|
Name |
Accession |
Description |
Interval |
E-value |
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
50-416 |
1.56e-168 |
|
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: 483.63 E-value: 1.56e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 50 VIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGlvVGDNIVGKIKGRGGKNLLLMSHMDTVYLKGIL 129
Cdd:cd03885 1 MLDLLERLVNIESGTYDKEGVDRVAELLAEELEALGFTVERRPLGE--FGDHLIATFKGTGGKRVLLIGHMDTVFPEGTL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 130 AKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKLADYVLSFEPT 209
Cdd:cd03885 79 AFRPFTVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRELIEEEAKGADYVLVFEPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 210 SAgDEKLSLGTSGIAYVQVQITGKASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFQWTIAKAGQVSNIIPASAT 289
Cdd:cd03885 159 RA-DGNLVTARKGIGRFRLTVKGRAAHAGNAPEKGRSAIYELAHQVLALHALTDPEKGTTVNVGVISGGTRVNVVPDHAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 290 LNADVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYKEAGGTLgVEERTGGGTD 369
Cdd:cd03885 238 AQVDVRFATAEEADRVEEALRAIVATTLVPGTSVELTGGLNRPPMEETPASRRLLARAQEIAAELGLTL-DWEATGGGSD 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 3717826 370 AAYAALSGKPVIESLGLPGFGYHSDkAEYVDISAIPRRLYMAARLIM 416
Cdd:cd03885 317 ANFTAALGVPTLDGLGPVGGGAHTE-DEYLELDSLVPRIKLLARLLM 362
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
22-418 |
4.04e-168 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 484.13 E-value: 4.04e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 22 STQVCTGSALAQKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRsKSAGLVVGDN 101
Cdd:PRK06133 11 LAAAAAAGAAAAAPDAELLAAAQQEQPAYLDTLKELVSIESGSGDAEGLKQVAALLAERLKALGAKVER-APTPPSAGDM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 102 IVGKIKGRGGKNLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTD 181
Cdd:PRK06133 90 VVATFKGTGKRRIMLIAHMDTVYLPGMLAKQPFRIDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 182 EEKGSFGSRDLIQEEAKLADYVLSFEPTSAgDEKLSLGTSGIAYVQVQITGKASHAGAAPELGVNALVEASDLVLRTMNI 261
Cdd:PRK06133 170 EETGSPGSRELIAELAAQHDVVFSCEPGRA-KDALTLATSGIATALLEVKGKASHAGAAPELGRNALYELAHQLLQLRDL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 262 DDKAKNLRFQWTIAKAGQVSNIIPASATLNADVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIVTRGRPAFNAGEGGK 341
Cdd:PRK06133 249 GDPAKGTTLNWTVAKAGTNRNVIPASASAQADVRYLDPAEFDRLEADLQEKVKNKLVPDTEVTLRFERGRPPLEANAASR 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3717826 342 KLVDKAVAYYKEAGGTLGV-EERTGGGTDAAYAALSGK-PVIESLGLPGFGYHSDkAEYVDISAIPRRLYMAARLIMDL 418
Cdd:PRK06133 329 ALAEHAQGIYGELGRRLEPiDMGTGGGTDAAFAAGSGKaAVLEGFGLVGFGAHSN-DEYIELNSIVPRLYLLTRMIMEL 406
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
39-418 |
1.83e-80 |
|
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: 258.28 E-value: 1.83e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 39 LFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAagnFLEAELKNLGFTVTRSKSAGLVvgDNIVGKIKGR-GGKNLLLM 117
Cdd:COG0624 3 VLAAIDAHLDEALELLRELVRIPSVSGEEAAAAE---LLAELLEALGFEVERLEVPPGR--PNLVARRPGDgGGPTLLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 118 SHMDTVYLKGILA--KAPF--RVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLI 193
Cdd:COG0624 78 GHLDVVPPGDLELwtSDPFepTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSPGARALV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 194 QEEAKL--ADYVLSFEPTSAGdeKLSLGTSGIAYVQVQITGKASHAGaAPELGVNALVEASDLVLRtmnIDDKAKNLR-- 269
Cdd:COG0624 158 EELAEGlkADAAIVGEPTGVP--TIVTGHKGSLRFELTVRGKAAHSS-RPELGVNAIEALARALAA---LRDLEFDGRad 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 270 -------FQWTIAKAGQVSNIIPASATLNADVRYARNEDFDAAMKTLEERAqQKKLPEADVKV-IVTRGRPAFNAGEGGk 341
Cdd:COG0624 232 plfgrttLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALL-AAAAPGVEVEVeVLGDGRPPFETPPDS- 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3717826 342 KLVDKAVAYYKEAGGTLGVEERTGGGTDAAYAALS-GKPVIEsLGL-PGFGYHSDKaEYVDISAIPRRLYMAARLIMDL 418
Cdd:COG0624 310 PLVAAARAAIREVTGKEPVLSGVGGGTDARFFAEAlGIPTVV-FGPgDGAGAHAPD-EYVELDDLEKGARVLARLLERL 386
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
115-417 |
2.20e-48 |
|
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: 170.99 E-value: 2.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 115 LLMSHMDTVYlKGILAKAPFR-VEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDyGTITVLFNTDEEKGSFGSRDLI 193
Cdd:pfam01546 1 LLRGHMDVVP-DEETWGWPFKsTEDGKLYGRGHDDMKGGLLAALEALRALKEEGLKK-GTVKLLFQPDEEGGMGGARALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 194 QE---EAKLADYVLSF---EPTSAGDEK---LSLGTSGIAYVQVQITGKASHAgAAPELGVNALVEASDLVLRTMNIDDK 264
Cdd:pfam01546 79 EDgllEREKVDAVFGLhigEPTLLEGGIaigVVTGHRGSLRFRVTVKGKGGHA-STPHLGVNAIVAAARLILALQDIVSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 265 AKNLRF-------QWTIAKAGqvSNIIPASATLNADVRYARNEDFDAAMKTLEERAqQKKLPEADVKVIVTRGRPAFNAG 337
Cdd:pfam01546 158 NVDPLDpavvtvgNITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERIREIL-EAIAAAYGVKVEVEYVEGGAPPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 338 EGGKKLVDKAVAYYKEAGGTLGVEERTG--GGTDAAYAALSGKPVIESLGLPGFGYHSdKAEYVDISAIPRRLYMAARLI 415
Cdd:pfam01546 235 VNDSPLVAALREAAKELFGLKVELIVSGsmGGTDAAFFLLGVPPTVVFFGPGSGLAHS-PNEYVDLDDLEKGAKVLARLL 313
|
..
gi 3717826 416 MD 417
Cdd:pfam01546 314 LK 315
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
49-418 |
6.72e-48 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 171.51 E-value: 6.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 49 AVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTR-SKSAGLvvGDNIVGKI--KGRGGKNLLLMSHMDTVYL 125
Cdd:PRK07473 12 AMLAGLRPWVECESPTWDAAAVNRMLDLAARDMAIMGATIERiPGRQGF--GDCVRARFphPRQGEPGILIAGHMDTVHP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 126 KGILAKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKLADYVLS 205
Cdd:PRK07473 90 VGTLEKLPWRREGNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFTPDEEVGTPSTRDLIEAEAARNKYVLV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 206 FEPTSAgDEKLSLGTSGIAYVQVQITGKASHAGAAPELGVNALVEASD--LVLRTMNIDDkaknLRFQWTIAKAGQVSNI 283
Cdd:PRK07473 170 PEPGRP-DNGVVTGRYAIARFNLEATGRPSHAGATLSEGRSAIREMARqiLAIDAMTTED----CTFSVGIVHGGQWVNC 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 284 IPASATLNADVRYARNEDFD---AAMKTLEERaqqkklpEADVKVIVTRG--RPAFNAGEGGKKLVDKAvayyKEAGGTL 358
Cdd:PRK07473 245 VATTCTGEALSMAKRQADLDrgvARMLALSGT-------EDDVTFTVTRGvtRPVWEPDAGTMALYEKA----RAIAGQL 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3717826 359 GVE---ERTGGGTDAAYAALSGKPVIESLGLPGFGYHSDKaEYVDISAIPRRLYMAARLIMDL 418
Cdd:PRK07473 314 GLSlphGSAGGGSDGNFTGAMGIPTLDGLGVRGADYHTLN-EHIEVDSLAERGRLMAGLLATL 375
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
43-418 |
1.15e-45 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 166.29 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 43 ATDEQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVV------------GDNIVGKIKGRG 110
Cdd:PRK07338 12 IDDRQAPMLEQLIAWAAINSGSRNLDGLARMAELLADAFAALPGEIELIPLPPVEVidadgrtleqahGPALHVSVRPEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 111 GKNLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSR 190
Cdd:PRK07338 92 PRQVLLTGHMDTVFPADHPFQTLSWLDDGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLGYDVLINPDEEIGSPASA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 191 DLIQEEAKLADYVLSFEPTSAgDEKLSLGTSGIAYVQVQITGKASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRF 270
Cdd:PRK07338 172 PLLAELARGKHAALTYEPALP-DGTLAGARKGSGNFTIVVTGRAAHAGRAFDEGRNAIVAAAELALALHALNGQRDGVTV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 271 QwtIAK--AGQVSNIIPASATLNADVRYARNED---FDAAMKTLEERAQQKklPEADVKVIVTRGRPA--FNAgeGGKKL 343
Cdd:PRK07338 251 N--VAKidGGGPLNVVPDNAVLRFNIRPPTPEDaawAEAELKKLIAQVNQR--HGVSLHLHGGFGRPPkpIDA--AQQRL 324
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3717826 344 VDkAVayyKEAGGTLGVEER---TGGGTDAAYAALSGKPVIESLGLPGFGYHSDkAEYVDISAIPRRLYMAARLIMDL 418
Cdd:PRK07338 325 FE-AV---QACGAALGLTIDwkdSGGVCDGNNLAAAGLPVVDTLGVRGGNIHSE-DEFVILDSLVERAQLSALILMRL 397
|
|
| PDGF |
smart00141 |
Platelet-derived and vascular endothelial growth factors (PDGF, VEGF) family; Platelet-derived ... |
454-536 |
5.08e-45 |
|
Platelet-derived and vascular endothelial growth factors (PDGF, VEGF) family; Platelet-derived growth factor is a potent activator for cells of mesenchymal origin. PDGF-A and PDGF-B form AA and BB homodimers and an AB heterodimer. Members of the VEGF family are homologues of PDGF.
Pssm-ID: 197537 Cd Length: 83 Bit Score: 154.12 E-value: 5.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 454 SYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCE 533
Cdd:smart00141 1 SQCKPRETVVEVSREYPDETNFLFKPPCVTVKRCGGCCNDEGLECVPTETSNVTMQLLEISRPLSQHLVEVSFEEHTKCE 80
|
...
gi 3717826 534 CRP 536
Cdd:smart00141 81 CRP 83
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
54-406 |
9.18e-45 |
|
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: 162.85 E-value: 9.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 54 LEKLVNIETGTGDAEGIAAagnFLEAELKNLGFTVTRSKSAGLvvgDNIVGKIKGRGGKNLLLMSHMDTVYLKGILA--K 131
Cdd:cd08659 3 LQDLVQIPSVNPPEAEVAE---YLAELLAKRGYGIESTIVEGR---GNLVATVGGGDGPVLLLNGHIDTVPPGDGDKwsF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 132 APF--RVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEE-AKLADYVLSFEP 208
Cdd:cd08659 77 PPFsgRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLEAGyADRLDALIVGEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 209 TsagDEKLSLGTSGIAYVQVQITGKASHAgAAPELGVNALVEASDLV--LRTM----NIDDKAKNLRFQWTIAKAGQVSN 282
Cdd:cd08659 157 T---GLDVVYAHKGSLWLRVTVHGKAAHS-SMPELGVNAIYALADFLaeLRTLfeelPAHPLLGPPTLNVGVINGGTQVN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 283 IIPASATLNADVRYARNEDFDAAMKTLEERAQQKKlPEADVKVIVTRGRPAFNAGEGgkKLVDKAVAYYKEAGGTLGVEE 362
Cdd:cd08659 233 SIPDEATLRVDIRLVPGETNEGVIARLEAILEEHE-AKLTVEVSLDGDPPFFTDPDH--PLVQALQAAARALGGDPVVRP 309
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 3717826 363 rTGGGTDAAY-AALSGKPVIE----SLGLPgfgyHSdKAEYVDISAIPR 406
Cdd:cd08659 310 -FTGTTDASYfAKDLGFPVVVygpgDLALA----HQ-PDEYVSLEDLLR 352
|
|
| PDGF |
cd00135 |
Platelet-derived and vascular endothelial growth factors (PDGF, VEGF) family domain; PDGF is a ... |
454-537 |
1.12e-41 |
|
Platelet-derived and vascular endothelial growth factors (PDGF, VEGF) family domain; PDGF is a potent activator for cells of mesenchymal origin; PDGF-A and PDGF-B form AA and BB homodimers and an AB heterodimer; VEGF is a potent mitogen in embryonic and somatic angiogenesis with a unique specificity for vascular endothelial cells; VEGF forms homodimers and exists in 4 different isoforms; overall, the VEGF monomer resembles that of PDGF, but its N-terminal segment is helical rather than extended; the cysteine knot motif is a common feature of this domain
Pssm-ID: 238079 Cd Length: 86 Bit Score: 145.20 E-value: 1.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 454 SYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPH--QGQHIGEMSFLQHNK 531
Cdd:cd00135 1 SSCKPRETLVEISEELPDETNTIFKPPCVEVKRCGGCCNDESLECVPTETSNVTMQVLKISPKrkPRSKLVEISFEEHTE 80
|
....*.
gi 3717826 532 CECRPK 537
Cdd:cd00135 81 CECRPR 86
|
|
| PDGF |
pfam00341 |
PDGF/VEGF domain; |
456-534 |
4.29e-39 |
|
PDGF/VEGF domain;
Pssm-ID: 425620 Cd Length: 82 Bit Score: 137.80 E-value: 4.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 456 CHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIK---PHQGQHIGEMSFLQHNKC 532
Cdd:pfam00341 1 CKPRETLVEIRRELPDETNAFFKPSCVEVQRCSGCCNDEGLECVPTETHNVTMQVLKIEyapRRPSPELVEVSFEEHVQC 80
|
..
gi 3717826 533 EC 534
Cdd:pfam00341 81 EC 82
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
46-418 |
6.79e-39 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 146.35 E-value: 6.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 46 EQPAVIKTLEKLVNIETGTGDAEGIAaagNFLEAELKNLGFTVTRSKSAglvvgdNIVGKIKGRGGKN---LLLMSHMDT 122
Cdd:COG2195 1 NPERLLERFLEYVKIPTPSDHEEALA---DYLVEELKELGLEVEEDEAG------NVIATLPATPGYNvptIGLQAHMDT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 123 V--YL-KGILAkapfRVEGD--KAYGPGI--ADDKGGNAVILHTLKLLKEYGVrDYGTITVLFNTDEEKGSFGSRDLiqE 195
Cdd:COG2195 72 VpqFPgDGIKP----QIDGGliTADGTTTlgADDKAGVAAILAALEYLKEPEI-PHGPIEVLFTPDEEIGLRGAKAL--D 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 196 EAKL-ADYVLSFEptsAGDE-KLSLGTSGIAYVQVQITGKASHAGAAPELGVNALVEASDLvLRTMNIDDKAKNLRFQWT 273
Cdd:COG2195 145 VSKLgADFAYTLD---GGEEgELEYECAGAADAKITIKGKGGHSGDAKEKMINAIKLAARF-LAALPLGRIPEETEGNEG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 274 IAKAGQVSNIIPASATLNADVRYARNEDFDAAMKTLEERAQQ--KKLPEADVKVIVTRGRPAFNAgEGGKKLVDKAVAYY 351
Cdd:COG2195 221 FIHGGSATNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEenAKYGVGVVEVEIEDQYPNWKP-EPDSPIVDLAKEAY 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3717826 352 KEAGGTLGVeERTGGGTDAAYaaLSGK--PVIeSLGLPGFGYHSdKAEYVDISAiprrLYMAARLIMDL 418
Cdd:COG2195 300 EELGIEPKI-KPIRGGLDGGI--LSFKglPTP-NLGPGGHNFHS-PDERVSIES----MEKAWELLVEI 359
|
|
| VEGF_C |
pfam14554 |
VEGF heparin-binding domain; This short domain is found at the C-terminus of VEGF. It has been ... |
547-595 |
4.08e-33 |
|
VEGF heparin-binding domain; This short domain is found at the C-terminus of VEGF. It has been shown to have heparin binding activity.
Pssm-ID: 405273 Cd Length: 49 Bit Score: 120.49 E-value: 4.08e-33
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 3717826 547 CGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR 595
Cdd:pfam14554 1 CSTCSERRKRLFVQDPETCKCSCKHTDADCKSRQLELNERTCRCDKPRR 49
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
50-418 |
4.56e-33 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 130.88 E-value: 4.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 50 VIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVT-----RSKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTVY 124
Cdd:PRK08651 8 IVEFLKDLIKIPTVNPPGENYEEIAEFLRDTLEELGFSTEiievpNEYVKKHDGPRPNLIARRGSGNPHLHFNGHYDVVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 125 LKGILAKA-PF--RVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVrdyGTITVLFNTDEEKGSFGSRDLIQEEAKLAD 201
Cdd:PRK08651 88 PGEGWSVNvPFepKVKDGKVYGRGASDMKGGIAALLAAFERLDPAGD---GNIELAIVPDEETGGTGTGYLVEEGKVTPD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 202 YVLSFEPTsaGDEKLSLGTSGIAYVQVQITGKASHaGAAPELGVNALVEASDLVLRTMNI-----------DDKAKNLRF 270
Cdd:PRK08651 165 YVIVGEPS--GLDNICIGHRGLVWGVVKVYGKQAH-ASTPWLGINAFEAAAKIAERLKSSlstikskyeydDERGAKPTV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 271 QW---TIaKAGQVSNIIPASATLNADVR----YARNEDFDAAMKTLEERAqqKKLPeADVKVIVTRGRPAFnAGEGGKKL 343
Cdd:PRK08651 242 TLggpTV-EGGTKTNIVPGYCAFSIDRRlipeETAEEVRDELEALLDEVA--PELG-IEVEFEITPFSEAF-VTDPDSEL 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3717826 344 VDKAVAYYKEAGGTLGVEERTGGGTDAAYAALSGKPVIeSLGlPG--FGYHSDKaEYVDISAIPRrlymAARLIMDL 418
Cdd:PRK08651 317 VKALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTV-VYG-PGelELAHAPD-EYVEVKDVEK----AAKVYEEV 386
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
51-404 |
2.79e-30 |
|
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: 122.51 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 51 IKTLEKLVNIET--GTGDAEGIAAagNFLEAELKNLGFTVTR---SKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTVYl 125
Cdd:TIGR01910 1 VELLKDLISIPSvnPPGGNEETIA--NYIKDLLREFGFSTDVieiTDDRLKVLGKVVVKEPGNGNEKSLIFNGHYDVVP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 126 KGILAK---APFR--VEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEA-KL 199
Cdd:TIGR01910 78 AGDLELwktDPFKpvEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLLQRGYfKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 200 ADYVLSFEPTsaGDEKLSLGTSGIAYVQVQITGKASHAGaAPELGVNALVEASDLV------LRTMNIDDKAKN----LR 269
Cdd:TIGR01910 158 ADGVLIPEPS--GGDNIVIGHKGSIWFKLRVKGKQAHAS-FPQFGVNAIMKLAKLItelnelEEHIYARNSYGFipgpIT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 270 FQWTIAKAGQVSNIIPASATLNADVRYARNEDFDAAMKTLEE-RAQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAV 348
Cdd:TIGR01910 235 FNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDvVKALSKSDGWLYENEPVVKWSGPNETPPDSRLVKALE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 3717826 349 AYYKEAGGTLGVEERTGGGTDAAYAALSGKPVIE-SLGLPGFGYHSDkaEYVDISAI 404
Cdd:TIGR01910 315 AIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVyGPGDLETAHQVN--EYISIKNL 369
|
|
| PHA02661 |
PHA02661 |
vascular endothelial growth factor like protein; Provisional |
434-537 |
7.88e-30 |
|
vascular endothelial growth factor like protein; Provisional
Pssm-ID: 177444 Cd Length: 146 Bit Score: 114.72 E-value: 7.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 434 AEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIM-- 511
Cdd:PHA02661 26 GSTGSSSASSLSSWLDTSDKSSCQPRDTVVQLSDEYPGNTNDRYNPRCVTVRRCGGCCNDESQICTPTETSNVTVTVMlt 105
|
90 100
....*....|....*....|....*...
gi 3717826 512 --RIKPHQGQHIGEMSFLQHNKCECRPK 537
Cdd:PHA02661 106 svSGSTGATSNFQTISVEEHTKCKCEFK 133
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
50-418 |
1.39e-29 |
|
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: 120.25 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 50 VIKTLEKLVNIETGTGDAEGIAAagnFLEAELKNLGFTVTR---SKSAGLVVGdNIVGKIKG--RGGKNLLLMSHMDTVy 124
Cdd:cd05683 5 LINTFLELVQIDSETLHEKEISK---VLKKKFENLGLSVIEddaGKTTGGGAG-NLICTLKAdkEEVPKILFTSHMDTV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 125 LKGILAKaPFRVEGDKAYGPGI----ADDKGGNAVILHTLKLLKEYGVRdYGTITVLFNTDEEKGSFGSRDLIQEEAKlA 200
Cdd:cd05683 80 TPGINVK-PPQIADGYIYSDGTtilgADDKAGIAAILEAIRVIKEKNIP-HGQIQFVITVGEESGLVGAKALDPELID-A 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 201 DYvlSFEPTSAGD-EKLSLGTSGIAYVQVQITGKASHAGAAPELGVNALVEASDLVLRtMN---IDDK--AKNLRFQwti 274
Cdd:cd05683 157 DY--GYALDSEGDvGTIIVGAPTQDKINAKIYGKTAHAGTSPEKGISAINIAAKAISN-MKlgrIDEEttANIGKFQ--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 275 akAGQVSNIIPASATLNADVRYARNEDFDAAMK----TLEERAQQKKlpeADVKVIVTRGRPAFNAGEGgkklvDKAVAY 350
Cdd:cd05683 231 --GGTATNIVTDEVNIEAEARSLDEEKLDAQVKhmkeTFETTAKEKG---AHAEVEVETSYPGFKINED-----EEVVKL 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3717826 351 YKEAGGTLGVE---ERTGGGTDAAyaalsgkpVIESLGLP----GFGY---HSdKAEYVDISAiprrLYMAARLIMDL 418
Cdd:cd05683 301 AKRAANNLGLEintTYSGGGSDAN--------IINGLGIPtvnlGIGYeniHT-TNERIPIED----LYDTAVLVVEI 365
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
53-415 |
7.66e-28 |
|
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: 115.00 E-value: 7.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 53 TLEKLVNIETGTGDAEGiaAAGNFLEAELKNLGFTVTRSKSAGlvvGD--NIVGKIKGRGGKNLLLMSHMDTVYLKG-IL 129
Cdd:cd03894 2 LLARLVAFDTVSRNSNL--ALIEYVADYLAALGVKSRRVPVPE---GGkaNLLATLGPGGEGGLLLSGHTDVVPVDGqKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 130 AKAPFRV--EGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRdyGTITVLFNTDEEKGSFGSRDLIQEEAKL---ADYVL 204
Cdd:cd03894 77 SSDPFTLteRDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLR--KPLHLAFSYDEEVGCLGVRHLIAALAARggrPDAAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 205 SFEPTSAgdeKLSLGTSGIAYVQVQITGKASHAgAAPELGVNALVEASDLVLRTMNI-DDKAKNLR----------FQWT 273
Cdd:cd03894 155 VGEPTSL---QPVVAHKGIASYRIRVRGRAAHS-SLPPLGVNAIEAAARLIGKLRELaDRLAPGLRdppfdppyptLNVG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 274 IAKAGQVSNIIPASATLNADVRYARNEDFDAAMKTLEERAQQKKL-PEADVKVIVTRGRPAFNAGEGgkklvDKAVAYYK 352
Cdd:cd03894 231 LIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEfPEAGIEVEPLFEVPGLETDED-----APLVRLAA 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3717826 353 EAGGTLGVeERTGGGTDAAYAALSGKPVIeSLGlPGFGYHSDKA-EYVDISAIPRRLYMAARLI 415
Cdd:cd03894 306 ALAGDNKV-RTVAYGTEAGLFQRAGIPTV-VCG-PGSIAQAHTPdEFVELEQLDRCEEFLRRLI 366
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
101-411 |
1.08e-27 |
|
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: 110.21 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 101 NIVGKIKGR-GGKNLLLMSHMDTVYLKGILAKAPF----RVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTIT 175
Cdd:cd18669 1 NVIARYGGGgGGKRVLLGAHIDVVPAGEGDPRDPPffvdTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 176 VLFNTDEEKGSFGSRDLI----QEEAKLADYVLSFEPTsagdeklslgtsgiayvqvqitgkashagaapelgvnalvea 251
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLskdaLEEDLKVDYLFVGDAT------------------------------------------ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 252 sdlvlrtmniddkaknlrfqWTIAKAGQVSNiipasatlnadvryarnedfdaamktleeraqqkklpeadvkvivtrgr 331
Cdd:cd18669 119 --------------------PAPQKGVGIRT------------------------------------------------- 129
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 332 pafnageggkKLVDKAVAYYKEAGGTLGVEERTGGGTDAAYAALSGKPVIESLGLPGFGYHSdKAEYVDISAIPRRLYMA 411
Cdd:cd18669 130 ----------PLVDALSEAARKVFGKPQHAEGTGGGTDGRYLQELGIPGVTLGAGGGKGAHS-PNERVNLEDLESALAVL 198
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
51-401 |
2.18e-25 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 107.86 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 51 IKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVVGD--NIVGkikGRGGKNLLLMSHMDTVYLKGI 128
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDNTSAIAAYIKLLLEDLGYPVELHEPPEEIYGVvsNIVG---GRKGKRLLFNGHYDVVPAGDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 129 LA--KAPF--RVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSF-GSRDLIQEEAKLADYV 203
Cdd:cd08011 78 EGwtVDPYsgKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRaGTKYLLEKVRIKPNDV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 204 LSFEPTsaGDEKLSLGTSGIAYVQVQITGKASHaGAAPELGVNALVEASDLVLRTMNIdDKAKNLrfqwTIAKAGQVSNI 283
Cdd:cd08011 158 LIGEPS--GSDNIRIGEKGLVWVIIEITGKPAH-GSLPHRGESAVKAAMKLIERLYEL-EKTVNP----GVIKGGVKVNL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 284 IPASATLNADVRYARNEDFDAAMKTLEERaqqkkLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYKEaggTLGVEER 363
Cdd:cd08011 230 VPDYCEFSVDIRLPPGISTDEVLSRIIDH-----LDSIEEVSFEIKSFYSPTVSNPDSEIVKKTEEAITE---VLGIRPK 301
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 3717826 364 T---GGGTDAAYAALSGKPVIE-SLGLPGFGYHSDkaEYVDI 401
Cdd:cd08011 302 EvisVGASDARFYRNAGIPAIVyGPGRLGQMHAPN--EYVEI 341
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
53-415 |
1.92e-24 |
|
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: 105.29 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 53 TLEKLVNIETGTGDAEgiAAAGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTV-YLKGILAK 131
Cdd:TIGR01892 2 ILTKLVAFDSTSFRPN--VDLIDWAQAYLEALGFSVEVQPFPDGAEKSNLVAVIGPSGAGGLALSGHTDVVpYDDAAWTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 132 APFR--VEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRdyGTITVLFNTDEEKGSFGSRDLIQEEAKLADYVLSFEPT 209
Cdd:TIGR01892 80 DPFRltEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLK--KPLHLALTADEEVGCTGAPKMIEAGAGRPRHAIIGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 210 SAGDEKlslGTSGIAYVQVQITGKASHAgAAPELGVNALVEASDLVLRTMNIDDKAKNLRF-----------QWTIAKAG 278
Cdd:TIGR01892 158 RLIPVR---AHKGYASAEVTVRGRSGHS-SYPDSGVNAIFRAGRFLQRLVHLADTLLREDLdegftppyttlNIGVIQGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 279 QVSNIIPASATLNADVRYARNEDFDAAMKTLEERAQ--QKKLPEADVKVIVTRGRPAFNAGEGGkklvdKAVAYYKEAGG 356
Cdd:TIGR01892 234 KAVNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQalVRDEPGFEVQIEVVSTDPGVNTEPDA-----ELVAFLEELSG 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3717826 357 TlgVEERTGGGTDAayaalsgkPVIESLGLPG--FGYHS-DKA----EYVDISAIPRRLYMAARLI 415
Cdd:TIGR01892 309 N--APEVVSYGTEA--------PQFQELGAEAvvCGPGDiRQAhqpdEYVEIEDLVRCRAVLARLV 364
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
54-355 |
3.62e-24 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 104.07 E-value: 3.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 54 LEKLVNIETGTGDAEGIAaagNFLEAELKNLGFTVtRSKSAGLVVgdNIVGKIKGRggknLLLMSHMDTVYLKgilakAP 133
Cdd:PRK08652 8 LKQLVKIPSPSGQEDEIA---LHIMEFLESLGYDV-HIESDGEVI--NIVVNSKAE----LFVEVHYDTVPVR-----AE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 134 FRVEGDKAYGPGIADDKGGNAVILHTLKLLKeYGVRDYGtITVLFNTDEEKGSFGSRDLIQEEAKlaDYVLSFEPTsagD 213
Cdd:PRK08652 73 FFVDGVYVYGTGACDAKGGVAAILLALEELG-KEFEDLN-VGIAFVSDEEEGGRGSALFAERYRP--KMAIVLEPT---D 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 214 EKLSLGTSGIAYVQVQITGKASHaGAAPELGVNALVEASDLVLRTMNIdDKAKNLRFQWTIA----KAGQVSNIIPASAT 289
Cdd:PRK08652 146 LKVAIAHYGNLEAYVEVKGKPSH-GACPESGVNAIEKAFEMLEKLKEL-LKALGKYFDPHIGiqeiIGGSPEYSIPALCR 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3717826 290 LNADVRYARNEDFDAAMKTLEEraqqkKLPEADVKVIVTRGRPAFNAGEGGK--KLVDKAvayYKEAG 355
Cdd:PRK08652 224 LRLDARIPPEVEVEDVLDEIDP-----ILDEYTVKYEYTEIWDGFELDEDEEivQLLEKA---MKEVG 283
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
50-381 |
2.09e-23 |
|
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: 102.54 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 50 VIKTLEKLVNIET--GTGDAEGIAAAGNFLEAELKNLGF-TVTRSKSAGLVVG--DNIVGKIKGRGGKNLLLMSHMDTVy 124
Cdd:cd05650 3 IIELERDLIRIPAvnPESGGEGEKEKADYLEKKLREYGFyTLERYDAPDERGIirPNIVAKIPGGNDKTLWIISHLDTV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 125 LKGILA---KAPFR--VEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGS-FGSRDLIQEEAK 198
Cdd:cd05650 82 PPGDLSlweTDPWEpvVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSeYGIQYLLNKFDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 199 LADYVLSFEPtSAGDEK---LSLGTSGIAYVQVQITGKASHAgAAPELGVNALVEASDLVLRTMNIDDKAKNLR------ 269
Cdd:cd05650 162 FKKDDLIIVP-DFGTEDgefIEIAEKSILWIKVNVKGKQCHA-STPENGINAFVAASNFALELDELLHEKFDEKddlfnp 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 270 ----FQWTIAKAgQVSNI--IPASATLNADVRYARNEDFDAAMKTLEERAQQ-KKLPEADVKVIVTRGRPAFNAGEGGKK 342
Cdd:cd05650 240 pystFEPTKKEA-NVPNVntIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDfENSYGAGITYEIVQKEQAPPATPEDSE 318
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 3717826 343 LVDKAVAYYKEaggTLGVEERT---GGGTDAAYAALSGKPVI 381
Cdd:cd05650 319 IVVRLSKAIKK---VRGREAKLigiGGGTVAAFLRKKGYPAV 357
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
51-418 |
2.10e-22 |
|
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: 99.09 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 51 IKTLEKLVNIETGTGdAEGiaAAGNFLEAELKNLGFTVTRSKSAGlvvgdNIVGKIKGRGGK-NLLLMSHMDTVYLKGIL 129
Cdd:cd03896 1 VDTAIELGEIPAPTF-REG--ARADLVAEWMADLGLGDVERDGRG-----NVVGRLRGTGGGpALLFSAHLDTVFPGDTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 130 AKApfRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGS--FGSRDLIQEEAKLADYVLSFE 207
Cdd:cd03896 73 ATV--RHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEGLGdlRGARYLLSAHGARLDYFVVAE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 208 PTsagDEKLSLGTSGIAYVQVQITGKASHAgAAPELGVNALVEASDLVLRTMNIDDKAK-NLRFQWTIAKAGQVSNIIPA 286
Cdd:cd03896 151 GT---DGVPHTGAVGSKRFRITTVGPGGHS-YGAFGSPSAIVAMAKLVEALYEWAAPYVpKTTFAAIRGGGGTSVNRIAN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 287 SATLNADVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIVTR--GRPAFNAgEGGKKLVDKAVAYYKEAGGTlgveERT 364
Cdd:cd03896 227 LCSMYLDIRSNPDAELADVQREVEAVVSKLAAKHLRVKARVKPvgDRPGGEA-QGTEPLVNAAVAAHREVGGD----PRP 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 3717826 365 G-GGTDAAYAALSGKPVIeSLGLPGFGYHSDKAEYVDISAIPRRLYMAARLIMDL 418
Cdd:cd03896 302 GsSSTDANPANSLGIPAV-TYGLGRGGNAHRGDEYVLKDDMLKGAKAYLMLAAAL 355
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
50-332 |
2.11e-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 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: 98.50 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 50 VIKTLEKLVNIETGTGDAegiAAAGNFLEAELKNLGFTVTRSKSAGlVVGDNIVGKIKGRGGKNLLLMSHMDTVylkgil 129
Cdd:cd05652 1 LLSLHKSLVEIPSISGNE---AAVGDFLAEYLESLGFTVEKQPVEN-KDRFNVYAYPGSSRQPRVLLTSHIDTV------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 130 akAPF-----RVEGDKAYGPGIADDKGG-NAVILHTLKLLKEyGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKLADYV 203
Cdd:cd05652 71 --PPFipysiSDGGDTIYGRGSVDAKGSvAAQIIAVEELLAE-GEVPEGDLGLLFVVGEETGGDGMKAFNDLGLNTWDAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 204 LSFEPTsagDEKLSLGTSGIAYVQVQITGKASHAGaAPELGVNA-------LVEASDLVL--------RTMNIDdkaknl 268
Cdd:cd05652 148 IFGEPT---ELKLASGHKGMLGFKLTAKGKAGHSG-YPWLGISAieilveaLVKLIDADLpssellgpTTLNIG------ 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3717826 269 RFQwtiakAGQVSNIIPASATLNADVRYARneDFDAAMKTLEERAQQKKLPEADVKVIVTRGRP 332
Cdd:cd05652 218 RIS-----GGVAANVVPAAAEASVAIRLAA--GPPEVKDIVKEAVAGILTDTEDIEVTFTSGYG 274
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
49-326 |
1.10e-21 |
|
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: 96.65 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 49 AVIKTLEKLVNIETGTGDAEGIAAagnFLEAELKNLGFTVTRSkSAGLVVGdnivgkIKGRGGKNLLLMSHMDTVYlkGI 128
Cdd:cd05653 2 DAVELLLDLLSIYSPSGEEARAAK---FLEEIMKELGLEAWVD-EAGNAVG------GAGSGPPDVLLLGHIDTVP--GE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 129 LakaPFRVEGDKAYGPGIADDKGG-NAVILHTLKLLKEYGVRdygtITVLFNTDEEKGSFGSRDLIQEEAKlADYVLSFE 207
Cdd:cd05653 70 I---PVRVEGGVLYGRGAVDAKGPlAAMILAASALNEELGAR----VVVAGLVDEEGSSKGARELVRRGPR-PDYIIIGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 208 PTsaGDEKLSLGTSGIAYVQVQITGKASHAgAAPElgVNALVEASDLVLRTMNIDDKAK-----NLRFQWTIAKAGQVSN 282
Cdd:cd05653 142 PS--GWDGITLGYRGSLLVKIRCEGRSGHS-SSPE--RNAAEDLIKKWLEVKKWAEGYNvggrdFDSVVPTLIKGGESSN 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 3717826 283 IIPASATLNADVRYarnedfdAAMKTLEERAQQ--KKLPEADVKVI 326
Cdd:cd05653 217 GLPQRAEATIDLRL-------PPRLSPEEAIALatALLPTCELEFI 255
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
49-372 |
1.68e-21 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 96.84 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 49 AVIKTLEKLVNI-----ETGtGDAEgiAAAGNFLEAELKNLGFTV-----TRSKSAGLVVGDNIVGKIKGRGGK-NLLLM 117
Cdd:PRK13983 6 EMIELLSELIAIpavnpDFG-GEGE--KEKAEYLESLLKEYGFDEverydAPDPRVIEGVRPNIVAKIPGGDGKrTLWII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 118 SHMDTVyLKGILAK---APF--RVEGDKAYGPGIADDkgGNAVI--LHTLKLLKEYGVRDYGTITVLFNTDEEKGS-FGS 189
Cdd:PRK13983 83 SHMDVV-PPGDLSLwetDPFkpVVKDGKIYGRGSEDN--GQGIVssLLALKALMDLGIRPKYNLGLAFVSDEETGSkYGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 190 RDLIQEEAKL---ADYVLSfeP---TSAGD-----EKlslgtsGIAYVQVQITGKASHAgAAPELGVNALVEASDLVLrt 258
Cdd:PRK13983 160 QYLLKKHPELfkkDDLILV--PdagNPDGSfieiaEK------SILWLKFTVKGKQCHA-STPENGINAHRAAADFAL-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 259 mNIDDK------AKNLR-------FQWTIAKAGqVSNI--IPASATLNADVRYARNEDFDAAMKTLEERA---QQKKLPE 320
Cdd:PRK13983 229 -ELDEAlhekfnAKDPLfdppystFEPTKKEAN-VDNIntIPGRDVFYFDCRVLPDYDLDEVLKDIKEIAdefEEEYGVK 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 3717826 321 ADVKVIVTRGRPAFNAGEGgkKLVDKAVAYYKEaggTLGVEERT---GGGTDAAY 372
Cdd:PRK13983 307 IEVEIVQREQAPPPTPPDS--EIVKKLKRAIKE---VRGIEPKVggiGGGTVAAF 356
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
54-406 |
3.58e-20 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 92.54 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 54 LEKLVNIETGTGDAEGIAAAG-----NFLEAELKNLGFTVTRSKSA-GLVvgdNIVGKIKGRGG-KNLLLMSHMDTVYLK 126
Cdd:cd08013 7 TQTLVRINSSNPSLSATGGAGeaeiaTYVAAWLAHRGIEAHRIEGTpGRP---SVVGVVRGTGGgKSLMLNGHIDTVTLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 127 GILAKAPFRVEGDKA-YGPGIADDKGGNAVILHTLKLLKEYGVRdyGTITVLFNTDEEKGSFGSRDLIQEEAKlADYVLS 205
Cdd:cd08013 84 GYDGDPLSGEIADGRvYGRGTLDMKGGLAACMAALADAKEAGLR--GDVILAAVADEEDASLGTQEVLAAGWR-ADAAIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 206 FEPTSagdEKLSLGTSGIAYVQVQITGKASHaGAAPELGVNALVEA-----------SDLVLRTMNIDDKAKNLrfQWTI 274
Cdd:cd08013 161 TEPTN---LQIIHAHKGFVWFEVDIHGRAAH-GSRPDLGVDAILKAgyflvaleeyqQELPERPVDPLLGRASV--HASL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 275 AKAGQVSNIIPASATLNADVRYARNEDFDAAMK----TLEERAQQKKLPEADVKVIVTRgRPAFNAGEggkklvDKAVA- 349
Cdd:cd08013 235 IKGGEEPSSYPARCTLTIERRTIPGETDESVLAeltaILGELAQTVPNFSYREPRITLS-RPPFEVPK------EHPFVq 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3717826 350 -YYKEAGGTLG---VEERTGGGTDAAYAALSGKPVIeSLGLPGFGYHSdKAEYVDISAIPR 406
Cdd:cd08013 308 lVAAHAAKVLGeapQIRSETFWTDAALLAEAGIPSV-VFGPSGAGLHA-KEEWVDVESIRQ 366
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
51-390 |
6.48e-20 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 92.10 E-value: 6.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 51 IKTLEKLVNIETGTGDAEGIAAAgnfLEAELKNLGFTVTRSKSAGlvvgdNIVGKIKGrgGKNLLLM-SHMDTVYLKGIL 129
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVER---IEEEMEKLGFDEVEIDPMG-----NVIGYIGG--GKKKILFdGHIDTVGIGNID 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 130 --AKAPF--RVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDY-GTITVLFNTDEEK-GSFGSRDLIQEEAKLADYV 203
Cdd:cd05649 71 nwKFDPYegYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLRDFaYTILVAGTVQEEDcDGVCWQYISKADKIKPDFV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 204 LSFEPTSAGdekLSLGTSGIAYVQVQITGKASHaGAAPELGVNALVEASDLV--LRTMNIDDKAKNLRFQWTIAkagqVS 281
Cdd:cd05649 151 VSGEPTDGN---IYRGQRGRMEIRVDTKGVSCH-GSAPERGDNAVYKMADIIqdIRQLNPNFPEAPFLGRGTLT----VT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 282 NIIPASATLNA---------DVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIVTRGRPAFnAGEGGK----------- 341
Cdd:cd05649 223 DIFSTSPSRCAvpdscrisiDRRLTVGETWEGCLEEIRALPAVKKYGDDVAVSMYNYDRPSY-TGEVYEseryfptwllp 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 3717826 342 ---KLVDKAVAYYKEAGGTL-GVEERTGGGTDAAYAALSGKPVIeslglpGFG 390
Cdd:cd05649 302 edhELVKALLEAYKALFGARpLIDKWTFSTNGVSIMGRAGIPCI------GFG 348
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
37-334 |
7.56e-20 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 91.93 E-value: 7.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 37 NVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAAgnfLEAELKNLGFTVTRSKSAGlvvgdNIVGKIKGrgGKNLLL 116
Cdd:PRK13004 4 KLILMLAEKYKADMTRFLRDLIRIPSESGDEKRVVKR---IKEEMEKVGFDKVEIDPMG-----NVLGYIGH--GKKLIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 117 M-SHMDTVylkGILAKA-----PF--RVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEE--KGs 186
Cdd:PRK13004 74 FdAHIDTV---GIGDIKnwdfdPFegEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEEdcDG- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 187 FGSRDLIQEEAKLADYVLSFEPTSAGdekLSLGTSGIAYVQVQITGKASHaGAAPELGVNALVEASDLV--LRTMNIDDK 264
Cdd:PRK13004 150 LCWRYIIEEDKIKPDFVVITEPTDLN---IYRGQRGRMEIRVETKGVSCH-GSAPERGDNAIYKMAPILneLEELNPNLK 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3717826 265 AKNLRFQWTIAkagqVSNII--PASATLNAD---VRYAR----NEDFDAAMKTLEERAQQKKLpEADVKVIVTRgRPAF 334
Cdd:PRK13004 226 EDPFLGKGTLT----VSDIFstSPSRCAVPDscaISIDRrltvGETWESVLAEIRALPAVKKA-NAKVSMYNYD-RPSY 298
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
76-372 |
8.32e-20 |
|
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: 91.25 E-value: 8.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 76 FLEAELKNLGFTVTRsksaGLVVGDNIVGKIK-GRGGKNLLLMSHMDTVYLKGiLAKAPFRVEGdkaygPGIADDKGGN- 153
Cdd:TIGR01891 24 LIAEALESLGIEVRR----GVGGATGVVATIGgGKPGPVVALRADMDALPIQE-QTDLPYKSTN-----PGVMHACGHDl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 154 --AVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSfGSRDLIQEEA-KLADYVLSFEP-TSAGDEKLSLG----TSGIAY 225
Cdd:TIGR01891 94 htAILLGTAKLLKKLADLLEGTVRLIFQPAEEGGG-GATKMIEDGVlDDVDAILGLHPdPSIPAGTVGLRpgtiMAAADK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 226 VQVQITGKASHAgAAPELGVNALVEASDLVLRTMNID----DKAKNLRFQWTIAKAGQVSNIIPASATLNADVRYARNED 301
Cdd:TIGR01891 173 FEVTIHGKGAHA-ARPHLGRDALDAAAQLVVALQQIVsrnvDPSRPAVVSVGIIEAGGAPNVIPDKASMSGTVRSLDPEV 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3717826 302 FDAAMKTLEERAQQKKLP-EADVKVIVTRGRPAFNAGEGGKKLVDKAVayyKEAGGTLGVEERTG---GGTDAAY 372
Cdd:TIGR01891 252 RDQIIDRIERIVEGAAAMyGAKVELNYDRGLPAVTNDPALTQILKEVA---RHVVGPENVAEDPEvtmGSEDFAY 323
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
51-402 |
2.02e-19 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 90.33 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 51 IKTLEKLVNIETgTGDAEGIAAagNFLEAELKNLGFTvtrSKSagLVVGD---NIVGKIkGRGGKNLLLMSHMDTVYLkG 127
Cdd:PRK08588 5 IQILADIVKINS-VNDNEIEVA--NYLQDLFAKHGIE---SKI--VKVNDgraNLVAEI-GSGSPVLALSGHMDVVAA-G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 128 ILAK---APFRV--EGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEE-AKLAD 201
Cdd:PRK08588 75 DVDKwtyDPFELteKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGELGAKQLTEKGyADDLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 202 YVLSFEPTsagdeklslgTSGIAY-------VQVQITGKASHAgAAPELGVNALV-------EASDLVLRTMNIDDKAKN 267
Cdd:PRK08588 155 ALIIGEPS----------GHGIVYahkgsmdYKVTSTGKAAHS-SMPELGVNAIDpllefynEQKEYFDSIKKHNPYLGG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 268 LRFQWTIAKAG-QVsNIIPASATLNADVRY---ARNEDFDAAMKTLEERAQQKKLPEADVKVIVTRgRPAFNAGEGgkKL 343
Cdd:PRK08588 224 LTHVVTIINGGeQV-NSVPDEAELEFNIRTipeYDNDQVISLLQEIINEVNQNGAAQLSLDIYSNH-RPVASDKDS--KL 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3717826 344 VDKAVAYYKEAGGTLGVEERTGGGTDAAYAALSGK--PVIeSLGlPGFgyhSDKA----EYVDIS 402
Cdd:PRK08588 300 VQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKPdfPVI-IFG-PGN---NLTAhqvdEYVEKD 359
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
50-311 |
5.91e-19 |
|
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: 88.65 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 50 VIKTLEKLVNIETGTGDAEGIAAAgnfLEAELKNLG-FTVTRSksaglvvGDNIVGKIKGRGGKNLLLMSHMDTVYLKGI 128
Cdd:cd05647 1 PIELTAALVDIPSVSGNEKPIADE---IEAALRTLPhLEVIRD-------GNTVVARTERGLASRVILAGHLDTVPVAGN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 129 LakaPFRVEGD-KAYGPGIADDKGGNAVILHTLKLLKEYGVRDygTITVLFNTDEEKGSF--GSRDLIQEEAKL--ADYV 203
Cdd:cd05647 71 L---PSRVEEDgVLYGCGATDMKAGDAVQLKLAATLAAATLKH--DLTLIFYDCEEVAAElnGLGRLAEEHPEWlaADFA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 204 LSFEPTSAGDEKlslGTSGIAYVQVQITGKASHAgAAPELGVNALVEASDLVLR-------TMNIDDKAKNLRFQWTIAK 276
Cdd:cd05647 146 VLGEPTDGTIEG---GCQGTLRFKVTTHGVRAHS-ARSWLGENAIHKLAPILARlaayeprTVNIDGLTYREGLNAVFIS 221
|
250 260 270
....*....|....*....|....*....|....*
gi 3717826 277 AGQVSNIIPASATLNADVRYARNEDFDAAMKTLEE 311
Cdd:cd05647 222 GGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVRE 256
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
52-326 |
1.17e-18 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 87.53 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 52 KTLEKLVNIETGTGDAEgiaAAGNFLE---AELkNLGFTVTRSKSAGLVvgdnivgkikgrGGKNLLLMSHMDTVYlkGI 128
Cdd:PRK00466 14 ELLLDLLSIYTPSGNET---NATKFFEkisNEL-NLKLEILPDSNSFIL------------GEGDILLASHVDTVP--GY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 129 LakaPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRdygtITVLFNTDEEKGSFGSRDLIQEeAKLADYVLSFEP 208
Cdd:PRK00466 76 I---EPKIEGEVIYGRGAVDAKGPLISMIIAAWLLNEKGIK----VMVSGLADEESTSIGAKELVSK-GFNFKHIIVGEP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 209 TSAGDekLSLGTSGIAYVQVQITGKASHAGAAPElgvNALVEASDLVLRTMNIDDKAKNLRFQWTIAKAGQVSNIIPASA 288
Cdd:PRK00466 148 SNGTD--IVVEYRGSIQLDIMCEGTPEHSSSAKS---NLIVDISKKIIEVYKQPENYDKPSIVPTIIRAGESYNVTPAKL 222
|
250 260 270
....*....|....*....|....*....|....*...
gi 3717826 289 TLNADVRYARNEDFDAAMKTLEEraqqkKLPEADVKVI 326
Cdd:PRK00466 223 YLHFDVRYAINNKRDDLISEIKD-----KFQECGLKIV 255
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
218-319 |
1.63e-16 |
|
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: 75.46 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 218 LGTSGIAYVQVQITGKASHAGAaPELGVNALVEASDLVLR----TMNIDDKAKNLRFQWTIAKAGQVSNIIPASATLNAD 293
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGA-PGKGVNAIKLLARLLAElpaeYGDIGFDFPRTTLNITGIEGGTATNVIPAEAEAKFD 79
|
90 100
....*....|....*....|....*.
gi 3717826 294 VRYARNEDFDAAMKTLEERAQQKKLP 319
Cdd:pfam07687 80 IRLLPGEDLEELLEEIEAILEKELPE 105
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
54-402 |
4.23e-15 |
|
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: 77.16 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 54 LEKLVNIETGTGDAEGiaaAGNFLEAELKNLGFTVTRSKSAGLvvgDNIVGKiKGRGGKNLLLMSHMDTVYlKGILAK-- 131
Cdd:cd03891 4 AKELIRRPSVTPDDAG---AQDLIAERLKALGFTCERLEFGGV---KNLWAR-RGTGGPHLCFAGHTDVVP-PGDLEGws 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 132 -APF--RVEGDKAYGPGIADDKGGNAVILH-TLKLLKEYGVRDyGTITVLFNTDEE-KGSFGSRDLIQEEAK---LADYV 203
Cdd:cd03891 76 sDPFspTIKDGMLYGRGAADMKGGIAAFVAaAERFVAKHPNHK-GSISFLITSDEEgPAIDGTKKVLEWLKArgeKIDYC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 204 LSFEPTSA---GDeKLSLGTSGIAYVQVQITGKASHAgAAPELGVNALVEASDLV--LRTMNIDDKakNLRFQWT----- 273
Cdd:cd03891 155 IVGEPTSEkklGD-TIKIGRRGSLNGKLTIKGKQGHV-AYPHLADNPIHLLAPILaeLTATVLDEG--NEFFPPSslqit 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 274 -IAKAGQVSNIIPASATLNADVRYARNEDFDAAMKTLEERAQQKKLpeaDVKVIVTRGRPAFNAGEGgkKLVDKAVAYYK 352
Cdd:cd03891 231 nIDVGNGATNVIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGL---DYDLEWKLSGEPFLTKPG--KLVDAVSAAIK 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 3717826 353 EaggTLGVEER--TGGGT-DAAYAALSGKPVIEsLGLPGFGYHSDKaEYVDIS 402
Cdd:cd03891 306 E---VTGITPElsTSGGTsDARFIASYGCPVVE-FGLVNATIHKVN-ERVSVA 353
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
52-393 |
1.02e-14 |
|
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: 76.60 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 52 KTLEKLVNIETGTGDA---EGIAAAGNFLEAELKNLGFTVT--RSKSAGLVVgdniVGKIKGRGG-KNLLLMSHMDTV-- 123
Cdd:cd03893 2 QTLAELVAIPSVSAQPdrrEELRRAAEWLADLLRRLGFTVEivDTSNGAPVV----FAEFPGAPGaPTVLLYGHYDVQpa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 124 YLKGILAKAPFR--VEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKL-- 199
Cdd:cd03893 78 GDEDGWDSDPFEltERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEESGSPSLDQLVEAHRDLla 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 200 ADYVLSFEPTSAGDEKLSLGTS--GIAYVQVQITG--KASHAG----AAPELGVNA--------------LV-----EAS 252
Cdd:cd03893 158 ADAIVISDSTWVGQEQPTLTYGlrGNANFDVEVKGldHDLHSGlyggVVPDPMTALaqllaslrdetgriLVpglydAVR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 253 DLVLRTMNID------------DKAKNLRFQWT--------IAKAGQVS---NIIPASATLNADVRYARNEDFDAAMKTL 309
Cdd:cd03893 238 ELPEEEFRLDagvleeveiiggTTGSVAERLWTrpaltvlgIDGGFPGEgskTVIPPRARAKISIRLVPGQDPEEASRLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 310 EerAQQKKLPEADVKVIVTRgrpafnaGEGGKKLV-----DKAVAYYKEAGGTLGVEE--RTGGGT---DAAYAALSGKP 379
Cdd:cd03893 318 E--AHLEKHAPSGAKVTVSY-------VEGGMPWRsdpsdPAYQAAKDALRTAYGVEPplTREGGSipfISVLQEFPQAP 388
|
410
....*....|....*
gi 3717826 380 -VIESLGLPGFGYHS 393
Cdd:cd03893 389 vLLIGVGDPDDNAHS 403
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
50-349 |
5.30e-14 |
|
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: 73.50 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 50 VIKTLEKLVNIETGTGDAEGIAaagNFLEAELKNLGFTVTRsksaglvVGDNIVGKIK--GRGGKNLLLMSHMDTVYLKG 127
Cdd:cd05651 2 AIELLKSLIATPSFSREEHKTA---DLIENYLEQKGIPFKR-------KGNNVWAENGhfDEGKPTLLLNSHHDTVKPNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 128 ILAKAPF--RVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKLaDYVLS 205
Cdd:cd05651 72 GWTKDPFepVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGPLNYNLIYAASAEEEISGKNGIESLLPHLPPL-DLAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 206 FEPTSAgdeKLSLGTSGIAYVQVQITGKASHAgAAPElGVNALVEASDLVLRTMNID-DKAKNL----RFQWTIAKAGQV 280
Cdd:cd05651 151 GEPTEM---QPAIAEKGLLVLDCTARGKAGHA-ARNE-GDNAIYKALDDIQWLRDFRfDKVSPLlgpvKMTVTQINAGTQ 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 281 SNIIPASATLNADVRyaRNEDFdaamkTLEERAQQ-KKLPEADVKVIVTRGRPAFNAGEggKKLVDKAVA 349
Cdd:cd05651 226 HNVVPDSCTFVVDIR--TTEAY-----TNEEIFEIiRGNLKSEIKPRSFRLNSSAIPPD--HPIVQAAIA 286
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
49-373 |
9.09e-14 |
|
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: 73.82 E-value: 9.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 49 AVIKTLEKLVNIETGTGDA-------EGIAAAgnfLEAEL---KNLGFTVtrsksaglVVGDNIVGKIK-GRGGKNLLLM 117
Cdd:cd03888 9 EILEDLKELVAIPSVRDEAtegapfgEGPRKA---LDKFLdlaKRLGFKT--------KNIDNYAGYAEyGEGEEVLGIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 118 SHMDTV-------YlkgilakAPFRVE--GDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGS-- 186
Cdd:cd03888 78 GHLDVVpagegwtT-------DPFKPVikDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGWkc 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 187 ------------FG-----------------SRDLIQEEAKLADYVL-SFE----------------PTSAGDEKLSLGT 220
Cdd:cd03888 151 iehyfeheeypdFGftpdaefpvingekgivTVDLTFKIDDDKGYRLiSIKggeatnmvpdkaeaviPGKDKEELALSAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 221 SGIAY--------VQVQITGKASHAgAAPELGVNAlveASDLV--LRTMNIDDKAKNLrFQWTIAKAGQVSN---IIPAS 287
Cdd:cd03888 231 TDLKGnieiddggVELTVTGKSAHA-SAPEKGVNA---ITLLAkfLAELNKDGNDKDF-IKFLAKNLHEDYNgkkLGINF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 288 A-------TLNA--------------DVRYARNEDFDAAMKTLEERAQQKklpeadvKVIVTRGR---PAFNAGEGgkKL 343
Cdd:cd03888 306 EdevmgelTLNPgiitlddgklelglNVRYPVGTSAEDIIKQIEEALEKY-------GVEVEGHKhqkPLYVPKDS--PL 376
|
410 420 430
....*....|....*....|....*....|
gi 3717826 344 VDKAVAYYKEAGGTLGVEERTGGGTdaaYA 373
Cdd:cd03888 377 VKTLLKVYEEQTGKEGEPVAIGGGT---YA 403
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
76-369 |
1.34e-13 |
|
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: 72.70 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 76 FLEAELKNLGFTVTRsksagLVVGDNIVGKI-KGRGGKNLLLMSHMDTVylkgilakaPFRVEGDKAYGPGIADDkGGNA 154
Cdd:cd08018 29 YLAKKLEEMGFRVTT-----FEGGTGVVAEIgSGKPGPVVALRADMDAL---------WQEVDGEFKANHSCGHD-AHMT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 155 VILHTLKLLKEYGVRDYGTITVLFNTDEEKGsFGSRDLIqEEAKL--ADYVLSF--EPtsagDEKLSLGTSGIA------ 224
Cdd:cd08018 94 MVLGAAELLKKIGLVKKGKLKFLFQPAEEKG-TGALKMI-EDGVLddVDYLFGVhlRP----IQELPFGTAAPAiyhgas 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 225 -YVQVQITGKASHaGAAPELGVNALVEASDLV--LRTMNIDDK----AKNLRFQwtiaKAGQVSNIIPASATLNADVRYA 297
Cdd:cd08018 168 tFLEGTIKGKQAH-GARPHLGINAIEAASAIVnaVNAIHLDPNipwsVKMTKLQ----AGGEATNIIPDKAKFALDLRAQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 298 RNEdfdaAMKTLEERAQQ-----KKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVayykeaGGTLGvEER------TGG 366
Cdd:cd08018 243 SNE----AMEELKEKVEHaieaaAALYGASIEITEKGGMPAAEYDEEAVELMEEAI------TEVLG-EEKlagpcvTPG 311
|
...
gi 3717826 367 GTD 369
Cdd:cd08018 312 GED 314
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
54-391 |
1.87e-13 |
|
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: 72.78 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 54 LEKLVNIETG-TGDAEG-IAAAGNFLEAELKNLGFtVTRSKSAGLVVGD-NIVGKIKGRGG--KNLLLMSHMDTVYlkgi 128
Cdd:cd05675 4 LQELIRIDTTnSGDGTGsETRAAEVLAARLAEAGI-QTEIFVVESHPGRaNLVARIGGTDPsaGPLLLLGHIDVVP---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 129 lAKA------PFR--VEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGS-FGSRDLIQEEAKL 199
Cdd:cd05675 79 -ADAsdwsvdPFSgeIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGeNGAKWLVDNHPEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 200 ---ADYVLS----FEPTSAGDEKL---SLGTSGIAYVQVQITGKASH-------------AGA----------------- 239
Cdd:cd05675 158 fdgATFALNegggGSLPVGKGRRLypiQVAEKGIAWMKLTVRGRAGHgsrptddnaitrlAEAlrrlgahnfpvrltdet 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 240 ---------APELGVNALVEASDLVLRTMN-IDDKAKNLR------FQWTIAKAGQVSNIIPASATLNADVRY---ARNE 300
Cdd:cd05675 238 ayfaqmaelAGGEGGALMLTAVPVLDPALAkLGPSAPLLNamlrntASPTMLDAGYATNVLPGRATAEVDCRIlpgQSEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 301 DFDAAMKTLEERaqqkklPEADVKVIvtrGRPAFNAGEGGKKLVD---KAVAyyKEAGGTLGVEERTGGGTDAAYAAlsg 377
Cdd:cd05675 318 EVLDTLDKLLGD------PDVSVEAV---HLEPATESPLDSPLVDameAAVQ--AVDPGAPVVPYMSPGGTDAKYFR--- 383
|
410
....*....|....
gi 3717826 378 kpvieSLGLPGFGY 391
Cdd:cd05675 384 -----RLGIPGYGF 392
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
154-372 |
1.98e-13 |
|
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: 72.25 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 154 AVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSfGSRDLIqEEAKLA----DYVLSF--EPTsagdekLSLGT------- 220
Cdd:cd03886 95 AMLLGAAKLLAERRDPLKGTVRFIFQPAEEGPG-GAKAMI-EEGVLEnpgvDAAFGLhvWPG------LPVGTvgvrsga 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 221 --SGIAYVQVQITGKASHaGAAPELGVNALVEASDLVLRTMNI----DDKAKNLRFQWTIAKAGQVSNIIPASATLNADV 294
Cdd:cd03886 167 lmASADEFEITVKGKGGH-GASPHLGVDPIVAAAQIVLALQTVvsreLDPLEPAVVTVGKFHAGTAFNVIPDTAVLEGTI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 295 RYARNEDFDAAMKTLEERAQQK-KLPEADVKVIVTRGRPA-FNAGEggkkLVDKAVAYYKEAGGTLGVE--ERTGGGTDA 370
Cdd:cd03886 246 RTFDPEVREALEARIKRLAEGIaAAYGATVELEYGYGYPAvINDPE----LTELVREAAKELLGEEAVVepEPVMGSEDF 321
|
..
gi 3717826 371 AY 372
Cdd:cd03886 322 AY 323
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
101-211 |
1.87e-12 |
|
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 66.29 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 101 NIVGKIKGR-GGKNLLLMSHMDTVYLK----GILAKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTIT 175
Cdd:cd03873 1 NLIARLGGGeGGKSVALGAHLDVVPAGegdnRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 3717826 176 VLFNTDEEKGSFGSRDLI----QEEAKLADYVLSFEPTSA 211
Cdd:cd03873 81 VAFTADEEVGSGGGKGLLskflLAEDLKVDAAFVIDATAG 120
|
|
| M20_Acy1L2 |
cd03887 |
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
161-313 |
2.03e-12 |
|
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: 68.76 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 161 KLLKEYGVRdyGTITVLFNTDEEKGSfGSRDLIQEEA-KLADYVLSFEPTSAGdeklSLGTSGIAYVQVQI--TGKASHA 237
Cdd:cd03887 100 AALKALGLP--GTVVVLGTPAEEGGG-GKIDLIKAGAfDDVDIALMVHPGPKD----VAGPKSLAVSKLRVefHGKAAHA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 238 GAAPELGVNALveaSDLVLRTMNIDdkakNLRFQ----W----TIAKAGQVSNIIPASATLNADVRyARNedfDAAMKTL 309
Cdd:cd03887 173 AAAPWEGINAL---DAAVLAYNNIS----ALRQQlkptVrvhgIITEGGKAPNIIPDYAEAEFYVR-APT---LKELEEL 241
|
....
gi 3717826 310 EERA 313
Cdd:cd03887 242 TERV 245
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
36-248 |
3.69e-12 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 68.63 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 36 DNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGlVVGD-------NIVGKIKG 108
Cdd:PRK13013 2 DDRLFAAIEARRDDLVALTQDLIRIPTLNPPGRAYREICEFLAARLAPRGFEVELIRAEG-APGDsetyprwNLVARRQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 109 RG-GKNLLLMSHMDTVYLKGILAKAPF--RVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKG 185
Cdd:PRK13013 81 ARdGDCVHFNSHHDVVEVGHGWTRDPFggEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3717826 186 SFGSRDLIQEEAKLA----DYVLSFEPTSAgdEKLSLGTSGIAYVQVQITGKASHaGAAPELGVNAL 248
Cdd:PRK13013 161 GFGGVAYLAEQGRFSpdrvQHVIIPEPLNK--DRICLGHRGVWWAEVETRGRIAH-GSMPFLGDSAI 224
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
49-373 |
4.98e-12 |
|
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: 68.17 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 49 AVIKTLEKLVNIETGTGDAEGIAAAgNFLEAELKNLGFTVTRSKSAGLVVG--DNIVGKIK-GRGGKNLLLMSHMDTVYL 125
Cdd:TIGR01887 3 EILEDLKELIAIDSVEDLEKAKEGA-PFGEGPRKALDKFLEIAKRDGFTTEnvDNYAGYIEyGQGEEVLGILGHLDVVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 126 KGILAKAPFRVE--GDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGS--------------FG- 188
Cdd:TIGR01887 82 GDGWTSPPFEPTikDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEESGWkcidyyfeheempdIGf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 189 SRD----LIQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAY--------------------------------------- 225
Cdd:TIGR01887 162 TPDaefpIIYGEKGITTLEIKFKDDTEGDVVLESFKAGEAYnmvpdhatavisgkklteveqlkfvffiakelegdfevn 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 226 ---VQVQITGKASHaGAAPELGVNALVEASdLVLRTMNIDDKAKN-LRF------------QWTIAKAGQVSniipASAT 289
Cdd:TIGR01887 242 dgtLTITLEGKSAH-GSAPEKGINAATYLA-LFLAQLNLAGGAKAfLQFlaeylhedhygeKLGIKFHDDVS----GDLT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 290 LNA---------------DVRYARNEDFDAAMKTLEERAQQkklpeadvKVIVTRGR---PAFNAGEggKKLVDKAVAYY 351
Cdd:TIGR01887 316 MNVgvidyenaeagliglNVRYPVGNDPDTMLKNELAKESG--------VVEVTLNGylkPLYVPKD--DPLVQTLMKVY 385
|
410 420
....*....|....*....|..
gi 3717826 352 KEAGGTLGVEERTGGGTDAAYA 373
Cdd:TIGR01887 386 EKQTGDEGEPVAIGGGTYARLM 407
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
44-323 |
7.38e-12 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 67.15 E-value: 7.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 44 TDEQPAVIKTLEKLVNIETGTgDAEGIAAAGNF--LEAELKnlGFTVTRSKSaglvvGDNIVGKIKGRGGKNLLLMSHMD 121
Cdd:PRK08737 2 TDLLESTLDHLQALVSFDTRN-PPRAITTGGIFdyLRAQLP--GFQVEVIDH-----GAGAVSLYAVRGTPKYLFNVHLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 122 TVYLKGILAKAPF--RVEGDKAYGPGIADDKGGNAVILHTLkllkEYGVRDYGtitVLFNTDEEKGSfgSRDLIQEEAKL 199
Cdd:PRK08737 74 TVPDSPHWSADPHvmRRTDDRVIGLGVCDIKGAAAALLAAA----NAGDGDAA---FLFSSDEEAND--PRCVAAFLARG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 200 ADY--VLSFEPTSAgdeKLSLGTSGIAYVQVQITGKASHAGAAPELGVNALVEASDLVLRTMN-IDDKA-------KNLR 269
Cdd:PRK08737 145 IPYeaVLVAEPTMS---EAVLAHRGISSVLMRFAGRAGHASGKQDPSASALHQAMRWGGQALDhVESLAharfgglTGLR 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3717826 270 FQWTIAKAGQVSNIIPASATLNADVRYARNEDFD-----------AAMKTLEERAQQKKLPEADV 323
Cdd:PRK08737 222 FNIGRVEGGIKANMIAPAAELRFGFRPLPSMDVDgllatfagfaePAAATFEETFRGPSLPSGDI 286
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
147-415 |
8.05e-12 |
|
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; tripeptide aminopeptidase; tripeptidase) subfamily and similar proteins. PepT acts only on tripeptide substrates, and is thus termed 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: 349897 [Multi-domain] Cd Length: 400 Bit Score: 67.40 E-value: 8.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 147 ADDKGGNAVILHTLKLLKEYGVrDYGTITVLFNTDEEKGsFGSRDLiQEEAKLADYVLSFEPTSAGDekLSLGTSGIAYV 226
Cdd:cd05645 136 ADDKAGLAEIFTALAVLKEKNI-PHGDIEVAFTPDEEVG-KGAKHF-DVEAFTAKWAYTVDGGGVGE--LEFENFNAASV 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 227 QVQITGKASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFQwTIAKAGQVSNIIPaSATLNADVRYARNEDFDAAM 306
Cdd:cd05645 211 NIKIVGNNVHPGTAKGVGVNALSLAARIHAEVPADESPEGTEGYE-GFYHLASFKGTVD-RAQIHYIIRDFDRKQFEARK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 307 KTLEERAQ---QKKLPEADVKVIVTRGRPAFN-AGEGGKKLVDKAVAYYKEAGGTLGVEErTGGGTDAAYAALSGKPVIe 382
Cdd:cd05645 289 RK*KEIAKkvgKGLHPDCYIELVIEDSYYNFReKVVEHPHILDIAQQAARDCGITPELKP-IRGGTDGAQLSFHGLPCP- 366
|
250 260 270
....*....|....*....|....*....|...
gi 3717826 383 SLGLPGFGYHSdKAEYVDISAIPRRLYMAARLI 415
Cdd:cd05645 367 NLFTGGYNYHG-KHEFVTLEGLEKAVQVIVRIA 398
|
|
| PRK06915 |
PRK06915 |
peptidase; |
101-269 |
8.64e-12 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 67.41 E-value: 8.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 101 NIVGKIKGRG-GKNLLLMSHMDTVyLKGILAK---APFR--VEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGti 174
Cdd:PRK06915 82 NIVATLKGSGgGKSMILNGHIDVV-PEGDVNQwdhHPYSgeVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKG-- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 175 TVLFNT--DEEKGSFGSRDLIQEEAKlADYVLSFEPTsagDEKLSLGTSGIAYVQVQITGKASHAGAAPElGVNALvEAS 252
Cdd:PRK06915 159 DVIFQSviEEESGGAGTLAAILRGYK-ADGAIIPEPT---NMKFFPKQQGSMWFRLHVKGKAAHGGTRYE-GVSAI-EKS 232
|
170
....*....|....*..
gi 3717826 253 DLVLRTMNIDDKAKNLR 269
Cdd:PRK06915 233 MFVIDHLRKLEEKRNDR 249
|
|
| Peptidase_M28 |
pfam04389 |
Peptidase family M28; |
101-237 |
1.01e-11 |
|
Peptidase family M28;
Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 64.23 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 101 NIVGKIKGRGGKN-LLLMSHMDTVYlkgilakapfrvegdkaYGPGIADDKGGNAVILHTLKLLKEYGVRDYGtITVLFN 179
Cdd:pfam04389 1 NVIAKLPGKAPDEvVLLSAHYDSVG-----------------TGPGADDNASGVAALLELARVLAAGQRPKRS-VRFLFF 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 180 TDEEKGSFGSRDLIQEEAKLAD--YVLSFEptsagdeklSLGTSGIAYVqVQITGKASHA 237
Cdd:pfam04389 63 DAEEAGLLGSHHFAKSHPPLKKirAVINLD---------MIGSGGPALL-FQSGPKGSSL 112
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
51-204 |
1.89e-11 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 66.22 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 51 IKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKsagLVVGD-NIVGKIKGRGG---KNLLLMSHMDTVYLK 126
Cdd:PRK08596 16 LELLKTLVRFETPAPPARNTNEAQEFIAEFLRKLGFSVDKWD---VYPNDpNVVGVKKGTESdayKSLIINGHMDVAEVS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 127 GILA--KAPF--RVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKlADY 202
Cdd:PRK08596 93 ADEAweTNPFepTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEVGEAGTLQCCERGYD-ADF 171
|
..
gi 3717826 203 VL 204
Cdd:PRK08596 172 AV 173
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
72-374 |
2.74e-11 |
|
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.
Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 65.62 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 72 AAGNFLEAELKNLGFTVTRSKsaglvVGdNIVGKIKGR--GGKNLLLMSHMDTVYLKGILakapfrvegDKAYGpgiadd 149
Cdd:cd03884 30 AARDLFVEWMEEAGLSVRVDA-----VG-NLFGRLEGTdpDAPPVLTGSHLDTVPNGGRY---------DGILG------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 150 kggnaVI--LHTLKLLKEYGVRDYGTITVLFNTDEEkGS------FGSR----DLIQEEAK------------------- 198
Cdd:cd03884 89 -----VLagLEALRALKEAGIRPRRPIEVVAFTNEE-GSrfppsmLGSRafagTLDLEELLslrdadgvslaealkaigy 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 199 -LADYVLSFEPTSAG--------------DEKLSLG--TS--GIAYVQVQITGKASHAGAAP-ELGVNALVEASDLVLRt 258
Cdd:cd03884 163 dGDRPASARRPGDIKayvelhieqgpvleEEGLPIGvvTGiaGQRWLEVTVTGEAGHAGTTPmALRRDALLAAAELILA- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 259 mnIDDKAKNLRFQwTIAKAGQVS------NIIPASATLNADVRYARNEDFDAAMKTLEER----AQQKKLpEADVKVIVT 328
Cdd:cd03884 242 --VEEIALEHGDD-LVATVGRIEvkpnavNVIPGEVEFTLDLRHPDDAVLDAMVERIRAEaeaiAAERGV-EVEVERLWD 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 3717826 329 rgRPAFNAGEGGKKLVDKAVAyykeaggTLGVEERT---GGGTDAAYAA 374
Cdd:cd03884 318 --SPPVPFDPELVAALEAAAE-------ALGLSYRRmpsGAGHDAMFMA 357
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
52-404 |
3.29e-11 |
|
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: 65.41 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 52 KTLEKLVNIETGTGDAegiAAAGNFLEAELKNLGFTVTRSK----------SAGLVVGD-----NIVGKIKGR--GGKNL 114
Cdd:cd03895 1 AFLQDLVRFPSLRGEE---AAAQDLVAAALRSRGYTVDRWEidveklkhhpGFSPVAVDyagapNVVGTHRPRgeTGRSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 115 LLMSHMDTVyLKGILA---KAPF--RVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGS 189
Cdd:cd03895 78 ILNGHIDVV-PEGPVElwtRPPFeaTIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 190 RDLIQEEAKlADYVLSFEPTsagDEKLSLGTSGIAYVQVQITGKASHAGAAPElGVNALVEASDLV--LRTMNI------ 261
Cdd:cd03895 157 LAALMRGYR-ADAALIPEPT---ELKLVRAQVGVIWFRVKVRGTPAHVAEASE-GVNAIEKAMHLIqaLQELERewnark 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 262 ------DDKAKNLRFQWTIAKAGQVSNIIPASATLNADVRYARNEDFDAAMKTLEE-----RAQQKKLPEADVKVIVTRG 330
Cdd:cd03895 232 kshphfSDHPHPINFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEEcvadaAATDPWLSNHPPEVEWNGF 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3717826 331 RPAFNAGEGGKKLVDKAVAYYKEAGGTLGVEERTGGGTDAAYAALSGK-PVI----ESLGLPGFGyhsdkaEYVDISAI 404
Cdd:cd03895 312 QAEGYVLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGDiPALcygpGSRDAHGFD------ESVDLESL 384
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
50-204 |
3.31e-11 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 65.57 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 50 VIKTLEKLVNIETGTGDAEGIAAAGN---FLEAELKNLGFTVTRSKSAGLVVgdnIVGKIkGRGGKNLLLMSHMDTVYL- 125
Cdd:PRK08554 3 VLELLSSLVSFETVNDPSKGIKPSKEcpkFIKDTLESWGIESELIEKDGYYA---VYGEI-GEGKPKLLFMAHFDVVPVn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 126 KGILAKAPFR--VEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRdyGTITVLFNTDEEKGSFGSRDL---IQEEAKLA 200
Cdd:PRK08554 79 PEEWNTEPFKltVKGDKAYGRGSADDKGNVASVMLALKELSKEPLN--GKVIFAFTGDEEIGGAMAMHIaekLREEGKLP 156
|
....
gi 3717826 201 DYVL 204
Cdd:PRK08554 157 KYMI 160
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
41-204 |
7.59e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 64.64 E-value: 7.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 41 QAATDEQPAVIKTLEKLVNIET--GTGDAEGIAAAgnfLEAELKNLGF-------TVTRSKSAGLVVGdnivgkIKGRG- 110
Cdd:PRK09133 30 AAPTADQQAARDLYKELIEINTtaSTGSTTPAAEA---MAARLKAAGFadadievTGPYPRKGNLVAR------LRGTDp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 111 GKNLLLMSHMDTVYlkgilAKA------PFR--VEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDE 182
Cdd:PRK09133 101 KKPILLLAHMDVVE-----AKRedwtrdPFKlvEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDE 175
|
170 180
....*....|....*....|....*
gi 3717826 183 EKGSF-GSRDLIQEEAKL--ADYVL 204
Cdd:PRK09133 176 EGTPMnGVAWLAENHRDLidAEFAL 200
|
|
| M20_ACY1L2-like |
cd05672 |
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 ... |
161-313 |
8.76e-11 |
|
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. This subfamily includes Staphylococcus aureus antibiotic resistance factor HmrA that has been shown to participate in methicillin resistance mechanisms in vivo in the presence of beta-lactams. Aminoacylase 1 (ACY1) proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349921 [Multi-domain] Cd Length: 360 Bit Score: 63.74 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 161 KLLKEYGVRdyGTITVLFNTDEEKGSfGSRDLIQEEA-KLADYVLSFEPTSAGdeklSLGTSGIAYVQVQI--TGKASHA 237
Cdd:cd05672 100 EALKALGLP--GKVVVLGTPAEEGGG-GKIDLIKAGAfDDVDAALMVHPGPRD----VAGVPSLAVDKLTVefHGKSAHA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 238 GAAPELGVNALvEAsdLVLRTMNIDdkakNLRFQ----W----TIAKAGQVSNIIPASATLNADVRYARNEDFDAamktL 309
Cdd:cd05672 173 AAAPWEGINAL-DA--AVLAYNAIS----ALRQQlkptWrihgIITEGGKAPNIIPDYAEARFYVRAPTRKELEE----L 241
|
....
gi 3717826 310 EERA 313
Cdd:cd05672 242 RERV 245
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
51-255 |
1.06e-10 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 63.44 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 51 IKTLEKLVNIETGTGDAEGIAAagnFLEAELKNLGFTVtRSKSAGLVVGdnivgkIKGRGGKNLLLMSHMDTVylKGILa 130
Cdd:PRK04443 9 RELLKGLVEIPSPSGEEAAAAE---FLVEFMESHGREA-WVDEAGNARG------PAGDGPPLVLLLGHIDTV--PGDI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 131 kaPFRVEGDKAYGPGIADDKGG-NAVILHTLKLLKEYGVRdygtITVLFNTDEEKGSFGSRDLIQEEAKlADYVLSFEPT 209
Cdd:PRK04443 76 --PVRVEDGVLWGRGSVDAKGPlAAFAAAAARLEALVRAR----VSFVGAVEEEAPSSGGARLVADRER-PDAVIIGEPS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 3717826 210 saGDEKLSLGTSGIAYVQVQITGKASHaGAAPElgVNAlveASDLV 255
Cdd:PRK04443 149 --GWDGITLGYKGRLLVTYVATSESFH-SAGPE--PNA---AEDAI 186
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
71-388 |
2.14e-10 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 62.80 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 71 AAAGNFLEAELKNLGFTVTRsksagLVVGD--NIVGKiKGRGGKNLLLMSHMDTVyLKGILAK---APF--RVEGDKAYG 143
Cdd:PRK13009 22 AGCQDLLAERLEALGFTCER-----MDFGDvkNLWAR-RGTEGPHLCFAGHTDVV-PPGDLEAwtsPPFepTIRDGMLYG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 144 PGIADDKGGNAVILH-TLKLLKEYGVRDyGTITVLFNTDEE-KGSFGSR---DLIQEEAKLADYVLSFEPTSAgdEKL-- 216
Cdd:PRK13009 95 RGAADMKGSLAAFVVaAERFVAAHPDHK-GSIAFLITSDEEgPAINGTVkvlEWLKARGEKIDYCIVGEPTST--ERLgd 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 217 --------SLgtSGIAYVQvqitGKASHAgAAPELGVNALVEASDLVLRTMNID-DKAkNLRFQ---WTIA--KAG-QVS 281
Cdd:PRK13009 172 vikngrrgSL--TGKLTVK----GVQGHV-AYPHLADNPIHLAAPALAELAATEwDEG-NEFFPptsLQITniDAGtGAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 282 NIIPASATLNADVRYARNEDFDAAMKTLEERAQQKKLpeaDVKVIVTRGRPAFNAGEGgkKLVDKAVAYYKEaggTLGV- 360
Cdd:PRK13009 244 NVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGL---DYTLEWTLSGEPFLTPPG--KLVDAVVAAIEA---VTGIt 315
|
330 340 350
....*....|....*....|....*....|
gi 3717826 361 -EERTGGGT-DAAYAALSGKPVIEsLGLPG 388
Cdd:PRK13009 316 pELSTSGGTsDARFIADYGAQVVE-FGPVN 344
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
81-248 |
4.75e-10 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 61.76 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 81 LKNLGFTV-------TRSKSaglvvgdNIVGKI-KGRGGknLLLMSHMDTV-YLKGILAKAPFRV--EGDKAYGPGIADD 149
Cdd:PRK05111 42 FEDLGFNVeiqpvpgTRGKF-------NLLASLgSGEGG--LLLAGHTDTVpFDEGRWTRDPFTLteHDGKLYGLGTADM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 150 KGGNAVILHTLKLLkeygvrDYGTIT----VLFNTDEEKGSFGSRDLIQEEAKLADYVLSFEPTSAgdeKLSLGTSGIAY 225
Cdd:PRK05111 113 KGFFAFILEALRDI------DLTKLKkplyILATADEETSMAGARAFAEATAIRPDCAIIGEPTSL---KPVRAHKGHMS 183
|
170 180
....*....|....*....|...
gi 3717826 226 VQVQITGKASHAgAAPELGVNAL 248
Cdd:PRK05111 184 EAIRITGQSGHS-SDPALGVNAI 205
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
51-344 |
7.19e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 61.31 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 51 IKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVVgdnIVGKIKGRGGKNLLLMSHMDTVYLKGI-- 128
Cdd:PRK06446 5 LYTLIEFLKKPSISATGEGIEETANYLKDTMEKLGIKANIERTKGHPV---VYGEINVGAKKTLLIYNHYDVQPVDPLse 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 129 LAKAPF--RVEGDKAYGPGIADDKGgnaVILHTLKLLKEYGVRDYG--TITVLFNTDEEKGSFGSRDLIQEEAKL--ADY 202
Cdd:PRK06446 82 WKRDPFsaTIENGRIYARGASDNKG---TLMARLFAIKHLIDKHKLnvNVKFLYEGEEEIGSPNLEDFIEKNKNKlkADS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 203 VLSFEPT--SAGDEKLSLGTSGIAYVQ--VQITGKASHAGAAPeLGVNALVEASDLV--LRTMNID-------DKAKNLr 269
Cdd:PRK06446 159 VIMEGAGldPKGRPQIVLGVKGLLYVElvLRTGTKDLHSSNAP-IVRNPAWDLVKLLstLVDGEGRvlipgfyDDVREL- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 270 fqwtiakAGQVSNIIpasATLNADVRYARnedfdaamKTLEERAQQKKLPEADVKVIVTrgRPAFN--------AGEGGK 341
Cdd:PRK06446 237 -------TEEERELL---KKYDIDVEELR--------KALGFKELKYSDREKIAEALLT--EPTCNidgfysgyTGKGSK 296
|
...
gi 3717826 342 KLV 344
Cdd:PRK06446 297 TIV 299
|
|
| M20_Acy1L2-like |
cd09849 |
M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
201-307 |
8.81e-10 |
|
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: 60.95 E-value: 8.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 201 DYVLSFEPTSAGDEKLSLG--TSGIAYVQVQITGKASHAGAAPELGVNALvEASDLVLRTMNID----DKAKNLRFQWTI 274
Cdd:cd09849 165 DISLMFHALDLGEDKALINpeSNGFIGKKVKFTGKESHAGSAPFSGINAL-NAATLAINNVNAQretfKESDKVRFHPII 243
|
90 100 110
....*....|....*....|....*....|....*
gi 3717826 275 AKAGQVSNIIPASATLNADVRyARNEDF--DAAMK 307
Cdd:cd09849 244 TKGGDIVNVVPADVRVESYVR-ARSIDYmkEANSK 277
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
51-396 |
1.16e-09 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 60.82 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 51 IKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVVgdnIVGKIKGRGGKNLLLMSHMDTVYLKGiLA 130
Cdd:cd05681 2 LEDLRDLLKIPSVSAQGRGIPETADFLKEFLRRLGAEVEIFETDGNPI---VYAEFNSGDAKTLLFYNHYDVQPAEP-LE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 131 K---APFR--VEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKL--ADYV 203
Cdd:cd05681 78 LwtsDPFEltIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPNLEKFVAEHADLlkADGC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 204 LsFEptSAG-DEK----LSLGTSGIAYVQVQITGKAS--HAGAAP------------------ELG----------VNAL 248
Cdd:cd05681 158 I-WE--GGGkNPKgrpqISLGVKGIVYVELRVKTADFdlHSSYGAivenpawrlvqalnslrdEDGrvlipgfyddVRPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 249 VEASDLVLRTMNIDDKA-------------------KNLRFQWTIAKAGQVS--------NIIPASATLNADVRYARNED 301
Cdd:cd05681 235 SEAERALIDTYDFDPEElrktyglkrplqvegkdplRALFTEPTCNINGIYSgytgegskTILPSEAFAKLDFRLVPDQD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 302 fdaAMKTLEE-RAQQKKLPEADVKVIVTRGRPAFNAgEGGKKLVDKAVAYYKEAGGTLGVEERTGGGTDAAYaalsgkPV 380
Cdd:cd05681 315 ---PAKILSLlRKHLDKNGFDDIEIHDLLGEKPFRT-DPDAPFVQAVIESAKEVYGQDPIVLPNSAGTGPMY------PF 384
|
410 420
....*....|....*....|
gi 3717826 381 IESLGLP----GFGYHSDKA 396
Cdd:cd05681 385 YDALEVPvvaiGVGNAGSNA 404
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
49-326 |
1.29e-09 |
|
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: 60.82 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 49 AVIKTLEKLVNIETGTGdAEGIAAAGNFLEAELKNLG-FTVTRSKSAGLVVGD-----NIVGKIKGRGG--KNLLLMSHM 120
Cdd:cd05654 2 RLEQLLKSLVSWPSVTG-TEGERSFADFLKEILKELPyFKENPSHVWQLLPPDdlgrrNVTALVKGKKPskRTIILISHF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 121 DTV--------------------YLKGILAKAPFRVE-----GDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDyGTIT 175
Cdd:cd05654 81 DTVgiedygelkdiafdpdeltkAFSEYVEELDEEVRedllsGEWLFGRGTMDMKSGLAVHLALLEQASEDEDFD-GNLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 176 VLFNTDEEKGSFGSRDLIQEEAKLA-----DYVLSF--EPTSA---GDEK--LSLGTSGIAYVQVQITGKASHAGaAPEL 243
Cdd:cd05654 160 LMAVPDEEVNSRGMRAAVPALLELKkkhdlEYKLAInsEPIFPqydGDQTryIYTGSIGKILPGFLCYGKETHVG-EPFA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 244 GVNALVEASDLVLR-TMNID--DK-------------AKNLR--------------FQWTIAK--AGQVSNIipasatLN 291
Cdd:cd05654 239 GINANLMASEITARlELNADlcEKvegeitpppvclkQKDLKesysvqtpvravayFNLFLHKktAKELMEL------LR 312
|
330 340 350
....*....|....*....|....*....|....*.
gi 3717826 292 ADVRYARNEDFDAAMKTLEERAQ-QKKLPEADVKVI 326
Cdd:cd05654 313 KIAEKAAEETIKAIYEEYKKYCKrPEVKLPAKVRVL 348
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
42-251 |
1.12e-08 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 57.70 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 42 AATDEQ-PAVIKTLEKLVNIETGTGdAEgiAAAGNFLEAELKNLGFTVTRSK----------SAGLVVGD-----NIVGK 105
Cdd:PRK06837 13 AAVDAGfDAQVAFTQDLVRFPSTRG-AE--APCQDFLARAFRERGYEVDRWSidpddlkshpGAGPVEIDysgapNVVGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 106 IKGRG--GKNLLLMSHMDTVYLK--GILAKAPFR--VEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFN 179
Cdd:PRK06837 90 YRPAGktGRSLILQGHIDVVPEGplDLWSRPPFDpvIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSV 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3717826 180 TDEEKGSFGSRDLIQEEAKlADYVLSFEPTsagDEKLSLGTSGIAYVQVQITGKASHAGAApELGVNALVEA 251
Cdd:PRK06837 170 IEEESTGNGALSTLQRGYR-ADACLIPEPT---GEKLVRAQVGVIWFRLRVRGAPVHVREA-GTGANAIDAA 236
|
|
| M28_Fxna_like |
cd03875 |
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ... |
99-212 |
1.65e-08 |
|
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic reticulum metallopeptidase 1 (ERMP1; Felix-ina, FXNA or Fxna peptidase; KIAA1815) subfamily. ERMP1 is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organization of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolyzed has not yet been determined. Another member of this subfamily is the 24-kDa vacuolar protein (VP24) which is probably involved in the formation of intravacuolar pigmented globules (cyanoplasts) in highly anthocyanin-containing vacuoles; however, the biological function of the C-terminal region which includes the putative transmembrane metallopeptidase domain is unknown.
Pssm-ID: 349872 [Multi-domain] Cd Length: 307 Bit Score: 56.44 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 99 GDNIVGKIKGRGGKN---LLLMSHMDTVylkgilakapfrvegdkAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTIT 175
Cdd:cd03875 79 VTNIVVRISGKNSNSlpaLLLNAHFDSV-----------------PTSPGATDDGMGVAVMLEVLRYLSKSGHQPKRDII 141
|
90 100 110
....*....|....*....|....*....|....*....
gi 3717826 176 VLFNTDEEKGSFGSRDLIQEE--AKLADYVLSFEPTSAG 212
Cdd:cd03875 142 FLFNGAEENGLLGAHAFITQHpwAKNVRAFINLEAAGAG 180
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
77-300 |
1.66e-08 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349914 [Multi-domain] Cd Length: 399 Bit Score: 56.96 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 77 LEAELKNLGFTVTRSksaglVVGDNIVGKIKGRGGKNLLLMSHMDTVYLK---GILAKAPFRVEGDKAYGPGIADDKGGN 153
Cdd:cd05664 27 IAEELRKLGFEVTTG-----IGGTGVVAVLRNGEGPTVLLRADMDALPVEentGLPYASTVRMKDWDGKEVPVMHACGHD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 154 ---AVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSfGSRDLIQ----EEAKLADYVLSFE--PTSAGDEKLSLG--TSG 222
Cdd:cd05664 102 mhvAALLGAARLLVEAKDAWSGTLIAVFQPAEETGG-GAQAMVDdglyDKIPKPDVVLAQHvmPGPAGTVGTRPGrfLSA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 223 IAYVQVQITGKASHaGAAPELGVNALVEASDLVLRTMNIDDKAKNLR---------FQwtiakAGQVSNIIPASATLNAD 293
Cdd:cd05664 181 ADSLDITIFGRGGH-GSMPHLTIDPVVMAASIVTRLQTIVSREVDPQefavvtvgsIQ-----AGSAENIIPDEAELKLN 254
|
....*..
gi 3717826 294 VRYARNE 300
Cdd:cd05664 255 VRTFDPE 261
|
|
| Iap |
COG2234 |
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ... |
61-222 |
1.68e-08 |
|
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];
Pssm-ID: 441835 [Multi-domain] Cd Length: 257 Bit Score: 55.91 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 61 ETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGKN--LLLMSHMDTVYlkgilakapfrveg 138
Cdd:COG2234 8 GGGTTAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPDevVVLGAHYDSVG-------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 139 dkAYGPGIADDKGGNAVILHTLKLLKEYGVR-DYgTITVLFNTDEEKGSFGSR----DLIQEEAKLAdYVLSFEPTSAGD 213
Cdd:COG2234 74 --SIGPGADDNASGVAALLELARALAALGPKpKR-TIRFVAFGAEEQGLLGSRyyaeNLKAPLEKIV-AVLNLDMIGRGG 149
|
....*....
gi 3717826 214 EKLSLGTSG 222
Cdd:COG2234 150 PRNYLYVDG 158
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
154-372 |
3.48e-08 |
|
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349919 [Multi-domain] Cd Length: 371 Bit Score: 55.76 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 154 AVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSfGSRDLIQEEA-KLADYVLSFEptsaGDEKLSLGTSGI------AYV 226
Cdd:cd05669 98 ASLLGAAVLLKEREAELKGTVRLIFQPAEETGA-GAKKVIEAGAlDDVSAIFGFH----NKPDLPVGTIGLksgalmAAV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 227 ---QVQITGKASHAgAAPELGVNALVEASDLVL-------RTMNIDDKAknlrfQWTIAK--AGQVSNIIPASATLNADV 294
Cdd:cd05669 173 drfEIEIAGKGAHA-AKPENGVDPIVAASQIINalqtivsRNISPLESA-----VVSVTRihAGNTWNVIPDSAELEGTV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 295 RyarneDFDAAM-KTLEERAQQ--KKLPEA-DVKVIV--TRGRPA-FNAGEggkkLVDKAVAYYKEAGGTLGVEERTGGG 367
Cdd:cd05669 247 R-----TFDAEVrQLVKERFEQivEGIAAAfGAKIEFkwHSGPPAvINDEE----LTDLASEVAAQAGYEVVHAEPSLGG 317
|
....*
gi 3717826 368 TDAAY 372
Cdd:cd05669 318 EDFAF 322
|
|
| PRK12890 |
PRK12890 |
allantoate amidohydrolase; Reviewed |
65-374 |
2.62e-07 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 237248 [Multi-domain] Cd Length: 414 Bit Score: 53.37 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 65 GDAEGIAAAgnFLEAELKNLGFTVTRSKsAGlvvgdNIVGKIKGRGG--KNLLLMSHMDTVYLKGILakapfrvegDKAY 142
Cdd:PRK12890 34 SDEERAARA--LLAAWMRAAGLEVRRDA-AG-----NLFGRLPGRDPdlPPLMTGSHLDTVPNGGRY---------DGIL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 143 GpgIAddkGGNAVIlHTLKllkEYGVRDYGTITVLFNTDEEkGS------FGSR----DLIQEEAK---------LAD-- 201
Cdd:PRK12890 97 G--VL---AGLEVV-AALR---EAGIRPPHPLEVIAFTNEE-GVrfgpsmIGSRalagTLDVEAVLatrdddgttLAEal 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 202 ----YVLSFEPTSAGD--------------------EKLSLGT----SGIAYVQVQITGKASHAGAAP-ELGVNALVEAS 252
Cdd:PRK12890 167 rrigGDPDALPGALRPpgavaaflelhieqgpvleaEGLPIGVvtaiQGIRRQAVTVEGEANHAGTTPmDLRRDALVAAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 253 DLVLRtmnIDDKAKNLRFQwTIAKAGQVS------NIIPASATLNADVRYARNEDFDAAMKTLEERAQQkKLPEADVKVI 326
Cdd:PRK12890 247 ELVTA---MERRARALLHD-LVATVGRLDvepnaiNVVPGRVVFTLDLRSPDDAVLEAAEAALLAELEA-IAAARGVRIE 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 3717826 327 VT---RGRPA-FNAGeggkkLVDkAVAyykEAGGTLGVEERT---GGGTDAAYAA 374
Cdd:PRK12890 322 LErlsRSEPVpCDPA-----LVD-AVE---AAAARLGYPSRRmpsGAGHDAAAIA 367
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
154-374 |
5.44e-07 |
|
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in 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 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. ACY1L2 family 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 E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.
Pssm-ID: 349945 [Multi-domain] Cd Length: 366 Bit Score: 51.86 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 154 AVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRD-----LIQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQV 228
Cdd:cd08660 96 TSIIGTA*LLNQRRAELKGTVVFIFQPAEEGAAGARKVleagvLNGVSAIFGIHNKPDLPVGTIGVKEGPL*ASVDVFEI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 229 QITGKASHAgAAPELGVNALVEASDLV-----LRTMNIDDKaKNLRFQWTIAKAGQVSNIIPASATLNADVRYARNEDFD 303
Cdd:cd08660 176 VIKGKGGHA-SIPNNSIDPIAAAGQIIsglqsVVSRNISSL-QNAVVSITRVQGGTAWNVIPDQAE*EGTVRAFTKEARQ 253
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3717826 304 AAMKTLEERAQQkklpeadvKVIVTRGRPAFNAGEGG-------KKLVDKAVAYYKEAGGTLGVEERTGGGTDAAYAA 374
Cdd:cd08660 254 AVPEH*RRVAEG--------IAAGYGCQAEFKWFPNGpsevqndGTLLNAFSKAAARLGYATVHAEQSPGSEDFALYQ 323
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
39-238 |
6.45e-07 |
|
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: 52.22 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 39 LFQAATDEQPAVIKTLEKLVNIETGTGDAE---GIAAAGNFLEAELKNLGFTVTrsksagLV-VGDN------------- 101
Cdd:cd05676 1 VFKYIDEHQDEFIERLREAVAIQSVSADPEkrpELIRMMEWAAERLEKLGFKVE------LVdIGTQtlpdgeelplppv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 102 IVGKIKGRGGKN-LLLMSHMDT--VYLKGILAKAPFR-VEGD-KAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITV 176
Cdd:cd05676 75 LLGRLGSDPSKKtVLIYGHLDVqpAKLEDGWDTDPFElTEKDgKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 177 LFNTDEEKGSFGSRDLIQEEAKL----ADYVLSFEPTSAGDEK--LSLGTSGIAYVQVQITG--KASHAG 238
Cdd:cd05676 155 CFEGMEESGSEGLDELIEARKDTffsdVDYVCISDNYWLGKKKpcLTYGLRGICYFFIEVEGpnKDLHSG 224
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
76-372 |
7.72e-07 |
|
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: 51.57 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 76 FLEAELKNLGFTVTRSKSAGLVVgdNIVGkikGRGGKNLLLMSHMDTVYLKGiLAKAPFrvegdKAYGPGI----ADDkG 151
Cdd:cd08019 24 RIKEELDKLGIPYVETGGTGVIA--TIKG---GKAGKTVALRADIDALPVEE-CTDLEY-----KSKNPGLmhacGHD-G 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 152 GNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSfGSRDLIqEEAKLAD-------YVLSFEPTSagdeKLSLGT---- 220
Cdd:cd08019 92 HTAMLLGAAKILNEIKDTIKGTVKLIFQPAEEVGE-GAKQMI-EEGVLEDvdavfgiHLWSDVPAG----KISVEAgprm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 221 SGIAYVQVQITGKASHaGAAPELGVNALVEASDLVLRTMNI----DDKAKNLRFQWTIAKAGQVSNIIPASATLNADVRY 296
Cdd:cd08019 166 ASADIFKIEVKGKGGH-GSMPHQGIDAVLAAASIVMNLQSIvsreIDPLEPVVVTVGKLNSGTRFNVIADEAKIEGTLRT 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3717826 297 ARNEDFDAAMKTLEERAQQ-KKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAyyKEAGGT-LGVEERTGGGTDAAY 372
Cdd:cd08019 245 FNPETREKTPEIIERIAKHtAASYGAEAELTYGAATPPVINDEKLSKIARQAAI--KIFGEDsLTEFEKTTGSEDFSY 320
|
|
| M20_Acy1_IAAspH |
cd05665 |
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, ... |
152-315 |
8.51e-07 |
|
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, bacterial and archaeal aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349915 [Multi-domain] Cd Length: 415 Bit Score: 51.55 E-value: 8.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 152 GNAVI-LHTLKLLKEYGVRDYGTITVLFNTDEEkGSFGSRDLIqeEAKL---ADYVLSFE-PTSAGDEKLSLGTSGI--- 223
Cdd:cd05665 140 GHTAIgLGLAHALAQLKDSLSGTIKLIFQPAEE-GVRGARAMA--EAGVvddVDYFLASHiGFGVPSGEVVCGPDNFlat 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 224 AYVQVQITGKASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNL-RFQWTIAKAGQVSNIIPASATLNADVRYARNEdf 302
Cdd:cd05665 217 TKLDARFTGVSAHAGAAPEDGRNALLAAATAALNLHAIPRHGEGAtRINVGVLGAGEGRNVIPASAELQVETRGETTA-- 294
|
170
....*....|...
gi 3717826 303 daAMKTLEERAQQ 315
Cdd:cd05665 295 --INEYMFEQAQR 305
|
|
| M20_IAA_Hyd |
cd08017 |
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ... |
154-311 |
1.22e-06 |
|
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349938 [Multi-domain] Cd Length: 376 Bit Score: 50.78 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 154 AVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSfGSRDLIQE------EAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQ 227
Cdd:cd08017 94 AMLLGAAKLLKARKHLLKGTVRLLFQPAEEGGA-GAKEMIKEgalddvEAIFGMHVSPALPTGTIASRPGPFLAGAGRFE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 228 VQITGKASHAgAAPELGVNALVEASDLVLRTMNI----DDKAKNLRFQWTIAKAGQVSNIIPASATLNADVRYARNEDFD 303
Cdd:cd08017 173 VVIRGKGGHA-AMPHHTVDPVVAASSAVLALQQLvsreTDPLDSQVVSVTRFNGGHAFNVIPDSVTFGGTLRALTTEGFY 251
|
....*...
gi 3717826 304 AAMKTLEE 311
Cdd:cd08017 252 RLRQRIEE 259
|
|
| PRK12893 |
PRK12893 |
Zn-dependent hydrolase; |
88-315 |
1.23e-06 |
|
Zn-dependent hydrolase;
Pssm-ID: 237250 [Multi-domain] Cd Length: 412 Bit Score: 51.03 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 88 VTRSKSAGLVVG-D---NIVGKIKGRGGKNLLLM--SHMDTVYLKGILakapfrvegDKAYGpgiaddkggnaVI--LHT 159
Cdd:PRK12893 47 AQWMEEAGLTVSvDaigNLFGRRAGTDPDAPPVLigSHLDTQPTGGRF---------DGALG-----------VLaaLEV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 160 LKLLKEYGVRDYGTITVLFNTDEEKGSF-----GSR----DLIQEEAK---------LADYV--LSFEPTSA-------- 211
Cdd:PRK12893 107 VRTLNDAGIRTRRPIEVVSWTNEEGARFapamlGSGvftgALPLDDALarrdadgitLGEALarIGYRGTARvgrravda 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 212 --------G----DEKLSLGT----SGIAYVQVQITGKASHAGAAP-ELGVNALVEASDLVLRtmnIDDKAKNL--RFQW 272
Cdd:PRK12893 187 ylelhieqGpvleAEGLPIGVvtgiQGIRWLEVTVEGQAAHAGTTPmAMRRDALVAAARIILA---VERIAAALapDGVA 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 3717826 273 TIakaGQV------SNIIPASATLNADVRYARNEDFDAAMKTLEERAQQ 315
Cdd:PRK12893 264 TV---GRLrvepnsRNVIPGKVVFTVDIRHPDDARLDAMEAALRAACAK 309
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
42-241 |
7.70e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 48.75 E-value: 7.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 42 AATDEQ-PAVIKTLEKLVNIET---GTGDAEGIAAAGNFLEAELKNLGF---TVTRSKSAGLVVGDnivgKIKGRGGKNL 114
Cdd:PRK07907 11 ARVAELlPRVRADLEELVRIPSvaaDPFRREEVARSAEWVADLLREAGFddvRVVSADGAPAVIGT----RPAPPGAPTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 115 LLMSHMDtVYLKGILAK---APFR-VE-GDKAYGPGIADDKGGnaVILHtLKLLKEYGVRDYGTITVLFNTDEEKGSFGS 189
Cdd:PRK07907 87 LLYAHHD-VQPPGDPDAwdsPPFElTErDGRLYGRGAADDKGG--IAMH-LAALRALGGDLPVGVTVFVEGEEEMGSPSL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3717826 190 RDLIQEEAKL--ADYVLSFEPTSAGDEKLSLGTS--GIA--YVQVQITGKASHA----GAAP 241
Cdd:PRK07907 163 ERLLAEHPDLlaADVIVIADSGNWSVGVPALTTSlrGNAdvVVTVRTLEHAVHSgqfgGAAP 224
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
47-185 |
7.86e-06 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 48.81 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 47 QPAVIKTLEKLVNIETGTgdAEGIAAAGN--FLE--AELKNLgftvtrSKSAGLVVG--DNIVGKIK--GRGGKNLLLMS 118
Cdd:PRK06156 45 GAAAIESLRELVAFPTVR--VEGVPQHENpeFIGfkKLLKSL------ARDFGLDYRnvDNRVLEIGlgGSGSDKVGILT 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3717826 119 HMDTV------YLKGILAKAPFRV--EGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKG 185
Cdd:PRK06156 117 HADVVpanpelWVLDGTRLDPFKVtlVGDRLYGRGTEDDKGAIVTALYAMKAIKDSGLPLARRIELLVYTTEETD 191
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
67-255 |
1.14e-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: 349929 [Multi-domain] Cd Length: 437 Bit Score: 48.07 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 67 AEGIAAAGNFLEAELKNLGFTVTRSKSAG---LVVGDnivgKIKGRGGKNLLLMSHMDtVYLKGILA---KAPFR--VEG 138
Cdd:cd05680 20 KGDVRRAAEWLADKLTEAGFEHTEVLPTGghpLVYAE----WLGAPGAPTVLVYGHYD-VQPPDPLElwtSPPFEpvVRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 139 DKAYGPGIADDKGGNAVILHTLK-LLKEYG---VRdygtITVLFNTDEEKGSFGSRDLIQEEAKL--ADYVLSFEPT--S 210
Cdd:cd05680 95 GRLYARGASDDKGQVFIHIKAVEaWLAVEGalpVN----VKFLIEGEEEIGSPSLPAFLEENAERlaADVVLVSDTSmwS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 3717826 211 AGDEKLSLGTSGIAYVQVQITG------KASHAGAAPelgvNALVEASDLV 255
Cdd:cd05680 171 PDTPTITYGLRGLAYLEISVTGpnrdlhSGSYGGAVP----NPANALARLL 217
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
226-312 |
1.17e-05 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349916 [Multi-domain] Cd Length: 373 Bit Score: 47.91 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 226 VQVQITGKASHaGAAPELGVNALVEASDLVLRTMNIddKAKNL-----------RFQwtiakAGQVSNIIPASATLNADV 294
Cdd:cd05666 175 FEITIRGKGGH-AAMPHLGVDPIVAAAQLVQALQTI--VSRNVdpldaavvsvtQIH-----AGDAYNVIPDTAELRGTV 246
|
90
....*....|....*....
gi 3717826 295 RYarnedFDAAM-KTLEER 312
Cdd:cd05666 247 RA-----FDPEVrDLIEER 260
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
45-249 |
1.35e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 47.77 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 45 DEQPAVIKTLEKLVNIETGTGDAEGIAAAG----NFLEAEL---KNLGFTVTRSKsaglvvgDNIVGKIK-GRGGKNLLL 116
Cdd:PRK07205 8 KVQDACVAAIKTLVSYPSVLNEGENGTPFGqaiqDVLEATLdlcQGLGFKTYLDP-------KGYYGYAEiGQGEELLAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 117 MSHMDTVyLKGILAK---APFR--VEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEE-------- 183
Cdd:PRK07205 81 LCHLDVV-PEGDLSDwqtPPFEavEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGTDEEtlwrcmnr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 184 ------KGSFG-----SRDLIQEE-----AKL---ADYVLSFE--------PTSA---GD--EKL--SLGTSGIAYV--- 226
Cdd:PRK07205 160 yneveeQATMGfapdsSFPLTYAEkgllqAKLvgpGSDQLELEvgqafnvvPAKAsyqGPklEAVkkELDKLGFEYVvke 239
|
250 260
....*....|....*....|....
gi 3717826 227 -QVQITGKASHAGAAPElGVNALV 249
Cdd:PRK07205 240 nEVTVLGKSVHAKDAPQ-GINAVI 262
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
45-255 |
2.47e-05 |
|
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: 46.78 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 45 DEQpavIKTLEKLVNIETGTgdAEGIAAAGNFLEAEL-KNLGFTVTR-------SKSAGLVVGDN-IVGKIKGRGGKNLL 115
Cdd:cd02697 3 DEE---VRFLQKLVRVPTDT--PPGNNAPHAERTAALlQGFGFEAERhpvpeaeVRAYGMESITNlIVRRRYGDGGRTVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 116 LMSHMDTVYLKGILAKAPF--RVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEE-KGSFGSRDL 192
Cdd:cd02697 78 LNAHGDVVPPGDGWTRDPYgaVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEfGGELGPGWL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3717826 193 IQEEAKLADYVL----SFEPTSAGDeklslgtsGIAYVQVQITGKASHAgAAPELGVNALVEASDLV 255
Cdd:cd02697 158 LRQGLTKPDLLIaagfSYEVVTAHN--------GCLQMEVTVHGKQAHA-AIPDTGVDALQGAVAIL 215
|
|
| M28_like |
cd05662 |
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ... |
51-200 |
5.56e-05 |
|
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins that do not contain a protease-associated (PA) domain.
Pssm-ID: 349912 [Multi-domain] Cd Length: 268 Bit Score: 45.15 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 51 IKTL--EKLVNIETGTgdaEGIAAAGNFLEAELKNLG---------FTVTRSKSAGLVVGDNIVGKIKG--RGGKNLLLM 117
Cdd:cd05662 6 VKILssDKFEGRKTGT---KGAAKTRAYIIERFKQIGllpwgdrfeHPFSYTKRFSTRQGVNVLAVIKGsePPTKWRVVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 118 SHMDTVYLKgilakapfrveGDKAYgPGIADDKGGNAVILHtlklLKEYGVRDYGTITVLF-NTD-EEKGSFGSR----D 191
Cdd:cd05662 83 AHYDHLGIR-----------GGKIY-NGADDNASGVAALLA----LAEYFKKHPPKHNVIFaATDaEEPGLRGSYafveA 146
|
....*....
gi 3717826 192 LIQEEAKLA 200
Cdd:cd05662 147 LKVPRAQIE 155
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
76-371 |
7.60e-05 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of uncharacterized bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349936 [Multi-domain] Cd Length: 371 Bit Score: 45.34 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 76 FLEAELKNLGFTVTRsksagLVVGDNIVGKIKG-RGGKNLLLMSHMD---TVYLKGIlakaPFRVEGdkaygPGIADDKG 151
Cdd:cd08014 24 FVAERLRDLGLKPKE-----FPGGTGLVCDIGGkRDGRTVALRADMDalpIQEQTGL----PYRSTV-----PGVMHACG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 152 ---------GNAVILHTLKLLKEYGVRdygtitVLFNTDEEKGSFGSRDLIQEEAkLAD----YVLSFEPT-SAGDEKLS 217
Cdd:cd08014 90 hdahtaialGAALVLAALEEELPGRVR------LIFQPAEETMPGGALDMIRAGA-LDGvsaiFALHVDPRlPVGRVGVR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 218 LG--TSGIAYVQVQITGKASHaGAAPELGVNALVEASDLVLRTMNIDDKAKNLR----FQWTIAKAGQVSNIIPASATLN 291
Cdd:cd08014 163 YGpiTAAADSLEIRIQGEGGH-GARPHLTVDLVWAAAQVVTDLPQAISRRIDPRspvvLTWGSIEGGRAPNVIPDSVELS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 292 ADVRYARNEDFDAAMKTLEERAQQKKLP-EADVKVIVTRGRPAFNAGEGGKKLVDKAVayyKEAGGT---LGVEERTGGG 367
Cdd:cd08014 242 GTVRTLDPDTWAQLPDLVEEIVAGICAPyGAKYELEYRRGVPPVINDPASTALLEAAV---REILGEdnvVALAEPSMGG 318
|
....
gi 3717826 368 TDAA 371
Cdd:cd08014 319 EDFA 322
|
|
| FrvX |
COG1363 |
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ... |
51-123 |
8.28e-05 |
|
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];
Pssm-ID: 440974 [Multi-domain] Cd Length: 353 Bit Score: 45.12 E-value: 8.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3717826 51 IKTLEKLVNIETGTGDAEGIAAagnFLEAELKNLGFTVTRSKsAGlvvgdNIVGKIKGRG-GKNLLLMSHMDTV 123
Cdd:COG1363 5 LELLKELTEAPGPSGFEDEVRE---YIKEELEPLGDEVETDR-LG-----NLIATKKGKGdGPKVMLAAHMDEI 69
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
38-204 |
1.12e-04 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 44.93 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 38 VLFQAATDEQPAViKTLEKLVNIET--GTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGR--GGKN 113
Cdd:PRK08262 35 AVAPVAVDEDAAA-ERLSEAIRFRTisNRDRAEDDAAAFDALHAHLEESYPAVHAALEREVVGGHSLLYTWKGSdpSLKP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 114 LLLMSHMDTV----YLKGILAKAPF--RVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSF 187
Cdd:PRK08262 114 IVLMAHQDVVpvapGTEGDWTHPPFsgVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVGGL 193
|
170 180
....*....|....*....|
gi 3717826 188 GSR---DLIQEEAKLADYVL 204
Cdd:PRK08262 194 GARaiaELLKERGVRLAFVL 213
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
76-312 |
1.14e-04 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 44.57 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 76 FLEAELKNLGFTVTRsksagLVVGDNIVGKIKGRG-GKNLLLMSHMDTVYLKGiLAKAPFrvegdKAYGPGIA-----Dd 149
Cdd:cd08021 35 YIANELKKLGLEVET-----NVGGTGVVATLKGGKpGKTVALRADMDALPIEE-ETDLPF-----KSKNPGVMhacghD- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 150 kGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQE------EAKLADYVLSFEPTsaGDEKLSLG--TS 221
Cdd:cd08021 103 -GHTAMLLGAAKVLAENKDEIKGTVRFIFQPAEEVPPGGAKPMIEAgvlegvDAVFGLHLWSTLPT--GTIAVRPGaiMA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 222 GIAYVQVQITGKASHaGAAPELGVNALVEASDLVL-------RTMNIDDKAknlrfQWTIAK--AGQVSNIIPASATLNA 292
Cdd:cd08021 180 APDEFDITIKGKGGH-GSMPHETVDPIVIAAQIVTalqtivsRRVDPLDPA-----VVTIGTfqGGTSFNVIPDTVELKG 253
|
250 260
....*....|....*....|
gi 3717826 293 DVRYaRNEDFDAAMKTLEER 312
Cdd:cd08021 254 TVRT-FDEEVREQVPKRIER 272
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
101-330 |
1.17e-04 |
|
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: 44.76 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 101 NIVGKIKGRGGKNLL--LMSHMDTVYL-KGILAKAPFR--VEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTIT 175
Cdd:cd08012 66 NIIVEYPGTVDGKTVsfVGSHMDVVTAnPETWEFDPFSlsIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 176 VLFNTDEEKGSF---GSRDLIQ--EEAKLADYVLSFEPTSagDEKLSLGTSGIAYVQVQITGKASHAGAaPELGVNAL-- 248
Cdd:cd08012 146 AVFIANEENSEIpgvGVDALVKsgLLDNLKSGPLYWVDSA--DSQPCIGTGGMVTWKLTATGKLFHSGL-PHKAINALel 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 249 -VEASDLVLRTMNID----DKAKNLRF---------QWTIAkAGQVsNIIPASATLNADVRYARNEDFDAAMKTLEERAQ 314
Cdd:cd08012 223 vMEALAEIQKRFYIDfpphPKEEVYGFatpstmkptQWSYP-GGSI-NQIPGECTICGDCRLTPFYDVKEVREKLEEYVD 300
|
250
....*....|....*.
gi 3717826 315 QKKlpeADVKVIVTRG 330
Cdd:cd08012 301 DIN---ANIEELPTRG 313
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
71-374 |
1.83e-04 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 43.99 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 71 AAAGNFLEAELKNLGFTVtRSKSAGlvvgdNIVGKIKGRG-GKNLLLM-SHMDTVYLKGILakapfrvegDKAYGpgiad 148
Cdd:PRK09290 37 LQARDLFAEWMEAAGLTV-RVDAVG-----NLFGRLEGRDpDAPAVLTgSHLDTVPNGGRF---------DGPLG----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 149 dkggnaVI--LHTLKLLKEYGVRDYGTITVLFNTDEEkGS------FGSR----DLIQEEAK---------LADyVLS-- 205
Cdd:PRK09290 97 ------VLagLEAVRTLNERGIRPRRPIEVVAFTNEE-GSrfgpamLGSRvftgALTPEDALalrdadgvsFAE-ALAai 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 206 -FEPTSAG------------------------DEKLSLG-TSGIA---YVQVQITGKASHAGAAP-ELGVNALVEASDLV 255
Cdd:PRK09290 169 gYDGDEAVgaararrdikafvelhieqgpvleAEGLPIGvVTGIVgqrRYRVTFTGEANHAGTTPmALRRDALLAAAEII 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 256 LRTMNI-DDKAKNLRfqwtiAKAGQVS------NIIPASATLNADVRYARNEDFDAA----MKTLEERAQQKKLpEADVK 324
Cdd:PRK09290 249 LAVERIaAAHGPDLV-----ATVGRLEvkpnsvNVIPGEVTFTLDIRHPDDAVLDALvaelRAAAEAIAARRGV-EVEIE 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 3717826 325 VIVTRGRPAFNAGeggkkLVDKAvayyKEAGGTLGVEER---TGGGTDAAYAA 374
Cdd:PRK09290 323 LISRRPPVPFDPG-----LVAAL----EEAAERLGLSYRrlpSGAGHDAQILA 366
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
35-201 |
3.03e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 43.75 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 35 RDNVLFQAATD-EQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAE----LKNLGFTVTRSKSAGLVVGDNIVG-KIKG 108
Cdd:PRK07079 3 REAAIARAAAYfDSGAFFADLARRVAYRTESQNPDRAPALRAYLTDEiapaLAALGFTCRIVDNPVAGGGPFLIAeRIED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 109 RGGKNLLLMSHMDTVylKGILAK-----APFR--VEGDKAYGPGIADDKGGNAVILHTLKL-LKEYGVRDYGTITVLFNT 180
Cdd:PRK07079 83 DALPTVLIYGHGDVV--RGYDEQwreglSPWTltEEGDRWYGRGTADNKGQHTINLAALEQvLAARGGRLGFNVKLLIEM 160
|
170 180
....*....|....*....|...
gi 3717826 181 DEEKGSFGSRDLIQEEAKL--AD 201
Cdd:PRK07079 161 GEEIGSPGLAEVCRQHREAlaAD 183
|
|
| M28_like_PA |
cd05660 |
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ... |
61-190 |
3.57e-04 |
|
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.
Pssm-ID: 349910 [Multi-domain] Cd Length: 290 Bit Score: 42.73 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 61 ETGTgdaEGIAAAGNFLEAELKNLGF-----------TVTRSKSAGLVVGDNIVGKIKGRGGKN--LLLMSHMDTVylkG 127
Cdd:cd05660 13 APGS---EGEKKTVDYLAEQFKELGLkpagsdgsylqAVPLVSKIEYSTSHNVVAILPGSKLPDeyIVLSAHWDHL---G 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3717826 128 ILAKApfrvEGDKAYgPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSR 190
Cdd:cd05660 87 IGPPI----GGDEIY-NGAVDNASGVAAVLELARVFAAQDQRPKRSIVFLAVTAEEKGLLGSR 144
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
108-287 |
6.38e-04 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 42.32 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 108 GRGGKNLLLMSHMD-----TVYLKGILAKAPfRVEGDKAYGPGIADDkgGNAVI--LHTLKLLKEYGVrDYGTITVLFNT 180
Cdd:cd05682 70 EQDDDTVLLYGHMDkqppfTGWDEGLGPTKP-VIRGDKLYGRGGADD--GYAIFasLTAIKALQEQGI-PHPRCVVLIEA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 181 DEEKGSFgsrDLIQEEAKLA------DYVLSFEPTSAGDEKLSLGTS--GI--AYVQVQITGKASHAGAApelgvNALVE 250
Cdd:cd05682 146 CEESGSA---DLPFYLDKLKerignvDLVVCLDSGCGNYEQLWLTTSlrGVlgGDLTVQVLNEGVHSGDA-----SGIVP 217
|
170 180 190
....*....|....*....|....*....|....*....
gi 3717826 251 ASDLVLRTM--NIDDKAKNlrfqwTIAKAGQVSNiIPAS 287
Cdd:cd05682 218 SSFRILRQLlsRIEDENTG-----EVKLDEQHCD-IPAH 250
|
|
| M20_Acy1L2_AbgB |
cd05673 |
M20 Peptidase Aminoacylase 1-like protein 2 aminobenzoyl-glutamate utilization protein B ... |
161-312 |
1.98e-03 |
|
M20 Peptidase Aminoacylase 1-like protein 2 aminobenzoyl-glutamate utilization protein B subfamily; Peptidase M20 family, ACY1L2 aminobenzoyl-glutamate utilization protein B (AbgB) subfamily. This group contains mostly bacterial amidohydrolases, including gene products of abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate is a natural end product of folate catabolism, and its utilization is initiated by the abg region gene product, AbgT, by enabling uptake of its into the cell in a concentration-dependent, saturable manner. It is subsequently cleaved by AbgA and AbgB (sometimes referred to as AbgAB).
Pssm-ID: 349922 [Multi-domain] Cd Length: 437 Bit Score: 40.75 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 161 KLLKEYGVRdyGTItVLFNTDEEKGSFGSRDLIQEEA-KLADYVLSFEPTS--AGDEklslgTSGIAYVQVQ--ITGKAS 235
Cdd:cd05673 116 DYMEENNLA--GTV-RFYGCPAEEGGSGKTFMVRDGVfDDVDAAISWHPASfnGVWS-----TSSLANISVKfkFKGISA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 236 HAGAAPELGVNALvEASDLvlrtMNID---------DKAknlRFQWTIAKAGQVS-NIIPAsatlNADVRYA-RNEDFDa 304
Cdd:cd05673 188 HAAAAPHLGRSAL-DAVEL----MNVGvnylrehmiPEA---RVHYAITNGGGAApNVVPA----FAEVWYYiRAPKME- 254
|
....*...
gi 3717826 305 AMKTLEER 312
Cdd:cd05673 255 AAEELYDR 262
|
|
| M28_Pgcp_like |
cd03883 |
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate ... |
143-222 |
2.15e-03 |
|
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate carboxypeptidase (PGCP; blood plasma glutamate carboxypeptidase; EC 3.4.17.21) subfamily. PGCP is a 56kDa glutamate carboxypeptidase that is mainly produced in mammalian placenta and kidney, the majority of which is thought to be secreted into the bloodstream. Similar proteins are also found in other species, including bacteria. These proteins contain protease-associated (PA) domain inserts between the first and second strands of the central beta sheet in the protease-like domain. The PA domains may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. The exact physiological substrates of PGCP are unknown, although this enzyme may play an important role in the hydrolysis of circulating peptides. Its closest homolog encodes an important brain glutamate carboxypeptidase II (NAALADase) identical to the prostate-specific membrane antigen (PSMA), which serves as a marker for prostatic cancer metastasis. Hypermethylation of PGCP gene has been associated with human bronchial epithelial (HBE) cell immortalization and lung cancer. PGCP also provides an attractive target for serological analysis in hepatitis C virus (HCV)-induced hepatocellular carcinoma (HCC) patients.
Pssm-ID: 349879 [Multi-domain] Cd Length: 425 Bit Score: 40.76 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 143 GPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRD-LIQEEAKLADYVLSFEPTSAGDEKLSLGTS 221
Cdd:cd03883 255 GTGAMDDGGGVAISWEALKLIKDLGLKPKRTIRVVLWTGEEQGLVGAKAyAEAHKDELENHVFAMESDIGTFTPYGLQFT 334
|
.
gi 3717826 222 G 222
Cdd:cd03883 335 G 335
|
|
| M28_like |
cd08015 |
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ... |
101-195 |
2.33e-03 |
|
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.
Pssm-ID: 349937 [Multi-domain] Cd Length: 218 Bit Score: 39.89 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3717826 101 NIVGKIKGRGGKNLLLM--SHMDTVYlkgilakapfrvegdkaYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLF 178
Cdd:cd08015 3 NVIAEIPGSDKKDEVVIlgAHLDSWH-----------------GATGATDNGAGTAVMMEAMRILKAIGSKPKRTIRVAL 65
|
90
....*....|....*..
gi 3717826 179 NTDEEKGSFGSRDLIQE 195
Cdd:cd08015 66 WGSEEQGLHGSRAYVEK 82
|
|
| |
