|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
2-469 |
0e+00 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 989.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 2 STLSLDKVLNHLDANLNKSLDRLFNLLRIKSISTDPAYKADCRKAAEWLVEDLNSIGFDASVRDTPGHPMVVAHHEGATA 81
Cdd:PRK09104 1 SMADLDPVLDHIDANLDASLERLFALLRIPSISTDPAYAADCRKAADWLVADLASLGFEASVRDTPGHPMVVAHHEGPTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 82 DAPHVLFYGHYDVQPVDPLSLWENDPFDPAIKDVGDasngGRKILTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTL 161
Cdd:PRK09104 81 DAPHVLFYGHYDVQPVDPLDLWESPPFEPRIKETPD----GRKVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 162 LFEGEEESGSPSLKPFLEANRQELKADVALVCDTAMWDAETPAISVGLRGLVGEEIVIKAADRDLHSGFFGGAAANPIHI 241
Cdd:PRK09104 157 LFEGEEESGSPSLVPFLEANAEELKADVALVCDTGMWDRETPAITTSLRGLVGEEVTITAADRDLHSGLFGGAAANPIRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 242 LTKILADLHDETGRITIPDFYEGVEETPTQILKSWESLGRTAESFLGPIGLSIPAGEKGRSVLELTWARPTAEVNGIIGG 321
Cdd:PRK09104 237 LTRILAGLHDETGRVTLPGFYDGVEELPPEILAQWKALGFTAEAFLGPVGLSIPAGEKGRSVLEQIWSRPTCEINGIWGG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 322 YTGEGFKTVIAAEASAKVSFRLVHKQDPVKIREAFRAFVKERVPADCSVEFHPHGGSPAIQLPYDSPLVSKAKNALSDEW 401
Cdd:PRK09104 317 YTGEGFKTVIPAEASAKVSFRLVGGQDPAKIREAFRAYVRARLPADCSVEFHDHGGSPAIALPYDSPALAAAKAALSDEW 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 479375213 402 PKPAVLIAMGGSIPIVGDFNTFLGMESLLVGFGLEDDRIHSPNEKYELNSFHKGQRSWARILAAIAAK 469
Cdd:PRK09104 397 GKPAVLIGSGGSIPIVGDFKRILGMDSLLVGFGLDDDRIHSPNEKYDLESFHKGIRSWARILAALAEA 464
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
21-466 |
0e+00 |
|
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: 572.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 21 LDRLFNLLRIKSISTDPAYKADCRKAAEWLVEDLNSIGFD-ASVRDTPGHPMVVAHHEGAtADAPHVLFYGHYDVQPVDP 99
Cdd:cd05680 1 LEELFELLRIPSVSADPAHKGDVRRAAEWLADKLTEAGFEhTEVLPTGGHPLVYAEWLGA-PGAPTVLVYGHYDVQPPDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 100 LSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESGSPSLKPFLE 179
Cdd:cd05680 80 LELWTSPPFEPVVRD-------GR--LYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIGSPSLPAFLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 180 ANRQELKADVALVCDTAMWDAETPAISVGLRGLVGEEIVIKAADRDLHSGFFGGAAANPIHILTKILADLHDETGRITIP 259
Cdd:cd05680 151 ENAERLAADVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNRDLHSGSYGGAVPNPANALARLLASLHDEDGRVAIP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 260 DFYEGVEETPTQILKSWESLGRTAESFLGPIGLSIPAGEKGRSVLELTWARPTAEVNGIIGGYTGEGFKTVIAAEASAKV 339
Cdd:cd05680 231 GFYDDVRPLTDAEREAWAALPFDEAAFKASLGVPALGGEAGYTTLERLWARPTLDVNGIWGGYQGEGSKTVIPSKAHAKI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 340 SFRLVHKQDPVKIREAFRAFVKERVPADCSVEFHPHGGSPAIQLPYDSPLVSKAKNALSDEWPKPAVLIAMGGSIPIVGD 419
Cdd:cd05680 311 SMRLVPGQDPDAIADLLEAHLRAHAPPGVTLSVKPLHGGRPYLVPTDHPALQAAERALEEAFGKPPVFVREGGSIPIVAL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 479375213 420 FNTFLGMESLLVGFGLEDDRIHSPNEKYELNSFHKGQRSWARILAAI 466
Cdd:cd05680 391 FEKVLGIPTVLMGFGLPDDAIHAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
21-468 |
9.91e-148 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 429.55 E-value: 9.91e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 21 LDRLFNLLRIKSISTDPAYKADCRKAAEWLVEDLNSIGFD-ASVRDTPGHPMVVA---HHEGAtadaPHVLFYGHYDVQP 96
Cdd:PRK08201 17 LEELKEFLRIPSISALSEHKEDVRKAAEWLAGALEKAGLEhVEIMETAGHPIVYAdwlHAPGK----PTVLIYGHYDVQP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 97 VDPLSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESGSPSLKP 176
Cdd:PRK08201 93 VDPLNLWETPPFEPTIRD-------GK--LYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEEIGSPNLDS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 177 FLEANRQELKADVALVCDTAMWDAETPAISVGLRGLVGEEIVIKAADRDLHSGFFGGAAANPIHILTKILADLHDETGRI 256
Cdd:PRK08201 164 FVEEEKDKLAADVVLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLHSGLYGGAVPNALHALVQLLASLHDEHGTV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 257 TIPDFYEGVEETPTQILKSWESLGRTAESFLGPIGLSIPAGEKGRSVLELTWARPTAEVNGIIGGYTGEGFKTVIAAEAS 336
Cdd:PRK08201 244 AVEGFYDGVRPLTPEEREEFAALGFDEEKLKRELGVDELFGEEGYTALERTWARPTLELNGVYGGFQGEGTKTVIPAEAH 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 337 AKVSFRLVHKQDPVKIREAFRAFVKERVPADCSVEFHPHGGSPAIQLPYDSPLVSKAKNALSDEWPKPAVLIAMGGSIPI 416
Cdd:PRK08201 324 AKITCRLVPDQDPQEILDLIEAHLQAHTPAGVRVTIRRFDKGPAFVAPIDHPAIQAAARAYEAVYGTEAAFTRMGGSIPV 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 479375213 417 VGDFNTFLGMESLLVGFGLEDDRIHSPNEKYELNSFHKGQRSWARILAAIAA 468
Cdd:PRK08201 404 VETFSSQLHIPIVLMGFGLPSENFHAPNEHFHLENFDKGLRTLVEYWHQLAE 455
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
24-455 |
1.95e-120 |
|
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: 358.56 E-value: 1.95e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 24 LFNLLRIKSISTDPAYKADCRKAAEWLVEDLNSIGFD-ASVRDTPGHPMVVAHHEGAtADAPHVLFYGHYDVQPVDPLSL 102
Cdd:cd03893 4 LAELVAIPSVSAQPDRREELRRAAEWLADLLRRLGFTvEIVDTSNGAPVVFAEFPGA-PGAPTVLLYGHYDVQPAGDEDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 103 WENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESGSPSLKPFLEANR 182
Cdd:cd03893 83 WDSDPFELTERD-------GR--LYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEESGSPSLDQLVEAHR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 183 QELKADVALVCDTAMWDAETPAISVGLRGLVGEEIVIKAADRDLHSGFFGGAAANPIHILTKILADLHDETGRITIPDFY 262
Cdd:cd03893 154 DLLAADAIVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLDHDLHSGLYGGVVPDPMTALAQLLASLRDETGRILVPGLY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 263 EGVEETP-------TQILKSWESLGRTAEsflgpiglsipagekgrSVLELTWARPTAEVNGIIGGYTGEGFKTVIAAEA 335
Cdd:cd03893 234 DAVRELPeeefrldAGVLEEVEIIGGTTG-----------------SVAERLWTRPALTVLGIDGGFPGEGSKTVIPPRA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 336 SAKVSFRLVHKQDPVKIREAFRAFVKERVPADCSVEFHPHGGSPAIQLPYDSPLVSKAKNALSDEWPKPAVLIAMGGSIP 415
Cdd:cd03893 297 RAKISIRLVPGQDPEEASRLLEAHLEKHAPSGAKVTVSYVEGGMPWRSDPSDPAYQAAKDALRTAYGVEPPLTREGGSIP 376
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 479375213 416 IVGDFNTFLGMESLLVGFGLEDDRIHSPNEKYELNSFHKG 455
Cdd:cd03893 377 FISVLQEFPQAPVLLIGVGDPDDNAHSPNESLRLGNYKEG 416
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
21-455 |
3.23e-101 |
|
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: 309.66 E-value: 3.23e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 21 LDRLFNLLRIKSIStdpAYKADCRKAAEWLVEDLNSIGFDASVRDTPGHPMVVAH-HEGataDAPHVLFYGHYDVQPVDP 99
Cdd:cd05681 2 LEDLRDLLKIPSVS---AQGRGIPETADFLKEFLRRLGAEVEIFETDGNPIVYAEfNSG---DAKTLLFYNHYDVQPAEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 100 LSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESGSPSLKPFLE 179
Cdd:cd05681 76 LELWTSDPFELTIRN-------GK--LYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPNLEKFVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 180 ANRQELKADvALVCDTAMWDAE-TPAISVGLRGLVGEEIVIKAADRDLHSGFfGGAAANPIHILTKILADLHDETGRITI 258
Cdd:cd05681 147 EHADLLKAD-GCIWEGGGKNPKgRPQISLGVKGIVYVELRVKTADFDLHSSY-GAIVENPAWRLVQALNSLRDEDGRVLI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 259 PDFYEGVEETPTQILKSWESLGRTAESFLGPIGLSIPAGEKGRSVLELTWARPTAEVNGIIGGYTGEGFKTVIAAEASAK 338
Cdd:cd05681 225 PGFYDDVRPLSEAERALIDTYDFDPEELRKTYGLKRPLQVEGKDPLRALFTEPTCNINGIYSGYTGEGSKTILPSEAFAK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 339 VSFRLVHKQDPVKIREAFRAFVKERVPADcsVEFHPHGGSPAIQLPYDSPLV----SKAKNALSDEwpkPAVLIAMGGSI 414
Cdd:cd05681 305 LDFRLVPDQDPAKILSLLRKHLDKNGFDD--IEIHDLLGEKPFRTDPDAPFVqaviESAKEVYGQD---PIVLPNSAGTG 379
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 479375213 415 PiVGDFNTFLGMESLLVGFGLEDDRIHSPNEKYELNSFHKG 455
Cdd:cd05681 380 P-MYPFYDALEVPVVAIGVGNAGSNAHAPNENIRIADYYKG 419
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
7-468 |
2.31e-98 |
|
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: 300.65 E-value: 2.31e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 7 DKVLNHLDANLNKSLDRLFNLLRIKSIStdpaykADCRKAAEWLVEDLNSIGFDASVRDT-PGHPMVVAHHEGaTADAPH 85
Cdd:COG0624 1 AAVLAAIDAHLDEALELLRELVRIPSVS------GEEAAAAELLAELLEALGFEVERLEVpPGRPNLVARRPG-DGGGPT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 86 VLFYGHYDVQPVDPLSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEG 165
Cdd:COG0624 74 LLLYGHLDVVPPGDLELWTSDPFEPTIED-------GR--LYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 166 EEESGSPSLKPFLEANRQELKADVALVCDTAMWdaetPAISVGLRGLVGEEIVIKAADRdlHSGFFgGAAANPIHILTKI 245
Cdd:COG0624 145 DEEVGSPGARALVEELAEGLKADAAIVGEPTGV----PTIVTGHKGSLRFELTVRGKAA--HSSRP-ELGVNAIEALARA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 246 LADLHDetgritipdfyegveetptqilksWESLGRTAESFlgpiglsipagekgrsvleltwARPTAEVNGIIGGYTGe 325
Cdd:COG0624 218 LAALRD------------------------LEFDGRADPLF----------------------GRTTLNVTGIEGGTAV- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 326 gfkTVIAAEASAKVSFRLVHKQDPVKIREAFRAFVKERVPaDCSVEFHP-HGGSPAIQLPYDSPLVSKAKNALSDEWPKP 404
Cdd:COG0624 251 ---NVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAP-GVEVEVEVlGDGRPPFETPPDSPLVAAARAAIREVTGKE 326
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 479375213 405 AVLIAMGGSIPIVGdFNTFLGMESLLVGFGlEDDRIHSPNEKYELNSFHKGQRSWARILAAIAA 468
Cdd:COG0624 327 PVLSGVGGGTDARF-FAEALGIPTVVFGPG-DGAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
1-468 |
1.38e-95 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 295.66 E-value: 1.38e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 1 MSTLSLDKVLNHLDANLNKSLDRLFNLLRIKSISTDPAYKADCRKAAEWLVEDLNSIGF-DASVRDTPGHPMVVAHHEGA 79
Cdd:PRK07907 1 MTILTADDLRARVAELLPRVRADLEELVRIPSVAADPFRREEVARSAEWVADLLREAGFdDVRVVSADGAPAVIGTRPAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 80 tADAPHVLFYGHYDVQPVDPLSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAykaVNGSLPVKV 159
Cdd:PRK07907 81 -PGAPTVLLYAHHDVQPPGDPDAWDSPPFELTERD-------GR--LYGRGAADDKGGIAMHLAALRA---LGGDLPVGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 160 TLLFEGEEESGSPSLKPFLEANRQELKADVALVCDTAMWDAETPAISVGLRGLVGEEIVIKAADRDLHSGFFGGAAANPI 239
Cdd:PRK07907 148 TVFVEGEEEMGSPSLERLLAEHPDLLAADVIVIADSGNWSVGVPALTTSLRGNADVVVTVRTLEHAVHSGQFGGAAPDAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 240 HILTKILADLHDETGRITIpdfyEGVEETPTqilksWESLGRTAESFLGPIGLSIPAGEKGR-SVLELTWARPTAEVNGI 318
Cdd:PRK07907 228 TALVRLLATLHDEDGNVAV----DGLDATEP-----WLGVDYDEERFRADAGVLDGVELIGTgSVADRLWAKPAITVIGI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 319 IGGYTGEGFKTVIaAEASAKVSFRLVHKQDPVKIREAFRAFVKERVPADCSVEFHPHGGSPAIQLPYDSPLVSKAKNALS 398
Cdd:PRK07907 299 DAPPVAGASNALP-PSARARLSLRVAPGQDAAEAQDALVAHLEAHAPWGAHVTVERGDAGQPFAADASGPAYDAARAAMR 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 479375213 399 DEWPKPAVLIAMGGSIPIVGDF-NTFLGMESLLvgFGLED--DRIHSPNEKYELNSFHKGQRSWARILAAIAA 468
Cdd:PRK07907 378 EAWGKDPVDMGMGGSIPFIAELqEAFPQAEILV--TGVEDpkTRAHSPNESVHLGELERAAVAEALLLARLAA 448
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
19-455 |
2.72e-79 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 253.14 E-value: 2.72e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 19 KSLDRLFNLLRIKSIStdpAYKADCRKAAEWLVEDLNSIGFDASVRDTPGHPMVVAH-HEGATADaphVLFYGHYDVQPV 97
Cdd:PRK06446 3 EELYTLIEFLKKPSIS---ATGEGIEETANYLKDTMEKLGIKANIERTKGHPVVYGEiNVGAKKT---LLIYNHYDVQPV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 98 DPLSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMT----FVEACRAYKavngsLPVKVTLLFEGEEESGSPS 173
Cdd:PRK06446 77 DPLSEWKRDPFSATIEN-------GR--IYARGASDNKGTLMArlfaIKHLIDKHK-----LNVNVKFLYEGEEEIGSPN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 174 LKPFLEANRQELKADVALVCDTAMWDAETPAISVGLRGLVGEEIVIKAADRDLHSGFfGGAAANPIHILTKILADLHDET 253
Cdd:PRK06446 143 LEDFIEKNKNKLKADSVIMEGAGLDPKGRPQIVLGVKGLLYVELVLRTGTKDLHSSN-APIVRNPAWDLVKLLSTLVDGE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 254 GRITIPDFYEGVEETPTQILKSWESLGRTAESFLGPIGLSIPAGEKGRSVLELTWARPTAEVNGIIGGYTGEGFKTVIAA 333
Cdd:PRK06446 222 GRVLIPGFYDDVRELTEEERELLKKYDIDVEELRKALGFKELKYSDREKIAEALLTEPTCNIDGFYSGYTGKGSKTIVPS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 334 EASAKVSFRLVHKQDPVKIreaFRAFVKERVPADCSVEFHPHGGSPAIQLPYDSP----LVSKAKNALSDEwpkPAVLIA 409
Cdd:PRK06446 302 RAFAKLDFRLVPNQDPYKI---FELLKKHLQKVGFNGEIIVHGFEYPVRTSVNSKvvkaMIESAKRVYGTE---PVVIPN 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 479375213 410 MGGSIPIvGDFNTFLGMESLLVGFGLED--DRIHSPNEKYELNSFHKG 455
Cdd:PRK06446 376 SAGTQPM-GLFVYKLGIRDIVSAIGVGGyySNAHAPNENIRIDDYYKA 422
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
9-455 |
7.82e-77 |
|
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: 247.52 E-value: 7.82e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 9 VLNHLDANLNKSLDRLFNLLRIKSISTDPAYKADCRKAAEWLVEDLNSIGFDASVRDTPGHPMvvahHEGATADAPHVLF 88
Cdd:cd05676 1 VFKYIDEHQDEFIERLREAVAIQSVSADPEKRPELIRMMEWAAERLEKLGFKVELVDIGTQTL----PDGEELPLPPVLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 89 --------------YGHYDVQPVDPLSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGS 154
Cdd:cd05676 77 grlgsdpskktvliYGHLDVQPAKLEDGWDTDPFELTEKD-------GK--LYGRGSTDDKGPVLGWLNAIEAYQKLGQE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 155 LPVKVTLLFEGEEESGSPSLKPFLEANRQELKADVALVC--DTAMWDAETPAISVGLRGLVGEEIVIKAADRDLHSGFFG 232
Cdd:cd05676 148 LPVNLKFCFEGMEESGSEGLDELIEARKDTFFSDVDYVCisDNYWLGKKKPCLTYGLRGICYFFIEVEGPNKDLHSGVFG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 233 GAAANPIHILTKILADLHDETGRITIPDFYEGVEETPTQILKSWESLGRTAESFLGPIGLSIPAGEKGRSVLELTWARPT 312
Cdd:cd05676 228 GSVHEPMTDLIALMSSLVDSDGKILIPGIYDAVAPLTEEEWELYEKIDFDMEEYREDIGVRRLLYDNKEELLMHRWRYPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 313 AEVNGIIGGYTGEGFKTVIAAEASAKVSFRLVHKQDPVKIREAFRAFVKE-----RVPADCSVEFhPHGGSPAIQlPYDS 387
Cdd:cd05676 308 LSIHGIEGAFSGPGAKTVIPAKVIGKFSIRLVPNMDPEVVEKQVTDYLEKvfaelKSPNKLKVYM-GHGGKPWVA-DPDH 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 479375213 388 PLVSKAKNALSDEWPKPAVLIAMGGSIPIVGDFNTFLGMESLLVGFGLEDDRIHSPNEKYELNSFHKG 455
Cdd:cd05676 386 PNYKAARKATKRVFGVEPDLTREGGSIPITLTFQEATGKNVMLLPIGAADDGAHSQNEKINRRNYIEG 453
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
20-463 |
3.94e-63 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 211.96 E-value: 3.94e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 20 SLDRLFNLLRIKSISTDPAykaDCRKAAEWLVEDLNSIGFDASVRDTPGHPMVVAHHEGATADaPHVLFYGHYDVQPVDP 99
Cdd:cd05678 1 SYREHRELVSIPNDATDEE---EMRKNVDWLEQAFRKRGFKTSQLPTSGLPLLLAEKPISDAR-KTVLFYMHLDGQPVDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 100 LSLWENDPFDPAIKDVGDASNggRKILT---------------GRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFE 164
Cdd:cd05678 77 SKWDQKSPYTPVLKRKDAAGN--WEEINwdaifsnldpewrvfARAAADDKGPIMMMLAALDALKAGGIAPKFNVKIILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 165 GEEESGSPSLKPFLEANRQELKADVALVCDTAMWDAETPAISVGLRGLVGEEIVIKAADRDLHSGFFGGAAANPIHILTK 244
Cdd:cd05678 155 SEEEKGSPSLPKAVKEYKELLAADALIIMDGPAHATNKPTLTFGCRGIATATLTTYGAKVPQHSGHYGNYAPNPAFRLSS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 245 ILADLHDETGRITIPDFYEGV---EETpTQILKS----WESLGRTaesflgpigLSIPAGEK-GRSVLElTWARPTAEVN 316
Cdd:cd05678 235 LLASMKDDTGKVTIPGFYDGIsidEET-QKILAAvpddEESINKR---------LGIAQTDKvGRNYQE-ALQYPSLNVR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 317 GIIGGYTGEGFKTVIAAEASAKVSFRLVHKQDPVKIREAFRA-------FVKERVPADCS-------VEFHPHGGSPAIQ 382
Cdd:cd05678 304 GMESGWKGDKVRTIIPEIAEAEIDIRLVPESDGPYLLDLVKAhiekqgyFVTDRAPTDEErlahdkiAKFTYRNGADAFR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 383 LPYDSPLVSKAKNALSDEW-PKPAVLIAMGGSIPIVGDFNTfLGMESLLVGFGLEDDRIHSPNEKYELNSFHKGQRSWAR 461
Cdd:cd05678 384 TDINSPIGNWLRKALTDEFgEEPIQIRMMGGTVPIAPFVNV-LDIPAIIVPMVNMDNNQHSPNENLRIGNIRTGIRTCYA 462
|
..
gi 479375213 462 IL 463
Cdd:cd05678 463 IL 464
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
21-457 |
1.70e-57 |
|
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex.
Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 196.03 E-value: 1.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 21 LDRLFNLLRIKSISTDP--AYKADCRKAAEWLVEDLNSIGFDASVRDTP---GHPMVVAHHEGATADAP--HVLFYGHYD 93
Cdd:cd05677 2 LNTLSEFIAFQTVSQSPttENAEDSRRCAIFLRQLFKKLGATNCLLLPSgpgTNPIVLATFSGNSSDAKrkRILFYGHYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 94 VQPVDPLSLWENDPFDPAikdvgdASNGgrkILTGRGTSDDKGQLMTFVEACrAYKAVNGSLPVKVTLLFEGEEESGSPS 173
Cdd:cd05677 82 VIPAGETDGWDTDPFTLT------CENG---YLYGRGVSDNKGPLLAAIYAV-AELFQEGELDNDVVFLIEGEEESGSPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 174 LKPFLEANRQELKA-DVALVCDTAMWDAETPAISVGLRGLVGEEIVIKAADRDLHSGFFGGAAANPIHILTKILADLHDE 252
Cdd:cd05677 152 FKEVLRKNKELIGDiDWILLSNSYWLDDNIPCLNYGLRGVIHATIVVSSDKPDLHSGVDGGVLREPTADLIKLLSKLQDP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 253 TGRITIPDFYEGVEETPTQILKSWESLGRTAEsflgpiglsIPAGEKGRSVLELtWARPTAEVNGIigGYTGEGFKTVIA 332
Cdd:cd05677 232 DGRILIPHFYDPVKPLTEAERARFTAIAETAL---------IHEDTTVDSLIAK-WRKPSLTVHTV--KVSGPGNTTVIP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 333 AEASAKVSFRLVHKQDPVKIREAFRAFVKE-----RVPADCSVE-FH---PHGGSPaiqlpyDSPLVSKAKNALSDEWPK 403
Cdd:cd05677 300 KSASASVSIRLVPDQDLDVIKQDLTDYIQScfaelKSQNHLDIEvLNeaePWLGDP------DNPAYQILREAVTAAWGV 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 479375213 404 PAVLIAMGGSIPIVGDFNTFLGMESLLVGFGLEDDRIHSPNEKYELNSFHKGQR 457
Cdd:cd05677 374 EPLYIREGGSIPTIRFLEKEFNAPAVQLPCGQSSDNAHLDNERLRIKNLYKMRE 427
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
87-465 |
1.63e-45 |
|
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: 160.98 E-value: 1.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 87 LFYGHYDVQPVDPLSLWendPFDPAIKDVgdasnggrkiLTGRGTSDDKGQLMTFVEACRAYKAvNGSLPVKVTLLFEGE 166
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTEDGK----------LYGRGHDDMKGGLLAALEALRALKE-EGLKKGTVKLLFQPD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 167 EESGSPSLKPFLEANRQE---LKADVAL-VCDTAMWDAE-TPAISVGLRGLVGEEIVIKAADRdlHSGFFgGAAANPIHI 241
Cdd:pfam01546 67 EEGGMGGARALIEDGLLErekVDAVFGLhIGEPTLLEGGiAIGVVTGHRGSLRFRVTVKGKGG--HASTP-HLGVNAIVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 242 LTKILADLHDETGRITIPDFYEGVeetptqilksweSLGRtaesflgpiglsipagekgrsvleltwarptaeVNGIIGG 321
Cdd:pfam01546 144 AARLILALQDIVSRNVDPLDPAVV------------TVGN---------------------------------ITGIPGG 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 322 YtgegfkTVIAAEASAKVSFRLVHKQDPVKIREAFRAFVKERVPA-DCSVEFHPHGGSPAIQLPyDSPLVSKAKNALSDE 400
Cdd:pfam01546 179 V------NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAyGVKVEVEYVEGGAPPLVN-DSPLVAALREAAKEL 251
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 479375213 401 WPKPAVLIAMGgsIPIVGDFNTFL-GMESLLVGFGLEDDRIHSPNEKYELNSFHKGQRSWARILAA 465
Cdd:pfam01546 252 FGLKVELIVSG--SMGGTDAAFFLlGVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
54-445 |
2.22e-39 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 148.14 E-value: 2.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 54 LNSIGFDASVRDTP---GHPMVVAH-HEGAtaDAPHVLFYGHYDVQPVDPlSLWEnDPFDP-AIKDVGDAsnggrkiLTG 128
Cdd:PRK07079 54 LAALGFTCRIVDNPvagGGPFLIAErIEDD--ALPTVLIYGHGDVVRGYD-EQWR-EGLSPwTLTEEGDR-------WYG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 129 RGTSDDKGQLMTFVEACRA-YKAVNGSLPVKVTLLFEGEEESGSPSLKPFLEANRQELKADVALVCDTAMWDAETPAISV 207
Cdd:PRK07079 123 RGTADNKGQHTINLAALEQvLAARGGRLGFNVKLLIEMGEEIGSPGLAEVCRQHREALAADVLIASDGPRLSAERPTLFL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 208 GLRGLVGEEIVIKAADRDLHSGFFGGAAANPIHILTKILADLHDETGRITIPDFyegveeTPTQILKSWESLGRTAESFL 287
Cdd:PRK07079 203 GSRGAVNFRLRVNLRDGAHHSGNWGGLLRNPGTVLAHAIASLVDARGRIQVPGL------RPPPLPAAVRAALADITVGG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 288 GPIGLSIPA--GEKGRSVLELTWARPTAEVNGIIggyTGEGFKTV--IAAEASAKVSFRLVHKQDPVKIREAFRAFVKER 363
Cdd:PRK07079 277 GPGDPAIDPdwGEPGLTPAERVFGWNTLEVLAFK---TGNPDAPVnaIPGSARAVCQLRFVVGTDWENLAPHLRAHLDAH 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 364 VPADcsVEFHPHGGSPAIQLPYDSPLVSKAKNALSDEWPK-PAVLIAMGGSIPivGD-FNTFLGMESLLVGFGLEDDRIH 441
Cdd:PRK07079 354 GFPM--VEVTVERGSPATRLDPDDPWVRWALASIARTTGKkPALLPNLGGSLP--NDvFADILGLPTLWVPHSYPACSQH 429
|
....
gi 479375213 442 SPNE 445
Cdd:PRK07079 430 APNE 433
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
30-445 |
1.48e-35 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 137.25 E-value: 1.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 30 IKSISTDPAYKADCRKAAEWLVE-DLNSIGFDASVRDTP---GHPMVVA-HHEGATAdaPHVLFYGHYDVQP------VD 98
Cdd:cd05679 16 VPTESQEPARKPELRAYLDQEMRpRFERLGFTVHIHDNPvagRAPFLIAeRIEDPSL--PTLLIYGHGDVVPgyegrwRD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 99 PLSLWEndpfdpaIKDVGDAsnggrkiLTGRGTSDDKGQLMTFVEACRA-YKAVNGSLPVKVTLLFEGEEESGSPSLKPF 177
Cdd:cd05679 94 GRDPWT-------VTVWGER-------WYGRGTADNKGQHSINMAALRQvLEARGGKLGFNVKFLIEMGEEMGSPGLRAF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 178 LEANRQELKADVALVCDTAMWDAETPAISVGLRGLVGEEIVIKAADRDLHSGFFGGAAANPIHILTKILADLHDETGRIT 257
Cdd:cd05679 160 CFSHREALKADLFIASDGPRLAADRPTMFLGSRGGLNFELRVNLREGGHHSGNWGGLLANPGIILANAIASLVDGKGRIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 258 IPDFyegveeTPTQILKSWESLGRTAESFLGPIGLSIPA--GEKGRSVLELTWARPTAEVNGIIGGyTGEGFKTVIAAEA 335
Cdd:cd05679 240 LPAL------KPAHLPNSVRSALADVEVGGGPDDPSIDPwwGEPGLTAAERVFGWNTLEVLAFKTG-NPDAPVNAIPGHA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 336 SAKVSFRLVHKQDPVKIREAFRA------FVKERVPADCSVeFHphggspAIQLPYDSPLVSKAKNALSDEWPK-PAVLI 408
Cdd:cd05679 313 EAICQIRFVVGTDPDTFIPAVRAhldangFDGVEVTASQMV-FA------ATRLDPDSPWVGWALASLQKTTGKkPALLP 385
|
410 420 430
....*....|....*....|....*....|....*...
gi 479375213 409 AMGGSIPivGD-FNTFLGMESLLVGFGLEDDRIHSPNE 445
Cdd:cd05679 386 NLGGSLP--NDvFSEVLGLPTLWVPHSYPACSQHAPNE 421
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
24-445 |
1.87e-34 |
|
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: 134.00 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 24 LFNLLRI--KSISTDPAYKAD------CRKAAEWlVEDLNSIGFDASVRDTPGH-PMVVAHHEGATADAPHVLFYGHYDV 94
Cdd:cd05682 6 LSDYIRIpnQSPLFDPEWATNgllekaANLIADW-VKAQNIKGAKVEVVELEGRtPLLFVEIPGTEQDDDTVLLYGHMDK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 95 QPvdPLSLWEND--PFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPvKVTLLFEGEEESGSP 172
Cdd:cd05682 85 QP--PFTGWDEGlgPTKPVIRG-------DK--LYGRGGADDGYAIFASLTAIKALQEQGIPHP-RCVVLIEACEESGSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 173 SLKPFLEANRQELKADVALVC-DTAMWDAETPAISVGLRGLVGEEIVIKAADRDLHSGFFGGAAANPIHILTKILADLHD 251
Cdd:cd05682 153 DLPFYLDKLKERIGNVDLVVClDSGCGNYEQLWLTTSLRGVLGGDLTVQVLNEGVHSGDASGIVPSSFRILRQLLSRIED 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 252 E-TGRITIPdfyEGVEETPT----QILKSWESLGRTAESFLGPI-GLSIPAGEKGRSVLELTWaRPTAEVNGIIGGYTGE 325
Cdd:cd05682 233 EnTGEVKLD---EQHCDIPAhryeQAKKIAEILGEAVYEEFPFVsGVQPVTTDLVQLYLNRTW-KPQLSVTGADGLPPAS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 326 GFKTVIAAEASAKVSFRLVHKQDPVKIREAFRAFVKERVPADCSVEFHPHGGSPAIQLPYDSPLVSKAKNALS-DEWPKP 404
Cdd:cd05682 309 TAGNVLRPETTLKLSLRLPPTVDAEKASAALKKLLETDPPYNAKVTFKSDGAGSGWNAPLLSPWLAKALNEASqLFFGKP 388
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 479375213 405 AVLIAMGGSIPIVGDFN-TFLGMESLLVGFGLEDDRIHSPNE 445
Cdd:cd05682 389 AAYQGEGGSIPFMNMLGeKFPKAQFIVTGVLGPKSNAHGPNE 430
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
27-463 |
2.15e-25 |
|
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: 107.00 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 27 LLRIKSIStdpaykADCRKAAEWLVEDLNSIGFDASVRDTPGHPMVVAHHEGAtaDAPHVLFYGHYDVQPVDPLSLWEND 106
Cdd:cd08659 6 LVQIPSVN------PPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVATVGGG--DGPVLLLNGHIDTVPPGDGDKWSFP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 107 PFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESGSPSLKPFLEANRQElK 186
Cdd:cd08659 78 PFSGRIRD-------GR--LYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLEAGYAD-R 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 187 ADVALVCDTAMWDaetpaISVGLRGLVGEEIVI--KAAdrdlHSGfFGGAAANPIHILTKILADLHdetgritipDFYEG 264
Cdd:cd08659 148 LDALIVGEPTGLD-----VVYAHKGSLWLRVTVhgKAA----HSS-MPELGVNAIYALADFLAELR---------TLFEE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 265 VEETPtqilksweslgrtaesFLGPIGLSIpagekgrsvleltwarptaevnGIIGGytgeGFKT-VIAAEASAKVSFRL 343
Cdd:cd08659 209 LPAHP----------------LLGPPTLNV----------------------GVING----GTQVnSIPDEATLRVDIRL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 344 VHKQDPVKIREAFRAFVkERVPADCSVEFhPHGGSPAIQLPYDSPLVSKAKNAlSDEWPKPAVLIAMGGSIpivgD---F 420
Cdd:cd08659 247 VPGETNEGVIARLEAIL-EEHEAKLTVEV-SLDGDPPFFTDPDHPLVQALQAA-ARALGGDPVVRPFTGTT----DasyF 319
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 479375213 421 NTFLGMESLLVGFGlEDDRIHSPNEKYELNSFHKGQRSWARIL 463
Cdd:cd08659 320 AKDLGFPVVVYGPG-DLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
27-463 |
4.90e-22 |
|
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: 98.20 E-value: 4.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 27 LLRIKSiSTDPAYKADCRKAAEWLVEDLNSIGFDASVRDTPGHP---MVVAHHEGATADAPHVLFYGHYDVQPVDPlSLW 103
Cdd:cd05675 7 LIRIDT-TNSGDGTGSETRAAEVLAARLAEAGIQTEIFVVESHPgraNLVARIGGTDPSAGPLLLLGHIDVVPADA-SDW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 104 ENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESGSPSLKPFLEANRQ 183
Cdd:cd05675 85 SVDPFSGEIKD-------GY--VYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDNHP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 184 EL--KADVALvCDTAMWDAETPAISVGLRGLVGEEIVikaADRDLHSGFFGGAAANPiHILTKI--LADLHDETGRITIP 259
Cdd:cd05675 156 ELfdGATFAL-NEGGGGSLPVGKGRRLYPIQVAEKGI---AWMKLTVRGRAGHGSRP-TDDNAItrLAEALRRLGAHNFP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 260 dfyegVEETP-TQILKSWESLGRTAESFL--GPIGLSIPAGEKGRSVLELTWA--RPTAEVNGIIGGYTGegfkTVIAAE 334
Cdd:cd05675 231 -----VRLTDeTAYFAQMAELAGGEGGALmlTAVPVLDPALAKLGPSAPLLNAmlRNTASPTMLDAGYAT----NVLPGR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 335 ASAKVSFRLVhkqdPVKIREAFRAFVKERV-PADCSVEFHPHggSPAIQLPYDSPLVSKAKNALSDEWPK-PAVLIAMGG 412
Cdd:cd05675 302 ATAEVDCRIL----PGQSEEEVLDTLDKLLgDPDVSVEAVHL--EPATESPLDSPLVDAMEAAVQAVDPGaPVVPYMSPG 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 479375213 413 S----------IPIVGDFNTFLGMEsllvgfGLEDDRIHSPNEKYELNSFHKGQRSWARIL 463
Cdd:cd05675 376 GtdakyfrrlgIPGYGFAPLFLPPE------LDYTGLFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
26-249 |
1.05e-18 |
|
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: 87.17 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 26 NLLRIKSISTDpaykaDCrKAAEWLVEDLNSIGFDASVRDTPGHPMVVAHHEGataDAPHVLFYGHYDVQPVDPLSLWEN 105
Cdd:cd03891 6 ELIRRPSVTPD-----DA-GAQDLIAERLKALGFTCERLEFGGVKNLWARRGT---GGPHLCFAGHTDVVPPGDLEGWSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 106 DPFDPAIKDvgdasnggrKILTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEES----GSPSLKPFLEAn 181
Cdd:cd03891 77 DPFSPTIKD---------GMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGpaidGTKKVLEWLKA- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 479375213 182 RQElKADVALV----CDTAMWDaetpAISVGLRGLVGEEIVIKaadrdlhsGFFGGAA-----ANPIHILTKILADL 249
Cdd:cd03891 147 RGE-KIDYCIVgeptSEKKLGD----TIKIGRRGSLNGKLTIK--------GKQGHVAyphlaDNPIHLLAPILAEL 210
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
21-464 |
1.17e-18 |
|
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: 87.26 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 21 LDRLFNLLRIKSISTDPAYKAdcrKAAEWLVEDLNSIGFDASVRDTPGH-PMVVAHHEGAtaDAPHVLFYGHYD-VQPVD 98
Cdd:cd03885 2 LDLLERLVNIESGTYDKEGVD---RVAELLAEELEALGFTVERRPLGEFgDHLIATFKGT--GGKRVLLIGHMDtVFPEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 99 plSLWENdPFdpAIKDvgdasnggrKILTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESGSPSLKPFL 178
Cdd:cd03885 77 --TLAFR-PF--TVDG---------DRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRELI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 179 EanRQELKADVALVCDTAMWDAetpAISVGLRGLVGEEIVIK--AAdrdlHSGffggaaANPihiltkiladlhdETGRI 256
Cdd:cd03885 143 E--EEAKGADYVLVFEPARADG---NLVTARKGIGRFRLTVKgrAA----HAG------NAP-------------EKGRS 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 257 TIpdfyegvEETPTQILKsweslgrtAESFLGPiglsipagEKGrsvLELTWarptaevnGIIGGYTGegfKTVIAAEAS 336
Cdd:cd03885 195 AI-------YELAHQVLA--------LHALTDP--------EKG---TTVNV--------GVISGGTR---VNVVPDHAE 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 337 AKVSFRLVHKQDPVKIREAFRAFVKERVPADCSVEFHPHGGSPAIQLPYDS-PLVSKAKnALSDEWPKPAVLIAMGGsip 415
Cdd:cd03885 238 AQVDVRFATAEEADRVEEALRAIVATTLVPGTSVELTGGLNRPPMEETPASrRLLARAQ-EIAAELGLTLDWEATGG--- 313
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 479375213 416 iVGDFNtFLGMESL--LVGFGLEDDRIHSPNEKYELNSFHKGQRSWARILA 464
Cdd:cd03885 314 -GSDAN-FTAALGVptLDGLGPVGGGAHTEDEYLELDSLVPRIKLLARLLM 362
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
19-470 |
1.85e-16 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 80.80 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 19 KSLDRLFNLLRIKSISTDPAYKADCRkaaEWLVEDLNSIGFDASVRDTP------GHPMVVAHHEGATADAPHVLFYGHY 92
Cdd:PRK08651 7 DIVEFLKDLIKIPTVNPPGENYEEIA---EFLRDTLEELGFSTEIIEVPneyvkkHDGPRPNLIARRGSGNPHLHFNGHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 93 DVqpVDPLSLWEN-DPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACrayKAVNGSLPVKVTLLFEGEEESGS 171
Cdd:PRK08651 84 DV--VPPGEGWSVnVPFEPKVKD-------GK--VYGRGASDMKGGIAALLAAF---ERLDPAGDGNIELAIVPDEETGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 172 PSLKPFLEANRqeLKADVALVcdtamwdAETPA---ISVGLRGLVgeEIVIKAADRDLHSGfFGGAAANPIHILTKILAD 248
Cdd:PRK08651 150 TGTGYLVEEGK--VTPDYVIV-------GEPSGldnICIGHRGLV--WGVVKVYGKQAHAS-TPWLGINAFEAAAKIAER 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 249 LHDETGRITIPDFYEgveetptqilkswESLGRTAESFLGpiGLSIPAGEKgrsvleltwarptaeVNgiiggytgegfk 328
Cdd:PRK08651 218 LKSSLSTIKSKYEYD-------------DERGAKPTVTLG--GPTVEGGTK---------------TN------------ 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 329 tVIAAEASAKVSFRLVHKQDPVKIREAFRAFVKERVPAD-CSVEFHPHGGSPAIQLPYDSPLVSKAKNALSDEW-PKPAV 406
Cdd:PRK08651 256 -IVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELgIEVEFEITPFSEAFVTDPDSELVKALREAIREVLgVEPKK 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 479375213 407 LIAMGGsipivGD--FNTFLGMESLLVGFGlEDDRIHSPNEKYELNSFHKGQRSWARILAAIAAKQ 470
Cdd:PRK08651 335 TISLGG-----TDarFFGAKGIPTVVYGPG-ELELAHAPDEYVEVKDVEKAAKVYEEVLKRLAKGS 394
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
26-249 |
5.95e-15 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 76.28 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 26 NLLRIKSISTDPAykadcrKAAEWLVEDLNSIGFDAsvrdtpgHPMVV-------AHHEGataDAPHVLFYGHYDVQPVD 98
Cdd:PRK13009 10 DLIRRPSVTPDDA------GCQDLLAERLEALGFTC-------ERMDFgdvknlwARRGT---EGPHLCFAGHTDVVPPG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 99 PLSLWENDPFDPAIKDvgdasnggrKILTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEES----GSPSL 174
Cdd:PRK13009 74 DLEAWTSPPFEPTIRD---------GMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGpainGTVKV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 175 KPFLEAnRQElKADVALV----CDTAMWDaetpAISVGLRGLVGEEIVIK-----AADRDLhsgffggaAANPIHILTKI 245
Cdd:PRK13009 145 LEWLKA-RGE-KIDYCIVgeptSTERLGD----VIKNGRRGSLTGKLTVKgvqghVAYPHL--------ADNPIHLAAPA 210
|
....
gi 479375213 246 LADL 249
Cdd:PRK13009 211 LAEL 214
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
24-445 |
1.68e-14 |
|
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: 75.11 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 24 LFNLLRIKSISTDPAYKADC------RKAAEWLVEDLNSIGFDasVRDTPGHpmvVAHHE-GATADAPHVLfyGHYDVQP 96
Cdd:TIGR01887 8 LKELIAIDSVEDLEKAKEGApfgegpRKALDKFLEIAKRDGFT--TENVDNY---AGYIEyGQGEEVLGIL--GHLDVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 97 VDplSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESGSPSLKP 176
Cdd:TIGR01887 81 AG--DGWTSPPFEPTIKD-------GR--IYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEESGWKCIDY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 177 FLEanrQELKADVALVCdtamwDAETPAIsVGLRGLVGEEIVIK---AADRDLHSgFFGGAAAN--PIHILTKILADLHD 251
Cdd:TIGR01887 150 YFE---HEEMPDIGFTP-----DAEFPII-YGEKGITTLEIKFKddtEGDVVLES-FKAGEAYNmvPDHATAVISGKKLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 252 EtgriTIPDFYEGVEETPTQIlkSWESLGRTAESFLgpIGLSIPAG--EKG-RSVLELTWARPTAEVNG----------- 317
Cdd:TIGR01887 220 E----VEQLKFVFFIAKELEG--DFEVNDGTLTITL--EGKSAHGSapEKGiNAATYLALFLAQLNLAGgakaflqflae 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 318 -IIGGYTGEGFKTVIAAEASAKVSFRL----VHKQDPVKIREAFR---------AFVKERVPADCSVEFHPHGGSPAIQL 383
Cdd:TIGR01887 292 yLHEDHYGEKLGIKFHDDVSGDLTMNVgvidYENAEAGLIGLNVRypvgndpdtMLKNELAKESGVVEVTLNGYLKPLYV 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 479375213 384 PYDSPLVSKAKNALSDEWPKPAVLIAMGGsipivGDFNTFlgMESlLVGFGL----EDDRIHSPNE 445
Cdd:TIGR01887 372 PKDDPLVQTLMKVYEKQTGDEGEPVAIGG-----GTYARL--MPN-GVAFGAlfpgEEDTMHQANE 429
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
6-195 |
6.31e-14 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 73.53 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 6 LDKVLNHLDANLNKSLDRLFNLLRIKSISTdPAYKADcrKAAEWLVEDLNSIGFDASVRDT-PGHPMVVAHHEGATADAP 84
Cdd:PRK08596 1 VSQLLEQIELRKDELLELLKTLVRFETPAP-PARNTN--EAQEFIAEFLRKLGFSVDKWDVyPNDPNVVGVKKGTESDAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 85 HVLFY-GHYDVQPVDPLSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKvtLLF 163
Cdd:PRK08596 78 KSLIInGHMDVAEVSADEAWETNPFEPTIKD-------GW--LYGRGAADMKGGLAGALFAIQLLHEAGIELPGD--LIF 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 479375213 164 E---GEE--ESGSpslkpfLEANRQELKADVALVCDT 195
Cdd:PRK08596 147 QsviGEEvgEAGT------LQCCERGYDADFAVVVDT 177
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
78-265 |
8.78e-14 |
|
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: 69.77 E-value: 8.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 78 GATADAPHVLFYGHYDVQPVDPLSLWENDPFDPAIKDvgdasnggrKILTGRGTSDDKGQLMTFVEACRAYKAVNGSLPV 157
Cdd:cd18669 7 GGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEE---------GRLYGRGALDDKGGVAAALEALKLLKENGFKLKG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 158 KVTLLFEGEEESGSP----SLKPFLEANrqELKADVALVCDTAMWDAETPAISVGLR---GLVGEEIVIKAADRDLHSGF 230
Cdd:cd18669 78 TVVVAFTPDEEVGSGagkgLLSKDALEE--DLKVDYLFVGDATPAPQKGVGIRTPLVdalSEAARKVFGKPQHAEGTGGG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 479375213 231 FGGAAANPIHI-----LTKILADLHDETGRITIPDFYEGV 265
Cdd:cd18669 156 TDGRYLQELGIpgvtlGAGGGKGAHSPNERVNLEDLESAL 195
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
207-368 |
2.88e-13 |
|
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: 65.83 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 207 VGLRGLVGEEIVIKaaDRDLHSGFfGGAAANPIHILTKILADLHDETGRITipdfyegveetptqilksweslgrtaesf 286
Cdd:pfam07687 1 IGHKGLAGGHLTVK--GKAGHSGA-PGKGVNAIKLLARLLAELPAEYGDIG----------------------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 287 lgpiglsipagekgrsvleLTWARPTAEVNGIIGGYtgegFKTVIAAEASAKVSFRLVHKQDPVKIREAFRAFVKERVPA 366
Cdd:pfam07687 49 -------------------FDFPRTTLNITGIEGGT----ATNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEKELPE 105
|
..
gi 479375213 367 DC 368
Cdd:pfam07687 106 GE 107
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
44-263 |
3.05e-13 |
|
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: 70.88 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 44 RKAAEWLVEDLNSIGFDASVRDTP-GHPMVVAHHEGATAdAPHVLFYGHYDVQPVDPLSLWENDPFDPAIKDvgdasngG 122
Cdd:cd08011 21 SAIAAYIKLLLEDLGYPVELHEPPeEIYGVVSNIVGGRK-GKRLLFNGHYDVVPAGDGEGWTVDPYSGKIKD-------G 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 123 RkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEES-GSPSLKPFLEANRqeLKADVALVCDtamwDAE 201
Cdd:cd08011 93 K--LYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETgGRAGTKYLLEKVR--IKPNDVLIGE----PSG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 479375213 202 TPAISVGLRGLVgeEIVIKAADRDLHSGFFgGAAANPIHILTKILADLHDE-----TGRI-------TIPDFYE 263
Cdd:cd08011 165 SDNIRIGEKGLV--WVIIEITGKPAHGSLP-HRGESAVKAAMKLIERLYELektvnPGVIkggvkvnLVPDYCE 235
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
26-445 |
4.11e-13 |
|
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: 71.12 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 26 NLLRIKSISTDPAYKA----DCRKAAEWLVEDLNSIGFDasVRDTPGHpmvVAHHE-GATADAPHVLfyGHYDVQPvdPL 100
Cdd:cd03888 16 ELVAIPSVRDEATEGApfgeGPRKALDKFLDLAKRLGFK--TKNIDNY---AGYAEyGEGEEVLGIL--GHLDVVP--AG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 101 SLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESGSPSLKPFLEA 180
Cdd:cd03888 87 EGWTTDPFKPVIKD-------GK--LYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGWKCIEHYFEH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 181 NRQelkADVALVCdtamwDAETPAISvGLRGLVGEEIVIKAADRDLHS--GFFGGAAAN--PIHILTKILADLHDETGRI 256
Cdd:cd03888 158 EEY---PDFGFTP-----DAEFPVIN-GEKGIVTVDLTFKIDDDKGYRliSIKGGEATNmvPDKAEAVIPGKDKEELALS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 257 TIPDFYEGVEETPTQIL---------KSWESLGRTAESFLGPIGLSIPAGEKGRSVLELtwarpTAEVNGiiGGYTGEGF 327
Cdd:cd03888 229 AATDLKGNIEIDDGGVEltvtgksahASAPEKGVNAITLLAKFLAELNKDGNDKDFIKF-----LAKNLH--EDYNGKKL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 328 KTVIAAEASAKVS-----FRLVHKQD--------PVKIR-EAFRAFVKERVPADcSVEFHPHGGSPAIQLPYDSPLVSKA 393
Cdd:cd03888 302 GINFEDEVMGELTlnpgiITLDDGKLelglnvryPVGTSaEDIIKQIEEALEKY-GVEVEGHKHQKPLYVPKDSPLVKTL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 479375213 394 KNALSDEWPKPAVLIAMGGsipivGDFNTFlgMESlLVGFGLE----DDRIHSPNE 445
Cdd:cd03888 381 LKVYEEQTGKEGEPVAIGG-----GTYARE--LPN-GVAFGPEfpgqKDTMHQANE 428
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
27-170 |
1.47e-12 |
|
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: 68.97 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 27 LLRIKSIS-TDPAYKadcrKAAEWLVEDLNSIGFDASVRDTPG-----HPMVVAHHEGaTADAPHVLFYGHYDVQPVDPL 100
Cdd:TIGR01910 7 LISIPSVNpPGGNEE----TIANYIKDLLREFGFSTDVIEITDdrlkvLGKVVVKEPG-NGNEKSLIFNGHYDVVPAGDL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 101 SLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESG 170
Cdd:TIGR01910 82 ELWKTDPFKPVEKD-------GK--LYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESG 142
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
78-265 |
3.08e-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: 65.52 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 78 GATADAPHVLFYGHYDVQPVDPLSLWENDPFDPAIKDvgdasngGRKIltGRGTSDDKGQLMTFVEACRAYKAVNGSLPV 157
Cdd:cd03873 7 GGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEE-------GRLY--GRGALDDKGGVAAALEALKRLKENGFKPKG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 158 KVTLLFEGEEESGSPSLK----PFLEANrqELKADVALVCDTAMWDAETPAisVGLRGLVGEEIVIKAADRDLH----SG 229
Cdd:cd03873 78 TIVVAFTADEEVGSGGGKgllsKFLLAE--DLKVDAAFVIDATAGPILQKG--VVIRNPLVDALRKAAREVGGKpqraSV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 479375213 230 FFGGAAANPIH--------ILTKILADLHDETGRITIPDFYEGV 265
Cdd:cd03873 154 IGGGTDGRLFAelgipgvtLGPPGDKGAHSPNEFLNLDDLEKAT 197
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
9-251 |
4.98e-12 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 67.66 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 9 VLNHLDANLNKSLDRLFNLLRIKSISTDPAYKADcrkAAEWlvedlnsIGFDASVRDTpgHPMV--------VAHH---- 76
Cdd:PRK08262 35 AVAPVAVDEDAAAERLSEAIRFRTISNRDRAEDD---AAAF-------DALHAHLEES--YPAVhaalerevVGGHslly 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 77 --EGATADAPHVLFYGHYDVQPVDPLSL--WENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRaYKAVN 152
Cdd:PRK08262 103 twKGSDPSLKPIVLMAHQDVVPVAPGTEgdWTHPPFSGVIAD-------GY--VWGRGALDDKGSLVAILEAAE-ALLAQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 153 GSLPVK-VTLLFEGEEE---SGSPSLKPFLEANRQELkadvALVCDtamwdaETPAISVGLRGLVGEEI-VIKAADRdlh 227
Cdd:PRK08262 173 GFQPRRtIYLAFGHDEEvggLGARAIAELLKERGVRL----AFVLD------EGGAITEGVLPGVKKPVaLIGVAEK--- 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 479375213 228 sGFF---------GGAAANP-----IHILTKILADLHD 251
Cdd:PRK08262 240 -GYAtleltaratGGHSSMPprqtaIGRLARALTRLED 276
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
18-170 |
6.51e-12 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 66.91 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 18 NKSLDRLFNLLRIKSISTDPAYKAdcrkAAEWLVEDLNSIGFDA-SVRDTPGHPMVVAHHEGATADAPHVLFYGHYDVQP 96
Cdd:cd05646 2 DPAVTRFREYLRINTVHPNPDYDA----CVEFLKRQADELGLPVrVIEVVPGKPVVVLTWEGSNPELPSILLNSHTDVVP 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 479375213 97 VDPLSlWENDPFDpAIKDvgdasNGGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESG 170
Cdd:cd05646 78 VFEEK-WTHDPFS-AHKD-----EDGN--IYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIG 142
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
28-197 |
2.23e-11 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 65.20 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 28 LRIKSISTDPAYKAdcrkAAEWLVEDLNSIGFDASVRDT-PGHPMVVAHHEGATADAPHVLFYGHYDVQPVDPlSLWEND 106
Cdd:TIGR01880 19 LRINTVQPNPDYAA----CVDFLIKQADELGLARKTIEFvPGKPVVVLTWPGSNPELPSILLNSHTDVVPVFR-EHWTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 107 PFDPAIKDVGDasnggrkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEE-SGSPSLKPFleANRQEL 185
Cdd:TIGR01880 94 PFSAFKDEDGN--------IYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEiGGHDGMEKF--AKTDEF 163
|
170
....*....|...
gi 479375213 186 KA-DVALVCDTAM 197
Cdd:TIGR01880 164 KAlNLGFALDEGL 176
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
58-195 |
3.73e-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: 64.64 E-value: 3.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 58 GFDASVRDTPGHPMVVAHHEGATADAPHVLFYGHYDVQPVDPLSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQ 137
Cdd:cd03895 49 GFSPVAVDYAGAPNVVGTHRPRGETGRSLILNGHIDVVPEGPVELWTRPPFEATIVD-------GW--MYGRGAGDMKAG 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 479375213 138 LMTFVEACRAYKAVNGSLPVKVtlLFE---GEEESGSPSLKPFLEANRqelkADVALVCDT 195
Cdd:cd03895 120 LAANLFALDALRAAGLQPAADV--HFQsvvEEECTGNGALAALMRGYR----ADAALIPEP 174
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
26-206 |
4.06e-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 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: 64.40 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 26 NLLRIKSIStdPAYKADCRKA-AEWLVEDLNSIGF----DASVRDTPG--HPMVVAHHEGATADAPHVLfyGHYDVQPVD 98
Cdd:cd05650 9 DLIRIPAVN--PESGGEGEKEkADYLEKKLREYGFytleRYDAPDERGiiRPNIVAKIPGGNDKTLWII--SHLDTVPPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 99 PLSLWENDPFDPAIKDvgdasnggrKILTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESGSP-SLKPF 177
Cdd:cd05650 85 DLSLWETDPWEPVVKD---------GKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEyGIQYL 155
|
170 180
....*....|....*....|....*....
gi 479375213 178 LEANRQELKADVALVCDTAMWDAETPAIS 206
Cdd:cd05650 156 LNKFDLFKKDDLIIVPDFGTEDGEFIEIA 184
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
44-402 |
5.51e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 64.10 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 44 RKAAEWLVEDLNSIGFDAS-VRDTPGHPMVVAHHEGATADAPHVLFYGHYDVQPVDPlSLWENDPFDPAIKDvgdasngg 122
Cdd:PRK07906 25 REAAEYVAEKLAEVGLEPTyLESAPGRANVVARLPGADPSRPALLVHGHLDVVPAEA-ADWSVHPFSGEIRD-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 123 rKILTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESGSPSLKPFLEANRQELKADValvcdtamwdaeT 202
Cdd:PRK07906 96 -GYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEAGGTYGAHWLVDNHPELFEGV------------T 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 203 PAIS-VGlrGL---VGEEI---VIKAADRDLH------SGFFG---------------------GAAANPIHiLTKILAD 248
Cdd:PRK07906 163 EAISeVG--GFsltVPGRDrlyLIETAEKGLAwmrltaRGRAGhgsmvnddnavtrlaeavariGRHRWPLV-LTPTVRA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 249 LHDETGRITipdfyeGVEETPTQILKSWESLGrTAESFLGPiglsipagekgrsVLeltwaRPTAEVNGIIGGYtgegfK 328
Cdd:PRK07906 240 FLDGVAELT------GLEFDPDDPDALLAKLG-PAARMVGA-------------TL-----RNTANPTMLKAGY-----K 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 479375213 329 T-VIAAEASAKVSFRLVHKQdpvkiREAFRAFVKERVPADCSVEFHPHggSPAIQLPYDSPLVSKAKNALSDEWP 402
Cdd:PRK07906 290 VnVIPGTAEAVVDGRFLPGR-----EEEFLATVDELLGPDVEREWVHR--DPALETPFDGPLVDAMNAALLAEDP 357
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
42-191 |
2.32e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 62.33 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 42 DCRKAAEWLVEDLNSIGF-DASVRDTPGHPM---VVAHHEGATADAPhVLFYGHYDVqpVDPL-SLWENDPFDPAIKdvg 116
Cdd:PRK09133 57 STTPAAEAMAARLKAAGFaDADIEVTGPYPRkgnLVARLRGTDPKKP-ILLLAHMDV--VEAKrEDWTRDPFKLVEE--- 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 479375213 117 dasNGgrkILTGRGTSDDKGQLMTFVEACRAYKAvNGSLPVK-VTLLFEGEEESGSPSLKPFLEANRQEL-KADVAL 191
Cdd:PRK09133 131 ---NG---YFYGRGTSDDKADAAIWVATLIRLKR-EGFKPKRdIILALTGDEEGTPMNGVAWLAENHRDLiDAEFAL 200
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
47-399 |
4.23e-10 |
|
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: 61.07 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 47 AEWLVEDLNSIGFDASV--RDTPGHPMVVAHHEGAtaDAPHVLFYGHYDVQPVDPlSLWENDPFDPAIKDvgdasngGRk 124
Cdd:cd03894 21 IEYVADYLAALGVKSRRvpVPEGGKANLLATLGPG--GEGGLLLSGHTDVVPVDG-QKWSSDPFTLTERD-------GR- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 125 iLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKvtLLFEGEEESGSPSLKPFLEANR-QELKADVALVCD-TAMwdaet 202
Cdd:cd03894 90 -LYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLH--LAFSYDEEVGCLGVRHLIAALAaRGGRPDAAIVGEpTSL----- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 203 pAISVGLRGLVGEEIVI--KAAdrdlHSGfFGGAAANPIHILTKILadlhdetgritipdfyegveetpTQILKSWESLG 280
Cdd:cd03894 162 -QPVVAHKGIASYRIRVrgRAA----HSS-LPPLGVNAIEAAARLI-----------------------GKLRELADRLA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 281 RTAESFlgpiGLSIPAgekgrsvleltwarPTAEVNGIIGGYTgegfKTVIAAEASAKVSFRLVHKQDPVKIREAFRAFV 360
Cdd:cd03894 213 PGLRDP----PFDPPY--------------PTLNVGLIHGGNA----VNIVPAECEFEFEFRPLPGEDPEAIDARLRDYA 270
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 479375213 361 KERVPAD-CSVEFHPHGGSPAIQLPYDSPLVSKAKNALSD 399
Cdd:cd03894 271 EALLEFPeAGIEVEPLFEVPGLETDEDAPLVRLAAALAGD 310
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
21-170 |
7.17e-10 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 60.94 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 21 LDRLFNLLRIKSIStDPAYKADCRKAAEWLVED-LNSIGFDASVRDTPGHPMVVAHhegATADAPHVLFYGHYDVQPVDP 99
Cdd:PRK08554 4 LELLSSLVSFETVN-DPSKGIKPSKECPKFIKDtLESWGIESELIEKDGYYAVYGE---IGEGKPKLLFMAHFDVVPVNP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 479375213 100 lSLWENDPFDPAIKdvgdasnGGRkiLTGRGTSDDKGQLMTFVEACRAYKavNGSLPVKVTLLFEGEEESG 170
Cdd:PRK08554 80 -EEWNTEPFKLTVK-------GDK--AYGRGSADDKGNVASVMLALKELS--KEPLNGKVIFAFTGDEEIG 138
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
6-169 |
9.61e-10 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 60.40 E-value: 9.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 6 LDKVLNHLDANLNKSLDRLFNLLRIKSISTDPAykadcrKAAEWLVEDLNSIGF--------DASVRDTPGH-------- 69
Cdd:PRK06837 8 TQRILAAVDAGFDAQVAFTQDLVRFPSTRGAEA------PCQDFLARAFRERGYevdrwsidPDDLKSHPGAgpveidys 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 70 --PMVVAHHEGATADAPHVLFYGHYDVQPVDPLSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRA 147
Cdd:PRK06837 82 gaPNVVGTYRPAGKTGRSLILQGHIDVVPEGPLDLWSRPPFDPVIVD-------GW--MYGRGAADMKAGLAAMLFALDA 152
|
170 180
....*....|....*....|..
gi 479375213 148 YKAVNGSLPVKVTLLFEGEEES 169
Cdd:PRK06837 153 LRAAGLAPAARVHFQSVIEEES 174
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
77-362 |
3.95e-09 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 58.42 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 77 EGATADAPHVLFYGHYDVQPVDPLSL--WENDPFDPAIKDvgdasnggrKILTGRGTSDDKGQLMTFVEACrAYKAVNGS 154
Cdd:cd05674 63 EGSDPSLKPLLLMAHQDVVPVNPETEdqWTHPPFSGHYDG---------GYIWGRGALDDKNSLIGILEAV-ELLLKRGF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 155 LPVK-VTLLFEGEEES----GSPSLKPFLEANRQelKADVALVCD-----TAMWDAETPAISVGL--RGLVGEEIVIKAA 222
Cdd:cd05674 133 KPRRtIILAFGHDEEVggerGAGAIAELLLERYG--VDGLAAILDeggavLEGVFLGVPFALPGVaeKGYMDVEITVHTP 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 223 drdlhsgffGGAAANP-----IHILTKILADLHDE------TGRITIPDFYEGVEETPTQILKSWESLGRTAESFLGPIG 291
Cdd:cd05674 211 ---------GGHSSVPpkhtgIGILSEAVAALEANpfppklTPGNPYYGMLQCLAEHSPLPPRSLKSNLWLASPLLKALL 281
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 479375213 292 LSIPA--GEKGRSVLELTWArPTaevngIIGGytgeGFKT-VIAAEASAKVSFRLVHKQDPVKIREAFRAFVKE 362
Cdd:cd05674 282 ASELLstSPLTRALLRTTQA-VD-----IING----GVKInALPETATATVNHRIAPGSSVEEVLEHVKNLIAD 345
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
26-194 |
2.51e-08 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 56.01 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 26 NLLRIKSISTDPAYKADCRKAaEWLVEDLNSIGFDASVR-DTP------GH-PMVVAHHEGATaDAPHVLFYGHYDVQPV 97
Cdd:PRK13983 13 ELIAIPAVNPDFGGEGEKEKA-EYLESLLKEYGFDEVERyDAPdprvieGVrPNIVAKIPGGD-GKRTLWIISHMDVVPP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 98 DPLSLWENDPFDPAIKDvgdasnggRKILtGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESGSPSLKPF 177
Cdd:PRK13983 91 GDLSLWETDPFKPVVKD--------GKIY-GRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYGIQY 161
|
170
....*....|....*....
gi 479375213 178 LEANRQEL--KADVALVCD 194
Cdd:PRK13983 162 LLKKHPELfkKDDLILVPD 180
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
21-252 |
5.49e-08 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 54.85 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 21 LDRLFNLLRIKSISTDPAYKADC------RKAAEWLVEDLNSIGFDasVRDTPGhpmVVAHHE-GATADAPHVLfyGHYD 93
Cdd:PRK07318 17 IEDLQELLRINSVRDDSKAKEGApfgpgpVKALEKFLEIAERDGFK--TKNVDN---YAGHIEyGEGEEVLGIL--GHLD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 94 VQPVDplSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMtfveAC-RAYKAVNGS-LPV--KVTLLFEGEEES 169
Cdd:PRK07318 90 VVPAG--DGWDTDPYEPVIKD-------GK--IYARGTSDDKGPTM----AAyYALKIIKELgLPLskKVRFIVGTDEES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 170 GSPSLKPFLEanrQELKADVALVCdtamwDAETPAISvGLRGLVGEEIVIKAADRD----LHSgFFGGAAANPI------ 239
Cdd:PRK07318 155 GWKCMDYYFE---HEEAPDFGFSP-----DAEFPIIN-GEKGITTFDLVHFEGENEgdyvLVS-FKSGLRENMVpdsaea 224
|
250
....*....|...
gi 479375213 240 HILTKILADLHDE 252
Cdd:PRK07318 225 VITGDDLDDLIAA 237
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
91-239 |
2.36e-07 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 53.05 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 91 HYDVQPVDPlSLW--ENDPFDPAIKD-VGDAsnggrkiLTGRGTSDDKGQLMTfveACRAYKAVNGS-LPVK--VTLLFE 164
Cdd:PRK06156 117 HADVVPANP-ELWvlDGTRLDPFKVTlVGDR-------LYGRGTEDDKGAIVT---ALYAMKAIKDSgLPLArrIELLVY 185
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 479375213 165 GEEESGSPSLKPFLEANRQelkADVALVCdtamwDAETPAIsVGLRG--LVGEEIVIKAADRDLHS--GFFGGAAANPI 239
Cdd:PRK06156 186 TTEETDGDPLKYYLERYTP---PDYNITL-----DAEYPVV-TAEKGwgTIMATFPKRAADGKGAEivAMTGGAFANQI 255
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
27-166 |
4.37e-07 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 51.86 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 27 LLRIKSISTDPAYKADCRKaaewlvEDLNSIGFDASVRDTPGHPMvvahheGATADAPH-VLFYGHYDVQPVDPLSLWEN 105
Cdd:PRK13004 24 LIRIPSESGDEKRVVKRIK------EEMEKVGFDKVEIDPMGNVL------GYIGHGKKlIAFDAHIDTVGIGDIKNWDF 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 479375213 106 DPFDPAIKDvgdasnggrKILTGRGTSDDKGQLMTFVEACRAYKavngslpvKVTLLFEGE 166
Cdd:PRK13004 92 DPFEGEEDD---------GRIYGRGTSDQKGGMASMVYAAKIIK--------DLGLDDEYT 135
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
26-388 |
8.67e-07 |
|
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: 50.74 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 26 NLLRIKSISTDPAykadcrKAAEWLVEDLNSIGF-------DASVRDTpghpmVVAHHEGAtaDAPHVLFYGHYDVQPvd 98
Cdd:cd05652 7 SLVEIPSISGNEA------AVGDFLAEYLESLGFtvekqpvENKDRFN-----VYAYPGSS--RQPRVLLTSHIDTVP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 99 plslwendPFDPA-IKDVGDasnggrkILTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFE-GEEESGSpslkP 176
Cdd:cd05652 72 --------PFIPYsISDGGD-------TIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVvGEETGGD----G 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 177 FLEANRQELKAdvalvcdtamWDAetpAI---------SVGLRGLVGEEIVI--KAAdrdlHSGF--FGGAAanpIHILT 243
Cdd:cd05652 133 MKAFNDLGLNT----------WDA---VIfgeptelklASGHKGMLGFKLTAkgKAG----HSGYpwLGISA---IEILV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 244 KILADLHDETgritipdfyegveetptqiLKSWESLGRTAESflgpIGLsIPAGEKGrsvleltwarptaevngiiggyt 323
Cdd:cd05652 193 EALVKLIDAD-------------------LPSSELLGPTTLN----IGR-ISGGVAA----------------------- 225
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 479375213 324 gegfkTVIAAEASAKVSFRLVhkQDPVKIREAFRAFVKERVPADCSVEFHPHGGSPAIQLPYDSP 388
Cdd:cd05652 226 -----NVVPAAAEASVAIRLA--AGPPEVKDIVKEAVAGILTDTEDIEVTFTSGYGPVDLDCDVD 283
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
65-170 |
1.04e-06 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 50.91 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 65 DTPGHPM--VVAHHEGATaDAPHVLFYGHYDVQPVDplSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFV 142
Cdd:PRK13013 65 DSETYPRwnLVARRQGAR-DGDCVHFNSHHDVVEVG--HGWTRDPFGGEVKD-------GR--IYGRGACDMKGGLAASI 132
|
90 100
....*....|....*....|....*...
gi 479375213 143 EACRAYKAVNGSLPVKVTLLFEGEEESG 170
Cdd:PRK13013 133 IAAEAFLAVYPDFAGSIEISGTADEESG 160
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
90-169 |
1.15e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 50.85 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 90 GHYDVQPVDPLSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEES 169
Cdd:PRK07205 82 CHLDVVPEGDLSDWQTPPFEAVEKD-------GC--LFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGTDEET 152
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
37-168 |
3.64e-06 |
|
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: 48.96 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 37 PAYKADCRKAAEWLVEDLNSIGFDASVRDTPGHpmVVAHHEGATadaPHVLFYGHYDVQPVDPLSLWENDPFDPAIKDVg 116
Cdd:cd05649 11 PSESGEEKGVVERIEEEMEKLGFDEVEIDPMGN--VIGYIGGGK---KKILFDGHIDTVGIGNIDNWKFDPYEGYETDG- 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 479375213 117 dasnggrkILTGRGTSDDKGQLMTFVEACrAYKAVNGSLPVKVTLLFEG--EEE 168
Cdd:cd05649 85 --------KIYGRGTSDQKGGLASMVYAA-KIMKDLGLRDFAYTILVAGtvQEE 129
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
50-454 |
6.82e-06 |
|
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: 48.22 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 50 LVEDLNSIGFDASVRD---TPGHPM--VVAHHEGATADAPHVLFYGHYDVqpVDPlslWENDPfdPAIKDVGDASNGGRK 124
Cdd:cd05683 29 LKKKFENLGLSVIEDDagkTTGGGAgnLICTLKADKEEVPKILFTSHMDT--VTP---GINVK--PPQIADGYIYSDGTT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 125 ILTgrgtSDDKGQLMTFVEACRAYKAVNgsLP-VKVTLLFEGEEESGSPSLKpflEANRQELKADVALVCDTAmwdaetp 203
Cdd:cd05683 102 ILG----ADDKAGIAAILEAIRVIKEKN--IPhGQIQFVITVGEESGLVGAK---ALDPELIDADYGYALDSE------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 204 aisvglrGLVGEeIVIKAadrdlhsgffggaaanpihiltkiladlhdetgritipdfyegveetPTQILKSWESLGRTA 283
Cdd:cd05683 166 -------GDVGT-IIVGA-----------------------------------------------PTQDKINAKIYGKTA 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 284 ESFLGPiglsipagEKG--------RSVLELTWARPTAEVNGIIGGYTGEGFKTVIAAEASAKVSFRlVHKQDPV----- 350
Cdd:cd05683 191 HAGTSP--------EKGisainiaaKAISNMKLGRIDEETTANIGKFQGGTATNIVTDEVNIEAEAR-SLDEEKLdaqvk 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 351 KIREAFRAFVKERvpaDCSVEFHPHGGSPAIQLPYDSPLVSKAKNALSDEWPKPAVLIAMGGSipivgDFNTF--LGMES 428
Cdd:cd05683 262 HMKETFETTAKEK---GAHAEVEVETSYPGFKINEDEEVVKLAKRAANNLGLEINTTYSGGGS-----DANIIngLGIPT 333
|
410 420
....*....|....*....|....*.
gi 479375213 429 LLVGFGLEDdrIHSPNEKYELNSFHK 454
Cdd:cd05683 334 VNLGIGYEN--IHTTNERIPIEDLYD 357
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
58-180 |
1.29e-05 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 47.09 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 58 GFDASVRDTPGHPmvvahhegaTADAPHVLFYGHYD-VQPVDPLSL--WENDpfdpaikdvgdasnGGRkiLTGRGTSDD 134
Cdd:PRK07473 59 GFGDCVRARFPHP---------RQGEPGILIAGHMDtVHPVGTLEKlpWRRE--------------GNK--CYGPGILDM 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 479375213 135 KGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESGSPSLKPFLEA 180
Cdd:PRK07473 114 KGGNYLALEAIRQLARAGITTPLPITVLFTPDEEVGTPSTRDLIEA 159
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
24-219 |
2.82e-05 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 46.10 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 24 LFNLLRIKSISTDPAykadcrKAAEWLVEDLNSIGFDASVrDTPGHPMVVAHHEGatadaPHVLFYGHYDVQPVD-PLSL 102
Cdd:PRK04443 12 LKGLVEIPSPSGEEA------AAAEFLVEFMESHGREAWV-DEAGNARGPAGDGP-----PLVLLLGHIDTVPGDiPVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 103 wENDpfdpaikdvgdasnggrkILTGRGTSDDKGQLMTFVEAcraykAVNGSLPVKVTLLFEG--EEESGSpSLKPFLEA 180
Cdd:PRK04443 80 -EDG------------------VLWGRGSVDAKGPLAAFAAA-----AARLEALVRARVSFVGavEEEAPS-SGGARLVA 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 479375213 181 NRqeLKADVALVCDTAMWDaetpAISVGLRGLVGEEIVI 219
Cdd:PRK04443 135 DR--ERPDAVIIGEPSGWD----GITLGYKGRLLVTYVA 167
|
|
| PRK06915 |
PRK06915 |
peptidase; |
7-192 |
5.29e-05 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 45.45 E-value: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 7 DKVLNHLDANLNKSLDRLFNLLRIKSISTDPaykadcRKAAEWLVEDLNSIGFD--------ASVRDTP----------G 68
Cdd:PRK06915 6 KQICDYIESHEEEAVKLLKRLIQEKSVSGDE------SGAQAIVIEKLRELGLDldiwepsfKKLKDHPyfvsprtsfsD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 69 HPMVVAHHEGaTADAPHVLFYGHYDVQPVDPLSLWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGQLMTFVEACRAY 148
Cdd:PRK06915 80 SPNIVATLKG-SGGGKSMILNGHIDVVPEGDVNQWDHHPYSGEVIG-------GR--IYGRGTTDMKGGNVALLLAMEAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 479375213 149 KAVNGSLpvKVTLLFEG--EEESGSPSLkpfLEANRQELKADVALV 192
Cdd:PRK06915 150 IESGIEL--KGDVIFQSviEEESGGAGT---LAAILRGYKADGAII 190
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
24-316 |
6.22e-05 |
|
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: 45.04 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 24 LFNLLRIKSISTDPAykadcrKAAEWLVEDLNSIGFDASVrDTPGHpmVVAhheGATADAPHVLFYGHYDVQPvdplslw 103
Cdd:cd05653 7 LLDLLSIYSPSGEEA------RAAKFLEEIMKELGLEAWV-DEAGN--AVG---GAGSGPPDVLLLGHIDTVP------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 104 enDPFDPAIKDvgdasnggrKILTGRGTSDDKGQLMTFVEACRaykAVNGSLPVKVTLLFEGEEESGSPSLKpflEANRQ 183
Cdd:cd05653 68 --GEIPVRVEG---------GVLYGRGAVDAKGPLAAMILAAS---ALNEELGARVVVAGLVDEEGSSKGAR---ELVRR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 184 ELKADVALVCDTAMWDaetpAISVGLRGLVGEEIVIKAadRDLHSgffGGAAANPIHILTKILADLHDETGRITiPDFYE 263
Cdd:cd05653 131 GPRPDYIIIGEPSGWD----GITLGYRGSLLVKIRCEG--RSGHS---SSPERNAAEDLIKKWLEVKKWAEGYN-VGGRD 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 479375213 264 GVEETPTqILKSWESLGRTAESFLGPIGLSIPAGEKGRSVLEL-TWARPTAEVN 316
Cdd:cd05653 201 FDSVVPT-LIKGGESSNGLPQRAEATIDLRLPPRLSPEEAIALaTALLPTCELE 253
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
46-468 |
7.81e-05 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 44.79 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 46 AAEWLvEDLnsIGFDaSVRDTPGHPMV-----------VAHH-----EG------AT---ADAPHVLFYGHYDVQPVDPL 100
Cdd:PRK07522 6 SLDIL-ERL--VAFD-TVSRDSNLALIewvrdylaahgVESElipdpEGdkanlfATigpADRGGIVLSGHTDVVPVDGQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 101 SlWENDPFDPAIKDvgdasngGRkiLTGRGTSDDKGqlmtFVEACRAYKAVNGSLPVK--VTLLFEGEEESGS---PSLK 175
Cdd:PRK07522 82 A-WTSDPFRLTERD-------GR--LYGRGTCDMKG----FIAAALAAVPELAAAPLRrpLHLAFSYDEEVGClgvPSMI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 176 PFLEANrqelkadvalvcdtamwdAETPAISVglrglVGE----EIVI----KAADRdLHsgfFGGAAA---------NP 238
Cdd:PRK07522 148 ARLPER------------------GVKPAGCI-----VGEptsmRPVVghkgKAAYR-CT---VRGRAAhsslapqgvNA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 239 IHILTKILADLHDETGRITIPDFYEGVEETPtqilksweslgrtaesflgpiglsipagekgrsvleltWArpTAEVNGI 318
Cdd:PRK07522 201 IEYAARLIAHLRDLADRLAAPGPFDALFDPP--------------------------------------YS--TLQTGTI 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 319 IGGytgegfkT---VIAAEASAKVSFRLVHKQDPVKIREAFRAFVKE-------RVPADCSVEFHPHGGSPAIQLPYDSP 388
Cdd:PRK07522 241 QGG-------TalnIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAellpemrAVHPEAAIEFEPLSAYPGLDTAEDAA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 389 LVSKAKnALSDEWPKPAVLIAMGGsipivGDFNTfLGMESLLVGFGleD-DRIHSPNEKYELNSFHKGQRSWARILAAIA 467
Cdd:PRK07522 314 AARLVR-ALTGDNDLRKVAYGTEA-----GLFQR-AGIPTVVCGPG--SiEQAHKPDEFVELAQLAACEAFLRRLLASLA 384
|
.
gi 479375213 468 A 468
Cdd:PRK07522 385 A 385
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
84-192 |
7.75e-04 |
|
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: 41.53 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 84 PHVLFYGHYDVqpVDPLSLWENDPFDPAIKdvgdasnGGRkiLTGRGTSDDKGQLM----TFVEACRaykavNGSLPVKV 159
Cdd:cd05651 56 PTLLLNSHHDT--VKPNAGWTKDPFEPVEK-------GGK--LYGLGSNDAGASVVsllaTFLHLYS-----EGPLNYNL 119
|
90 100 110
....*....|....*....|....*....|....
gi 479375213 160 TLLFEGEEESgspSLKPFLEANRQEL-KADVALV 192
Cdd:cd05651 120 IYAASAEEEI---SGKNGIESLLPHLpPLDLAIV 150
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
44-469 |
4.60e-03 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 39.26 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 44 RKAAEWLVEDLNSIGFDASVRDTpGHpmVVAHHEG-ATADAPHVLFYGHYDVQPVDPlslweNDPFDPAIKDvgdasngg 122
Cdd:COG2195 23 EALADYLVEELKELGLEVEEDEA-GN--VIATLPAtPGYNVPTIGLQAHMDTVPQFP-----GDGIKPQIDG-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 123 rKILTGRGTS----DDKGQLMTFVEACRAYKavNGSLPV-KVTLLFEGEEESGS-------PSLkpfleanrqeLKADVA 190
Cdd:COG2195 87 -GLITADGTTtlgaDDKAGVAAILAALEYLK--EPEIPHgPIEVLFTPDEEIGLrgakaldVSK----------LGADFA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 191 LVCDTAMWD---AETP-AISVglrglvgeEIVI--KAAdrdlHSGFFGGAAANPIHILTKILADLHdetgritipdfyeg 264
Cdd:COG2195 154 YTLDGGEEGeleYECAgAADA--------KITIkgKGG----HSGDAKEKMINAIKLAARFLAALP-------------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 265 veetptqilkswesLGRTAEsflgpiglsipagekgrsvleltwarptaEVNGIIGGYTGEGFKTVIAAEASAKVSFRLv 344
Cdd:COG2195 208 --------------LGRIPE-----------------------------ETEGNEGFIHGGSATNAIPREAEAVYIIRD- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 345 HKQDPVK-----IREAFRAFVKErVPAdCSVEFHPHGGSPAIQLPYDSPLVSKAKNALSDEWPKPAVLIAMGGS------ 413
Cdd:COG2195 244 HDREKLEarkaeLEEAFEEENAK-YGV-GVVEVEIEDQYPNWKPEPDSPIVDLAKEAYEELGIEPKIKPIRGGLdggils 321
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 479375213 414 ---IPIVgdfNTFLGMESllvgfgleddrIHSPNEKYELNSFhkgQRSWaRILAAIAAK 469
Cdd:COG2195 322 fkgLPTP---NLGPGGHN-----------FHSPDERVSIESM---EKAW-ELLVEILKL 362
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
40-170 |
7.64e-03 |
|
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: 38.69 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 40 KADCRKAAEWLVEDLNSIGFDASVRDTPGHPMVVAHHEGAT--------ADAPH-VLFYGHYDVQPvdPLSLWENDPFDP 110
Cdd:cd02697 21 PGNNAPHAERTAALLQGFGFEAERHPVPEAEVRAYGMESITnlivrrryGDGGRtVALNAHGDVVP--PGDGWTRDPYGA 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 479375213 111 AIKDvgdasnggrKILTGRGTSDDKGQLMTFVEACRAYKAVNGSLPVKVTLLFEGEEESG 170
Cdd:cd02697 99 VVED---------GVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFG 149
|
|
| |
