN 388
Cdd:TIGR01246 297 LIDKAREAIEETNGIKPELSTGGGTSDGRFIALMGAEVVEFGPVNATIHKVNECVSIEDLEKLSDVYQDLLEN 369
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
16-372 |
1.36e-34 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 131.46 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 16 QVTDLLQAMVRIPSVAAK-EGQVADLIEAFLApelSTGLikRERISYAPGRD--NLVLTIGdPNAQRWLGVDGHMDVVDA 92
Cdd:PRK07522 5 SSLDILERLVAFDTVSRDsNLALIEWVRDYLA---AHGV--ESELIPDPEGDkaNLFATIG-PADRGGIVLSGHTDVVPV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 93 GDPNkWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHGVQLMATVGEEIDNYGARQLAA--AGYGDRL 170
Cdd:PRK07522 79 DGQA-WTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPSMIArlPERGVKP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 171 TGLLVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIH---GLFAFANA---ALTATAPLQAKDDPilGHATH 244
Cdd:PRK07522 158 AGCIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEyaaRLIAHLRDladRLAAPGPFDALFDP--PYSTL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 245 NIDIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSVP---KGVHLSLSID-SVLSAA---AAAPDNALi 317
Cdd:PRK07522 236 QTGTIQGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAELLpemRAVHPEAAIEfEPLSAYpglDTAEDAAA- 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 872387442 318 qkVQQARQRIGLQ-RGAVAYrtGiTDAALFFHDGLDLAIYGPGN-DTSHETDEYVDL 372
Cdd:PRK07522 315 --ARLVRALTGDNdLRKVAY--G-TEAGLFQRAGIPTVVCGPGSiEQAHKPDEFVEL 366
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
17-389 |
4.47e-34 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 129.82 E-value: 4.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 17 VTDLLQAMVRIPSVAAKEGQVADLIEAFLAP---ELstglikrERISYApGRDNLVLTIGdpNAQRWLGVDGHMDVVDAG 93
Cdd:PRK13009 4 VLELAQDLIRRPSVTPDDAGCQDLLAERLEAlgfTC-------ERMDFG-DVKNLWARRG--TEGPHLCFAGHTDVVPPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 94 DPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHG--VQLMATVGEE---IDnyGARQL--AAAGY 166
Cdd:PRK13009 74 DLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKgsIAFLITSDEEgpaIN--GTVKVleWLKAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 167 GDRLTGLLVAEPGNSNV--DAAE---RGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFAnAALTATaPLQAKDD--Pil 239
Cdd:PRK13009 152 GEKIDYCIVGEPTSTERlgDVIKngrRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPAL-AELAAT-EWDEGNEffP-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 240 ghAThNIDI--IHGGNQI-NSLPESAYLRGNVR-TTMIADND--AFIAALkqAAKTSVPKGVHLSLSIDSVLSaaaaaPD 313
Cdd:PRK13009 228 --PT-SLQItnIDAGTGAtNVIPGELEAQFNFRfSTEHTAESlkARVEAI--LDKHGLDYTLEWTLSGEPFLT-----PP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 314 NALIQKVQQARQRIglqrgavayrTGIT----------DAALFFHDGLDLAIYGPGNDTSHETDEYVDLQDVFDSIKVYK 383
Cdd:PRK13009 298 GKLVDAVVAAIEAV----------TGITpelstsggtsDARFIADYGAQVVEFGPVNATIHKVNECVSVADLEKLTRIYE 367
|
....*.
gi 872387442 384 DVFKNY 389
Cdd:PRK13009 368 RILERL 373
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
19-380 |
2.03e-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: 127.71 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 19 DLLQAMVRIPS-VAAKEG--QVADLIEAFLApelSTGlIKRERISYAPGRDNLVLTIGDPNAQRWLgVDGHMDVVdagdp 95
Cdd:cd03885 3 DLLERLVNIESgTYDKEGvdRVAELLAEELE---ALG-FTVERRPLGEFGDHLIATFKGTGGKRVL-LIGHMDTV----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 96 nkwqFP-------PFSaqIEDGKLYGRGATDMKSGLAAAVVAFKQIAHE--ELDHGVQLMATVGEEIDNYGARQL----- 161
Cdd:cd03885 73 ----FPegtlafrPFT--VDGDRAYGPGVADMKGGLVVILHALKALKAAggRDYLPITVLLNSDEEIGSPGSRELieeea 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 162 AAAGYGdrltglLVAEPG--NSNVDAAERGIIDYTLTAQGKAAHSSR-PDLGANAIHGLfafANAALTatapLQAKDDPI 238
Cdd:cd03885 147 KGADYV------LVFEPAraDGNLVTARKGIGRFRLTVKGRAAHAGNaPEKGRSAIYEL---AHQVLA----LHALTDPE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 239 LGhATHNIDIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSVPKGVHLSLSIDSVLSAAAAAPDN-ALI 317
Cdd:cd03885 214 KG-TTVNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTLVPGTSVELTGGLNRPPMEETPASrRLL 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872387442 318 QKVQQARQRIGLQRGAVAyRTGITDAALFFHDG---LD-LAIYGPGNdtsHETDEYVDLQDVFDSIK 380
Cdd:cd03885 293 ARAQEIAAELGLTLDWEA-TGGGSDANFTAALGvptLDgLGPVGGGA---HTEDEYLELDSLVPRIK 355
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
19-385 |
4.70e-33 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 126.27 E-value: 4.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 19 DLLQAMVRIPSVAAKEGQVADLIEAFLapelstglikrERISYAPGR-DNLVLTIG---DPNAQRWLgVDGHMDVVDagd 94
Cdd:cd05651 4 ELLKSLIATPSFSREEHKTADLIENYL-----------EQKGIPFKRkGNNVWAENghfDEGKPTLL-LNSHHDTVK--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 95 PNK-WQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEE-LDHGVQLMATVGEEIDNYGarqlaaaGYGDRLTG 172
Cdd:cd05651 69 PNAgWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGpLNYNLIYAASAEEEISGKN-------GIESLLPH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 173 L------LVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDlGANAIHglfafanAALTATAPLQA----KDDPILGHA 242
Cdd:cd05651 142 LppldlaIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAARNE-GDNAIY-------KALDDIQWLRDfrfdKVSPLLGPV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 243 THNIDIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSV-PKGVHL-SLSIDsvlsaaaaaPDNALIQKV 320
Cdd:cd05651 214 KMTVTQINAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLKSEIkPRSFRLnSSAIP---------PDHPIVQAA 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872387442 321 QQA-RQRIGlqrgavayRTGITDAALFFHDGLDLaiyGPGNDT-SHETDEYVDLQDVFDSIKVYKDV 385
Cdd:cd05651 285 IAAgRTPFG--------SPTLSDQALMPFPSVKI---GPGDSSrSHTADEFIELSEIEEGIDIYIEL 340
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
18-382 |
1.38e-32 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 126.00 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 18 TDLLQAMVRIPSVAAKEGQVADLIEAFLApelSTGLIKRERISYApgrdNLVLTIGdpNAQRWLGVDGHMDVVDAGDPNK 97
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEME---KLGFDEVEIDPMG----NVIGYIG--GGKKKILFDGHIDTVGIGNIDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 98 WQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHE-ELDHGVQLM--ATVGEEI-DNYGARQLAAAgYGDRLTGL 173
Cdd:cd05649 72 WKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLgLRDFAYTILvaGTVQEEDcDGVCWQYISKA-DKIKPDFV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 174 LVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIhglFAFAN-----AALTATAPlqakDDPILGHATHNI-D 247
Cdd:cd05649 151 VSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAV---YKMADiiqdiRQLNPNFP----EAPFLGRGTLTVtD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 248 IIHGGNQINSLPESAYLRGNVRTTMiadNDAFIAALKQAAK-TSVPKG---VHLSLSI-------DSVLSAAAAAP---- 312
Cdd:cd05649 224 IFSTSPSRCAVPDSCRISIDRRLTV---GETWEGCLEEIRAlPAVKKYgddVAVSMYNydrpsytGEVYESERYFPtwll 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872387442 313 --DNALIQKVQQARQRIGLQRGAVAYRTGITDAALFF-HDGLDLAIYGPGNDT-SHETDEYVDLQDVFDSIKVY 382
Cdd:cd05649 301 peDHELVKALLEAYKALFGARPLIDKWTFSTNGVSIMgRAGIPCIGFGPGAENqAHAPNEYTWKEDLVRCAAGY 374
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
19-387 |
5.22e-31 |
|
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: 122.47 E-value: 5.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 19 DLLQAMVRIPSVAA-----KEGQVADLIEAFLApelSTGLIKRERI-SYAPGRDNLVLTIG--DPNAqRWLGVDGHMDVV 90
Cdd:cd05675 2 DLLQELIRIDTTNSgdgtgSETRAAEVLAARLA---EAGIQTEIFVvESHPGRANLVARIGgtDPSA-GPLLLLGHIDVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 91 DAgDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHE--ELDHGVQLMATVGEEIDN-YGARQLAA---- 163
Cdd:cd05675 78 PA-DASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREgfKPKRDLVFAFVADEEAGGeNGAKWLVDnhpe 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 164 --AGYGDRLT---GLLVAEPGNS---NVDAAERGIIDYTLTAQGKAAHSSRPDlGANAIHGLFA---------------- 219
Cdd:cd05675 157 lfDGATFALNeggGGSLPVGKGRrlyPIQVAEKGIAWMKLTVRGRAGHGSRPT-DDNAITRLAEalrrlgahnfpvrltd 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 220 ----FANAALTATAPLQAKDDPI----------------LGHA----THNIDIIHGGNQINSLPESAYLRGNVRTTMIAD 275
Cdd:cd05675 236 etayFAQMAELAGGEGGALMLTAvpvldpalaklgpsapLLNAmlrnTASPTMLDAGYATNVLPGRATAEVDCRILPGQS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 276 NDAFIAALKQAA---KTSVpKGVHLSLSIDSvlsaaaaAPDNALIQKVQQARQRIGLQRGAVAY-RTGITDAALFfhDGL 351
Cdd:cd05675 316 EEEVLDTLDKLLgdpDVSV-EAVHLEPATES-------PLDSPLVDAMEAAVQAVDPGAPVVPYmSPGGTDAKYF--RRL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 872387442 352 DLAIYG-------PGNDTS---HETDEYVDLQDVFDSIKVYKDVFK 387
Cdd:cd05675 386 GIPGYGfaplflpPELDYTglfHGVDERVPVESLYFGVRFLDRLVK 431
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
20-381 |
2.18e-30 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 120.63 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 20 LLQAMVRIPSV---AAKEGQVADLIEAFLAPELSTglIKRERISYAPG------RDNLVLTIGDPNAQRWLGVDGHMDVV 90
Cdd:PRK13013 19 LTQDLIRIPTLnppGRAYREICEFLAARLAPRGFE--VELIRAEGAPGdsetypRWNLVARRQGARDGDCVHFNSHHDVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 91 DAGdpNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHG--VQLMATVGEEIDNY-GARQLAAAGY- 166
Cdd:PRK13013 97 EVG--HGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAgsIEISGTADEESGGFgGVAYLAEQGRf 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 167 -GDRLTGLLVAEPGNSN-VDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAALTATAPLQAK---DDPILG- 240
Cdd:PRK13013 175 sPDRVQHVIIPEPLNKDrICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEIEERLFPLLATrrtAMPVVPe 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 241 ---HATHNIDIIHGGNqinslPESAYLRGNVRTTMIADN------------------DAFIAALKQAAKTSVPKgvhLSL 299
Cdd:PRK13013 255 garQSTLNINSIHGGE-----PEQDPDYTGLPAPCVADRcrividrrflieedldevKAEITALLERLKRARPG---FAY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 300 SIDSVLSAAAAAPDN---------ALIQKV--QQARQ-------------RIGLQRGAVAYRTGItdaalffhdgLDLAi 355
Cdd:PRK13013 327 EIRDLFEVLPTMTDRdapvvrsvaAAIERVlgRQADYvvspgtydqkhidRIGKLKNCIAYGPGI----------LDLA- 395
|
410 420
....*....|....*....|....*.
gi 872387442 356 ygpgndtsHETDEYVDLQDVFDSIKV 381
Cdd:PRK13013 396 --------HQPDEWVGIADMVDSAKV 413
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
17-375 |
3.81e-30 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 118.70 E-value: 3.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 17 VTDLLQAMVRIPSVAAKEGQVADLIEAFLA--PELStglIKRERisyapgrDNLVLTIGDPNAQRWLGVdGHMDVVDAGD 94
Cdd:cd05647 1 PIELTAALVDIPSVSGNEKPIADEIEAALRtlPHLE---VIRDG-------NTVVARTERGLASRVILA-GHLDTVPVAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 95 --PNKWQfppfsaqiEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHGVQLMATVGEEIDNY--GARQLAAAgYGDRL 170
Cdd:cd05647 70 nlPSRVE--------EDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLTLIFYDCEEVAAElnGLGRLAEE-HPEWL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 171 TG--LLVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLfAFANAALTATAPLQAKDDPILGHATHNIDI 248
Cdd:cd05647 141 AAdfAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKL-APILARLAAYEPRTVNIDGLTYREGLNAVF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 249 IHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAaktsvpkGVHLSLSIDSVLSAAAAAP--DNALiqkvqqARQR 326
Cdd:cd05647 220 ISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREV-------FEGLGYEIEVTDLSPGALPglDHPV------ARDL 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 872387442 327 IGLQRGAVAYRTGITDAALFFHDGLDLAIYGPGNDT-SHETDEYVDLQDV 375
Cdd:cd05647 287 IEAVGGKVRAKYGWTDVARFSALGIPAVNFGPGDPLlAHKRDEQVPVEQI 336
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
14-382 |
4.72e-30 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 119.72 E-value: 4.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 14 EQQVtDLLQAMVRIPSVAAKEGQVADLIEAFLAP--------ELSTGLIKRERiSYAP------GRDNLVLTI-GDPNAQ 78
Cdd:PRK06837 20 DAQV-AFTQDLVRFPSTRGAEAPCQDFLARAFRErgyevdrwSIDPDDLKSHP-GAGPveidysGAPNVVGTYrPAGKTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 79 RWLGVDGHMDVVDAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQI--AHEELDHGVQLMATVGEEIDNY 156
Cdd:PRK06837 98 RSLILQGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALraAGLAPAARVHFQSVIEEESTGN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 157 GArqLAAAGYGDRLTGLLVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANA--ALTATAPLQAK 234
Cdd:PRK06837 178 GA--LSTLQRGYRADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQAlrELEAEWNARKA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 235 DDPILGHATH----NIDIIHGGNQINSLPesAYLRGNVRT-----TMIADNDAFI-AALKQAAKT------SVPKGVHLS 298
Cdd:PRK06837 256 SDPHFEDVPHpinfNVGIIKGGDWASSVP--AWCDLDCRIaiypgVTAADAQAEIeACLAAAARDdrflsnNPPEVVWSG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 299 LSIDSVLSAAAAAPDNALiqkvQQARQRIglQRGAVAYR--TGITDAALFfhdGLDLAI----YGPGNDTSHETDEYVDL 372
Cdd:PRK06837 334 FLAEGYVLEPGSEAEAAL----ARAHAAV--FGGPLRSFvtTAYTDTRFY---GLYYGIpalcYGPSGEGIHGFDERVDL 404
|
410
....*....|
gi 872387442 373 QDVFDSIKVY 382
Cdd:PRK06837 405 ESVRKVTKTI 414
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
20-389 |
1.14e-29 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 117.17 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 20 LLQAMVRIPSVAAKEGQVADLIEAFLapelstglikrERISYAPGRD------NLVLtigDPNAQRWLGVdgHMDVVDAg 93
Cdd:PRK08652 7 LLKQLVKIPSPSGQEDEIALHIMEFL-----------ESLGYDVHIEsdgeviNIVV---NSKAELFVEV--HYDTVPV- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 94 dpnkwQFPPFsaqIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHGVQLMATVGEEIDNYGARQLAAAgYGDRLTgl 173
Cdd:PRK08652 70 -----RAEFF---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSDEEEGGRGSALFAER-YRPKMA-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 174 LVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANaALTATAPLQAKD-DPILGhathnIDIIHGG 252
Cdd:PRK08652 139 IVLEPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLE-KLKELLKALGKYfDPHIG-----IQEIIGG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 253 NQINSLPESAYLRGNVRttmIADNDAFIAALKQAAKTSVPKGVHLSLSidSVLSAAAAAPDNALIQKVQQARQRIGLQRG 332
Cdd:PRK08652 213 SPEYSIPALCRLRLDAR---IPPEVEVEDVLDEIDPILDEYTVKYEYT--EIWDGFELDEDEEIVQLLEKAMKEVGLEPE 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 872387442 333 AVAYRTGiTDAALFFHDGLDLAIYGPGN-DTSHETDEYVDLQDVFDSIKVYKDVFKNY 389
Cdd:PRK08652 288 FTVMRSW-TDAINFRYNGTKTVVWGPGElDLCHTKFERIDVREVEKAKEFLKALNEIL 344
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
20-383 |
4.78e-29 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 115.45 E-value: 4.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 20 LLQAMVRIPSVAAKEGQVADLIEAFLApelSTGL-IKRERISYApGRDNLVLTIGDPNAQRWLgVDGHMDVVdagdpnkw 98
Cdd:cd05652 4 LHKSLVEIPSISGNEAAVGDFLAEYLE---SLGFtVEKQPVENK-DRFNVYAYPGSSRQPRVL-LTSHIDTV-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 99 qfPPF---SAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHG--VQLMATVGEEIDNYGARqlAAAGYG-DRLTG 172
Cdd:cd05652 71 --PPFipySISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEgdLGLLFVVGEETGGDGMK--AFNDLGlNTWDA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 173 LLVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAALTATAPlqakDDPILGHATHNIDIIHGG 252
Cdd:cd05652 147 VIFGEPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLP----SSELLGPTTLNIGRISGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 253 NQINSLPESAYLRGNVRttMIADNDAFIAALKQAAKTsvpkgvHLSLSIDSVLSAAAAAPDNALIQKVqqarqrIGLQRG 332
Cdd:cd05652 223 VAANVVPAAAEASVAIR--LAAGPPEVKDIVKEAVAG------ILTDTEDIEVTFTSGYGPVDLDCDV------DGFETD 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 872387442 333 AVAYRtgiTDAALFFHDGLDLaIYGPGN-DTSHETDEYVDLQDVFDSIKVYK 383
Cdd:cd05652 289 VVAYG---TDIPYLKGDHKRY-LYGPGSiLVAHGPDEAITVSELEEAVEGYK 336
|
|
| PRK06915 |
PRK06915 |
peptidase; |
8-381 |
4.16e-28 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 114.40 E-value: 4.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 8 GSLTDEEQQVTDLLQAMVRIPSVAAKEGQ----VADLIEAFLAP----ELSTGLIKRERISYAPGRD-----NLVLTIGD 74
Cdd:PRK06915 10 DYIESHEEEAVKLLKRLIQEKSVSGDESGaqaiVIEKLRELGLDldiwEPSFKKLKDHPYFVSPRTSfsdspNIVATLKG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 75 PNAQRWLGVDGHMDVVDAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIahEELdhGVQL-----MATV 149
Cdd:PRK06915 90 SGGGKSMILNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEAL--IES--GIELkgdviFQSV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 150 GEEiDNYGARQLAAAGYGDRLTGLLVAEPGNSNVDAAERGIIDYTLTAQGKAAHssrpdlGANAIHGLFAFANAA--LTA 227
Cdd:PRK06915 166 IEE-ESGGAGTLAAILRGYKADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAH------GGTRYEGVSAIEKSMfvIDH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 228 TAPLQAK-----DDPILGH----ATHNIDIIHGGNQINSLPESAYLRGNV----RTTMIADNDAFIAALKQAAKTSV--- 291
Cdd:PRK06915 239 LRKLEEKrndriTDPLYKGipipIPINIGKIEGGSWPSSVPDSVILEGRCgiapNETIEAAKEEFENWIAELNDVDEwfv 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 292 --PKGVH------LSLSIDsvlsaaaaaPDNALIQKVQQARQRIGLQRGAVAYRTGITDAALFFH-DGLDLAIYGPG-ND 361
Cdd:PRK06915 319 ehPVEVEwfgarwVPGELE---------ENHPLMTTLEHNFVEIEGNKPIIEASPWGTDGGLLTQiAGVPTIVFGPGeTK 389
|
410 420
....*....|....*....|
gi 872387442 362 TSHETDEYVDLQDVFDSIKV 381
Cdd:PRK06915 390 VAHYPNEYIEVDKMIAAAKI 409
|
|
| selenium_YgeY |
TIGR03526 |
putative selenium metabolism hydrolase; SelD, selenophosphate synthase, is the selenium donor ... |
15-382 |
6.83e-27 |
|
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: 110.27 E-value: 6.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 15 QQVTDLLQAMVRIPSVAAKEGQVADLIEAFLApelSTGLIKRERISYApgrdNLVLTIGdpNAQRWLGVDGHMDVVDAGD 94
Cdd:TIGR03526 13 GDMIRFLRDLVAIPSESGDEGRVALRIKQEME---KLGFDKVEIDPMG----NVLGYIG--HGPKLIAMDAHIDTVGIGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 95 PNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHGVQLMATVG-EEIDNYG-ARQLAAAGYGDRLTG 172
Cdd:TIGR03526 84 MDQWQFDPYEGYEDEEIIYGRGASDQEGGIASMVYAGKIIKDLGLLDDYTLLVTGTvQEEDCDGlCWQYIIEEDKIKPEF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 173 LLVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAALTATAPLqaKDDPILGHATHNI-DIIHG 251
Cdd:TIGR03526 164 VVITEPTDMNIYRGQRGRMEIKVTVKGVSCHGSAPERGDNAIYKMAPILKELSQLNANL--VEDPFLGKGTLTVsEIFFS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 252 GNQINSLPESAYLRGNVRTTmiaDNDAFIAALKQAAKTSVPKGVHLSLSI---------DSVLSAAAAAP------DNAL 316
Cdd:TIGR03526 242 SPSRCAVADGCTISIDRRLT---WGETWEYALEQIRNLPAVQGAEAEVEMyeydrpsytGLVYPTECYFPtwvlpeDHLI 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872387442 317 IQKVQQARQRIGLQRGAVAYRTGITDA-ALFFHDGLDLAIYGPGN-DTSHETDEYVDLQDVFDSIKVY 382
Cdd:TIGR03526 319 TKAALETYKRLFGKEPGVDKWTFSTNGvSIMGRHGIPVIGFGPGDeDQAHAPNEKTWKEDLVKAAAMY 386
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
15-383 |
1.32e-26 |
|
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: 108.59 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 15 QQVTDLLQAMVRIPSVAAKEGQVADLIEAFLApELSTGLikrerisYAPGRDNLVLTIGDPNAQRWLGvdGHMDVVdagd 94
Cdd:cd05653 1 QDAVELLLDLLSIYSPSGEEARAAKFLEEIMK-ELGLEA-------WVDEAGNAVGGAGSGPPDVLLL--GHIDTV---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 95 PNkwQFPPfsaQIEDGKLYGRGATDMKSGLAAAVVAFkQIAHEELDHGVQLMATVGEEIDNYGARQLAAAGYgdRLTGLL 174
Cdd:cd05653 67 PG--EIPV---RVEGGVLYGRGAVDAKGPLAAMILAA-SALNEELGARVVVAGLVDEEGSSKGARELVRRGP--RPDYII 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 175 VAEPGNSN-VDAAERGIIDYTLTAQGKAAHSSRPdlGANAIHGLFAFANAALTataplQAKDDPILGHATHNI--DIIHG 251
Cdd:cd05653 139 IGEPSGWDgITLGYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLIKKWLEVKK-----WAEGYNVGGRDFDSVvpTLIKG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 252 GNQINSLPESAYLRGNVRttmIADNDAFIAALKQAAktsvPKGVHLSLSIDSVLSAAAAAPDNALIQKVQQARQRIGLQR 331
Cdd:cd05653 212 GESSNGLPQRAEATIDLR---LPPRLSPEEAIALAT----ALLPTCELEFIDDTEPVKVSKNNPLARAFRRAIRKQGGKP 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 872387442 332 gAVAYRTGITDA-ALFFHDGLDLAIYGPGNDT-SHETDEYVDLQDVFDSIKVYK 383
Cdd:cd05653 285 -RLKRKTGTSDMnVLAPLWTVPIVAYGPGDSTlDHTPNEHIELAEIERAAAVLK 337
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
13-389 |
2.37e-25 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 105.52 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 13 EEQQVTDLLQAMVRIPSVAAKEGQVADLIEAFLApELstGLIKRErisyapgrD---NLVLTI---GDPNAQRwLGVDGH 86
Cdd:COG2195 1 NPERLLERFLEYVKIPTPSDHEEALADYLVEELK-EL--GLEVEE--------DeagNVIATLpatPGYNVPT-IGLQAH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 87 MDVVDagdpnkwQFP--PFSAQIEDGKLYGRGAT----DMKSGLAAAVVAFKQIAHEELDHG-VQLMATVGEEIDNYGAR 159
Cdd:COG2195 69 MDTVP-------QFPgdGIKPQIDGGLITADGTTtlgaDDKAGVAAILAALEYLKEPEIPHGpIEVLFTPDEEIGLRGAK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 160 QLAAagygDRLTG--LLvaepgnsNVDAAERGII--------DYTLTAQGKAAHS-SRPDLGANAIHgLFAFANAALtat 228
Cdd:COG2195 142 ALDV----SKLGAdfAY-------TLDGGEEGELeyecagaaDAKITIKGKGGHSgDAKEKMINAIK-LAARFLAAL--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 229 aPLQAKDDpilgHATHNIDIIHGGNQINSLPESAYLRGNVR----TTMIADNDAFIAALKQAAKTsVPKGVhLSLSIDSV 304
Cdd:COG2195 207 -PLGRIPE----ETEGNEGFIHGGSATNAIPREAEAVYIIRdhdrEKLEARKAELEEAFEEENAK-YGVGV-VEVEIEDQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 305 LSAAAAAPDNALIQKVQQARQRIGLQRGAVAYRTGiTDAALFFHDGLDLAIYGPGNDTSHETDEYVDLQDVFDSIKVYKD 384
Cdd:COG2195 280 YPNWKPEPDSPIVDLAKEAYEELGIEPKIKPIRGG-LDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWELLVE 358
|
....*
gi 872387442 385 VFKNY 389
Cdd:COG2195 359 ILKLI 363
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
15-385 |
9.15e-25 |
|
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: 104.46 E-value: 9.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 15 QQVTDLLQAMVRIPSVAAKEG-----QVADLIEAFLApELSTGLIKRERI--SYAPGRDNLVLTIGDPNAQRwLGVDGHM 87
Cdd:cd05650 1 EEIIELERDLIRIPAVNPESGgegekEKADYLEKKLR-EYGFYTLERYDApdERGIIRPNIVAKIPGGNDKT-LWIISHL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 88 DVVDAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEEL--DHGVQLMATVGEEI-DNYGARQLAAA 164
Cdd:cd05650 79 DTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGItpKYNFGLLFVADEEDgSEYGIQYLLNK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 165 G---YGDRLtgLLVAEPGNSN---VDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAALTATAP-LQAKDDP 237
Cdd:cd05650 159 FdlfKKDDL--IIVPDFGTEDgefIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFALELDELLHEkFDEKDDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 238 ILGHATHNIDIIHGGN--QINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSVPK-GVHLSLSIDSVLSAAAAAPDN 314
Cdd:cd05650 237 FNPPYSTFEPTKKEANvpNVNTIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDFENSyGAGITYEIVQKEQAPPATPED 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872387442 315 ALIqkVQQARQRIGLQRGAVAYRTGI---TDAALFFHDGLDLAIYGPGNDTSHETDEYVDLQDVFDSIKVYKDV 385
Cdd:cd05650 317 SEI--VVRLSKAIKKVRGREAKLIGIgggTVAAFLRKKGYPAVVWSTLDETAHQPNEYIRISHIVKDAKVFAEM 388
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
14-388 |
9.66e-24 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 101.46 E-value: 9.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 14 EQQVTDLLQAMVRIPSVA---AKEGQV--ADLIEAFLApELSTGLIKR-----ERISYAPgRDNLVLTIGDPNAQRWLGV 83
Cdd:PRK13983 4 RDEMIELLSELIAIPAVNpdfGGEGEKekAEYLESLLK-EYGFDEVERydapdPRVIEGV-RPNIVAKIPGGDGKRTLWI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 84 DGHMDVVDAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIaheeLDHGVQLMATVG------EEIDN-Y 156
Cdd:PRK13983 82 ISHMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKAL----MDLGIRPKYNLGlafvsdEETGSkY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 157 GARQLAAAGYG----DRLtgLLVAEPGN---SNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANA---ALT 226
Cdd:PRK13983 158 GIQYLLKKHPElfkkDDL--ILVPDAGNpdgSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRAAADFALEldeALH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 227 ATAPlqAKD---DP--------ILGHATHNIDIIHGGNQIN----SLPEsaYLRGNVRTTMiadnDAFIAALKQAaktsv 291
Cdd:PRK13983 236 EKFN--AKDplfDPpystfeptKKEANVDNINTIPGRDVFYfdcrVLPD--YDLDEVLKDI----KEIADEFEEE----- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 292 pKGVHLSLSIDSVLSAAAAAPDNALIqkVQQARQRIGLQRGAVAYRTGI---TDAALFFHDGLDLAIYGPGNDTSHETDE 368
Cdd:PRK13983 303 -YGVKIEVEIVQREQAPPPTPPDSEI--VKKLKRAIKEVRGIEPKVGGIgggTVAAFLRKKGYPAVVWSTLDETAHQPNE 379
|
410 420
....*....|....*....|
gi 872387442 369 YVDLQDVFDSIKVYKDVFKN 388
Cdd:PRK13983 380 YAKISNLIEDAKVFALLLLE 399
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
62-372 |
1.28e-22 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 97.97 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 62 APGRDNLVLTIGdpNAQRWLGVDGHMDVVDAgDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDH 141
Cdd:PRK05111 57 TRGKFNLLASLG--SGEGGLLLAGHTDTVPF-DEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 142 GVQLMATVGEEIDNYGARQLAAAG--YGDRltgLLVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFA 219
Cdd:PRK05111 134 PLYILATADEETSMAGARAFAEATaiRPDC---AIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 220 FANAALTATAPLQAK-DDPI--LGHATHNIDIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSVPK-GV 295
Cdd:PRK05111 211 VIGELLQLRDELQERyHNPAftVPYPTLNLGHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSERwPG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 296 HLSLS-----IDSvlsaAAAAPDNALIQKVQQArqrIGLQRGAVAYRTgitdAALFFHD-GLDLAIYGPGN-DTSHETDE 368
Cdd:PRK05111 291 RITVAplhppIPG----YECPADHQLVRVVEKL---LGHKAEVVNYCT----EAPFIQQlGCPTLVLGPGSiEQAHQPDE 359
|
....
gi 872387442 369 YVDL 372
Cdd:PRK05111 360 YLEL 363
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
14-381 |
4.30e-21 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 93.95 E-value: 4.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 14 EQQVTDLLQAMVRIPSVA-----AKEGQvaDLIEAFLApelSTGL-IKRERIsYaPGRDNLVLTI--GDPNAQRWLGVDG 85
Cdd:PRK08596 12 KDELLELLKTLVRFETPApparnTNEAQ--EFIAEFLR---KLGFsVDKWDV-Y-PNDPNVVGVKkgTESDAYKSLIING 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 86 HMDVVDAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIaHEeldHGVQL------MATVGEEIDNYGAR 159
Cdd:PRK08596 85 HMDVAEVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLL-HE---AGIELpgdlifQSVIGEEVGEAGTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 160 QLAAAGYGDRLTglLVAEPGNSNVDaAERGIIDYTLTAQGKAAHSSrpDLGANAIH---GLFAfANAALTATAPLQA--- 233
Cdd:PRK08596 161 QCCERGYDADFA--VVVDTSDLHMQ-GQGGVITGWITVKSPQTFHD--GTRRQMIHaggGLFG-ASAIEKMMKIIQSlqe 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 234 --------KDDPIL--GHATHNIDIIHGGNQ-------------INSLPESAYlrgnvrTTMIADNDAFIAALKQA---- 286
Cdd:PRK08596 235 lerhwavmKSYPGFppGTNTINPAVIEGGRHaafiadecrlwitVHFYPNETY------EQVIKEIEEYIGKVAAAdpwl 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 287 ---------AKTS--VPKG-VHLSLSIDsvlsaaaaaPDNALIQKVQQARQRIGLQRGAVAYRTGITDAALFFHDGLDLA 354
Cdd:PRK08596 309 renppqfkwGGESmiEDRGeIFPSLEID---------SEHPAVKTLSSAHESVLSKNAILDMSTTVTDGGWFAEFGIPAV 379
|
410 420
....*....|....*....|....*...
gi 872387442 355 IYGPGNDT-SHETDEYVDLQDVFDSIKV 381
Cdd:PRK08596 380 IYGPGTLEeAHSVNEKVEIEQLIEYTKV 407
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
64-378 |
7.35e-20 |
|
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: 89.82 E-value: 7.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 64 GRDNLVLTI-GDPNAQRWLGVDGHMDVVDAGDPNKwqfPPfsaQIEDGKLYGRGAT----DMKSGLAAAVVAFKQIAHEE 138
Cdd:cd05683 52 GAGNLICTLkADKEEVPKILFTSHMDTVTPGINVK---PP---QIADGYIYSDGTTilgaDDKAGIAAILEAIRVIKEKN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 139 LDHG-VQLMATVGEEIDNYGARQLAA----AGYGDRLTGllVAEPGNSNVDAAERGIIDytLTAQGKAAHSS-RPDLGAN 212
Cdd:cd05683 126 IPHGqIQFVITVGEESGLVGAKALDPelidADYGYALDS--EGDVGTIIVGAPTQDKIN--AKIYGKTAHAGtSPEKGIS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 213 AIHglfafanaaLTATAPLQAKDDPILGHATHNIDIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSVP 292
Cdd:cd05683 202 AIN---------IAAKAISNMKLGRIDEETTANIGKFQGGTATNIVTDEVNIEAEARSLDEEKLDAQVKHMKETFETTAK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 293 K-GVHLSLSIDSVLSAAAAAPDNALIQKVQQARQRIGLQrGAVAYRTGITDAALFFHDGLDLAIYGPGNDTSHETDEYVD 371
Cdd:cd05683 273 EkGAHAEVEVETSYPGFKINEDEEVVKLAKRAANNLGLE-INTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIP 351
|
....*..
gi 872387442 372 LQDVFDS 378
Cdd:cd05683 352 IEDLYDT 358
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
21-381 |
2.42e-19 |
|
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: 88.77 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 21 LQAMVRIPS------VAAKEGQVADLIEAF----------------LAPELSTGLIKRERisYAPGrdnlvltigdpnaQ 78
Cdd:cd02697 9 LQKLVRVPTdtppgnNAPHAERTAALLQGFgfeaerhpvpeaevraYGMESITNLIVRRR--YGDG-------------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 79 RWLGVDGHMDVVDAGDpnKWQFPPFSAQIEDGKLYGRGATDMKSGLAA---AVVAFKQIAhEELDHGVQLMATVGEEidn 155
Cdd:cd02697 74 RTVALNAHGDVVPPGD--GWTRDPYGAVVEDGVMYGRAAAVSKSDFASftfAVRALESLG-APLRGAVELHFTYDEE--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 156 YGArqLAAAGY----GDRLTGLLVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAALTATAPL 231
Cdd:cd02697 148 FGG--ELGPGWllrqGLTKPDLLIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNAQY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 232 QAKDDPILG--HATHNIDIIHGGNQINSLPESAYLRGNVRttMIADND-----AFIAALKQAAKTSVPkGVHLSLSIDSV 304
Cdd:cd02697 226 RQVSSQVEGitHPYLNVGRIEGGTNTNVVPGKVTFKLDRR--MIPEENpveveAEIRRVIADAAASMP-GISVDIRRLLL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 305 LSAAAAAPDNA-LIQKVQQARQRIgLQRGAVAYRTGI-TDAALFFHDGLDLAIYGPGNDT-----SHETDEYVDLQDVFD 377
Cdd:cd02697 303 ANSMRPLPGNApLVEAIQTHGEAV-FGEPVPAMGTPLyTDVRLYAEAGIPGVIYGAGPRTvleshAKRADERLQLEDLRR 381
|
....
gi 872387442 378 SIKV 381
Cdd:cd02697 382 ATKV 385
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
10-385 |
3.88e-19 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 87.70 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 10 LTDEEQQVTDLLQAMVRIPSVAAKEGQVADLIEAFLApelstgliKRERISYAPGRDNLVLTIGDpnAQRWLGVDGHMDV 89
Cdd:PRK04443 1 MTISALEARELLKGLVEIPSPSGEEAAAAEFLVEFME--------SHGREAWVDEAGNARGPAGD--GPPLVLLLGHIDT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 90 VdAGD-PnkwqfppfsAQIEDGKLYGRGATDMKSGLAAAVVAFKQiAHEELDHGVQLMATVGEEIDNYGARQLAAagygD 168
Cdd:PRK04443 71 V-PGDiP---------VRVEDGVLWGRGSVDAKGPLAAFAAAAAR-LEALVRARVSFVGAVEEEAPSSGGARLVA----D 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 169 RLT--GLLVAEP-GNSNVDAAERGIIDYTLTAQGKAAHSSRPdlGANAIHGLFAFANaALTATAPLQAKDDPILGHATHN 245
Cdd:PRK04443 136 RERpdAVIIGEPsGWDGITLGYKGRLLVTYVATSESFHSAGP--EPNAAEDAIEWWL-AVEAWFEANDGRERVFDQVTPK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 246 IDIIHGGNqiNSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTsvpkgvhLSLSIDSVLSAAAAAPDNALIQKVQQARQ 325
Cdd:PRK04443 213 LVDFDSSS--DGLTVEAEMTVGLRLPPGLSPEEAREILDALLPT-------GTVTFTGAVPAYMVSKRTPLARAFRVAIR 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 872387442 326 RIGLQRGAVaYRTGITDAALFF-HDGLDLAIYGPGN-DTSHETDEYVDLQDVFDSIKVYKDV 385
Cdd:PRK04443 284 EAGGTPRLK-RKTGTSDMNVVApAWGCPMVAYGPGDsDLDHTPDEHLPLAEYLRAIAVLTDV 344
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
10-217 |
6.13e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 88.13 E-value: 6.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 10 LTDEEQQVTDLLQAMVRIPSVAAkEGQVADLIEAFLAPELSTGLIKR--ERISYAPGRDNLVLTIGDPNAQRWLGVDGHM 87
Cdd:PRK09133 32 PTADQQAARDLYKELIEINTTAS-TGSTTPAAEAMAARLKAAGFADAdiEVTGPYPRKGNLVARLRGTDPKKPILLLAHM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 88 DVVDAgDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEEL--DHGVQLMATVGEEIDNY-GARQLaAA 164
Cdd:PRK09133 111 DVVEA-KREDWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFkpKRDIILALTGDEEGTPMnGVAWL-AE 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872387442 165 GYGDRLT---------GLLVAEPGNS---NVDAAERGIIDYTLTAQGKAAHSSRPDLGaNAIHGL 217
Cdd:PRK09133 189 NHRDLIDaefalneggGGTLDEDGKPvllTVQAGEKTYADFRLEVTNPGGHSSRPTKD-NAIYRL 252
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
16-382 |
7.22e-19 |
|
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: 87.69 E-value: 7.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 16 QVTDLLQAMVRIPSV--AAKEGQ-----VADLIEAFLapELSTGL-IKRERIsyapgrDNLVLTIGDPNAQRWLGVDGHM 87
Cdd:cd03888 9 EILEDLKELVAIPSVrdEATEGApfgegPRKALDKFL--DLAKRLgFKTKNI------DNYAGYAEYGEGEEVLGILGHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 88 DVVDAGDpnKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIaheeLDHGVQLMATV------GEE-----IDNY 156
Cdd:cd03888 81 DVVPAGE--GWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKIL----KDLGLPLKKKIrlifgtDEEtgwkcIEHY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 157 GARQlAAAGYG---DRLTGLLVAEPGNSNVDA------------------------------------------------ 185
Cdd:cd03888 155 FEHE-EYPDFGftpDAEFPVINGEKGIVTVDLtfkidddkgyrlisikggeatnmvpdkaeavipgkdkeelalsaatdl 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 186 ---AERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAF---ANAALTATAPLQ-----------------AKDDPILGHA 242
Cdd:cd03888 234 kgnIEIDDGGVELTVTGKSAHASAPEKGVNAITLLAKFlaeLNKDGNDKDFIKflaknlhedyngkklgiNFEDEVMGEL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 243 THNIDIIhggnQINslPESAYLRGNVRTTMIADNDAFIAALKQAAktsvpKGVHLSLSIDSVLSAAAAAPDNALIQKVQQ 322
Cdd:cd03888 314 TLNPGII----TLD--DGKLELGLNVRYPVGTSAEDIIKQIEEAL-----EKYGVEVEGHKHQKPLYVPKDSPLVKTLLK 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872387442 323 ARQRIGLQRGAVAYRTGITDAALFfhdgLDLAIYGP----GNDTSHETDEYVDLQDVFDSIKVY 382
Cdd:cd03888 383 VYEEQTGKEGEPVAIGGGTYAREL----PNGVAFGPefpgQKDTMHQANEFIPIDDLIKALAIY 442
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
10-375 |
1.54e-18 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 86.02 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 10 LTDEEQQVTDLLQAMV----RIPSVAAKEGQVADLIEAFLaPELSTglikrERISYAPGRDNLVLTIGDPNAQrwlgVDG 85
Cdd:PRK08737 1 MTDLLESTLDHLQALVsfdtRNPPRAITTGGIFDYLRAQL-PGFQV-----EVIDHGAGAVSLYAVRGTPKYL----FNV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 86 HMDVVDAGDpnKWQFPPFSAQIEDGKLYGRGATDMKsGLAAAVVAfkqiAHEELDHGVQLMATVGEEIDNygARQLAA-A 164
Cdd:PRK08737 71 HLDTVPDSP--HWSADPHVMRRTDDRVIGLGVCDIK-GAAAALLA----AANAGDGDAAFLFSSDEEAND--PRCVAAfL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 165 GYGDRLTGLLVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRP-DLGANAIHGLFAFANAALTATAPLQAKDDPILGHAT 243
Cdd:PRK08737 142 ARGIPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKqDPSASALHQAMRWGGQALDHVESLAHARFGGLTGLR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 244 HNIDIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALkqaAKTSVPKGVHLSLSI--DSVLSAAAAAPDNALIQKVQ 321
Cdd:PRK08737 222 FNIGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATF---AGFAEPAAATFEETFrgPSLPSGDIARAEERRLAARD 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 872387442 322 QArQRIGLQRG-AVAYrtgITDAALFFHDGLDLAIYGPGN-DTSHETDEYVDLQDV 375
Cdd:PRK08737 299 VA-DALDLPIGnAVDF---WTEASLFSAAGYTALVYGPGDiAQAHTADEFVTLDQL 350
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
75-299 |
1.84e-17 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 83.09 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 75 PNAQRWLGVDGHMDVVdagdpnkwqFPPFSA-----QIEDGKLYGRGATDMKSGLA---AAVVAFKQIAHEElDHGVQLM 146
Cdd:PRK07338 89 PEAPRQVLLTGHMDTV---------FPADHPfqtlsWLDDGTLNGPGVADMKGGIVvmlAALLAFERSPLAD-KLGYDVL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 147 ATVGEEIDNYGARQL---AAAGYgdrlTGLLVAEPG--NSNVDAAERGIIDYTLTAQGKAAHSSR-PDLGANAIHGLFAF 220
Cdd:PRK07338 159 INPDEEIGSPASAPLlaeLARGK----HAALTYEPAlpDGTLAGARKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 221 AnaalTATAPLQAKDDPIlghaTHNIDIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQ-AAKTSVPKGVHLSL 299
Cdd:PRK07338 235 A----LALHALNGQRDGV----TVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKlIAQVNQRHGVSLHL 306
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
19-383 |
2.01e-17 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 82.53 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 19 DLLQAMVRIPSVAAKEGQVADLIEAFLApelSTGLIKRERIsyapGRDNLVLTIGDPNAQRWLGVDGHMDVVDAGDPnkw 98
Cdd:cd03896 2 DTAIELGEIPAPTFREGARADLVAEWMA---DLGLGDVERD----GRGNVVGRLRGTGGGPALLFSAHLDTVFPGDT--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 99 qfpPFSAQIEDGKLYGRGATDMKSGLA---AAVVAFKQiAHEELDHGVQLMATVGEE--IDNYGARQLAAAgYGDRLTGL 173
Cdd:cd03896 72 ---PATVRHEGGRIYGPGIGDNKGSLAcllAMARAMKE-AGAALKGDVVFAANVGEEglGDLRGARYLLSA-HGARLDYF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 174 LVAEPGNSNVDAAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFafanaalTATAPLQAKDDPILGHATHNIDIIHGGN 253
Cdd:cd03896 147 VVAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMA-------KLVEALYEWAAPYVPKTTFAAIRGGGGT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 254 QINSLPESAYLRGNVRTtmiaDNDAFIAALKQAAKTSVPKGVH----LSLSIDSVLS--AAAAAPDNALIQKVQQARQRI 327
Cdd:cd03896 220 SVNRIANLCSMYLDIRS----NPDAELADVQREVEAVVSKLAAkhlrVKARVKPVGDrpGGEAQGTEPLVNAAVAAHREV 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 872387442 328 GLQrgaVAYRTGITDAALFFHDGLDLAIYGPGN-DTSHETDEYVDLQDVFDSIKVYK 383
Cdd:cd03896 296 GGD---PRPGSSSTDANPANSLGIPAVTYGLGRgGNAHRGDEYVLKDDMLKGAKAYL 349
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
186-295 |
4.96e-17 |
|
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: 76.23 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 186 AERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAaltatapLQAKDDPI---LGHATHNIDIIHGGNQINSLPESA 262
Cdd:pfam07687 2 GHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAE-------LPAEYGDIgfdFPRTTLNITGIEGGTATNVIPAEA 74
|
90 100 110
....*....|....*....|....*....|...
gi 872387442 263 YLRGNVRTTMIADNDAFIAALKQAAKTSVPKGV 295
Cdd:pfam07687 75 EAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
14-382 |
8.42e-17 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 80.60 E-value: 8.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 14 EQQVTDLLQAMVRIPSVAAKEGQVADLIEAfLAPELSTGL-IKRERISYAPGRDNLVLTigdpnaqrwlgvdGHMDVVda 92
Cdd:PRK00466 9 KQKAKELLLDLLSIYTPSGNETNATKFFEK-ISNELNLKLeILPDSNSFILGEGDILLA-------------SHVDTV-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 93 gdpnkwqfPPF-SAQIEDGKLYGRGATDMKSGLAAAVVAfKQIAHEElDHGVQLMATVGEEIDNYGARQLAAAgyGDRLT 171
Cdd:PRK00466 73 --------PGYiEPKIEGEVIYGRGAVDAKGPLISMIIA-AWLLNEK-GIKVMVSGLADEESTSIGAKELVSK--GFNFK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 172 GLLVAEPGNSNVDAAE-RGIIDYTLTAQGKAAHSSRPDlgANAIhglFAFANAALTATAPLQAKDDPILghathNIDIIH 250
Cdd:PRK00466 141 HIIVGEPSNGTDIVVEyRGSIQLDIMCEGTPEHSSSAK--SNLI---VDISKKIIEVYKQPENYDKPSI-----VPTIIR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 251 GGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSvpkgvhlSLSIDSVLSAAAAAPDNALIQKVQQARQRIGLQ 330
Cdd:PRK00466 211 AGESYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQEC-------GLKIVDETPPVKVSINNPVVKALMRALLKQNIK 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 872387442 331 RGAVAYRtGITDAALFFHDGLDLAIYGPGNDT-SHETDEYVDLQDVFDSIKVY 382
Cdd:PRK00466 284 PRLVRKA-GTSDMNILQKITTSIATYGPGNSMlEHTNQEKITLDEIYIAVKTY 335
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
13-375 |
1.64e-16 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 80.45 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 13 EEQQVTDLLQAMVRIPSVAAKE---GQVADLIEAFLApelSTGLiKRERISYAPGRDNLVLTIGDPNAQRWLGVDGHMDV 89
Cdd:PRK06133 35 EQPAYLDTLKELVSIESGSGDAeglKQVAALLAERLK---ALGA-KVERAPTPPSAGDMVVATFKGTGKRRIMLIAHMDT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 90 VDAGDPNKWQfpPFsaQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHGVQLmaTV----GEEIDNYGARQLAAAg 165
Cdd:PRK06133 111 VYLPGMLAKQ--PF--RIDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTL--TVlfnpDEETGSPGSRELIAE- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 166 YGDRLTGLLVAEPG--NSNVDAAERGIIDYTLTAQGKAAHS-SRPDLGANAIHGLfafanaaltATAPLQAKD--DPILG 240
Cdd:PRK06133 184 LAAQHDVVFSCEPGraKDALTLATSGIATALLEVKGKASHAgAAPELGRNALYEL---------AHQLLQLRDlgDPAKG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 241 hATHNIDIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSVPKGVHLSLSIDSVLSAAAAAP-DNALIQK 319
Cdd:PRK06133 255 -TTLNWTVAKAGTNRNVIPASASAQADVRYLDPAEFDRLEADLQEKVKNKLVPDTEVTLRFERGRPPLEANAaSRALAEH 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872387442 320 VQQARQRIGLQRGAVAYRTG-ITDAALF-------FHDGLDLAIYGpgndtSHETDEYVDLQDV 375
Cdd:PRK06133 334 AQGIYGELGRRLEPIDMGTGgGTDAAFAagsgkaaVLEGFGLVGFG-----AHSNDEYIELNSI 392
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
21-269 |
1.66e-16 |
|
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: 80.76 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 21 LQAMVRIPSVAAKEGQVADLIEAFLA------------PELSTgLIKRERIsyapGRDNLVLTigdpnaqrWLGVD---- 84
Cdd:cd05674 4 LSGAVQIPTVSFDDMPPIDEDERWDAfykfhdylektfPLVHK-TLKVEVV----NEYGLLYT--------WEGSDpslk 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 85 -----GHMDVVDA--GDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIaheeLDHGVQLMATV----G--E 151
Cdd:cd05674 71 plllmAHQDVVPVnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELL----LKRGFKPRRTIilafGhdE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 152 EID-NYGARQLAA---AGYGDR----------------LTGLLVAEPGNsnvdaAERGIIDYTLTAQGKAAHSSRP---- 207
Cdd:cd05674 147 EVGgERGAGAIAElllERYGVDglaaildeggavlegvFLGVPFALPGV-----AEKGYMDVEITVHTPGGHSSVPpkht 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 208 ----------DLGANAIHGLFAFANAA---LTATAPLQAKDDPILGHATHN----------------------------- 245
Cdd:cd05674 222 gigilseavaALEANPFPPKLTPGNPYygmLQCLAEHSPLPPRSLKSNLWLaspllkallasellstspltrallrttqa 301
|
330 340
....*....|....*....|....
gi 872387442 246 IDIIHGGNQINSLPESAYLRGNVR 269
Cdd:cd05674 302 VDIINGGVKINALPETATATVNHR 325
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
28-288 |
2.35e-16 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 80.20 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 28 PSVAAKEGQVADLIEAFLAPELST--GLIKRERISYAPGRDNLVLTIGDPNAQRWLGVDG-HMDVVDAgDPNKWQFPPFS 104
Cdd:cd08012 25 PQLVPKEDNAGRHVLEALTPYSTEngGPLVIDHVSYVKGRGNIIVEYPGTVDGKTVSFVGsHMDVVTA-NPETWEFDPFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 105 AQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEE--LDHGVQLMATVGEE---IDNYGARQLAAAGYGDRL-TGLLVAep 178
Cdd:cd08012 104 LSIDGDKLYGRGTTDCLGHVALVTELFRQLATEKpaLKRTVVAVFIANEEnseIPGVGVDALVKSGLLDNLkSGPLYW-- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 179 gnsnVDAAER-------GIIDYTLTAQGKAAHSSRPDLGANAIHglfafanAALTATAPLQAK---------DDPILGHA 242
Cdd:cd08012 182 ----VDSADSqpcigtgGMVTWKLTATGKLFHSGLPHKAINALE-------LVMEALAEIQKRfyidfpphpKEEVYGFA 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 872387442 243 THN----IDIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAAK 288
Cdd:cd08012 251 TPStmkpTQWSYPGGSINQIPGECTICGDCRLTPFYDVKEVREKLEEYVD 300
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
17-214 |
3.97e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 79.51 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 17 VTDLLQAMVRIPSV-----------AAKEGQVADLIEAFLAPELstglikrerISYAPGRDNLVLTI--GDPNAQRWLgV 83
Cdd:PRK07906 1 VVDLCSELIRIDTTntgdgtgkgerEAAEYVAEKLAEVGLEPTY---------LESAPGRANVVARLpgADPSRPALL-V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 84 DGHMDVVDAgDPNKWQFPPFSAQIEDGKLYGRGATDMKSG----LAAA--------------VVAFkqIAHEE------- 138
Cdd:PRK07906 71 HGHLDVVPA-EAADWSVHPFSGEIRDGYVWGRGAVDMKDMdammLAVVrhlartgrrpprdlVFAF--VADEEaggtyga 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 872387442 139 ---LDHGVQLMATVGEEIDNYGARQLAAAGyGDRLtgLLVAepgnsnvdAAERGIIDYTLTAQGKAAHSSRPDlGANAI 214
Cdd:PRK07906 148 hwlVDNHPELFEGVTEAISEVGGFSLTVPG-RDRL--YLIE--------TAEKGLAWMRLTARGRAGHGSMVN-DDNAV 214
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
21-382 |
3.20e-15 |
|
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: 76.65 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 21 LQAMVRIPSV----AAKEGQ-----VADLIEAFLapELStglikrERISYAPGR-DNLVLTIGDPNAQRWLGVDGHMDVV 90
Cdd:TIGR01887 8 LKELIAIDSVedleKAKEGApfgegPRKALDKFL--EIA------KRDGFTTENvDNYAGYIEYGQGEEVLGILGHLDVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 91 DAGDpnKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAheelDHGVQLMATV------GEE-----IDNY-GA 158
Cdd:TIGR01887 80 PAGD--GWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILK----ELGLKLKKKIrfifgtDEEsgwkcIDYYfEH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 159 RQLAAAGYG-DRLTGLLVAEPGNSNVD----------------------------------------------------- 184
Cdd:TIGR01887 154 EEMPDIGFTpDAEFPIIYGEKGITTLEikfkddtegdvvlesfkageaynmvpdhatavisgkklteveqlkfvffiake 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 185 ---AAERGIIDYTLTAQGKAAHSSRPDLGANAIHGLFAF---------ANAALTATAPLQAKD-----------DPILGH 241
Cdd:TIGR01887 234 legDFEVNDGTLTITLEGKSAHGSAPEKGINAATYLALFlaqlnlaggAKAFLQFLAEYLHEDhygeklgikfhDDVSGD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 242 ATHNIDIIHGGNQinslpESAYLRGNVRTTMIADNDAFIAalKQAAKTSVPKGVHLslsiDSVLSAAAAAPDNALIQKVQ 321
Cdd:TIGR01887 314 LTMNVGVIDYENA-----EAGLIGLNVRYPVGNDPDTMLK--NELAKESGVVEVTL----NGYLKPLYVPKDDPLVQTLM 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872387442 322 QARQRiglQRGAVAYRTGITDA--ALFFHDGLDL-AIYGPGNDTSHETDEYVDLQDVFDSIKVY 382
Cdd:TIGR01887 383 KVYEK---QTGDEGEPVAIGGGtyARLMPNGVAFgALFPGEEDTMHQANEYIMIDDLLLATAIY 443
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
21-207 |
4.56e-15 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 76.52 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 21 LQAMVRIPSVAAKEGQVADlIEAFLA---------PELSTGLiKRERIsyapGRDNLVLTigdpnaqrWLGVD------- 84
Cdd:PRK08262 50 LSEAIRFRTISNRDRAEDD-AAAFDAlhahleesyPAVHAAL-EREVV----GGHSLLYT--------WKGSDpslkpiv 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 85 --GHMDVV--DAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAfkqiAHEELDHGVQLMATV------GEEID 154
Cdd:PRK08262 116 lmAHQDVVpvAPGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEA----AEALLAQGFQPRRTIylafghDEEVG 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872387442 155 NYGARQLAA--AGYGDRLT-----GLLVAEPGNSNVDA-------AERGIIDYTLTAQGKAAHSSRP 207
Cdd:PRK08262 192 GLGARAIAEllKERGVRLAfvldeGGAITEGVLPGVKKpvaligvAEKGYATLELTARATGGHSSMP 258
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
67-153 |
7.78e-14 |
|
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: 69.77 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 67 NLVLTIGDPNAQRWLGVDGHMDVVDAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQ--IAHEELDHGVQ 144
Cdd:cd18669 1 NVIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLlkENGFKLKGTVV 80
|
....*....
gi 872387442 145 LMATVGEEI 153
Cdd:cd18669 81 VAFTPDEEV 89
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
81-288 |
3.88e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 70.49 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 81 LGVDGHMDVVDAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIaheeLDHGVQLMATV----------- 149
Cdd:PRK07205 78 LAILCHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKAL----LDAGVQFNKRIrfifgtdeetl 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 150 ---------GEEIDNYG---------------ARQLAAAGYGD-----RLTGLLVAEPGNSNVD---------AAERGII 191
Cdd:PRK07205 154 wrcmnryneVEEQATMGfapdssfpltyaekgLLQAKLVGPGSdqlelEVGQAFNVVPAKASYQgpkleavkkELDKLGF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 192 DYTLTAQ-----GKAAHSSRPDLGANAI------------HGLFAF-ANAA---LTATAPLQAKDDPILGHATHNIdiih 250
Cdd:PRK07205 234 EYVVKENevtvlGKSVHAKDAPQGINAVirlakalvvlepHPALDFlANVIgedATGLNIFGDIEDEPSGKLSFNI---- 309
|
250 260 270
....*....|....*....|....*....|....*...
gi 872387442 251 GGNQINslPESAYLRGNVRTTMIADNDAFIAALKQAAK 288
Cdd:PRK07205 310 AGLTIT--KEKSEIRIDIRIPVLADKEKLVQQLSQKAQ 345
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
13-389 |
4.58e-13 |
|
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: 69.99 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 13 EEQQVTdLLQAMVRIPSVAAK---EGQVADLIEAflAPELStglIKRERISYAPGRDNLVLTigdpnaqrWLGVD----- 84
Cdd:cd05646 1 EDPAVT-RFREYLRINTVHPNpdyDACVEFLKRQ--ADELG---LPVRVIEVVPGKPVVVLT--------WEGSNpelps 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 85 ----GHMDVVDAgDPNKWQFPPFSAQI-EDGKLYGRGATDMKS-GLA--AAVVAFKQiaheeldHGVQLMATV------G 150
Cdd:cd05646 67 illnSHTDVVPV-FEEKWTHDPFSAHKdEDGNIYARGAQDMKCvGIQylEAIRRLKA-------SGFKPKRTIhlsfvpD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 151 EEI-DNYGARQLAAAGYGDRLT-------GLlvAEPGNS-NVDAAERGIIDYTLTAQGKAAHSSR--PDlgaNAIHGLFA 219
Cdd:cd05646 139 EEIgGHDGMEKFVKTEEFKKLNvgfaldeGL--ASPTEEyRVFYGERSPWWVVITAPGTPGHGSKllEN---TAGEKLRK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 220 FANAALT----ATAPLQAKDDPILGHATH-NIDIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQAAKTSVPkG 294
Cdd:cd05646 214 VIESIMEfresQKQRLKSNPNLTLGDVTTvNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGR-G 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 295 VHLSLSIDSVLSAAAAAPD-NALIQKVQQARQRIGLQrGAVAYRTGITDAALFFHDGLDLAIYGPGNDTS---HETDEYV 370
Cdd:cd05646 293 VTYEFEQKSPEKDPTSLDDsNPWWAAFKKAVKEMGLK-LKPEIFPAATDSRYIRALGIPALGFSPMNNTPillHDHNEFL 371
|
410 420
....*....|....*....|
gi 872387442 371 DlQDVF-DSIKVYKDVFKNY 389
Cdd:cd05646 372 N-EDVFlRGIEIYEKIIPAL 390
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
67-153 |
1.69e-12 |
|
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: 65.91 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 67 NLVLTIGDPNAQRWLGVDGHMDVVDAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQ--IAHEELDHGVQ 144
Cdd:cd03873 1 NLIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRlkENGFKPKGTIV 80
|
....*....
gi 872387442 145 LMATVGEEI 153
Cdd:cd03873 81 VAFTADEEV 89
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
13-382 |
3.50e-12 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 67.56 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 13 EEQQVTDLlQAMVRIPSV----AAKEGQ-----VADLIEAFLApelstgLIKRE------------RISYAPGRDnlvlt 71
Cdd:PRK07318 13 KDDLIEDL-QELLRINSVrddsKAKEGApfgpgPVKALEKFLE------IAERDgfktknvdnyagHIEYGEGEE----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 72 igdpnaqrWLGVDGHMDVVDAGDpnKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQI----------------- 134
Cdd:PRK07318 81 --------VLGILGHLDVVPAGD--GWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIkelglplskkvrfivgt 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 135 -------------AHEEL----------------DHGVQLMATVGEEIDNYGARQLAAAGYGDRL-------TGLLVAEP 178
Cdd:PRK07318 151 deesgwkcmdyyfEHEEApdfgfspdaefpiingEKGITTFDLVHFEGENEGDYVLVSFKSGLREnmvpdsaEAVITGDD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 179 GNSNVDAAERGIID-------------YTLTAQGKAAHSSRPDLGANAIHGLFAF---------ANAALTATAPLQAKD- 235
Cdd:PRK07318 231 LDDLIAAFEAFLAEnglkgeleeeggkLVLTVIGKSAHGSTPEKGVNAATYLAKFlnqlnldgdAKAFLDFAAEYLHEDt 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 236 ----------DPILGHATHNIDIIHGGNQinslpESAYLRGNVRTTMIADNDAFIAALKQAAKtsvPKGVHLSLSIDSVL 305
Cdd:PRK07318 311 rgeklgiayeDDVMGDLTMNVGVFSFDEE-----KGGTLGLNFRYPVGTDFEKIKAKLEKLIG---VTGVELSEHEHQKP 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 306 saAAAAPDNALIQKVQQARQR----------IG-------LQRGaVAYrtgitdAALFfhdgldlaiygPGN-DTSHETD 367
Cdd:PRK07318 383 --HYVPKDDPLVKTLLKVYEKqtglkgeeqvIGggtyarlLKRG-VAF------GAMF-----------PGSeDTMHQAN 442
|
490
....*....|....*
gi 872387442 368 EYVDLQDVFDSIKVY 382
Cdd:PRK07318 443 EYIEIDDLIKAAAIY 457
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
9-285 |
8.67e-12 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 65.97 E-value: 8.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 9 SLTDEEQQVTDLLQAMVRIPSVAAKEGQVADLieAFL---APELStglIKRERISYAPGRDNLVLTI--GDPNAQRWLgV 83
Cdd:TIGR01880 3 SSKWEEDIAVTRFREYLRINTVQPNPDYAACV--DFLikqADELG---LARKTIEFVPGKPVVVLTWpgSNPELPSIL-L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 84 DGHMDVVDAgDPNKWQFPPFSAQI-EDGKLYGRGATDMKS-GLA--AAVVAFKQIAHEELdHGVQLMATVGEEI-DNYGA 158
Cdd:TIGR01880 77 NSHTDVVPV-FREHWTHPPFSAFKdEDGNIYARGAQDMKCvGVQylEAVRNLKASGFKFK-RTIHISFVPDEEIgGHDGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 159 RQLAAAGYGDRLTGLLVAEPGNSNVDA------AERGIIDYTLTAQGKAAHSSR--PDLGANAIHGLFAFANA-ALTATA 229
Cdd:TIGR01880 155 EKFAKTDEFKALNLGFALDEGLASPDDvyrvfyAERVPWWVVVTAPGNPGHGSKlmENTAMEKLEKSVESIRRfRESQFQ 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 872387442 230 PLQAKDDPILGHATH-NIDIIHGGNQINSLPESAYLRGNVRTTMIADNDAFIAALKQ 285
Cdd:TIGR01880 235 LLQSNPDLAIGDVTSvNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDE 291
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
21-164 |
2.51e-11 |
|
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: 64.66 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 21 LQAMVRIPSVAAKEGQVADLIEA--FLAPELstgliKRE----RISYAPGRDNLVLT--IGDPNAQRWLgVDGHMDVVDA 92
Cdd:cd03893 4 LAELVAIPSVSAQPDRREELRRAaeWLADLL-----RRLgftvEIVDTSNGAPVVFAefPGAPGAPTVL-LYGHYDVQPA 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872387442 93 GDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIA--HEELDHGVQLMATVGEEIDNYGARQLAAA 164
Cdd:cd03893 78 GDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMqqGGDLPVNVKFIIEGEEESGSPSLDQLVEA 151
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
14-235 |
3.92e-11 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 64.22 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 14 EQQVTDLLQAMVRIPSVAaKEGQVADLIEAFLA-PELSTGLIKRERISYApGRDNLVLTIG-DPNAQRWLGVDGHMDVVD 91
Cdd:PRK06156 45 GAAAIESLRELVAFPTVR-VEGVPQHENPEFIGfKKLLKSLARDFGLDYR-NVDNRVLEIGlGGSGSDKVGILTHADVVP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 92 AgDPNKWQFP-----PFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEE--LDHGVQLMATVGEEIDNYGARQ---- 160
Cdd:PRK06156 123 A-NPELWVLDgtrldPFKVTLVGDRLYGRGTEDDKGAIVTALYAMKAIKDSGlpLARRIELLVYTTEETDGDPLKYyler 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 161 -----------------LAAAGYG------------------DRLTG---------------------LLVAE------- 177
Cdd:PRK06156 202 ytppdynitldaeypvvTAEKGWGtimatfpkraadgkgaeiVAMTGgafanqipqtavatlsggdpaALAAAlqaaaaa 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872387442 178 -----PGNSNVDAAERGiIDYTLTAQGKAAHSSRPDLGANAIHGLFAFANAALTATAPLQAKD 235
Cdd:PRK06156 282 qvkrhGGGFSIDFKRDG-KDVTITVTGKSAHSSTPESGVNPVTRLALFLQSLDGDLPHNHAAD 343
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
14-159 |
5.01e-11 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 64.11 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 14 EQQVTDLLQAMVRIPSVA--AKEGQVADLIEAFLA--------PE---------------LSTGLIKRERisyaPGRDNL 68
Cdd:COG4187 7 KEQLEELLCELVSIPSVTgtEGEKEVAEFIYEKLSelpyfqenPEhlglhplpddplgrkNVTALVKGKG----ESKKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 69 VLTigdpnaqrwlgvdGHMDVVDAGDPNKWQ-----------------FPPFSAQ-IEDGK-LYGRGATDMKSGLAAAVV 129
Cdd:COG4187 83 ILI-------------SHFDVVDVEDYGSLKplafdpeeltealkeikLPEDVRKdLESGEwLFGRGTMDMKAGLALHLA 149
|
170 180 190
....*....|....*....|....*....|.
gi 872387442 130 AFKQIA-HEELDHGVQLMATVGEEIDNYGAR 159
Cdd:COG4187 150 LLEEASeNEEFPGNLLLLAVPDEEVNSAGMR 180
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
16-204 |
1.43e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 62.62 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 16 QVTDLLQAMVRIPSVAAKEGQVADLIEA--FLAPELSTGLIKRERISYAPGRDNLV-LTIGDPNAQRWLgVDGHMDVVDA 92
Cdd:PRK07907 19 RVRADLEELVRIPSVAADPFRREEVARSaeWVADLLREAGFDDVRVVSADGAPAVIgTRPAPPGAPTVL-LYAHHDVQPP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 93 GDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKqiAHEE-LDHGVQLMATVGEEIDNYGARQLAAAgYGDRLT 171
Cdd:PRK07907 98 GDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALR--ALGGdLPVGVTVFVEGEEEMGSPSLERLLAE-HPDLLA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 872387442 172 G--LLVAEPGNSNVD-----AAERGIIDYTLTAQ--GKAAHS 204
Cdd:PRK07907 175 AdvIVIADSGNWSVGvpaltTSLRGNADVVVTVRtlEHAVHS 216
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
15-164 |
2.07e-10 |
|
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: 62.36 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 15 QQVTDLLQAMVRIPSVAAKEGQV--ADLIEAFLA--------PELSTGLIKRERisyaPGRDNLV-LTIGDPNAQRWLGV 83
Cdd:cd05654 1 ERLEQLLKSLVSWPSVTGTEGERsfADFLKEILKelpyfkenPSHVWQLLPPDD----LGRRNVTaLVKGKKPSKRTIIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 84 DGHMDVVD----------AGDPNKWQ---------FPPFSAQ-IEDGK-LYGRGATDMKSGLAAAVVAFKQ-IAHEELDH 141
Cdd:cd05654 77 ISHFDTVGiedygelkdiAFDPDELTkafseyveeLDEEVREdLLSGEwLFGRGTMDMKSGLAVHLALLEQaSEDEDFDG 156
|
170 180
....*....|....*....|...
gi 872387442 142 GVQLMATVGEEIDNYGARQLAAA 164
Cdd:cd05654 157 NLLLMAVPDEEVNSRGMRAAVPA 179
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
19-205 |
2.64e-10 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 61.59 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 19 DLLQAMVRIPSVAAKEG---QVADLIEAFLapelsTGLIKRERISYAPGRDNLVLTIGDpNAQRWLGVDGHMDVVDAgDP 95
Cdd:cd05681 3 EDLRDLLKIPSVSAQGRgipETADFLKEFL-----RRLGAEVEIFETDGNPIVYAEFNS-GDAKTLLFYNHYDVQPA-EP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 96 -NKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFK--QIAHEELDHGVQLMATVGEEIdnyGARQLA--AAGYGDRL 170
Cdd:cd05681 76 lELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRalLQHLGELPVNIKFLVEGEEEV---GSPNLEkfVAEHADLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 872387442 171 TG-LLVAEPGnsNVDAAER--------GIIDYTLTAQGKAA--HSS 205
Cdd:cd05681 153 KAdGCIWEGG--GKNPKGRpqislgvkGIVYVELRVKTADFdlHSS 196
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
21-217 |
4.50e-10 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 60.79 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 21 LQAMVRIPSVAAKEGQVADLIEA--FLAPEL-STGLIKRERISyaPGRDNLVL--TIGDPNAQRWLgVDGHMDVVDAgDP 95
Cdd:cd05680 4 LFELLRIPSVSADPAHKGDVRRAaeWLADKLtEAGFEHTEVLP--TGGHPLVYaeWLGAPGAPTVL-VYGHYDVQPP-DP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 96 -NKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQI--AHEELDHGVQLMATVGEEIdnyGARQLAA--AGYGDRL 170
Cdd:cd05680 80 lELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWlaVEGALPVNVKFLIEGEEEI---GSPSLPAflEENAERL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 872387442 171 TG--LLVA-----EPGNSNVDAAERGIIDYTLTAQG--KAAHSSRpdLG---ANAIHGL 217
Cdd:cd05680 157 AAdvVLVSdtsmwSPDTPTITYGLRGLAYLEISVTGpnRDLHSGS--YGgavPNPANAL 213
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
85-160 |
1.12e-09 |
|
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: 59.66 E-value: 1.12e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872387442 85 GHMDVVDAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHE-ELDHGVQLMATVGEEIDNYGARQ 160
Cdd:cd05677 78 GHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQEgELDNDVVFLIEGEEESGSPGFKE 154
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
86-162 |
1.76e-09 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 59.02 E-value: 1.76e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872387442 86 HMDVVDAGdPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDHGVQLMATVGEEIDNYGARQLA 162
Cdd:PRK08554 71 HFDVVPVN-PEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLNGKVIFAFTGDEEIGGAMAMHIA 146
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
74-153 |
6.35e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 57.46 E-value: 6.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 74 DPNAQRWLGVDGHMDVVDAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHE-ELDHGVQLMATVGEE 152
Cdd:PRK06446 58 NVGAKKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKhKLNVNVKFLYEGEEE 137
|
.
gi 872387442 153 I 153
Cdd:PRK06446 138 I 138
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
11-139 |
2.68e-08 |
|
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: 55.30 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 11 TDEEQQVTDLLQAmVRIPSVAAKEGQVADLIEA--FLAPELSTglIKRERISYAPGRDNL----------VL--TIGDPN 76
Cdd:cd05676 7 EHQDEFIERLREA-VAIQSVSADPEKRPELIRMmeWAAERLEK--LGFKVELVDIGTQTLpdgeelplppVLlgRLGSDP 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872387442 77 AQRWLGVDGHMDVVDAGDPNKWQFPPFSAQIEDGKLYGRGATDMKSGLAA---AVVAFKQIaHEEL 139
Cdd:cd05676 84 SKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGwlnAIEAYQKL-GQEL 148
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
83-262 |
1.66e-07 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 52.86 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 83 VDGHMDVVD-AGDPNKWQFppfsaQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEELDH--GVQLMATVGEEIDNYGAR 159
Cdd:PRK07473 80 IAGHMDTVHpVGTLEKLPW-----RREGNKCYGPGILDMKGGNYLALEAIRQLARAGITTplPITVLFTPDEEVGTPSTR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 160 QLAAAgYGDRLTGLLVAEPG--NSNVDAAERGIIDYTLTAQGKAAHS-SRPDLGANAIHglfAFANAALTATAplQAKDD 236
Cdd:PRK07473 155 DLIEA-EAARNKYVLVPEPGrpDNGVVTGRYAIARFNLEATGRPSHAgATLSEGRSAIR---EMARQILAIDA--MTTED 228
|
170 180
....*....|....*....|....*.
gi 872387442 237 pilghATHNIDIIHGGNQINSLPESA 262
Cdd:PRK07473 229 -----CTFSVGIVHGGQWVNCVATTC 249
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
122-288 |
9.10e-07 |
|
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 50.50 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 122 SGLAAAVVAFKQIaHEELDHGVQLMATVGEEIDNyGARQLAAAGYGDRL---------------TGLLVAEPG--NSNVD 184
Cdd:COG1473 107 AMLLGAAKALAEL-RDELKGTVRLIFQPAEEGGG-GAKAMIEDGLLDRPdvdaifglhvwpglpVGTIGVRPGpiMAAAD 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 185 AaergiIDYTLTaqGKAAHSSRPDLGANAIHGLFAFANAALTATAPLQAKDDPILGHATHnidiIHGGNQINSLPESAYL 264
Cdd:COG1473 185 S-----FEITIK--GKGGHAAAPHLGIDPIVAAAQIVTALQTIVSRNVDPLDPAVVTVGI----IHGGTAPNVIPDEAEL 253
|
170 180
....*....|....*....|....
gi 872387442 265 RGNVRTTMIADNDAFIAALKQAAK 288
Cdd:COG1473 254 EGTVRTFDPEVRELLEERIERIAE 277
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
116-270 |
1.74e-06 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 49.58 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 116 GATDMKSGLAAAVVAFKQiaheELDHGVQLMATVGEEIDNYGARQLAAAGY---GDRLTGLLVAEPGNSNVDAAERGII- 191
Cdd:cd08021 103 GHTAMLLGAAKVLAENKD----EIKGTVRFIFQPAEEVPPGGAKPMIEAGVlegVDAVFGLHLWSTLPTGTIAVRPGAIm 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 192 ----DYTLTAQGKAAHSSRPDLGANAIHGLFAFANAALTATA----PLQAkddpilghATHNIDIIHGGNQINSLPESAY 263
Cdd:cd08021 179 aapdEFDITIKGKGGHGSMPHETVDPIVIAAQIVTALQTIVSrrvdPLDP--------AVVTIGTFQGGTSFNVIPDTVE 250
|
....*..
gi 872387442 264 LRGNVRT 270
Cdd:cd08021 251 LKGTVRT 257
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
119-288 |
2.55e-06 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 48.87 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 119 DMKSGLAAAVVAFKQIAhEELDHGVQLMATVG--EEIDN-YGARQlaaagYGDRLTGLLVAEPG--NSNVDaaergIIDY 193
Cdd:cd08019 105 EIKDTIKGTVKLIFQPA-EEVGEGAKQMIEEGvlEDVDAvFGIHL-----WSDVPAGKISVEAGprMASAD-----IFKI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 194 TLTaqGKAAHSSRPDLGANAIHGLFAFANAALTATAplqAKDDPiLGHATHNIDIIHGGNQINSLPESAYLRGNVRTTMI 273
Cdd:cd08019 174 EVK--GKGGHGSMPHQGIDAVLAAASIVMNLQSIVS---REIDP-LEPVVVTVGKLNSGTRFNVIADEAKIEGTLRTFNP 247
|
170
....*....|....*
gi 872387442 274 ADNDAFIAALKQAAK 288
Cdd:cd08019 248 ETREKTPEIIERIAK 262
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
10-121 |
4.19e-06 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 48.59 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 10 LTDEEQQVTDLLQAMVRIPSVAAKEGQVADLIEA--FLAPELSTglIKRERISyapgrdnLVLTIGDPNA-QRWLGVD-- 84
Cdd:PRK08201 9 LRERREAHLEELKEFLRIPSISALSEHKEDVRKAaeWLAGALEK--AGLEHVE-------IMETAGHPIVyADWLHAPgk 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 872387442 85 ------GHMDVVDAGDPNKWQFPPFSAQIEDGKLYGRGATDMK 121
Cdd:PRK08201 80 ptvliyGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDK 122
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
120-288 |
1.23e-04 |
|
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: 43.87 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 120 MKSGLAAAVVaFKQIAHeeLDHG-VQLMATVGEEIDNyGARQLAAAGYGDRLTGLLVAEPGnSNVDAAERGIIDYTLTAQ 198
Cdd:TIGR01891 95 TAILLGTAKL-LKKLAD--LLEGtVRLIFQPAEEGGG-GATKMIEDGVLDDVDAILGLHPD-PSIPAGTVGLRPGTIMAA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 199 ---------GKAAHSSRPDLGANAIHGLfAFANAALTATAPLQAkdDPILGHATHnIDIIHGGNQINSLPESAYLRGNVR 269
Cdd:TIGR01891 170 adkfevtihGKGAHAARPHLGRDALDAA-AQLVVALQQIVSRNV--DPSRPAVVS-VGIIEAGGAPNVIPDKASMSGTVR 245
|
170
....*....|....*....
gi 872387442 270 TTMIADNDAFIAALKQAAK 288
Cdd:TIGR01891 246 SLDPEVRDQIIDRIERIVE 264
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
123-270 |
1.64e-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: 43.42 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 123 GLAAAVVAFKQiaHEELDHGVQLMATVGEEIDNYGARQLAAAGYGDRLTGLLV--AEPgnsNVDAAERGIIDYTLTA--- 197
Cdd:cd08014 97 ALGAALVLAAL--EEELPGRVRLIFQPAEETMPGGALDMIRAGALDGVSAIFAlhVDP---RLPVGRVGVRYGPITAaad 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 198 ------QGKAAHSSRPDLGANAIHGlfafanAALTATAPLQAKD---DPILGhATHNIDIIHGGNQINSLPESAYLRGNV 268
Cdd:cd08014 172 sleiriQGEGGHGARPHLTVDLVWA------AAQVVTDLPQAISrriDPRSP-VVLTWGSIEGGRAPNVIPDSVELSGTV 244
|
..
gi 872387442 269 RT 270
Cdd:cd08014 245 RT 246
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
20-205 |
2.61e-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: 349928 [Multi-domain] Cd Length: 448 Bit Score: 42.87 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 20 LLQAMVRIPSVAAKEGQVADL---IEAFLAPELST-GLIKRERISYAPGRDNLVLT--IGDPNAQRWLgVDGHMDVVDaG 93
Cdd:cd05679 9 ELARRVAVPTESQEPARKPELrayLDQEMRPRFERlGFTVHIHDNPVAGRAPFLIAerIEDPSLPTLL-IYGHGDVVP-G 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 94 DPNKWQ--FPPFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHE---ELDHGVQLMATVGEEIDNYGARQLAAAgYGD 168
Cdd:cd05679 87 YEGRWRdgRDPWTVTVWGERWYGRGTADNKGQHSINMAALRQVLEArggKLGFNVKFLIEMGEEMGSPGLRAFCFS-HRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 872387442 169 RLTG-LLVAEPGnSNVDAAE-------RGIIDYTLTAQGKA-AHSS 205
Cdd:cd05679 166 ALKAdLFIASDG-PRLAADRptmflgsRGGLNFELRVNLREgGHHS 210
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
195-288 |
6.76e-04 |
|
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: 41.43 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 195 LTAQGKAAHSSRPDLGANAIHGLFAFANAALTATAPLQAKDDPilghATHNIDIIHGGNQINSLPESAYLRGNVRTTmia 274
Cdd:cd03886 176 ITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVVSRELDPLEP----AVVTVGKFHAGTAFNVIPDTAVLEGTIRTF--- 248
|
90
....*....|....
gi 872387442 275 dNDAFIAALKQAAK 288
Cdd:cd03886 249 -DPEVREALEARIK 261
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
198-270 |
7.50e-04 |
|
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349919 [Multi-domain] Cd Length: 371 Bit Score: 41.13 E-value: 7.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872387442 198 QGKAAHSSRPDLGANAIHGLFAFANAALT----ATAPLQAkddpilghATHNIDIIHGGNQINSLPESAYLRGNVRT 270
Cdd:cd05669 180 AGKGAHAAKPENGVDPIVAASQIINALQTivsrNISPLES--------AVVSVTRIHAGNTWNVIPDSAELEGTVRT 248
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
85-179 |
8.85e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 41.05 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 85 GHMDVVDaGDPNKWQFP--PFSAQIEDGKLYGRGATDMKSGLAAAVVAFKQIAHEE---LDHGVQLMATVGEEIDNYGAR 159
Cdd:PRK07079 92 GHGDVVR-GYDEQWREGlsPWTLTEEGDRWYGRGTADNKGQHTINLAALEQVLAARggrLGFNVKLLIEMGEEIGSPGLA 170
|
90 100
....*....|....*....|.
gi 872387442 160 QLAAAgYGDRLTG-LLVAEPG 179
Cdd:PRK07079 171 EVCRQ-HREALAAdVLIASDG 190
|
|
| M20_Acy1L2 |
cd03887 |
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
122-287 |
1.66e-03 |
|
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: 40.25 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 122 SGLAAAVVAFKQIAHEELDHGVQLMATVGEEiDNYGARQLAAAGYGDRLTGLLVAEPGNSNV-DAAERGIIDYTLTAQGK 200
Cdd:cd03887 90 ASVAAALALKAALKALGLPGTVVVLGTPAEE-GGGGKIDLIKAGAFDDVDIALMVHPGPKDVaGPKSLAVSKLRVEFHGK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 201 AAH-SSRPDLGANAIHGL-FAFAN-AALTatapLQAKDDPILghatHNIdIIHGGNQINSLPESAYLRGNVRTTMIAD-- 275
Cdd:cd03887 169 AAHaAAAPWEGINALDAAvLAYNNiSALR----QQLKPTVRV----HGI-ITEGGKAPNIIPDYAEAEFYVRAPTLKEle 239
|
170
....*....|....
gi 872387442 276 --NDAFIAALKQAA 287
Cdd:cd03887 240 elTERVIACFEGAA 253
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
196-364 |
1.72e-03 |
|
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: 39.96 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 196 TAQGKAAHSSRPDLGANAIHGLfAFANAALTATaplqaKDDPILGHATHNIDIIHGGNQINSLPESAYLRGNVRttmiAD 275
Cdd:cd08018 173 TIKGKQAHGARPHLGINAIEAA-SAIVNAVNAI-----HLDPNIPWSVKMTKLQAGGEATNIIPDKAKFALDLR----AQ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872387442 276 NDAFIAALKQAAKT---SVPKGVHLSLSIDSVLSAAAAAPDNALIQKVQQArqriglqrgavayrtgITDAalFFHDGLD 352
Cdd:cd08018 243 SNEAMEELKEKVEHaieAAAALYGASIEITEKGGMPAAEYDEEAVELMEEA----------------ITEV--LGEEKLA 304
|
170
....*....|..
gi 872387442 353 LAIYGPGNDTSH 364
Cdd:cd08018 305 GPCVTPGGEDFH 316
|
|
| |
