|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
1-371 |
0e+00 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 700.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 1 MPGSRDILADLVAFDTVSRESNLALIDYVRDYLAGFGVDSELFFDADGRKANLYATIGPSDRGGVCLSGHTDVVPADGQA 80
Cdd:PRK07522 3 SMSSLDILERLVAFDTVSRDSNLALIEWVRDYLAAHGVESELIPDPEGDKANLFATIGPADRGGIVLSGHTDVVPVDGQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 81 WSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAFSYDEEVGCLGVRSLLAALERRPHKPLLCII 160
Cdd:PRK07522 83 WTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPSMIARLPERGVKPAGCIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 161 GEPTELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAVPERHDRRFDPPYSTVQTGLIQG 240
Cdd:PRK07522 163 GEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLAAPGPFDALFDPPYSTLQTGTIQG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 241 GRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAESELLPRMRAVERSTDIRFTPLSAYPGLLTADDSQAAELIGLLS 320
Cdd:PRK07522 243 GTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAELLPEMRAVHPEAAIEFEPLSAYPGLDTAEDAAAARLVRALT 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489196727 321 GSTDFSTVAFGTEGGLFHQAGIPAVICGPGSMDQGHKPDEFVSLAQLEACD 371
Cdd:PRK07522 323 GDNDLRKVAYGTEAGLFQRAGIPTVVCGPGSIEQAHKPDEFVELAQLAACE 373
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
6-370 |
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: 560.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSRESNLALIDYVRDYLAGFGVDSELFFDADGRKANLYATIGPSDRGGVCLSGHTDVVPADGQAWSVPP 85
Cdd:cd03894 1 ELLARLVAFDTVSRNSNLALIEYVADYLAALGVKSRRVPVPEGGKANLLATLGPGGEGGLLLSGHTDVVPVDGQKWSSDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 86 FRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAFSYDEEVGCLGVRSLLAALERRPHKPLLCIIGEPTE 165
Cdd:cd03894 81 FTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALAARGGRPDAAIVGEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 166 LKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAvPERHDRRFDPPYSTVQTGLIQGGRALN 245
Cdd:cd03894 161 LQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRLA-PGLRDPPFDPPYPTLNVGLIHGGNAVN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 246 IVPAECRFDFEVRALPADDPRQVAEELRDYAESELlprmraVERSTDIRFTPLSAYPGLLTADDSQAAELIGLLSGSTDF 325
Cdd:cd03894 240 IVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALL------EFPEAGIEVEPLFEVPGLETDEDAPLVRLAAALAGDNKV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 489196727 326 STVAFGTEGGLFHQAGIPAVICGPGSMDQGHKPDEFVSLAQLEAC 370
Cdd:cd03894 314 RTVAYGTEAGLFQRAGIPTVVCGPGSIAQAHTPDEFVELEQLDRC 358
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
6-370 |
5.42e-132 |
|
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: 382.63 E-value: 5.42e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSRESNLALIDYVRDYLAGFGVDSELFFDADGR-KANLYATIGPSDRGGVCLSGHTDVVPADGQAWSVP 84
Cdd:TIGR01892 1 EILTKLVAFDSTSFRPNVDLIDWAQAYLEALGFSVEVQPFPDGAeKSNLVAVIGPSGAGGLALSGHTDVVPYDDAAWTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 85 PFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAFSYDEEVGCLGVRSLLAALERRphkPLLCIIGEPT 164
Cdd:TIGR01892 81 PFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIEAGAGR---PRHAIIGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 165 ELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLaVPERHDRRFDPPYSTVQTGLIQGGRAL 244
Cdd:TIGR01892 158 RLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTL-LREDLDEGFTPPYTTLNIGVIQGGKAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 245 NIVPAECRFDFEVRALPADDPRQVAEELRDYAESelLPRmRAVERSTDIRFtpLSAYPGLLTADDSQAAELIGLLSGSTd 324
Cdd:TIGR01892 237 NIIPGACEFVFEWRPIPGMDPEELLQLLETIAQA--LVR-DEPGFEVQIEV--VSTDPGVNTEPDAELVAFLEELSGNA- 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 489196727 325 FSTVAFGTEGGLFHQAGIPAVICGPGSMDQGHKPDEFVSLAQLEAC 370
Cdd:TIGR01892 311 PEVVSYGTEAPQFQELGAEAVVCGPGDIRQAHQPDEYVEIEDLVRC 356
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
5-370 |
8.50e-112 |
|
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: 331.85 E-value: 8.50e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 5 RDILADLVAFDTVSREsNLALIDYVRDYLAGFGVDSELFFDADGRkANLYATI-GPSDRGGVCLSGHTDVVPADGQA-WS 82
Cdd:COG0624 15 LELLRELVRIPSVSGE-EAAAAELLAELLEALGFEVERLEVPPGR-PNLVARRpGDGGGPTLLLYGHLDVVPPGDLElWT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 83 VPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLP--VHLAFSYDEEVGCLGVRSLLAALeRRPHKPLLCII 160
Cdd:COG0624 93 SDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPgnVTLLFTGDEEVGSPGARALVEEL-AEGLKADAAIV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 161 GEPTE-LKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLgeigARLAVPERHDRRFDPPysTVQTGLIQ 239
Cdd:COG0624 172 GEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAAL----RDLEFDGRADPLFGRT--TLNVTGIE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 240 GGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYaesellprMRAVERSTDIRFTPLS-AYPGLLTADDSQAAELI-- 316
Cdd:COG0624 246 GGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRAL--------LAAAAPGVEVEVEVLGdGRPPFETPPDSPLVAAAra 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489196727 317 ---GLLSGSTDFSTVAFGTEGGLFHQ-AGIPAVICGPGSMDQGHKPDEFVSLAQLEAC 370
Cdd:COG0624 318 airEVTGKEPVLSGVGGGTDARFFAEaLGIPTVVFGPGDGAGAHAPDEYVELDDLEKG 375
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
6-370 |
1.07e-79 |
|
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: 248.75 E-value: 1.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSRESnLALIDYVRDYLA--GFGVDSELFFDAdgrkANLYATIGPSDRGGVCLSGHTDVVPA-DGQAWS 82
Cdd:cd08659 1 SLLQDLVQIPSVNPPE-AEVAEYLAELLAkrGYGIESTIVEGR----GNLVATVGGGDGPVLLLNGHIDTVPPgDGDKWS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 83 VPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLP--VHLAFSYDEEVGCLGVRSLLAALERRphKPLLCII 160
Cdd:cd08659 76 FPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGgrVALLATVDEEVGSDGARALLEAGYAD--RLDALIV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 161 GEPTELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAVPERHDRrfdppySTVQTGLIQG 240
Cdd:cd08659 154 GEPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPAHPLLGP------PTLNVGVING 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 241 GRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAES-------ELLPRMRAVERStdirfTPLSAYPGLLTA--DDSQ 311
Cdd:cd08659 228 GTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEheakltvEVSLDGDPPFFT-----DPDHPLVQALQAaaRALG 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 489196727 312 AAELIGLLSGSTDFSTVAfgtegglfHQAGIPAVICGPGSMDQGHKPDEFVSLAQLEAC 370
Cdd:cd08659 303 GDPVVRPFTGTTDASYFA--------KDLGFPVVVYGPGDLALAHQPDEYVSLEDLLRA 353
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
2-368 |
2.21e-78 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 246.27 E-value: 2.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 2 PGSRDILADLVAFDTVSR------ESNLALIDYVRDYLA--GFGVDSELFFDADGrKANLYATIGpSDRGGVCLSGHTDV 73
Cdd:PRK05111 5 PSFIEMYRALIATPSISAtdpaldQSNRAVIDLLAGWFEdlGFNVEIQPVPGTRG-KFNLLASLG-SGEGGLLLAGHTDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 74 VPADGQAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAFSYDEEVGCLGVRSLLAAlerRPH 153
Cdd:PRK05111 83 VPFDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAEA---TAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 154 KPLLCIIGEPTELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAvpER-HDRRFDPPYST 232
Cdd:PRK05111 160 RPDCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQ--ERyHNPAFTVPYPT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 233 VQTGLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAEsELLPRmraveRSTDIRFTPL-SAYPGLLTADDSQ 311
Cdd:PRK05111 238 LNLGHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALA-PVSER-----WPGRITVAPLhPPIPGYECPADHQ 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489196727 312 AAELIGLLSGsTDFSTVAFGTEGGLFHQAGIPAVICGPGSMDQGHKPDEFVSLAQLE 368
Cdd:PRK05111 312 LVRVVEKLLG-HKAEVVNYCTEAPFIQQLGCPTLVLGPGSIEQAHQPDEYLELSFIK 367
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
66-370 |
1.61e-64 |
|
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: 208.35 E-value: 1.61e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 66 CLSGHTDVVPaDGQAWSVPpFRlSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRL-PVHLAFSYDEEVGCLGVRSL 144
Cdd:pfam01546 1 LLRGHMDVVP-DEETWGWP-FK-STEDGKLYGRGHDDMKGGLLAALEALRALKEEGLKKgTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 145 LAALERRPHKP---LLCIIGEPTEL------KPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGAR 215
Cdd:pfam01546 78 IEDGLLEREKVdavFGLHIGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 216 LAVPERHdrrfdPPYSTVQTGLIQGGRalNIVPAECRFDFEVRALPADDPRQVAEELRDYAESELLPRMRAVERSTDIRF 295
Cdd:pfam01546 158 NVDPLDP-----AVVTVGNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEYVEGG 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489196727 296 TP-LSAYPGLLTADDSQAAELIGlLSGSTDFSTVAFGTEGGLFhQAGIPA--VICGPGSmDQGHKPDEFVSLAQLEAC 370
Cdd:pfam01546 231 APpLVNDSPLVAALREAAKELFG-LKVELIVSGSMGGTDAAFF-LLGVPPtvVFFGPGS-GLAHSPNEYVDLDDLEKG 305
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
6-368 |
1.01e-62 |
|
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: 205.33 E-value: 1.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVS--RESNLALIDYVRDYLAGFGVDSELFF----DADGRKANLYATIGPSDRGGVCLSGHTDVVPA-DG 78
Cdd:TIGR01910 2 ELLKDLISIPSVNppGGNEETIANYIKDLLREFGFSTDVIEitddRLKVLGKVVVKEPGNGNEKSLIFNGHYDVVPAgDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 79 QAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLP--VHLAFSYDEEVGCLGVRSLlaaLERRPHKPL 156
Cdd:TIGR01910 82 ELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNgnIILQSVVDEESGEAGTLYL---LQRGYFKDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 157 -LCIIGEPTE-LKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEigARLAVPERHDRRFDPPYSTVQ 234
Cdd:TIGR01910 159 dGVLIPEPSGgDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNE--LEEHIYARNSYGFIPGPITFN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 235 TGLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYaesellprMRAVERST--DIRFTPLSAYPGLLTADDsqA 312
Cdd:TIGR01910 237 PGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDV--------VKALSKSDgwLYENEPVVKWSGPNETPP--D 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489196727 313 AELIGLLSGS------TDFSTVAF--GTEGGLFHQAGIPAVICGPGSMDQGHKPDEFVSLAQLE 368
Cdd:TIGR01910 307 SRLVKALEAIikkvrgIEPEVLVStgGTDARFLRKAGIPSIVYGPGDLETAHQVNEYISIKNLV 370
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
6-369 |
1.38e-59 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 197.91 E-value: 1.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVS--RESNLALIDYVRDYLAGFGVDSELFFDADG--RKANLYATIGPSDRGG----VCLSGHTDVVPAD 77
Cdd:PRK08651 10 EFLKDLIKIPTVNppGENYEEIAEFLRDTLEELGFSTEIIEVPNEyvKKHDGPRPNLIARRGSgnphLHFNGHYDVVPPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 78 GQAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFlAAPLRLPVHLAFSYDEEVGCLGVRSLlaaLERRPHKPLL 157
Cdd:PRK08651 90 EGWSVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERL-DPAGDGNIELAIVPDEETGGTGTGYL---VEEGKVTPDY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 158 CIIGEPTELKPV-LGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAVPERHDRRFDPPYS-TVQT 235
Cdd:PRK08651 166 VIVGEPSGLDNIcIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYEYDDERGAKPTvTLGG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 236 GLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAESellprmRAVERSTDIRFTPLSAYPGLLTADDSQ---- 311
Cdd:PRK08651 246 PTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDE------VAPELGIEVEFEITPFSEAFVTDPDSElvka 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 489196727 312 AAELIGLLSGSTDFSTVAFG-TEGGLFHQAGIPAVICGPGSMDQGHKPDEFVSLAQLEA 369
Cdd:PRK08651 320 LREAIREVLGVEPKKTISLGgTDARFFGAKGIPTVVYGPGELELAHAPDEYVEVKDVEK 378
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-370 |
1.69e-52 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349933 [Multi-domain] Cd Length: 355 Bit Score: 178.35 E-value: 1.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSRESN--LALIDYVRDYLAGFGVDSELFfDADGRKANLYATIgPSDRGG--VCLSGHTDVVPA-DGQA 80
Cdd:cd08011 2 KLLQELVQIPSPNPPGDntSAIAAYIKLLLEDLGYPVELH-EPPEEIYGVVSNI-VGGRKGkrLLFNGHYDVVPAgDGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 81 WSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAA--PLRLPVHLAFSYDEE-VGCLGVRSLlaaLERRPHKPLL 157
Cdd:cd08011 80 WTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAkaPWDLPVVLTFVPDEEtGGRAGTKYL---LEKVRIKPND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 158 CIIGEPTELKPV-LGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGArlavperhdrrfdppysTVQTG 236
Cdd:cd08011 157 VLIGEPSGSDNIrIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELEK-----------------TVNPG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 237 LIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAESELLPRMRAVERSTdirFTPLSAYPGLLTADDSQAAELI 316
Cdd:cd08011 220 VIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSIEEVSFEIKSFYS---PTVSNPDSEIVKKTEEAITEVL 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489196727 317 GLLSGsTDFSTVAFgtEGGLFHQAGIPAVICGPGSMDQGHKPDEFVSLAQLEAC 370
Cdd:cd08011 297 GIRPK-EVISVGAS--DARFYRNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKV 347
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
10-370 |
7.75e-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: 160.13 E-value: 7.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 10 DLVAFDTVSR-ESNLAliDYVRDYLAGFGVDSELFFDADGRKANLYATIGPSDRGGVCLSGHTDVVPadgqawsvP--PF 86
Cdd:cd05652 7 SLVEIPSISGnEAAVG--DFLAEYLESLGFTVEKQPVENKDRFNVYAYPGSSRQPRVLLTSHIDTVP--------PfiPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 87 RLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLP--VHLAFSYDEEVGCLGVRSLLAALERRPHkplLCIIGEPT 164
Cdd:cd05652 77 SISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEgdLGLLFVVGEETGGDGMKAFNDLGLNTWD---AVIFGEPT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 165 ELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYaarLIGRLGEIgARLAVPErhDRRFDPpySTVQTGLIQGGRAL 244
Cdd:cd05652 154 ELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEI---LVEALVKL-IDADLPS--SELLGP--TTLNIGRISGGVAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 245 NIVPAECRFDFEVRAlpADDPRQVAEELRDYAESELLPrmravERSTDIRFTplSAYPGLLTADDSQAAELIgllsgstd 324
Cdd:cd05652 226 NVVPAAAEASVAIRL--AAGPPEVKDIVKEAVAGILTD-----TEDIEVTFT--SGYGPVDLDCDVDGFETD-------- 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 489196727 325 fsTVAFGTEgglfhqagIP-------AVICGPGSMDQGHKPDEFVSLAQLEAC 370
Cdd:cd05652 289 --VVAYGTD--------IPylkgdhkRYLYGPGSILVAHGPDEAITVSELEEA 331
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
6-369 |
1.06e-44 |
|
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: 158.05 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSRESNLAlIDYVRDYLAGFGVDSElFFDADGRKaNLYATIGpsdRGG--VCLSGHTDVVPA-DGQAWS 82
Cdd:cd03891 2 ELAKELIRRPSVTPDDAGA-QDLIAERLKALGFTCE-RLEFGGVK-NLWARRG---TGGphLCFAGHTDVVPPgDLEGWS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 83 VPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAF--SYDEE-VGCLGVRSLLAALERRPHKPLLCI 159
Cdd:cd03891 76 SDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFliTSDEEgPAIDGTKKVLEWLKARGEKIDYCI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 160 IGEPTELKpVL------GHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIgarlaVPERHDRRFDPpySTV 233
Cdd:cd03891 156 VGEPTSEK-KLgdtikiGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTAT-----VLDEGNEFFPP--SSL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 234 QTGLIQGG-RALNIVPAECRFDFEVRAlpadDPRQVAEELRDYAESELlprmRAVERSTDIRFTpLSAYP-----GLLTA 307
Cdd:cd03891 228 QITNIDVGnGATNVIPGELKAKFNIRF----NDEHTGESLKARIEAIL----DKHGLDYDLEWK-LSGEPfltkpGKLVD 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489196727 308 DDSQA-AELIGLlsgSTDFSTvAFGTEGGLFHQA-GIPAVICGP--GSMdqgHKPDEFVSLAQLEA 369
Cdd:cd03891 299 AVSAAiKEVTGI---TPELST-SGGTSDARFIASyGCPVVEFGLvnATI---HKVNERVSVADLEK 357
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
8-367 |
1.43e-43 |
|
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: 155.93 E-value: 1.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 8 LADLVAFDTVSRESNLALiDYVRDYLAGFGVDSELF---------------FDADGRKA-NLYATIGPSDRGG--VCLSG 69
Cdd:cd03895 3 LQDLVRFPSLRGEEAAAQ-DLVAAALRSRGYTVDRWeidveklkhhpgfspVAVDYAGApNVVGTHRPRGETGrsLILNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 70 HTDVVPADGQA-WSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLP--VHLAFSYDEEVGCLGVrslLA 146
Cdd:cd03895 82 HIDVVPEGPVElWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAadVHFQSVVEEECTGNGA---LA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 147 ALERrPHKPLLCIIGEPTELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAVPERHDRRF 226
Cdd:cd03895 159 ALMR-GYRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEREWNARKKSHPHF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 227 D--PPYSTVQTGLIQGGRALNIVPAECRFDFEVRALPADDP----RQVAEELRDYAESEllPRMRavERSTDIRFTPLSA 300
Cdd:cd03895 238 SdhPHPINFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPeearREIEECVADAAATD--PWLS--NHPPEVEWNGFQA 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489196727 301 yPGLLTADDSQAAELIG-----LLSGSTDFSTVAFGTEGGLF-HQAGIPAVICGPGSMDQgHKPDEFVSLAQL 367
Cdd:cd03895 314 -EGYVLEPGSDAEQVLAaahqaVFGTPPVQSAMTATTDGRFFvLYGDIPALCYGPGSRDA-HGFDESVDLESL 384
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
6-368 |
2.64e-41 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 148.81 E-value: 2.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSRESNLA---LIDYVRDYLAGFGVdsELFFDADGrKANLYATIGPSDrggVCLSGHTDVVPaDGQAWS 82
Cdd:PRK08737 10 DHLQALVSFDTRNPPRAITtggIFDYLRAQLPGFQV--EVIDHGAG-AVSLYAVRGTPK---YLFNVHLDTVP-DSPHWS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 83 VPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAaplrlPVHLAFSYDEEVG-CLGVRSLLAalerRPHKPLLCIIG 161
Cdd:PRK08737 83 ADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANAGDG-----DAAFLFSSDEEANdPRCVAAFLA----RGIPYEAVLVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 162 EPTELKPVLGHKGKLAMRCEVHGAACHSAYAPQ-GVNAIEYAARLIGRLGEIGARLAvperHDRRFDPPYSTVQTGLIQG 240
Cdd:PRK08737 154 EPTMSEAVLAHRGISSVLMRFAGRAGHASGKQDpSASALHQAMRWGGQALDHVESLA----HARFGGLTGLRFNIGRVEG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 241 GRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAESELlprmraverstdIRFTPLSAYPGLLTADDSQA-------- 312
Cdd:PRK08737 230 GIKANMIAPAAELRFGFRPLPSMDVDGLLATFAGFAEPAA------------ATFEETFRGPSLPSGDIARAeerrlaar 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489196727 313 --AELIGLLSGSTdfstVAFGTEGGLFHQAGIPAVICGPGSMDQGHKPDEFVSLAQLE 368
Cdd:PRK08737 298 dvADALDLPIGNA----VDFWTEASLFSAAGYTALVYGPGDIAQAHTADEFVTLDQLQ 351
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
6-370 |
6.05e-40 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 145.61 E-value: 6.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSRESNLALiDYVRDYL--AGFGVDSELFFDADgrkaNLYATIGpsdRGG--VCLSGHTDVVPA-DGQA 80
Cdd:PRK13009 6 ELAQDLIRRPSVTPDDAGCQ-DLLAERLeaLGFTCERMDFGDVK----NLWARRG---TEGphLCFAGHTDVVPPgDLEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 81 WSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAF---SyDEE-VGCLGVRSLLAALERRPHKPL 156
Cdd:PRK13009 78 WTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFlitS-DEEgPAINGTVKVLEWLKARGEKID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 157 LCIIGEPTELKpVL------GHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGeigarlavperhDRRFD--- 227
Cdd:PRK13009 157 YCIVGEPTSTE-RLgdviknGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELA------------ATEWDegn 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 228 ---PPySTVQTGLIQGG-RALNIVPAECRFDFEVRAlpadDPRQVAEELRDYAESELlprmRAVERSTDIRFTpLSAYPg 303
Cdd:PRK13009 224 effPP-TSLQITNIDAGtGATNVIPGELEAQFNFRF----STEHTAESLKARVEAIL----DKHGLDYTLEWT-LSGEP- 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489196727 304 LLTADDsqaaELIGLLSGS--------TDFSTvAFGTEGGLF-HQAGIPAVICGP--GSMdqgHKPDEFVSLAQLEAC 370
Cdd:PRK13009 293 FLTPPG----KLVDAVVAAieavtgitPELST-SGGTSDARFiADYGAQVVEFGPvnATI---HKVNECVSVADLEKL 362
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
7-364 |
8.94e-40 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 145.03 E-value: 8.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 7 ILADLVAFDTVSR-ESNLAliDYVRDYLAGFGVDSELFFDADGRkANLYATIGpSDRGGVCLSGHTDVVPA-DGQAWSVP 84
Cdd:PRK08588 7 ILADIVKINSVNDnEIEVA--NYLQDLFAKHGIESKIVKVNDGR-ANLVAEIG-SGSPVLALSGHMDVVAAgDVDKWTYD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 85 PFRLSERDGRLYGRGTADMKGYLAcvlAAVPAFLA-----APLRLPVHLAFSYDEEVGCLGVRSL--------LAALerr 151
Cdd:PRK08588 83 PFELTEKDGKLYGRGATDMKSGLA---ALVIAMIElkeqgQLLNGTIRLLATAGEEVGELGAKQLtekgyaddLDAL--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 152 phkpllcIIGEPTELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEyaaRLIGRLGEIGARLAVPERHDRRFDPPys 231
Cdd:PRK08588 157 -------IIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAID---PLLEFYNEQKEYFDSIKKHNPYLGGL-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 232 TVQTGLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAESelLPRMRAVERSTDIrftPLSAYPgLLTADDS- 310
Cdd:PRK08588 225 THVVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINE--VNQNGAAQLSLDI---YSNHRP-VASDKDSk 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 311 --QAAELIG--LLSGSTDFSTVAFGTEGGLFHQAG--IPAVICGPGSMDQGHKPDEFVSL 364
Cdd:PRK08588 299 lvQLAKDVAksYVGQDIPLSAIPGATDASSFLKKKpdFPVIIFGPGNNLTAHQVDEYVEK 358
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-369 |
1.32e-39 |
|
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: 143.99 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 5 RDILADLVAFDTVSR-ESNLAliDYVRDYLAGFGVdselffdADGRKA-NLYATIGPSDRG--GVCLSGHTDVVPAdGQA 80
Cdd:cd05651 3 IELLKSLIATPSFSReEHKTA--DLIENYLEQKGI-------PFKRKGnNVWAENGHFDEGkpTLLLNSHHDTVKP-NAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 81 WSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLA-APLRLPVHLAFSYDEEV-GCLGVRSLLaalerrPHKPLL- 157
Cdd:cd05651 73 WTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSeGPLNYNLIYAASAEEEIsGKNGIESLL------PHLPPLd 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 158 -CIIGEPTELKPVLGHKGKLAMRCEVHGAACHSAYaPQGVNAIEYAARLIGRLgeigarlavperHDRRFD-------PP 229
Cdd:cd05651 147 lAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAAR-NEGDNAIYKALDDIQWL------------RDFRFDkvspllgPV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 230 YSTVQTglIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAESELLPRmraverstDIRFTPlSAYPglLTADD 309
Cdd:cd05651 214 KMTVTQ--INAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLKSEIKPR--------SFRLNS-SAIP--PDHPI 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489196727 310 SQAAELIGLLS-GSTDFSTVAFgtegglfhqAGIPAVICGPGSMDQGHKPDEFVSLAQLEA 369
Cdd:cd05651 281 VQAAIAAGRTPfGSPTLSDQAL---------MPFPSVKIGPGDSSRSHTADEFIELSEIEE 332
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
20-370 |
1.66e-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: 141.85 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 20 ESNLAliDYVRDYLAGFGVDSELFFDADGRKANLYATIGPSDRGGVCLSGHTDVVPADGqaWSVPPFRLSERDGRLYGRG 99
Cdd:cd08013 28 EAEIA--TYVAAWLAHRGIEAHRIEGTPGRPSVVGVVRGTGGGKSLMLNGHIDTVTLDG--YDGDPLSGEIADGRVYGRG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 100 TADMKGYLACVLAAVPAFLAAPLRLPVHLAFSYDEEVGCLGVRSLLAALERRPHkpllCIIGEPTELKPVLGHKGKLAMR 179
Cdd:cd08013 104 TLDMKGGLAACMAALADAKEAGLRGDVILAAVADEEDASLGTQEVLAAGWRADA----AIVTEPTNLQIIHAHKGFVWFE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 180 CEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLavPERHDRRF-DPPysTVQTGLIQGGRALNIVPAECRFDFEVR 258
Cdd:cd08013 180 VDIHGRAAHGSRPDLGVDAILKAGYFLVALEEYQQEL--PERPVDPLlGRA--SVHASLIKGGEEPSSYPARCTLTIERR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 259 ALPADDPRQVAEELRDYAE--SELLPRMRAVERSTDIRFTPLSAypglltADDSQ-----AAELIGLLSGSTDFSTVAFG 331
Cdd:cd08013 256 TIPGETDESVLAELTAILGelAQTVPNFSYREPRITLSRPPFEV------PKEHPfvqlvAAHAAKVLGEAPQIRSETFW 329
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489196727 332 TEGGLFHQAGIPAVICGPGSmdQG-HKPDEFVSLAQLEAC 370
Cdd:cd08013 330 TDAALLAEAGIPSVVFGPSG--AGlHAKEEWVDVESIRQL 367
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
6-367 |
2.32e-38 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 142.48 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVS---RESNlALIDYVRDYL--AGFGVDSELFFDADgrkANLYATIGPSDRG---GVCLSGHTDVVPAD 77
Cdd:PRK08596 17 ELLKTLVRFETPAppaRNTN-EAQEFIAEFLrkLGFSVDKWDVYPND---PNVVGVKKGTESDaykSLIINGHMDVAEVS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 78 G-QAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAFS--YDEEVGCLGVrslLAALERRPHK 154
Cdd:PRK08596 93 AdEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQsvIGEEVGEAGT---LQCCERGYDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 155 PlLCIIGEPTELKpVLGHKGKLAMRCEV------HGAA----CHSAYAPQGVNAIEYAARLIGRLGEIGARLAVPERHDr 224
Cdd:PRK08596 170 D-FAVVVDTSDLH-MQGQGGVITGWITVkspqtfHDGTrrqmIHAGGGLFGASAIEKMMKIIQSLQELERHWAVMKSYP- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 225 RFDPPYSTVQTGLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDY----AESEL-----LPRMR-----AVERS 290
Cdd:PRK08596 247 GFPPGTNTINPAVIEGGRHAAFIADECRLWITVHFYPNETYEQVIKEIEEYigkvAAADPwlrenPPQFKwggesMIEDR 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489196727 291 TDI--RFTPLSAYPGLLTAddSQAAELIGLLSGSTDFSTVAfgTEGGLFHQAGIPAVICGPGSMDQGHKPDEFVSLAQL 367
Cdd:PRK08596 327 GEIfpSLEIDSEHPAVKTL--SSAHESVLSKNAILDMSTTV--TDGGWFAEFGIPAVIYGPGTLEEAHSVNEKVEIEQL 401
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
6-368 |
1.85e-37 |
|
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: 138.49 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSResNLALIDYVRDYLA------GFGVDSElffDADGRKANLYATIGPSDRGGVCLSGHTDVVPADGQ 79
Cdd:cd03885 3 DLLERLVNIESGTY--DKEGVDRVAELLAeelealGFTVERR---PLGEFGDHLIATFKGTGGKRVLLIGHMDTVFPEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 80 AWSVPpfrLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLR--LPVHLAFSYDEEVGCLGVRSLLAALERRPHkplL 157
Cdd:cd03885 78 LAFRP---FTVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRdyLPITVLLNSDEEIGSPGSRELIEEEAKGAD---Y 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 158 CIIGEPTEL--KPVLGHKGKLAMRCEVHGAACHSAYAPQ-GVNAIEYAARLIGRLGEigarLAVPERHdrrfdppySTVQ 234
Cdd:cd03885 152 VLVFEPARAdgNLVTARKGIGRFRLTVKGRAAHAGNAPEkGRSAIYELAHQVLALHA----LTDPEKG--------TTVN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 235 TGLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAESELLPRMRAVERSTDIR--FTPLSAYPGLLTaddsQA 312
Cdd:cd03885 220 VGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTLVPGTSVELTGGLNRppMEETPASRRLLA----RA 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 489196727 313 AELIGLLSGSTDFSTVAFGTEGGLFHQAGIPaVICGPGSMDQG-HKPDEFVSLAQLE 368
Cdd:cd03885 296 QEIAAELGLTLDWEATGGGSDANFTAALGVP-TLDGLGPVGGGaHTEDEYLELDSLV 351
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
8-367 |
1.71e-33 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 128.97 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 8 LADLVAFDTVsRESNLALIDYVRDYLA--GFGVD---------------SELFFDADGRKaNLYATIGPSDRGG--VCLS 68
Cdd:PRK06837 26 TQDLVRFPST-RGAEAPCQDFLARAFRerGYEVDrwsidpddlkshpgaGPVEIDYSGAP-NVVGTYRPAGKTGrsLILQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 69 GHTDVVPAdGQA--WSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRL--PVHLAFSYDEEvgCLGVRSL 144
Cdd:PRK06837 104 GHIDVVPE-GPLdlWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPaaRVHFQSVIEEE--STGNGAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 145 LAALerRPHKPLLCIIGEPTELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAVPERHDR 224
Cdd:PRK06837 181 STLQ--RGYRADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRELEAEWNARKASDP 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 225 RF-DPPYS-TVQTGLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDY-AESELLPRMRAvERSTDIRFTPLSAY 301
Cdd:PRK06837 259 HFeDVPHPiNFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAADAQAEIEAClAAAARDDRFLS-NNPPEVVWSGFLAE 337
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489196727 302 PGLLTadDSQAAELI-----GLLSGSTDFSTVAFGTEGGLFHQ--AGIPAVICGPGSmDQGHKPDEFVSLAQL 367
Cdd:PRK06837 338 GYVLE--PGSEAEAAlarahAAVFGGPLRSFVTTAYTDTRFYGlyYGIPALCYGPSG-EGIHGFDERVDLESV 407
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
6-370 |
3.54e-33 |
|
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: 127.15 E-value: 3.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSRESnLALIDYVRDYLAGFGVDSE-LFFdadGRKANLYATIGPSDRGgVCLSGHTDVVPA-DGQAWSV 83
Cdd:TIGR01246 3 ELAKELISRPSVTPND-AGCQDIIAERLEKLGFEIEwMHF---GDTKNLWATRGTGEPV-LAFAGHTDVVPAgPEEQWSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 84 PPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAF--SYDEEVGCL-GVRSLLAALERRPHKPLLCII 160
Cdd:TIGR01246 78 PPFEPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLliTSDEEGTAIdGTKKVVETLMARDELIDYCIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 161 GEPTELKPV-----LGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIgarlaVPERHDRRFDPpySTVQT 235
Cdd:TIGR01246 158 GEPSSVKKLgdvikNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAI-----KWDEGNEFFPP--TSLQI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 236 GLIQGGR-ALNIVPAECRFDFEVRalpaDDPRQVAEELRDYAESELlprmraveRSTDIRFT---PLSAYPgLLTADD-- 309
Cdd:TIGR01246 231 TNIHAGTgANNVIPGELYVQFNLR----FSTEVSDEILKQRVEAIL--------DQHGLDYDlewSLSGEP-FLTNDGkl 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489196727 310 -SQAAELIGLLSGST-DFSTVAFGTEGGLFHQAGIPAVICGPGSmDQGHKPDEFVSLAQLEAC 370
Cdd:TIGR01246 298 iDKAREAIEETNGIKpELSTGGGTSDGRFIALMGAEVVEFGPVN-ATIHKVNECVSIEDLEKL 359
|
|
| PRK06915 |
PRK06915 |
peptidase; |
67-370 |
1.89e-32 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 126.34 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 67 LSGHTDVVPA-DGQAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLP--VHLAFSYDEEVGCLGVrs 143
Cdd:PRK06915 98 LNGHIDVVPEgDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKgdVIFQSVIEEESGGAGT-- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 144 lLAALErRPHKPLLCIIGEPTELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGArlavpERHD 223
Cdd:PRK06915 176 -LAAIL-RGYKADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEE-----KRND 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 224 RRFDPPYSTV------QTGLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAesELLPRMRA--VERSTDIRF 295
Cdd:PRK06915 249 RITDPLYKGIpipipiNIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWI--AELNDVDEwfVEHPVEVEW 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 296 TPLSAYPGLLTADDsqaaELIGLLSGStdFSTVA----------FGTEGGLFHQAG-IPAVICGPGSMDQGHKPDEFVSL 364
Cdd:PRK06915 327 FGARWVPGELEENH----PLMTTLEHN--FVEIEgnkpiieaspWGTDGGLLTQIAgVPTIVFGPGETKVAHYPNEYIEV 400
|
....*.
gi 489196727 365 AQLEAC 370
Cdd:PRK06915 401 DKMIAA 406
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
5-368 |
4.49e-32 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 123.72 E-value: 4.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 5 RDILADLVAFDTVSRESNlALIDYVRDYLAGFGVDseLFFDADGRKANLYATIGPSdrggVCLSGHTDVVPadgqawsvP 84
Cdd:PRK08652 5 KELLKQLVKIPSPSGQED-EIALHIMEFLESLGYD--VHIESDGEVINIVVNSKAE----LFVEVHYDTVP--------V 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 85 PFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAFSYDEEVGCLGVRSLLaalERRPhkPLLCIIGEPT 164
Cdd:PRK08652 70 RAEFFVDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSDEEEGGRGSALFA---ERYR--PKMAIVLEPT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 165 ELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAvperhdRRFDPPYStVQtgLIQGGRAL 244
Cdd:PRK08652 145 DLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALG------KYFDPHIG-IQ--EIIGGSPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 245 NIVPAECRFDFEVRALPAddprqvaEELRDyAESELLPRMRAVErstdIRFTPLSAYPGLLTADDSQAAELIGLLSGST- 323
Cdd:PRK08652 216 YSIPALCRLRLDARIPPE-------VEVED-VLDEIDPILDEYT----VKYEYTEIWDGFELDEDEEIVQLLEKAMKEVg 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 489196727 324 ---DFSTVAFGTEGGLFHQAGIPAVICGPGSMDQGHKPDEFVSLAQLE 368
Cdd:PRK08652 284 lepEFTVMRSWTDAINFRYNGTKTVVWGPGELDLCHTKFERIDVREVE 331
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-370 |
1.98e-31 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 122.53 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 7 ILADLVAFDTVSRESNlALIDYVRDYLAGFGVDsELFFDADGrkaNLYATIGPSDRGgVCLSGHTDVVP-ADGQAWSVPP 85
Cdd:cd05649 3 FLRDLIQIPSESGEEK-GVVERIEEEMEKLGFD-EVEIDPMG---NVIGYIGGGKKK-ILFDGHIDTVGiGNIDNWKFDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 86 FRLSERDGRLYGRGTADMKGYLACVLAAVPAFlaAPLRLP-----VHLAFSYDEEVgCLGV--RSLLAALERRPHkplLC 158
Cdd:cd05649 77 YEGYETDGKIYGRGTSDQKGGLASMVYAAKIM--KDLGLRdfaytILVAGTVQEED-CDGVcwQYISKADKIKPD---FV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 159 IIGEPTELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAvperhDRRFDPPYSTVQTGLI 238
Cdd:cd05649 151 VSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFP-----EAPFLGRGTLTVTDIF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 239 QGGRALNIVPAECRFDFEVRALPADDPRQVAEELRD------YAESELLPRMRAVERS-TDIRFTPLSAYPGLLTADDS- 310
Cdd:cd05649 226 STSPSRCAVPDSCRISIDRRLTVGETWEGCLEEIRAlpavkkYGDDVAVSMYNYDRPSyTGEVYESERYFPTWLLPEDHe 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489196727 311 --QAAE--LIGLLSGSTDFSTVAFGTEGGLFH-QAGIPAVICGPGSMDQGHKPDEFVSLAQLEAC 370
Cdd:cd05649 306 lvKALLeaYKALFGARPLIDKWTFSTNGVSIMgRAGIPCIGFGPGAENQAHAPNEYTWKEDLVRC 370
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
6-370 |
8.94e-31 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 121.20 E-value: 8.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVS-RESNLALIdyVRDYLAGFGVDsELFFDADGrkaNLYATIGPSDRGgVCLSGHTDVVPA-DGQAWSV 83
Cdd:PRK13004 19 RFLRDLIRIPSESgDEKRVVKR--IKEEMEKVGFD-KVEIDPMG---NVLGYIGHGKKL-IAFDAHIDTVGIgDIKNWDF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 84 PPFRLSERDGRLYGRGTADMKGYLACVLAAVPAF--LAAPLRLPVHLAFSYDEEVgCLGV--RSLLaalERRPHKPLLCI 159
Cdd:PRK13004 92 DPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIkdLGLDDEYTLYVTGTVQEED-CDGLcwRYII---EEDKIKPDFVV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 160 IGEPTELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARL--------AVPERHDRRFDPPys 231
Cdd:PRK13004 168 ITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNLkedpflgkGTLTVSDIFSTSP-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 232 tvqtgliqgGRalNIVPAECRFDFEVRALPADDPRQVAEELRDYAESellPRMRA-VERSTDIR--FTPLSA-----YPG 303
Cdd:PRK13004 246 ---------SR--CAVPDSCAISIDRRLTVGETWESVLAEIRALPAV---KKANAkVSMYNYDRpsYTGLVYptecyFPT 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489196727 304 LLTADDS---QAAE--LIGLLSGSTDFSTVAFGTEG----GlfhQAGIPAVICGPGSMDQGHKPDEFVSLAQLEAC 370
Cdd:PRK13004 312 WLYPEDHefvKAAVeaYKGLFGKAPEVDKWTFSTNGvsiaG---RAGIPTIGFGPGKEPLAHAPNEYTWKEQLVKA 384
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
7-370 |
3.60e-30 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 118.70 E-value: 3.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 7 ILADLVAFDTVSR-ESNLAliDYVRDYLAGFGvDSELFFDADgrkaNLYAT--IGPSDRggVCLSGHTDVVPADGqawSV 83
Cdd:cd05647 4 LTAALVDIPSVSGnEKPIA--DEIEAALRTLP-HLEVIRDGN----TVVARteRGLASR--VILAGHLDTVPVAG---NL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 84 PPFRlsERDGRLYGRGTADMKGYLAcVLAAVPAFLAAPlRLPVHLAF-SYDEEvgclGVRSLLAALER--RPHKPLL--- 157
Cdd:cd05647 72 PSRV--EEDGVLYGCGATDMKAGDA-VQLKLAATLAAA-TLKHDLTLiFYDCE----EVAAELNGLGRlaEEHPEWLaad 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 158 -CIIGEPTELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAVPERHDRRfdppySTVQTG 236
Cdd:cd05647 144 fAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLAAYEPRTVNIDGLTYR-----EGLNAV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 237 LIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAESEllprmraverSTDIRFTPLS--AYPGLltaDDSQAAE 314
Cdd:cd05647 219 FISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGL----------GYEIEVTDLSpgALPGL---DHPVARD 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489196727 315 LIGLLSGS-------TDFSTvafgtegglFHQAGIPAVICGPGSMDQGHKPDEFVSLAQLEAC 370
Cdd:cd05647 286 LIEAVGGKvrakygwTDVAR---------FSALGIPAVNFGPGDPLLAHKRDEQVPVEQITAC 339
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
5-368 |
2.65e-29 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 115.91 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 5 RDILADLVAFDTVSRESNLAlIDYVRDYLAGFGVdsELFFDADGrkaNLYATIGPSDRGgVCLSGHTDVVPADgqawsVP 84
Cdd:cd05653 4 VELLLDLLSIYSPSGEEARA-AKFLEEIMKELGL--EAWVDEAG---NAVGGAGSGPPD-VLLLGHIDTVPGE-----IP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 85 PfRLSErdGRLYGRGTADMKGYLACVLAAVpAFLAAPLRLPVHLAFSYDEEVGCLGVRSLLaaleRRPHKPLLCIIGEPT 164
Cdd:cd05653 72 V-RVEG--GVLYGRGAVDAKGPLAAMILAA-SALNEELGARVVVAGLVDEEGSSKGARELV----RRGPRPDYIIIGEPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 165 ELKPV-LGHKGKLAM--RCEVHGAacHSAYApqGVNAIEyaaRLIGRLGEIGARLAVPERHDRRFDppysTVQTGLIQGG 241
Cdd:cd05653 144 GWDGItLGYRGSLLVkiRCEGRSG--HSSSP--ERNAAE---DLIKKWLEVKKWAEGYNVGGRDFD----SVVPTLIKGG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 242 RALNIVPAECRFDFEVR---ALPADDPRQVAEELRDYAESELLPRMRAVErsTDIRfTPLSAypGLLTADDSQAAE-LIG 317
Cdd:cd05653 213 ESSNGLPQRAEATIDLRlppRLSPEEAIALATALLPTCELEFIDDTEPVK--VSKN-NPLAR--AFRRAIRKQGGKpRLK 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489196727 318 LLSGSTDFSTVAfgtegglfHQAGIPAVICGPGSMDQGHKPDEFVSLAQLE 368
Cdd:cd05653 288 RKTGTSDMNVLA--------PLWTVPIVAYGPGDSTLDHTPNEHIELAEIE 330
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
170-284 |
9.66e-29 |
|
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: 107.82 E-value: 9.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 170 LGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEigarlavpERHDRRFDPPYSTVQTGLIQGGRALNIVPA 249
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPA--------EYGDIGFDFPRTTLNITGIEGGTATNVIPA 72
|
90 100 110
....*....|....*....|....*....|....*
gi 489196727 250 ECRFDFEVRALPADDPRQVAEELRDYAESELLPRM 284
Cdd:pfam07687 73 EAEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
5-368 |
8.96e-28 |
|
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: 113.22 E-value: 8.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 5 RDILADLVAFDTVSRESNL----ALIDYVRDYL--AGFGVDSELFFDADGRkANLYATIGPSD--RGGVCLSGHTDVVPA 76
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTgsetRAAEVLAARLaeAGIQTEIFVVESHPGR-ANLVARIGGTDpsAGPLLLLGHIDVVPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 77 DGQAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRL--PVHLAFSYDEEV-GCLGVRSLLAAlerrpH 153
Cdd:cd05675 80 DASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPkrDLVFAFVADEEAgGENGAKWLVDN-----H 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 154 KPLL-----CI---------IGEPTELKPV-LGHKGKLAMRCEVHGAACHSAyAPQGVNAIeyaARLIGRLGEIGARLAV 218
Cdd:cd05675 155 PELFdgatfALneggggslpVGKGRRLYPIqVAEKGIAWMKLTVRGRAGHGS-RPTDDNAI---TRLAEALRRLGAHNFP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 219 PERHDR--------RFDPPY--------------------------------STVQTGLiQGGRALNIVPAECRFDFEVR 258
Cdd:cd05675 231 VRLTDEtayfaqmaELAGGEggalmltavpvldpalaklgpsapllnamlrnTASPTML-DAGYATNVLPGRATAEVDCR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 259 ALPADDPRQVAEELRDYAES-----ELLPRMRAVERSTDIR-FTPLSAypgLLTADDSQAAELIGLLSGSTD---FSTVA 329
Cdd:cd05675 310 ILPGQSEEEVLDTLDKLLGDpdvsvEAVHLEPATESPLDSPlVDAMEA---AVQAVDPGAPVVPYMSPGGTDakyFRRLG 386
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 489196727 330 FGTEG--GLFHQAGIpavicgpGSMDQGHKPDEFVSLAQLE 368
Cdd:cd05675 387 IPGYGfaPLFLPPEL-------DYTGLFHGVDERVPVESLY 420
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
6-370 |
2.01e-27 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 111.30 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSREsNLALIDYVRDYLAGFGVDSELffDADGrkaNLYATIgPSDRG----GVCLSGHTDVVP---ADG 78
Cdd:COG2195 7 ERFLEYVKIPTPSDH-EEALADYLVEELKELGLEVEE--DEAG---NVIATL-PATPGynvpTIGLQAHMDTVPqfpGDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 79 qawsVPPFRlseRDGRLYGRGT----ADMKGYLACVLAAVpAFLAAPlRLPvH----LAFSYDEEVGCLGVR----SLLA 146
Cdd:COG2195 80 ----IKPQI---DGGLITADGTttlgADDKAGVAAILAAL-EYLKEP-EIP-HgpieVLFTPDEEIGLRGAKaldvSKLG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 147 AlerrphKPLLCIIGEPTelkpvlghkGKLAMRC--------EVHGAACHSAYAP-QGVNAIEYAARLIGRLgeigARLA 217
Cdd:COG2195 150 A------DFAYTLDGGEE---------GELEYECagaadakiTIKGKGGHSGDAKeKMINAIKLAARFLAAL----PLGR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 218 VPERHDRRFdppystvqtGLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAESELlprmRAVERSTdIRFTP 297
Cdd:COG2195 211 IPEETEGNE---------GFIHGGSATNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEEN----AKYGVGV-VEVEI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 298 LSAYPGLLTADDS-------QAAELIGLlsgstDFSTVAF--GTEGGLFHQAGIPAVICGPGsMDQGHKPDEFVSLAQLE 368
Cdd:COG2195 277 EDQYPNWKPEPDSpivdlakEAYEELGI-----EPKIKPIrgGLDGGILSFKGLPTPNLGPG-GHNFHSPDERVSIESME 350
|
..
gi 489196727 369 AC 370
Cdd:COG2195 351 KA 352
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
65-367 |
2.89e-26 |
|
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: 108.41 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 65 VCLSGHTDVVPAdGQAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAF--LAAPLRLPVHLAFSYDEEVG-CLGV 141
Cdd:cd02697 76 VALNAHGDVVPP-GDGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALesLGAPLRGAVELHFTYDEEFGgELGP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 142 RSLLAALERRPHkpLLCIIGEPTELkpVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAVPER 221
Cdd:cd02697 155 GWLLRQGLTKPD--LLIAAGFSYEV--VTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNAQYRQVSS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 222 HDRRFDPPYSTVqtGLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAEsELLPRMRAVerSTDIR------- 294
Cdd:cd02697 231 QVEGITHPYLNV--GRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIA-DAAASMPGI--SVDIRrlllans 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489196727 295 FTPLSAYPGLLTADDSQAAELIGLLSGSTDfstVAFGTEGGLFHQAGIPAVICGPGSM----DQGHKPDEFVSLAQL 367
Cdd:cd02697 306 MRPLPGNAPLVEAIQTHGEAVFGEPVPAMG---TPLYTDVRLYAEAGIPGVIYGAGPRtvleSHAKRADERLQLEDL 379
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
6-367 |
5.29e-25 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 104.93 E-value: 5.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSRESN----LALIDYVRDYLAGFGVDSELFFDA------DGRKANLYATI-GPSDRGGVCLSGHTDVV 74
Cdd:PRK13983 9 ELLSELIAIPAVNPDFGgegeKEKAEYLESLLKEYGFDEVERYDApdprviEGVRPNIVAKIpGGDGKRTLWIISHMDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 75 PA-DGQAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLP--VHLAFSYDEEVGCL-GVRSLLAAlER 150
Cdd:PRK13983 89 PPgDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKynLGLAFVSDEETGSKyGIQYLLKK-HP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 151 RPHKPLLCII----GEPTELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEigaRL--AVPERhDR 224
Cdd:PRK13983 168 ELFKKDDLILvpdaGNPDGSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRAAADFALELDE---ALheKFNAK-DP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 225 RFDPPYSTVQ-TGLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAESellprmraVERSTDIRFT-----PL 298
Cdd:PRK13983 244 LFDPPYSTFEpTKKEANVDNINTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIADE--------FEEEYGVKIEveivqRE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489196727 299 SAYPGllTADDSQAAEL----IGLLSGstdFSTVAFGTEGG----LFHQAGIPAVICGPGsMDQGHKPDEFVSLAQL 367
Cdd:PRK13983 316 QAPPP--TPPDSEIVKKlkraIKEVRG---IEPKVGGIGGGtvaaFLRKKGYPAVVWSTL-DETAHQPNEYAKISNL 386
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
58-368 |
1.83e-24 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 103.69 E-value: 1.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 58 GPSDRGGVCLSGHTDVVPAdGQAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLP--VHLAFSYDEE 135
Cdd:PRK13013 80 GARDGDCVHFNSHHDVVEV-GHGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAgsIEISGTADEE 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 136 VGCLGVRSLLAALER-RPHKPLLCIIGEPTELKPV-LGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLigrLGEIG 213
Cdd:PRK13013 159 SGGFGGVAYLAEQGRfSPDRVQHVIIPEPLNKDRIcLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAV---LAEIE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 214 ARLaVPERHDRRFDPP-------YSTVQTGLIQGGRALN----------IVPAECRFDFEVRALPADDPRQVAEELRDya 276
Cdd:PRK13013 236 ERL-FPLLATRRTAMPvvpegarQSTLNINSIHGGEPEQdpdytglpapCVADRCRIVIDRRFLIEEDLDEVKAEITA-- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 277 eseLLPRMRAVERSTDIRFTPLSAYPGLLTADD-----SQAAELIGLLSGSTDFsTVAFGT--EGGLFHQAGIPAVIC-G 348
Cdd:PRK13013 313 ---LLERLKRARPGFAYEIRDLFEVLPTMTDRDapvvrSVAAAIERVLGRQADY-VVSPGTydQKHIDRIGKLKNCIAyG 388
|
330 340
....*....|....*....|
gi 489196727 349 PGSMDQGHKPDEFVSLAQLE 368
Cdd:PRK13013 389 PGILDLAHQPDEWVGIADMV 408
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
8-368 |
3.85e-24 |
|
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: 102.79 E-value: 3.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 8 LADLVAFDTVS-----RESNLALIDYVRDYLAGFGVDSELFFDADGRKAnLYATI-GPSDRGGVCLSGHTDVVPADGQA- 80
Cdd:cd03893 4 LAELVAIPSVSaqpdrREELRRAAEWLADLLRRLGFTVEIVDTSNGAPV-VFAEFpGAPGAPTVLLYGHYDVQPAGDEDg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 81 WSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAFSYD--EEVGCLGVRSLLAAlerrpHKPLL- 157
Cdd:cd03893 83 WDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEgeEESGSPSLDQLVEA-----HRDLLa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 158 ---CIIGEPTEL---KPVL--GHKGKLAMRCEVHGAA--CHSAYApQGV--NAIEYAARLIGRLGEIGARLAVPERHDRR 225
Cdd:cd03893 158 adaIVISDSTWVgqeQPTLtyGLRGNANFDVEVKGLDhdLHSGLY-GGVvpDPMTALAQLLASLRDETGRILVPGLYDAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 226 FDPPYSTVQT----------------------------------GLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEE 271
Cdd:cd03893 237 RELPEEEFRLdagvleeveiiggttgsvaerlwtrpaltvlgidGGFPGEGSKTVIPPRARAKISIRLVPGQDPEEASRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 272 LRDYAES------ELLPRMRAVERSTDirfTPLSAYPGLLTADDSQAA----ELIGLLSGStdfstVAFGTEGGLFHQAg 341
Cdd:cd03893 317 LEAHLEKhapsgaKVTVSYVEGGMPWR---SDPSDPAYQAAKDALRTAygvePPLTREGGS-----IPFISVLQEFPQA- 387
|
410 420
....*....|....*....|....*...
gi 489196727 342 iPAVICGPGSMD-QGHKPDEFVSLAQLE 368
Cdd:cd03893 388 -PVLLIGVGDPDdNAHSPNESLRLGNYK 414
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
6-275 |
1.09e-23 |
|
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: 101.65 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSRESN--LALIDYVRDYLAGFGVDSELFfDADGRKAnLYATIGPSDRGGVCLSGHTDVVPADG-QAWS 82
Cdd:cd05681 3 EDLRDLLKIPSVSAQGRgiPETADFLKEFLRRLGAEVEIF-ETDGNPI-VYAEFNSGDAKTLLFYNHYDVQPAEPlELWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 83 VPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAFSYD--EEVGCLGVRSLLAAlerrpHKPLL--- 157
Cdd:cd05681 81 SDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEgeEEVGSPNLEKFVAE-----HADLLkad 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 158 -CII---GEPTELKP--VLGHKGKLAMRCEVHGAA--CHSAYAPQGVNAIEYAARLIGRLGEIGARLAVPERHDR----- 224
Cdd:cd05681 156 gCIWeggGKNPKGRPqiSLGVKGIVYVELRVKTADfdLHSSYGAIVENPAWRLVQALNSLRDEDGRVLIPGFYDDvrpls 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 225 ----------RFDP---------------------------PYSTVQtGLI---QGGRALNIVPAECRFDFEVRALPADD 264
Cdd:cd05681 236 eaeralidtyDFDPeelrktyglkrplqvegkdplralftePTCNIN-GIYsgyTGEGSKTILPSEAFAKLDFRLVPDQD 314
|
330
....*....|.
gi 489196727 265 PRQVAEELRDY 275
Cdd:cd05681 315 PAKILSLLRKH 325
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
5-304 |
1.31e-23 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 102.00 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 5 RDILADLVAFDTV-SRESNLALIDYVRDYL--AGFGVDSELFFDADGRKANLYATIGPSDRGG-VCLSGHTDVVPADGQA 80
Cdd:PRK09133 40 RDLYKELIEINTTaSTGSTTPAAEAMAARLkaAGFADADIEVTGPYPRKGNLVARLRGTDPKKpILLLAHMDVVEAKRED 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 81 WSVPPFRLSERDGRLYGRGTADMKgylacvlAAVPAFLAAPLRL---------PVHLAFSYDEEVGclGVRSLLAALERR 151
Cdd:PRK09133 120 WTRDPFKLVEENGYFYGRGTSDDK-------ADAAIWVATLIRLkregfkpkrDIILALTGDEEGT--PMNGVAWLAENH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 152 PH--KPLLCII----GEPTEL-KPVL-----GHKGKLAMRCEVHGAACHSAyAPQGVNAIEYAARLIGRLG--------- 210
Cdd:PRK09133 191 RDliDAEFALNegggGTLDEDgKPVLltvqaGEKTYADFRLEVTNPGGHSS-RPTKDNAIYRLAAALSRLAayrfpvmln 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 211 -------EIGARLAVPERHD--RRF---------------DPPY-STVQT----GLIQGGRALNIVPAECRFDFEVRALP 261
Cdd:PRK09133 270 dvtrayfKQSAAIETGPLAAamRAFaanpadeaaiallsaDPSYnAMLRTtcvaTMLEGGHAENALPQRATANVNCRIFP 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489196727 262 ADDPRQVAEELRDY-----------------AESELLPR-MRAVERSTDIRftplsaYPGL 304
Cdd:PRK09133 350 GDTIEAVRATLKQVvadpaikitrigdpspsPASPLRPDiMKAVEKLTAAM------WPGV 404
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
27-361 |
1.25e-22 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 98.30 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 27 DYVRDYLAGFGVDSELFFDA-DGR---KANLYATIGPSDRGGVCLSGHTDVVP-ADGQAWSVPPFRLSERDGRLYGRGTA 101
Cdd:cd05650 30 DYLEKKLREYGFYTLERYDApDERgiiRPNIVAKIPGGNDKTLWIISHLDTVPpGDLSLWETDPWEPVVKDGKIYGRGVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 102 DMKGYLACVLAAVPAFLAAPLRlPVH---LAFSYDEEVGC-LGVRSLLAALERRPHKPLLCI--IGEPTELKPVLGHKGK 175
Cdd:cd05650 110 DNQQGIVSSLLALKAIIKNGIT-PKYnfgLLFVADEEDGSeYGIQYLLNKFDLFKKDDLIIVpdFGTEDGEFIEIAEKSI 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 176 LAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAvpERHDRRFDPPYSTVQ-TGLIQGGRALNIVPAECRFD 254
Cdd:cd05650 189 LWIKVNVKGKQCHASTPENGINAFVAASNFALELDELLHEKF--DEKDDLFNPPYSTFEpTKKEANVPNVNTIPGYDVFY 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 255 FEVRALPADDPRQVAEELRDYAESELLPRMRAVERSTDIRFTPLSAYPglltaddsQAAELIGLLSGS--------TDFS 326
Cdd:cd05650 267 FDCRVLPTYKLDEVLKFVNKIISDFENSYGAGITYEIVQKEQAPPATP--------EDSEIVVRLSKAikkvrgreAKLI 338
|
330 340 350
....*....|....*....|....*....|....*
gi 489196727 327 TVAFGTEGGLFHQAGIPAVICGPGsMDQGHKPDEF 361
Cdd:cd05650 339 GIGGGTVAAFLRKKGYPAVVWSTL-DETAHQPNEY 372
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
5-368 |
2.37e-22 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 96.56 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 5 RDILADLVAFDTVSRESNlALIDYVRDYLAGFGVDSelFFDADGRkanlyaTIGPSDRGG--VCLSGHTDVVPADgqaws 82
Cdd:PRK04443 9 RELLKGLVEIPSPSGEEA-AAAEFLVEFMESHGREA--WVDEAGN------ARGPAGDGPplVLLLGHIDTVPGD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 83 vPPFRLseRDGRLYGRGTADMKGYLACVLAAVpAFLAAPLRLPVHLAFSYDEEVGCLGVRSLLAalERrpHKPLLCIIGE 162
Cdd:PRK04443 75 -IPVRV--EDGVLWGRGSVDAKGPLAAFAAAA-ARLEALVRARVSFVGAVEEEAPSSGGARLVA--DR--ERPDAVIIGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 163 PTELKPV-LGHKGKLAMRCEVHGAACHSAYapQGVNAIEyaaRLIGRLGEIGARLAVPERHDRRFDppysTVQTGLiqgg 241
Cdd:PRK04443 147 PSGWDGItLGYKGRLLVTYVATSESFHSAG--PEPNAAE---DAIEWWLAVEAWFEANDGRERVFD----QVTPKL---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 242 RALNIVPA----ECRFDFEVRALPADDPRQVAEELRDYAESELLPRMRAVERSTDIRFTPLSAypGLLTADDSQAAELIG 317
Cdd:PRK04443 214 VDFDSSSDgltvEAEMTVGLRLPPGLSPEEAREILDALLPTGTVTFTGAVPAYMVSKRTPLAR--AFRVAIREAGGTPRL 291
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489196727 318 LL-SGSTDFSTVAfgtegGLFhqaGIPAVICGPGSMDQGHKPDEFVSLAQLE 368
Cdd:PRK04443 292 KRkTGTSDMNVVA-----PAW---GCPMVAYGPGDSDLDHTPDEHLPLAEYL 335
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
6-137 |
9.59e-22 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 96.07 E-value: 9.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSR-------ESNLAliDYVRDYLAGFGVDSELFFDADGRkANLYATIGPSD--RGGVCLSGHTDVVPA 76
Cdd:PRK07906 3 DLCSELIRIDTTNTgdgtgkgEREAA--EYVAEKLAEVGLEPTYLESAPGR-ANVVARLPGADpsRPALLVHGHLDVVPA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489196727 77 DGQAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLP--VHLAFSYDEEVG 137
Cdd:PRK07906 80 EAADWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPrdLVFAFVADEEAG 142
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
8-147 |
3.53e-21 |
|
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: 94.59 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 8 LADLVAFDTVS-----RESNLALIDYVRDYLAGFGVDSELFF-----DADGRKANL----YATIGPS-DRGGVCLSGHTD 72
Cdd:cd05676 16 LREAVAIQSVSadpekRPELIRMMEWAAERLEKLGFKVELVDigtqtLPDGEELPLppvlLGRLGSDpSKKTVLIYGHLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 73 VVPA---DGqaWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAFSYD--EEVGCLGVRSLLAA 147
Cdd:cd05676 96 VQPAkleDG--WDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEgmEESGSEGLDELIEA 173
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
45-369 |
3.36e-20 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 91.18 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 45 DADGRKA------NLYATIGPSDRGGVCLSGHTDVV-PADGqawsvpPFR-LSER-DGRLYGRGTADMKGYLACVLAAVP 115
Cdd:PRK07338 69 DADGRTLeqahgpALHVSVRPEAPRQVLLTGHMDTVfPADH------PFQtLSWLdDGTLNGPGVADMKGGIVVMLAALL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 116 AFLAAPL--RLPVHLAFSYDEEVGCLGVRSLLAALERRPHKPLlciIGEPTELKPVLGH--KGKLAMRCEVHGAACHSAY 191
Cdd:PRK07338 143 AFERSPLadKLGYDVLINPDEEIGSPASAPLLAELARGKHAAL---TYEPALPDGTLAGarKGSGNFTIVVTGRAAHAGR 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 192 APQ-GVNAIEYAARLIGRLgeigarlavperHDRRFDPPYSTVQTGLIQGGRALNIVP--AECRFDFEVRaLPADdprqv 268
Cdd:PRK07338 220 AFDeGRNAIVAAAELALAL------------HALNGQRDGVTVNVAKIDGGGPLNVVPdnAVLRFNIRPP-TPED----- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 269 aeelRDYAESELLPRMRAVERSTDIRFT----------PLSAYPGLLTADDSQAAELIGLlsgSTDFSTVAFGTEGGLFH 338
Cdd:PRK07338 282 ----AAWAEAELKKLIAQVNQRHGVSLHlhggfgrppkPIDAAQQRLFEAVQACGAALGL---TIDWKDSGGVCDGNNLA 354
|
330 340 350
....*....|....*....|....*....|....*...
gi 489196727 339 QAGIPaVICGPGSMDQG-HKPDEFVSL------AQLEA 369
Cdd:PRK07338 355 AAGLP-VVDTLGVRGGNiHSEDEFVILdslverAQLSA 391
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
1-147 |
5.72e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 91.12 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 1 MPGSRDILADLVAFDTVS-----RESNLALIDYVRDYLAGFGVDSELFFDADGRKANLYATIGPSDRGGVCLSGHTDVVP 75
Cdd:PRK07907 17 LPRVRADLEELVRIPSVAadpfrREEVARSAEWVADLLREAGFDDVRVVSADGAPAVIGTRPAPPGAPTVLLYAHHDVQP 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489196727 76 A-DGQAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAaplRLPVHLAFSYD--EEVGCLGVRSLLAA 147
Cdd:PRK07907 97 PgDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRALGG---DLPVGVTVFVEgeEEMGSPSLERLLAE 168
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
27-367 |
1.72e-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.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 89.29 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 27 DYVRDYLAGFGVDSELFFDADGRKANLYATIGPSDRGGVCLSGHTDVVPADG-QAWSVPPFRLSERDGRLYGRGTADMKG 105
Cdd:cd05680 28 EWLADKLTEAGFEHTEVLPTGGHPLVYAEWLGAPGAPTVLVYGHYDVQPPDPlELWTSPPFEPVVRDGRLYARGASDDKG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 106 YLACVLAAVPAFLAAPLRLPVHLAFSYD--EEVGCLGVRSLLAAlerrpHKPLL----CIIGEPTELKPVL-----GHKG 174
Cdd:cd05680 108 QVFIHIKAVEAWLAVEGALPVNVKFLIEgeEEIGSPSLPAFLEE-----NAERLaadvVLVSDTSMWSPDTptityGLRG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 175 KLAMRCEVHGAA--CHSA-YAPQGVNAIEYAARLIGRLGEIGARLAVPERHDRRFDPP---------------------- 229
Cdd:cd05680 183 LAYLEISVTGPNrdLHSGsYGGAVPNPANALARLLASLHDEDGRVAIPGFYDDVRPLTdaereawaalpfdeaafkaslg 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 230 ---------YSTVQ-------------TGLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAESELLPRMRav 287
Cdd:cd05680 263 vpalggeagYTTLErlwarptldvngiWGGYQGEGSKTVIPSKAHAKISMRLVPGQDPDAIADLLEAHLRAHAPPGVT-- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 288 erstdIRFTPLSAYPGLLTADDS---QAAEligllsgstDFSTVAFGTE------GG------LFHQA-GIPAVICGPGS 351
Cdd:cd05680 341 -----LSVKPLHGGRPYLVPTDHpalQAAE---------RALEEAFGKPpvfvreGGsipivaLFEKVlGIPTVLMGFGL 406
|
410
....*....|....*..
gi 489196727 352 MDQG-HKPDEFVSLAQL 367
Cdd:cd05680 407 PDDAiHAPNEKFRLECF 423
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
52-165 |
6.72e-19 |
|
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: 84.02 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 52 NLYATIGPS-DRGGVCLSGHTDVVPA-DGQAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLP--VH 127
Cdd:cd18669 1 NVIARYGGGgGGKRVLLGAHIDVVPAgEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKgtVV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 489196727 128 LAFSYDEEVGCLGVRSLLAALERRPHKPL-LCIIGEPTE 165
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLSKDALEEDLKVdYLFVGDATP 119
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
24-362 |
6.77e-19 |
|
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: 87.15 E-value: 6.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 24 ALIDYVRDYLAGFGVDSelfFDADGRkANLYATI-GPSDRGGVCLSGHTDVVPADGQAWSVppfrlSERDGRLYGRGTAD 102
Cdd:cd03896 19 ARADLVAEWMADLGLGD---VERDGR-GNVVGRLrGTGGGPALLFSAHLDTVFPGDTPATV-----RHEGGRIYGPGIGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 103 MKGYLACVLAAVPAFLAAPLRLPVHLAFSY---DEEVGCL-GVRSLLAAlerrpHKPLL--CIIGEPTELKPVLGHKGKL 176
Cdd:cd03896 90 NKGSLACLLAMARAMKEAGAALKGDVVFAAnvgEEGLGDLrGARYLLSA-----HGARLdyFVVAEGTDGVPHTGAVGSK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 177 AMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAvperhdrrfdpPYSTVQTGLIQGGRALNIVPAECRFDFE 256
Cdd:cd03896 165 RFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAPYV-----------PKTTFAAIRGGGGTSVNRIANLCSMYLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 257 VRALPADDPRQVAEELRDyaeseLLPRMRAVERSTDIRFTPLSAYPGLLTADDSQ-------AAELIGLlsgstDFSTVA 329
Cdd:cd03896 234 IRSNPDAELADVQREVEA-----VVSKLAAKHLRVKARVKPVGDRPGGEAQGTEPlvnaavaAHREVGG-----DPRPGS 303
|
330 340 350
....*....|....*....|....*....|...
gi 489196727 330 FGTEGGLFHQAGIPAVICGPGSMDQGHKPDEFV 362
Cdd:cd03896 304 SSTDANPANSLGIPAVTYGLGRGGNAHRGDEYV 336
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
6-364 |
3.18e-18 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 85.45 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSR-ESNLALI-DYVRDYLAGFGVDSELFFDADGRKANLYATIGPSDRGGVCLSGHTDVVPADGQAwSV 83
Cdd:PRK06133 41 DTLKELVSIESGSGdAEGLKQVaALLAERLKALGAKVERAPTPPSAGDMVVATFKGTGKRRIMLIAHMDTVYLPGML-AK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 84 PPFRlsERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLR----LPVhlAFSYDEEVGCLGVRSLLAALERRPHKPLLCi 159
Cdd:PRK06133 120 QPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKdygtLTV--LFNPDEETGSPGSRELIAELAAQHDVVFSC- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 160 igEPTELKP--VLGHKGKLAMRCEVHGAACHSAYAP-QGVNAIEYAARLIGRLGEIGarlavperhdrrfDP-PYSTVQT 235
Cdd:PRK06133 195 --EPGRAKDalTLATSGIATALLEVKGKASHAGAAPeLGRNALYELAHQLLQLRDLG-------------DPaKGTTLNW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 236 GLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAESELLPRMRaVERSTDIRFTPLSAYPGlltADD--SQAA 313
Cdd:PRK06133 260 TVAKAGTNRNVIPASASAQADVRYLDPAEFDRLEADLQEKVKNKLVPDTE-VTLRFERGRPPLEANAA---SRAlaEHAQ 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489196727 314 ELIGLLSGSTDFSTVAFG--TEGGLFHQAGIPAVICGPGSMDQG-HKPDEFVSL 364
Cdd:PRK06133 336 GIYGELGRRLEPIDMGTGggTDAAFAAGSGKAAVLEGFGLVGFGaHSNDEYIEL 389
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
6-137 |
1.11e-17 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 84.05 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTV---------SRESNlaliDYVRDYLAGFGVDSELFfDADGRKAnLYATIGpSDRGGVCLSGHTDVVPA 76
Cdd:PRK08554 5 ELLSSLVSFETVndpskgikpSKECP----KFIKDTLESWGIESELI-EKDGYYA-VYGEIG-EGKPKLLFMAHFDVVPV 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489196727 77 DGQAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAFSYDEEVG 137
Cdd:PRK08554 78 NPEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLNGKVIFAFTGDEEIG 138
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
67-209 |
2.99e-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: 83.07 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 67 LSGHTDVVPA-DGQA--WSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAA---PLRlPVHLAFSYDEEV-GCL 139
Cdd:cd05674 74 LMAHQDVVPVnPETEdqWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRgfkPRR-TIILAFGHDEEVgGER 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 140 GVRSLLAAL-ERRPHKPLLCII------------GEPTELkPVLGHKGKLAMRCEVHGAACHSAYAPQGvNAIEYAARLI 206
Cdd:cd05674 153 GAGAIAELLlERYGVDGLAAILdeggavlegvflGVPFAL-PGVAEKGYMDVEITVHTPGGHSSVPPKH-TGIGILSEAV 230
|
...
gi 489196727 207 GRL 209
Cdd:cd05674 231 AAL 233
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
52-137 |
1.09e-16 |
|
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: 77.85 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 52 NLYATIGPSDRGG-VCLSGHTDVVPAD-GQAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLP--VH 127
Cdd:cd03873 1 NLIARLGGGEGGKsVALGAHLDVVPAGeGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKgtIV 80
|
90
....*....|
gi 489196727 128 LAFSYDEEVG 137
Cdd:cd03873 81 VAFTADEEVG 90
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
10-367 |
2.34e-16 |
|
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: 79.80 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 10 DLVAFDTVS-RESNLALIdyVRDYLAGFGVdsELFFDADGRKA-----NLYATIgPSDRGGV---CLSGHTD-VVPADGq 79
Cdd:cd05683 11 ELVQIDSETlHEKEISKV--LKKKFENLGL--SVIEDDAGKTTgggagNLICTL-KADKEEVpkiLFTSHMDtVTPGIN- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 80 awsVPPfrLSERDGRLYGRGT----ADMKGYLACVLAAVPAFLAAPLRL-PVHLAFSYDEEVGCLGVRSLLAALERRPHK 154
Cdd:cd05683 85 ---VKP--PQIADGYIYSDGTtilgADDKAGIAAILEAIRVIKEKNIPHgQIQFVITVGEESGLVGAKALDPELIDADYG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 155 PLLCIIGEPTELkpVLGHKGKLAMRCEVHGAACHSAYAPQ-GVNAIEYAARLIGR--LGEIGArlavperhdrrfdppYS 231
Cdd:cd05683 160 YALDSEGDVGTI--IVGAPTQDKINAKIYGKTAHAGTSPEkGISAINIAAKAISNmkLGRIDE---------------ET 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 232 TVQTGLIQGGRALNIVPAECRFDFEVRALpadDPRQVAEELRDYAES-ELLprmrAVERSTDIRFTPLSAYPGLLTADDS 310
Cdd:cd05683 223 TANIGKFQGGTATNIVTDEVNIEAEARSL---DEEKLDAQVKHMKETfETT----AKEKGAHAEVEVETSYPGFKINEDE 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489196727 311 -------QAAELIGlLSGSTDFStvAFGTEGGLFHQAGIPAVICGPGsMDQGHKPDEFVSLAQL 367
Cdd:cd05683 296 evvklakRAANNLG-LEINTTYS--GGGSDANIINGLGIPTVNLGIG-YENIHTTNERIPIEDL 355
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
58-277 |
1.54e-15 |
|
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: 77.50 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 58 GPSDRGGVCLSG-HTDVVPADGQAWSVPPFRLSeRDG-RLYGRGTADMKGYLACV--LAAVPAFLAAPLRLPVHLAFSYD 133
Cdd:cd08012 73 GTVDGKTVSFVGsHMDVVTANPETWEFDPFSLS-IDGdKLYGRGTTDCLGHVALVteLFRQLATEKPALKRTVVAVFIAN 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 134 EE---VGCLGVRSLLAALERRPHK--PLLCIigEPTELKPVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARligR 208
Cdd:cd08012 152 EEnseIPGVGVDALVKSGLLDNLKsgPLYWV--DSADSQPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVME---A 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489196727 209 LGEIGARLAV-----PERHDRRFDPPYSTVQTGLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAE 277
Cdd:cd08012 227 LAEIQKRFYIdfpphPKEEVYGFATPSTMKPTQWSYPGGSINQIPGECTICGDCRLTPFYDVKEVREKLEEYVD 300
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
65-209 |
5.09e-15 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 76.14 E-value: 5.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 65 VCLSGHTDVVPADG---QAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAA---PLRlPVHLAFSYDEEVGC 138
Cdd:PRK08262 114 IVLMAHQDVVPVAPgteGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQgfqPRR-TIYLAFGHDEEVGG 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 139 LGVRSLLAALERRPHKPLLCI-------------IGEPTELKPVlGHKGKLAMRCEVHGAACHSAyAPQGVNAIEYAARL 205
Cdd:PRK08262 193 LGARAIAELLKERGVRLAFVLdeggaitegvlpgVKKPVALIGV-AEKGYATLELTARATGGHSS-MPPRQTAIGRLARA 270
|
....
gi 489196727 206 IGRL 209
Cdd:PRK08262 271 LTRL 274
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
65-344 |
1.36e-12 |
|
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: 68.45 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 65 VCLSGHTDVVPADGQAWSVPPFR-LSERDGRLYGRGTADMKgylaCV----LAAVPAFLAAPLRLP--VHLAFSYDEEV- 136
Cdd:cd05646 67 ILLNSHTDVVPVFEEKWTHDPFSaHKDEDGNIYARGAQDMK----CVgiqyLEAIRRLKASGFKPKrtIHLSFVPDEEIg 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 137 GCLGVRSLLAALERRPHKPLLCI---IGEPTELKPVL-GHKGKLAMRCEVHGAACHSAYAPQGvNAIEYAARLIGRLGEI 212
Cdd:cd05646 143 GHDGMEKFVKTEEFKKLNVGFALdegLASPTEEYRVFyGERSPWWVVITAPGTPGHGSKLLEN-TAGEKLRKVIESIMEF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 213 GArlavpERHDRRFDPP------YSTVQTGLIQGGRALNIVPAECRFDFEVRALPADDPRQVAEELRDYAESELlprmra 286
Cdd:cd05646 222 RE-----SQKQRLKSNPnltlgdVTTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAG------ 290
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489196727 287 veRSTDIRFTPLSAYPGLLTADDS--------QAAELIGLLSGSTDFSTvafGTEGGLFHQAGIPA 344
Cdd:cd05646 291 --RGVTYEFEQKSPEKDPTSLDDSnpwwaafkKAVKEMGLKLKPEIFPA---ATDSRYIRALGIPA 351
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
65-224 |
1.34e-11 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 65.54 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 65 VCLSGHTDVVPADG-QAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLAFSY--DEEVGCLGV 141
Cdd:PRK08201 82 VLIYGHYDVQPVDPlNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIegEEEIGSPNL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 142 RSLLAAlERRPHKPLLCIIGEPTELKP-----VLGHKGKLAMRCEVHGAA--CHSAYAPQGV-NAIEYAARLIGRLGEIG 213
Cdd:PRK08201 162 DSFVEE-EKDKLAADVVLISDTTLLGPgkpaiCYGLRGLAALEIDVRGAKgdLHSGLYGGAVpNALHALVQLLASLHDEH 240
|
170
....*....|.
gi 489196727 214 ARLAVPERHDR 224
Cdd:PRK08201 241 GTVAVEGFYDG 251
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
67-345 |
1.35e-11 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 65.58 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 67 LSGHTDVVPADGQAWSVPPFR-LSERDGRLYGRGTADMKgylaCV----LAAVPAFLAA---PLRlPVHLAFSYDEEVGc 138
Cdd:TIGR01880 76 LNSHTDVVPVFREHWTHPPFSaFKDEDGNIYARGAQDMK----CVgvqyLEAVRNLKASgfkFKR-TIHISFVPDEEIG- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 139 lGVRSLLAALERRPHKPL-LCI-----IGEPTELKPVL-GHKGKLAMRCEVHGAACHSA--YAPQGVNAIEYAARLIGR- 208
Cdd:TIGR01880 150 -GHDGMEKFAKTDEFKALnLGFaldegLASPDDVYRVFyAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRRf 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 209 ------LGEIGARLAVPErhdrrfdppYSTVQTGLIQGGRALNIVPAECRFDFEVRALPADDPrqvaEELRDYAESELLP 282
Cdd:TIGR01880 229 resqfqLLQSNPDLAIGD---------VTSVNLTKLKGGVQSNVIPSEAEAGFDIRLAPSVDF----EEMENRLDEWCAD 295
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489196727 283 RMRAVErstdIRFTPLSAYPGLLTADDS--------QAAELIGLLSGSTDFSTvafGTEGGLFHQAGIPAV 345
Cdd:TIGR01880 296 AGEGVT----YEFSQHSGKPLVTPHDDSnpwwvafkDAVKEMGCTFKPEILPG---STDSRYIRAAGVPAL 359
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
69-137 |
2.13e-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: 64.96 E-value: 2.13e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489196727 69 GHTDVVPAdGQAWSVPPFRLSERDGRLYGRGTADMKGylacvlAAVPAFLAA--------PLRLPVHLAFSYDEEVG 137
Cdd:cd03888 78 GHLDVVPA-GEGWTTDPFKPVIKDGKLYGRGTIDDKG------PTIAALYALkilkdlglPLKKKIRLIFGTDEETG 147
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
69-137 |
2.30e-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: 64.71 E-value: 2.30e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489196727 69 GHTDVVPAdGQAWSVPPFRLSERDGRLYGRGTADMKG-YLACvLAAVPAF--LAAPLRLPVHLAFSYDEEVG 137
Cdd:TIGR01887 74 GHLDVVPA-GDGWTSPPFEPTIKDGRIYGRGTLDDKGpTIAA-YYAMKILkeLGLKLKKKIRFIFGTDEESG 143
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
5-147 |
3.15e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 64.55 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 5 RDILADLVAFDTVSRE--SNLALIDYVRD----YLAGFGVDSELFFDADGRKAN-LYAT-IGPSDRGGVCLSGHTDVVPA 76
Cdd:PRK07079 20 FADLARRVAYRTESQNpdRAPALRAYLTDeiapALAALGFTCRIVDNPVAGGGPfLIAErIEDDALPTVLIYGHGDVVRG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489196727 77 DGQAWSVP--PFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAA---PLRLPVHLAFSYDEEVGCLGVRSLLAA 147
Cdd:PRK07079 100 YDEQWREGlsPWTLTEEGDRWYGRGTADNKGQHTINLAALEQVLAArggRLGFNVKLLIEMGEEIGSPGLAEVCRQ 175
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
8-157 |
9.28e-11 |
|
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: 63.13 E-value: 9.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 8 LADLVAFDTVSR--------ESNLALIdYVRDYLAGFGV-DSELFFDADGRKANLYATI---GPSDRGGVCL-SGHTDVV 74
Cdd:cd05677 5 LSEFIAFQTVSQspttenaeDSRRCAI-FLRQLFKKLGAtNCLLLPSGPGTNPIVLATFsgnSSDAKRKRILfYGHYDVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 75 PADG-QAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVpAFLAAPLRLPVHLAFSYDEEVGClGVRSLLAALERrpH 153
Cdd:cd05677 84 PAGEtDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAV-AELFQEGELDNDVVFLIEGEEES-GSPGFKEVLRK--N 159
|
....
gi 489196727 154 KPLL 157
Cdd:cd05677 160 KELI 163
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
6-223 |
2.13e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 61.69 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAF---DTVS------RESNLALIDYVRDYlagfGVDSELffdaDGRKAN--LYATIGPSDRGGVCLSGHTDVV 74
Cdd:PRK06446 3 EELYTLIEFlkkPSISatgegiEETANYLKDTMEKL----GIKANI----ERTKGHpvVYGEINVGAKKTLLIYNHYDVQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 75 PADG-QAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPlRLPVHLAFSY--DEEVGCLGVRSLLAALERR 151
Cdd:PRK06446 75 PVDPlSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKH-KLNVNVKFLYegEEEIGSPNLEDFIEKNKNK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 152 PHKPllCIIGEPTELKP------VLGHKGKL--AMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAVPERHD 223
Cdd:PRK06446 154 LKAD--SVIMEGAGLDPkgrpqiVLGVKGLLyvELVLRTGTKDLHSSNAPIVRNPAWDLVKLLSTLVDGEGRVLIPGFYD 231
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
63-258 |
2.24e-10 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 61.34 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 63 GGVCLSGHTDVVPAdgqawSVPPFRLSERdgrLYGRGTADMKGYLACVLAAvpAFLAAPLRLPVHLAFSYDEEVGCLGVR 142
Cdd:PRK00466 61 GDILLASHVDTVPG-----YIEPKIEGEV---IYGRGAVDAKGPLISMIIA--AWLLNEKGIKVMVSGLADEESTSIGAK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 143 SLLaaleRRPHKPLLCIIGEPTE-LKPVLGHKGKLAMRCEVHGAACHSAYAPQGVnAIEYAARLIgrlgEIgarLAVPER 221
Cdd:PRK00466 131 ELV----SKGFNFKHIIVGEPSNgTDIVVEYRGSIQLDIMCEGTPEHSSSAKSNL-IVDISKKII----EV---YKQPEN 198
|
170 180 190
....*....|....*....|....*....|....*..
gi 489196727 222 HDrrfDPpySTVQTgLIQGGRALNIVPAECRFDFEVR 258
Cdd:PRK00466 199 YD---KP--SIVPT-IIRAGESYNVTPAKLYLHFDVR 229
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
54-135 |
4.71e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 60.86 E-value: 4.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 54 YATIGPSDRGGVCLsGHTDVVPA-DGQAWSVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAAPLRLP--VHLAF 130
Cdd:PRK07205 68 YAEIGQGEELLAIL-CHLDVVPEgDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNkrIRFIF 146
|
....*
gi 489196727 131 SYDEE 135
Cdd:PRK07205 147 GTDEE 151
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
181-355 |
2.64e-09 |
|
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: 58.12 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 181 EVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARLAVPERhdrrfdppYSTVQTGLIQGGRALNIVPAECRFDFEVRAL 260
Cdd:TIGR01891 176 TIHGKGAHAARPHLGRDALDAAAQLVVALQQIVSRNVDPSR--------PAVVSVGIIEAGGAPNVIPDKASMSGTVRSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 261 PADDPRQVAEELRDYAESELLPRMRAVERSTDIRFTPLSAYPGLLTADDSQAAELIGLLSGSTDFSTVAFGTEGGLFHQA 340
Cdd:TIGR01891 248 DPEVRDQIIDRIERIVEGAAAMYGAKVELNYDRGLPAVTNDPALTQILKEVARHVVGPENVAEDPEVTMGSEDFAYYSQK 327
|
170
....*....|....*
gi 489196727 341 gIPAVICGPGSMDQG 355
Cdd:TIGR01891 328 -VPGAFFFLGIGNEG 341
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
69-137 |
8.09e-09 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 57.16 E-value: 8.09e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489196727 69 GHTDVVPAdGQAWSVPPFRLSERDGRLYGRGTADMKG-YLACVLAavpafLAA------PLRLPVHLAFSYDEEVG 137
Cdd:PRK07318 86 GHLDVVPA-GDGWDTDPYEPVIKDGKIYARGTSDDKGpTMAAYYA-----LKIikelglPLSKKVRFIVGTDEESG 155
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
64-252 |
1.30e-08 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 55.95 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 64 GVCLSGHTDVVPADGQAWSVPpFRlseRDG-RLYGRGTADMKGYLACVLAAVPAFLAAPLR--LPVHLAFSYDEEVGCLG 140
Cdd:PRK07473 77 GILIAGHMDTVHPVGTLEKLP-WR---REGnKCYGPGILDMKGGNYLALEAIRQLARAGITtpLPITVLFTPDEEVGTPS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 141 VRSLLAAlERRPHKPLLciIGEP--TELKPVLGHKGKLAMRCEVHGAACHS-AYAPQGVNAIEYAARLIgrlgeigarLA 217
Cdd:PRK07473 153 TRDLIEA-EAARNKYVL--VPEPgrPDNGVVTGRYAIARFNLEATGRPSHAgATLSEGRSAIREMARQI---------LA 220
|
170 180 190
....*....|....*....|....*....|....*
gi 489196727 218 VPERHDRRfdppySTVQTGLIQGGRALNIVPAECR 252
Cdd:PRK07473 221 IDAMTTED-----CTFSVGIVHGGQWVNCVATTCT 250
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
6-137 |
1.40e-08 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 56.52 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 6 DILADLVAFDTVSRE-----SNLALIDY---VRDYLAGFGVDselFFDADGRKanLYATIGPSDRGGVCLSGHTDVVPAD 77
Cdd:PRK06156 50 ESLRELVAFPTVRVEgvpqhENPEFIGFkklLKSLARDFGLD---YRNVDNRV--LEIGLGGSGSDKVGILTHADVVPAN 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489196727 78 GQAWSVP-----PFRLSERDGRLYGRGTADMKGYLACVLAAVPAF------LAAPLRLPVHLAfsydEEVG 137
Cdd:PRK06156 125 PELWVLDgtrldPFKVTLVGDRLYGRGTEDDKGAIVTALYAMKAIkdsglpLARRIELLVYTT----EETD 191
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
178-326 |
2.22e-07 |
|
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: 52.22 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 178 MRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIgarlavperHDRRFDPPYSTVQT-GLIQGGRALNIVPAECRFDFE 256
Cdd:cd03886 174 FEITVKGKGGHGASPHLGVDPIVAAAQIVLALQTV---------VSRELDPLEPAVVTvGKFHAGTAFNVIPDTAVLEGT 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 257 VRALpaddprqvAEELRDYAESELLPRMRAVERS--TDIRFTPLSAYPglLTADDSQ--------AAELIGL-------- 318
Cdd:cd03886 245 IRTF--------DPEVREALEARIKRLAEGIAAAygATVELEYGYGYP--AVINDPEltelvreaAKELLGEeavvepep 314
|
....*...
gi 489196727 319 LSGSTDFS 326
Cdd:cd03886 315 VMGSEDFA 322
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
8-147 |
1.48e-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: 49.80 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 8 LADLVAFDTVSRESNLALIdyVRDYLAGFGVDS--ELFFDAD-------GRKANLYAT-IGPSDRGGVCLSGHTDVVPAD 77
Cdd:cd05679 10 LARRVAVPTESQEPARKPE--LRAYLDQEMRPRfeRLGFTVHihdnpvaGRAPFLIAErIEDPSLPTLLIYGHGDVVPGY 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489196727 78 GQAW--SVPPFRLSERDGRLYGRGTADMKGYLACVLAAVPAFLAA---PLRLPVHLAFSYDEEVGCLGVRSLLAA 147
Cdd:cd05679 88 EGRWrdGRDPWTVTVWGERWYGRGTADNKGQHSINMAALRQVLEArggKLGFNVKFLIEMGEEMGSPGLRAFCFS 162
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
168-259 |
1.68e-06 |
|
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349939 [Multi-domain] Cd Length: 365 Bit Score: 49.59 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 168 PVLGHKGKLAMRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIgarlavperhdrRFDP--PYSTVQTGLIQGGRALN 245
Cdd:cd08018 160 PAIYHGASTFLEGTIKGKQAHGARPHLGINAIEAASAIVNAVNAI------------HLDPniPWSVKMTKLQAGGEATN 227
|
90
....*....|....
gi 489196727 246 IVPAECRFDFEVRA 259
Cdd:cd08018 228 IIPDKAKFALDLRA 241
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
178-326 |
3.16e-06 |
|
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 48.57 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 178 MRCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARlavperhdrRFDPPYSTVQT-GLIQGGRALNIVPAECRFDFE 256
Cdd:COG1473 186 FEITIKGKGGHAAAPHLGIDPIVAAAQIVTALQTIVSR---------NVDPLDPAVVTvGIIHGGTAPNVIPDEAELEGT 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 257 VRALPADDPRQVAEELRDYAEsellprmrAVERST--DIRFTPLSAYPGLLTADD------SQAAELIGL--------LS 320
Cdd:COG1473 257 VRTFDPEVRELLEERIERIAE--------GIAAAYgaTAEVEYLRGYPPTVNDPEltelarEAAREVLGEenvvdaepSM 328
|
....*.
gi 489196727 321 GSTDFS 326
Cdd:COG1473 329 GSEDFA 334
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
1-137 |
5.93e-06 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 47.97 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 1 MPGSRDILADLVAFDTVS-----RESNLALIDYVRDYLAGFGVDSELFfDADGRKANLYATIGPSDRG-GVCLSGHTDVV 74
Cdd:PRK09104 16 LDASLERLFALLRIPSIStdpayAADCRKAADWLVADLASLGFEASVR-DTPGHPMVVAHHEGPTGDApHVLFYGHYDVQ 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489196727 75 PADGQA-WSVPPF--RLSER-DGR--LYGRGTADMKGYLACVLAAVPAFLAAPLRLPVHLA--FSYDEEVG 137
Cdd:PRK09104 95 PVDPLDlWESPPFepRIKETpDGRkvIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTilFEGEEESG 165
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
27-282 |
6.32e-06 |
|
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: 47.65 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 27 DYVRDYLAGFGVDSELFFDADGrkanLYATIGPSDRGG-VCLSGHTDVVPADGQawSVPPFRlSERDGRLYGRG----TA 101
Cdd:cd08014 23 AFVAERLRDLGLKPKEFPGGTG----LVCDIGGKRDGRtVALRADMDALPIQEQ--TGLPYR-STVPGVMHACGhdahTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 102 DMKGyLACVLAAVPAflaaPLRLPVHLAFSYDEEVGCLGVRSLLA--ALERRPHkpLLCIIGEPTelKPVlghkGKLAMR 179
Cdd:cd08014 96 IALG-AALVLAALEE----ELPGRVRLIFQPAEETMPGGALDMIRagALDGVSA--IFALHVDPR--LPV----GRVGVR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 180 ------------CEVHGAACHSAYAPQGVNAIEYAARLIGrlgeigarlAVPERHDRRFDPPYSTVQT-GLIQGGRALNI 246
Cdd:cd08014 163 ygpitaaadsleIRIQGEGGHGARPHLTVDLVWAAAQVVT---------DLPQAISRRIDPRSPVVLTwGSIEGGRAPNV 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 489196727 247 VPAECRFDFEVRALPADDPRQVAEELRDYAESELLP 282
Cdd:cd08014 234 IPDSVELSGTVRTLDPDTWAQLPDLVEEIVAGICAP 269
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
176-278 |
7.67e-06 |
|
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349920 [Multi-domain] Cd Length: 367 Bit Score: 47.64 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 176 LAMRCEVH----GAACHSAYAPQGVNAIEYAARLIGRLGEIgarlavperHDRRFDPPYSTVQT-GLIQGGRALNIVPAE 250
Cdd:cd05670 169 FAGTSELHidfiGKSGHAAYPHNANDMVVAAANFVTQLQTI---------VSRNVDPIDGAVVTiGKIHAGTARNVIAGT 239
|
90 100
....*....|....*....|....*...
gi 489196727 251 CRFDFEVRALPADDPRQVAEELRDYAES 278
Cdd:cd05670 240 AHLEGTIRTLTQEMMELVKQRVRDIAEG 267
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
45-234 |
2.82e-05 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 46.18 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 45 DADGRKaNLYATI-GPSD-RGGVCLSGHTDVVPADG----QAWSVPPFRLSER----------DGR--------LYGRGT 100
Cdd:cd05654 53 DDLGRR-NVTALVkGKKPsKRTIILISHFDTVGIEDygelKDIAFDPDELTKAfseyveeldeEVRedllsgewLFGRGT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 101 ADMKGYLACVLAAVpAFLAAPLRLPVHLAFSY--DEEVGCLGVRSLLAALERRPHKP----LLCIIGEP-TELKP----- 168
Cdd:cd05654 132 MDMKSGLAVHLALL-EQASEDEDFDGNLLLMAvpDEEVNSRGMRAAVPALLELKKKHdleyKLAINSEPiFPQYDgdqtr 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489196727 169 --VLGHKGKLAMRCEVHGAACHSAYAPQGVNAiEYAARLIGRLGEIGARLAvpERHDRRFDPPYSTVQ 234
Cdd:cd05654 211 yiYTGSIGKILPGFLCYGKETHVGEPFAGINA-NLMASEITARLELNADLC--EKVEGEITPPPVCLK 275
|
|
| M20_Acy1L2 |
cd03887 |
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
177-328 |
8.09e-04 |
|
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, Aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase) subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349883 [Multi-domain] Cd Length: 360 Bit Score: 41.02 E-value: 8.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 177 AMRCEVHGAACHSAYAP-QGVNAIEyAARL----IGRLgeigarlavperhdRRFDPPYSTVQtGLI-QGGRALNIVPAE 250
Cdd:cd03887 160 KLRVEFHGKAAHAAAAPwEGINALD-AAVLaynnISAL--------------RQQLKPTVRVH-GIItEGGKAPNIIPDY 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 251 CRFDFEVRALPADDPRQVAEELRDYAESELLprmrAVERSTDIRFTPLSAYPGL----LTADDSQAAELIGL-------- 318
Cdd:cd03887 224 AEAEFYVRAPTLKELEELTERVIACFEGAAL----ATGCEVEIEELEGYYDELLpnktLANIYAENMEALGEevldgdeg 299
|
170
....*....|.
gi 489196727 319 -LSGSTDFSTV 328
Cdd:cd03887 300 vGSGSTDFGNV 310
|
|
| DUF2744 |
pfam10910 |
Protein of unknown function (DUF2744); This is a viral family of proteins with unknown ... |
192-274 |
2.28e-03 |
|
Protein of unknown function (DUF2744); This is a viral family of proteins with unknown function.
Pssm-ID: 287830 Cd Length: 119 Bit Score: 37.52 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 192 APQGVNAIEYAARLIGRLGEIGARLAVPERhDRRFDPPYSTVQTGLIQGGRALNI-VPAECRFDFE--VRALPADDPRQV 268
Cdd:pfam10910 30 APAIVLPEEYLRAISKHLWECGARPVDPAQ-AIKYQAPYRGEQSPLNPLGDWVSIdEPEPPKVRLQdpAAMTPQERRALV 108
|
....*.
gi 489196727 269 AEELRD 274
Cdd:pfam10910 109 AKALYD 114
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
179-278 |
6.58e-03 |
|
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: 38.47 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489196727 179 RCEVHGAACHSAYAPQGVNAIEYAARLIGRLGEIGARlavperhdrRFDPPYSTVQT-GLIQGGRALNIVPAECRFDFEV 257
Cdd:cd08019 172 KIEVKGKGGHGSMPHQGIDAVLAAASIVMNLQSIVSR---------EIDPLEPVVVTvGKLNSGTRFNVIADEAKIEGTL 242
|
90 100
....*....|....*....|.
gi 489196727 258 RALPADDPRQVAEELRDYAES 278
Cdd:cd08019 243 RTFNPETREKTPEIIERIAKH 263
|
|
| |
