|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
1-383 |
0e+00 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 692.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 1 MPSSRDLLARLVAFPTVSRNSNLALIEFVRDYLQGLGVACELDYNAERSKANLYASIGPSDRGGVLLSGHSDVVPTDGQA 80
Cdd:PRK07522 3 SMSSLDILERLVAFDTVSRDSNLALIEWVRDYLAAHGVESELIPDPEGDKANLFATIGPADRGGIVLSGHTDVVPVDGQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 81 WTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSYDEEVGCLGVRSLLSKLQQRPNPPALCII 160
Cdd:PRK07522 83 WTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPSMIARLPERGVKPAGCIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 161 GEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLTALERQDARFDPPYSTVQTGLIQG 240
Cdd:PRK07522 163 GEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLAAPGPFDALFDPPYSTLQTGTIQG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 241 GRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAETELLPRMRACSASSAIDLQPLSAYPGLATEPHSEAAELLALLA 320
Cdd:PRK07522 243 GTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAELLPEMRAVHPEAAIEFEPLSAYPGLDTAEDAAAARLVRALT 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222390563 321 GSRDFATVAFGTEGGLFHQAGIATVICGPGSMAQGHKPDEFVSQQQLDGCDAMLVRLADWLRE 383
Cdd:PRK07522 323 GDNDLRKVAYGTEAGLFQRAGIPTVVCGPGSIEQAHKPDEFVELAQLAACEAFLRRLLASLAA 385
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
6-379 |
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: 555.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVSRNSNLALIEFVRDYLQGLGVACELDYNAERSKANLYASIGPSDRGGVLLSGHSDVVPTDGQAWTVPP 85
Cdd:cd03894 1 ELLARLVAFDTVSRNSNLALIEYVADYLAALGVKSRRVPVPEGGKANLLATLGPGGEGGLLLSGHTDVVPVDGQKWSSDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 86 FALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSYDEEVGCLGVRSLLSKLQQRPNPPALCIIGEPTE 165
Cdd:cd03894 81 FTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALAARGGRPDAAIVGEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 166 LKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLtALERQDARFDPPYSTVQTGLIQGGRALN 245
Cdd:cd03894 161 LQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRL-APGLRDPPFDPPYPTLNVGLIHGGNAVN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 246 IVPAECQFDFEVRALPSDDPQQVAEELRAYAETELLPrmracsASSAIDLQPLSAYPGLATEPHSEAAELLALLAGSRDF 325
Cdd:cd03894 240 IVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEF------PEAGIEVEPLFEVPGLETDEDAPLVRLAAALAGDNKV 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1222390563 326 ATVAFGTEGGLFHQAGIATVICGPGSMAQGHKPDEFVSQQQLDGCDAMLVRLAD 379
Cdd:cd03894 314 RTVAYGTEAGLFQRAGIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
6-377 |
8.06e-128 |
|
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: 371.85 E-value: 8.06e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVSRNSNLALIEFVRDYLQGLGVACELDYNAE-RSKANLYASIGPSDRGGVLLSGHSDVVPTDGQAWTVP 84
Cdd:TIGR01892 1 EILTKLVAFDSTSFRPNVDLIDWAQAYLEALGFSVEVQPFPDgAEKSNLVAVIGPSGAGGLALSGHTDVVPYDDAAWTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 85 PFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSYDEEVGCLGVRSLLSKLQQRpnpPALCIIGEPT 164
Cdd:TIGR01892 81 PFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIEAGAGR---PRHAIIGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 165 ELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLgeIGQRLTALERQ-DARFDPPYSTVQTGLIQGGRA 243
Cdd:TIGR01892 158 RLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRL--VHLADTLLREDlDEGFTPPYTTLNIGVIQGGKA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 244 LNIVPAECQFDFEVRALPSDDPQQVAEELRAYAETellprMRACSASSAIDLQPLSAYPGLATEPHSEAAELLALLAGsR 323
Cdd:TIGR01892 236 VNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQA-----LVRDEPGFEVQIEVVSTDPGVNTEPDAELVAFLEELSG-N 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1222390563 324 DFATVAFGTEGGLFHQAGIATVICGPGSMAQGHKPDEFVSQQQLDGCDAMLVRL 377
Cdd:TIGR01892 310 APEVVSYGTEAPQFQELGAEAVVCGPGDIRQAHQPDEYVEIEDLVRCRAVLARL 363
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
1-381 |
4.39e-108 |
|
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: 322.60 E-value: 4.39e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 1 MPSSRDLLARLVAFPTVSRNsNLALIEFVRDYLQGLGVACELDYNAErSKANLYASI-GPSDRGGVLLSGHSDVVPTDGQ 79
Cdd:COG0624 11 LDEALELLRELVRIPSVSGE-EAAAAELLAELLEALGFEVERLEVPP-GRPNLVARRpGDGGGPTLLLYGHLDVVPPGDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 80 A-WTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLP--LHLAFSYDEEVGCLGVRSLLSKLQQRPNpPA 156
Cdd:COG0624 89 ElWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPgnVTLLFTGDEEVGSPGARALVEELAEGLK-AD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 157 LCIIGEPTE-LKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLtaleRQDARFDPPysTVQT 235
Cdd:COG0624 168 AAIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDG----RADPLFGRT--TLNV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 236 GLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYaetellprMRACSASSAIDLQPLS-AYPGLATEPHS---- 310
Cdd:COG0624 242 TGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRAL--------LAAAAPGVEVEVEVLGdGRPPFETPPDSplva 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222390563 311 EAAELLALLAGSR-DFATVAFGTEGGLFHQ-AGIATVICGPGSMAQGHKPDEFVSQQQLDGCDAMLVRLADWL 381
Cdd:COG0624 314 AARAAIREVTGKEpVLSGVGGGTDARFFAEaLGIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERL 386
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
2-368 |
2.63e-83 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 258.98 E-value: 2.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 2 PSSRDLLARLVAFPTVSRN------SNLALIEFVRDYLQGLGVACE-LDYNAERSKANLYASIGpSDRGGVLLSGHSDVV 74
Cdd:PRK05111 5 PSFIEMYRALIATPSISATdpaldqSNRAVIDLLAGWFEDLGFNVEiQPVPGTRGKFNLLASLG-SGEGGLLLAGHTDTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 75 PTDGQAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSYDEEVGCLGVRSLLSKLQQRPNp 154
Cdd:PRK05111 84 PFDEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAEATAIRPD- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 155 paLCIIGEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLtALERQDARFDPPYSTVQ 234
Cdd:PRK05111 163 --CAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDEL-QERYHNPAFTVPYPTLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 235 TGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAEtELLPRMracsaSSAIDLQPL-SAYPGLATEPHSEAA 313
Cdd:PRK05111 240 LGHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALA-PVSERW-----PGRITVAPLhPPIPGYECPADHQLV 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1222390563 314 ELLALLAGSRDfATVAFGTEGGLFHQAGIATVICGPGSMAQGHKPDEFVSQQQLD 368
Cdd:PRK05111 314 RVVEKLLGHKA-EVVNYCTEAPFIQQLGCPTLVLGPGSIEQAHQPDEYLELSFIK 367
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
6-378 |
1.31e-74 |
|
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: 235.66 E-value: 1.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVSRNSnLALIEFVRDYLQGLGvaCELDYNAERSKANLYASIGPSDRGGVLLSGHSDVVPT-DGQAWTVP 84
Cdd:cd08659 1 SLLQDLVQIPSVNPPE-AEVAEYLAELLAKRG--YGIESTIVEGRGNLVATVGGGDGPVLLLNGHIDTVPPgDGDKWSFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 85 PFALSERDGKLYGRGTADMKGFIACVLAAVPRFLA--QPLRLPLHLAFSYDEEVGCLGVRSLLSKLQQRPnpPALCIIGE 162
Cdd:cd08659 78 PFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEagALLGGRVALLATVDEEVGSDGARALLEAGYADR--LDALIVGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 163 PTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLTAlerqdarfDP--PYSTVQTGLIQG 240
Cdd:cd08659 156 PTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPA--------HPllGPPTLNVGVING 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 241 GRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAETEllprmracSASSAIDLQpLSAYPGLATEPHSEAAELLALLA 320
Cdd:cd08659 228 GTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEH--------EAKLTVEVS-LDGDPPFFTDPDHPLVQALQAAA 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222390563 321 GSRDFATVAFG----TEGGLF-HQAGIATVICGPGSMAQGHKPDEFVSQQQLDGCDAMLVRLA 378
Cdd:cd08659 299 RALGGDPVVRPftgtTDASYFaKDLGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
6-367 |
9.27e-60 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 198.29 E-value: 9.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVSRN-SNL-ALIEFVRDYLQGLGVACELDY--NAERSKANLYASIGPSDRGG----VLLSGHSDVVPTD 77
Cdd:PRK08651 10 EFLKDLIKIPTVNPPgENYeEIAEFLRDTLEELGFSTEIIEvpNEYVKKHDGPRPNLIARRGSgnphLHFNGHYDVVPPG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 78 GQAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFlAQPLRLPLHLAFSYDEEVGCLGVRSLLSKLQQRPNppaL 157
Cdd:PRK08651 90 EGWSVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERL-DPAGDGNIELAIVPDEETGGTGTGYLVEEGKVTPD---Y 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 158 CIIGEPTELKPV-LGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGE-IGQRLTALERQDARFDPPYSTVQT 235
Cdd:PRK08651 166 VIVGEPSGLDNIcIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSsLSTIKSKYEYDDERGAKPTVTLGG 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 236 GLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAETellprmRACSASSAIDLQPLSAYPGLATEPHS----E 311
Cdd:PRK08651 246 PTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDE------VAPELGIEVEFEITPFSEAFVTDPDSelvkA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1222390563 312 AAELLALLAGSRDFATVAFG-TEGGLFHQAGIATVICGPGSMAQGHKPDEFVSQQQL 367
Cdd:PRK08651 320 LREAIREVLGVEPKKTISLGgTDARFFGAKGIPTVVYGPGELELAHAPDEYVEVKDV 376
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
66-378 |
1.29e-58 |
|
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: 192.95 E-value: 1.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 66 LLSGHSDVVPtDGQAWTVPpFAlSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRL-PLHLAFSYDEEVGCLGVRSL 144
Cdd:pfam01546 1 LLRGHMDVVP-DEETWGWP-FK-STEDGKLYGRGHDDMKGGLLAALEALRALKEEGLKKgTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 145 LSKLQQRPNPPALCI---IGEPTEL------KPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQR 215
Cdd:pfam01546 78 IEDGLLEREKVDAVFglhIGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 216 ltaleRQDARFDPPYSTVQTGLIQGGRalNIVPAECQFDFEVRALPSDDPQQVAEELRAYAETELLPRMRACSassaIDL 295
Cdd:pfam01546 158 -----NVDPLDPAVVTVGNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVE----VEY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 296 QPLSAYPGLATEPHSEAAELLALLAGSRDFATVAFGTEGG-----LFHQAGIATVICGPGSmAQGHKPDEFVSQQQLDGC 370
Cdd:pfam01546 227 VEGGAPPLVNDSPLVAALREAAKELFGLKVELIVSGSMGGtdaafFLLGVPPTVVFFGPGS-GLAHSPNEYVDLDDLEKG 305
|
....*...
gi 1222390563 371 DAMLVRLA 378
Cdd:pfam01546 306 AKVLARLL 313
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
6-367 |
1.86e-56 |
|
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: 189.15 E-value: 1.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVS--RNSNLALIEFVRDYLQGLGVACEL-DYNAERSKAN---LYASIGPSDRGGVLLSGHSDVVPT-DG 78
Cdd:TIGR01910 2 ELLKDLISIPSVNppGGNEETIANYIKDLLREFGFSTDViEITDDRLKVLgkvVVKEPGNGNEKSLIFNGHYDVVPAgDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 79 QAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLP--LHLAFSYDEEVGCLGVRSLLSKLQQRpnPPA 156
Cdd:TIGR01910 82 ELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNgnIILQSVVDEESGEAGTLYLLQRGYFK--DAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 157 LCIIGEPTE-LKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLTAleRQDARFDPPYSTVQT 235
Cdd:TIGR01910 160 GVLIPEPSGgDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEEHIYA--RNSYGFIPGPITFNP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 236 GLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAY-----AETELLPRMRACSA-SSAIDLQPLSAYPGLATEPH 309
Cdd:TIGR01910 238 GVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVvkalsKSDGWLYENEPVVKwSGPNETPPDSRLVKALEAII 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1222390563 310 SEAAELLALLAGSrdfatvAFGTEGGLFHQAGIATVICGPGSMAQGHKPDEFVSQQQL 367
Cdd:TIGR01910 318 KKVRGIEPEVLVS------TGGTDARFLRKAGIPSIVYGPGDLETAHQVNEYISIKNL 369
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-378 |
8.59e-50 |
|
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: 171.03 E-value: 8.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVS--RNSNLALIEFVRDYLQGLGVACELdYNAERSKANLYASIgPSDRGG--VLLSGHSDVVPT-DGQA 80
Cdd:cd08011 2 KLLQELVQIPSPNppGDNTSAIAAYIKLLLEDLGYPVEL-HEPPEEIYGVVSNI-VGGRKGkrLLFNGHYDVVPAgDGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 81 WTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLA--QPLRLPLHLAFSYDEE-VGCLGVRSLLSKLQQRPNppaL 157
Cdd:cd08011 80 WTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADakAPWDLPVVLTFVPDEEtGGRAGTKYLLEKVRIKPN---D 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 158 CIIGEPTELKPV-LGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEigqrltaLERqdarfdppysTVQTG 236
Cdd:cd08011 157 VLIGEPSGSDNIrIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYE-------LEK----------TVNPG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 237 LIQGGRALNIVPAECQFDFEVRALPSDDPqqvaEELRAYAEtELLPRMracSASSAIDLQPLSAYPGLATEPH-SEAAEL 315
Cdd:cd08011 220 VIKGGVKVNLVPDYCEFSVDIRLPPGIST----DEVLSRII-DHLDSI---EEVSFEIKSFYSPTVSNPDSEIvKKTEEA 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1222390563 316 LALLAGSRDFATVAFG-TEGGLFHQAGIATVICGPGSMAQGHKPDEFVSQQQLDGCDAMLVRLA 378
Cdd:cd08011 292 ITEVLGIRPKEVISVGaSDARFYRNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-367 |
1.11e-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 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: 154.74 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 7 LLARLVAFPTVSRNSnLALIEFVRDYLQGLGVACELDYNAERSKANLYASIGPSDRGGVLLSGHSDVVPtdgqawtvP-- 84
Cdd:cd05652 4 LHKSLVEIPSISGNE-AAVGDFLAEYLESLGFTVEKQPVENKDRFNVYAYPGSSRQPRVLLTSHIDTVP--------Pfi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 85 PFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLP--LHLAFSYDEEVGCLGVRSLlSKLqqRPNPPALCIIGE 162
Cdd:cd05652 75 PYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEgdLGLLFVVGEETGGDGMKAF-NDL--GLNTWDAVIFGE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 163 PTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLgeigqRLTALERqDARFDPpySTVQTGLIQGGR 242
Cdd:cd05652 152 PTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKL-----IDADLPS-SELLGP--TTLNIGRISGGV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 243 ALNIVPAECQFDFEVRAlpSDDPQQVAEELRAyAETELLPRMRACSASSAIDLQPLSA---YPGLATephseaaellall 319
Cdd:cd05652 224 AANVVPAAAEASVAIRL--AAGPPEVKDIVKE-AVAGILTDTEDIEVTFTSGYGPVDLdcdVDGFET------------- 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1222390563 320 agsrdfATVAFGTEGGLFHQAGiATVICGPGSMAQGHKPDEFVSQQQL 367
Cdd:cd05652 288 ------DVVAYGTDIPYLKGDH-KRYLYGPGSILVAHGPDEAITVSEL 328
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
6-280 |
1.57e-43 |
|
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: 154.97 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVSRNSNLAlIEFVRDYLQGLGVACE-LDYNAERskaNLYASIGpsdRGGVLL--SGHSDVVPT-DGQAW 81
Cdd:cd03891 2 ELAKELIRRPSVTPDDAGA-QDLIAERLKALGFTCErLEFGGVK---NLWARRG---TGGPHLcfAGHTDVVPPgDLEGW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 82 TVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAF--SYDEE-VGCLGVRSLLSKLQQRPNPPALC 158
Cdd:cd03891 75 SSDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFliTSDEEgPAIDGTKKVLEWLKARGEKIDYC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 159 IIGEPTELKpVL------GHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEigqrlTALERQDARFDPpyST 232
Cdd:cd03891 155 IVGEPTSEK-KLgdtikiGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTA-----TVLDEGNEFFPP--SS 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1222390563 233 VQTGLIQGG-RALNIVPAECQFDFEVRAlpsdDPQQVAEELRAYAETEL 280
Cdd:cd03891 227 LQITNIDVGnGATNVIPGELKAKFNIRF----NDEHTGESLKARIEAIL 271
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-368 |
2.60e-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 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: 153.62 E-value: 2.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 5 RDLLARLVAFPTVSRN-SNLALieFVRDYLQGLGVAceldynAERSKANLYASIGPSDRG--GVLLSGHSDVVPTdGQAW 81
Cdd:cd05651 3 IELLKSLIATPSFSREeHKTAD--LIENYLEQKGIP------FKRKGNNVWAENGHFDEGkpTLLLNSHHDTVKP-NAGW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 82 TVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQ-PLRLPLHLAFSYDEEV-GCLGVRSLLSKLqqrpnPPA-LC 158
Cdd:cd05651 74 TKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEgPLNYNLIYAASAEEEIsGKNGIESLLPHL-----PPLdLA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 159 IIGEPTELKPVLGHKGKLAMRCQVQGAACHSAYaPQGVNAIEYAARLINRLgeigqrltalerQDARFD-------PPYS 231
Cdd:cd05651 149 IVGEPTEMQPAIAEKGLLVLDCTARGKAGHAAR-NEGDNAIYKALDDIQWL------------RDFRFDkvspllgPVKM 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 232 TVQTglIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAETELLPR-MRacSASSAIDL-QPL-SAYPGLATEP 308
Cdd:cd05651 216 TVTQ--INAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLKSEIKPRsFR--LNSSAIPPdHPIvQAAIAAGRTP 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 309 HseaaellallaGSRDFATVAFgtegglfhqAGIATVICGPGSMAQGHKPDEFVSQQQLD 368
Cdd:cd05651 292 F-----------GSPTLSDQAL---------MPFPSVKIGPGDSSRSHTADEFIELSEIE 331
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
6-280 |
5.94e-40 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 145.61 E-value: 5.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVSRNSNLALiEFVRDYLQGLGVACElDYNAERSKaNLYASIGpsdRGGVLL--SGHSDVVPT-DGQAWT 82
Cdd:PRK13009 6 ELAQDLIRRPSVTPDDAGCQ-DLLAERLEALGFTCE-RMDFGDVK-NLWARRG---TEGPHLcfAGHTDVVPPgDLEAWT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 83 VPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAF---SyDEE-VGCLGVRSLLSKLQQRPNPPALC 158
Cdd:PRK13009 80 SPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFlitS-DEEgPAINGTVKVLEWLKARGEKIDYC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 159 IIGEPTELKpVL------GHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEigqrlTALERQDARFDPpyST 232
Cdd:PRK13009 159 IVGEPTSTE-RLgdviknGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAA-----TEWDEGNEFFPP--TS 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1222390563 233 VQTGLIQGG-RALNIVPAECQFDFEVRAlpSDdpQQVAEELRAYAETEL 280
Cdd:PRK13009 231 LQITNIDAGtGATNVIPGELEAQFNFRF--ST--EHTAESLKARVEAIL 275
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
3-367 |
2.79e-36 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 135.71 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 3 SSRDLLARLVAFPTVSRNSNLA---LIEFVRDYLQGLGVACeLDYNAerSKANLYASIGPSDrggVLLSGHSDVVPtDGQ 79
Cdd:PRK08737 7 STLDHLQALVSFDTRNPPRAITtggIFDYLRAQLPGFQVEV-IDHGA--GAVSLYAVRGTPK---YLFNVHLDTVP-DSP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 80 AWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAqplrlPLHLAFSYDEEVG-CLGVRSLLsklqQRPNPPALC 158
Cdd:PRK08737 80 HWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANAGDG-----DAAFLFSSDEEANdPRCVAAFL----ARGIPYEAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 159 IIGEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQ-GVNAIEYAARLINRlgeigqrltALERQDARFDPPYSTVQT-- 235
Cdd:PRK08737 151 LVAEPTMSEAVLAHRGISSVLMRFAGRAGHASGKQDpSASALHQAMRWGGQ---------ALDHVESLAHARFGGLTGlr 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 236 ---GLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAETELL---PRMRAcsassaidlqplsayPGLatePH 309
Cdd:PRK08737 222 fniGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFAGFAEPAAAtfeETFRG---------------PSL---PS 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1222390563 310 SEAAELLALLAGSRDFA---------TVAFGTEGGLFHQAGIATVICGPGSMAQGHKPDEFVSQQQL 367
Cdd:PRK08737 284 GDIARAEERRLAARDVAdaldlpignAVDFWTEASLFSAAGYTALVYGPGDIAQAHTADEFVTLDQL 350
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
6-277 |
8.95e-36 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 134.46 E-value: 8.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVSRNSnLALIEFVRDYLQGLGVACE-LDYNaerSKANLYASIGPSdrGGVL-LSGHSDVVPT-DGQAWT 82
Cdd:TIGR01246 3 ELAKELISRPSVTPND-AGCQDIIAERLEKLGFEIEwMHFG---DTKNLWATRGTG--EPVLaFAGHTDVVPAgPEEQWS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 83 VPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAF--SYDEEVGCL-GVRSLLSKLQQRPNPPALCI 159
Cdd:TIGR01246 77 SPPFEPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLliTSDEEGTAIdGTKKVVETLMARDELIDYCI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 160 IGEPTELKPV-----LGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIgqrltALERQDARFDPpySTVQ 234
Cdd:TIGR01246 157 VGEPSSVKKLgdvikNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAI-----KWDEGNEFFPP--TSLQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1222390563 235 TGLIQGGR-ALNIVPAECQFDFEVRalpsDDPQQVAEELRAYAE 277
Cdd:TIGR01246 230 ITNIHAGTgANNVIPGELYVQFNLR----FSTEVSDEILKQRVE 269
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
6-380 |
6.77e-35 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 132.85 E-value: 6.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVS---RNSNlALIEFVRDYLQGLGvaCELD----YNAERSKANLYASIGPSDRGGVLLSGHSDVVPTDG 78
Cdd:PRK08596 17 ELLKTLVRFETPAppaRNTN-EAQEFIAEFLRKLG--FSVDkwdvYPNDPNVVGVKKGTESDAYKSLIINGHMDVAEVSA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 79 -QAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFS--YDEEVGCLGVRSLLsklqQRPNPP 155
Cdd:PRK08596 94 dEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQsvIGEEVGEAGTLQCC----ERGYDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 156 ALCIIGEPTELKpVLGHKGKL--------------AMRCQVqgaaCHSAYAPQGVNAIEYAARLINRLGEIgQRLTALER 221
Cdd:PRK08596 170 DFAVVVDTSDLH-MQGQGGVItgwitvkspqtfhdGTRRQM----IHAGGGLFGASAIEKMMKIIQSLQEL-ERHWAVMK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 222 QDARFDPPYSTVQTGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAY----AETEL-----LPRMRACSASSA 292
Cdd:PRK08596 244 SYPGFPPGTNTINPAVIEGGRHAAFIADECRLWITVHFYPNETYEQVIKEIEEYigkvAAADPwlrenPPQFKWGGESMI 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 293 ID-------LQPLSAYPGLAT--EPHSEAAELLALLAGSrdfATVafgTEGGLFHQAGIATVICGPGSMAQGHKPDEFVS 363
Cdd:PRK08596 324 EDrgeifpsLEIDSEHPAVKTlsSAHESVLSKNAILDMS---TTV---TDGGWFAEFGIPAVIYGPGTLEEAHSVNEKVE 397
|
410
....*....|....*...
gi 1222390563 364 QQQL-DGCDAMLVRLADW 380
Cdd:PRK08596 398 IEQLiEYTKVITAFIYEW 415
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
6-367 |
2.11e-34 |
|
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: 130.40 E-value: 2.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVSRNSN--LALIEFVRDYLQGLGVACELDYNAERSkANLYASIGPSDRGGVLLSGHSDVVPTDGqawTV 83
Cdd:cd03885 3 DLLERLVNIESGTYDKEgvDRVAELLAEELEALGFTVERRPLGEFG-DHLIATFKGTGGKRVLLIGHMDTVFPEG---TL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 84 PPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLR--LPLHLAFSYDEEVGCLGVRSLLSKLQQRPnppALCIIG 161
Cdd:cd03885 79 AFRPFTVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRdyLPITVLLNSDEEIGSPGSRELIEEEAKGA---DYVLVF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 162 EPTEL--KPVLGHKGKLAMRCQVQGAACHSAYAPQ-GVNAIEYAARLINRLgeigQRLTALERQdarfdppySTVQTGLI 238
Cdd:cd03885 156 EPARAdgNLVTARKGIGRFRLTVKGRAAHAGNAPEkGRSAIYELAHQVLAL----HALTDPEKG--------TTVNVGVI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 239 QGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAETELLPRMRacsassaIDLQPLSAYPGLATEPHSEAAELLAL 318
Cdd:cd03885 224 SGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTLVPGTS-------VELTGGLNRPPMEETPASRRLLARAQ 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1222390563 319 LAGSR-----DFATVAFGTEGGLFHQAGIATvICGPGSMAQG-HKPDEFVSQQQL 367
Cdd:cd03885 297 EIAAElgltlDWEATGGGSDANFTAALGVPT-LDGLGPVGGGaHTEDEYLELDSL 350
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-274 |
4.04e-34 |
|
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: 130.51 E-value: 4.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 7 LLARLVAFPtvSRNSNLALI-EFVRDYLQGLG-------VACE--------LDYNAERSKA-NLYASIGPSDRGG--VLL 67
Cdd:cd03895 2 FLQDLVRFP--SLRGEEAAAqDLVAAALRSRGytvdrweIDVEklkhhpgfSPVAVDYAGApNVVGTHRPRGETGrsLIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 68 SGHSDVVPTDGQA-WTVPPFALSERDGKLYGRGTADMK-GFIACVLA--AVPRFLAQPlRLPLHLAFSYDEEVGCLGVRS 143
Cdd:cd03895 80 NGHIDVVPEGPVElWTRPPFEATIVDGWMYGRGAGDMKaGLAANLFAldALRAAGLQP-AADVHFQSVVEEECTGNGALA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 144 LLsklqQRPNPPALCIIGEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLTALERQD 223
Cdd:cd03895 159 AL----MRGYRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEREWNARKKSH 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1222390563 224 ARFD--PPYSTVQTGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRA 274
Cdd:cd03895 235 PHFSdhPHPINFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEE 287
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
63-377 |
1.99e-32 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 125.28 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 63 GG--VLLSGHSDVVPTDGqaWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSYDEEVGCLG 140
Cdd:cd08013 67 GGksLMLNGHIDTVTLDG--YDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGLRGDVILAAVADEEDASLG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 141 VRSLLsKLQQRPNPpalCIIGEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLTALE 220
Cdd:cd08013 145 TQEVL-AAGWRADA---AIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALEEYQQELPERP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 221 rQDARFDPPysTVQTGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAET--ELLPRMRACSASSAidlqpL 298
Cdd:cd08013 221 -VDPLLGRA--SVHASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTAILGElaQTVPNFSYREPRIT-----L 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 299 SAYPGLATEPHSEAAELLALLAGSRDFATV----AFGTEGGLFHQAGIATVICGPgSMAQGHKPDEFVSQQQLDGCDAML 374
Cdd:cd08013 293 SRPPFEVPKEHPFVQLVAAHAAKVLGEAPQirseTFWTDAALLAEAGIPSVVFGP-SGAGLHAKEEWVDVESIRQLREVL 371
|
...
gi 1222390563 375 VRL 377
Cdd:cd08013 372 SAV 374
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
7-277 |
2.59e-32 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 125.00 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 7 LLARLVAFPTVSRNSnlalIEfVRDYLQGL----GVACELD-YNAERskANLYASIGPSDRggVL-LSGHSDVV-PTDGQ 79
Cdd:PRK08588 7 ILADIVKINSVNDNE----IE-VANYLQDLfakhGIESKIVkVNDGR--ANLVAEIGSGSP--VLaLSGHMDVVaAGDVD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 80 AWTVPPFALSERDGKLYGRGTADMK-GFIACVLAAVP------------RFLAqplrlplhlafSYDEEVGCLGVRSLLS 146
Cdd:PRK08588 78 KWTYDPFELTEKDGKLYGRGATDMKsGLAALVIAMIElkeqgqllngtiRLLA-----------TAGEEVGELGAKQLTE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 147 K-----LQqrpnppALcIIGEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLTALER 221
Cdd:PRK08588 147 KgyaddLD------AL-IIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYFDSIKKHNP 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1222390563 222 QDARFdppysTVQTGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAE 277
Cdd:PRK08588 220 YLGGL-----THVVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIIN 270
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
1-383 |
1.32e-30 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 119.86 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 1 MPSSRDLLARLVAFPTVSrNSNLALIEFVRDYLQGLGVACELDYNAErsKANLYASIGPSdrggVLLSGHSDVVPTdgqa 80
Cdd:PRK08652 1 TERAKELLKQLVKIPSPS-GQEDEIALHIMEFLESLGYDVHIESDGE--VINIVVNSKAE----LFVEVHYDTVPV---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 81 wTVPPFalsERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSYDEEVGCLGVRSLLSKLqqrpnPPALCII 160
Cdd:PRK08652 70 -RAEFF---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVSDEEEGGRGSALFAERY-----RPKMAIV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 161 GEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIgqrltaLERQDARFDPPYStVQtgLIQG 240
Cdd:PRK08652 141 LEPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKEL------LKALGKYFDPHIG-IQ--EIIG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 241 GRALNIVPAECQFDFEVRALPSDDPQQVAEELRA--------YAETELLPRMRaCSASSAIDLQPLSAYPGLATEPhsea 312
Cdd:PRK08652 212 GSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPildeytvkYEYTEIWDGFE-LDEDEEIVQLLEKAMKEVGLEP---- 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222390563 313 aellallagsrDFATVAFGTEGGLFHQAGIATVICGPGSMAQGHKPDEFVSQQQLDGCDAMLVRLADWLRE 383
Cdd:PRK08652 287 -----------EFTVMRSWTDAINFRYNGTKTVVWGPGELDLCHTKFERIDVREVEKAKEFLKALNEILLE 346
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
6-378 |
3.44e-28 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 113.22 E-value: 3.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVSRNsNLALIEFVRDYLQGLGVACELDynaerSKANLYASIgPSDRG----GVLLSGHSDVVP---TDG 78
Cdd:COG2195 7 ERFLEYVKIPTPSDH-EEALADYLVEELKELGLEVEED-----EAGNVIATL-PATPGynvpTIGLQAHMDTVPqfpGDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 79 qawtVPPFalsERDGKLYGRGT----ADMKGFIACVLAAVpRFLAQPlRLPlH----LAFSYDEEVGCLGVRSL-LSKLQ 149
Cdd:COG2195 80 ----IKPQ---IDGGLITADGTttlgADDKAGVAAILAAL-EYLKEP-EIP-HgpieVLFTPDEEIGLRGAKALdVSKLG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 150 QRPnppALCIIGEPTelkpvlghkGKLAMRC--------QVQGAACHSAYAP-QGVNAIEYAARLINRL--GEIGQRLTA 218
Cdd:COG2195 150 ADF---AYTLDGGEE---------GELEYECagaadakiTIKGKGGHSGDAKeKMINAIKLAARFLAALplGRIPEETEG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 219 LErqdarfdppystvqtGLIQGGRALNIVPAECQFDFEVRalpSDDPQQVAEELRAYAET--ELLPRMRACSASSAIDLQ 296
Cdd:COG2195 218 NE---------------GFIHGGSATNAIPREAEAVYIIR---DHDREKLEARKAELEEAfeEENAKYGVGVVEVEIEDQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 297 plsaYPGLATEPHSEaaellallagSRDFATVAF--------------GTEGGLFHQAGIATVICGPGsMAQGHKPDEFV 362
Cdd:COG2195 280 ----YPNWKPEPDSP----------IVDLAKEAYeelgiepkikpirgGLDGGILSFKGLPTPNLGPG-GHNFHSPDERV 344
|
410
....*....|....*.
gi 1222390563 363 SQQQLDGCDAMLVRLA 378
Cdd:COG2195 345 SIESMEKAWELLVEIL 360
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
8-274 |
4.95e-28 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 113.94 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 8 LARLVAFPTVsRNSNLALIEFVRDYLQGLGVAC---ELD------------YNAERSKA-NLYASIGPSDRGG--VLLSG 69
Cdd:PRK06837 26 TQDLVRFPST-RGAEAPCQDFLARAFRERGYEVdrwSIDpddlkshpgagpVEIDYSGApNVVGTYRPAGKTGrsLILQG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 70 HSDVVPTdGQA--WTVPPFALSERDGKLYGRGTADMK-GFIACVLA--AVPRFLAQPLRlPLHLAFSYDEEvgCLGVRSL 144
Cdd:PRK06837 105 HIDVVPE-GPLdlWSRPPFDPVIVDGWMYGRGAADMKaGLAAMLFAldALRAAGLAPAA-RVHFQSVIEEE--STGNGAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 145 lSKLQQRPNPPAlCIIGEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLTALERQDA 224
Cdd:PRK06837 181 -STLQRGYRADA-CLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRELEAEWNARKASDP 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1222390563 225 RF-DPPYS-TVQTGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRA 274
Cdd:PRK06837 259 HFeDVPHPiNFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAADAQAEIEA 310
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
170-284 |
1.34e-27 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 104.74 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 170 LGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEigqrltalERQDARFDPPYSTVQTGLIQGGRALNIVPA 249
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPA--------EYGDIGFDFPRTTLNITGIEGGTATNVIPA 72
|
90 100 110
....*....|....*....|....*....|....*
gi 1222390563 250 ECQFDFEVRALPSDDPQQVAEELRAYAETELLPRM 284
Cdd:pfam07687 73 EAEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
26-373 |
1.35e-27 |
|
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: 112.13 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 26 IEFVRDYLQGLGVACELDYNAERSKA----------------NLYASIGPSDRGgVLLSGHSDVVP-TDGQAWTVPPFAL 88
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEemeklgfdeveidpmgNVIGYIGGGKKK-ILFDGHIDTVGiGNIDNWKFDPYEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 89 SERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRL---PLHLAFSYDEEVgCLGV--RSLLSKLQQRPNppaLCIIGEP 163
Cdd:cd05649 80 YETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLRDfayTILVAGTVQEED-CDGVcwQYISKADKIKPD---FVVSGEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 164 TELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLtalerQDARFDPPYSTVQTGLIQGGRA 243
Cdd:cd05649 156 TDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNF-----PEAPFLGRGTLTVTDIFSTSPS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 244 LNIVPAECQFDFEVRALPSDDPQQVAEELRA------YAETELLPRMRACSASSAIDLQPLSAY-PGLA---TEPHSEAA 313
Cdd:cd05649 231 RCAVPDSCRISIDRRLTVGETWEGCLEEIRAlpavkkYGDDVAVSMYNYDRPSYTGEVYESERYfPTWLlpeDHELVKAL 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222390563 314 ELLALLAGSRDFATV--AFGTEGGLFH-QAGIATVICGPGSMAQGHKPDEFVSQQQLDGCDAM 373
Cdd:cd05649 311 LEAYKALFGARPLIDkwTFSTNGVSIMgRAGIPCIGFGPGAENQAHAPNEYTWKEDLVRCAAG 373
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
5-277 |
1.63e-27 |
|
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: 112.45 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 5 RDLLARLVAFPTVSRNSNL----ALIEFVRDYLQGLGVACELDYNAER-SKANLYASIGPSD--RGGVLLSGHSDVVPTD 77
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTgsetRAAEVLAARLAEAGIQTEIFVVESHpGRANLVARIGGTDpsAGPLLLLGHIDVVPAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 78 GQAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVpRFLAQP---LRLPLHLAFSYDEEV-GCLGVRSLLSKLQQRPN 153
Cdd:cd05675 81 ASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVL-RHYKREgfkPKRDLVFAFVADEEAgGENGAKWLVDNHPELFD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 154 PPALCI---------IGEPTELKPV-LGHKGKLAMRCQVQGAACHSAyAPQGVNAIEYAARLINRLGEIGQRL-----TA 218
Cdd:cd05675 160 GATFALneggggslpVGKGRRLYPIqVAEKGIAWMKLTVRGRAGHGS-RPTDDNAITRLAEALRRLGAHNFPVrltdeTA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 219 LERQDARFDPPY--------------------------------STVQTGLiQGGRALNIVPAECQFDFEVRALPSDDPQ 266
Cdd:cd05675 239 YFAQMAELAGGEggalmltavpvldpalaklgpsapllnamlrnTASPTML-DAGYATNVLPGRATAEVDCRILPGQSEE 317
|
330
....*....|.
gi 1222390563 267 QVAEELRAYAE 277
Cdd:cd05675 318 EVLDTLDKLLG 328
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
8-367 |
3.88e-27 |
|
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: 111.11 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 8 LARLVAFPTVSRNSNLA-LIEFVRDYLQGLGVACEL---------DYNAErSKANLYASIGPSDRGG-VLLSGHSDVVPT 76
Cdd:cd02697 9 LQKLVRVPTDTPPGNNApHAERTAALLQGFGFEAERhpvpeaevrAYGME-SITNLIVRRRYGDGGRtVALNAHGDVVPP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 77 dGQAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRF--LAQPLRLPLHLAFSYDEEVGCLGVRSLLskLQQRPNP 154
Cdd:cd02697 88 -GDGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALesLGAPLRGAVELHFTYDEEFGGELGPGWL--LRQGLTK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 155 PALcIIGEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLTALERQDARFDPPYSTVq 234
Cdd:cd02697 165 PDL-LIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNAQYRQVSSQVEGITHPYLNV- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 235 tGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAETELlprmrACSASSAIDLQPLSAYPGLATEPHSEAAE 314
Cdd:cd02697 243 -GRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAA-----ASMPGISVDIRRLLLANSMRPLPGNAPLV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222390563 315 LLALLAGSRDF--ATVAFG----TEGGLFHQAGIATVICGPGSM----AQGHKPDEFVSQQQL 367
Cdd:cd02697 317 EAIQTHGEAVFgePVPAMGtplyTDVRLYAEAGIPGVIYGAGPRtvleSHAKRADERLQLEDL 379
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
25-373 |
9.43e-27 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 110.03 E-value: 9.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 25 LIEFVRDYLQGLGVACELDYNAERSKA----------------NLYASIGPSDRGgVLLSGHSDVVP-TDGQAWTVPPFA 87
Cdd:PRK13004 17 MTRFLRDLIRIPSESGDEKRVVKRIKEemekvgfdkveidpmgNVLGYIGHGKKL-IAFDAHIDTVGiGDIKNWDFDPFE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 88 LSERDGKLYGRGTADMKGFIACVLAAVPRF--LAQPLRLPLHLAFSYDEEVgCLGV--RSLLSKLQQRPnppALCIIGEP 163
Cdd:PRK13004 96 GEEDDGRIYGRGTSDQKGGMASMVYAAKIIkdLGLDDEYTLYVTGTVQEED-CDGLcwRYIIEEDKIKP---DFVVITEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 164 TELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLT--------ALERQDARFDPPystvqt 235
Cdd:PRK13004 172 TDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNLKedpflgkgTLTVSDIFSTSP------ 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 236 gliqgGRalNIVPAEC--QFDF-------------EVRALPSDDPQQVAEELRAY---------AETE------LLPRmr 285
Cdd:PRK13004 246 -----SR--CAVPDSCaiSIDRrltvgetwesvlaEIRALPAVKKANAKVSMYNYdrpsytglvYPTEcyfptwLYPE-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 286 acsaSSAIDLQPLSAYPGL-ATEPhseaaellalLAGSRDFATVAFGTEGglfhQAGIATVICGPGSMAQGHKPDEFVSQ 364
Cdd:PRK13004 317 ----DHEFVKAAVEAYKGLfGKAP----------EVDKWTFSTNGVSIAG----RAGIPTIGFGPGKEPLAHAPNEYTWK 378
|
....*....
gi 1222390563 365 QQLDGCDAM 373
Cdd:PRK13004 379 EQLVKAAAM 387
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
7-381 |
2.11e-26 |
|
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: 108.30 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 7 LLARLVAFPTVSRNSNlALIEFVRDYLQGLGvacelDYNAERSKANLYAS--IGPSDRggVLLSGHSDVVPTDGqawTVP 84
Cdd:cd05647 4 LTAALVDIPSVSGNEK-PIADEIEAALRTLP-----HLEVIRDGNTVVARteRGLASR--VILAGHLDTVPVAG---NLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 85 PFAlsERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSYDEEVGclgvrSLLSKLQ--QRPNPPAL----C 158
Cdd:cd05647 73 SRV--EEDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHDLTLIFYDCEEVA-----AELNGLGrlAEEHPEWLaadfA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 159 IIGEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLTALERQDARfdppySTVQTGLI 238
Cdd:cd05647 146 VLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLAAYEPRTVNIDGLTYR-----EGLNAVFI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 239 QGGRALNIVPAECQFDFEVRALPSDDPQQVAEELR---AYAETELlprmracsasSAIDLQPlSAYPGLATEphseaael 315
Cdd:cd05647 221 SGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVRevfEGLGYEI----------EVTDLSP-GALPGLDHP-------- 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222390563 316 lallaGSRDFATvAFG---------TEGGLFHQAGIATVICGPGSMAQGHKPDEFVSQQQLDGCDAMlvrLADWL 381
Cdd:cd05647 282 -----VARDLIE-AVGgkvrakygwTDVARFSALGIPAVNFGPGDPLLAHKRDEQVPVEQITACAAI---LRRWL 347
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
5-278 |
2.65e-26 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 107.82 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 5 RDLLARLVAFPTVSRNSNlALIEFVRDYLQglgvacELDYNAERSKA-NLYASIGPSDRGgVLLSGHSDVVPTDgqawtV 83
Cdd:cd05653 4 VELLLDLLSIYSPSGEEA-RAAKFLEEIMK------ELGLEAWVDEAgNAVGGAGSGPPD-VLLLGHIDTVPGE-----I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 84 PPfalSERDGKLYGRGTADMKG-FIACVLAAvpRFLAQPLRLPLHLAFSYDEEVGCLGVRSLLSklqQRPNPPAlCIIGE 162
Cdd:cd05653 71 PV---RVEGGVLYGRGAVDAKGpLAAMILAA--SALNEELGARVVVAGLVDEEGSSKGARELVR---RGPRPDY-IIIGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 163 PTELKPV-LGHKGKLAMRCQVQGAACHSAYApqGVNAIEyaaRLINRLGEIGQRLTALERQDARFDppysTVQTGLIQGG 241
Cdd:cd05653 142 PSGWDGItLGYRGSLLVKIRCEGRSGHSSSP--ERNAAE---DLIKKWLEVKKWAEGYNVGGRDFD----SVVPTLIKGG 212
|
250 260 270
....*....|....*....|....*....|....*..
gi 1222390563 242 RALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAET 278
Cdd:cd05653 213 ESSNGLPQRAEATIDLRLPPRLSPEEAIALATALLPT 249
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
6-275 |
7.92e-26 |
|
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: 107.81 E-value: 7.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVSRNSN--LALIEFVRDYLQGLGVACELdynaERSKAN--LYASIGPSDRGGVLLSGHSDVVPTDG-QA 80
Cdd:cd05681 3 EDLRDLLKIPSVSAQGRgiPETADFLKEFLRRLGAEVEI----FETDGNpiVYAEFNSGDAKTLLFYNHYDVQPAEPlEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 81 WTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSYD--EEVGCLGVRSLLSKlqqrpNPPAL- 157
Cdd:cd05681 79 WTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEgeEEVGSPNLEKFVAE-----HADLLk 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 158 ---CII---GEPTELKP--VLGHKGKLAMRCQVQGAA--CHSAYAPQGVNAIEYAARLINRLGEIGQR------------ 215
Cdd:cd05681 154 adgCIWeggGKNPKGRPqiSLGVKGIVYVELRVKTADfdLHSSYGAIVENPAWRLVQALNSLRDEDGRvlipgfyddvrp 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 216 LTALER---QDARFDP---------------------------PYSTVQtGLI---QGGRALNIVPAECQFDFEVRALPS 262
Cdd:cd05681 234 LSEAERaliDTYDFDPeelrktyglkrplqvegkdplralftePTCNIN-GIYsgyTGEGSKTILPSEAFAKLDFRLVPD 312
|
330
....*....|...
gi 1222390563 263 DDPQQVAEELRAY 275
Cdd:cd05681 313 QDPAKILSLLRKH 325
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
8-277 |
1.77e-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: 103.95 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 8 LARLVAFPTVS-----RNSNLALIEFVRDYLQGLGVACELDYNAERSKAnLYASI-GPSDRGGVLLSGHSDVVPTDGQA- 80
Cdd:cd03893 4 LAELVAIPSVSaqpdrREELRRAAEWLADLLRRLGFTVEIVDTSNGAPV-VFAEFpGAPGAPTVLLYGHYDVQPAGDEDg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 81 WTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSYD--EEVGCLGVRSLLSKLQQRPNPPALC 158
Cdd:cd03893 83 WDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEgeEESGSPSLDQLVEAHRDLLAADAIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 159 IIGEP--TELKPVL--GHKGKLAMRCQVQGAA--CHSAYApQGV--NAIEYAARLINRL----GEI-------------G 213
Cdd:cd03893 163 ISDSTwvGQEQPTLtyGLRGNANFDVEVKGLDhdLHSGLY-GGVvpDPMTALAQLLASLrdetGRIlvpglydavrelpE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 214 QRLTALERQDARFDPPYSTVQTGLI-----------------QGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYA 276
Cdd:cd03893 242 EEFRLDAGVLEEVEIIGGTTGSVAErlwtrpaltvlgidggfPGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLEAHL 321
|
.
gi 1222390563 277 E 277
Cdd:cd03893 322 E 322
|
|
| PRK06915 |
PRK06915 |
peptidase; |
65-380 |
2.90e-24 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 103.23 E-value: 2.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 65 VLLSGHSDVVPT-DGQAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFS--YDEEVGCLGV 141
Cdd:PRK06915 96 MILNGHIDVVPEgDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQsvIEEESGGAGT 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 142 RSLLsklqQRPNPPALCIIGEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQrltalER 221
Cdd:PRK06915 176 LAAI----LRGYKADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEE-----KR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 222 QDARFDPPYSTV------QTGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYaeTELLPRMRACSASSAIDL 295
Cdd:PRK06915 247 NDRITDPLYKGIpipipiNIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENW--IAELNDVDEWFVEHPVEV 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 296 QPLSAY--PGLATEPHSEAAELlallagSRDFATVA----------FGTEGGLFHQAG-IATVICGPGSMAQGHKPDEFV 362
Cdd:PRK06915 325 EWFGARwvPGELEENHPLMTTL------EHNFVEIEgnkpiieaspWGTDGGLLTQIAgVPTIVFGPGETKVAHYPNEYI 398
|
330
....*....|....*....
gi 1222390563 363 SQQQL-DGCDAMLVRLADW 380
Cdd:PRK06915 399 EVDKMiAAAKIIALTLLDW 417
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
6-277 |
7.75e-24 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 101.85 E-value: 7.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVSRNSN----LALIEFVRDYLQGLGVACELDYNAERSKA------NLYASIGPSDRGGVL-LSGHSDVV 74
Cdd:PRK13983 9 ELLSELIAIPAVNPDFGgegeKEKAEYLESLLKEYGFDEVERYDAPDPRViegvrpNIVAKIPGGDGKRTLwIISHMDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 75 PT-DGQAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLP--LHLAFSYDEEVGCL-GVRSLLSKLQQ 150
Cdd:PRK13983 89 PPgDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKynLGLAFVSDEETGSKyGIQYLLKKHPE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 151 RPNPPALCII---GEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEigqRL-TALERQDARF 226
Cdd:PRK13983 169 LFKKDDLILVpdaGNPDGSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRAAADFALELDE---ALhEKFNAKDPLF 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1222390563 227 DPPYSTVQ-TGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAE 277
Cdd:PRK13983 246 DPPYSTFEpTKKEANVDNINTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIAD 297
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-276 |
1.61e-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: 97.91 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 7 LLARLVAFPTVSRNSN----LALIEFVRDYLQGLGVAC--ELDYNAERSK--ANLYASIGPSDRGGVLLSGHSDVVPT-D 77
Cdd:cd05650 6 LERDLIRIPAVNPESGgegeKEKADYLEKKLREYGFYTleRYDAPDERGIirPNIVAKIPGGNDKTLWIISHLDTVPPgD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 78 GQAWTVPPFALSERDGKLYGRGTAD-MKGFIACVLAAVPRF-LAQPLRLPLHLAFSYDEEVGC-LGVRSLLSKLQQRpNP 154
Cdd:cd05650 86 LSLWETDPWEPVVKDGKIYGRGVEDnQQGIVSSLLALKAIIkNGITPKYNFGLLFVADEEDGSeYGIQYLLNKFDLF-KK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 155 PALCII---GEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLtaLERQDARFDPPYS 231
Cdd:cd05650 165 DDLIIVpdfGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFALELDELLHEK--FDEKDDLFNPPYS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1222390563 232 TVQ-TGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYA 276
Cdd:cd05650 243 TFEpTKKEANVPNVNTIPGYDVFYFDCRVLPTYKLDEVLKFVNKII 288
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
5-309 |
5.93e-22 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 96.99 E-value: 5.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 5 RDLLARLVAFPTV-SRNSNLALIEFVRDYLQGLGVACElDYNAERS---KANLYASIGPSDRGG-VLLSGHSDVVPTDGQ 79
Cdd:PRK09133 40 RDLYKELIEINTTaSTGSTTPAAEAMAARLKAAGFADA-DIEVTGPyprKGNLVARLRGTDPKKpILLLAHMDVVEAKRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 80 AWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQ---PLRlPLHLAFSYDEEVGCL-GVRSLLSKLQQRPNPp 155
Cdd:PRK09133 119 DWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREgfkPKR-DIILALTGDEEGTPMnGVAWLAENHRDLIDA- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 156 ALCII----GEPTEL-KPVL-----GHKGKLAMRCQVQGAACHSAyAPQGVNAIEYAARLINRL---------------- 209
Cdd:PRK09133 197 EFALNegggGTLDEDgKPVLltvqaGEKTYADFRLEVTNPGGHSS-RPTKDNAIYRLAAALSRLaayrfpvmlndvtray 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 210 ---------GEIGQRLTALE--RQDA------RFDPPY-STVQTG----LIQGGRALNIVPAECQFDFEVRALPSDDPQQ 267
Cdd:PRK09133 276 fkqsaaietGPLAAAMRAFAanPADEaaiallSADPSYnAMLRTTcvatMLEGGHAENALPQRATANVNCRIFPGDTIEA 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1222390563 268 VAEEL-RAYAETEL-LPRMRACSASSAIDLQP--------LSA--YPGLATEPH 309
Cdd:PRK09133 356 VRATLkQVVADPAIkITRIGDPSPSPASPLRPdimkavekLTAamWPGVPVIPS 409
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
5-278 |
3.52e-21 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 93.48 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 5 RDLLARLVAFPTVSRNSNlALIEFVRDYLQGLGVACELDY--NAerskanlyasIGPSDRGG--VLLSGHSDVVPTDgqa 80
Cdd:PRK04443 9 RELLKGLVEIPSPSGEEA-AAAEFLVEFMESHGREAWVDEagNA----------RGPAGDGPplVLLLGHIDTVPGD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 81 wtVPPFAlseRDGKLYGRGTADMKGFIACVLAAVPRfLAQPLRLPLHLAFSYDEEVGCLGVRSLlskLQQRpNPPALCII 160
Cdd:PRK04443 75 --IPVRV---EDGVLWGRGSVDAKGPLAAFAAAAAR-LEALVRARVSFVGAVEEEAPSSGGARL---VADR-ERPDAVII 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 161 GEPTELKPV-LGHKGKLAMRCQVQGAACHSAYapQGVNAIEyaaRLINRLGEIGQRltaLERQDARfDPPYSTVQTGLiq 239
Cdd:PRK04443 145 GEPSGWDGItLGYKGRLLVTYVATSESFHSAG--PEPNAAE---DAIEWWLAVEAW---FEANDGR-ERVFDQVTPKL-- 213
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1222390563 240 ggRALNIVPA----ECQFDFEVRALPSDDPQQVAEELRAYAET 278
Cdd:PRK04443 214 --VDFDSSSDgltvEAEMTVGLRLPPGLSPEEAREILDALLPT 254
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
6-137 |
3.09e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 91.45 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVSRNSNL-----ALIEFVRDYLQGLGVACELdYNAERSKANLYASIGPSD--RGGVLLSGHSDVVPTDG 78
Cdd:PRK07906 3 DLCSELIRIDTTNTGDGTgkgerEAAEYVAEKLAEVGLEPTY-LESAPGRANVVARLPGADpsRPALLVHGHLDVVPAEA 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222390563 79 QAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFL---AQPLRlPLHLAFSYDEEVG 137
Cdd:PRK07906 82 ADWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLArtgRRPPR-DLVFAFVADEEAG 142
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
7-382 |
4.59e-20 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 90.97 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 7 LLARLVAFPTVS---RNSNlALIEFVRDYLQGLGVACELdYNAERSKA--------NLYASI-GPSDRGGVLLSGHSDVV 74
Cdd:PRK13013 19 LTQDLIRIPTLNppgRAYR-EICEFLAARLAPRGFEVEL-IRAEGAPGdsetyprwNLVARRqGARDGDCVHFNSHHDVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 75 PTdGQAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLP--LHLAFSYDEEVGCLGVRSLLSKlQQRP 152
Cdd:PRK13013 97 EV-GHGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAgsIEISGTADEESGGFGGVAYLAE-QGRF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 153 NPPAL--CIIGEPTELKPV-LGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRLTALERQDARFDPP 229
Cdd:PRK13013 175 SPDRVqhVIIPEPLNKDRIcLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAEIEERLFPLLATRRTAMPVVPE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 230 ---YSTVQTGLIQGGRALN----------IVPAECQFDFEVRALPSDDPQQVAEELRAyaeteLLPRMRACSASSAIDLQ 296
Cdd:PRK13013 255 garQSTLNINSIHGGEPEQdpdytglpapCVADRCRIVIDRRFLIEEDLDEVKAEITA-----LLERLKRARPGFAYEIR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 297 PLSAYPGLATEphseaaellallagsRD---FATVAFGTEGGLFHQAGIAT-------------------VICGPGSMAQ 354
Cdd:PRK13013 330 DLFEVLPTMTD---------------RDapvVRSVAAAIERVLGRQADYVVspgtydqkhidrigklkncIAYGPGILDL 394
|
410 420
....*....|....*....|....*....
gi 1222390563 355 GHKPDEFVS-QQQLDGCDAMLVRLADWLR 382
Cdd:PRK13013 395 AHQPDEWVGiADMVDSAKVMALVLADLLA 423
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
6-147 |
5.45e-20 |
|
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: 91.12 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVS-----RNSNLALIEFVRDYLQGLGVACELDYNAERSKAN---------LYASIGPS-DRGGVLLSGH 70
Cdd:cd05676 14 ERLREAVAIQSVSadpekRPELIRMMEWAAERLEKLGFKVELVDIGTQTLPDgeelplppvLLGRLGSDpSKKTVLIYGH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 71 SDVVP---TDGqaWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSYD--EEVGCLGVRSLL 145
Cdd:cd05676 94 LDVQPaklEDG--WDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEgmEESGSEGLDELI 171
|
..
gi 1222390563 146 SK 147
Cdd:cd05676 172 EA 173
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
61-165 |
4.17e-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: 84.41 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 61 DRGGVLLSGHSDVVP-TDGQAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLP--LHLAFSYDEEVG 137
Cdd:cd18669 11 GGKRVLLGAHIDVVPaGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKgtVVVAFTPDEEVG 90
|
90 100
....*....|....*....|....*....
gi 1222390563 138 CLGVRSLLSKLQQRP-NPPALCIIGEPTE 165
Cdd:cd18669 91 SGAGKGLLSKDALEEdLKVDYLFVGDATP 119
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
1-114 |
1.16e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 87.27 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 1 MPSSRDLLARLVAFPTVS-----RNSNLALIEFVRDYLQGLGVACELDYNAERSKANLYASIGPSDRGGVLLSGHSDVVP 75
Cdd:PRK07907 17 LPRVRADLEELVRIPSVAadpfrREEVARSAEWVADLLREAGFDDVRVVSADGAPAVIGTRPAPPGAPTVLLYAHHDVQP 96
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1222390563 76 T-DGQAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAV 114
Cdd:PRK07907 97 PgDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAAL 136
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
65-279 |
1.71e-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: 83.84 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 65 VLLSGHSDVVP----TDGQaWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLA---QPLRlPLHLAFSYDEEV- 136
Cdd:cd05674 72 LLLMAHQDVVPvnpeTEDQ-WTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKrgfKPRR-TIILAFGHDEEVg 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 137 GCLGVRSLLSKLQQR--PNPPALCI-----------IGEPTELkPVLGHKGKLAMRCQVQGAACHSAYAPQGvNAIEYAA 203
Cdd:cd05674 150 GERGAGAIAELLLERygVDGLAAILdeggavlegvfLGVPFAL-PGVAEKGYMDVEITVHTPGGHSSVPPKH-TGIGILS 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 204 RLINRL------------GEIGQRLTALERQDARFDPPY-------------------------------STVQTGLIQG 240
Cdd:cd05674 228 EAVAALeanpfppkltpgNPYYGMLQCLAEHSPLPPRSLksnlwlaspllkallasellstspltrallrTTQAVDIING 307
|
250 260 270
....*....|....*....|....*....|....*....
gi 1222390563 241 GRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAETE 279
Cdd:cd05674 308 GVKINALPETATATVNHRIAPGSSVEEVLEHVKNLIADI 346
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
6-170 |
4.63e-17 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 82.13 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVsrNSNLALI-------EFVRDYLQGLGVACELdynAERSKA-NLYASIGpSDRGGVLLSGHSDVVPTD 77
Cdd:PRK08554 5 ELLSSLVSFETV--NDPSKGIkpskecpKFIKDTLESWGIESEL---IEKDGYyAVYGEIG-EGKPKLLFMAHFDVVPVN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 78 GQAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSYDEEVGCLGVRSLLSKLQQRPNPPAL 157
Cdd:PRK08554 79 PEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLNGKVIFAFTGDEEIGGAMAMHIAEKLREEGKLPKY 158
|
170
....*....|...
gi 1222390563 158 CIIGEPTELKPVL 170
Cdd:PRK08554 159 MINADGIGMKPII 171
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
8-294 |
1.15e-16 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 81.14 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 8 LARLVAFPTVSRNSN--------LALIEFVRDYLQGLGVACELDYNAERSKanLY------ASIGPsdrggVLLSGHSDV 73
Cdd:PRK08262 50 LSEAIRFRTISNRDRaeddaaafDALHAHLEESYPAVHAALEREVVGGHSL--LYtwkgsdPSLKP-----IVLMAHQDV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 74 VP-TDG--QAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLA---QPLRlPLHLAFSYDEEVGCLGVRSLLSK 147
Cdd:PRK08262 123 VPvAPGteGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAqgfQPRR-TIYLAFGHDEEVGGLGARAIAEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 148 LQQRPNPPALCI-------------IGEPTELKPVlGHKGKLAMRCQVQGAACHSAyAPQGVNAIEYAARLINRLGE--- 211
Cdd:PRK08262 202 LKERGVRLAFVLdeggaitegvlpgVKKPVALIGV-AEKGYATLELTARATGGHSS-MPPRQTAIGRLARALTRLEDnpl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 212 --------------------IGQRLTA---------LERQDARFDPPYSTVQT----GLIQGGRALNIVPAECQFDFEVR 258
Cdd:PRK08262 280 pmrlrgpvaemfdtlapemsFAQRVVLanlwlfeplLLRVLAKSPETAAMLRTttapTMLKGSPKDNVLPQRATATVNFR 359
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1222390563 259 ALPSDDPQQVAEELRAYA-----ETELLPRMRACSASSAID 294
Cdd:PRK08262 360 ILPGDSVESVLAHVRRAVaddrvEIEVLGGNSEPSPVSSTD 400
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
65-279 |
6.06e-16 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 78.47 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 65 VLLSGHSDVV-PTDGqawtvpPF-ALSER-DGKLYGRGTADMKGFIACVLAAVPRFLAQPL--RLPLHLAFSYDEEVGCL 139
Cdd:PRK07338 95 VLLTGHMDTVfPADH------PFqTLSWLdDGTLNGPGVADMKGGIVVMLAALLAFERSPLadKLGYDVLINPDEEIGSP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 140 GVRSLLSKLQQRpNPPALciIGEPTELKPVLGH--KGKLAMRCQVQGAACHSAYAPQ-GVNAIEYAArlinrlgEIGQRL 216
Cdd:PRK07338 169 ASAPLLAELARG-KHAAL--TYEPALPDGTLAGarKGSGNFTIVVTGRAAHAGRAFDeGRNAIVAAA-------ELALAL 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1222390563 217 TALERQDarfdpPYSTVQTGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAETE 279
Cdd:PRK07338 239 HALNGQR-----DGVTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQV 296
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
14-272 |
9.16e-16 |
|
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: 78.29 E-value: 9.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 14 FPTVSRNSNL-ALIEFVRDYLQGLGVACELDYNAERSKANLYASIG-----PSdrggVLLSGHSDVVPTDGQAWTVPPF- 86
Cdd:TIGR01880 21 INTVQPNPDYaACVDFLIKQADELGLARKTIEFVPGKPVVVLTWPGsnpelPS----ILLNSHTDVVPVFREHWTHPPFs 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 87 ALSERDGKLYGRGTADMKgfiaCV----LAAVPRFLA---QPLRlPLHLAFSYDEEVGClgvRSLLSKLQQRPNPPALCI 159
Cdd:TIGR01880 97 AFKDEDGNIYARGAQDMK----CVgvqyLEAVRNLKAsgfKFKR-TIHISFVPDEEIGG---HDGMEKFAKTDEFKALNL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 160 -------IGEPTELKPVL-GHKGKLAMRCQVQGAACHSA--YAPQGVNAIEYAARLINRLgeigqRLTALERQDARFDPP 229
Cdd:TIGR01880 169 gfaldegLASPDDVYRVFyAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRRF-----RESQFQLLQSNPDLA 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1222390563 230 YSTVQT---GLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEEL 272
Cdd:TIGR01880 244 IGDVTSvnlTKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRL 289
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
52-165 |
1.46e-15 |
|
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: 74.77 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 52 NLYASIGPSDRGG-VLLSGHSDVVP-TDGQAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLP--LH 127
Cdd:cd03873 1 NLIARLGGGEGGKsVALGAHLDVVPaGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKgtIV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1222390563 128 LAFSYDEEVGCLGVRSLLSK-LQQRPNPPALCIIGEPTE 165
Cdd:cd03873 81 VAFTADEEVGSGGGKGLLSKfLLAEDLKVDAAFVIDATA 119
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
28-367 |
1.80e-15 |
|
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: 77.11 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 28 FVRDYLQGLGVACELDYNAERSK---ANLYASIgPSDRGGV---LLSGHSD-VVPTDGqawtVPPfaLSERDGKLYGRGT 100
Cdd:cd05683 28 VLKKKFENLGLSVIEDDAGKTTGggaGNLICTL-KADKEEVpkiLFTSHMDtVTPGIN----VKP--PQIADGYIYSDGT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 101 ----ADMKGFIACVLAAVPRFLAQPLRL-PLHLAFSYDEEVGCLGVRSLLSKLQQRP--------NPPALCIIGEPTELK 167
Cdd:cd05683 101 tilgADDKAGIAAILEAIRVIKEKNIPHgQIQFVITVGEESGLVGAKALDPELIDADygyaldseGDVGTIIVGAPTQDK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 168 PVLGHKGKLAmrcqvqgaacHSAYAPQ-GVNAIEYAARLINR--LGEIGQRLTAlerqdarfdppystvQTGLIQGGRAL 244
Cdd:cd05683 181 INAKIYGKTA----------HAGTSPEkGISAINIAAKAISNmkLGRIDEETTA---------------NIGKFQGGTAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 245 NIVPAECQFDFEVRALpsdDPQQVAEELRAYAET-ELLPRMRACSAssaiDLQPLSAYPGLATEPHSEAAELLALLAGSR 323
Cdd:cd05683 236 NIVTDEVNIEAEARSL---DEEKLDAQVKHMKETfETTAKEKGAHA----EVEVETSYPGFKINEDEEVVKLAKRAANNL 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1222390563 324 DFATVAFGTEGG----LFHQAGIATVICGPGsMAQGHKPDEFVSQQQL 367
Cdd:cd05683 309 GLEINTTYSGGGsdanIINGLGIPTVNLGIG-YENIHTTNERIPIEDL 355
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
14-277 |
2.43e-15 |
|
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: 76.93 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 14 FPTVSRNSNL-ALIEFVRDYLQGLGVACELDYNA----------ERSKANLyasigPSdrggVLLSGHSDVVPTDGQAWT 82
Cdd:cd05646 14 INTVHPNPDYdACVEFLKRQADELGLPVRVIEVVpgkpvvvltwEGSNPEL-----PS----ILLNSHTDVVPVFEEKWT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 83 VPPF-ALSERDGKLYGRGTADMKgfiaCV----LAAVPRFLAQPLRLP--LHLAFSYDEEV-GCLGVRsllsKLQQRPNP 154
Cdd:cd05646 85 HDPFsAHKDEDGNIYARGAQDMK----CVgiqyLEAIRRLKASGFKPKrtIHLSFVPDEEIgGHDGME----KFVKTEEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 155 PALCI-------IGEPTELKPVL-GHKGKLAMRCQVQGAACHSAYAPQGvNAIEYAARLINRLGEIGQRltalERQDARF 226
Cdd:cd05646 157 KKLNVgfaldegLASPTEEYRVFyGERSPWWVVITAPGTPGHGSKLLEN-TAGEKLRKVIESIMEFRES----QKQRLKS 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1222390563 227 DPPY-----STVQTGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAE 277
Cdd:cd05646 232 NPNLtlgdvTTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCA 287
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
2-282 |
2.96e-15 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 76.59 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 2 PSSRDLLARLVAFPTVSRN-SNLALI-EFVRDYLQGLGVACELDYNAERSKANLYASIGPSDRGGVLLSGHSDVVPTDGQ 79
Cdd:PRK06133 37 PAYLDTLKELVSIESGSGDaEGLKQVaALLAERLKALGAKVERAPTPPSAGDMVVATFKGTGKRRIMLIAHMDTVYLPGM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 80 AWTVPpfaLSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLR--LPLHLAFSYDEEVGCLGVRSLLSKLQQRPNPPAL 157
Cdd:PRK06133 117 LAKQP---FRIDGDRAYGPGIADDKGGVAVILHALKILQQLGFKdyGTLTVLFNPDEETGSPGSRELIAELAAQHDVVFS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 158 CiigEPTELKP--VLGHKGKLAMRCQVQGAACHSAYAP-QGVNAIEYAARLINRLGEIGQrltalerqdarfDPPYSTVQ 234
Cdd:PRK06133 194 C---EPGRAKDalTLATSGIATALLEVKGKASHAGAAPeLGRNALYELAHQLLQLRDLGD------------PAKGTTLN 258
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1222390563 235 TGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAETELLP 282
Cdd:PRK06133 259 WTVAKAGTNRNVIPASASAQADVRYLDPAEFDRLEADLQEKVKNKLVP 306
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
52-362 |
3.36e-15 |
|
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: 75.98 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 52 NLYASI-GPSDRGGVLLSGHSDVVPTDGQAWTVppfalSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAF 130
Cdd:cd03896 43 NVVGRLrGTGGGPALLFSAHLDTVFPGDTPATV-----RHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 131 SY---DEEVGCL-GVRSLLSKLQQRPNppaLCIIGEPTELKPVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLI 206
Cdd:cd03896 118 AAnvgEEGLGDLrGARYLLSAHGARLD---YFVVAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 207 NRLGEIGqrltalerqdarfDP--PYSTVQTGLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRAyaeteLLPRM 284
Cdd:cd03896 195 EALYEWA-------------APyvPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPDAELADVQREVEA-----VVSKL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 285 RACSASSAIDLQPLSAYPGLATePHSEAAELLALLAGSRDFATVAFG---TEGGLFHQAGIATVICGPGSMAQGHKPDEF 361
Cdd:cd03896 257 AAKHLRVKARVKPVGDRPGGEA-QGTEPLVNAAVAAHREVGGDPRPGsssTDANPANSLGIPAVTYGLGRGGNAHRGDEY 335
|
.
gi 1222390563 362 V 362
Cdd:cd03896 336 V 336
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
25-288 |
1.77e-14 |
|
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: 74.42 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 25 LIEFVRDYLQGLGVACELDY-NAERSKANLYASIGPSDRGGVL--LSGHSDVVPTDGQAWTVPPFALSeRDG-KLYGRGT 100
Cdd:cd08012 38 VLEALTPYSTENGGPLVIDHvSYVKGRGNIIVEYPGTVDGKTVsfVGSHMDVVTANPETWEFDPFSLS-IDGdKLYGRGT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 101 ADMKGFIAcVLAAVPRFLAQ---PLRLPLHLAFSYDEE---VGCLGVRSLLS--KLQQRPNPPALCIigEPTELKPVLGH 172
Cdd:cd08012 117 TDCLGHVA-LVTELFRQLATekpALKRTVVAVFIANEEnseIPGVGVDALVKsgLLDNLKSGPLYWV--DSADSQPCIGT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 173 KGKLAMRCQVQGAACHSAYAPQGVNAIEYAarlINRLGEIGQRLTA-----LERQDARFDPPYSTVQTGLIQGGRALNIV 247
Cdd:cd08012 194 GGMVTWKLTATGKLFHSGLPHKAINALELV---MEALAEIQKRFYIdfpphPKEEVYGFATPSTMKPTQWSYPGGSINQI 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1222390563 248 PAECQFDFEVRALPSDDPQQVAEELRAY-----AETELLPRMRACS 288
Cdd:cd08012 271 PGECTICGDCRLTPFYDVKEVREKLEEYvddinANIEELPTRGPVS 316
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
28-217 |
3.70e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 73.63 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 28 FVRDYLQGLGVACELdynaERSKAN--LYASIGPSDRGGVLLSGHSDVVPTDG-QAWTVPPFALSERDGKLYGRGTADMK 104
Cdd:PRK06446 30 YLKDTMEKLGIKANI----ERTKGHpvVYGEINVGAKKTLLIYNHYDVQPVDPlSEWKRDPFSATIENGRIYARGASDNK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 105 GFIACVLAAVPRFLAQPlRLPLHLAFSY--DEEVGCLGVRSLLSKLQQRPNPPALCI--IGEPTELKP--VLGHKGKLAM 178
Cdd:PRK06446 106 GTLMARLFAIKHLIDKH-KLNVNVKFLYegEEEIGSPNLEDFIEKNKNKLKADSVIMegAGLDPKGRPqiVLGVKGLLYV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1222390563 179 RCQVQGAA--CHSAYAPQGVNAIEYAARLINRLGEIGQRLT 217
Cdd:PRK06446 185 ELVLRTGTkdLHSSNAPIVRNPAWDLVKLLSTLVDGEGRVL 225
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
65-277 |
6.56e-14 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 72.86 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 65 VLLSGHSDVVPTDG-QAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSY--DEEVGCLGV 141
Cdd:PRK08201 82 VLIYGHYDVQPVDPlNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIegEEEIGSPNL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 142 RSLLSKLQQR---------------PNPPALC------------IIGEPTELkpvlgHKGKL---------AM------- 178
Cdd:PRK08201 162 DSFVEEEKDKlaadvvlisdttllgPGKPAICyglrglaaleidVRGAKGDL-----HSGLYggavpnalhALvqllasl 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 179 -----RCQVQG---------AACHSAYAPQGVNAIEYAARL-INRL-GEIGqrLTALERQDARFDPPYSTVQTGLiQGGR 242
Cdd:PRK08201 237 hdehgTVAVEGfydgvrpltPEEREEFAALGFDEEKLKRELgVDELfGEEG--YTALERTWARPTLELNGVYGGF-QGEG 313
|
250 260 270
....*....|....*....|....*....|....*
gi 1222390563 243 ALNIVPAECQFDFEVRALPSDDPQQVAEELRAYAE 277
Cdd:PRK08201 314 TKTVIPAEAHAKITCRLVPDQDPQEILDLIEAHLQ 348
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
8-377 |
2.02e-12 |
|
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: 68.10 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 8 LARLVAF---PTVSRNSN-----LALIEFVRDYLQGLGVAceldyNAERSKAN----LYAS-IGPSDRGGVLLSGHSDVV 74
Cdd:cd05680 1 LEELFELlriPSVSADPAhkgdvRRAAEWLADKLTEAGFE-----HTEVLPTGghplVYAEwLGAPGAPTVLVYGHYDVQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 75 PTDG-QAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSYD--EEVGCLGVRSLLSKLQQR 151
Cdd:cd05680 76 PPDPlELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEgeEEIGSPSLPAFLEENAER 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 152 ---------------PNPPALCIigeptelkpvlGHKGKLAMRCQVQGAA--CHSA-YAPQGVNAIEYAARLINRLGEIG 213
Cdd:cd05680 156 laadvvlvsdtsmwsPDTPTITY-----------GLRGLAYLEISVTGPNrdLHSGsYGGAVPNPANALARLLASLHDED 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 214 QR------------LTALERQ--------DARF-----------DPPYSTVQ-------------TGLIQGGRALNIVPA 249
Cdd:cd05680 225 GRvaipgfyddvrpLTDAEREawaalpfdEAAFkaslgvpalggEAGYTTLErlwarptldvngiWGGYQGEGSKTVIPS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 250 ECQFDFEVRALPSDDPQQVAEELRAYAETELLPRMRacsassaidlqpLSAYPGLATEPHSEAAELLALLAGSRDFATVa 329
Cdd:cd05680 305 KAHAKISMRLVPGQDPDAIADLLEAHLRAHAPPGVT------------LSVKPLHGGRPYLVPTDHPALQAAERALEEA- 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1222390563 330 FGTE------GG------LFHQA-GIATVICGPGSMAQG-HKPDEFVSQQQLDGCDAMLVRL 377
Cdd:cd05680 372 FGKPpvfvreGGsipivaLFEKVlGIPTVLMGFGLPDDAiHAPNEKFRLECFHKGIEAIAHL 433
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
69-137 |
4.28e-11 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 64.19 E-value: 4.28e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1222390563 69 GHSDVVPTdGQAWTVPPFALSERDGKLYGRGTADMKG-FIACVLA-AVPRFLAQPLRLPLHLAFSYDEEVG 137
Cdd:cd03888 78 GHLDVVPA-GEGWTTDPFKPVIKDGKLYGRGTIDDKGpTIAALYAlKILKDLGLPLKKKIRLIFGTDEETG 147
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
5-105 |
1.01e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 63.01 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 5 RDLLARLVAFPTVSRNSNLA------LIEFVRDYLQGLGVACELDYNAERSKAN-LYAS-IGPSDRGGVLLSGHSDVVPT 76
Cdd:PRK07079 20 FADLARRVAYRTESQNPDRApalrayLTDEIAPALAALGFTCRIVDNPVAGGGPfLIAErIEDDALPTVLIYGHGDVVRG 99
|
90 100 110
....*....|....*....|....*....|.
gi 1222390563 77 DGQAWTVP--PFALSERDGKLYGRGTADMKG 105
Cdd:PRK07079 100 YDEQWREGlsPWTLTEEGDRWYGRGTADNKG 130
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
64-137 |
1.83e-10 |
|
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: 62.01 E-value: 1.83e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1222390563 64 GVLlsGHSDVVPtDGQAWTVPPFALSERDGKLYGRGTADMKG-FIACVLAAvpRFLAQ---PLRLPLHLAFSYDEEVG 137
Cdd:TIGR01887 71 GIL--GHLDVVP-AGDGWTSPPFEPTIKDGRIYGRGTLDDKGpTIAAYYAM--KILKElglKLKKKIRFIFGTDEESG 143
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
38-298 |
5.05e-10 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 60.18 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 38 VACELDYNAE-RSKANLYASIGpsdrGGVLLSGHSDVVPTdgqawTVPPFALSErdgKLYGRGTADMKG-FIACVLAAvp 115
Cdd:PRK00466 39 ISNELNLKLEiLPDSNSFILGE----GDILLASHVDTVPG-----YIEPKIEGE---VIYGRGAVDAKGpLISMIIAA-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 116 rFLAQPLRLPLHLAFSYDEEVGCLGVRSLLSKlQQRPNppaLCIIGEPTE-LKPVLGHKGKLAMRCQVQGAACHSAYAPQ 194
Cdd:PRK00466 105 -WLLNEKGIKVMVSGLADEESTSIGAKELVSK-GFNFK---HIIVGEPSNgTDIVVEYRGSIQLDIMCEGTPEHSSSAKS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 195 GVnAIEYAARLINRLgeigqrltaleRQDARFDPPySTVQTgLIQGGRALNIVPAECQFDFEVRALPSDDPQQVAEELRA 274
Cdd:PRK00466 180 NL-IVDISKKIIEVY-----------KQPENYDKP-SIVPT-IIRAGESYNVTPAKLYLHFDVRYAINNKRDDLISEIKD 245
|
250 260
....*....|....*....|....
gi 1222390563 275 YAETellprmraCSASSAIDLQPL 298
Cdd:PRK00466 246 KFQE--------CGLKIVDETPPV 261
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
64-112 |
1.30e-09 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 59.47 E-value: 1.30e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1222390563 64 GVLlsGHSDVVPTdGQAWTVPPFALSERDGKLYGRGTADMKG-FIACVLA 112
Cdd:PRK07318 83 GIL--GHLDVVPA-GDGWDTDPYEPVIKDGKIYARGTSDDKGpTMAAYYA 129
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
6-113 |
1.44e-09 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 59.60 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 6 DLLARLVAFPTVSRN-----SNLALIEF---VRDYLQGLGvaceLDYnaeRSKAN--LYASIGPS--DRGGVLLsgHSDV 73
Cdd:PRK06156 50 ESLRELVAFPTVRVEgvpqhENPEFIGFkklLKSLARDFG----LDY---RNVDNrvLEIGLGGSgsDKVGILT--HADV 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1222390563 74 VPTDGQAWTVP-----PFALSERDGKLYGRGTADMKGFIACVLAA 113
Cdd:PRK06156 121 VPANPELWVLDgtrldPFKVTLVGDRLYGRGTEDDKGAIVTALYA 165
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
8-135 |
4.03e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 57.78 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 8 LARLVAFPTV----------SRNSNLALiEFVRDYLQGLGVACELD----YNaerskanlYASIGPSDRG-GVLlsGHSD 72
Cdd:PRK07205 17 IKTLVSYPSVlnegengtpfGQAIQDVL-EATLDLCQGLGFKTYLDpkgyYG--------YAEIGQGEELlAIL--CHLD 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1222390563 73 VVPT-DGQAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLAFSY--DEE 135
Cdd:PRK07205 86 VVPEgDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFgtDEE 151
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
8-120 |
2.16e-08 |
|
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: 55.81 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 8 LARLVAFPTVSRNSNLALIE-------FVRDYLQGLGV-ACELDYNAERSKANLYAS-IGPSD---RGGVLLSGHSDVVP 75
Cdd:cd05677 5 LSEFIAFQTVSQSPTTENAEdsrrcaiFLRQLFKKLGAtNCLLLPSGPGTNPIVLATfSGNSSdakRKRILFYGHYDVIP 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1222390563 76 TDG-QAWTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQ 120
Cdd:cd05677 85 AGEtDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQE 130
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
182-277 |
3.08e-07 |
|
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: 51.96 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 182 VQGAACHSAYAPQGVNAIEYAARLINRLGEIgqrltaLERQDARFDPPYSTVqtGLIQGGRALNIVPAECQFDFEVRALP 261
Cdd:TIGR01891 177 IHGKGAHAARPHLGRDALDAAAQLVVALQQI------VSRNVDPSRPAVVSV--GIIEAGGAPNVIPDKASMSGTVRSLD 248
|
90
....*....|....*.
gi 1222390563 262 SDDPQQVAEELRAYAE 277
Cdd:TIGR01891 249 PEVRDQIIDRIERIVE 264
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
168-259 |
1.35e-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: 49.97 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 168 PVLGHKGKLAMRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIgqrltalerqdaRFDP--PYSTVQTGLIQGGRALN 245
Cdd:cd08018 160 PAIYHGASTFLEGTIKGKQAHGARPHLGINAIEAASAIVNAVNAI------------HLDPniPWSVKMTKLQAGGEATN 227
|
90
....*....|....
gi 1222390563 246 IVPAECQFDFEVRA 259
Cdd:cd08018 228 IIPDKAKFALDLRA 241
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
64-251 |
1.52e-05 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 46.70 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 64 GVLLSGHSDVVPTDGqawTVPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLAQPLR--LPLHLAFSYDEEVGCLGV 141
Cdd:PRK07473 77 GILIAGHMDTVHPVG---TLEKLPWRREGNKCYGPGILDMKGGNYLALEAIRQLARAGITtpLPITVLFTPDEEVGTPST 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 142 RSLLSKLQQR------PNPpalciiGEPtELKPVLGHKGKLAMRCQVQGAACHS-AYAPQGVNAIEYAARLInrlgeigQ 214
Cdd:PRK07473 154 RDLIEAEAARnkyvlvPEP------GRP-DNGVVTGRYAIARFNLEATGRPSHAgATLSEGRSAIREMARQI-------L 219
|
170 180 190
....*....|....*....|....*....|....*..
gi 1222390563 215 RLTALERQDArfdppysTVQTGLIQGGRALNIVPAEC 251
Cdd:PRK07473 220 AIDAMTTEDC-------TFSVGIVHGGQWVNCVATTC 249
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
5-119 |
1.70e-05 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 46.72 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 5 RDLLARLVAFPTVSRNSNLA------LIEFVRDYLQGLGVACELDYN--AERSKANLYASIGPSDRGGVLLSGHSDVVPT 76
Cdd:cd05679 7 LAELARRVAVPTESQEPARKpelrayLDQEMRPRFERLGFTVHIHDNpvAGRAPFLIAERIEDPSLPTLLIYGHGDVVPG 86
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1222390563 77 DGQAWT--VPPFALSERDGKLYGRGTADMKGFIACVLAAVPRFLA 119
Cdd:cd05679 87 YEGRWRdgRDPWTVTVWGERWYGRGTADNKGQHSINMAALRQVLE 131
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
182-277 |
2.62e-05 |
|
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: 45.88 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 182 VQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRltalerqdaRFDPPYSTVQT-GLIQGGRALNIVPAECQFDFEVRAL 260
Cdd:COG1473 190 IKGKGGHAAAPHLGIDPIVAAAQIVTALQTIVSR---------NVDPLDPAVVTvGIIHGGTAPNVIPDEAELEGTVRTF 260
|
90
....*....|....*..
gi 1222390563 261 PSDDPQQVAEELRAYAE 277
Cdd:COG1473 261 DPEVRELLEERIERIAE 277
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
178-302 |
3.89e-05 |
|
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: 45.28 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 178 MRCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRltalerqdaRFDPPYSTVQT-GLIQGGRALNIVPAECQFDFE 256
Cdd:cd03886 174 FEITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVVSR---------ELDPLEPAVVTvGKFHAGTAFNVIPDTAVLEGT 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1222390563 257 VRALPSDDPQQVAEELRAYAEtellprmRACSASSA-IDLQPLSAYP 302
Cdd:cd03886 245 IRTFDPEVREALEARIKRLAE-------GIAAAYGAtVELEYGYGYP 284
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
5-234 |
4.09e-05 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 45.41 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 5 RDLLARLVAFPTVSRNSNLALI-EFVRDYLQglgvacELDY-------------NAERSKANLYASI-GPSD-RGGVLLS 68
Cdd:cd05654 4 EQLLKSLVSWPSVTGTEGERSFaDFLKEILK------ELPYfkenpshvwqllpPDDLGRRNVTALVkGKKPsKRTIILI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 69 GHSDVVPTDG----QAWTVPPFALSE--------------RDGK----LYGRGTADMKGFIACVLAAVpRFLAQPLRLP- 125
Cdd:cd05654 78 SHFDTVGIEDygelKDIAFDPDELTKafseyveeldeevrEDLLsgewLFGRGTMDMKSGLAVHLALL-EQASEDEDFDg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 126 -LHLAFSYDEEVGCLGVRS----LLSKLQQRPNPPALCIIGEP-TELKP-------VLGHKGKLAMRCQVQGAACHSAYA 192
Cdd:cd05654 157 nLLLMAVPDEEVNSRGMRAavpaLLELKKKHDLEYKLAINSEPiFPQYDgdqtryiYTGSIGKILPGFLCYGKETHVGEP 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1222390563 193 PQGVNAiEYAARLINRLGEIGQRLTalERQDARFDPPYSTVQ 234
Cdd:cd05654 237 FAGINA-NLMASEITARLELNADLC--EKVEGEITPPPVCLK 275
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
5-209 |
4.34e-05 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 45.62 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 5 RDLLARLVAFPTVSRNSN-LALIEFVRDYLQglgvacELDY---NAERSK-----------ANLYASI-GPSD-RGGVLL 67
Cdd:COG4187 11 EELLCELVSIPSVTGTEGeKEVAEFIYEKLS------ELPYfqeNPEHLGlhplpddplgrKNVTALVkGKGEsKKTVIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 68 SGHSDVVPTDG----QAWTVPPFALSE--RDGKL--------------YGRGTADMKGFIACVLAAVPRFlAQPLRLPLH 127
Cdd:COG4187 85 ISHFDVVDVEDygslKPLAFDPEELTEalKEIKLpedvrkdlesgewlFGRGTMDMKAGLALHLALLEEA-SENEEFPGN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 128 LAFSY--DEEVGCLGVRS---LLSKLQQRPN-PPALCIIGEPTELK-PVLGHK-------GKLaMRC-QVQGAACHSAYA 192
Cdd:COG4187 164 LLLLAvpDEEVNSAGMRAavpLLAELKEKYGlEYKLAINSEPSFPKyPGDETRyiytgsiGKL-MPGfYCYGKETHVGEP 242
|
250
....*....|....*..
gi 1222390563 193 PQGVNAIEYAARLINRL 209
Cdd:COG4187 243 FSGLNANLLASELTREL 259
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
1-137 |
2.31e-04 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 42.97 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 1 MPSSRDLLARLVAFPTVSRNSNLA-----LIEFVRDYLQGLGVACELdynaeRSKANLYASIG--PSDRGG---VLLSGH 70
Cdd:PRK09104 16 LDASLERLFALLRIPSISTDPAYAadcrkAADWLVADLASLGFEASV-----RDTPGHPMVVAhhEGPTGDaphVLFYGH 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1222390563 71 SDVVPTDGQA-WTVPPF--ALSER-DGK--LYGRGTADMKGFIACVLAAVPRFLAQPLRLPLHLA--FSYDEEVG 137
Cdd:PRK09104 91 YDVQPVDPLDlWESPPFepRIKETpDGRkvIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTilFEGEEESG 165
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
182-277 |
6.28e-04 |
|
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349920 [Multi-domain] Cd Length: 367 Bit Score: 41.48 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 182 VQGAACHSAYAPQGVNAIEYAARLINrlgeigQRLTALERQdarFDPPYSTVQT-GLIQGGRALNIVPAECQFDFEVRAL 260
Cdd:cd05670 179 FIGKSGHAAYPHNANDMVVAAANFVT------QLQTIVSRN---VDPIDGAVVTiGKIHAGTARNVIAGTAHLEGTIRTL 249
|
90
....*....|....*..
gi 1222390563 261 PSDDPQQVAEELRAYAE 277
Cdd:cd05670 250 TQEMMELVKQRVRDIAE 266
|
|
| M20_Acy1L2-like |
cd09849 |
M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
174-276 |
6.41e-04 |
|
M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli , to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. 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: 349947 [Multi-domain] Cd Length: 389 Bit Score: 41.69 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 174 GKLAMRCQVQGAACHSAYAP-QGVNAIEYAARLINRLGeiGQRLTALERQDARFDPPystvqtgLIQGGRALNIVPAECQ 252
Cdd:cd09849 188 GFIGKKVKFTGKESHAGSAPfSGINALNAATLAINNVN--AQRETFKESDKVRFHPI-------ITKGGDIVNVVPADVR 258
|
90 100
....*....|....*....|....*
gi 1222390563 253 FDFEVRALPSDDPQQVAEEL-RAYA 276
Cdd:cd09849 259 VESYVRARSIDYMKEANSKVnRALR 283
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
179-277 |
2.38e-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: 39.63 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 179 RCQVQGAACHSAYAPQGVNAIEYAARLINRLGEIGQRltalerqdaRFDPPYSTVQT-GLIQGGRALNIVPAECQFDFEV 257
Cdd:cd08019 172 KIEVKGKGGHGSMPHQGIDAVLAAASIVMNLQSIVSR---------EIDPLEPVVVTvGKLNSGTRFNVIADEAKIEGTL 242
|
90 100
....*....|....*....|
gi 1222390563 258 RALPSDDPQQVAEELRAYAE 277
Cdd:cd08019 243 RTFNPETREKTPEIIERIAK 262
|
|
| M20_Acy1L2 |
cd03887 |
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
184-277 |
6.87e-03 |
|
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, Aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase) subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349883 [Multi-domain] Cd Length: 360 Bit Score: 38.33 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222390563 184 GAACHSAYAP-QGVNAIEYAARLINRLGEIGQRLtaleRQDARfdppystVQtGLI-QGGRALNIVPAECQFDFEVRALP 261
Cdd:cd03887 167 GKAAHAAAAPwEGINALDAAVLAYNNISALRQQL----KPTVR-------VH-GIItEGGKAPNIIPDYAEAEFYVRAPT 234
|
90
....*....|....*.
gi 1222390563 262 SDDPQQVAEELRAYAE 277
Cdd:cd03887 235 LKELEELTERVIACFE 250
|
|
| |
