|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
4-378 |
0e+00 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 679.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 4 ILAALLAFDTTSRHSNLAMIDWIADFLAARGVASRRFYDPSGGKANLYARLGPSGGGGVMLSGHTDVVPVDGQAWSVPPF 83
Cdd:PRK07522 9 ILERLVAFDTVSRDSNLALIEWVRDYLAAHGVESELIPDPEGDKANLFATIGPADRGGIVLSGHTDVVPVDGQAWTSDPF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 84 SLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAFSYDEEVGCLGVRSLVDFLQASPEKPALCLIGEPTEM 163
Cdd:PRK07522 89 RLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPSMIARLPERGVKPAGCIVGEPTSM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 164 QPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLGVRLARQ--QDSRFSPPFSTLQVGTIQGGAALNI 241
Cdd:PRK07522 169 RPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLAAPgpFDALFDPPYSTLQTGTIQGGTALNI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 242 VPQSCRFDFEIRYLPGMRPEAVTEALAAYARRQLLPEMRRVGSGSDIQFQLLSHYPPLLSDPQSDFARWLAQWCGSDRFS 321
Cdd:PRK07522 249 VPAECEFDFEFRNLPGDDPEAILARIRAYAEAELLPEMRAVHPEAAIEFEPLSAYPGLDTAEDAAAARLVRALTGDNDLR 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1396632015 322 TVAFGTEGGLFDEMGVATLVCGPGSMAQGHKADEYISIAQTERCMTMLRQLCAWMRA 378
Cdd:PRK07522 329 KVAYGTEAGLFQRAGIPTVVCGPGSIEQAHKPDEFVELAQLAACEAFLRRLLASLAA 385
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
4-374 |
0e+00 |
|
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: 573.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 4 ILAALLAFDTTSRHSNLAMIDWIADFLAARGVASRRFYDPSGGKANLYARLGPSGGGGVMLSGHTDVVPVDGQAWSVPPF 83
Cdd:cd03894 2 LLARLVAFDTVSRNSNLALIEYVADYLAALGVKSRRVPVPEGGKANLLATLGPGGEGGLLLSGHTDVVPVDGQKWSSDPF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 84 SLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAFSYDEEVGCLGVRSLVDFLQASPEKPALCLIGEPTEM 163
Cdd:cd03894 82 TLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALAARGGRPDAAIVGEPTSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 164 QPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLGVRLARQ-QDSRFSPPFSTLQVGTIQGGAALNIV 242
Cdd:cd03894 162 QPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLAPGlRDPPFDPPYPTLNVGLIHGGNAVNIV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 243 PQSCRFDFEIRYLPGMRPEAVTEALAAYARRQLLPEmrrvgsGSDIQFQLLSHYPPLLSDPQSDFARWLAQWCGSDRFST 322
Cdd:cd03894 242 PAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFP------EAGIEVEPLFEVPGLETDEDAPLVRLAAALAGDNKVRT 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1396632015 323 VAFGTEGGLFDEMGVATLVCGPGSMAQGHKADEYISIAQTERCMTMLRQLCA 374
Cdd:cd03894 316 VAYGTEAGLFQRAGIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
4-372 |
5.95e-134 |
|
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: 387.64 E-value: 5.95e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 4 ILAALLAFDTTSRHSNLAMIDWIADFLAARGVASRRFYDPSGG-KANLYARLGPSGGGGVMLSGHTDVVPVDGQAWSVPP 82
Cdd:TIGR01892 2 ILTKLVAFDSTSFRPNVDLIDWAQAYLEALGFSVEVQPFPDGAeKSNLVAVIGPSGAGGLALSGHTDVVPYDDAAWTRDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 83 FSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAFSYDEEVGCLGVRSLVDflqASPEKPALCLIGEPTE 162
Cdd:TIGR01892 82 FRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIE---AGAGRPRHAIIGEPTR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 163 MQPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLGVRLARQQ-DSRFSPPFSTLQVGTIQGGAALNI 241
Cdd:TIGR01892 159 LIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLLREDlDEGFTPPYTTLNIGVIQGGKAVNI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 242 VPQSCRFDFEIRYLPGMRPEAVTEALaayarRQLLPEMRRVGSGSDIQFQLLSHYPPLLSDPQSDFARWLAQWCGsDRFS 321
Cdd:TIGR01892 239 IPGACEFVFEWRPIPGMDPEELLQLL-----ETIAQALVRDEPGFEVQIEVVSTDPGVNTEPDAELVAFLEELSG-NAPE 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1396632015 322 TVAFGTEGGLFDEMGVATLVCGPGSMAQGHKADEYISIAQTERCMTMLRQL 372
Cdd:TIGR01892 313 VVSYGTEAPQFQELGAEAVVCGPGDIRQAHQPDEYVEIEDLVRCRAVLARL 363
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
4-378 |
3.69e-117 |
|
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: 345.72 E-value: 3.69e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 4 ILAALLAFDTTSrHSNLAMIDWIADFLAARGVASRRFYDPsGGKANLYARL-GPSGGGGVMLSGHTDVVPVDGQA-WSVP 81
Cdd:COG0624 17 LLRELVRIPSVS-GEEAAAAELLAELLEALGFEVERLEVP-PGRPNLVARRpGDGGGPTLLLYGHLDVVPPGDLElWTSD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 82 PFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAA--PLRMPLHLAFSYDEEVGCLGVRSLVDFLqASPEKPALCLIGE 159
Cdd:COG0624 95 PFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAglRLPGNVTLLFTGDEEVGSPGARALVEEL-AEGLKADAAIVGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 160 PTE-MQPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLgvRLARQQDSRFSPPfsTLQVGTIQGGAA 238
Cdd:COG0624 174 PTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDL--EFDGRADPLFGRT--TLNVTGIEGGTA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 239 LNIVPQSCRFDFEIRYLPGMRPEAVTEALAAYarrqllpeMRRVGSGSDIQFQLLSH-YPPLLSDPQSDFARWL----AQ 313
Cdd:COG0624 250 VNVIPDEAEAKVDIRLLPGEDPEEVLAALRAL--------LAAAAPGVEVEVEVLGDgRPPFETPPDSPLVAAAraaiRE 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1396632015 314 WCGSD-RFSTVAFGTEGGLF-DEMGVATLVCGPGSMAQGHKADEYISIAQTERCMTMLRQLCAWMRA 378
Cdd:COG0624 322 VTGKEpVLSGVGGGTDARFFaEALGIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
4-372 |
1.32e-83 |
|
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: 258.77 E-value: 1.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 4 ILAALLAFDTTSRHSnLAMIDWIADFLAARGVASRRFydPSGGKANLYARLGPSGGGGVMLSGHTDVVPV-DGQAWSVPP 82
Cdd:cd08659 2 LLQDLVQIPSVNPPE-AEVAEYLAELLAKRGYGIEST--IVEGRGNLVATVGGGDGPVLLLNGHIDTVPPgDGDKWSFPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 83 FSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAA--PLRMPLHLAFSYDEEVGCLGVRSLVDflQASPEKPALCLIGEP 160
Cdd:cd08659 79 FSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAgaLLGGRVALLATVDEEVGSDGARALLE--AGYADRLDALIVGEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 161 TEMQPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLGVRLARQQDsrFSPPfsTLQVGTIQGGAALN 240
Cdd:cd08659 157 TGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPAHPL--LGPP--TLNVGVINGGTQVN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 241 IVPQSCRFDFEIRYLPGMRPEAVTEALAAYArrqllpemRRVGSGSDIQFQlLSHYPPLLSDPQSDF----ARWLAQWCG 316
Cdd:cd08659 233 SIPDEATLRVDIRLVPGETNEGVIARLEAIL--------EEHEAKLTVEVS-LDGDPPFFTDPDHPLvqalQAAARALGG 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1396632015 317 SDRFSTVAFGTEGGLFDEM-GVATLVCGPGSMAQGHKADEYISIAQTERCMTMLRQL 372
Cdd:cd08659 304 DPVVRPFTGTTDASYFAKDlGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEI 360
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
17-372 |
2.26e-83 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 258.98 E-value: 2.26e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 17 HSNLAMIDWIADFLAARG-------VASRRfydpsgGKANLYARLGpSGGGGVMLSGHTDVVPVDGQAWSVPPFSLTERD 89
Cdd:PRK05111 29 QSNRAVIDLLAGWFEDLGfnveiqpVPGTR------GKFNLLASLG-SGEGGLLLAGHTDTVPFDEGRWTRDPFTLTEHD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 90 GRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAFSYDEEVGCLGVRSlvdFLQASPEKPALCLIGEPTEMQPVFGH 169
Cdd:PRK05111 102 GKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARA---FAEATAIRPDCAIIGEPTSLKPVRAH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 170 KGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLGVRLARQ-QDSRFSPPFSTLQVGTIQGGAALNIVPQSCRF 248
Cdd:PRK05111 179 KGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQERyHNPAFTVPYPTLNLGHIHGGDAPNRICGCCEL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 249 DFEIRYLPGMRPE----AVTEALAAYARRQllpemrrvgsGSDIQFQLLshYPPLLS---DPQSDFARWLAQWCGSdRFS 321
Cdd:PRK05111 259 HFDIRPLPGMTLEdlrgLLREALAPVSERW----------PGRITVAPL--HPPIPGyecPADHQLVRVVEKLLGH-KAE 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1396632015 322 TVAFGTEGGLFDEMGVATLVCGPGSMAQGHKADEYISIAQTERCMTMLRQL 372
Cdd:PRK05111 326 VVNYCTEAPFIQQLGCPTLVLGPGSIEQAHQPDEYLELSFIKPTRELLRQL 376
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
63-372 |
3.96e-61 |
|
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: 199.50 E-value: 3.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 63 MLSGHTDVVPvDGQAWSVPpFSLTErDGRYYGRGSADMKGFLACVLAAVDDFLAA-PLRMPLHLAFSYDEEVGCLGVRSL 141
Cdd:pfam01546 1 LLRGHMDVVP-DEETWGWP-FKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEgLKKGTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 142 VDFLQASPEKPALCL---IGEPTEMQ------PVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLgvr 212
Cdd:pfam01546 78 IEDGLLEREKVDAVFglhIGEPTLLEggiaigVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDI--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 213 LARQQDSRFSPPFSTLQVGTIQGGAalNIVPQSCRFDFEIRYLPGMRPEAVTEALAAYARRQLLPEMRRVgsgsDIQFQl 292
Cdd:pfam01546 155 VSRNVDPLDPAVVTVGNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKV----EVEYV- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 293 LSHYPPLLSDPQ-SDFARWLA-QWCGS---DRFSTVAFGTEGGLF-DEMGVATLVCGPGSmAQGHKADEYISIAQTERCM 366
Cdd:pfam01546 228 EGGAPPLVNDSPlVAALREAAkELFGLkveLIVSGSMGGTDAAFFlLGVPPTVVFFGPGS-GLAHSPNEYVDLDDLEKGA 306
|
....*.
gi 1396632015 367 TMLRQL 372
Cdd:pfam01546 307 KVLARL 312
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
24-361 |
2.05e-52 |
|
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: 178.75 E-value: 2.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 24 DWIADFLAARGVASRRfYDPSGGKAN-----LYARLGPSGGGGVMLSGHTDVVPV-DGQAWSVPPFSLTERDGRYYGRGS 97
Cdd:TIGR01910 25 NYIKDLLREFGFSTDV-IEITDDRLKvlgkvVVKEPGNGNEKSLIFNGHYDVVPAgDLELWKTDPFKPVEKDGKLYGRGA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 98 ADMKGFLACVLAAVDDFLAAPLRMP--LHLAFSYDEEVGCLGVRSLVDflQASPEKPALCLIGEPTE-MQPVFGHKGKLA 174
Cdd:TIGR01910 104 TDMKGGLVALLYALKAIREAGIKPNgnIILQSVVDEESGEAGTLYLLQ--RGYFKDADGVLIPEPSGgDNIVIGHKGSIW 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 175 MRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLGVRLARQQDSRFSPPFSTLQVGTIQGGAALNIVPQSCRFDFEIRY 254
Cdd:TIGR01910 182 FKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEEHIYARNSYGFIPGPITFNPGVIKGGDWVNSVPDYCEFSIDVRI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 255 LPGMRPEAVTEALAAYARRqllpemRRVGSGSDIQFQLLSHYP-PLLSDPQSDFARwLAQWCGSD------RFSTVAFGT 327
Cdd:TIGR01910 262 IPEENLDEVKQIIEDVVKA------LSKSDGWLYENEPVVKWSgPNETPPDSRLVK-ALEAIIKKvrgiepEVLVSTGGT 334
|
330 340 350
....*....|....*....|....*....|....
gi 1396632015 328 EGGLFDEMGVATLVCGPGSMAQGHKADEYISIAQ 361
Cdd:TIGR01910 335 DARFLRKAGIPSIVYGPGDLETAHQVNEYISIKN 368
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
22-364 |
1.62e-50 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 174.02 E-value: 1.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 22 MIDWIADFLAARGVaSRRFYDPSGGKANLYARLGP----SGGGG---VMLSGHTDVVPVDGQAWSVPPFSLTERDGRYYG 94
Cdd:PRK08651 31 IAEFLRDTLEELGF-STEIIEVPNEYVKKHDGPRPnliaRRGSGnphLHFNGHYDVVPPGEGWSVNVPFEPKVKDGKVYG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 95 RGSADMKGFLACVLAAVDDFlAAPLRMPLHLAFSYDEEVGCLGVRSLVDFLQAspeKPALCLIGEPTEMQPVF-GHKGKL 173
Cdd:PRK08651 110 RGASDMKGGIAALLAAFERL-DPAGDGNIELAIVPDEETGGTGTGYLVEEGKV---TPDYVIVGEPSGLDNICiGHRGLV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 174 AMRCCIEGQACHSAYAPQGVNAIRYAARLI---NHLDRLGVRLARQQDSRFSPPFSTLQVGTIQGGAALNIVPQSCRFDF 250
Cdd:PRK08651 186 WGVVKVYGKQAHASTPWLGINAFEAAAKIAerlKSSLSTIKSKYEYDDERGAKPTVTLGGPTVEGGTKTNIVPGYCAFSI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 251 EIRYLPGMRPEAVTEALAAYArRQLLPEmrrvgSGSDIQFQLLSHYPPLLSDPQSDFARWLA----QWCGSDRFSTVAFG 326
Cdd:PRK08651 266 DRRLIPEETAEEVRDELEALL-DEVAPE-----LGIEVEFEITPFSEAFVTDPDSELVKALReairEVLGVEPKKTISLG 339
|
330 340 350
....*....|....*....|....*....|....*....
gi 1396632015 327 -TEGGLFDEMGVATLVCGPGSMAQGHKADEYISIAQTER 364
Cdd:PRK08651 340 gTDARFFGAKGIPTVVYGPGELELAHAPDEYVEVKDVEK 378
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
24-365 |
4.80e-49 |
|
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: 169.10 E-value: 4.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 24 DWIADFLAARGVASRRFyDPSGGKANLYARLGPSGGGG-VMLSGHTDVVPV-DGQAWSVPPFSLTERDGRYYGRGSADMK 101
Cdd:cd08011 25 AYIKLLLEDLGYPVELH-EPPEEIYGVVSNIVGGRKGKrLLFNGHYDVVPAgDGEGWTVDPYSGKIKDGKLYGRGSSDMK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 102 GFLACVLAAVDDFLAA--PLRMPLHLAFSYDEE-VGCLGVRSLVDflqASPEKPALCLIGEPTEMQPV-FGHKGKLAMRC 177
Cdd:cd08011 104 GGIAASIIAVARLADAkaPWDLPVVLTFVPDEEtGGRAGTKYLLE---KVRIKPNDVLIGEPSGSDNIrIGEKGLVWVII 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 178 CIEGQACHSAYAPQGVNAIRYAARLINHLDRLGVrlarqqdsrfsppfsTLQVGTIQGGAALNIVPQSCRFDFEIRYLPG 257
Cdd:cd08011 181 EITGKPAHGSLPHRGESAVKAAMKLIERLYELEK---------------TVNPGVIKGGVKVNLVPDYCEFSVDIRLPPG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 258 MRPEAVtealaayarRQLLPEMrrVGSGSDIQFQLLSHYPPLLSDPQSDFARWLAQwCGSDRFSTVAF------GTEGGL 331
Cdd:cd08011 246 ISTDEV---------LSRIIDH--LDSIEEVSFEIKSFYSPTVSNPDSEIVKKTEE-AITEVLGIRPKevisvgASDARF 313
|
330 340 350
....*....|....*....|....*....|....
gi 1396632015 332 FDEMGVATLVCGPGSMAQGHKADEYISIAQTERC 365
Cdd:cd08011 314 YRNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKV 347
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
3-363 |
2.32e-48 |
|
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: 167.68 E-value: 2.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 3 NILAALLAFDTTSRHSNLAMiDWIADFLAARGVASRRFydPSGGKANLYARLGpSGGGGVMLSGHTDVVPV-DGQAWSVP 81
Cdd:cd03891 2 ELAKELIRRPSVTPDDAGAQ-DLIAERLKALGFTCERL--EFGGVKNLWARRG-TGGPHLCFAGHTDVVPPgDLEGWSSD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 82 PFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAF--SYDEE-VGCLGVRSLVDFLQASPEKPALCLIG 158
Cdd:cd03891 78 PFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFliTSDEEgPAIDGTKKVLEWLKARGEKIDYCIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 159 EPT------EMQPVfGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLdrlgvrLARQQD--SRFSPPfSTLQV 230
Cdd:cd03891 158 EPTsekklgDTIKI-GRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAEL------TATVLDegNEFFPP-SSLQI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 231 GTIQGGA-ALNIVPQSCRFDFEIRYlpgmRPEAVTEALAAYARRQLlpemRRVGSGSDIQFQLLSHypPLLSDPQ---SD 306
Cdd:cd03891 230 TNIDVGNgATNVIPGELKAKFNIRF----NDEHTGESLKARIEAIL----DKHGLDYDLEWKLSGE--PFLTKPGklvDA 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 307 FARWLAQWCGSD-RFSTvAFGTEGGLF-DEMGVATLVCGP-GSMAqgHKADEYISIAQTE 363
Cdd:cd03891 300 VSAAIKEVTGITpELST-SGGTSDARFiASYGCPVVEFGLvNATI--HKVNERVSVADLE 356
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
8-365 |
3.08e-46 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 161.29 E-value: 3.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 8 LLAFDTTSRHSnLAMIDWIADFLAARGVASRRFYDPSGGKANLYARLGPSGGGGVMLSGHTDVVPvdgqawsvP--PFSL 85
Cdd:cd05652 8 LVEIPSISGNE-AAVGDFLAEYLESLGFTVEKQPVENKDRFNVYAYPGSSRQPRVLLTSHIDTVP--------PfiPYSI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 86 TERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMP--LHLAFSYDEEVGCLGVRSLVDFLQASPEkpaLCLIGEPTEM 163
Cdd:cd05652 79 SDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEgdLGLLFVVGEETGGDGMKAFNDLGLNTWD---AVIFGEPTEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 164 QPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLGVrlarQQDSRFSPpfSTLQVGTIQGGAALNIVP 243
Cdd:cd05652 156 KLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADL----PSSELLGP--TTLNIGRISGGVAANVVP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 244 QSCRFDFEIRYLPGmrPEAVTEALAAYARRQLLPEmrrvgsgSDIQFQLLSHYPPLLSDpqsdfarwlaqwCGSDRFST- 322
Cdd:cd05652 230 AAAEASVAIRLAAG--PPEVKDIVKEAVAGILTDT-------EDIEVTFTSGYGPVDLD------------CDVDGFETd 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1396632015 323 -VAFGTEGGLFDEMGVATLVcGPGSMAQGHKADEYISIAQTERC 365
Cdd:cd05652 289 vVAYGTDIPYLKGDHKRYLY-GPGSILVAHGPDEAITVSELEEA 331
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
23-254 |
3.89e-44 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 156.78 E-value: 3.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 23 IDWIADFLAARGVASRRFydPSGGKANLYARLGpSGGGGVMLSGHTDVVPV-DGQAWSVPPFSLTERDGRYYGRGSADMK 101
Cdd:PRK13009 25 QDLLAERLEALGFTCERM--DFGDVKNLWARRG-TEGPHLCFAGHTDVVPPgDLEAWTSPPFEPTIRDGMLYGRGAADMK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 102 GFLACVLAAVDDFLAAPLRMPLHLAF---SyDEE-VGCLGVRSLVDFLQASPEKPALCLIGEPT------EMQPVfGHKG 171
Cdd:PRK13009 102 GSLAAFVVAAERFVAAHPDHKGSIAFlitS-DEEgPAINGTVKVLEWLKARGEKIDYCIVGEPTsterlgDVIKN-GRRG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 172 KLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLdrlgvrLARQQD--SRFSPPfSTLQVGTIQGG-AALNIVPQSCRF 248
Cdd:PRK13009 180 SLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAEL------AATEWDegNEFFPP-TSLQITNIDAGtGATNVIPGELEA 252
|
....*.
gi 1396632015 249 DFEIRY 254
Cdd:PRK13009 253 QFNFRF 258
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
26-372 |
9.29e-38 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 139.92 E-value: 9.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 26 IADFLAA----RGVASRRFyDPSGGKANLYARLGPSGGG-GVMLSGHTDVVPVDGqaWSVPPFSLTERDGRYYGRGSADM 100
Cdd:cd08013 31 IATYVAAwlahRGIEAHRI-EGTPGRPSVVGVVRGTGGGkSLMLNGHIDTVTLDG--YDGDPLSGEIADGRVYGRGTLDM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 101 KGFLACVLAAVDDFLAAPLRMPLHLAFSYDEEVGCLGVRSLvdfLQASPEKPAlCLIGEPTEMQPVFGHKGKLAMRCCIE 180
Cdd:cd08013 108 KGGLAACMAALADAKEAGLRGDVILAAVADEEDASLGTQEV---LAAGWRADA-AIVTEPTNLQIIHAHKGFVWFEVDIH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 181 GQACHSAYAPQGVNAIRYAARLINHLDRLGVRL-ARQQDSRFSPPfsTLQVGTIQGGAALNIVPQSCRFDFEIRYLPGMR 259
Cdd:cd08013 184 GRAAHGSRPDLGVDAILKAGYFLVALEEYQQELpERPVDPLLGRA--SVHASLIKGGEEPSSYPARCTLTIERRTIPGET 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 260 PEAVTEALAAYARR--QLLPEMRRVgsgsdiQFQLLSHYPPLLSDPQSDFARWLAQWCGS-----DRFSTVAFGTEGGLF 332
Cdd:cd08013 262 DESVLAELTAILGElaQTVPNFSYR------EPRITLSRPPFEVPKEHPFVQLVAAHAAKvlgeaPQIRSETFWTDAALL 335
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1396632015 333 DEMGVATLVCGPgSMAQGHKADEYISIAQTERCMTMLRQL 372
Cdd:cd08013 336 AEAGIPSVVFGP-SGAGLHAKEEWVDVESIRQLREVLSAV 374
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
9-368 |
1.24e-37 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 139.47 E-value: 1.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 9 LAFDTTSRHS----NLAMIDWIADFLAARGVASRRFydPSGGKANLYARLGpSGGGGVMLSGHTDVVPV-DGQAWSVPPF 83
Cdd:TIGR01246 4 LAKELISRPSvtpnDAGCQDIIAERLEKLGFEIEWM--HFGDTKNLWATRG-TGEPVLAFAGHTDVVPAgPEEQWSSPPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 84 SLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAF--SYDEEVGCL-GVRSLVDFLQASPEKPALCLIGEP 160
Cdd:TIGR01246 81 EPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLliTSDEEGTAIdGTKKVVETLMARDELIDYCIVGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 161 TEMQPV-----FGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLdrlgvrLARQQD--SRFSPPfSTLQVGTI 233
Cdd:TIGR01246 161 SSVKKLgdvikNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAEL------TAIKWDegNEFFPP-TSLQITNI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 234 QGG-AALNIVPQSCRFDFEIRYlpgmRPEAVTEALaayarRQLLPEMRRvGSGSDIQFQLLSHYPPLLSDPQ---SDFAR 309
Cdd:TIGR01246 234 HAGtGANNVIPGELYVQFNLRF----STEVSDEIL-----KQRVEAILD-QHGLDYDLEWSLSGEPFLTNDGkliDKARE 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 310 WLAQWCG-SDRFSTVAFGTEGGLFDEMGVATLVCGPGSmAQGHKADEYISIAQTERCMTM 368
Cdd:TIGR01246 304 AIEETNGiKPELSTGGGTSDGRFIALMGAEVVEFGPVN-ATIHKVNECVSIEDLEKLSDV 362
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
3-372 |
2.56e-36 |
|
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: 135.13 E-value: 2.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 3 NILAALLAFDTTSR-HSNLAmiDWIADFLAARGVASRRFydpsggKANLYARLG------PSggggVMLSGHTDVVPvDG 75
Cdd:cd05651 4 ELLKSLIATPSFSReEHKTA--DLIENYLEQKGIPFKRK------GNNVWAENGhfdegkPT----LLLNSHHDTVK-PN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 76 QAWSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLA-APLRMPLHLAFSYDEEV-GCLGVRSLVDFLQaspeKPA 153
Cdd:cd05651 71 AGWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSeGPLNYNLIYAASAEEEIsGKNGIESLLPHLP----PLD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 154 LCLIGEPTEMQPVFGHKGKLAMRCCIEGQACHSAYaPQGVNAIRYAARLInhldrlgvrlARQQDSRF---SPPFS--TL 228
Cdd:cd05651 147 LAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAAR-NEGDNAIYKALDDI----------QWLRDFRFdkvSPLLGpvKM 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 229 QVGTIQGGAALNIVPQSCRFDFEIRYLPGMRPEAVTEALAAYARRQLLPEMRRVGSgsdiqfqllSHYPPllSDPqsdfa 308
Cdd:cd05651 216 TVTQINAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLKSEIKPRSFRLNS---------SAIPP--DHP----- 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1396632015 309 rwLAQWC--------GSDRFSTVAFgtegglfdeMGVATLVCGPGSMAQGHKADEYISIAQTERCMTMLRQL 372
Cdd:cd05651 280 --IVQAAiaagrtpfGSPTLSDQAL---------MPFPSVKIGPGDSSRSHTADEFIELSEIEEGIDIYIEL 340
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-360 |
6.75e-36 |
|
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: 135.13 E-value: 6.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 5 LAALLAFDTTSRHSNLAMiDWIADFLAARGVASRRF----------------YDPSGGKANLYARLGPSGGGG--VMLSG 66
Cdd:cd03895 3 LQDLVRFPSLRGEEAAAQ-DLVAAALRSRGYTVDRWeidveklkhhpgfspvAVDYAGAPNVVGTHRPRGETGrsLILNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 67 HTDVVPVDGQA-WSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMP--LHLAFSYDEEvgCLGVRSLVD 143
Cdd:cd03895 82 HIDVVPEGPVElWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAadVHFQSVVEEE--CTGNGALAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 144 FLQASpeKPALCLIGEPTEMQPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLGVRLARQQDSrfSP 223
Cdd:cd03895 160 LMRGY--RADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEREWNARKKS--HP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 224 PFS------TLQVGTIQGGAALNIVPQSCRFDFEIRYLPGMRPEA----VTEALAAYARRQllpemrrvgsgsdiqfQLL 293
Cdd:cd03895 236 HFSdhphpiNFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEarreIEECVADAAATD----------------PWL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 294 SHYPPLLS-----------DPQSDFARWLAQ-----WCGSDRFSTVAFGTEGGLFDEMG-VATLVCGPGSMAQgHKADEY 356
Cdd:cd03895 300 SNHPPEVEwngfqaegyvlEPGSDAEQVLAAahqavFGTPPVQSAMTATTDGRFFVLYGdIPALCYGPGSRDA-HGFDES 378
|
....
gi 1396632015 357 ISIA 360
Cdd:cd03895 379 VDLE 382
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
5-364 |
9.86e-36 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 134.17 E-value: 9.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 5 LAALLAFDTTSRHSNLA---MIDWIADFLAARGVasrRFYDPSGGKANLYARLGPSGgggVMLSGHTDVVPvDGQAWSVP 81
Cdd:PRK08737 12 LQALVSFDTRNPPRAITtggIFDYLRAQLPGFQV---EVIDHGAGAVSLYAVRGTPK---YLFNVHLDTVP-DSPHWSAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 82 PFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAaplrmPLHLAFSYDEEVG-CLGVRSlvdFLQASPEKPALcLIGEP 160
Cdd:PRK08737 85 PHVMRRTDDRVIGLGVCDIKGAAAALLAAANAGDG-----DAAFLFSSDEEANdPRCVAA---FLARGIPYEAV-LVAEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 161 TEMQPVFGHKGKLAMRCCIEGQACHSAYAPQ-GVNAIRYAARLINH-LDRLgvrlARQQDSRFSPPFST-LQVGTIQGGA 237
Cdd:PRK08737 156 TMSEAVLAHRGISSVLMRFAGRAGHASGKQDpSASALHQAMRWGGQaLDHV----ESLAHARFGGLTGLrFNIGRVEGGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 238 ALNIVPQSCRFDFEIRYLPGMRPEAVTEALAAYARRQLLPEMRRVGSGSdiqfqllshyPPLLSDPQSDF----ARWLAQ 313
Cdd:PRK08737 232 KANMIAPAAELRFGFRPLPSMDVDGLLATFAGFAEPAAATFEETFRGPS----------LPSGDIARAEErrlaARDVAD 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1396632015 314 WCGSDRFSTVAFGTEGGLFDEMGVATLVCGPGSMAQGHKADEYISIAQTER 364
Cdd:PRK08737 302 ALDLPIGNAVDFWTEASLFSAAGYTALVYGPGDIAQAHTADEFVTLDQLQR 352
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
4-359 |
6.47e-34 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 129.23 E-value: 6.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 4 ILAALLAFDTTSRHSnLAMIDWIADFLAARGVASRRfyDP-SGGKANLYARLGpSGGGGVMLSGHTDVV-PVDGQAWSVP 81
Cdd:PRK08588 7 ILADIVKINSVNDNE-IEVANYLQDLFAKHGIESKI--VKvNDGRANLVAEIG-SGSPVLALSGHMDVVaAGDVDKWTYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 82 PFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLrmPLH-----LAfSYDEEVGCLGVRSLV-----DFLQAspek 151
Cdd:PRK08588 83 PFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQ--LLNgtirlLA-TAGEEVGELGAKQLTekgyaDDLDA---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 152 palCLIGEPTEMQPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLgvrlaRQQDSRFSPPFSTLQ-- 229
Cdd:PRK08588 156 ---LIIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEY-----FDSIKKHNPYLGGLThv 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 230 VGTIQGGAALNIVPQSCRFDFEIRYLPGMRPEAVTEALAAYarrqllpeMRRVGS--GSDIQFQLLSHYPPLLSDPQSDF 307
Cdd:PRK08588 228 VTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEI--------INEVNQngAAQLSLDIYSNHRPVASDKDSKL 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1396632015 308 ARwLAQWCGSDRF------STVAFGTEGGLF----DEMGVAtlVCGPGSMAQGHKADEYISI 359
Cdd:PRK08588 300 VQ-LAKDVAKSYVgqdiplSAIPGATDASSFlkkkPDFPVI--IFGPGNNLTAHQVDEYVEK 358
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
5-273 |
7.47e-31 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 122.03 E-value: 7.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 5 LAALLAFDTTsRHSNLAMIDWIADFLAARGVASRRFY--------DPSGGKA--------NLYARLGPSGGGG--VMLSG 66
Cdd:PRK06837 26 TQDLVRFPST-RGAEAPCQDFLARAFRERGYEVDRWSidpddlksHPGAGPVeidysgapNVVGTYRPAGKTGrsLILQG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 67 HTDVVPVdGQA--WSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRM--PLHLAFSYDEEvgCLGVRSLV 142
Cdd:PRK06837 105 HIDVVPE-GPLdlWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPaaRVHFQSVIEEE--STGNGALS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 143 DFLQASpeKPALCLIGEPTEMQPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLGVRLARQQDSRfs 222
Cdd:PRK06837 182 TLQRGY--RADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRELEAEWNARKASD-- 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1396632015 223 PPFST------LQVGTIQGGAALNIVPQSCRFDFEIRYLPGMRPEAV----TEALAAYARR 273
Cdd:PRK06837 258 PHFEDvphpinFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAADAqaeiEACLAAAARD 318
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
19-361 |
4.56e-30 |
|
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: 118.46 E-value: 4.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 19 NLAMIDWIADFLAAR----GVASRRfYDPSGGKANLYARLGPSGGGGVMLSGHTDVVPVDGQAWSVPpfsLTERDGRYYG 94
Cdd:cd03885 17 DKEGVDRVAELLAEElealGFTVER-RPLGEFGDHLIATFKGTGGKRVLLIGHMDTVFPEGTLAFRP---FTVDGDRAYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 95 RGSADMKGFLACVLAAVDDFLAAPLR--MPLHLAFSYDEEVGCLGVRSLvdfLQASPEKPALCLIGEPT--EMQPVFGHK 170
Cdd:cd03885 93 PGVADMKGGLVVILHALKALKAAGGRdyLPITVLLNSDEEIGSPGSREL---IEEEAKGADYVLVFEPAraDGNLVTARK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 171 GKLAMRCCIEGQACHSAYAPQ-GVNAIRYAARLINHLDRLGvRLARQqdsrfsppfSTLQVGTIQGGAALNIVPQSCRFD 249
Cdd:cd03885 170 GIGRFRLTVKGRAAHAGNAPEkGRSAIYELAHQVLALHALT-DPEKG---------TTVNVGVISGGTRVNVVPDHAEAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 250 FEIRYLPGMRPEAVTEALAAYARRQLLPEMRrvgsgsdIQFQLLSHYPPLLSDPQS----DFARWLAQWCG-SDRFSTVA 324
Cdd:cd03885 240 VDVRFATAEEADRVEEALRAIVATTLVPGTS-------VELTGGLNRPPMEETPASrrllARAQEIAAELGlTLDWEATG 312
|
330 340 350
....*....|....*....|....*....|....*...
gi 1396632015 325 FGTEGGLFDEMGVATLvCGPGSMAQG-HKADEYISIAQ 361
Cdd:cd03885 313 GGSDANFTAALGVPTL-DGLGPVGGGaHTEDEYLELDS 349
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
4-267 |
1.50e-29 |
|
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: 118.23 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 4 ILAALLAFDTTSRHSNL----AMIDWIADFLAARGVASRRFYDPSG-GKANLYARLGPSGG--GGVMLSGHTDVVPVDGQ 76
Cdd:cd05675 3 LLQELIRIDTTNSGDGTgsetRAAEVLAARLAEAGIQTEIFVVESHpGRANLVARIGGTDPsaGPLLLLGHIDVVPADAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 77 AWSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAA--PLRMPLHLAFSYDEEV-GCLGVRSLVDFLQASPEKPA 153
Cdd:cd05675 83 DWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREgfKPKRDLVFAFVADEEAgGENGAKWLVDNHPELFDGAT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 154 LCL---------IGEPTEMQPV-FGHKGKLAMRCCIEGQACHSAyAPQGVNAIryaARLINHLDRLG-----VRL----- 213
Cdd:cd05675 163 FALneggggslpVGKGRRLYPIqVAEKGIAWMKLTVRGRAGHGS-RPTDDNAI---TRLAEALRRLGahnfpVRLtdeta 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 214 -ARQQDSRFSPPFSTLQVGT------------------------------IQGGAALNIVPQSCRFDFEIRYLPGMRPEA 262
Cdd:cd05675 239 yFAQMAELAGGEGGALMLTAvpvldpalaklgpsapllnamlrntasptmLDAGYATNVLPGRATAEVDCRILPGQSEEE 318
|
....*
gi 1396632015 263 VTEAL 267
Cdd:cd05675 319 VLDTL 323
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
1-371 |
8.81e-29 |
|
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: 114.85 E-value: 8.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 1 MNNILAALLAFDTTSRHSNlAMIDWIADFLaaRGVAS---RRFYDpsggkaNLYARLGPSGGGGVMLSGHTDVVPVDGqa 77
Cdd:cd05647 1 PIELTAALVDIPSVSGNEK-PIADEIEAAL--RTLPHlevIRDGN------TVVARTERGLASRVILAGHLDTVPVAG-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 78 wSVPpfSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAFsYDEEVGCLGVRSLVDFLQASPEKPA--LC 155
Cdd:cd05647 70 -NLP--SRVEEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLTLIF-YDCEEVAAELNGLGRLAEEHPEWLAadFA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 156 LIGEPTEMQPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLinhLDRLGVRLARQQDSRFSPPFSTLQVGTIQG 235
Cdd:cd05647 146 VLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPI---LARLAAYEPRTVNIDGLTYREGLNAVFISG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 236 GAALNIVPQSCRFDFEIRYLPGMRPEavtEALAayarrqllpEMRRVGSGSDIQFQLLSHYP---PLLSDP-QSDFARWL 311
Cdd:cd05647 223 GVAGNVIPDEARVNLNYRFAPDKSLA---EAIA---------HVREVFEGLGYEIEVTDLSPgalPGLDHPvARDLIEAV 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1396632015 312 AQ-------WCGSDRFStvafgtegglfdEMGVATLVCGPGSMAQGHKADEYISIAQTERCMTMLRQ 371
Cdd:cd05647 291 GGkvrakygWTDVARFS------------ALGIPAVNFGPGDPLLAHKRDEQVPVEQITACAAILRR 345
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
8-374 |
1.19e-28 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 114.76 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 8 LLAFDTTSRHsNLAMIDWIADFLAARGVASRRfyDPSGgkaNLYARLGPSGGGG---VMLSGHTDVVPV---DGqawsVP 81
Cdd:COG2195 12 YVKIPTPSDH-EEALADYLVEELKELGLEVEE--DEAG---NVIATLPATPGYNvptIGLQAHMDTVPQfpgDG----IK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 82 PFsltERDGRYYGRGS----ADMKGFLACVLAAV----DDFLAAPlrmPLHLAFSYDEEVGCLGVRSL-VDFLQAspeKP 152
Cdd:COG2195 82 PQ---IDGGLITADGTttlgADDKAGVAAILAALeylkEPEIPHG---PIEVLFTPDEEIGLRGAKALdVSKLGA---DF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 153 ALCLIGEPTemqpvfghkGKLAMRCC--------IEGQACHSAYAP-QGVNAIRYAARLINHLDRLGVrlarqqdsrfsP 223
Cdd:COG2195 153 AYTLDGGEE---------GELEYECAgaadakitIKGKGGHSGDAKeKMINAIKLAARFLAALPLGRI-----------P 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 224 PFSTLQVGTIQGGAALNIVPQSCRFDFEIRYLpgmRPEAVtEALAAYARRQLLPEMRRVGSGSdIQFQLLSHYPPLLSDP 303
Cdd:COG2195 213 EETEGNEGFIHGGSATNAIPREAEAVYIIRDH---DREKL-EARKAELEEAFEEENAKYGVGV-VEVEIEDQYPNWKPEP 287
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1396632015 304 QS---DFARWLAQWCGSDrFSTVAF--GTEGGLFDEMGVATLVCGPGsmaqGHKA---DEYISIAQTERCMTMLRQLCA 374
Cdd:COG2195 288 DSpivDLAKEAYEELGIE-PKIKPIrgGLDGGILSFKGLPTPNLGPG----GHNFhspDERVSIESMEKAWELLVEILK 361
|
|
| PRK06915 |
PRK06915 |
peptidase; |
46-359 |
1.23e-28 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 115.56 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 46 GKANLYARLGPSGGG-GVMLSGHTDVVPV-DGQAWSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAA--PLRM 121
Cdd:PRK06915 79 DSPNIVATLKGSGGGkSMILNGHIDVVPEgDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESgiELKG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 122 PLHLAFSYDEEVGclGVRSLVDFLQASPEKPAlcLIGEPTEMQPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAAR 201
Cdd:PRK06915 159 DVIFQSVIEEESG--GAGTLAAILRGYKADGA--IIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMF 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 202 LINHLDRL-GVRLARQQDSRFS--PPFSTLQVGTIQGGAALNIVPQSCRFDFEIRYLPGMRPEAVTEALAAYArrQLLPE 278
Cdd:PRK06915 235 VIDHLRKLeEKRNDRITDPLYKgiPIPIPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWI--AELND 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 279 MrrvgsgsDIQFQllsHYP-------------------PLLSDPQSDFARWLAQ--------WcgsdrfstvafGTEGGL 331
Cdd:PRK06915 313 V-------DEWFV---EHPvevewfgarwvpgeleenhPLMTTLEHNFVEIEGNkpiieaspW-----------GTDGGL 371
|
330 340
....*....|....*....|....*....
gi 1396632015 332 FDEMG-VATLVCGPGSMAQGHKADEYISI 359
Cdd:PRK06915 372 LTQIAgVPTIVFGPGETKVAHYPNEYIEV 400
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
3-364 |
7.66e-28 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 112.16 E-value: 7.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 3 NILAALLAFDTTSRHSNlAMIDWIADFLAARGvasrrfYDPSGGKANLYARLGPSGGGGVMLSGHTDVVPVdgqawSVPP 82
Cdd:PRK08652 6 ELLKQLVKIPSPSGQED-EIALHIMEFLESLG------YDVHIESDGEVINIVVNSKAELFVEVHYDTVPV-----RAEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 83 FsltERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAFSYDEEVGCLGVRSLvdflqASPEKPALCLIGEPTE 162
Cdd:PRK08652 74 F---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSDEEEGGRGSALF-----AERYRPKMAIVLEPTD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 163 MQPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLGVRLARqqdsRFSPPFStLQVgtIQGGAALNIV 242
Cdd:PRK08652 146 LKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGK----YFDPHIG-IQE--IIGGSPEYSI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 243 PQSCRFDFEIRYLPGMRPEAVtealaayarrqlLPEMRRVGSGSDIQFQLLSHYPPLLSDPQSDFARwLAQWCGSDRFST 322
Cdd:PRK08652 219 PALCRLRLDARIPPEVEVEDV------------LDEIDPILDEYTVKYEYTEIWDGFELDEDEEIVQ-LLEKAMKEVGLE 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1396632015 323 VAFG-----TEGGLFDEMGVATLVCGPGSMAQGHKADEYISIAQTER 364
Cdd:PRK08652 286 PEFTvmrswTDAINFRYNGTKTVVWGPGELDLCHTKFERIDVREVEK 332
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
167-277 |
1.88e-27 |
|
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: 104.35 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 167 FGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDrlgvrlARQQDSRFSPPFSTLQVGTIQGGAALNIVPQSC 246
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELP------AEYGDIGFDFPRTTLNITGIEGGTATNVIPAEA 74
|
90 100 110
....*....|....*....|....*....|.
gi 1396632015 247 RFDFEIRYLPGMRPEAVTEALAAYARRQLLP 277
Cdd:pfam07687 75 EAKFDIRLLPGEDLEELLEEIEAILEKELPE 105
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
5-369 |
3.77e-27 |
|
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: 111.65 E-value: 3.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 5 LAALLAFDTTSRHSNLA-----MIDWIADFLAARGvASRRFYDPSGGKANLYARLGPSGGGG-VMLSGHTDVVPVDGQA- 77
Cdd:cd03893 4 LAELVAIPSVSAQPDRReelrrAAEWLADLLRRLG-FTVEIVDTSNGAPVVFAEFPGAPGAPtVLLYGHYDVQPAGDEDg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 78 WSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAFSYD--EEVGClgvRSLVDFLQASPE--KPA 153
Cdd:cd03893 83 WDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEgeEESGS---PSLDQLVEAHRDllAAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 154 LCLIGEPTEM---QP--VFGHKGKLAMRCCIEG--QACHSAYApQGV--NAIRYAARLINHL-DRLG------------- 210
Cdd:cd03893 160 AIVISDSTWVgqeQPtlTYGLRGNANFDVEVKGldHDLHSGLY-GGVvpDPMTALAQLLASLrDETGrilvpglydavre 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 211 -----VRLARQQDSRFSPPFS-------------TLQVGTIQGG----AALNIVPQSCRFDFEIRYLPGMRPEAVTEALA 268
Cdd:cd03893 239 lpeeeFRLDAGVLEEVEIIGGttgsvaerlwtrpALTVLGIDGGfpgeGSKTVIPPRARAKISIRLVPGQDPEEASRLLE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 269 AYARRQLLP----EMRRVGSGSdiqfqllshypPLLSDPQSDFARWLAqwcgsdRFSTVAFGT------EGG------LF 332
Cdd:cd03893 319 AHLEKHAPSgakvTVSYVEGGM-----------PWRSDPSDPAYQAAK------DALRTAYGVeppltrEGGsipfisVL 381
|
410 420 430
....*....|....*....|....*....|....*....
gi 1396632015 333 DEM-GVATLVCGPG-SMAQGHKADEYISIAQTERCMTML 369
Cdd:cd03893 382 QEFpQAPVLLIGVGdPDDNAHSPNESLRLGNYKEGTQAE 420
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
58-355 |
3.09e-25 |
|
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: 105.71 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 58 GGGGVMLSGHTDVVPvDGQAWSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDF--LAAPLRMPLHLAFSYDEEVGc 135
Cdd:cd02697 72 GGRTVALNAHGDVVP-PGDGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALesLGAPLRGAVELHFTYDEEFG- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 136 lGVRSLVDFLQASPEKPALcLIGEPTEMQPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHL--DRLGVRL 213
Cdd:cd02697 150 -GELGPGWLLRQGLTKPDL-LIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALyaLNAQYRQ 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 214 ARQQDSRFSPPFstLQVGTIQGGAALNIVPQSCRFDFEIRYLPGMRPEAVTEALaayarRQLLPEMRRVGSGSDIQFQLL 293
Cdd:cd02697 228 VSSQVEGITHPY--LNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEI-----RRVIADAAASMPGISVDIRRL 300
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1396632015 294 SHYPPLLSDPQSDFARWLAQWCGSDRF--STVAFG----TEGGLFDEMGVATLVCGPGSM----AQGHKADE 355
Cdd:cd02697 301 LLANSMRPLPGNAPLVEAIQTHGEAVFgePVPAMGtplyTDVRLYAEAGIPGVIYGAGPRtvleSHAKRADE 372
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
66-368 |
4.98e-25 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 105.02 E-value: 4.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 66 GHTDVVPV-DGQAWSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDF--LAAPLRMPLHLAFSYDEEVgCLGV--RS 140
Cdd:PRK13004 76 AHIDTVGIgDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIkdLGLDDEYTLYVTGTVQEED-CDGLcwRY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 141 LVDflqASPEKPALCLIGEPTEMQPVFGHKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLGVRLARQQ--- 217
Cdd:PRK13004 155 IIE---EDKIKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNLKEDPflg 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 218 -------DSRFSPPfstlqvgtiqgGAalNIVPQSCRFDF---------------EIRYLPGMRPEAVTEALAAYARRQ- 274
Cdd:PRK13004 232 kgtltvsDIFSTSP-----------SR--CAVPDSCAISIdrrltvgetwesvlaEIRALPAVKKANAKVSMYNYDRPSy 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 275 --------------LLPEMRRVGSGSDIQFQLLSHYPPLLSdpqsdfarwlaQWCgsdrFSTVAFGTEGglfdEMGVATL 340
Cdd:PRK13004 299 tglvyptecyfptwLYPEDHEFVKAAVEAYKGLFGKAPEVD-----------KWT----FSTNGVSIAG----RAGIPTI 359
|
330 340
....*....|....*....|....*...
gi 1396632015 341 VCGPGSMAQGHKADEYISIAQTERCMTM 368
Cdd:PRK13004 360 GFGPGKEPLAHAPNEYTWKEQLVKAAAM 387
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
42-368 |
1.90e-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. 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: 103.27 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 42 DPSGgkaNLYARLGpSGGGGVMLSGHTDVVPV-DGQAWSVPPFSLTERDGRYYGRGSADMKGFLACVLAAV----DDFLA 116
Cdd:cd05649 39 DPMG---NVIGYIG-GGKKKILFDGHIDTVGIgNIDNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAkimkDLGLR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 117 aPLRMPLHLAFSYDEEVgCLGV--RSLVdflQASPEKPALCLIGEPTEMQPVFGHKGKLAMRCCIEGQACHSAYAPQGVN 194
Cdd:cd05649 115 -DFAYTILVAGTVQEED-CDGVcwQYIS---KADKIKPDFVVSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 195 AIRYAARLINHLDRLGvrlARQQDSRFSPPfSTLQVGTIQGGA-ALNIVPQSCRFDFEIRYLPGMRPEAVTEALAAYARR 273
Cdd:cd05649 190 AVYKMADIIQDIRQLN---PNFPEAPFLGR-GTLTVTDIFSTSpSRCAVPDSCRISIDRRLTVGETWEGCLEEIRALPAV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 274 QLLPEMRRVG-------SGSDIQFQLLSHYPPLLSDPQSDFARWL--------AQWCGSDRFStvaFGTEG-GLFDEMGV 337
Cdd:cd05649 266 KKYGDDVAVSmynydrpSYTGEVYESERYFPTWLLPEDHELVKALleaykalfGARPLIDKWT---FSTNGvSIMGRAGI 342
|
330 340 350
....*....|....*....|....*....|.
gi 1396632015 338 ATLVCGPGSMAQGHKADEYISIAQTERCMTM 368
Cdd:cd05649 343 PCIGFGPGAENQAHAPNEYTWKEDLVRCAAG 373
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
39-370 |
7.04e-24 |
|
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: 100.89 E-value: 7.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 39 RFYDPSGGKANLYARL--------------------GPSGGGG--VMLSGHTDVVPvdGQawsVPPfslTERDGRYYGRG 96
Cdd:cd05653 12 SIYSPSGEEARAAKFLeeimkelgleawvdeagnavGGAGSGPpdVLLLGHIDTVP--GE---IPV---RVEGGVLYGRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 97 SADMKGFLACVLAAVDDfLAAPLRMPLHLAFSYDEEVGCLGVRSLVdflqASPEKPALCLIGEPTEMQPV-FGHKGKLAM 175
Cdd:cd05653 84 AVDAKGPLAAMILAASA-LNEELGARVVVAGLVDEEGSSKGARELV----RRGPRPDYIIIGEPSGWDGItLGYRGSLLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 176 RCCIEGQACHSAyapqgvNAIRYAA-RLINHLDRlgVRLARQQDSRFSPPFSTLQVGTIQGGAALNIVPQSCRFDFEIRY 254
Cdd:cd05653 159 KIRCEGRSGHSS------SPERNAAeDLIKKWLE--VKKWAEGYNVGGRDFDSVVPTLIKGGESSNGLPQRAEATIDLRL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 255 LPGMRPEAvtealaayARRQLLPEMrrvgSGSDIQFqlLSHYPPLLSDPQSDFARWLAQwcgsdrfstvAFGTEGG---- 330
Cdd:cd05653 231 PPRLSPEE--------AIALATALL----PTCELEF--IDDTEPVKVSKNNPLARAFRR----------AIRKQGGkprl 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1396632015 331 -----------LFDEMGVATLVCGPGSMAQGHKADEYISIAQTERCMTMLR 370
Cdd:cd05653 287 krktgtsdmnvLAPLWTVPIVAYGPGDSTLDHTPNEHIELAEIERAAAVLK 337
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
3-361 |
3.41e-23 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 100.11 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 3 NILAALLAFDTTS---RHSNLAMiDWIADFLAARGVASRRF--YDpsgGKANLYARL---GPSGGGGVMLSGHTDVVPVD 74
Cdd:PRK08596 17 ELLKTLVRFETPAppaRNTNEAQ-EFIAEFLRKLGFSVDKWdvYP---NDPNVVGVKkgtESDAYKSLIINGHMDVAEVS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 75 G-QAWSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAFS--YDEEVGCLGVRSLV------DFl 145
Cdd:PRK08596 93 AdEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQsvIGEEVGEAGTLQCCergydaDF- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 146 qaspekpALCLIGEPTEMQ--------------PVFGHKGklaMRccieGQACHSAYAPQGVNAIRYAARLINHLDRLGV 211
Cdd:PRK08596 172 -------AVVVDTSDLHMQgqggvitgwitvksPQTFHDG---TR----RQMIHAGGGLFGASAIEKMMKIIQSLQELER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 212 RLARQQDSR-FSPPFSTLQVGTIQGGAALNIVPQSCRFDFEIRYLPGMRPEAVTEALAAYARR--QLLPEMR------RV 282
Cdd:PRK08596 238 HWAVMKSYPgFPPGTNTINPAVIEGGRHAAFIADECRLWITVHFYPNETYEQVIKEIEEYIGKvaAADPWLRenppqfKW 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 283 GSGSDIQ--------FQLLSHYP---PLLSDPQSDFARWLAqwcgSDRFSTVafgTEGGLFDEMGVATLVCGPGSMAQGH 351
Cdd:PRK08596 318 GGESMIEdrgeifpsLEIDSEHPavkTLSSAHESVLSKNAI----LDMSTTV---TDGGWFAEFGIPAVIYGPGTLEEAH 390
|
410
....*....|
gi 1396632015 352 KADEYISIAQ 361
Cdd:PRK08596 391 SVNEKVEIEQ 400
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
18-360 |
8.63e-23 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 99.06 E-value: 8.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 18 SNLAMIDWIADFLAARGVASRRFYDPsggKANLYARL-GPSGGGGVMLSGHTDVVPVdGQAWSVPPFSLTERDGRYYGRG 96
Cdd:PRK13013 45 ARLAPRGFEVELIRAEGAPGDSETYP---RWNLVARRqGARDGDCVHFNSHHDVVEV-GHGWTRDPFGGEVKDGRIYGRG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 97 SADMKGFLACVLAAVDDFLAAPLRMP--LHLAFSYDEEVGCL-GVRSLVDFLQASPEKPALCLIGEPTEMQPV-FGHKGK 172
Cdd:PRK13013 121 ACDMKGGLAASIIAAEAFLAVYPDFAgsIEISGTADEESGGFgGVAYLAEQGRFSPDRVQHVIIPEPLNKDRIcLGHRGV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 173 LAMRCCIEGQACHSAYAPQGVNAIRYAARLINHL-DRLGVRLARQQDSRFSPP----FSTLQVGTIQGGAALN------- 240
Cdd:PRK13013 201 WWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEIeERLFPLLATRRTAMPVVPegarQSTLNINSIHGGEPEQdpdytgl 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 241 ---IVPQSCRFDFEIRYLPGMRPEAVTEALAAyarrqLLPEMRRVGSGSDIQFQLLSHYPPLLSDPQSDFARWLAQWCGS 317
Cdd:PRK13013 281 papCVADRCRIVIDRRFLIEEDLDEVKAEITA-----LLERLKRARPGFAYEIRDLFEVLPTMTDRDAPVVRSVAAAIER 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1396632015 318 DRFSTVAFGTEGGLFDEMGVA-------TLVCGPGSMAQGHKADEYISIA 360
Cdd:PRK13013 356 VLGRQADYVVSPGTYDQKHIDrigklknCIAYGPGILDLAHQPDEWVGIA 405
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
4-143 |
1.45e-22 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 98.39 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 4 ILAALLAFDTTSRHSNL-----AMIDWIADFLAARGVASRrFYDPSGGKANLYARL--GPSGGGGVMLSGHTDVVPVDGQ 76
Cdd:PRK07906 4 LCSELIRIDTTNTGDGTgkgerEAAEYVAEKLAEVGLEPT-YLESAPGRANVVARLpgADPSRPALLVHGHLDVVPAEAA 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 77 AWSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMP--LHLAFSYDEEV-GCLGVRSLVD 143
Cdd:PRK07906 83 DWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPrdLVFAFVADEEAgGTYGAHWLVD 152
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
42-362 |
1.17e-21 |
|
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: 95.22 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 42 DPSGG-KANLYARLGPSGGGGVMLSGHTDVVPV-DGQAWSVPPFSLTERDGRYYGRGSAD-MKGFLACVLAAVDDF-LAA 117
Cdd:cd05650 51 DERGIiRPNIVAKIPGGNDKTLWIISHLDTVPPgDLSLWETDPWEPVVKDGKIYGRGVEDnQQGIVSSLLALKAIIkNGI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 118 PLRMPLHLAFSYDEEVGC-LGVRSLVD----FlqaspEKPALCLI---GEPTEMQPVFGHKGKLAMRCCIEGQACHSAYA 189
Cdd:cd05650 131 TPKYNFGLLFVADEEDGSeYGIQYLLNkfdlF-----KKDDLIIVpdfGTEDGEFIEIAEKSILWIKVNVKGKQCHASTP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 190 PQGVNAIRYAARLINHLDRLGVRLARQQDSRFSPPFSTLQVGTIQGGAA-LNIVPQSCRFDFEIRYLPGMRPEAVTEALa 268
Cdd:cd05650 206 ENGINAFVAASNFALELDELLHEKFDEKDDLFNPPYSTFEPTKKEANVPnVNTIPGYDVFYFDCRVLPTYKLDEVLKFV- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 269 ayarRQLLPEMRRvGSGSDIQFQLL-SHYPPLLSDPQSDFARWLAQWCGSDRFST-----VAFGTEGGLFDEMGVATLVC 342
Cdd:cd05650 285 ----NKIISDFEN-SYGAGITYEIVqKEQAPPATPEDSEIVVRLSKAIKKVRGREakligIGGGTVAAFLRKKGYPAVVW 359
|
330 340
....*....|....*....|
gi 1396632015 343 GPGsMAQGHKADEYISIAQT 362
Cdd:cd05650 360 STL-DETAHQPNEYIRISHI 378
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
62-306 |
1.57e-21 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 95.78 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 62 VMLSGHTDVVPVDG---QAWSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAA---PLRMpLHLAFSYDEEVGC 135
Cdd:PRK08262 114 IVLMAHQDVVPVAPgteGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQgfqPRRT-IYLAFGHDEEVGG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 136 LGVRSLVDFLQASPEKPALCL-------------IGEPTEMQPVfGHKGKLAMRCCIEGQACHSAyAPQGVNAIRYAARL 202
Cdd:PRK08262 193 LGARAIAELLKERGVRLAFVLdeggaitegvlpgVKKPVALIGV-AEKGYATLELTARATGGHSS-MPPRQTAIGRLARA 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 203 INHLDR-----------------------LGVRLARQQDSRFSPPF---------------STLQVGTIQGGAALNIVPQ 244
Cdd:PRK08262 271 LTRLEDnplpmrlrgpvaemfdtlapemsFAQRVVLANLWLFEPLLlrvlakspetaamlrTTTAPTMLKGSPKDNVLPQ 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1396632015 245 SCRFDFEIRYLPGMRPEAVTEALaayarrqllpemRRVGSGSDIQFQLLSH--YPPLLSDPQSD 306
Cdd:PRK08262 351 RATATVNFRILPGDSVESVLAHV------------RRAVADDRVEIEVLGGnsEPSPVSSTDSA 402
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
49-162 |
7.35e-21 |
|
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 89.41 E-value: 7.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 49 NLYARLGPSGGGG-VMLSGHTDVVPV-DGQAWSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAP--LRMPLH 124
Cdd:cd18669 1 NVIARYGGGGGGKrVLLGAHIDVVPAgEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGfkLKGTVV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1396632015 125 LAFSYDEEVGCLGVR-SLVDFLQASPEKPALCLIGEPTE 162
Cdd:cd18669 81 VAFTPDEEVGSGAGKgLLSKDALEEDLKVDYLFVGDATP 119
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
24-272 |
1.56e-19 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 89.14 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 24 DWIADFLAARGVASRRFYD------PSGGKANLYARLgPSGGGGVMLS--GHTDVVPV-DGQAWSVPPFSLTERDGRYYG 94
Cdd:PRK13983 34 EYLESLLKEYGFDEVERYDapdprvIEGVRPNIVAKI-PGGDGKRTLWiiSHMDVVPPgDLSLWETDPFKPVVKDGKIYG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 95 RGSADMKGFLACVLAAVDDFLAAPLRMP--LHLAFSYDEEVGCL-GVRSLVDFLQASPEKPALCLI---GEPTEMQPVFG 168
Cdd:PRK13983 113 RGSEDNGQGIVSSLLALKALMDLGIRPKynLGLAFVSDEETGSKyGIQYLLKKHPELFKKDDLILVpdaGNPDGSFIEIA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 169 HKGKLAMRCCIEGQACHSAYAPQGVNAIRYAARLINHLDRLGVRLARQQDSRFSPPFSTLQVgTIQGG--AALNIVPQSC 246
Cdd:PRK13983 193 EKSILWLKFTVKGKQCHASTPENGINAHRAAADFALELDEALHEKFNAKDPLFDPPYSTFEP-TKKEAnvDNINTIPGRD 271
|
250 260
....*....|....*....|....*.
gi 1396632015 247 RFDFEIRYLPGMRPEAVTEALAAYAR 272
Cdd:PRK13983 272 VFYFDCRVLPDYDLDEVLKDIKEIAD 297
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
5-206 |
3.97e-19 |
|
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: 88.17 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 5 LAALLAFDTTSRHSN--LAMIDWIADFLAARGVASRRFYDPsgGKANLYARLGPSGGGGVMLSGHTDVVPVDG-QAWSVP 81
Cdd:cd05681 5 LRDLLKIPSVSAQGRgiPETADFLKEFLRRLGAEVEIFETD--GNPIVYAEFNSGDAKTLLFYNHYDVQPAEPlELWTSD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 82 PFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAFSYD--EEVGClgvRSLVDFLQASPEKPA--LCLI 157
Cdd:cd05681 83 PFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEgeEEVGS---PNLEKFVAEHADLLKadGCIW 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1396632015 158 ---GEPTEMQP--VFGHKGKLA--MRCCIEGQACHSAYAPQGVNAIRYAARLINHL 206
Cdd:cd05681 160 eggGKNPKGRPqiSLGVKGIVYveLRVKTADFDLHSSYGAIVENPAWRLVQALNSL 215
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
5-150 |
1.86e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 86.50 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 5 LAALLAFDTTS-----RHSNLAMIDWIADFLAARGVASRRFYDPSGGKANLYARLGPSGGGGVMLSGHTDVVPV-DGQAW 78
Cdd:PRK07907 24 LEELVRIPSVAadpfrREEVARSAEWVADLLREAGFDDVRVVSADGAPAVIGTRPAPPGAPTVLLYAHHDVQPPgDPDAW 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1396632015 79 SVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPlrmPLHLAFSYD--EEVGClgvRSLVDFLQASPE 150
Cdd:PRK07907 104 DSPPFELTERDGRLYGRGAADDKGGIAMHLAALRALGGDL---PVGVTVFVEgeEEMGS---PSLERLLAEHPD 171
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
25-373 |
1.94e-18 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 85.39 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 25 WIADFLAARGVASrrFYDPSGgkaNLYARLGpSGGGGVMLSGHTDVVPVDgqawsVPpfsLTERDGRYYGRGSADMKGFL 104
Cdd:PRK04443 31 FLVEFMESHGREA--WVDEAG---NARGPAG-DGPPLVLLLGHIDTVPGD-----IP---VRVEDGVLWGRGSVDAKGPL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 105 ACVLAAVDDfLAAPLRMPLHLAFSYDEEVGCLGVRSLVdflqASPEKPALCLIGEPTEMQPV-FGHKGKLAMRCCIEGQA 183
Cdd:PRK04443 97 AAFAAAAAR-LEALVRARVSFVGAVEEEAPSSGGARLV----ADRERPDAVIIGEPSGWDGItLGYKGRLLVTYVATSES 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 184 CHSAYapQGVNAIRYAARLINhldrlGVRLARQQDSRFSPPFSTLQvGTIQggaALNIVP----QSCRFDFEIRYLPGMR 259
Cdd:PRK04443 172 FHSAG--PEPNAAEDAIEWWL-----AVEAWFEANDGRERVFDQVT-PKLV---DFDSSSdgltVEAEMTVGLRLPPGLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 260 PEAVTEALAAYArrqllpemrrvgSGSDIQFQllSHYPPLLSDPQSDFARwlaqwcgsdRFsTVAFGTEGG--------- 330
Cdd:PRK04443 241 PEEAREILDALL------------PTGTVTFT--GAVPAYMVSKRTPLAR---------AF-RVAIREAGGtprlkrktg 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1396632015 331 ------LFDEMGVATLVCGPGSMAQGHKADEYISIAQTERCMTMLRQLC 373
Cdd:PRK04443 297 tsdmnvVAPAWGCPMVAYGPGDSDLDHTPDEHLPLAEYLRAIAVLTDVL 345
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
49-162 |
2.93e-18 |
|
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: 82.09 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 49 NLYARLGPSGGGG-VMLSGHTDVVPVDGQAWSVPPFS-LTERDGRYYGRGSADMKGFLACVLAAVDDFLAAP--LRMPLH 124
Cdd:cd03873 1 NLIARLGGGEGGKsVALGAHLDVVPAGEGDNRDPPFAeDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGfkPKGTIV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1396632015 125 LAFSYDEEVGC-LGVRSLVDFLQASPEKPALCLIGEPTE 162
Cdd:cd03873 81 VAFTADEEVGSgGGKGLLSKFLLAEDLKVDAAFVIDATA 119
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
31-374 |
1.01e-17 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 83.68 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 31 AARGVASRRFYDPSG-------GKANLYARLGPSGGG-GVMLSGHTDVVPVDGQAWSVppfslTERDGRYYGRGSADMKG 102
Cdd:cd03896 18 GARADLVAEWMADLGlgdverdGRGNVVGRLRGTGGGpALLFSAHLDTVFPGDTPATV-----RHEGGRIYGPGIGDNKG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 103 FLACVLAAVDDFLAA--PLRMPLHLAFSYDEE-VGCL-GVRSLvdfLQASPEKPALCLIGEPTEMQPVFGHKGKLAMRCC 178
Cdd:cd03896 93 SLACLLAMARAMKEAgaALKGDVVFAANVGEEgLGDLrGARYL---LSAHGARLDYFVVAEGTDGVPHTGAVGSKRFRIT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 179 IEGQACHSAYAPQGVNAIRYAARLINHLDRLGVRlarqqdsrfSPPFSTLQVGTIQGGAALNIVPQSCRFDFEIRYLPGM 258
Cdd:cd03896 170 TVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAP---------YVPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 259 RPEA--------VTEALAAYARRQLlpEMRRVGS--GSDIQfqllsHYPPLLSDPQsDFARWLAqwcGSDRFStvAFGTE 328
Cdd:cd03896 241 ELADvqreveavVSKLAAKHLRVKA--RVKPVGDrpGGEAQ-----GTEPLVNAAV-AAHREVG---GDPRPG--SSSTD 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1396632015 329 GGLFDEMGVATLVCGPGSMAQGHKADEYISIAQTERCMTMLRQLCA 374
Cdd:cd03896 308 ANPANSLGIPAVTYGLGRGGNAHRGDEYVLKDDMLKGAKAYLMLAA 353
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
62-333 |
1.55e-17 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 83.47 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 62 VMLSGHTDVV-PVDGqawsvpPFSLTER--DGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPL--HLAFSYDEEVGCL 136
Cdd:PRK07338 95 VLLTGHMDTVfPADH------PFQTLSWldDGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLgyDVLINPDEEIGSP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 137 GVRSLVDflQASPEKPAlCLIGEPteMQP----VFGHKGKLAMRCCIEGQACHSAYAPQ-GVNAIRYAArlinhldRLGV 211
Cdd:PRK07338 169 ASAPLLA--ELARGKHA-ALTYEP--ALPdgtlAGARKGSGNFTIVVTGRAAHAGRAFDeGRNAIVAAA-------ELAL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 212 RLARQQDSRfspPFSTLQVGTIQGGAALNIVPQSCRFDFEIRylpgmrpeAVTEALAAYARRQLLPEMRRVGSGSDIQFQ 291
Cdd:PRK07338 237 ALHALNGQR---DGVTVNVAKIDGGGPLNVVPDNAVLRFNIR--------PPTPEDAAWAEAELKKLIAQVNQRHGVSLH 305
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1396632015 292 LLSHY--PPLLSDPQSD--FARWlaQWCGSDRFSTVAFGTEGGLFD 333
Cdd:PRK07338 306 LHGGFgrPPKPIDAAQQrlFEAV--QACGAALGLTIDWKDSGGVCD 349
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
62-273 |
3.73e-17 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 82.69 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 62 VMLSGHTDVVPV-DGQA--WSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAA---PLRMpLHLAFSYDEEV-G 134
Cdd:cd05674 72 LLLMAHQDVVPVnPETEdqWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRgfkPRRT-IILAFGHDEEVgG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 135 CLGVRSLVDFLQASPEKPALCLI---GEPTEMQPVFG---------HKGKLAMRCCIEGQACHSA--------------- 187
Cdd:cd05674 151 ERGAGAIAELLLERYGVDGLAAIldeGGAVLEGVFLGvpfalpgvaEKGYMDVEITVHTPGGHSSvppkhtgigilseav 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 188 ---------------------------YAPQGVNAIRYAARL-INHLDRLGVRLARQQDSRFSPPFSTLQ-VGTIQGGAA 238
Cdd:cd05674 231 aaleanpfppkltpgnpyygmlqclaeHSPLPPRSLKSNLWLaSPLLKALLASELLSTSPLTRALLRTTQaVDIINGGVK 310
|
250 260 270
....*....|....*....|....*....|....*
gi 1396632015 239 LNIVPQSCRFDFEIRYLPGMRPEAVTEALAAYARR 273
Cdd:cd05674 311 INALPETATATVNHRIAPGSSVEEVLEHVKNLIAD 345
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
4-268 |
7.58e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 78.89 E-value: 7.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 4 ILAALLAFDTT-SRHSNLAMIDWIADFLAARGVASR--RFYDPSGGKANLYARLGPSGGGG-VMLSGHTDVVPVDGQAWS 79
Cdd:PRK09133 42 LYKELIEINTTaSTGSTTPAAEAMAARLKAAGFADAdiEVTGPYPRKGNLVARLRGTDPKKpILLLAHMDVVEAKREDWT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 80 VPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAA---PLRmPLHLAFSYDEEVGCL-GVRSLVDFLQASPEkPALC 155
Cdd:PRK09133 122 RDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREgfkPKR-DIILALTGDEEGTPMnGVAWLAENHRDLID-AEFA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 156 L----------IGEPTEMQPVFGHKGKLAMRCCIEGQACHSAyAPQGVNAIryaARLINHLDRLGV-------------- 211
Cdd:PRK09133 200 LneggggtldeDGKPVLLTVQAGEKTYADFRLEVTNPGGHSS-RPTKDNAI---YRLAAALSRLAAyrfpvmlndvtray 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 212 --RLARQQD----------------------SRFSPPFSTlQVGT------IQGGAALNIVPQSCRFDFEIRYLPGMRPE 261
Cdd:PRK09133 276 fkQSAAIETgplaaamrafaanpadeaaialLSADPSYNA-MLRTtcvatmLEGGHAENALPQRATANVNCRIFPGDTIE 354
|
....*..
gi 1396632015 262 AVTEALA 268
Cdd:PRK09133 355 AVRATLK 361
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
24-305 |
1.84e-15 |
|
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: 77.35 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 24 DWIADFLAARGVASRRFYDPSGGKAnLYA-RLGPSGGGGVMLSGHTDVVPVDG-QAWSVPPFSLTERDGRYYGRGSADMK 101
Cdd:cd05680 28 EWLADKLTEAGFEHTEVLPTGGHPL-VYAeWLGAPGAPTVLVYGHYDVQPPDPlELWTSPPFEPVVRDGRLYARGASDDK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 102 GFLACVLAAVDDFLAAPLRMPLHLAFSYD--EEVGCLGVRSLV----DFLQA-----------SPEKPALCligeptemq 164
Cdd:cd05680 107 GQVFIHIKAVEAWLAVEGALPVNVKFLIEgeEEIGSPSLPAFLeenaERLAAdvvlvsdtsmwSPDTPTIT--------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 165 pvFGHKGKLAMRCCIEG--QACHSA-YAPQGVNAIRYAARLINHL---------------------------DRLGVRLA 214
Cdd:cd05680 178 --YGLRGLAYLEISVTGpnRDLHSGsYGGAVPNPANALARLLASLhdedgrvaipgfyddvrpltdaereawAALPFDEA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 215 RQQDSRFSPP------FSTLQ-------------VGTIQGGAALNIVPQSCRFDFEIRYLPGMRPEAVTEALAAYARRQL 275
Cdd:cd05680 256 AFKASLGVPAlggeagYTTLErlwarptldvngiWGGYQGEGSKTVIPSKAHAKISMRLVPGQDPDAIADLLEAHLRAHA 335
|
330 340 350
....*....|....*....|....*....|
gi 1396632015 276 LPEMRrvgsgsdIQFQLLSHYPPLLSDPQS 305
Cdd:cd05680 336 PPGVT-------LSVKPLHGGRPYLVPTDH 358
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
22-143 |
4.33e-15 |
|
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: 76.49 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 22 MIDWIADFLAARGVASRRFY-----DPSGGKANL----YARLG--PSGGGgVMLSGHTDVVPV---DGqaWSVPPFSLTE 87
Cdd:cd05676 38 MMEWAAERLEKLGFKVELVDigtqtLPDGEELPLppvlLGRLGsdPSKKT-VLIYGHLDVQPAkleDG--WDTDPFELTE 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1396632015 88 RDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAFSYD--EEVGCLGVRSLVD 143
Cdd:cd05676 115 KDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEgmEESGSEGLDELIE 172
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
62-303 |
5.77e-15 |
|
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: 75.60 E-value: 5.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 62 VMLSGHTDVVPVDGQAWSVPPFS-LTERDGRYYGRGSADMKgflaCV----LAAVDDFLAA---PLRMpLHLAFSYDEEV 133
Cdd:TIGR01880 74 ILLNSHTDVVPVFREHWTHPPFSaFKDEDGNIYARGAQDMK----CVgvqyLEAVRNLKASgfkFKRT-IHISFVPDEEI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 134 GclGVRSLVDFLQaSPEKPALCL-------IGEPTEMQPVF-GHKGKLAMRCCIEGQACHSA--YAPQGVNAIRYAARLI 203
Cdd:TIGR01880 149 G--GHDGMEKFAK-TDEFKALNLgfaldegLASPDDVYRVFyAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 204 NHLDRLGVRLARQQDSRFSPPFSTLQVGTIQGGAALNIVPQSCRFDFEIRYLPGMRPEAVtealaayaRRQLLPEMRRVG 283
Cdd:TIGR01880 226 RRFRESQFQLLQSNPDLAIGDVTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEM--------ENRLDEWCADAG 297
|
250 260
....*....|....*....|....
gi 1396632015 284 SGSDIQFQLLSHYPPLL----SDP 303
Cdd:TIGR01880 298 EGVTYEFSQHSGKPLVTphddSNP 321
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
51-134 |
8.81e-15 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 75.20 E-value: 8.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 51 YARLGPSGGGG--VMLSGHTDVVPVDGQAWSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAFS 128
Cdd:PRK08554 53 YAVYGEIGEGKpkLLFMAHFDVVPVNPEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLNGKVIFAFT 132
|
....*.
gi 1396632015 129 YDEEVG 134
Cdd:PRK08554 133 GDEEIG 138
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
24-208 |
5.29e-13 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 70.16 E-value: 5.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 24 DWIADFLAARGVASRRFYDpSGGKANLYA-RLGPSGGGGVMLSGHTDVVPVDG-QAWSVPPFSLTERDGRYYGRGSADMK 101
Cdd:PRK08201 44 EWLAGALEKAGLEHVEIME-TAGHPIVYAdWLHAPGKPTVLIYGHYDVQPVDPlNLWETPPFEPTIRDGKLYARGASDDK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 102 GFLACVLAAVDDFLAAPLRMPLHLAFSY--DEEVGClgvRSLVDFLQASPEKPA--LCLIGEPTEMQP-----VFGHKGK 172
Cdd:PRK08201 123 GQVFMHLKAVEALLKVEGTLPVNVKFCIegEEEIGS---PNLDSFVEEEKDKLAadVVLISDTTLLGPgkpaiCYGLRGL 199
|
170 180 190
....*....|....*....|....*....|....*....
gi 1396632015 173 LAMRCCIEGQA--CHSAYAPQGV-NAIRYAARLINHLDR 208
Cdd:PRK08201 200 AALEIDVRGAKgdLHSGLYGGAVpNALHALVQLLASLHD 238
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
62-272 |
6.89e-13 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 69.22 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 62 VMLSGHTDVVPVDGQAWSVPPFS-LTERDGRYYGRGSADMKgflaCV----LAAVDDFLAAPLRMP--LHLAFSYDEEVG 134
Cdd:cd05646 67 ILLNSHTDVVPVFEEKWTHDPFSaHKDEDGNIYARGAQDMK----CVgiqyLEAIRRLKASGFKPKrtIHLSFVPDEEIG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 135 clGVRSLVDFLQaSPEKPAL----CL---IGEPTEMQPVF-GHKGKLAMRCCIEGQACHSAYAPQGvNAIRYAARLINHL 206
Cdd:cd05646 143 --GHDGMEKFVK-TEEFKKLnvgfALdegLASPTEEYRVFyGERSPWWVVITAPGTPGHGSKLLEN-TAGEKLRKVIESI 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1396632015 207 DRLgvrlaRQQDSRFSPPFSTLQVGT--------IQGGAALNIVPQSCRFDFEIRYLPGMRPEAVTEALAAYAR 272
Cdd:cd05646 219 MEF-----RESQKQRLKSNPNLTLGDvttvnltmLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCA 287
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
66-207 |
1.48e-11 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 65.48 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 66 GHTDVVPVdGQAWSVPPFSLTERDGRYYGRGSADMKG-FLACVLA--AVDDfLAAPLRMPLHLAFSYDEEVG--CL---- 136
Cdd:TIGR01887 74 GHLDVVPA-GDGWTSPPFEPTIKDGRIYGRGTLDDKGpTIAAYYAmkILKE-LGLKLKKKIRFIFGTDEESGwkCIdyyf 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 137 -----------------------GVrSLVDFLQASPEKPALCLI----GEPTEMQP------VFGHKGKLAMRCC----- 178
Cdd:TIGR01887 152 eheempdigftpdaefpiiygekGI-TTLEIKFKDDTEGDVVLEsfkaGEAYNMVPdhatavISGKKLTEVEQLKfvffi 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1396632015 179 ------------------IEGQACHSAYAPQGVNAIRYAARLINHLD 207
Cdd:TIGR01887 231 akelegdfevndgtltitLEGKSAHGSAPEKGINAATYLALFLAQLN 277
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
66-361 |
2.99e-11 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 64.57 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 66 GHTDVVPVdGQAWSVPPFSLTERDGRYYGRGSADMKG-FLAC--VLAAVDDfLAAPLRMPLHLAFSYDEEVG--CL---- 136
Cdd:cd03888 78 GHLDVVPA-GEGWTTDPFKPVIKDGKLYGRGTIDDKGpTIAAlyALKILKD-LGLPLKKKIRLIFGTDEETGwkCIehyf 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 137 ---GVRSL-------------------VDFLQASPEKPALCLI----GEPTEMQP-------VFGHKGKLAMRC------ 177
Cdd:cd03888 156 eheEYPDFgftpdaefpvingekgivtVDLTFKIDDDKGYRLIsikgGEATNMVPdkaeaviPGKDKEELALSAatdlkg 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 178 -----------CIEGQACHSAYAPQGVNAIRYAARLINHLDRLGV------RLARQ--QDSR-------FSPPFS---TL 228
Cdd:cd03888 236 nieiddggvelTVTGKSAHASAPEKGVNAITLLAKFLAELNKDGNdkdfikFLAKNlhEDYNgkklginFEDEVMgelTL 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 229 QVGTIqggaalNIVPQSCRFDFEIRYLPGMRPEAVTEALAAYArrqllpemrrvgSGSDIQFQLLSHYPPLLSDPQSDF- 307
Cdd:cd03888 316 NPGII------TLDDGKLELGLNVRYPVGTSAEDIIKQIEEAL------------EKYGVEVEGHKHQKPLYVPKDSPLv 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1396632015 308 -------------------------ARWLAQwcgsdrfsTVAFGTEgglFdemgvatlvcgPGSMAQGHKADEYISIAQ 361
Cdd:cd03888 378 ktllkvyeeqtgkegepvaigggtyARELPN--------GVAFGPE---F-----------PGQKDTMHQANEFIPIDD 434
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
25-206 |
3.77e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 60.92 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 25 WIADFLAARGVASRrfYDPSGGKANLYARLGPSGGGGVMLSGHTDVVPVDG-QAWSVPPFSLTERDGRYYGRGSADMKGF 103
Cdd:PRK06446 30 YLKDTMEKLGIKAN--IERTKGHPVVYGEINVGAKKTLLIYNHYDVQPVDPlSEWKRDPFSATIENGRIYARGASDNKGT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 104 LACVLAAVDDFLAAPlRMPLHLAFSY--DEEVGCLgvrSLVDFLQASPEKP-ALCLIGEPTEMQP------VFGHKGKL- 173
Cdd:PRK06446 108 LMARLFAIKHLIDKH-KLNVNVKFLYegEEEIGSP---NLEDFIEKNKNKLkADSVIMEGAGLDPkgrpqiVLGVKGLLy 183
|
170 180 190
....*....|....*....|....*....|....
gi 1396632015 174 -AMRCCIEGQACHSAYAPQGVNAIRYAARLINHL 206
Cdd:PRK06446 184 vELVLRTGTKDLHSSNAPIVRNPAWDLVKLLSTL 217
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
22-306 |
1.00e-09 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 59.64 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 22 MIDWIADFLAARGVASRRFYDPSGGKANLYARLGPSGGGGVMLSGHTDVVPVDGQAWSVPpfsLTERDGRYYGRGSADMK 101
Cdd:PRK06133 62 VAALLAERLKALGAKVERAPTPPSAGDMVVATFKGTGKRRIMLIAHMDTVYLPGMLAKQP---FRIDGDRAYGPGIADDK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 102 GFLACVLAAV--------DDFLAaplrmpLHLAFSYDEEVGCLGVRSLVDFLQASPEKPALCLIGEPTEmQPVFGHKGKL 173
Cdd:PRK06133 139 GGVAVILHALkilqqlgfKDYGT------LTVLFNPDEETGSPGSRELIAELAAQHDVVFSCEPGRAKD-ALTLATSGIA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 174 AMRCCIEGQACHSAYAP-QGVNAIRYAARLINHLDRLGVrlarqqdsrfSPPFSTLQVGTIQGGAALNIVPQSCRFDFEI 252
Cdd:PRK06133 212 TALLEVKGKASHAGAAPeLGRNALYELAHQLLQLRDLGD----------PAKGTTLNWTVAKAGTNRNVIPASASAQADV 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1396632015 253 RYLpgmRPEAVTEALAAYARR---QLLPEmrrvgsgSDIQFQLLSHYPPLLSDPQSD 306
Cdd:PRK06133 282 RYL---DPAEFDRLEADLQEKvknKLVPD-------TEVTLRFERGRPPLEANAASR 328
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
22-247 |
1.24e-09 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 59.41 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 22 MIDWIADFLAARGVASRRFYDPSGGKANLYARLgP---SGGGGVMLSGHTDVVPVDGQAWSVPpfslTERDG-RYYGRGS 97
Cdd:PRK07473 36 MLDLAARDMAIMGATIERIPGRQGFGDCVRARF-PhprQGEPGILIAGHMDTVHPVGTLEKLP----WRREGnKCYGPGI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 98 ADMKGFLACVLAAVDDFLAAPLRMPLHLA--FSYDEEVGCLGVRslvDFLQASPEKPALCLIGEPTemQPVFG-HKGKLA 174
Cdd:PRK07473 111 LDMKGGNYLALEAIRQLARAGITTPLPITvlFTPDEEVGTPSTR---DLIEAEAARNKYVLVPEPG--RPDNGvVTGRYA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1396632015 175 M-RCCIE--GQACHS-AYAPQGVNAIRYAARLINHLDRLgvrlaRQQDSRFSppfstlqVGTIQGGAALNIVPQSCR 247
Cdd:PRK07473 186 IaRFNLEatGRPSHAgATLSEGRSAIREMARQILAIDAM-----TTEDCTFS-------VGIVHGGQWVNCVATTCT 250
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
43-359 |
6.21e-09 |
|
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: 57.07 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 43 PSGGKANLYARLGPSGGGG--VMLSGHTD-VVPVDGqawsVPPFSltERDGRYYGRGS----ADMKGFLACVLAAVDDFL 115
Cdd:cd05683 49 TGGGAGNLICTLKADKEEVpkILFTSHMDtVTPGIN----VKPPQ--IADGYIYSDGTtilgADDKAGIAAILEAIRVIK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 116 AAPLRM-PLHLAFSYDEEVGCLGVRSL--------VDFLQASPEKPALCLIGEPTEMqpvfghkgKLAMRccIEGQACHS 186
Cdd:cd05683 123 EKNIPHgQIQFVITVGEESGLVGAKALdpelidadYGYALDSEGDVGTIIVGAPTQD--------KINAK--IYGKTAHA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 187 AYAPQ-GVNAIRYAARLINHLdRLGvrlarQQDSrfsppFSTLQVGTIQGGAALNIVPQSCRFDFEIRYLpgmRPEAVtE 265
Cdd:cd05683 193 GTSPEkGISAINIAAKAISNM-KLG-----RIDE-----ETTANIGKFQGGTATNIVTDEVNIEAEARSL---DEEKL-D 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 266 ALAAYARRQLLPEMRRVGSGSDIQFQLLshYPPLLSDPQSDFARWLAQWCGSDRFSTVAFGTEGG----LFDEMGVATLV 341
Cdd:cd05683 258 AQVKHMKETFETTAKEKGAHAEVEVETS--YPGFKINEDEEVVKLAKRAANNLGLEINTTYSGGGsdanIINGLGIPTVN 335
|
330
....*....|....*...
gi 1396632015 342 CGPGsMAQGHKADEYISI 359
Cdd:cd05683 336 LGIG-YENIHTTNERIPI 352
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
66-134 |
1.91e-08 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 56.00 E-value: 1.91e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1396632015 66 GHTDVVPVdGQAWSVPPFSLTERDGRYYGRGSADMKG-FLACVLA--AVDDfLAAPLRMPLHLAFSYDEEVG 134
Cdd:PRK07318 86 GHLDVVPA-GDGWDTDPYEPVIKDGKIYARGTSDDKGpTMAAYYAlkIIKE-LGLPLSKKVRFIVGTDEESG 155
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
5-141 |
2.21e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 55.69 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 5 LAALLAFDTTSRHSNLA------MIDWIADFLAARGVASRRFYDPSGGKAN-LYARLGPSGGGGVMLS-GHTDVVPVDGQ 76
Cdd:PRK07079 23 LARRVAYRTESQNPDRApalrayLTDEIAPALAALGFTCRIVDNPVAGGGPfLIAERIEDDALPTVLIyGHGDVVRGYDE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1396632015 77 AWSVP--PFSLTERDGRYYGRGSADMKG-------FLACVLAAVDDFLAAPLRMPLHLAfsydEEVGCLGVRSL 141
Cdd:PRK07079 103 QWREGlsPWTLTEEGDRWYGRGTADNKGqhtinlaALEQVLAARGGRLGFNVKLLIEMG----EEIGSPGLAEV 172
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
179-304 |
3.15e-08 |
|
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: 54.91 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 179 IEGQACHSAYAPQGVNAIRYAARLINHLDRLgvrlarqqDSRFSPPFS--TLQVGTIQGGAALNIVPQSCRFDFEIRylp 256
Cdd:cd03886 178 VKGKGGHGASPHLGVDPIVAAAQIVLALQTV--------VSRELDPLEpaVVTVGKFHAGTAFNVIPDTAVLEGTIR--- 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1396632015 257 gmrpeavteALAAYARRQLLPEMRRV------GSGSDIQFQLLSHYPPLLSDPQ 304
Cdd:cd03886 247 ---------TFDPEVREALEARIKRLaegiaaAYGATVELEYGYGYPAVINDPE 291
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
24-147 |
3.33e-08 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 55.29 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 24 DWIADFLAARGV-ASRRfydPSGGKANLYARLGPSGGGG--VMLSGHTDVVPVDGQA-WSVPPF--SLTER-DGR--YYG 94
Cdd:PRK09104 47 DWLVADLASLGFeASVR---DTPGHPMVVAHHEGPTGDAphVLFYGHYDVQPVDPLDlWESPPFepRIKETpDGRkvIVA 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1396632015 95 RGSADMKGFLACVLAAVDDFLAAPLRMPLHLA--FSYDEEVGClgvRSLVDFLQA 147
Cdd:PRK09104 124 RGASDDKGQLMTFVEACRAWKAVTGSLPVRVTilFEGEEESGS---PSLVPFLEA 175
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
51-132 |
5.95e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 54.32 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 51 YARLGPsggGGVMLS--GHTDVVPV-DGQAWSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLAAPLRMPLHLAF 127
Cdd:PRK07205 68 YAEIGQ---GEELLAilCHLDVVPEgDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRF 144
|
....*..
gi 1396632015 128 SY--DEE 132
Cdd:PRK07205 145 IFgtDEE 151
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
39-312 |
6.61e-08 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 53.63 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 39 RFYDPSGGKANLYA-------------RLGPS------GGGGVMLSGHTDVVPvdGQawsVPPFSLTErdgRYYGRGSAD 99
Cdd:PRK00466 21 SIYTPSGNETNATKffekisnelnlklEILPDsnsfilGEGDILLASHVDTVP--GY---IEPKIEGE---VIYGRGAVD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 100 MKGFLACVLAAVddFLAAPLRMPLHLAFSYDEEVGCLGVRSLVdflqASPEKPALCLIGEPTEMQPV-FGHKGKLAMRCC 178
Cdd:PRK00466 93 AKGPLISMIIAA--WLLNEKGIKVMVSGLADEESTSIGAKELV----SKGFNFKHIIVGEPSNGTDIvVEYRGSIQLDIM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 179 IEGQACHSAYAPQGVnAIRYAARLINHLdrlgvrlarQQDSRFSPPfsTLQVGTIQGGAALNIVPQSCRFDFEIRYlpgm 258
Cdd:PRK00466 167 CEGTPEHSSSAKSNL-IVDISKKIIEVY---------KQPENYDKP--SIVPTIIRAGESYNVTPAKLYLHFDVRY---- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1396632015 259 rPEAVTEAlaayarrQLLPEMRRVGSGSDIqfQLLSHYPPLLSDPQSDFARWLA 312
Cdd:PRK00466 231 -AINNKRD-------DLISEIKDKFQECGL--KIVDETPPVKVSINNPVVKALM 274
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
46-199 |
1.38e-06 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 50.15 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 46 GKANLYARLGPSGGGGVM--LSGHTDVVPVDGQAWSVPPFSLTeRDG-RYYGRGSADMKGFLACV------LAAvddfLA 116
Cdd:cd08012 63 GRGNIIVEYPGTVDGKTVsfVGSHMDVVTANPETWEFDPFSLS-IDGdKLYGRGTTDCLGHVALVtelfrqLAT----EK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 117 APLRMPLHLAFSYDEE---VGCLGVRSLVDFLQASPEKPALCLIGEPTEMQPVFGHKGKLAMRCCIEGQACHSAYAPQGV 193
Cdd:cd08012 138 PALKRTVVAVFIANEEnseIPGVGVDALVKSGLLDNLKSGPLYWVDSADSQPCIGTGGMVTWKLTATGKLFHSGLPHKAI 217
|
....*.
gi 1396632015 194 NAIRYA 199
Cdd:cd08012 218 NALELV 223
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
24-143 |
2.44e-06 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 49.42 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 24 DWIADFLAARGVASRRFYDPSGGKAN-LYARLGPSGGGGVMLS-GHTDVVPVDGQAW--SVPPFSLTERDGRYYGRGSAD 99
Cdd:cd05679 35 QEMRPRFERLGFTVHIHDNPVAGRAPfLIAERIEDPSLPTLLIyGHGDVVPGYEGRWrdGRDPWTVTVWGERWYGRGTAD 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1396632015 100 MKGFLACVLAAVDDFLAA---PLRMPLHLAFSYDEEVGCLGVRSLVD 143
Cdd:cd05679 115 NKGQHSINMAALRQVLEArggKLGFNVKFLIEMGEEMGSPGLRAFCF 161
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
1-116 |
2.65e-06 |
|
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: 49.26 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 1 MNNILAALLAFDTTSRHSNLAmidwiaDFLAARGVAS---RRFYD---------PSGGKAN--LYARLGPSGGGG----V 62
Cdd:cd05677 1 MLNTLSEFIAFQTVSQSPTTE------NAEDSRRCAIflrQLFKKlgatnclllPSGPGTNpiVLATFSGNSSDAkrkrI 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1396632015 63 MLSGHTDVVPVDG-QAWSVPPFSLTERDGRYYGRGSADMKGFLACVLAAVDDFLA 116
Cdd:cd05677 75 LFYGHYDVIPAGEtDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQ 129
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
62-229 |
8.23e-06 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 47.72 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 62 VMLSGHTDVVPVDG----QAWSVPPFSLTERDGRY------------------YGRGSADMKGFLACVLAAVdDFLAAPL 119
Cdd:cd05654 74 IILISHFDTVGIEDygelKDIAFDPDELTKAFSEYveeldeevredllsgewlFGRGTMDMKSGLAVHLALL-EQASEDE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 120 RMP--LHLAFSYDEEVGCLGVRSLVDFLQASPEKP----ALCLIGEP-TEMQP------VF-GHKGKLAMRCCIEGQACH 185
Cdd:cd05654 153 DFDgnLLLMAVPDEEVNSRGMRAAVPALLELKKKHdleyKLAINSEPiFPQYDgdqtryIYtGSIGKILPGFLCYGKETH 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1396632015 186 SAYAPQGVNAIRYAARLINHLDrLGVRLARQQDSRFSPPFSTLQ 229
Cdd:cd05654 233 VGEPFAGINANLMASEITARLE-LNADLCEKVEGEITPPPVCLK 275
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
179-313 |
1.52e-05 |
|
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: 46.52 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 179 IEGQACHSAYAPQGVNAIRYAARLINHLDRLGvrlarqqdSRFSPPF--STLQVGTIQGGAALNIVPQSCR-------FD 249
Cdd:cd05669 179 IAGKGAHAAKPENGVDPIVAASQIINALQTIV--------SRNISPLesAVVSVTRIHAGNTWNVIPDSAElegtvrtFD 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1396632015 250 FEIRYLPGMRPEAVTEALAAyarrqllpemrrvGSGSDIQFQLLSHYPPLLSDPQ-SDFARWLAQ 313
Cdd:cd05669 251 AEVRQLVKERFEQIVEGIAA-------------AFGAKIEFKWHSGPPAVINDEElTDLASEVAA 302
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
179-305 |
4.71e-05 |
|
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: 44.96 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 179 IEGQACHSAYAPQGVNAIRYAARLINHLDRLgvrLARQQDSRfSPpfSTLQVGTIQGGAALNIVPQSCRFDFEIRYL--- 255
Cdd:cd08014 177 IQGEGGHGARPHLTVDLVWAAAQVVTDLPQA---ISRRIDPR-SP--VVLTWGSIEGGRAPNVIPDSVELSGTVRTLdpd 250
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1396632015 256 -----PGMRPEAVTEALAAYarrqllpemrrvgsGSDIQFQLLSHYPPLLSDPQS 305
Cdd:cd08014 251 twaqlPDLVEEIVAGICAPY--------------GAKYELEYRRGVPPVINDPAS 291
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
179-304 |
2.39e-04 |
|
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273857 [Multi-domain] Cd Length: 363 Bit Score: 42.72 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 179 IEGQACHSAYAPQGVNAIRYAARLINHLDRLgvrLARQQDSrFSPPfsTLQVGTIQGGAALNIVPQSCRFDFEIRylpGM 258
Cdd:TIGR01891 177 IHGKGAHAARPHLGRDALDAAAQLVVALQQI---VSRNVDP-SRPA--VVSVGIIEAGGAPNVIPDKASMSGTVR---SL 247
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1396632015 259 RPEavtealaayARRQLLPEMRRVGS------GSDIQFQLLSHYPPLLSDPQ 304
Cdd:TIGR01891 248 DPE---------VRDQIIDRIERIVEgaaamyGAKVELNYDRGLPAVTNDPA 290
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
54-110 |
2.62e-04 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 43.03 E-value: 2.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1396632015 54 LGPSGGGGVMLSGHTDVVPVDGQAWSVP-----PFSLTERDGRYYGRGSADMKGFLACVLAA 110
Cdd:PRK06156 104 LGGSGSDKVGILTHADVVPANPELWVLDgtrldPFKVTLVGDRLYGRGTEDDKGAIVTALYA 165
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
174-323 |
3.41e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349914 [Multi-domain] Cd Length: 399 Bit Score: 42.33 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 174 AMRCCIEGQACHSAYAPQGVNAIRYAARLINhldRLGVRLARQQDSRfspPFSTLQVGTIQGGAALNIVPQSCRFDFEIR 253
Cdd:cd05664 183 SLDITIFGRGGHGSMPHLTIDPVVMAASIVT---RLQTIVSREVDPQ---EFAVVTVGSIQAGSAENIIPDEAELKLNVR 256
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1396632015 254 YLpgmrPEAVTEALAAYARRQLLPEMRRVGSGSDIQFQLLSHYPPLLSDPQ--SDFARWLAQWCGSDRFSTV 323
Cdd:cd05664 257 TF----DPEVREKVLNAIKRIVRAECAASGAPKPPEFTYTDSFPATVNDEDatARLAAAFREYFGEDRVVEV 324
|
|
| M20_Acy1-like |
cd05667 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
179-311 |
3.43e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349917 [Multi-domain] Cd Length: 403 Bit Score: 42.41 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 179 IEGQACHSAYAPQGVNAIRYAARLINHLDRLgvrLARQQDSRFSPpfSTLQVGTIQGGAALNIVPQSCRFDFEIRYL-PG 257
Cdd:cd05667 202 VKGKQTHGSRPWDGIDPIMASAQIIQGLQTI---ISRRIDLTKEP--AVISIGKINGGTRGNIIPEDAEMVGTIRTFdPE 276
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1396632015 258 MRPEavtealaAYARRQLLPEMRRVGSGSDIQFQLLSHYPPLLSDPqsDFARWL 311
Cdd:cd05667 277 MRED-------IFARLKTIAEHIAKAYGATAEVEFANGYPVTYNDP--ALTAKM 321
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
179-254 |
5.91e-04 |
|
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: 41.55 E-value: 5.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1396632015 179 IEGQACHSAYAPQGVNAIRYAARLINHLDRLgvrLARQQDSRFSPPFStlqVGTIQGGAALNIVPQSCRFDFEIRY 254
Cdd:cd08019 175 VKGKGGHGSMPHQGIDAVLAAASIVMNLQSI---VSREIDPLEPVVVT---VGKLNSGTRFNVIADEAKIEGTLRT 244
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
62-229 |
7.06e-04 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 41.76 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 62 VMLSGHTDVVPVDG----QAWSVPPFSLTER---------------DGRY-YGRGSADMKGFLA------CVLAAVDDF- 114
Cdd:COG4187 82 VILISHFDVVDVEDygslKPLAFDPEELTEAlkeiklpedvrkdleSGEWlFGRGTMDMKAGLAlhlallEEASENEEFp 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 115 -----LAAPlrmplhlafsyDEEVGCLGVRSLVDFLQASPEKPAL----CLIGEPTEMQ-PVFGHK-------GKLaMRC 177
Cdd:COG4187 162 gnlllLAVP-----------DEEVNSAGMRAAVPLLAELKEKYGLeyklAINSEPSFPKyPGDETRyiytgsiGKL-MPG 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1396632015 178 --CIeGQACHSAYAPQGVNAIRYAARLINHLDrLGVRLARQQDSRFSPPFSTLQ 229
Cdd:COG4187 230 fyCY-GKETHVGEPFSGLNANLLASELTRELE-LNPDFCEEVGGEVTPPPVSLK 281
|
|
| PRK12891 |
PRK12891 |
allantoate amidohydrolase; Reviewed |
181-303 |
7.84e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 237249 Cd Length: 414 Bit Score: 38.26 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396632015 181 GQACHSAYAPQGV--NAIRYAARLINHLDRLGVRLArqqdsrfspPFSTLQVGTIQG-GAALNIVPQSCRFDFEIRYLPG 257
Cdd:PRK12891 223 GVDAHAGTTPMAFrrDALVGAARMIAFLDALGRRDA---------PDARATVGMIDArPNSRNTVPGECFFTVEFRHPDD 293
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1396632015 258 MRPEAVTEALAAYARRQllpemrRVGSGSDIQFQLLSHYPPLLSDP 303
Cdd:PRK12891 294 AVLDRLDAALRAELARI------ADETGLRADIEQIFGYAPAPFAP 333
|
|
| |
