|
Name |
Accession |
Description |
Interval |
E-value |
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-346 |
0e+00 |
|
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: 588.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 7 EAVELLRRLIATPSTSRDESRTADLLFAFLEERGAAPERLHNNVFARSADFDPARPTLLLNSHHDTVRPAASYTRDPFTP 86
Cdd:cd05651 1 EAIELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRKGNNVWAENGHFDEGKPTLLLNSHHDTVKPNAGWTKDPFEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 87 TAEGDRLYGLGSNDAGASVVSLARTFLTF-REQSLPFNLLLALSAEEECMGEHGMRALLPQLGTIDMALVGEPTGMQAAV 165
Cdd:cd05651 81 VEKGGKLYGLGSNDAGASVVSLLATFLHLySEGPLNYNLIYAASAEEEISGKNGIESLLPHLPPLDLAIVGEPTEMQPAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 166 GERGLVVLDCEARGKSGHAARNEGINALYIALDDIARLRSFRFDRVSELLGPIGIAVTQIAAGTQHNVVPDSCRFVVDLR 245
Cdd:cd05651 161 AEKGLLVLDCTARGKAGHAARNEGDNAIYKALDDIQWLRDFRFDKVSPLLGPVKMTVTQINAGTQHNVVPDSCTFVVDIR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 246 TTDAYTNEETVEILRGALRSQAAPRSTRIRASALDAAHPLARAAQAAGRRSYVSPTTSDMALMPFPSLKMGPGESSRSHT 325
Cdd:cd05651 241 TTEAYTNEEIFEIIRGNLKSEIKPRSFRLNSSAIPPDHPIVQAAIAAGRTPFGSPTLSDQALMPFPSVKIGPGDSSRSHT 320
|
330 340
....*....|....*....|.
gi 313158256 326 ADEYVLLSEIGEGIGIYEEFI 346
Cdd:cd05651 321 ADEFIELSEIEEGIDIYIELL 341
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
1-351 |
4.54e-90 |
|
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 275.23 E-value: 4.54e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 1 MDAKTTEAVELLRRLIATPSTSRDESRTADLLFAFLEERGAAPERL-----HNNVFARsADFDPARPTLLLNSHHDTV-- 73
Cdd:COG0624 7 IDAHLDEALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLevppgRPNLVAR-RPGDGGGPTLLLYGHLDVVpp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 74 RPAASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQ--SLPFNLLLALSAEEECmGEHGMRALL---PQLG 148
Cdd:COG0624 86 GDLELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAglRLPGNVTLLFTGDEEV-GSPGARALVeelAEGL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 149 TIDMALVGEPTG-MQAAVGERGLVVLDCEARGKSGHAARNE-GINALYIALDDIARLRSFRFD-RVSELLGPIGIAVTQI 225
Cdd:COG0624 165 KADAAIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPElGVNAIEALARALAALRDLEFDgRADPLFGRTTLNVTGI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 226 AAGTQHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALRSQAAPRSTRIR-------ASALDAAHPLARAAQA------- 291
Cdd:COG0624 245 EGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEVEvlgdgrpPFETPPDSPLVAAARAairevtg 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313158256 292 AGRRSYVSPTTSDMAL----MPFPSLKMGPGESSRSHTADEYVLLSEIGEGIGIYEEFIRQLAG 351
Cdd:COG0624 325 KEPVLSGVGGGTDARFfaeaLGIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
10-346 |
3.20e-73 |
|
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: 231.03 E-value: 3.20e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 10 ELLRRLIATPSTSRDESRTADLLFAFLEERGAAPERLH----NNVFARSADFDParPTLLLNSHHDTVRPAASY--TRDP 83
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIvegrGNLVATVGGGDG--PVLLLNGHIDTVPPGDGDkwSFPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 84 FTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSLPFN--LLLALSAEEECmGEHGMRALLPQLGT--IDMALVGEPT 159
Cdd:cd08659 79 FSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGgrVALLATVDEEV-GSDGARALLEAGYAdrLDALIVGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 160 GMQAAVGERGLVVLDCEARGKSGHAARNE-GINALYIALDDIARLRSFRFDR-VSELLGPIGIAVTQIAAGTQHNVVPDS 237
Cdd:cd08659 158 GLDVVYAHKGSLWLRVTVHGKAAHSSMPElGVNAIYALADFLAELRTLFEELpAHPLLGPPTLNVGVINGGTQVNSIPDE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 238 CRFVVDLRTTDAYTNEETVEILRGALRSQAAP-----RSTRIRASALDAAHPLARAAQAAGRRSYVSP------TTSDMA 306
Cdd:cd08659 238 ATLRVDIRLVPGETNEGVIARLEAILEEHEAKltvevSLDGDPPFFTDPDHPLVQALQAAARALGGDPvvrpftGTTDAS 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 313158256 307 -LMP---FPSLKMGPGESSRSHTADEYVLLSEIGEGIGIYEEFI 346
Cdd:cd08659 318 yFAKdlgFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
10-350 |
4.41e-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: 171.24 E-value: 4.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 10 ELLRRLIATPSTSRD-ESRTADLLFAFLEERGAAPERLHN------NVFARsadFDPA-RPTLLLNSHHDTVrPAAS--Y 79
Cdd:cd03894 1 ELLARLVAFDTVSRNsNLALIEYVADYLAALGVKSRRVPVpeggkaNLLAT---LGPGgEGGLLLSGHTDVV-PVDGqkW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 80 TRDPFTPTAEGDRLYGLGSND---AGASVVSLARTFLtfrEQSLPFNLLLALSAEEE--CMG-EHGMRALLPQLGTIDMA 153
Cdd:cd03894 77 SSDPFTLTERDGRLYGRGTCDmkgFLAAVLAAVPRLL---AAKLRKPLHLAFSYDEEvgCLGvRHLIAALAARGGRPDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 154 LVGEPTGMQAAVGERGLVVLDCEARGKSGHAAR-NEGINALYIALDDIARLR----SFRFDRVSELLGPIG--IAVTQIA 226
Cdd:cd03894 154 IVGEPTSLQPVVAHKGIASYRIRVRGRAAHSSLpPLGVNAIEAAARLIGKLReladRLAPGLRDPPFDPPYptLNVGLIH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 227 AGTQHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALRSQAAPRSTRIR---------------ASALDAAHPLARAAQA 291
Cdd:cd03894 234 GGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPEAGIEveplfevpgletdedAPLVRLAAALAGDNKV 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313158256 292 AGrrsyVSPTT--SDMALMPFPSLKMGPGESSRSHTADEYVLLSEIGEGigiyEEFIRQLA 350
Cdd:cd03894 314 RT----VAYGTeaGLFQRAGIPTVVCGPGSIAQAHTPDEFVELEQLDRC----EEFLRRLI 366
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
8-350 |
3.78e-42 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 150.72 E-value: 3.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 8 AVELLRRLIATPSTSRDeSRTA--DLLFAFLEERGAAPERLHN------NVFARSADFDpaRPTLLLNSHHDTVrPAA-- 77
Cdd:PRK07522 6 SLDILERLVAFDTVSRD-SNLAliEWVRDYLAAHGVESELIPDpegdkaNLFATIGPAD--RGGIVLSGHTDVV-PVDgq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 78 SYTRDPFTPTAEGDRLYGLGSND-------AGASVVSLARTFLTfreqsLPfnLLLALSAEEE--CMGEHGMRALLPQLG 148
Cdd:PRK07522 82 AWTSDPFRLTERDGRLYGRGTCDmkgfiaaALAAVPELAAAPLR-----RP--LHLAFSYDEEvgCLGVPSMIARLPERG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 149 -TIDMALVGEPTGMQAAVGERGLVVLDCEARGKSGHAAR-NEGINALYIALDDIARLRsfrfdRVSELLGPIG------- 219
Cdd:PRK07522 155 vKPAGCIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLaPQGVNAIEYAARLIAHLR-----DLADRLAAPGpfdalfd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 220 -----IAVTQIAAGTQHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALRS------QAAPRSTRIRASALDAAHPLARA 288
Cdd:PRK07522 230 ppystLQTGTIQGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAellpemRAVHPEAAIEFEPLSAYPGLDTA 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313158256 289 AQAAGRrSYVSPTTSDMAL--------------MPFPSLKMGPGESSRSHTADEYVLLSEIGEGigiyEEFIRQLA 350
Cdd:PRK07522 310 EDAAAA-RLVRALTGDNDLrkvaygteaglfqrAGIPTVVCGPGSIEQAHKPDEFVELAQLAAC----EAFLRRLL 380
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
1-351 |
5.50e-39 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 142.44 E-value: 5.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 1 MDAKTTEAVELLRRLIATPS---TSRDESRTADLLFAFLEERGAAPE----------RLHNNVFARSADFDPARPTLLLN 67
Cdd:PRK08651 1 VEAMMFDIVEFLKDLIKIPTvnpPGENYEEIAEFLRDTLEELGFSTEiievpneyvkKHDGPRPNLIARRGSGNPHLHFN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 68 SHHDTVRP-AASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSlPFNLLLALSAEEEcMGEHGMRALLPQ 146
Cdd:PRK08651 81 GHYDVVPPgEGWSVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAG-DGNIELAIVPDEE-TGGTGTGYLVEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 147 LG-TIDMALVGEPTGMQ-AAVGERGLVVLDCEARGKSGHAAR-NEGINALYIALDDIARLRSFRFDRVS--ELLGPIGIA 221
Cdd:PRK08651 159 GKvTPDYVIVGEPSGLDnICIGHRGLVWGVVKVYGKQAHASTpWLGINAFEAAAKIAERLKSSLSTIKSkyEYDDERGAK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 222 VT------QIAAGTQHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALRSQAAPRSTRIR--------ASALDAAHPL-- 285
Cdd:PRK08651 239 PTvtlggpTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEfeitpfseAFVTDPDSELvk 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313158256 286 -----ARAAQAAGRRSYVSPTTSDMalMPF-----PSLKMGPGESSRSHTADEYVLLSEIGEGIGIYEEFIRQLAG 351
Cdd:PRK08651 319 alreaIREVLGVEPKKTISLGGTDA--RFFgakgiPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVLKRLAK 392
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
65-348 |
2.66e-37 |
|
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: 136.32 E-value: 2.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 65 LLNSHHDTVrPAASYTRDPFTPTAEGdRLYGLGSNDAGASVVSLARTFLTFREQSL-PFNLLLALSAEEECmGEHGMRAL 143
Cdd:pfam01546 1 LLRGHMDVV-PDEETWGWPFKSTEDG-KLYGRGHDDMKGGLLAALEALRALKEEGLkKGTVKLLFQPDEEG-GMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 144 LPQLGT----IDMAL---VGEPTGMQAAV------GERGLVVLDCEARGKSGHAAR-NEGINALYIALDDIARLRSFRFD 209
Cdd:pfam01546 78 IEDGLLerekVDAVFglhIGEPTLLEGGIaigvvtGHRGSLRFRVTVKGKGGHASTpHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 210 RVSELLGPIG--IAVTQIAAGTqhNVVPDSCRFVVDLRTTDAYTNEETVEILRGALRSQAAPRSTRIR------------ 275
Cdd:pfam01546 158 NVDPLDPAVVtvGNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEveyveggapplv 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 276 --ASALDAAHPLARAAQAAGRRSYVSPT--TSDMALM----PFPSLKMGPGeSSRSHTADEYVLLSEIGEGIGIYEEFIR 347
Cdd:pfam01546 236 ndSPLVAALREAAKELFGLKVELIVSGSmgGTDAAFFllgvPPTVVFFGPG-SGLAHSPNEYVDLDDLEKGAKVLARLLL 314
|
.
gi 313158256 348 Q 348
Cdd:pfam01546 315 K 315
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
10-349 |
4.22e-34 |
|
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: 128.78 E-value: 4.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 10 ELLRRLIATPSTS-RDESRTADLLFAFLEERGAAPERLHN-------NVFARSADfdPARPTLLLNSHHDTVrPA--ASY 79
Cdd:TIGR01892 1 EILTKLVAFDSTSfRPNVDLIDWAQAYLEALGFSVEVQPFpdgaeksNLVAVIGP--SGAGGLALSGHTDVV-PYddAAW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 80 TRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSLPFNLLLALSAEEE--CMGEHGMRALLPqlGTIDMALVGE 157
Cdd:TIGR01892 78 TRDPFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEvgCTGAPKMIEAGA--GRPRHAIIGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 158 PTGMQAAVGERGLVVLDCEARGKSGHAAR-NEGINALYIALDDIARLRSFR-------FDRVSELLGPIgIAVTQIAAGT 229
Cdd:TIGR01892 156 PTRLIPVRAHKGYASAEVTVRGRSGHSSYpDSGVNAIFRAGRFLQRLVHLAdtllredLDEGFTPPYTT-LNIGVIQGGK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 230 QHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALR--SQAAP-------RSTRIRASALDAAHPLARAAQAAG--RRSYV 298
Cdd:TIGR01892 235 AVNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQalVRDEPgfevqieVVSTDPGVNTEPDAELVAFLEELSgnAPEVV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 313158256 299 SPTTS--DMALMPFPSLKMGPGESSRSHTADEYVLLSEIGEGigiyEEFIRQL 349
Cdd:TIGR01892 315 SYGTEapQFQELGAEAVVCGPGDIRQAHQPDEYVEIEDLVRC----RAVLARL 363
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
9-341 |
2.84e-33 |
|
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: 126.75 E-value: 2.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 9 VELLRRLIATPS---TSRDESRTADLLFAFLEERG-------AAPERLHNNVFARSADFDPAR-PTLLLNSHHDTVRPA- 76
Cdd:TIGR01910 1 VELLKDLISIPSvnpPGGNEETIANYIKDLLREFGfstdvieITDDRLKVLGKVVVKEPGNGNeKSLIFNGHYDVVPAGd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 77 -ASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSLP--FNLLLALSAEEECmGEHGMRALLPQLG--TID 151
Cdd:TIGR01910 81 lELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKpnGNIILQSVVDEES-GEAGTLYLLQRGYfkDAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 152 MALVGEPTG-MQAAVGERGLVVLDCEARGKSGHAAR-NEGINA------LYIALDDIARLRSFRFDrVSELLGPIGIAVT 223
Cdd:TIGR01910 160 GVLIPEPSGgDNIVIGHKGSIWFKLRVKGKQAHASFpQFGVNAimklakLITELNELEEHIYARNS-YGFIPGPITFNPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 224 QIAAGTQHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALRsqAAPRSTRIRAS-----------ALDAAHPLARAAQA- 291
Cdd:TIGR01910 239 VIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVK--ALSKSDGWLYEnepvvkwsgpnETPPDSRLVKALEAi 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 313158256 292 ------AGRRSYVSPTTSDMALM---PFPSLKMGPGESSRSHTADEYVLLSEIGEGIGI 341
Cdd:TIGR01910 317 ikkvrgIEPEVLVSTGGTDARFLrkaGIPSIVYGPGDLETAHQVNEYISIKNLVESTKV 375
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
9-346 |
5.14e-31 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 120.18 E-value: 5.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 9 VELLRRLIATPSTS--RDESRT-ADLLFAFLEERGAaPERLHNnvFARSADFDP-------ARPTLLLNSHHDTV--RPA 76
Cdd:cd08011 1 VKLLQELVQIPSPNppGDNTSAiAAYIKLLLEDLGY-PVELHE--PPEEIYGVVsnivggrKGKRLLFNGHYDVVpaGDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 77 ASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSLPFNLLLALSA--EEECMGEHGMRALLPQ-LGTIDMA 153
Cdd:cd08011 78 EGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFvpDEETGGRAGTKYLLEKvRIKPNDV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 154 LVGEPTGMQA-AVGERGLVVLDCEARGKSGHAAR-NEGINALYIALDDIarlrsfrfDRVSELLGPIGiaVTQIAAGTQH 231
Cdd:cd08011 158 LIGEPSGSDNiRIGEKGLVWVIIEITGKPAHGSLpHRGESAVKAAMKLI--------ERLYELEKTVN--PGVIKGGVKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 232 NVVPDSCRFVVDLRTTDAYTNEETVEILRGALRS--QAAPRS-TRIRASALDAAHPLARAAQAAGRR-------SYVSPT 301
Cdd:cd08011 228 NLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSieEVSFEIkSFYSPTVSNPDSEIVKKTEEAITEvlgirpkEVISVG 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 313158256 302 TSDMALMP---FPSLKMGPGESSRSHTADEYVLLSEIGEGIGIYEEFI 346
Cdd:cd08011 308 ASDARFYRnagIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
6-349 |
5.72e-31 |
|
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: 119.76 E-value: 5.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 6 TEAVELLRRLIATPSTSRDESRTADLLFAFLEERGAAPERLH-NNVFARSadfDPARPTLLLNSHHDTVrPAasytrdPF 84
Cdd:cd05653 1 QDAVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEaGNAVGGA---GSGPPDVLLLGHIDTV-PG------EI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 85 TPTAEGDRLYGLGSNDAGASVVSLARTFLTFREqSLPFNLLLALSAEEECMGEhGMRALLPQLGTIDMALVGEPTGMQA- 163
Cdd:cd05653 71 PVRVEGGVLYGRGAVDAKGPLAAMILAASALNE-ELGARVVVAGLVDEEGSSK-GARELVRRGPRPDYIIIGEPSGWDGi 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 164 AVGERGLVVLDCEARGKSGHAARNEGiNALYIALDDIARLRsfrfDRVSELLGPIG----IAVTQIAAGTQHNVVPDSCR 239
Cdd:cd05653 149 TLGYRGSLLVKIRCEGRSGHSSSPER-NAAEDLIKKWLEVK----KWAEGYNVGGRdfdsVVPTLIKGGESSNGLPQRAE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 240 FVVDLRTTDAYTNEEtveilrgaLRSQAAPRSTRIRASALDAAHPLARAAQAAGRRSYV--------SPT------TSDM 305
Cdd:cd05653 224 ATIDLRLPPRLSPEE--------AIALATALLPTCELEFIDDTEPVKVSKNNPLARAFRrairkqggKPRlkrktgTSDM 295
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 313158256 306 ALM----PFPSLKMGPGESSRSHTADEYVLLSEIGEGIGIYEEFIRQL 349
Cdd:cd05653 296 NVLaplwTVPIVAYGPGDSTLDHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
8-346 |
1.01e-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: 119.47 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 8 AVELLRRLIATPSTSRDESRTADLLFAFLeeRGAAP---ERLHNNVFARSaDFDPARpTLLLNSHHDTVRPAASytrdpF 84
Cdd:cd05647 1 PIELTAALVDIPSVSGNEKPIADEIEAAL--RTLPHlevIRDGNTVVART-ERGLAS-RVILAGHLDTVPVAGN-----L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 85 TPTAEGDR-LYGLGSNDAGASVVSLARTFLTFREQSLPFNLLLALSAEEECMGE-HGMRAL---LPQLGTIDMALVGEPT 159
Cdd:cd05647 72 PSRVEEDGvLYGCGATDMKAGDAVQLKLAATLAAATLKHDLTLIFYDCEEVAAElNGLGRLaeeHPEWLAADFAVLGEPT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 160 GMQAAVGERGLVVLDCEARGKSGHAARN-EGINALYIALDDIARLRSFRFDRVS--ELLGPIGIAVTQIAAGTQHNVVPD 236
Cdd:cd05647 152 DGTIEGGCQGTLRFKVTTHGVRAHSARSwLGENAIHKLAPILARLAAYEPRTVNidGLTYREGLNAVFISGGVAGNVIPD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 237 SCRFVVDLRTTDAYTNEETVEILRGAL-RSQAAPRSTRIRASAL-----DAAHPLARAAQAAGRRSYVSPTTSDMALMPF 310
Cdd:cd05647 232 EARVNLNYRFAPDKSLAEAIAHVREVFeGLGYEIEVTDLSPGALpgldhPVARDLIEAVGGKVRAKYGWTDVARFSALGI 311
|
330 340 350
....*....|....*....|....*....|....*.
gi 313158256 311 PSLKMGPGESSRSHTADEYVLLSEIGEGIGIYEEFI 346
Cdd:cd05647 312 PAVNFGPGDPLLAHKRDEQVPVEQITACAAILRRWL 347
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
8-262 |
4.54e-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: 114.68 E-value: 4.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 8 AVELLRRLIATPSTSRDESRTADLLFAFLEERGAAPERL------HNNVFARSADFDpaRPTLLLNSHHDTVRPAASYTR 81
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKQpvenkdRFNVYAYPGSSR--QPRVLLTSHIDTVPPFIPYSI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 82 DpftptAEGDRLYGLGSNDAGASVVS--LARTFLTFREQSLPFNL-LLALSAEEEcmGEHGMRALlPQLG--TIDMALVG 156
Cdd:cd05652 79 S-----DGGDTIYGRGSVDAKGSVAAqiIAVEELLAEGEVPEGDLgLLFVVGEET--GGDGMKAF-NDLGlnTWDAVIFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 157 EPTGMQAAVGERGLVVLDCEARGKSGHAAR-NEGINALYI---ALDDI--ARLRSfrfdrvSELLGPIGIAVTQIAAGTQ 230
Cdd:cd05652 151 EPTELKLASGHKGMLGFKLTAKGKAGHSGYpWLGISAIEIlveALVKLidADLPS------SELLGPTTLNIGRISGGVA 224
|
250 260 270
....*....|....*....|....*....|..
gi 313158256 231 HNVVPDSCRFVVDLRTtdAYTNEETVEILRGA 262
Cdd:cd05652 225 ANVVPAAAEASVAIRL--AAGPPEVKDIVKEA 254
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
6-348 |
1.07e-24 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 103.04 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 6 TEAVELLRRLIATPSTSRDESRTADLLFAFLEErgaaperlhNNVFARSADFDPAR-----------PTLLLNSHHDTVR 74
Cdd:PRK08588 2 EEKIQILADIVKINSVNDNEIEVANYLQDLFAK---------HGIESKIVKVNDGRanlvaeigsgsPVLALSGHMDVVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 75 P--AASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSLPFN---LLLALSAEEecMGEHGMRALLPQ--L 147
Cdd:PRK08588 73 AgdVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNgtiRLLATAGEE--VGELGAKQLTEKgyA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 148 GTIDMALVGEPTGMQAAVGERGlvVLDCE--ARGKSGHAARNE-GINALYIALDDIARLRSF--RFDRVSELLGPIGIAV 222
Cdd:PRK08588 151 DDLDALIIGEPSGHGIVYAHKG--SMDYKvtSTGKAAHSSMPElGVNAIDPLLEFYNEQKEYfdSIKKHNPYLGGLTHVV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 223 TQIAAGTQHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALR--------------------------SQAAPRSTRIRA 276
Cdd:PRK08588 229 TIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINevnqngaaqlsldiysnhrpvasdkdSKLVQLAKDVAK 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 313158256 277 SALDAAHPLARaaqaagrrsyVSPTT--SDMALMP--FPSLKMGPGESSRSHTADEYVLLSEIGEGIGIYEEFIRQ 348
Cdd:PRK08588 309 SYVGQDIPLSA----------IPGATdaSSFLKKKpdFPVIIFGPGNNLTAHQVDEYVEKDMYLKFIDIYKEIIIQ 374
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
9-279 |
1.11e-24 |
|
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: 102.97 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 9 VELLRRLIATPSTSRDESRTADLLFAFLEERGAAPERLHN----NVFARsadFDPARPTLLLNSHHDTVRP--AASYTRD 82
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFggvkNLWAR---RGTGGPHLCFAGHTDVVPPgdLEGWSSD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 83 PFTPTAEGDRLYGLGSNDA----GASVVSLARtfltFREQSLPFN--LLLALSAEEECMGEHGMRALLPQLG----TIDM 152
Cdd:cd03891 78 PFSPTIKDGMLYGRGAADMkggiAAFVAAAER----FVAKHPNHKgsISFLITSDEEGPAIDGTKKVLEWLKargeKIDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 153 ALVGEPTGMQAA-----VGERG-----LVVldceaRGKSGHAARNE-GINALYIALDDIARLRSFRFDRVSELLGPIGIA 221
Cdd:cd03891 154 CIVGEPTSEKKLgdtikIGRRGslngkLTI-----KGKQGHVAYPHlADNPIHLLAPILAELTATVLDEGNEFFPPSSLQ 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 313158256 222 VTQIAAGTQ-HNVVPDSCRFVVDLRTTDAYTNEETVEILRGALRSQAAPRSTRIRASAL 279
Cdd:cd03891 229 ITNIDVGNGaTNVIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGE 287
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
2-217 |
3.86e-24 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 101.85 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 2 DAKTTEAVELLRRLIATPSTSRD-----ESRTADLLFAFLEERG------------AAPERLHNNVFARsADFDPARPTL 64
Cdd:PRK13983 1 DELRDEMIELLSELIAIPAVNPDfggegEKEKAEYLESLLKEYGfdeverydapdpRVIEGVRPNIVAK-IPGGDGKRTL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 65 LLNSHHDTVRP--AASYTRDPFTPTAEGDRLYGLGSNDAGASVVS---LARTFltFREQSLP-FNLLLALSAEEECMGEH 138
Cdd:PRK13983 80 WIISHMDVVPPgdLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSsllALKAL--MDLGIRPkYNLGLAFVSDEETGSKY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 139 GMRALLPQLGTI----DMALV---GEPTGMQAAVGERGLVVLDCEARGKSGHAAR-NEGINALYIALDDIARLRSF---R 207
Cdd:PRK13983 158 GIQYLLKKHPELfkkdDLILVpdaGNPDGSFIEIAEKSILWLKFTVKGKQCHASTpENGINAHRAAADFALELDEAlheK 237
|
250
....*....|
gi 313158256 208 FDRVSELLGP 217
Cdd:PRK13983 238 FNAKDPLFDP 247
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-284 |
8.34e-24 |
|
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: 101.00 E-value: 8.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 7 EAVELLRRLIATPSTS-----RDESRTADLLFAFLEERG--------AAPER--LHNNVFARsADFDPARpTLLLNSHHD 71
Cdd:cd05650 2 EIIELERDLIRIPAVNpesggEGEKEKADYLEKKLREYGfytlerydAPDERgiIRPNIVAK-IPGGNDK-TLWIISHLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 72 TVRP--AASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSL--PFNLLLALSAEEECMGEHGMRALLPQL 147
Cdd:cd05650 80 TVPPgdLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGItpKYNFGLLFVADEEDGSEYGIQYLLNKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 148 GTI---DMALV---GEPTGMQAAVGERGLVVLDCEARGKSGHAAR-NEGINALYIALD---DIARLRSFRFDRVSEL-LG 216
Cdd:cd05650 160 DLFkkdDLIIVpdfGTEDGEFIEIAEKSILWIKVNVKGKQCHASTpENGINAFVAASNfalELDELLHEKFDEKDDLfNP 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 217 PIGIAVTQIAAGTQHNV--VPDSCRFVVDLRTTDAYTNEETVEILRGALRSQAAPRSTRIRASALDAAHP 284
Cdd:cd05650 240 PYSTFEPTKKEANVPNVntIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDFENSYGAGITYEIVQKEQA 309
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
5-245 |
5.11e-23 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 97.91 E-value: 5.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 5 TTEAVELLRRLIATPSTSRDESRTADLLFAFLEERGAAP-----ERLHNNVFARSADfdparptLLLNSHHDTVRPAASy 79
Cdd:PRK08652 1 TERAKELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVhiesdGEVINIVVNSKAE-------LFVEVHYDTVPVRAE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 80 trdpftPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSLPFNLLLALSAEEECMG---EHGMRALLPQlgtidMALVG 156
Cdd:PRK08652 73 ------FFVDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSDEEEGGrgsALFAERYRPK-----MAIVL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 157 EPTGMQAAVGERGLVVLDCEARGKSGHAARNE-GINALYIALDDIARLRSFRFDRVSELLGPIGIavTQIAAGTQHNVVP 235
Cdd:PRK08652 142 EPTDLKVAIAHYGNLEAYVEVKGKPSHGACPEsGVNAIEKAFEMLEKLKELLKALGKYFDPHIGI--QEIIGGSPEYSIP 219
|
250
....*....|
gi 313158256 236 DSCRFVVDLR 245
Cdd:PRK08652 220 ALCRLRLDAR 229
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-348 |
1.07e-22 |
|
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: 97.55 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 7 EAVELLRRLI----ATPSTSRD----ESRTADLLFAFLEERGAAPERLHNNvfarsadfdPARP-------------TLL 65
Cdd:cd08013 2 DPVSLTQTLVrinsSNPSLSATggagEAEIATYVAAWLAHRGIEAHRIEGT---------PGRPsvvgvvrgtgggkSLM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 66 LNSHHDTVrPAASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSLPFNLLLALSAEEECMGEhGMRALLP 145
Cdd:cd08013 73 LNGHIDTV-TLDGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGLRGDVILAAVADEEDASL-GTQEVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 146 QLGTIDMALVGEPTGMQAAVGERGLVVLDCEARGKSGHAARNE-GINA------LYIALDDIArlRSFRFDRVSELLGPI 218
Cdd:cd08013 151 AGWRADAAIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRPDlGVDAilkagyFLVALEEYQ--QELPERPVDPLLGRA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 219 GIAVTQIAAGTQHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALRSQAA---------PRSTRIRAS-ALDAAHPLARA 288
Cdd:cd08013 229 SVHASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTAILGELAQtvpnfsyrePRITLSRPPfEVPKEHPFVQL 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 289 AQAAGRRSYVSPTT-------SDMALMP---FPSLKMGPgESSRSHTADEYVLLSEIGEGIGIYEEFIRQ 348
Cdd:cd08013 309 VAAHAAKVLGEAPQirsetfwTDAALLAeagIPSVVFGP-SGAGLHAKEEWVDVESIRQLREVLSAVVRE 377
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
9-275 |
1.16e-22 |
|
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: 97.28 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 9 VELLRRLIATPSTSRDES---RTADLLFAFLEERGAAPERLHN-----NVFARSADfdPARPTLLLNSHHDTVRPAASYT 80
Cdd:cd03885 2 LDLLERLVNIESGTYDKEgvdRVAELLAEELEALGFTVERRPLgefgdHLIATFKG--TGGKRVLLIGHMDTVFPEGTLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 81 RDPFTptAEGDRLYGLGSNDAGASVVSLARTFLTFREQSL--PFNLLLALSAEEEcMGEHGMRALLPQLGT-IDMALVGE 157
Cdd:cd03885 80 FRPFT--VDGDRAYGPGVADMKGGLVVILHALKALKAAGGrdYLPITVLLNSDEE-IGSPGSRELIEEEAKgADYVLVFE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 158 PTGM--QAAVGERGLVVLDCEARGKSGHAARN--EGINALYIALDDIARLRSfrfdrvseLLGP---IGIAVTQIAAGTQ 230
Cdd:cd03885 157 PARAdgNLVTARKGIGRFRLTVKGRAAHAGNApeKGRSAIYELAHQVLALHA--------LTDPekgTTVNVGVISGGTR 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 313158256 231 HNVVPDSCRFVVDLRttdAYTNEETVEILRG--ALRSQAAPRSTRIR 275
Cdd:cd03885 229 VNVVPDHAEAQVDVR---FATAEEADRVEEAlrAIVATTLVPGTSVE 272
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
7-260 |
1.02e-21 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 95.01 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 7 EAVELLRRLIATPSTSRDESRTADLLFAFLEERGaaperlhnnvFaRSADFDP----------ARPTLLLNSHHDTVrPA 76
Cdd:PRK13004 16 DMTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVG----------F-DKVEIDPmgnvlgyighGKKLIAFDAHIDTV-GI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 77 AS---YTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSLPFN--LLLALSAEEECMGEHGMRALLPQLGtI- 150
Cdd:PRK13004 84 GDiknWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEytLYVTGTVQEEDCDGLCWRYIIEEDK-Ik 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 151 -DMALVGEPTGMQAAVGERGLVVLDCEARGKSGHAARNE-GINALYIALDDIARLRSFRFDRVS-ELLGPIGIAVTQIAA 227
Cdd:PRK13004 163 pDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPErGDNAIYKMAPILNELEELNPNLKEdPFLGKGTLTVSDIFS 242
|
250 260 270
....*....|....*....|....*....|....
gi 313158256 228 GT-QHNVVPDSCRFVVDLRTTDAYTNEETVEILR 260
Cdd:PRK13004 243 TSpSRCAVPDSCAISIDRRLTVGETWESVLAEIR 276
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
1-349 |
3.59e-21 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 92.71 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 1 MDAKTTEAVELLRRLIATPSTSRDESRTADLLFAFLEERG--AAPERLHNNVfarsADFDPARPTLLLNSHHDTVrPAAS 78
Cdd:PRK04443 1 MTISALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGreAWVDEAGNAR----GPAGDGPPLVLLLGHIDTV-PGDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 79 YTRdpftptAEGDRLYGLGSNDAGASVVSLArtFLTFR-EQSLPFNLLLALSAEEECMGEHGMRALLPQLgTIDMALVGE 157
Cdd:PRK04443 76 PVR------VEDGVLWGRGSVDAKGPLAAFA--AAAARlEALVRARVSFVGAVEEEAPSSGGARLVADRE-RPDAVIIGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 158 PTGMQAAV-GERGLVVLDCEARGKSGHAARnEGINALYIALDDIARLRSF---------RFDRVSellgpigiaVTQIAA 227
Cdd:PRK04443 147 PSGWDGITlGYKGRLLVTYVATSESFHSAG-PEPNAAEDAIEWWLAVEAWfeandgrerVFDQVT---------PKLVDF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 228 GTQHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALRSQAAPRSTRIRASALDAAHPLARAAQAAGRRSYVSPT------ 301
Cdd:PRK04443 217 DSSSDGLTVEAEMTVGLRLPPGLSPEEAREILDALLPTGTVTFTGAVPAYMVSKRTPLARAFRVAIREAGGTPRlkrktg 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 313158256 302 TSDMALM----PFPSLKMGPGESSRSHTADEYVLLSEIGEGIGIYEEFIRQL 349
Cdd:PRK04443 297 TSDMNVVapawGCPMVAYGPGDSDLDHTPDEHLPLAEYLRAIAVLTDVLERL 348
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
9-263 |
3.97e-21 |
|
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: 93.58 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 9 VELLRRLIATPSTSR-----DESRTADLLFAFLEERG---------AAPERlhNNVFARSADFDPARPTLLLNSHHDTVr 74
Cdd:cd05675 1 VDLLQELIRIDTTNSgdgtgSETRAAEVLAARLAEAGiqteifvveSHPGR--ANLVARIGGTDPSAGPLLLLGHIDVV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 75 PA--ASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQS--LPFNLLLALSAEEECMGEHGMRALLP----- 145
Cdd:cd05675 78 PAdaSDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGfkPKRDLVFAFVADEEAGGENGAKWLVDnhpel 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 146 ---------QLGTIDMALVGEPTGMQAAVGERGLVVLDCEARGKSGHAARNEGINALYIALDDIARLRSFRF-------- 208
Cdd:cd05675 158 fdgatfalnEGGGGSLPVGKGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRPTDDNAITRLAEALRRLGAHNFpvrltdet 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 209 -------------------------DRVSELLGPIG----------IAVTQIAAGTQHNVVPDSCRFVVDLRTTDAYTNE 253
Cdd:cd05675 238 ayfaqmaelaggeggalmltavpvlDPALAKLGPSApllnamlrntASPTMLDAGYATNVLPGRATAEVDCRILPGQSEE 317
|
330
....*....|
gi 313158256 254 ETVEILRGAL 263
Cdd:cd05675 318 EVLDTLDKLL 327
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
9-260 |
4.45e-20 |
|
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: 90.17 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 9 VELLRRLIATPSTSRDESRTADLLFAFLEERG---AAPERLHNNV-FARSADfdparPTLLLNSHHDTV--RPAASYTRD 82
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGfdeVEIDPMGNVIgYIGGGK-----KKILFDGHIDTVgiGNIDNWKFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 83 PFTPTAEGDRLYGLGSND---AGASVVSLARTFLTFREQSLPFNLLLALSAEEECMGEHGMRALLPQLGT-IDMALVGEP 158
Cdd:cd05649 76 PYEGYETDGKIYGRGTSDqkgGLASMVYAAKIMKDLGLRDFAYTILVAGTVQEEDCDGVCWQYISKADKIkPDFVVSGEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 159 TGMQAAVGERGLVVLDCEARGKSGHAARNE-GINALYIALDDIARLRSFRFDRV-SELLGPIGIAVTQIAAGT-QHNVVP 235
Cdd:cd05649 156 TDGNIYRGQRGRMEIRVDTKGVSCHGSAPErGDNAVYKMADIIQDIRQLNPNFPeAPFLGRGTLTVTDIFSTSpSRCAVP 235
|
250 260
....*....|....*....|....*
gi 313158256 236 DSCRFVVDLRTTDAYTNEETVEILR 260
Cdd:cd05649 236 DSCRISIDRRLTVGETWEGCLEEIR 260
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
5-260 |
1.85e-19 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 88.22 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 5 TTEAVELLRRLIATPSTSRDESRTADLLFAFLEERGAAPERLH----NNVFARsadFDPARPTLLLNSHHDTVRP--AAS 78
Cdd:PRK13009 1 MSDVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDfgdvKNLWAR---RGTEGPHLCFAGHTDVVPPgdLEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 79 YTRDPFTPTAEGDRLYGLGSND-----AgASVVSLARtfltFREQSLPFNLLLAL--SAEEECMGEHGMRALLPQL---G 148
Cdd:PRK13009 78 WTSPPFEPTIRDGMLYGRGAADmkgslA-AFVVAAER----FVAAHPDHKGSIAFliTSDEEGPAINGTVKVLEWLkarG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 149 -TIDMALVGEPTGMQAA-----VGERG-----LVVldceaRGKSGHAARNE-GINALYIALDDIARLRSFRFDRVSELLG 216
Cdd:PRK13009 153 eKIDYCIVGEPTSTERLgdvikNGRRGsltgkLTV-----KGVQGHVAYPHlADNPIHLAAPALAELAATEWDEGNEFFP 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 313158256 217 PIGIAVTQIAAGTQ-HNVVPDSCRFVVDLRttdaYTNEETVEILR 260
Cdd:PRK13009 228 PTSLQITNIDAGTGaTNVIPGELEAQFNFR----FSTEHTAESLK 268
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
10-245 |
5.09e-19 |
|
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: 87.36 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 10 ELLRRLIATPSTSRDESRTADLLFAFLEERGAA-------PERLHNNVFARSADFD------------PARPT---LLLN 67
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTvdrweidVEKLKHHPGFSPVAVDyagapnvvgthrPRGETgrsLILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 68 SHHDTVR--PAASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQ--SLPFNLLLALSAEEECmGEHGMRAL 143
Cdd:cd03895 81 GHIDVVPegPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAglQPAADVHFQSVVEEEC-TGNGALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 144 LPQLGTIDMALVGEPTGMQAAVGERGLVVLDCEARGKSGHAA-RNEGINALYIALDDIARLRSFRFDRVSELL------- 215
Cdd:cd03895 160 LMRGYRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAeASEGVNAIEKAMHLIQALQELEREWNARKKshphfsd 239
|
250 260 270
....*....|....*....|....*....|..
gi 313158256 216 --GPIGIAVTQIAAGTQHNVVPDSCrfVVDLR 245
Cdd:cd03895 240 hpHPINFNIGKIEGGDWPSSVPAWC--VLDCR 269
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
10-348 |
1.27e-18 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 86.03 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 10 ELLRRLIATPSTSR-----DESRTA--DLLFAFLEERGAA----PERLHNNVFARSADFDPARPTLLLNSHHDTVrP--A 76
Cdd:PRK05111 9 EMYRALIATPSISAtdpalDQSNRAviDLLAGWFEDLGFNveiqPVPGTRGKFNLLASLGSGEGGLLLAGHTDTV-PfdE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 77 ASYTRDPFTPTAEGDRLYGLGSND-AG--ASVVSLARTFLTfREQSLPFnLLLALSAEEECMgeHGMRALLpQLGTI--D 151
Cdd:PRK05111 88 GRWTRDPFTLTEHDGKLYGLGTADmKGffAFILEALRDIDL-TKLKKPL-YILATADEETSM--AGARAFA-EATAIrpD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 152 MALVGEPTGMQAAVGERGLVVLDCEARGKSGHA---ARneGINALYIALDDIARLRSFRfdrvSEL-------------- 214
Cdd:PRK05111 163 CAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSsdpAL--GVNAIELMHDVIGELLQLR----DELqeryhnpaftvpyp 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 215 ---LGPI--GIAVTQIAAgtqhnvvpdSCRFVVDLRTTDAYTNEETVEILRGALRSQAAPRSTRIRASALDAAHPlaraa 289
Cdd:PRK05111 237 tlnLGHIhgGDAPNRICG---------CCELHFDIRPLPGMTLEDLRGLLREALAPVSERWPGRITVAPLHPPIP----- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 290 qaagrrSYVSPTTSDMAL------------------MPF------PSLKMGPGESSRSHTADEYVLLSEIGEGIGIYEEF 345
Cdd:PRK05111 303 ------GYECPADHQLVRvvekllghkaevvnycteAPFiqqlgcPTLVLGPGSIEQAHQPDEYLELSFIKPTRELLRQL 376
|
...
gi 313158256 346 IRQ 348
Cdd:PRK05111 377 IHH 379
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
9-342 |
2.09e-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: 82.14 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 9 VELLRRLIATPSTSRDESRTADLLFAFLEERG-AAPERL-HNNVFARSADfDPARPTLLLNSHHDTVRPAasytRDPFTP 86
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGlGDVERDgRGNVVGRLRG-TGGGPALLFSAHLDTVFPG----DTPATV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 87 TAEGDRLYGLGSNDAGASVVSLARTFLTFREQSLPF--NLLLALSAEEECMGE-HGMRALLPQLGTI-DMALVGEPTGMQ 162
Cdd:cd03896 76 RHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALkgDVVFAANVGEEGLGDlRGARYLLSAHGARlDYFVVAEGTDGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 163 AAVGERGLVVLDCEARGKSGHAARNEGINAlyiALDDIARLRSFRFDRVSELLGPIGIAVTQIAAGTQHNVVPDSCRFVV 242
Cdd:cd03896 156 PHTGAVGSKRFRITTVGPGGHSYGAFGSPS---AIVAMAKLVEALYEWAAPYVPKTTFAAIRGGGGTSVNRIANLCSMYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 243 DLRTTDAyTNEETVEILRGALRSQAAPRSTRI----------RASALDAAHPLARAAQAAGRRSYVSP------TTSDMA 306
Cdd:cd03896 233 DIRSNPD-AELADVQREVEAVVSKLAAKHLRVkarvkpvgdrPGGEAQGTEPLVNAAVAAHREVGGDPrpgsssTDANPA 311
|
330 340 350
....*....|....*....|....*....|....*..
gi 313158256 307 L-MPFPSLKMGPGESSRSHTADEYVLLSEIGEGIGIY 342
Cdd:cd03896 312 NsLGIPAVTYGLGRGGNAHRGDEYVLKDDMLKGAKAY 348
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
62-335 |
7.26e-16 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 77.93 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 62 PTLLLNSHHDTVRPAASYTRDPFTPTAEGDRLYGLGSND-AGASVVSLARTFLTFREQSLPFnlllalSAEEECMGEHGM 140
Cdd:PRK08737 64 PKYLFNVHLDTVPDSPHWSADPHVMRRTDDRVIGLGVCDiKGAAAALLAAANAGDGDAAFLF------SSDEEANDPRCV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 141 RALLPQLGTIDMALVGEPTGMQAAVGERGLVVLDCEARGKSGHAA--RNEGINALYIA-------LDDIARLRSFRFDRV 211
Cdd:PRK08737 138 AAFLARGIPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHASgkQDPSASALHQAmrwggqaLDHVESLAHARFGGL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 212 SELLGPIGiavtQIAAGTQHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALRSQAAPRSTRIRASALDAAHPLARAAQA 291
Cdd:PRK08737 218 TGLRFNIG----RVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFAGFAEPAAATFEETFRGPSLPSGDIARAEERR 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 313158256 292 AGRRSYV--------SPTT--SDMALMP---FPSLKMGPGESSRSHTADEYVLLSEI 335
Cdd:PRK08737 294 LAARDVAdaldlpigNAVDfwTEASLFSaagYTALVYGPGDIAQAHTADEFVTLDQL 350
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
165-269 |
1.48e-15 |
|
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: 71.61 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 165 VGERGLVVLDCEARGKSGHA-ARNEGINALYIALDDIARLRSFRFDrVSELLGPIGIAVTQIAAGTQHNVVPDSCRFVVD 243
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSgAPGKGVNAIKLLARLLAELPAEYGD-IGFDFPRTTLNITGIEGGTATNVIPAEAEAKFD 79
|
90 100
....*....|....*....|....*.
gi 313158256 244 LRTTDAYTNEETVEILRGALRSQAAP 269
Cdd:pfam07687 80 IRLLPGEDLEELLEEIEAILEKELPE 105
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
8-349 |
3.19e-15 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 75.59 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 8 AVELLRrlIATPSTSrdESRTADLLfafleERGAAPERLHNNVFARSADFDPARPTLLLNSHHDTVrPAAsytrdpFTPT 87
Cdd:PRK00466 16 LLDLLS--IYTPSGN--ETNATKFF-----EKISNELNLKLEILPDSNSFILGEGDILLASHVDTV-PGY------IEPK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 88 AEGDRLYGLGSNDAGASVVS--LARTFLTFREQSLPFnllLALSAEEEcmGEHGMRALLPQLGTIDMALVGEPT-GMQAA 164
Cdd:PRK00466 80 IEGEVIYGRGAVDAKGPLISmiIAAWLLNEKGIKVMV---SGLADEES--TSIGAKELVSKGFNFKHIIVGEPSnGTDIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 165 VGERGLVVLDCEARGKSGHA--ARNEGINALYIALDDIARLRSfRFDRVSellgpigIAVTQIAAGTQHNVVPDSCRFVV 242
Cdd:PRK00466 155 VEYRGSIQLDIMCEGTPEHSssAKSNLIVDISKKIIEVYKQPE-NYDKPS-------IVPTIIRAGESYNVTPAKLYLHF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 243 DLRTTdaytneetVEILRGALRSQAAPRSTRIRASALDAAHPLARAAQAAGRRSY--------VSPT------TSDMALM 308
Cdd:PRK00466 227 DVRYA--------INNKRDDLISEIKDKFQECGLKIVDETPPVKVSINNPVVKALmrallkqnIKPRlvrkagTSDMNIL 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 313158256 309 PFPS---LKMGPGESSRSHTADEYVLLSEIGEGIGIYEEFIRQL 349
Cdd:PRK00466 299 QKITtsiATYGPGNSMLEHTNQEKITLDEIYIAVKTYMLAIEEL 342
|
|
| PRK06915 |
PRK06915 |
peptidase; |
1-335 |
6.77e-15 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 75.11 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 1 MDAKTTEAVELLRRLIATPSTSRDESRTADLLFAFLEERG--------AAPERLHNNVFARS-ADFDPArP--------- 62
Cdd:PRK06915 12 IESHEEEAVKLLKRLIQEKSVSGDESGAQAIVIEKLRELGldldiwepSFKKLKDHPYFVSPrTSFSDS-Pnivatlkgs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 63 ----TLLLNSHHDTVrPA---ASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQ--SLPFNLLLALSAEEE 133
Cdd:PRK06915 91 gggkSMILNGHIDVV-PEgdvNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESgiELKGDVIFQSVIEEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 134 CMGEHGMRALLPQLgTIDMALVGEPTGMQAAVGERGLVVLDCEARGKSGHAA-RNEGINAL---YIALDDIARLRSFRFD 209
Cdd:PRK06915 170 SGGAGTLAAILRGY-KADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGtRYEGVSAIeksMFVIDHLRKLEEKRND 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 210 RVSELLG-----PIGIAVTQIAAGTQHNVVPDSC----RFVV------------------DLRTTDAYTNEETVEI-LRG 261
Cdd:PRK06915 249 RITDPLYkgipiPIPINIGKIEGGSWPSSVPDSVilegRCGIapnetieaakeefenwiaELNDVDEWFVEHPVEVeWFG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 262 AlrsqaaprstRIRASALDAAHPLaraaQAAGRRSYV-----------SPTTSDMALMP----FPSLKMGPGESSRSHTA 326
Cdd:PRK06915 329 A----------RWVPGELEENHPL----MTTLEHNFVeiegnkpiieaSPWGTDGGLLTqiagVPTIVFGPGETKVAHYP 394
|
....*....
gi 313158256 327 DEYVLLSEI 335
Cdd:PRK06915 395 NEYIEVDKM 403
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
2-245 |
1.79e-14 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 73.88 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 2 DAKTTEAVELLRRLIATPSTSRDESRTADLLFAFLEERGAAPERLHNNVFA---------RSADFD----------PARP 62
Cdd:PRK06837 16 DAGFDAQVAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDRWSIDPDDlkshpgagpVEIDYSgapnvvgtyrPAGK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 63 T---LLLNSHHDTV--RPAASYTRDPFTPTAEGDRLYGLGSND--AG-------------ASVVSLARTFLtfreQSLpf 122
Cdd:PRK06837 96 TgrsLILQGHIDVVpeGPLDLWSRPPFDPVIVDGWMYGRGAADmkAGlaamlfaldalraAGLAPAARVHF----QSV-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 123 nlllalsAEEECMGEHGMRALlpQLG-TIDMALVGEPTGMQAAVGERGLVVLDCEARGKSGHAARNE-GINALYIALDDI 200
Cdd:PRK06837 170 -------IEEESTGNGALSTL--QRGyRADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGtGANAIDAAYHLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 313158256 201 ARLRSFRF--------DRV-SELLGPIGIAVTQIAAGTQHNVVPDSCRFvvDLR 245
Cdd:PRK06837 241 QALRELEAewnarkasDPHfEDVPHPINFNVGIIKGGDWASSVPAWCDL--DCR 292
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
8-208 |
9.45e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 71.96 E-value: 9.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 8 AVELLRRLIATPST--SRDESRTADLLFAFLEERGAAPERLH--------NNVFARSADFDPARPTLLLnSHHDTVR-PA 76
Cdd:PRK09133 39 ARDLYKELIEINTTasTGSTTPAAEAMAARLKAAGFADADIEvtgpyprkGNLVARLRGTDPKKPILLL-AHMDVVEaKR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 77 ASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSlpF----NLLLALSAEEECMGEHGMRALLPQL----- 147
Cdd:PRK09133 118 EDWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREG--FkpkrDIILALTGDEEGTPMNGVAWLAENHrdlid 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313158256 148 ----------GTIDMAlvGEPTGMQAAVGERGLVVLDCEARGKSGHAARNEGINALYIALDDIARLRSFRF 208
Cdd:PRK09133 196 aefalnegggGTLDED--GKPVLLTVQAGEKTYADFRLEVTNPGGHSSRPTKDNAIYRLAAALSRLAAYRF 264
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
8-246 |
2.50e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 67.57 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 8 AVELLRRLIATPST------SRDESRTADLLFAFLEERGAAPERLHN-----NVFARSADFDPARPTLLLNSHHDTVrPA 76
Cdd:PRK07906 1 VVDLCSELIRIDTTntgdgtGKGEREAAEYVAEKLAEVGLEPTYLESapgraNVVARLPGADPSRPALLVHGHLDVV-PA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 77 --ASYTRDPFTPTAEGDRLYGLGS---NDAGASVVSLARTFLTFREQSlPFNLLLALSAEEECMGEHGMRALL---PQLG 148
Cdd:PRK07906 80 eaADWSVHPFSGEIRDGYVWGRGAvdmKDMDAMMLAVVRHLARTGRRP-PRDLVFAFVADEEAGGTYGAHWLVdnhPELF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 149 TIDMALVGEPTGMQAAVG-----------ERGLVVLDCEARGKSGHAARNEGINALYIALDDIARLRSFRF--------- 208
Cdd:PRK07906 159 EGVTEAISEVGGFSLTVPgrdrlylietaEKGLAWMRLTARGRAGHGSMVNDDNAVTRLAEAVARIGRHRWplvltptvr 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313158256 209 ---DRVSEL----------------LGPIGIAV----------TQIAAGTQHNVVPDSCRFVVDLRT 246
Cdd:PRK07906 239 aflDGVAELtglefdpddpdallakLGPAARMVgatlrntanpTMLKAGYKVNVIPGTAEAVVDGRF 305
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
7-249 |
9.90e-12 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 65.42 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 7 EAVELLRRLIATPSTSRDE---SRTADLLFAFLEERGA------APERLHNNVFARSADFDPARptLLLNSHHDTVRPAA 77
Cdd:PRK06133 38 AYLDTLKELVSIESGSGDAeglKQVAALLAERLKALGAkverapTPPSAGDMVVATFKGTGKRR--IMLIAHMDTVYLPG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 78 SYTRDPFTptAEGDRLYGLGSNDAGASVVSLARTF-----LTFREQSlpfNLLLALSAEEEcMGEHGMRALLPQLGTI-D 151
Cdd:PRK06133 116 MLAKQPFR--IDGDRAYGPGIADDKGGVAVILHALkilqqLGFKDYG---TLTVLFNPDEE-TGSPGSRELIAELAAQhD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 152 MALVGEPTGMQAA--VGERGLVVLDCEARGKSGHA--ARNEGINALYIALDDIARLRsfrfdrvsELLGPI-GIAV--TQ 224
Cdd:PRK06133 190 VVFSCEPGRAKDAltLATSGIATALLEVKGKASHAgaAPELGRNALYELAHQLLQLR--------DLGDPAkGTTLnwTV 261
|
250 260
....*....|....*....|....*
gi 313158256 225 IAAGTQHNVVPDSCRFVVDLRTTDA 249
Cdd:PRK06133 262 AKAGTNRNVIPASASAQADVRYLDP 286
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
6-193 |
1.20e-11 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 65.41 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 6 TEAVELLRrliaTPSTSRDESRTADL------LFAFLEERGAAPERL-----HNNVFArSADFDPARPTLLLNSHHDT-- 72
Cdd:cd05680 2 EELFELLR----IPSVSADPAHKGDVrraaewLADKLTEAGFEHTEVlptggHPLVYA-EWLGAPGAPTVLVYGHYDVqp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 73 VRPAASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFR--EQSLPFNLLLALSAEEECmGEHGMRALLPQLG-- 148
Cdd:cd05680 77 PDPLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLavEGALPVNVKFLIEGEEEI-GSPSLPAFLEENAer 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 149 -TIDMALVGEpTGMQAA------VGERGLVVLDCEARGKS--------GHAARNEgINAL 193
Cdd:cd05680 156 lAADVVLVSD-TSMWSPdtptitYGLRGLAYLEISVTGPNrdlhsgsyGGAVPNP-ANAL 213
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
7-268 |
1.54e-11 |
|
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: 64.88 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 7 EAVELLRRLIATPS------TSRDESRTADLL--FAFLEERGAAPERLHNNVFARSA-------DFDPARPTLLLNSHHD 71
Cdd:cd02697 4 EEVRFLQKLVRVPTdtppgnNAPHAERTAALLqgFGFEAERHPVPEAEVRAYGMESItnlivrrRYGDGGRTVALNAHGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 72 TVRPAASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSLPFN--LLLALSAEEECMGEHGMRALLPQLGT 149
Cdd:cd02697 84 VVPPGDGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRgaVELHFTYDEEFGGELGPGWLLRQGLT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 150 IDMALVGEPTGMQAAVGERGLVVLDCEARGKSGHAAR-NEGINALYIALDDIARLRSFR--FDRVSELLGPIG---IAVT 223
Cdd:cd02697 164 KPDLLIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIpDTGVDALQGAVAILNALYALNaqYRQVSSQVEGIThpyLNVG 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 313158256 224 QIAAGTQHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALRSQAA 268
Cdd:cd02697 244 RIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAA 288
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
9-347 |
2.01e-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: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 9 VELLRRLIATPSTSRDES------RTADLLFAFLEERGAAPERLHNNVFARS--ADF--DPARPTLLLNSHHDTVRPA-- 76
Cdd:cd03893 1 LQTLAELVAIPSVSAQPDrreelrRAAEWLADLLRRLGFTVEIVDTSNGAPVvfAEFpgAPGAPTVLLYGHYDVQPAGde 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 77 ASYTRDPFTPTAEGDRLYGLGSNDAGASVVS--LARTFLTFREQSLPFNLLLALSAEEEcMGEHGMRALL---PQLGTID 151
Cdd:cd03893 81 DGWDSDPFELTERDGRLYGRGAADDKGPILAhlAALRALMQQGGDLPVNVKFIIEGEEE-SGSPSLDQLVeahRDLLAAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 152 MALVGEPTGMQAA-----VGERGLVVLDCEARGKSG--HAARNEGI--NALYIALDDIARLRSF---------------- 206
Cdd:cd03893 160 AIVISDSTWVGQEqptltYGLRGNANFDVEVKGLDHdlHSGLYGGVvpDPMTALAQLLASLRDEtgrilvpglydavrel 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 207 ------RFDRVSELLGPIG---------------IAVTQIAAGTQ----HNVVPDSCRFVVDLRTTDAYTNEETVEILRG 261
Cdd:cd03893 240 peeefrLDAGVLEEVEIIGgttgsvaerlwtrpaLTVLGIDGGFPgegsKTVIPPRARAKISIRLVPGQDPEEASRLLEA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 262 ALRSQaAPRSTRIRASALDAAHPLARAA------QAAGRRSYVSPTTSDMALM----PF----------PSLKMGPGES- 320
Cdd:cd03893 320 HLEKH-APSGAKVTVSYVEGGMPWRSDPsdpayqAAKDALRTAYGVEPPLTREggsiPFisvlqefpqaPVLLIGVGDPd 398
|
410 420
....*....|....*....|....*..
gi 313158256 321 SRSHTADEYVLLSEIGEGIGIYEEFIR 347
Cdd:cd03893 399 DNAHSPNESLRLGNYKEGTQAEAALLY 425
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
11-143 |
5.36e-11 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 63.29 E-value: 5.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 11 LLRRLIATPSTSRDESRTADLlFAFLEERgAAPE--------RLHNNVFARSADF-------DPARPTLLLNSHHDTVRP 75
Cdd:cd05679 9 ELARRVAVPTESQEPARKPEL-RAYLDQE-MRPRferlgftvHIHDNPVAGRAPFliaerieDPSLPTLLIYGHGDVVPG 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 313158256 76 AASYTRD---PFTPTAEGDRLYGLGSND-AGASVVSLA--RTFLTFREQSLPFNLLLALSAEEEcMGEHGMRAL 143
Cdd:cd05679 87 YEGRWRDgrdPWTVTVWGERWYGRGTADnKGQHSINMAalRQVLEARGGKLGFNVKFLIEMGEE-MGSPGLRAF 159
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
1-264 |
7.40e-10 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 59.77 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 1 MDAKTTEAVELLRRLIATPSTS---RDESRTADLLFAFLEERGAAPE--RLHN-----------NVFARSADFDPaRPTL 64
Cdd:PRK13013 9 IEARRDDLVALTQDLIRIPTLNppgRAYREICEFLAARLAPRGFEVEliRAEGapgdsetyprwNLVARRQGARD-GDCV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 65 LLNSHHDTVRPAASYTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSLPFNLLLALS--AEEECMGEHGMrA 142
Cdd:PRK13013 88 HFNSHHDVVEVGHGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISgtADEESGGFGGV-A 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 143 LLPQLG-----TIDMALVGEPTGM-QAAVGERGLVVLDCEARGKSGHAAR----NEGINALYIALDDIAR-------LRS 205
Cdd:PRK13013 167 YLAEQGrfspdRVQHVIIPEPLNKdRICLGHRGVWWAEVETRGRIAHGSMpflgDSAIRHMGAVLAEIEErlfpllaTRR 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 313158256 206 FRFDRVSELLGPIGIAVTQIAAGT----------QHNVVPDSCRFVVDLRttdaYTNEETVEILRGALR 264
Cdd:PRK13013 247 TAMPVVPEGARQSTLNINSIHGGEpeqdpdytglPAPCVADRCRIVIDRR----FLIEEDLDEVKAEIT 311
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
10-133 |
1.55e-09 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 58.89 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 10 ELLRRLIATPSTSRDESR---TADLLFAFLEERGAAPERLHNNVF-ARSADFDP-ARPTLLLNSHHDT--VRPAASYTRD 82
Cdd:cd05681 3 EDLRDLLKIPSVSAQGRGipeTADFLKEFLRRLGAEVEIFETDGNpIVYAEFNSgDAKTLLFYNHYDVqpAEPLELWTSD 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 313158256 83 PFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQ--SLPFNLLLALSAEEE 133
Cdd:cd05681 83 PFELTIRNGKLYARGVADDKGELMARLAALRALLQHlgELPVNIKFLVEGEEE 135
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
132-268 |
3.75e-09 |
|
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: 57.61 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 132 EECMGEHGMRALlpQLGTIdmalVGEPTGMQAAVGERGLVVldceaRGKSGHAAR-NEGINALYIALDDIARLRSFrFDR 210
Cdd:cd03886 144 DAAFGLHVWPGL--PVGTV----GVRSGALMASADEFEITV-----KGKGGHGASpHLGVDPIVAAAQIVLALQTV-VSR 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 313158256 211 VSELLGPIGIAVTQIAAGTQHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALRSQAA 268
Cdd:cd03886 212 ELDPLEPAVVTVGKFHAGTAFNVIPDTAVLEGTIRTFDPEVREALEARIKRLAEGIAA 269
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
58-264 |
4.87e-09 |
|
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: 57.27 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 58 DPARPTLLLNSHHDTVrPAASYTRD-----PFTPTAEGDRLYGLGSNDAGASVVS--------LARTFltFREQSlpfnL 124
Cdd:cd05674 66 DPSLKPLLLMAHQDVV-PVNPETEDqwthpPFSGHYDGGYIWGRGALDDKNSLIGileavellLKRGF--KPRRT----I 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 125 LLALSAEEECMGEHGMRA----LLPQLGTIDMALV---------GEPTGMQAA---VGERGLVVLDCEARGKSGHAA--- 185
Cdd:cd05674 139 ILAFGHDEEVGGERGAGAiaelLLERYGVDGLAAIldeggavleGVFLGVPFAlpgVAEKGYMDVEITVHTPGGHSSvpp 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 186 RNEGI----------------------NALYIALDDIAR------------LRSFRFDRVSELL------GPIG------ 219
Cdd:cd05674 219 KHTGIgilseavaaleanpfppkltpgNPYYGMLQCLAEhsplpprslksnLWLASPLLKALLAsellstSPLTrallrt 298
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 313158256 220 -IAVTQIAAGTQHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALR 264
Cdd:cd05674 299 tQAVDIINGGVKINALPETATATVNHRIAPGSSVEEVLEHVKNLIA 344
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
10-143 |
9.79e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 56.46 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 10 ELLRRLIATPSTSRDESRTADLLFAFLEERGAAPERL------HNNVFARSADF-------DPARPTLLLNSHHDTVRPA 76
Cdd:PRK07079 21 ADLARRVAYRTESQNPDRAPALRAYLTDEIAPALAALgftcriVDNPVAGGGPFliaerieDDALPTVLIYGHGDVVRGY 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 313158256 77 ASYTR---DPFTPTAEGDRLYGLGSND-AGASVVSLA--RTFLTFREQSLPFNLLLALSAEEECmGEHGMRAL 143
Cdd:PRK07079 101 DEQWReglSPWTLTEEGDRWYGRGTADnKGQHTINLAalEQVLAARGGRLGFNVKLLIEMGEEI-GSPGLAEV 172
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
8-156 |
3.22e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 54.91 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 8 AVELLRRLIATPSTS-----RDES-RTADLLFAFLEERGAAPERLHN-----NVFARSADfDPARPTLLLNSHHDtVRPA 76
Cdd:PRK07907 20 VRADLEELVRIPSVAadpfrREEVaRSAEWVADLLREAGFDDVRVVSadgapAVIGTRPA-PPGAPTVLLYAHHD-VQPP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 77 ---ASYTRDPFTPTAEGDRLYGLGSNDAGASVVS-LArtflTFR--EQSLPFNLLLALSAEEEcMGEHGMRALL---PQL 147
Cdd:PRK07907 98 gdpDAWDSPPFELTERDGRLYGRGAADDKGGIAMhLA----ALRalGGDLPVGVTVFVEGEEE-MGSPSLERLLaehPDL 172
|
....*....
gi 313158256 148 GTIDMALVG 156
Cdd:PRK07907 173 LAADVIVIA 181
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
62-236 |
3.89e-08 |
|
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: 54.38 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 62 PTLLLNSHHDTVRPAasytRDPFTPTAEGDRLYG-----LGSNDAgASVVSLARTFLTFREQSLPF-NLLLALSAEEECm 135
Cdd:cd05683 68 PKILFTSHMDTVTPG----INVKPPQIADGYIYSdgttiLGADDK-AGIAAILEAIRVIKEKNIPHgQIQFVITVGEES- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 136 GEHGMRALLPQLGTIDMALVGEPTGmqaAVGErgLVV-------LDCEARGKSGHA--ARNEGINALYIALDDIARLRSF 206
Cdd:cd05683 142 GLVGAKALDPELIDADYGYALDSEG---DVGT--IIVgaptqdkINAKIYGKTAHAgtSPEKGISAINIAAKAISNMKLG 216
|
170 180 190
....*....|....*....|....*....|
gi 313158256 207 RFDrvSELLGPIGIavtqIAAGTQHNVVPD 236
Cdd:cd05683 217 RID--EETTANIGK----FQGGTATNIVTD 240
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
9-275 |
6.52e-08 |
|
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: 53.82 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 9 VELLRRLIATPSTSRDESRTADLLFAFLEERGAAPERL--HNNVFArsaDFDPAR--PTLLLNSHHDTVrPAASYTRDPF 84
Cdd:cd08014 2 VEWRRHLHAHPELSGQEYRTTAFVAERLRDLGLKPKEFpgGTGLVC---DIGGKRdgRTVALRADMDAL-PIQEQTGLPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 85 TPTAEGdRLYGLGsNDAGASVVSLARTFLTFREQSLPFNLLLALSAEEECM--GEHGMRA--LLPQLGTIdMALVGEPTG 160
Cdd:cd08014 78 RSTVPG-VMHACG-HDAHTAIALGAALVLAALEEELPGRVRLIFQPAEETMpgGALDMIRagALDGVSAI-FALHVDPRL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 161 MQAAVGERGLV------VLDCEARGKSGHAAR-NEGINALYIA---LDDIARLRSFRFDRvselLGPIGIAVTQIAAGTQ 230
Cdd:cd08014 155 PVGRVGVRYGPitaaadSLEIRIQGEGGHGARpHLTVDLVWAAaqvVTDLPQAISRRIDP----RSPVVLTWGSIEGGRA 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 313158256 231 HNVVPDSCRFVVDLRTTDAYTNEETVEILRGALRSQAAPRSTRIR 275
Cdd:cd08014 231 PNVIPDSVELSGTVRTLDPDTWAQLPDLVEEIVAGICAPYGAKYE 275
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
2-144 |
9.78e-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: 53.37 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 2 DAKTTEAVELLRRLIATPSTSRDESRTADLLFAF------LEERGA-------APERLHNN--------VFARSADfDPA 60
Cdd:cd05676 6 DEHQDEFIERLREAVAIQSVSADPEKRPELIRMMewaaerLEKLGFkvelvdiGTQTLPDGeelplppvLLGRLGS-DPS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 61 RPTLLLNSHHDtVRPAAS---YTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFRE--QSLPFNLLLALSAEEECm 135
Cdd:cd05676 85 KKTVLIYGHLD-VQPAKLedgWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKlgQELPVNLKFCFEGMEES- 162
|
....*....
gi 313158256 136 GEHGMRALL 144
Cdd:cd05676 163 GSEGLDELI 171
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
58-247 |
1.25e-07 |
|
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: 52.87 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 58 DPARPTLLLNSHHDTVrPAAS--YTRDPFTP--TAEGDrLYGLGSND---AGASVVSLARTfLTFREQSLPFNLLLALSA 130
Cdd:TIGR01880 68 NPELPSILLNSHTDVV-PVFRehWTHPPFSAfkDEDGN-IYARGAQDmkcVGVQYLEAVRN-LKASGFKFKRTIHISFVP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 131 EEECMGEHGMRALLP-------QLG-TIDMALVGEPTGMQAAVGERGLVVLDCEARGKSGHAAR---NEGINALYIALDD 199
Cdd:TIGR01880 145 DEEIGGHDGMEKFAKtdefkalNLGfALDEGLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSKlmeNTAMEKLEKSVES 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 313158256 200 IARLRSFRFDRVSEllGP-------IGIAVTQIAAGTQHNVVPDSCRFVVDLRTT 247
Cdd:TIGR01880 225 IRRFRESQFQLLQS--NPdlaigdvTSVNLTKLKGGVQSNVIPSEAEAGFDIRLA 277
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
47-140 |
1.48e-07 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 52.85 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 47 HNNVFARSADFDPARPTLLLNSHHDTVRPAAS-YTRDPFTPTAEGDRLYGLGSNDAGASVVSLARTFLTFREQSLPFNLL 125
Cdd:PRK08554 49 KDGYYAVYGEIGEGKPKLLFMAHFDVVPVNPEeWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLNGKVI 128
|
90
....*....|....*
gi 313158256 126 LALSAEEECMGEHGM 140
Cdd:PRK08554 129 FAFTGDEEIGGAMAM 143
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
59-159 |
3.20e-07 |
|
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: 50.12 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 59 PARPTLLLNSHHDTVRPAASYTRDPFTP--TAEGDRLYGLGSNDAGASVVSLARTFLTFRE--QSLPFNLLLALSAEEEC 134
Cdd:cd18669 10 GGGKRVLLGAHIDVVPAGEGDPRDPPFFvdTVEEGRLYGRGALDDKGGVAAALEALKLLKEngFKLKGTVVVAFTPDEEV 89
|
90 100
....*....|....*....|....*....
gi 313158256 135 MGEHG----MRALLPQLGTIDMALVGEPT 159
Cdd:cd18669 90 GSGAGkgllSKDALEEDLKVDYLFVGDAT 118
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
9-133 |
3.52e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 51.68 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 9 VELLRrLIATPSTSRDESRTADLLFAFLEERG--AAPERLHNNVFARSADFDPARPTLLLNSHHDT--VRPAASYTRDPF 84
Cdd:PRK06446 9 IEFLK-KPSISATGEGIEETANYLKDTMEKLGikANIERTKGHPVVYGEINVGAKKTLLIYNHYDVqpVDPLSEWKRDPF 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 313158256 85 TPTAEGDRLYGLG-SNDAGASVVSLARTFLTFREQSLPFNLLLALSAEEE 133
Cdd:PRK06446 88 SATIENGRIYARGaSDNKGTLMARLFAIKHLIDKHKLNVNVKFLYEGEEE 137
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
7-163 |
8.06e-07 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 50.42 E-value: 8.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 7 EAVELLRRLIATPSTS---RDESRTADLLFAFLEERGAAPERLH-----NNVFARSADFDPARP-TLLLNSHHD--TVRP 75
Cdd:PRK08596 14 ELLELLKTLVRFETPAppaRNTNEAQEFIAEFLRKLGFSVDKWDvypndPNVVGVKKGTESDAYkSLIINGHMDvaEVSA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 76 AASYTRDPFTPTAEGDRLYGLGSND--AGASVVSLARTFLTFREQSLPFNLLLALSAEEEcMGEHGMRALLPQLGTIDMA 153
Cdd:PRK08596 94 DEAWETNPFEPTIKDGWLYGRGAADmkGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEE-VGEAGTLQCCERGYDADFA 172
|
170
....*....|
gi 313158256 154 LVGEPTGMQA 163
Cdd:PRK08596 173 VVVDTSDLHM 182
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
178-268 |
1.19e-06 |
|
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 49.73 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 178 RGKSGHAAR-NEGINALYIALDDIARLRSFRFDRVSELlGPIGIAVTQIAAGTQHNVVPDSCRFVVDLRTTDAYTNEETV 256
Cdd:COG1473 191 KGKGGHAAApHLGIDPIVAAAQIVTALQTIVSRNVDPL-DPAVVTVGIIHGGTAPNVIPDEAELEGTVRTFDPEVRELLE 269
|
90
....*....|..
gi 313158256 257 EILRGALRSQAA 268
Cdd:COG1473 270 ERIERIAEGIAA 281
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
64-249 |
2.93e-06 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 48.81 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 64 LLLNSHHDTVRPAASytrdPFTPTA--EGDRLYGLGSND-AGASVVSLARtfLTFREQSlPFNLLLA----LSAEEEcMG 136
Cdd:PRK07338 95 VLLTGHMDTVFPADH----PFQTLSwlDDGTLNGPGVADmKGGIVVMLAA--LLAFERS-PLADKLGydvlINPDEE-IG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 137 EHGMRALLPQLGT-IDMALVGEPT---GMQAAvGERGLVVLDCEARGKSGHAARN--EGINALyIALDDIArlrsFRFDR 210
Cdd:PRK07338 167 SPASAPLLAELARgKHAALTYEPAlpdGTLAG-ARKGSGNFTIVVTGRAAHAGRAfdEGRNAI-VAAAELA----LALHA 240
|
170 180 190
....*....|....*....|....*....|....*....
gi 313158256 211 VSELLGPIGIAVTQIAAGTQHNVVPDSCRFVVDLRTTDA 249
Cdd:PRK07338 241 LNGQRDGVTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTP 279
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
173-264 |
4.41e-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: 48.04 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 173 LDCEARGKSGHAAR-NEGINALYIALDDIARLRSFRFDRVSELLGPIgIAVTQIAAGTQHNVVPDSCRFVVDLRTTDayt 251
Cdd:cd08021 184 FDITIKGKGGHGSMpHETVDPIVIAAQIVTALQTIVSRRVDPLDPAV-VTIGTFQGGTSFNVIPDTVELKGTVRTFD--- 259
|
90
....*....|...
gi 313158256 252 nEETVEILRGALR 264
Cdd:cd08021 260 -EEVREQVPKRIE 271
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
9-133 |
2.65e-05 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 45.94 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 9 VELLRRLIATPSTSRDES---RTADLLFAFLEERGAAPERLHNN---VFARSADFDPARPTLLLNSHHD--TVRPAASYT 80
Cdd:cd05678 2 YREHRELVSIPNDATDEEemrKNVDWLEQAFRKRGFKTSQLPTSglpLLLAEKPISDARKTVLFYMHLDgqPVDPSKWDQ 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313158256 81 RDPFTP-----TAEGD-----------------RLYGLGSNDAGASVVSL--ARTFLTFREQSLPFNLLLALSAEEE 133
Cdd:cd05678 82 KSPYTPvlkrkDAAGNweeinwdaifsnldpewRVFARAAADDKGPIMMMlaALDALKAGGIAPKFNVKIILDSEEE 158
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
7-138 |
3.69e-05 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 45.51 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 7 EAVELLRRLIATPSTS------RDESRTADLLFAFLEERGAAPERLHNN-----VFARSADfDPARPTLLLNSHHDT--V 73
Cdd:PRK08201 15 AHLEELKEFLRIPSISalsehkEDVRKAAEWLAGALEKAGLEHVEIMETaghpiVYADWLH-APGKPTVLIYGHYDVqpV 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 313158256 74 RPAASYTRDPFTPTAEGDRLYGLG-SNDAGASVVSL-ARTFLTFREQSLPFNLLLALSAEEECMGEH 138
Cdd:PRK08201 94 DPLNLWETPPFEPTIRDGKLYARGaSDDKGQVFMHLkAVEALLKVEGTLPVNVKFCIEGEEEIGSPN 160
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
176-268 |
9.10e-05 |
|
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: 43.86 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 176 EARGKSGHAAR-NEGINALYIALDDIARLRSFrFDRVSELLGPIGIAVTQIAAGTQHNVVPDSCRFVVDLRTTDAYTNEE 254
Cdd:cd08019 174 EVKGKGGHGSMpHQGIDAVLAAASIVMNLQSI-VSREIDPLEPVVVTVGKLNSGTRFNVIADEAKIEGTLRTFNPETREK 252
|
90
....*....|....
gi 313158256 255 TVEILRGALRSQAA 268
Cdd:cd08019 253 TPEIIERIAKHTAA 266
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
58-159 |
1.02e-04 |
|
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 42.80 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 58 DPARPTLLLNSHHDTVRPAASYTRDPFTP--TAEGDRLYGLGSNDAGASVVSLARTFLTFRE--QSLPFNLLLALSAEEE 133
Cdd:cd03873 9 GEGGKSVALGAHLDVVPAGEGDNRDPPFAedTEEEGRLYGRGALDDKGGVAAALEALKRLKEngFKPKGTIVVAFTADEE 88
|
90 100 110
....*....|....*....|....*....|
gi 313158256 134 CMGEHGMRALLPQL----GTIDMALVGEPT 159
Cdd:cd03873 89 VGSGGGKGLLSKFLlaedLKVDAAFVIDAT 118
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
176-260 |
2.44e-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: 42.67 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 176 EARGKSGHAAR-NEGINALYIALDDIARLRSFrfdrVSELLGPIG---IAVTQIAAGTQHNVVPDSCRFVVDLRTTDAYT 251
Cdd:cd05669 178 EIAGKGAHAAKpENGVDPIVAASQIINALQTI----VSRNISPLEsavVSVTRIHAGNTWNVIPDSAELEGTVRTFDAEV 253
|
....*....
gi 313158256 252 NEETVEILR 260
Cdd:cd05669 254 RQLVKERFE 262
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
2-108 |
3.76e-04 |
|
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: 42.23 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 2 DAKTTEAVELLRRLIATPStSRDESR--------TADLLFAFLE--ERGAAPERLHNNVFARsADFDPARPTLLLNSHHD 71
Cdd:cd03888 4 DKYKDEILEDLKELVAIPS-VRDEATegapfgegPRKALDKFLDlaKRLGFKTKNIDNYAGY-AEYGEGEEVLGILGHLD 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 313158256 72 TVRPAASYTRDPFTPTAEGDRLYGLGSND-AGASVVSL 108
Cdd:cd03888 82 VVPAGEGWTTDPFKPVIKDGKLYGRGTIDdKGPTIAAL 119
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
178-268 |
3.98e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349916 [Multi-domain] Cd Length: 373 Bit Score: 41.74 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 178 RGKSGHAARNE-GINALYIALDDIARLRSFrfdrVSELLGPIGIAV---TQIAAGTQHNVVPDSCRFVVDLRTTDAYTNE 253
Cdd:cd05666 180 RGKGGHAAMPHlGVDPIVAAAQLVQALQTI----VSRNVDPLDAAVvsvTQIHAGDAYNVIPDTAELRGTVRAFDPEVRD 255
|
90
....*....|....*
gi 313158256 254 ETVEILRGALRSQAA 268
Cdd:cd05666 256 LIEERIREIADGIAA 270
|
|
| PRK12890 |
PRK12890 |
allantoate amidohydrolase; Reviewed |
3-284 |
4.94e-04 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 237248 [Multi-domain] Cd Length: 414 Bit Score: 41.81 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 3 AKTTEAVELLRRLIATPstsrDESRTADLLFAFLEERGAAPERLH-NNVFARSADFDPARPTLLLNSHHDTVRPAASYtr 81
Cdd:PRK12890 19 AAIGRDGPGWTRLALSD----EERAARALLAAWMRAAGLEVRRDAaGNLFGRLPGRDPDLPPLMTGSHLDTVPNGGRY-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 82 dpftptaegDRLYGLGsndAGASVVslartfLTFREQ--SLPFNLLLALSAEEE-------CMGEHGMRALLPQ---LGT 149
Cdd:PRK12890 93 ---------DGILGVL---AGLEVV------AALREAgiRPPHPLEVIAFTNEEgvrfgpsMIGSRALAGTLDVeavLAT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 150 ID---------MALVG-EPTGMQAAVGERGLV------------VLDCEA-------------------RGKSGHAA--- 185
Cdd:PRK12890 155 RDddgttlaeaLRRIGgDPDALPGALRPPGAVaaflelhieqgpVLEAEGlpigvvtaiqgirrqavtvEGEANHAGttp 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 186 RNEGINALYIALDDIARLRSFRFDRVSELLGPIG-IAVTQIAagtqHNVVPDSCRFVVDLRTTDAYTNEETVEILRGALR 264
Cdd:PRK12890 235 MDLRRDALVAAAELVTAMERRARALLHDLVATVGrLDVEPNA----INVVPGRVVFTLDLRSPDDAVLEAAEAALLAELE 310
|
330 340
....*....|....*....|
gi 313158256 265 SQAAPRSTRIRASALDAAHP 284
Cdd:PRK12890 311 AIAAARGVRIELERLSRSEP 330
|
|
| M20_ACY1L2-like |
cd05672 |
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 ... |
150-262 |
5.41e-04 |
|
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. This subfamily includes Staphylococcus aureus antibiotic resistance factor HmrA that has been shown to participate in methicillin resistance mechanisms in vivo in the presence of beta-lactams. Aminoacylase 1 (ACY1) proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349921 [Multi-domain] Cd Length: 360 Bit Score: 41.39 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 150 IDMALVGEPTGMQAAVGE-RGLVVLDCEARGKSGHAARN--EGINAL------YIAlddIARLRSF--RFDRVSellgpi 218
Cdd:cd05672 137 VDAALMVHPGPRDVAGVPsLAVDKLTVEFHGKSAHAAAApwEGINALdaavlaYNA---ISALRQQlkPTWRIH------ 207
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 313158256 219 GIaVTQiaAGTQHNVVPDSCRFVVDLR-TTDAYTNE--ETVE-ILRGA 262
Cdd:cd05672 208 GI-ITE--GGKAPNIIPDYAEARFYVRaPTRKELEElrERVIaCFEGA 252
|
|
| M20_Acy1L2 |
cd03887 |
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
2-262 |
7.85e-04 |
|
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, Aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase) subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349883 [Multi-domain] Cd Length: 360 Bit Score: 41.02 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 2 DAKTTEAVELLRRLIATPSTSRDESRTADLLFAFLEERGaaperlhnnvfarsadFDPARPTLLLnshhDT-VRpaASYT 80
Cdd:cd03887 1 DEHAEELIELSRDIHDNPELGYEEYKAHDLLTDFLEELG----------------FDVTRGAYGL----ETaFR--AEYG 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 81 RDPFTPT----AEGDRLYGL----GSNDAGASvvSLArTFLTFRE----QSLPFNL-LLALSAEEEcmgeHGMRALLPQL 147
Cdd:cd03887 59 SGKGGPTvaflAEYDALPGIghacGHNLIATA--SVA-AALALKAalkaLGLPGTVvVLGTPAEEG----GGGKIDLIKA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 148 GT---IDMALVGEPTGMQAAVGE-RGLVVLDCEARGKSGHAARN--EGINAL------YIAlddIARLRSFRFDRVSell 215
Cdd:cd03887 132 GAfddVDIALMVHPGPKDVAGPKsLAVSKLRVEFHGKAAHAAAApwEGINALdaavlaYNN---ISALRQQLKPTVR--- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 313158256 216 gpIGIAVTQiaAGTQHNVVPDSCRFVVDLR-TTDAYTNE--ETVE-ILRGA 262
Cdd:cd03887 206 --VHGIITE--GGKAPNIIPDYAEAEFYVRaPTLKELEEltERVIaCFEGA 252
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
35-121 |
1.30e-03 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 40.39 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 35 FLEERGAAPErlhnnVFARSADFDPARPTLLLNSHHDTVRPAASYTRD--PFTPTAEGDRLYGLGSNDAGASVVSLARTF 112
Cdd:cd05682 52 VVELEGRTPL-----LFVEIPGTEQDDDTVLLYGHMDKQPPFTGWDEGlgPTKPVIRGDKLYGRGGADDGYAIFASLTAI 126
|
....*....
gi 313158256 113 LTFREQSLP 121
Cdd:cd05682 127 KALQEQGIP 135
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
176-268 |
1.71e-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: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 176 EARGKSGHAAR-NEGINALYIALDDIARLRSFRFDRVSellgPIGIAVTQI-AAGTQHNVVPDSCRFVVDLRTTDAYTNE 253
Cdd:cd08018 173 TIKGKQAHGARpHLGINAIEAASAIVNAVNAIHLDPNI----PWSVKMTKLqAGGEATNIIPDKAKFALDLRAQSNEAME 248
|
90
....*....|....*
gi 313158256 254 ETVEILRGALRSQAA 268
Cdd:cd08018 249 ELKEKVEHAIEAAAA 263
|
|
| M20_Acy1-like |
cd05667 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
178-260 |
2.67e-03 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349917 [Multi-domain] Cd Length: 403 Bit Score: 39.33 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 178 RGKSGHAARN-EGINALYIALDDIARLRSFRFDRVSELLGPIGIAVTQIAAGTQHNVVPDSCRFVVDLRTTDAYTNEETV 256
Cdd:cd05667 203 KGKQTHGSRPwDGIDPIMASAQIIQGLQTIISRRIDLTKEPAVISIGKINGGTRGNIIPEDAEMVGTIRTFDPEMREDIF 282
|
....
gi 313158256 257 EILR 260
Cdd:cd05667 283 ARLK 286
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
9-155 |
3.57e-03 |
|
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: 38.86 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 9 VELLRRLIATPSTSRDES--------RTADLLFAFLEERGA-----APERLHNN--VFAR--SADFDPARPTLLLNSHHD 71
Cdd:cd05677 2 LNTLSEFIAFQTVSQSPTtenaedsrRCAIFLRQLFKKLGAtncllLPSGPGTNpiVLATfsGNSSDAKRKRILFYGHYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313158256 72 TVrPA---ASYTRDPFTPTAEGDRLYGLG-SNDAGASVVSLARTFLTFREQSLPFNLLLALSAEEECmGEHGMRALL--- 144
Cdd:cd05677 82 VI-PAgetDGWDTDPFTLTCENGYLYGRGvSDNKGPLLAAIYAVAELFQEGELDNDVVFLIEGEEES-GSPGFKEVLrkn 159
|
170
....*....|..
gi 313158256 145 -PQLGTIDMALV 155
Cdd:cd05677 160 kELIGDIDWILL 171
|
|
| |
