|
Name |
Accession |
Description |
Interval |
E-value |
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
4-366 |
1.73e-120 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 352.43 E-value: 1.73e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 4 RERLQERFIEMIKIYSPSKGEKEMADWIENWLRERNIPFQSDHAGeayggngrNIVAFVKGNT-KERP-LGFAAHMDQIE 81
Cdd:COG2195 2 PERLLERFLEYVKIPTPSDHEEALADYLVEELKELGLEVEEDEAG--------NVIATLPATPgYNVPtIGLQAHMDTVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 82 --PCRNVNPVINGNIISTDKTTTLGGDDKAGISAIMEAVEDIIESGVPHRDIYLVFTCSEEISMMGTKHMDMSMLPCKEL 159
Cdd:COG2195 74 qfPGDGIKPQIDGGLITADGTTTLGADDKAGVAAILAALEYLKEPEIPHGPIEVLFTPDEEIGLRGAKALDVSKLGADFA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 160 VVVDaTGGAETLAYKAPAMEAIEITFKGKKAHAGIEPEKGINAIVVASKAISKMHIGRIDYETTSNIGHIEGGSATNIVT 239
Cdd:COG2195 154 YTLD-GGEEGELEYECAGAADAKITIKGKGGHSGDAKEKMINAIKLAARFLAALPLGRIPEETEGNEGFIHGGSATNAIP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 240 DEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMG-ACYEMKHEMAYPVLSLEEDCELIQDTVNAMAEERITANKMIIG 318
Cdd:COG2195 233 REAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGvGVVEVEIEDQYPNWKPEPDSPIVDLAKEAYEELGIEPKIKPIR 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 547812054 319 GGSDANVLAGHGYKSVILGCGMINVHTVEEALDTDETWKVTKVLRRLM 366
Cdd:COG2195 313 GGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWELLVEIL 360
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
3-360 |
1.38e-103 |
|
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: 309.77 E-value: 1.38e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 3 SRERLQERFIEMIKIYSPSKGEKEMADWIENWLRERNIPFQSDHAGEAYGGNGRNIVAFVKGNTKERP-LGFAAHMDQIE 81
Cdd:cd05683 1 NEDRLINTFLELVQIDSETLHEKEISKVLKKKFENLGLSVIEDDAGKTTGGGAGNLICTLKADKEEVPkILFTSHMDTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 82 PCRNV-NPVINGNIISTDKTTTLGGDDKAGISAIMEAVEDIIESGVPHRDIYLVFTCSEEISMMGTKHMDMSMLPCKELV 160
Cdd:cd05683 81 PGINVkPPQIADGYIYSDGTTILGADDKAGIAAILEAIRVIKEKNIPHGQIQFVITVGEESGLVGAKALDPELIDADYGY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 161 VVDATGGAETLAYKAPAMEAIEITFKGKKAHAGIEPEKGINAIVVASKAISKMHIGRIDYETTSNIGHIEGGSATNIVTD 240
Cdd:cd05683 161 ALDSEGDVGTIIVGAPTQDKINAKIYGKTAHAGTSPEKGISAINIAAKAISNMKLGRIDEETTANIGKFQGGTATNIVTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 241 EVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPVLSLEEDCELIQDTVNAMAEERITANKMIIGGG 320
Cdd:cd05683 241 EVNIEAEARSLDEEKLDAQVKHMKETFETTAKEKGAHAEVEVETSYPGFKINEDEEVVKLAKRAANNLGLEINTTYSGGG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 547812054 321 SDANVLAGHGYKSVILGCGMINVHTVEEALDTDETWKVTK 360
Cdd:cd05683 321 SDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAV 360
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
6-362 |
5.39e-90 |
|
peptidase T-like protein; This model represents a clade of enzymes closely related to Peptidase T, an aminotripeptidase found in bacteria. This clade consists of gram positive bacteria of which several additionally contain a Peptidase T gene.
Pssm-ID: 162579 [Multi-domain] Cd Length: 361 Bit Score: 274.89 E-value: 5.39e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 6 RLQERFIEMIKIYSPSKGEKEMADWIENWLRERNIPFQSDHAgEAYGGNGRNIVAFVKGNTKERPLGFAAHMDQIEPCRN 85
Cdd:TIGR01883 1 RLKKYFLELIQIDSESGKEKAILTYLKKQITKLGIPVSLDEV-PAEVSNDNNLIARLPGTVKFDTIFFCGHMDTVPPGAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 86 VNPVINGNIISTDKTTTLGGDDKAGISAIMEAVEDIIESGVPHRDIYLVFTCSEEISMMGTKHMDMSMLPCKELVVVDAT 165
Cdd:TIGR01883 80 PEPVVEDGIFTSLGGTILGADDKAGVAAMLEAMDVLSTEETPHGTIEFIFTVKEELGLIGMRLFDESKITAAYGYCLDAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 166 GGAETLAYKAPAMEAIEITFKGKKAHAGIEPEKGINAIVVASKAISKMHIGRIDYETTSNIGHIEGGSATNIVTDEVTFT 245
Cdd:TIGR01883 160 GEVGNIQLAAPTQVKVDATIAGKDAHAGLVPEDGISAISVARMAIHAMRLGRIDEETTANIGSFSGGVNTNIVQDEQLIV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 246 AEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPVLSLEEDCELIQDTVNAMAEERITANKMIIGGGSDANV 325
Cdd:TIGR01883 240 AEARSLSFRKAEAQVQTMRERFEQAAEKYGATLEEETRLIYEGFKIHPQHPLMNIFKKAAKKIGLKTSEIFSGGGSDANV 319
|
330 340 350
....*....|....*....|....*....|....*..
gi 547812054 326 LAGHGYKSVILGCGMINVHTVEEALDTDETWKVTKVL 362
Cdd:TIGR01883 320 LNEKGVPTVNLSAGYVHAHTEKETISIEQLVKLAELV 356
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
4-366 |
1.66e-53 |
|
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: 181.24 E-value: 1.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 4 RERLQERFIEMIKIYSPSKGEKEMADWIENWLRERNIPFQSDHAGEAYGgngrNIVAFVKGNTKERPLGFAAHMDqiepc 83
Cdd:COG0624 11 LDEALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPPGRP----NLVARRPGDGGGPTLLLYGHLD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 84 rnVNPVINGNIISTD--KTTTLGG--------DDKAGISAIMEAVEDIIESGV-PHRDIYLVFTCSEEISMMGTKHM--- 149
Cdd:COG0624 82 --VVPPGDLELWTSDpfEPTIEDGrlygrgaaDMKGGLAAMLAALRALLAAGLrLPGNVTLLFTGDEEVGSPGARALvee 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 150 DMSMLPCKELVVVDATGGAE-TLAYKAPAMeaIEITFKGKKAHAGIePEKGINAIVVASKAISKMH----IGRID---YE 221
Cdd:COG0624 160 LAEGLKADAAIVGEPTGVPTiVTGHKGSLR--FELTVRGKAAHSSR-PELGVNAIEALARALAALRdlefDGRADplfGR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 222 TTSNIGHIEGGSATNIVTDEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPVLSlEEDCELIQDT 301
Cdd:COG0624 237 TTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEVEVLGDGRPPFET-PPDSPLVAAA 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 547812054 302 VNAMAEER-ITANKMIIGGGSDANVLAG-HGYKSVILGCGMI-NVHTVEEALDTDETWKVTKVLRRLM 366
Cdd:COG0624 316 RAAIREVTgKEPVLSGVGGGTDARFFAEaLGIPTVVFGPGDGaGAHAPDEYVELDDLEKGARVLARLL 383
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
46-365 |
2.39e-39 |
|
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; tripeptide aminopeptidase; tripeptidase) subfamily and similar proteins. PepT acts only on tripeptide substrates, and is thus termed a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349897 [Multi-domain] Cd Length: 400 Bit Score: 144.06 E-value: 2.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 46 HAGEAYGGNGRNIVAFVKGNTKERPLGFAAHMDQIEPCR--NVNPVINGNIISTDKTTTLGGDDKAGISAIMEAVEDIIE 123
Cdd:cd05645 75 HVDTSPDGSGKNVNPQIVENYRGGDIALGIGDEVLSPVMfpVLHQLLGQTLITTDGKTLLGADDKAGLAEIFTALAVLKE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 124 SGVPHRDIYLVFTCSEEISmMGTKHMDMSMLPCKELVVVDATGGAEtLAYKAPAMEAIEITFKGKKAHAGIEPEKGINAI 203
Cdd:cd05645 155 KNIPHGDIEVAFTPDEEVG-KGAKHFDVEAFTAKWAYTVDGGGVGE-LEFENFNAASVNIKIVGNNVHPGTAKGVGVNAL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 204 VVASKAISKMH-----IGRIDYETTSNIGHIEGGsatnivTDEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMG-AC 277
Cdd:cd05645 233 SLAARIHAEVPadespEGTEGYEGFYHLASFKGT------VDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVGKGLHpDC 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 278 Y-EMKHEMAYPVLSlEEDCE--LIQDTVNAMAEE-RITANKMIIGGGSDANVLAGHGYKSVILGCGMINVHTVEEALDTD 353
Cdd:cd05645 307 YiELVIEDSYYNFR-EKVVEhpHILDIAQQAARDcGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVTLE 385
|
330
....*....|..
gi 547812054 354 ETWKVTKVLRRL 365
Cdd:cd05645 386 GLEKAVQVIVRI 397
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
13-365 |
5.04e-34 |
|
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: 128.96 E-value: 5.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 13 EMIKIYSPSKGEKEMADWIENWLRERNIPFQSDHAGEAYggngrNIVAfVKGNTKERPLGFAAHMDqiepcrnVNPVING 92
Cdd:cd08659 5 DLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRG-----NLVA-TVGGGDGPVLLLNGHID-------TVPPGDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 93 NIISTDKTTTLGGDD----------KAGISAIMEAVEDIIESGVPHR-DIYLVFTCSEEISMMGTKHMDmSMLPCKE--- 158
Cdd:cd08659 72 DKWSFPPFSGRIRDGrlygrgacdmKGGLAAMVAALIELKEAGALLGgRVALLATVDEEVGSDGARALL-EAGYADRlda 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 159 LVVVDATGGAETLAYKApAMEaIEITFKGKKAHAGiEPEKGINAIVVASKAISKMH-----IGRIDY--ETTSNIGHIEG 231
Cdd:cd08659 151 LIVGEPTGLDVVYAHKG-SLW-LRVTVHGKAAHSS-MPELGVNAIYALADFLAELRtlfeeLPAHPLlgPPTLNVGVING 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 232 GSATNIVTDEVTFTAEIRShSMEKLAAEVTHMeqcCKEAVEEMGACYEMKHEM-AYPVLSLEEDCELIQDTVNAMAEERI 310
Cdd:cd08659 228 GTQVNSIPDEATLRVDIRL-VPGETNEGVIAR---LEAILEEHEAKLTVEVSLdGDPPFFTDPDHPLVQALQAAARALGG 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 547812054 311 TANKMIIGGGSDANVLAG-HGYKSVILGCGMINV-HTVEEALDTDETWKVTKVLRRL 365
Cdd:cd08659 304 DPVVRPFTGTTDASYFAKdLGFPVVVYGPGDLALaHQPDEYVSLEDLLRAAEIYKEI 360
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
106-366 |
3.18e-32 |
|
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: 123.23 E-value: 3.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 106 DDKAGISAIMEAVEDIIESGVPHRDIYLVFTCSEEISMMGTKHM----DMSMLPCK---ELVVVDATGGAETLAYKAPAM 178
Cdd:pfam01546 34 DMKGGLLAALEALRALKEEGLKKGTVKLLFQPDEEGGMGGARALiedgLLEREKVDavfGLHIGEPTLLEGGIAIGVVTG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 179 EA----IEITFKGKKAHAGIePEKGINAIVVASKAISKMH--IGRIDYE------TTSNIGHIEGGsaTNIVTDEVTFTA 246
Cdd:pfam01546 114 HRgslrFRVTVKGKGGHAST-PHLGVNAIVAAARLILALQdiVSRNVDPldpavvTVGNITGIPGG--VNVIPGEAELKG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 247 EIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMK--HEMAYPVLSLEEDCELIQDTVNAMAEERITANKMIIGGGSDAN 324
Cdd:pfam01546 191 DIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEyvEGGAPPLVNDSPLVAALREAAKELFGLKVELIVSGSMGGTDAA 270
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 547812054 325 -VLAGHGYKSVILGCGMINVHTVEEALDTDETWKVTKVLRRLM 366
Cdd:pfam01546 271 fFLLGVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLL 313
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
21-366 |
2.47e-27 |
|
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: 110.76 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 21 SKGEKEMADWIENWLRERNIPFQSDHAGEayggNGR-NIVAfVKGNTKERPLGFAAHMDqiepcrnVNPViNGNIISTD- 98
Cdd:cd03894 14 RNSNLALIEYVADYLAALGVKSRRVPVPE----GGKaNLLA-TLGPGGEGGLLLSGHTD-------VVPV-DGQKWSSDp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 99 -KTTTLGG--------DDKAGISAIMEAVEDIIESGvPHRDIYLVFTCSEEISMMGTKHM--DMSMLPCK---------- 157
Cdd:cd03894 81 fTLTERDGrlygrgtcDMKGFLAAVLAAVPRLLAAK-LRKPLHLAFSYDEEVGCLGVRHLiaALAARGGRpdaaivgept 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 158 ELVVVDATGGaeTLAYKapameaieITFKGKKAHAGIePEKGINAIVVASKAISK-----------MHIGRIDY-ETTSN 225
Cdd:cd03894 160 SLQPVVAHKG--IASYR--------IRVRGRAAHSSL-PPLGVNAIEAAARLIGKlreladrlapgLRDPPFDPpYPTLN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 226 IGHIEGGSATNIVTDEVTFTAEIR---SHSMEKLAAEVthmEQCCKEAVEEMGACYEMKHEMAYPVLSLEEDCELIQdtv 302
Cdd:cd03894 229 VGLIHGGNAVNIVPAECEFEFEFRplpGEDPEAIDARL---RDYAEALLEFPEAGIEVEPLFEVPGLETDEDAPLVR--- 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 547812054 303 naMAEERITANKMI-IGGGSDANVLAGHGYKSVILGCGMINV-HTVEEALDTDETWKVTKVLRRLM 366
Cdd:cd03894 303 --LAAALAGDNKVRtVAYGTEAGLFQRAGIPTVVCGPGSIAQaHTPDEFVELEQLDRCEEFLRRLI 366
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
7-365 |
1.18e-26 |
|
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; tripeptide aminopeptidase; tripeptidase) subfamily. PepT 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: 349887 [Multi-domain] Cd Length: 400 Bit Score: 109.56 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 7 LQERFIEMIKIYSPS----------KGEKEMADWIENWLRE---RNIpFQSDHAgeaYggngrnIVAFVKGNTKE--RPL 71
Cdd:cd03892 1 LLERFLRYVKIDTQSdessetvpstEGQLELAKLLAKELKElglEDV-TLDEHG---Y------VTATLPANVDKdvPTI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 72 GFAAHMDQIE--PCRNVNPVINGN------------------------------IISTDKTTTLGGDDKAGISAIMEAVE 119
Cdd:cd03892 71 GFIAHMDTAPdnSGKNVKPQIIENydggdivlnesgivlspaefpelknykgqtLITTDGTTLLGADDKAGIAEIMTALE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 120 DIIES-GVPHRDIYLVFTCSEEISmMGTKHMDMSMLPCKELVVVDATGGAEtLAYKAPAMEAIEITFKGKKAHAGIEPEK 198
Cdd:cd03892 151 YLIEHpEIKHGDIRVGFTPDEEIG-RGADHFDVEKFGADFAYTLDGGELGE-LEYENFNAASATITITGVNVHPGTAKGK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 199 GINAIVVASKAISKMHIGRI-----DYETTSNIGHIEGGsatnivTDEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEE 273
Cdd:cd03892 229 MVNALLLAADFHSMLPREETpehteGYEGFYHLLSMEGT------VEEAELSYIIRDFDRDGFEARKELIKEIAKKLNAK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 274 MGAC---YEMKHE---MAYpvlSLEEDCELIQDTVNAMAEERITANKMIIGGGSDANVLAGHGYKSVILGCGMINVHTVE 347
Cdd:cd03892 303 YGEGrveLEIKDQyynMKE---KIEPHMHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNFHGRY 379
|
410
....*....|....*...
gi 547812054 348 EALDTDETWKVTKVLRRL 365
Cdd:cd03892 380 EFVPVESMEKAVEVIVKI 397
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
5-361 |
2.35e-25 |
|
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: 105.56 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 5 ERLQERFIEMIKIYSPSKGEKEMADWIENWLRERNIPFQSDHAGEAYGGNGRNIVAFVKGNTKERPLGFAAHMDQIEPCR 84
Cdd:TIGR01910 1 VELLKDLISIPSVNPPGGNEETIANYIKDLLREFGFSTDVIEITDDRLKVLGKVVVKEPGNGNEKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 85 ----NVNP----VINGNIISTDKTttlggDDKAGISAIMEAVEDIIESGV-PHRDIYLVFTCSEEISMMGTKH--MDMSM 153
Cdd:TIGR01910 81 lelwKTDPfkpvEKDGKLYGRGAT-----DMKGGLVALLYALKAIREAGIkPNGNIILQSVVDEESGEAGTLYllQRGYF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 154 LPCKELVVVDATGGAETLAYKAPAMEAIeITFKGKKAHAGIePEKGINAIVVASKAI-----------SKMHIGRIDYET 222
Cdd:TIGR01910 156 KDADGVLIPEPSGGDNIVIGHKGSIWFK-LRVKGKQAHASF-PQFGVNAIMKLAKLItelneleehiyARNSYGFIPGPI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 223 TSNIGHIEGGSATNIVTDEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPV-LSLEEDCELIQDT 301
Cdd:TIGR01910 234 TFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYENEPVVKWSGpNETPPDSRLVKAL 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547812054 302 VNAMAEER-ITANKMIIGGGSDANVLAGHGYKSVILGCGMI-NVHTVEEALDTDETWKVTKV 361
Cdd:TIGR01910 314 EAIIKKVRgIEPEVLVSTGGTDARFLRKAGIPSIVYGPGDLeTAHQVNEYISIKNLVESTKV 375
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
5-366 |
1.46e-24 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 103.53 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 5 ERLQERFIEMIKIYS---PSKGEKEMADWIENWLRERNIPFQSDHAGEAYG--GNGRNIVAFVKGNTKERPLGFAAHMDQ 79
Cdd:PRK08651 6 FDIVEFLKDLIKIPTvnpPGENYEEIAEFLRDTLEELGFSTEIIEVPNEYVkkHDGPRPNLIARRGSGNPHLHFNGHYDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 80 I---EPCRNVNP---VINGNIISTDKTTtlggDDKAGISAIMEAVEDIIESG-VPhrdIYLVFTCSEEISMMGTKHMDMS 152
Cdd:PRK08651 86 VppgEGWSVNVPfepKVKDGKVYGRGAS----DMKGGIAALLAAFERLDPAGdGN---IELAIVPDEETGGTGTGYLVEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 153 MLPCKELVVVDATGGAETLAYKAPAMEAIEITFKGKKAHAGiEPEKGINAIVVASKAI------SKMHIGRIDYET---- 222
Cdd:PRK08651 159 GKVTPDYVIVGEPSGLDNICIGHRGLVWGVVKVYGKQAHAS-TPWLGINAFEAAAKIAerlkssLSTIKSKYEYDDerga 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 223 --TSNIG--HIEGGSATNIVTDEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPVLSLEEDCELI 298
Cdd:PRK08651 238 kpTVTLGgpTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFEITPFSEAFVTDPDSELV 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 299 QDTVNAMAEER-ITANKMIIGGGSDANVLAGHGYKSVILGCGMINV-HTVEEALDTDETWKVTKVLRRLM 366
Cdd:PRK08651 318 KALREAIREVLgVEPKKTISLGGTDARFFGAKGIPTVVYGPGELELaHAPDEYVEVKDVEKAAKVYEEVL 387
|
|
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
4-365 |
2.22e-24 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 102.90 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 4 RERLQERFIEMIKIYSPSK----------GEKEMADWIENWLRErnIPFQ----SDHAgeaYggngrnIVAFVKGNT-KE 68
Cdd:PRK05469 1 MDKLLERFLRYVKIDTQSDensttvpsteGQWDLAKLLVEELKE--LGLQdvtlDENG---Y------VMATLPANVdKD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 69 RP-LGFAAHMDQIEPC--RNVNPVI----NGN--------------------------IISTDKTTTLGGDDKAGISAIM 115
Cdd:PRK05469 70 VPtIGFIAHMDTAPDFsgKNVKPQIienyDGGdialgdgnevlspaefpelknyigqtLITTDGTTLLGADDKAGIAEIM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 116 EAVEDIIESG-VPHRDIYLVFTCSEEISmMGTKHMDMSMLPCKELVVVDAtGGAETLAYKAPAMEAIEITFKGKKAHAGI 194
Cdd:PRK05469 150 TALEYLIAHPeIKHGDIRVAFTPDEEIG-RGADKFDVEKFGADFAYTVDG-GPLGELEYENFNAASAKITIHGVNVHPGT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 195 EPEKGINAIVVASKAISKMHIGRIDyETTSN------IGHIEGGSatnivtDEVTFTAEIRSHSMEKLAAEVTHMEQCCK 268
Cdd:PRK05469 228 AKGKMVNALLLAADFHAMLPADETP-ETTEGyegfyhLTSIKGTV------EEAELSYIIRDFDREGFEARKALMQEIAK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 269 EAVEEMGACY---EMK---HEMAYpvlSLEEDCELIQDTVNAMAEERITANKMIIGGGSDANVLAGHGyksviLGC---- 338
Cdd:PRK05469 301 KVNAKYGEGRvelEIKdqyYNMRE---KIEPHPHIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMG-----LPCpnif 372
|
410 420
....*....|....*....|....*...
gi 547812054 339 -GMINVHTVEEALDTDETWKVTKVLRRL 365
Cdd:PRK05469 373 tGGHNFHGKFEFVSLESMEKAVEVIVEI 400
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
13-353 |
1.49e-22 |
|
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: 97.28 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 13 EMIKIYSPSK---GEKEMADWIENWLRERNIPFQSdHAGEAYGGNgrniVAFVKGNTKERPLGFAAHMD--------QIE 81
Cdd:cd03885 7 RLVNIESGTYdkeGVDRVAELLAEELEALGFTVER-RPLGEFGDH----LIATFKGTGGKRVLLIGHMDtvfpegtlAFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 82 PCRNVNPVINGNIIStdktttlggDDKAGISAIMEAVEDIIESGV-PHRDIYLVFTCSEEISMMGTKhmdmsmlpckELV 160
Cdd:cd03885 82 PFTVDGDRAYGPGVA---------DMKGGLVVILHALKALKAAGGrDYLPITVLLNSDEEIGSPGSR----------ELI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 161 VVDATGGAETLAYKAPA-----------MEAIEITFKGKKAHAGIEPEKGINAIVVASKAISKMHiGRIDYE--TTSNIG 227
Cdd:cd03885 143 EEEAKGADYVLVFEPARadgnlvtarkgIGRFRLTVKGRAAHAGNAPEKGRSAIYELAHQVLALH-ALTDPEkgTTVNVG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 228 HIEGGSATNIVTDEVTFTAEIRSHSMEKLAAEVTHMEQCCKEaVEEMGACYEMKHEMAYPVLSLEEDCELIQDTVNAMAE 307
Cdd:cd03885 222 VISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVAT-TLVPGTSVELTGGLNRPPMEETPASRRLLARAQEIAA 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 547812054 308 ER-ITANKMIIGGGSDANVLAGHGyKSVILGCGMI--NVHTVEEALDTD 353
Cdd:cd03885 301 ELgLTLDWEATGGGSDANFTAALG-VPTLDGLGPVggGAHTEDEYLELD 348
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-366 |
1.04e-21 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 94.76 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 13 EMIKIYS---PSKGEKEMADWIENWLRERNIPfQSDHAGEAYGGNGRNIVafVKGNTKERpLGFAAHMDqiepcrnVNPV 89
Cdd:cd08011 6 ELVQIPSpnpPGDNTSAIAAYIKLLLEDLGYP-VELHEPPEEIYGVVSNI--VGGRKGKR-LLFNGHYD-------VVPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 90 INGNIISTD------KTTTLGG----DDKAGISAIMEAVEDIIESGVP-HRDIYLVFTCSEEiSM--MGTKHMDMSMLPC 156
Cdd:cd08011 75 GDGEGWTVDpysgkiKDGKLYGrgssDMKGGIAASIIAVARLADAKAPwDLPVVLTFVPDEE-TGgrAGTKYLLEKVRIK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 157 KELVVVDATGGAETLAYKAPAMEAIEITFKGKKAHAGIePEKGINAIVVASKAISKMHigriDYETTSNIGHIEGGSATN 236
Cdd:cd08011 154 PNDVLIGEPSGSDNIRIGEKGLVWVIIEITGKPAHGSL-PHRGESAVKAAMKLIERLY----ELEKTVNPGVIKGGVKVN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 237 IVTDEVTFTAEIRSHSMEKLaAEVTHmeQCCKEAVEEMGACYEMKHEMAYPVLSLEED-----CELIQDTVNamaeerIT 311
Cdd:cd08011 229 LVPDYCEFSVDIRLPPGIST-DEVLS--RIIDHLDSIEEVSFEIKSFYSPTVSNPDSEivkktEEAITEVLG------IR 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 547812054 312 ANKMIIGGGSDANVLAGHGYKSVILGCGMINV-HTVEEALDTDETWKVTKVLRRLM 366
Cdd:cd08011 300 PKEVISVGASDARFYRNAGIPAIVYGPGRLGQmHAPNEYVEIDELIKVIKVHALVA 355
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
7-365 |
1.18e-20 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 92.29 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 7 LQERFIEMIKIYSPSK----------GEKEMADWIENWLRE---RNIpFQSDHAgeayggngrNIVAFVKGNT-KERPLG 72
Cdd:PRK13381 3 LTDRFFRYLKVNSQSDaasgtlpstpGQHELAKLLADELRElglEDI-VIDEHA---------IVTAKLPGNTpGAPRIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 73 FAAHMD--------QIEP----------CRN--------------VNPVINGNIISTDKTTTLGGDDKAGISAIMEAVED 120
Cdd:PRK13381 73 FIAHLDtvdvglspDIHPqilrfdggdlCLNaeqgiwlrtaehpeLLNYQGEDIIFSDGTSVLGADNKAAIAVVMTLLEN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 121 IIESGVPHRDIYLVFTCSEEISMMGTKHMDMSMLPCKELVVVDATGGAEtLAYKAPAMEAIEITFKGKKAHAGiePEKG- 199
Cdd:PRK13381 153 LTENEVEHGDIVVAFVPDEEIGLRGAKALDLARFPVDFAYTIDCCELGE-VVYENFNAASAEITITGVTAHPM--SAKGv 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 200 -INAIVVASKAISKMHIGRIDYETTSNIGHI--EGGSATnivTDEVTFTAEIRSHSMEKLAAEvthmEQCCKEAVEEMGA 276
Cdd:PRK13381 230 lVNPILMANDFISHFPRQETPEHTEGREGYIwvNDLQGN---VNKAKLKLIIRDFDLDGFEAR----KQFIEEVVAKINA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 277 CY-------EMKHEMAYPVLSLEEDCELIQDTVNAMAEERITANKMIIGGGSDANVLAGHGYKSVILGCGMINVHTVEEA 349
Cdd:PRK13381 303 KYptarvslTLTDQYSNISNSIKDDRRAVDLAFDAMKELGIEPKVIPMRGGTDGAALSAKGLPTPNLFTGAHNFHSRFEF 382
|
410
....*....|....*.
gi 547812054 350 LDTDETWKVTKVLRRL 365
Cdd:PRK13381 383 LPVSSFVKSYEVTITI 398
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-296 |
1.01e-19 |
|
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: 88.87 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 13 EMIKIYSPSKGEKEMADWIENWLRERNIPF--QSDHAGEAYggngrNIVAFVKGNTKERPLgFAAHMDqiepcrNVNPVI 90
Cdd:cd05652 7 SLVEIPSISGNEAAVGDFLAEYLESLGFTVekQPVENKDRF-----NVYAYPGSSRQPRVL-LTSHID------TVPPFI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 91 NGNIisTDKTTTLGG----DDKAGISAIMEAVEDIIESG-VPHRDIYLVFTCSEEISMMGTKHMDMSMLPCKELVVV-DA 164
Cdd:cd05652 75 PYSI--SDGGDTIYGrgsvDAKGSVAAQIIAVEELLAEGeVPEGDLGLLFVVGEETGGDGMKAFNDLGLNTWDAVIFgEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 165 TGGAETLAYKApaMEAIEITFKGKKAHAGIePEKGINAI---VVASKAISKMHIGRIDY--ETTSNIGHIEGGSATNIVT 239
Cdd:cd05652 153 TELKLASGHKG--MLGFKLTAKGKAGHSGY-PWLGISAIeilVEALVKLIDADLPSSELlgPTTLNIGRISGGVAANVVP 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 240 DEVTFTAEIRshsmekLAAEVTHMEQCCKEAVEEMGACY---EMKHEMAYPVLSLEEDCE 296
Cdd:cd05652 230 AAAEASVAIR------LAAGPPEVKDIVKEAVAGILTDTediEVTFTSGYGPVDLDCDVD 283
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
5-365 |
1.24e-19 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 88.66 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 5 ERLQERFIEMIKIYSPSKGEKEMADWIENWLRERNIPFQSDHAGEAYggngrNIVafVKGNTKerpLGFAAHMDQIEPCR 84
Cdd:PRK08652 2 ERAKELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIESDGEVI-----NIV--VNSKAE---LFVEVHYDTVPVRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 85 NvnPVINGNIIstdkTTTLGGDDKAGISAIMEAVEdiiESGVPHRD--IYLVFTCSEEISMMGTKHMdMSMLPCKELVVV 162
Cdd:PRK08652 72 E--FFVDGVYV----YGTGACDAKGGVAAILLALE---ELGKEFEDlnVGIAFVSDEEEGGRGSALF-AERYRPKMAIVL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 163 DATGGAETLAYKApameAIEITF--KGKKAHAGIePEKGINAIVVASKAISKM----HIGRIDYETTSNIGHIEGGSATN 236
Cdd:PRK08652 142 EPTDLKVAIAHYG----NLEAYVevKGKPSHGAC-PESGVNAIEKAFEMLEKLkellKALGKYFDPHIGIQEIIGGSPEY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 237 IVTDEVTFTAEIRshsmekLAAEVThMEQCCKEaVEEMGACYEMKHEMA--YPVLSLEEDCELIQDTVNAMAEERITANK 314
Cdd:PRK08652 217 SIPALCRLRLDAR------IPPEVE-VEDVLDE-IDPILDEYTVKYEYTeiWDGFELDEDEEIVQLLEKAMKEVGLEPEF 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 547812054 315 MIIGGGSDANVLAGHGYKSVILGCGMINV-HTVEEALDTDETWKVTKVLRRL 365
Cdd:PRK08652 289 TVMRSWTDAINFRYNGTKTVVWGPGELDLcHTKFERIDVREVEKAKEFLKAL 340
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
170-322 |
8.34e-16 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 77.64 E-value: 8.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 170 TLAYKAPAMEA----IEITFKGKKAHAGIePEKGINAIVVASKAISKMH--IGRIDYETTS---NIGHIEGGSATNIVTD 240
Cdd:cd03886 159 TVGVRSGALMAsadeFEITVKGKGGHGAS-PHLGVDPIVAAAQIVLALQtvVSRELDPLEPavvTVGKFHAGTAFNVIPD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 241 EVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPVLSLEEDC-ELIQDTVNAMAEERITANKMIIGG 319
Cdd:cd03886 238 TAVLEGTIRTFDPEVREALEARIKRLAEGIAAAYGATVELEYGYGYPAVINDPELtELVREAAKELLGEEAVVEPEPVMG 317
|
...
gi 547812054 320 GSD 322
Cdd:cd03886 318 SED 320
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
162-326 |
2.45e-15 |
|
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273857 [Multi-domain] Cd Length: 363 Bit Score: 76.23 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 162 VDATGGAETLAYKAPAMEA----IEITFKGKKAHAGiEPEKGINAIVVASKAISKMH------IGRIDYETTSnIGHIEG 231
Cdd:TIGR01891 150 PDPSIPAGTVGLRPGTIMAaadkFEVTIHGKGAHAA-RPHLGRDALDAAAQLVVALQqivsrnVDPSRPAVVS-VGIIEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 232 GSATNIVTDEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPVLSLEEdcELIQDTVNAMAEERIT 311
Cdd:TIGR01891 228 GGAPNVIPDKASMSGTVRSLDPEVRDQIIDRIERIVEGAAAMYGAKVELNYDRGLPAVTNDP--ALTQILKEVARHVVGP 305
|
170 180
....*....|....*....|
gi 547812054 312 ANKMIIG----GGSD-ANVL 326
Cdd:TIGR01891 306 ENVAEDPevtmGSEDfAYYS 325
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-366 |
5.98e-15 |
|
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: 75.57 E-value: 5.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 7 LQERFIEmIKIYSPS---KGEKEMADWIENWLRERNIP-FQSDHAGEAYGGNGRNIVAFVKGNTKERpLGFAAHMDQIEP 82
Cdd:cd05650 6 LERDLIR-IPAVNPEsggEGEKEKADYLEKKLREYGFYtLERYDAPDERGIIRPNIVAKIPGGNDKT-LWIISHLDTVPP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 83 -------CRNVNPVINGNIISTDKTTtlggDDKAGISAIMEAVEDIIESG-VPHRDIYLVFTCSEEI-SMMGTKHM--DM 151
Cdd:cd05650 84 gdlslweTDPWEPVVKDGKIYGRGVE----DNQQGIVSSLLALKAIIKNGiTPKYNFGLLFVADEEDgSEYGIQYLlnKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 152 SMLPCKELVVVDATGG--AETLAYKAPAMEAIEITFKGKKAHAGIePEKGINAIVVASKAISKMHigRIDYETTSNIGHI 229
Cdd:cd05650 160 DLFKKDDLIIVPDFGTedGEFIEIAEKSILWIKVNVKGKQCHAST-PENGINAFVAASNFALELD--ELLHEKFDEKDDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 230 EGGSAT--------------NIVTDEVTFTAEIR---SHSMEKLAAEVthmeqccKEAVEEMGACYemKHEMAYPVLSLE 292
Cdd:cd05650 237 FNPPYStfeptkkeanvpnvNTIPGYDVFYFDCRvlpTYKLDEVLKFV-------NKIISDFENSY--GAGITYEIVQKE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 293 -------EDCELIQDTVNAMAEER-ITANKMIIGGGSDANVLAGHGYKSVILGCGMINVHTVEEALDTDETWKVTKVLRR 364
Cdd:cd05650 308 qappatpEDSEIVVRLSKAIKKVRgREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYIRISHIVKDAKVFAE 387
|
..
gi 547812054 365 LM 366
Cdd:cd05650 388 ML 389
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
12-250 |
2.43e-14 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349902 [Multi-domain] Cd Length: 341 Bit Score: 73.11 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 12 IEMIKIYSPSKGEKEMADWIENWLRERNIPFQSDhageayggnGRNIVAFVKGNTKERP-LGFAAHMDQIEPCRN--VNP 88
Cdd:cd05651 7 KSLIATPSFSREEHKTADLIENYLEQKGIPFKRK---------GNNVWAENGHFDEGKPtLLLNSHHDTVKPNAGwtKDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 89 VIngNIISTDKTTTLGGDD-KAGISAIMEAVEDIIESGVPHRDIYLVFTCSEEISmmGTKHMD--MSMLPCKELVVVdat 165
Cdd:cd05651 78 FE--PVEKGGKLYGLGSNDaGASVVSLLATFLHLYSEGPLNYNLIYAASAEEEIS--GKNGIEslLPHLPPLDLAIV--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 166 gGAETLAYKAPA---MEAIEITFKGKKAHAGiEPEkGINAIVVASKAISKMHIGRIDY------ETTSNIGHIEGGSATN 236
Cdd:cd05651 151 -GEPTEMQPAIAekgLLVLDCTARGKAGHAA-RNE-GDNAIYKALDDIQWLRDFRFDKvspllgPVKMTVTQINAGTQHN 227
|
250
....*....|....
gi 547812054 237 IVTDEVTFTAEIRS 250
Cdd:cd05651 228 VVPDSCTFVVDIRT 241
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
182-273 |
2.95e-14 |
|
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: 68.14 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 182 EITFKGKKAHAGIePEKGINAIVVASKAISKMH-----IGRIDYETTSNIGHIEGGSATNIVTDEVTFTAEIRSHSMEKL 256
Cdd:pfam07687 10 HLTVKGKAGHSGA-PGKGVNAIKLLARLLAELPaeygdIGFDFPRTTLNITGIEGGTATNVIPAEAEAKFDIRLLPGEDL 88
|
90
....*....|....*..
gi 547812054 257 AAEVTHMEQCCKEAVEE 273
Cdd:pfam07687 89 EELLEEIEAILEKELPE 105
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
21-366 |
9.76e-14 |
|
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.
Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 71.79 E-value: 9.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 21 SKGEKEMADWIENWLRERNIPFQSDHAGeayggngrNIVAFVKGNTKERP-LGFAAHMDqiepcrnvnpvingniistdk 99
Cdd:cd03884 25 TDEDRAARDLFVEWMEEAGLSVRVDAVG--------NLFGRLEGTDPDAPpVLTGSHLD--------------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 100 TTTLGG--DDKAGISAIMEAVEDIIESGV-PHRDIYLVFTCSEE-----ISMMGTKHMDMSMLPCKELVVVDATG----- 166
Cdd:cd03884 76 TVPNGGryDGILGVLAGLEALRALKEAGIrPRRPIEVVAFTNEEgsrfpPSMLGSRAFAGTLDLEELLSLRDADGvslae 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 167 ---------GAETLAYKAPAMEA-----IE-------------------------ITFKGKKAHAGIEP-EKGINAIVVA 206
Cdd:cd03884 156 alkaigydgDRPASARRPGDIKAyvelhIEqgpvleeeglpigvvtgiagqrwleVTVTGEAGHAGTTPmALRRDALLAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 207 SKAISKMH--IGRIDYETTSNIGHIEGG-SATNIVTDEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHE 283
Cdd:cd03884 236 AELILAVEeiALEHGDDLVATVGRIEVKpNAVNVIPGEVEFTLDLRHPDDAVLDAMVERIRAEAEAIAAERGVEVEVERL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 284 MAYPVLSLEEDCeliQDTVNAMAEER-ITANKMIIGGGSDANVLAGHGyksvilGCGMINV-------HTVEEALDTDET 355
Cdd:cd03884 316 WDSPPVPFDPEL---VAALEAAAEALgLSYRRMPSGAGHDAMFMARIC------PTAMIFVpsrdgisHNPAEYTSPEDL 386
|
410
....*....|.
gi 547812054 356 WKVTKVLRRLM 366
Cdd:cd03884 387 AAGVQVLLHAL 397
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
13-353 |
1.38e-13 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 71.59 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 13 EMIKIYSPSK---GEKEMADWIENWLRERNIPFQSDHAGEAyggNGRNIVAFVKGNTKERPLgFAAHMDQI--------E 81
Cdd:PRK06133 45 ELVSIESGSGdaeGLKQVAALLAERLKALGAKVERAPTPPS---AGDMVVATFKGTGKRRIM-LIAHMDTVylpgmlakQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 82 PCRnvnpvingniISTDKTTTLG-GDDKAGISAIMEAVEDIIESGVphRD---IYLVFTCSEEISMMGTKHMdMSMLPCK 157
Cdd:PRK06133 121 PFR----------IDGDRAYGPGiADDKGGVAVILHALKILQQLGF--KDygtLTVLFNPDEETGSPGSREL-IAELAAQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 158 ELVVV--DATGGAETLAYKAPAMEAIEITFKGKKAHAGIEPEKGINAIVVASKAISKMH-IGRIDYETTSNIGHIEGGSA 234
Cdd:PRK06133 188 HDVVFscEPGRAKDALTLATSGIATALLEVKGKASHAGAAPELGRNALYELAHQLLQLRdLGDPAKGTTLNWTVAKAGTN 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 235 TNIVTDEVTFTAEIRShsmeKLAAEVTHMEQCCKEAVEEM---GACYEMKHEMAYPVLSLEEDCELIQDTVNAMAEE--- 308
Cdd:PRK06133 268 RNVIPASASAQADVRY----LDPAEFDRLEADLQEKVKNKlvpDTEVTLRFERGRPPLEANAASRALAEHAQGIYGElgr 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 547812054 309 RITANKMIIGGGSDANVLAGHGYKSVILGCGMI--NVHTVEEALDTD 353
Cdd:PRK06133 344 RLEPIDMGTGGGTDAAFAAGSGKAAVLEGFGLVgfGAHSNDEYIELN 390
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
11-265 |
5.35e-13 |
|
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.
Pssm-ID: 349885 [Multi-domain] Cd Length: 474 Bit Score: 69.86 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 11 FIEMIKIYSPSKGEKEMADWIENWLRERNIPFQSDHAGeayggngrNIVAFV---KGNTKERPLGFAAHMDQI------- 80
Cdd:cd03890 8 FEEISKIPRPSGNEKQISDFLVKFAKKLGLEVIQDEVG--------NVIIRKpatPGYENAPPVILQGHMDMVceknads 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 81 ------EPcrnVNPVINGNIISTDKTTtLGGDDKAGISAIMEavedIIESG-VPHRDIYLVFTCSEEISMMGTKHMDMSM 153
Cdd:cd03890 80 ehdfekDP---IKLRIDGDWLKATGTT-LGADNGIGVAYALA----ILEDKdIEHPPLEVLFTVDEETGMTGALGLDPSL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 154 LPCKELVVVDA----------TGGAE---TLAYK----APAMEAIEITFKG-KKAHAGIEPEKG-INAIVVaskaiskmh 214
Cdd:cd03890 152 LKGKILLNLDSeeegeltvgcAGGIDvtiTLPIEreeaEGGYTGLKITVKGlKGGHSGVDIHKGrANANKL--------- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 547812054 215 IGRIDYETTSNIG----HIEGGSATNIVTDEVTFTAEIRSHSMEKLAAEVTHMEQ 265
Cdd:cd03890 223 MARLLYELAKELDfrlvSINGGTKRNAIPREAVAVIAVPAEDVEALKKLIKKLEK 277
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
177-289 |
7.22e-13 |
|
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 68.99 E-value: 7.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 177 AMEAIEITFKGKKAHAGiEPEKGINAIVVASKAISKMH--IGR-IDYETTS--NIGHIEGGSATNIVTDEVTFTAEIRSH 251
Cdd:COG1473 182 AADSFEITIKGKGGHAA-APHLGIDPIVAAAQIVTALQtiVSRnVDPLDPAvvTVGIIHGGTAPNVIPDEAELEGTVRTF 260
|
90 100 110
....*....|....*....|....*....|....*...
gi 547812054 252 SMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPVL 289
Cdd:COG1473 261 DPEVRELLEERIERIAEGIAAAYGATAEVEYLRGYPPT 298
|
|
| M20_ACY1L2-like |
cd05672 |
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 ... |
177-362 |
7.25e-12 |
|
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. This subfamily includes Staphylococcus aureus antibiotic resistance factor HmrA that has been shown to participate in methicillin resistance mechanisms in vivo in the presence of beta-lactams. Aminoacylase 1 (ACY1) proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349921 [Multi-domain] Cd Length: 360 Bit Score: 66.05 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 177 AMEAIEITFKGKKAHAGIEPEKGINA---IVVASKAISKM--HI---GRIDyettsniGHI-EGGSATNIVTDEVTFTAE 247
Cdd:cd05672 157 AVDKLTVEFHGKSAHAAAAPWEGINAldaAVLAYNAISALrqQLkptWRIH-------GIItEGGKAPNIIPDYAEARFY 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 248 IRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMA--YPVLSLEEDCELIQDTVNAMAEERITANKMIIGGGSD-AN 324
Cdd:cd05672 230 VRAPTRKELEELRERVIACFEGAALATGCTVEIEEDEPpyADLRPNKTLAEIYAENMEALGEEVIDDPEGVGTGSTDmGN 309
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 547812054 325 VL----AGHGYksVILGCGMINVHTVE--EALDTDE----TWKVTKVL 362
Cdd:cd05672 310 VSyvvpGIHPY--FGIPTPGAANHTPEfaEAAGTEEaheaALKAAKAL 355
|
|
| M20_Acy1L2 |
cd03887 |
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
167-362 |
1.18e-11 |
|
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, Aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase) subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349883 [Multi-domain] Cd Length: 360 Bit Score: 65.29 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 167 GAETLAYKAP-AMEAIEITFKGKKAHAGIEPEKGINA---IVVASKAISKMhigRIDYETTSNI-GHI-EGGSATNIVTD 240
Cdd:cd03887 146 GPKDVAGPKSlAVSKLRVEFHGKAAHAAAAPWEGINAldaAVLAYNNISAL---RQQLKPTVRVhGIItEGGKAPNIIPD 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 241 EVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAY--PVLSLEEDCELIQDTVNAMAEERITANKMIIG 318
Cdd:cd03887 223 YAEAEFYVRAPTLKELEELTERVIACFEGAALATGCEVEIEELEGYydELLPNKTLANIYAENMEALGEEVLDGDEGVGS 302
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 547812054 319 GGSD-ANVL----AGHGYksVILGCGMINVHTVE--EALDTDE----TWKVTKVL 362
Cdd:cd03887 303 GSTDfGNVSyvvpGIHPY--FGIPPPGAANHTPEfaEAAGTEEaheaALKAAKAL 355
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
12-365 |
2.49e-11 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 64.42 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 12 IEMIKIYSPSKGEKEMADWIENWLRERNI-PFQSDHAGeayggngrNIVAFVKGNTKERPLGFAAHMDQIEPCRN-VNPV 89
Cdd:cd03896 5 IELGEIPAPTFREGARADLVAEWMADLGLgDVERDGRG--------NVVGRLRGTGGGPALLFSAHLDTVFPGDTpATVR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 90 INGNIISTDKTttlgGDDKAGISAIMEAVEDIIESGVP-HRDIYLVFTCSEEIS--MMGTKHMDMSMLP-CKELVVVDAT 165
Cdd:cd03896 77 HEGGRIYGPGI----GDNKGSLACLLAMARAMKEAGAAlKGDVVFAANVGEEGLgdLRGARYLLSAHGArLDYFVVAEGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 166 GGaeTLAYKAPAMEAIEITFKGKKAHAgIEPEKGINAIVVASKAISKMHIGRIDY--ETTSNIGHIEGGSATNIVTDEVT 243
Cdd:cd03896 153 DG--VPHTGAVGSKRFRITTVGPGGHS-YGAFGSPSAIVAMAKLVEALYEWAAPYvpKTTFAAIRGGGGTSVNRIANLCS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 244 FTAEIRSHSmeklAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPVLSLEE-DCELIQDTVNAMaeerITANKMIIGG--- 319
Cdd:cd03896 230 MYLDIRSNP----DAELADVQREVEAVVSKLAAKHLRVKARVKPVGDRPGgEAQGTEPLVNAA----VAAHREVGGDprp 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 547812054 320 ---GSDANVLAGHGYKSVILGCGMI-NVHTVEEALDTDETWKVTKVLRRL 365
Cdd:cd03896 302 gssSTDANPANSLGIPAVTYGLGRGgNAHRGDEYVLKDDMLKGAKAYLML 351
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
14-353 |
3.69e-11 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 63.75 E-value: 3.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 14 MIKIYSPSKGEKEMADWIENWLRERNIPFQSDhageAYGGNGRNIVAFVkGNTKerP-LGFAAHMDQIEPcrnvnpvinG 92
Cdd:PRK08588 11 IVKINSVNDNEIEVANYLQDLFAKHGIESKIV----KVNDGRANLVAEI-GSGS--PvLALSGHMDVVAA---------G 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 93 NI-----------ISTDKTTTLGGDD-KAGISAIMEAVEDIIESGVP-HRDIYLVFTCSEEISMMGTKHM-------DMS 152
Cdd:PRK08588 75 DVdkwtydpfeltEKDGKLYGRGATDmKSGLAALVIAMIELKEQGQLlNGTIRLLATAGEEVGELGAKQLtekgyadDLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 153 mlpckELVVVDATGGAETLAYKApAMeAIEITFKGKKAHAGIePEKGINAIVVASKAISKMH-----IGRIDYE---TTS 224
Cdd:PRK08588 155 -----ALIIGEPSGHGIVYAHKG-SM-DYKVTSTGKAAHSSM-PELGVNAIDPLLEFYNEQKeyfdsIKKHNPYlggLTH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 225 NIGHIEGGSATNIVTDEVTFTAEIRS---HSMEKLAAEVthmeqccKEAVEEMGACYEMKHEMA-----YPVLSlEEDCE 296
Cdd:PRK08588 227 VVTIINGGEQVNSVPDEAELEFNIRTipeYDNDQVISLL-------QEIINEVNQNGAAQLSLDiysnhRPVAS-DKDSK 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547812054 297 LIQdTVNAMAEERITAN--KMIIGGGSDANVL--AGHGYKSVILGCGMINV-HTVEEALDTD 353
Cdd:PRK08588 299 LVQ-LAKDVAKSYVGQDipLSAIPGATDASSFlkKKPDFPVIIFGPGNNLTaHQVDEYVEKD 359
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
4-366 |
4.41e-11 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 63.71 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 4 RERLQERFIEMIKI-----YSPSKGEKEMADWIENWLRERNIP-FQSDHAGEAYGGNGR--NIVAFVKGNTKERPLGFAA 75
Cdd:PRK13983 4 RDEMIELLSELIAIpavnpDFGGEGEKEKAEYLESLLKEYGFDeVERYDAPDPRVIEGVrpNIVAKIPGGDGKRTLWIIS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 76 HMDQI----------EPCRnvnPVINGNII----STDktttlggDDKAGISAIMeAVEDIIESGV-PHRDIYLVFTCSEE 140
Cdd:PRK13983 84 HMDVVppgdlslwetDPFK---PVVKDGKIygrgSED-------NGQGIVSSLL-ALKALMDLGIrPKYNLGLAFVSDEE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 141 ------ISMMGTKHMDmsMLPCKELVVV-DAtgGAET-----LAYKapAMEAIEITFKGKKAHAGIePEKGINAIVVASK 208
Cdd:PRK13983 153 tgskygIQYLLKKHPE--LFKKDDLILVpDA--GNPDgsfieIAEK--SILWLKFTVKGKQCHAST-PENGINAHRAAAD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 209 AISKM------HIGRID---------YETT------SNIGHIEGgsatnivTDEVTFTAEI-RSHSMEklaaEVThmeqc 266
Cdd:PRK13983 226 FALELdealheKFNAKDplfdppystFEPTkkeanvDNINTIPG-------RDVFYFDCRVlPDYDLD----EVL----- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 267 ckEAVEEMGACYEMKH--EMAYPVLSLEE-------DCELIQDTVNAMAEER-ITANKMIIGGGSDANVLAGHGYKSVIL 336
Cdd:PRK13983 290 --KDIKEIADEFEEEYgvKIEVEIVQREQappptppDSEIVKKLKRAIKEVRgIEPKVGGIGGGTVAAFLRKKGYPAVVW 367
|
410 420 430
....*....|....*....|....*....|
gi 547812054 337 GCGMINVHTVEEALDTDETWKVTKVLRRLM 366
Cdd:PRK13983 368 STLDETAHQPNEYAKISNLIEDAKVFALLL 397
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
14-365 |
1.28e-10 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 62.07 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 14 MIKIYSPSKGEKEMADWIENWLRERNiPFQSDHageayggNGRNIVAFVKGNTKERPLgFAAHMDQIepcrnvnPVInGN 93
Cdd:cd05647 8 LVDIPSVSGNEKPIADEIEAALRTLP-HLEVIR-------DGNTVVARTERGLASRVI-LAGHLDTV-------PVA-GN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 94 IIST-DKTTTLGG----DDKAGISAIMEAVEDIIESGVPHrDIYLVFTCSEEIS--MMGTKHMDMSMlpcKELVVVD-AT 165
Cdd:cd05647 71 LPSRvEEDGVLYGcgatDMKAGDAVQLKLAATLAAATLKH-DLTLIFYDCEEVAaeLNGLGRLAEEH---PEWLAADfAV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 166 GGAETlaykAPAMEA-------IEITFKGKKAHAGiEPEKGINAIVVASKAISKMH--------IGRIDYETTSNIGHIE 230
Cdd:cd05647 147 LGEPT----DGTIEGgcqgtlrFKVTTHGVRAHSA-RSWLGENAIHKLAPILARLAayeprtvnIDGLTYREGLNAVFIS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 231 GGSATNIVTDEVTFTAEIRSHSMEKLAAEVTHMeqccKEAVEEMGACYEMKHEM--AYPVLsleeDCELIQDTVNAMAEE 308
Cdd:cd05647 222 GGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHV----REVFEGLGYEIEVTDLSpgALPGL----DHPVARDLIEAVGGK 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 547812054 309 riTANKMiigGGSDANVLAGHGYKSVILGCGMINV-HTVEEALdtdETWKVTKVLRRL 365
Cdd:cd05647 294 --VRAKY---GWTDVARFSALGIPAVNFGPGDPLLaHKRDEQV---PVEQITACAAIL 343
|
|
| PRK12890 |
PRK12890 |
allantoate amidohydrolase; Reviewed |
1-327 |
2.45e-10 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 237248 [Multi-domain] Cd Length: 414 Bit Score: 61.46 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 1 MLSRERLQERFIEMIKI-----------YSPskGEKEMADWIENWLRERNIPFQSDHAGeayggngrNIVAFVKG-NTKE 68
Cdd:PRK12890 5 PINGERLLARLEELAAIgrdgpgwtrlaLSD--EERAARALLAAWMRAAGLEVRRDAAG--------NLFGRLPGrDPDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 69 RPLGFAAHMDQiepcrnvnpVINGNIIstdktttlggDDKAGISAIMEAVEDIIESGV-PHRDIYLVFTCSEE-----IS 142
Cdd:PRK12890 75 PPLMTGSHLDT---------VPNGGRY----------DGILGVLAGLEVVAALREAGIrPPHPLEVIAFTNEEgvrfgPS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 143 MMGTKHMDMSMLPCKELVVVDATGG-----------------------AETLAY------KAPAMEA------------- 180
Cdd:PRK12890 136 MIGSRALAGTLDVEAVLATRDDDGTtlaealrriggdpdalpgalrppGAVAAFlelhieQGPVLEAeglpigvvtaiqg 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 181 ---IEITFKGKKAHAGIEPEKG-INAIVVASKAISKMH--IGRIDYETTSNIGHIE-GGSATNIVTDEVTFTAEIRSHSM 253
Cdd:PRK12890 216 irrQAVTVEGEANHAGTTPMDLrRDALVAAAELVTAMErrARALLHDLVATVGRLDvEPNAINVVPGRVVFTLDLRSPDD 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547812054 254 EKLAAEVTHMEQCCKEAVEEMGACYEM-KHEMAYPVlsleeDCE-LIQDTVNAMAEER-ITANKMIIGGGSDANVLA 327
Cdd:PRK12890 296 AVLEAAEAALLAELEAIAAARGVRIELeRLSRSEPV-----PCDpALVDAVEAAAARLgYPSRRMPSGAGHDAAAIA 367
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
19-366 |
2.65e-10 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349935 [Multi-domain] Cd Length: 379 Bit Score: 61.34 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 19 SPSKGEKEMADWIENWLRERNIPFqsdHAGEayGGNGR-NIVAFVKGNTKERPLGFAAHMDQI-------EPcrnVNPVI 90
Cdd:cd08013 23 TGGAGEAEIATYVAAWLAHRGIEA---HRIE--GTPGRpSVVGVVRGTGGGKSLMLNGHIDTVtldgydgDP---LSGEI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 91 NGNIISTDKTTtlggDDKAGISAIMEAVEDIIESGvPHRDIYLVFTCSEEISMMGTKHMDMSMLPCKELVVVDATGGAET 170
Cdd:cd08013 95 ADGRVYGRGTL----DMKGGLAACMAALADAKEAG-LRGDVILAAVADEEDASLGTQEVLAAGWRADAAIVTEPTNLQII 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 171 LAYKapAMEAIEITFKGKKAHaGIEPEKGINAIVVASKAISKMHigriDYETT-------SNIGH-------IEGGSATN 236
Cdd:cd08013 170 HAHK--GFVWFEVDIHGRAAH-GSRPDLGVDAILKAGYFLVALE----EYQQElperpvdPLLGRasvhaslIKGGEEPS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 237 IVTDEVTFTAEIRS---HSMEKLAAEVTHMEQccKEAVEEMGACYEmKHEMAY--PVLSLEEDCELIQDTVNAMAEerIT 311
Cdd:cd08013 243 SYPARCTLTIERRTipgETDESVLAELTAILG--ELAQTVPNFSYR-EPRITLsrPPFEVPKEHPFVQLVAAHAAK--VL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 547812054 312 ANKMIIGGGS---DANVLAGHGYKSVILGCGMINVHTVEEALDTDETWKVTKVLRRLM 366
Cdd:cd08013 318 GEAPQIRSETfwtDAALLAEAGIPSVVFGPSGAGLHAKEEWVDVESIRQLREVLSAVV 375
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
26-299 |
2.73e-10 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 61.36 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 26 EMADWIENWLRERNIPFQSDHAGEaygGNGRNIVAFVKGntKERPlG--FAAHMDqiepcrnVNPViNGNIISTD--KTT 101
Cdd:PRK07522 26 ALIEWVRDYLAAHGVESELIPDPE---GDKANLFATIGP--ADRG-GivLSGHTD-------VVPV-DGQAWTSDpfRLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 102 TLGG--------DDKAGISAIMEAVEDIIESGVpHRDIYLVFTCSEEISMMGTKHM--DMSMLPCK-ELVVV-DATGGAE 169
Cdd:PRK07522 92 ERDGrlygrgtcDMKGFIAAALAAVPELAAAPL-RRPLHLAFSYDEEVGCLGVPSMiaRLPERGVKpAGCIVgEPTSMRP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 170 TLAYKAPAmeAIEITFKGKKAHAGIEPeKGINAIVVASKAISkmHIGRI------------DYE---TTSNIGHIEGGSA 234
Cdd:PRK07522 171 VVGHKGKA--AYRCTVRGRAAHSSLAP-QGVNAIEYAARLIA--HLRDLadrlaapgpfdaLFDppySTLQTGTIQGGTA 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 547812054 235 TNIVTDEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVE-EM-----GACYEMKHEMAYPVLSLEEDCELIQ 299
Cdd:PRK07522 246 LNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAELLpEMravhpEAAIEFEPLSAYPGLDTAEDAAAAR 316
|
|
| M20_Acy1L2-like |
cd09849 |
M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
150-303 |
7.25e-10 |
|
M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase)-like subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli , to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349947 [Multi-domain] Cd Length: 389 Bit Score: 59.80 E-value: 7.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 150 DMSMLpckelvvVDATGGAETLAYKAPAMEAI---EITFKGKKAHAGIEPEKGINAIVVASKAISKMHIGRidyETTSNI 226
Cdd:cd09849 165 DISLM-------FHALDLGEDKALINPESNGFigkKVKFTGKESHAGSAPFSGINALNAATLAINNVNAQR---ETFKES 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 227 GHI-------EGGSATNIVTDEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAY-PVL---SLEE-- 293
Cdd:cd09849 235 DKVrfhpiitKGGDIVNVVPADVRVESYVRARSIDYMKEANSKVNRALRASAMAVGAEVEIKELPGYlPILqdrDLDNfl 314
|
170
....*....|....*
gi 547812054 294 -----DCELIQDTVN 303
Cdd:cd09849 315 kenlqDLGLIERIID 329
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
102-240 |
5.91e-09 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 57.28 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 102 TLGG----DDKAGISAIMEAVEDIIESgvPHRD---IYLVFTCSEEISMMGTKhmdmSMLpcKELvvvdATGGAETLAYK 174
Cdd:PRK07338 121 TLNGpgvaDMKGGIVVMLAALLAFERS--PLADklgYDVLINPDEEIGSPASA----PLL--AEL----ARGKHAALTYE 188
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 547812054 175 aPAMEA------------IEITFKGKKAHAGIEPEKGINAIVVASKAISKMHIGRIDYE-TTSNIGHIEGGSATNIVTD 240
Cdd:PRK07338 189 -PALPDgtlagarkgsgnFTIVVTGRAAHAGRAFDEGRNAIVAAAELALALHALNGQRDgVTVNVAKIDGGGPLNVVPD 266
|
|
| M20_Acy1_IAAspH |
cd05665 |
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, ... |
181-326 |
1.48e-08 |
|
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, bacterial and archaeal aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349915 [Multi-domain] Cd Length: 415 Bit Score: 55.79 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 181 IEITFKGKKAHAGIEPEKGINAIVVASKAISKMH-IGRIDYETTS-NIGHIEGGSATNIVTDEVTFTAEIRSHSMEKLAA 258
Cdd:cd05665 219 LDARFTGVSAHAGAAPEDGRNALLAAATAALNLHaIPRHGEGATRiNVGVLGAGEGRNVIPASAELQVETRGETTAINEY 298
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547812054 259 EVTHMEQCCKEAVEEMGACYEmkHEMAYPVLSLEEDCELIqDTVNAMAeERITANKMII-----GGGSDANVL 326
Cdd:cd05665 299 MFEQAQRVIKGAATMYGVTVE--IRTMGEAISAESDPELV-ALLREQA-ARVPGVQAVIdsaafGGSEDATLL 367
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
4-366 |
1.62e-08 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 55.93 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 4 RERLQERFIEMIKIYSPSKG----------EKEMADWIENWLRERNIPFQSDHAGeayggngrNIVAFVKGNTKERP-LG 72
Cdd:PRK09290 6 AERLWARLDELAKIGATPDGgvtrlalspeDLQARDLFAEWMEAAGLTVRVDAVG--------NLFGRLEGRDPDAPaVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 73 FAAHMDQiepcrnvnpVINGniistdktttlgG--DDKAGISAIMEAVEDIIESGV-PHRDIYLVFTCSEE-----ISMM 144
Cdd:PRK09290 78 TGSHLDT---------VPNG------------GrfDGPLGVLAGLEAVRTLNERGIrPRRPIEVVAFTNEEgsrfgPAML 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 145 GTKHM-------DMSMLPCKELVVV-----------DATGGAETLA--YKA---------PAMEA--------------- 180
Cdd:PRK09290 137 GSRVFtgaltpeDALALRDADGVSFaealaaigydgDEAVGAARARrdIKAfvelhieqgPVLEAeglpigvvtgivgqr 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 181 -IEITFKGKKAHAGIEP---EKgiNAIVVASKAISkmHIGRIDYETTSN----IGHIE---GgsATNIVTDEVTFTAEIR 249
Cdd:PRK09290 217 rYRVTFTGEANHAGTTPmalRR--DALLAAAEIIL--AVERIAAAHGPDlvatVGRLEvkpN--SVNVIPGEVTFTLDIR 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 250 SHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPVLSLEEDCeliQDTVNAMAEER-ITANKMIIGGGSDANVLAG 328
Cdd:PRK09290 291 HPDDAVLDALVAELRAAAEAIAARRGVEVEIELISRRPPVPFDPGL---VAALEEAAERLgLSYRRLPSGAGHDAQILAA 367
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 547812054 329 HgyksvilgC--GMINV-------HTVEEALDTDETWKVTKVLRRLM 366
Cdd:PRK09290 368 V--------VptAMIFVpsvggisHNPAEFTSPEDCAAGANVLLHAL 406
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
57-185 |
3.58e-08 |
|
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: 53.20 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 57 NIVAFVKGNTKERPLGFAAHMDQIePCRNVNPVINGNIISTDKTTTLGG----DDKAGISAIMEAVEDI-IESGVPHRDI 131
Cdd:cd03873 1 NLIARLGGGEGGKSVALGAHLDVV-PAGEGDNRDPPFAEDTEEEGRLYGrgalDDKGGVAAALEALKRLkENGFKPKGTI 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 547812054 132 YLVFTCSEEISMMGTKHMDMSMLPcKELVVVDATGGAETLAYKAPAME-AIEITF 185
Cdd:cd03873 80 VVAFTADEEVGSGGGKGLLSKFLL-AEDLKVDAAFVIDATAGPILQKGvVIRNPL 133
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
13-364 |
5.33e-08 |
|
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: 53.89 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 13 EMIKIYSPSKGEKEMADWIENWLRERNIPFQSDHAGEAYGGNGrnivafvkgnTKERPLGFAAHMD----QIEPcRNVNP 88
Cdd:cd05653 9 DLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEAGNAVGGAG----------SGPPDVLLLGHIDtvpgEIPV-RVEGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 89 VINGNiistdktttlGG-DDKAGISAIMEAVEDiiesGVPHRDIYLVFT--CSEEISMMGTKHMDMSMLPCKELVVVDAT 165
Cdd:cd05653 78 VLYGR----------GAvDAKGPLAAMILAASA----LNEELGARVVVAglVDEEGSSKGARELVRRGPRPDYIIIGEPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 166 GGAE-TLAYKAPAmeAIEITFKGKKAHAGiEPEKgiNAIVVASKAISKM-----HIGRIDYETTSNIGHI-EGGSATNIV 238
Cdd:cd05653 144 GWDGiTLGYRGSL--LVKIRCEGRSGHSS-SPER--NAAEDLIKKWLEVkkwaeGYNVGGRDFDSVVPTLiKGGESSNGL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 239 TDEVTFTAEIR---SHSMEKLAAEVTHMEQCCKeaVEEMGACYEMKHEMAYPvlsleedceLIQDTVNAMAEERITANKM 315
Cdd:cd05653 219 PQRAEATIDLRlppRLSPEEAIALATALLPTCE--LEFIDDTEPVKVSKNNP---------LARAFRRAIRKQGGKPRLK 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 547812054 316 IIGGGSDANVLAGHGYKSvILGCGMINV---HTVEEALDTDETWKVTKVLRR 364
Cdd:cd05653 288 RKTGTSDMNVLAPLWTVP-IVAYGPGDStldHTPNEHIELAEIERAAAVLKG 338
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
20-308 |
9.74e-08 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 53.11 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 20 PSKGEKEMADWIENWLRERNIPFQSdhageaYGGNGrnIVAFVKGNTKERPLGFAAHMD--QIEPCRN-----VNPVING 92
Cdd:cd08019 14 LSLKEERTSKRIKEELDKLGIPYVE------TGGTG--VIATIKGGKAGKTVALRADIDalPVEECTDleyksKNPGLMH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 93 NIISTDKTTTLGGddkaGISAIMEAVEDIiesgvpHRDIYLVFTCSEEISMmGTKHMdmsmlpCKELVV--VDATGGAE- 169
Cdd:cd08019 86 ACGHDGHTAMLLG----AAKILNEIKDTI------KGTVKLIFQPAEEVGE-GAKQM------IEEGVLedVDAVFGIHl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 170 --TLAY------KAPAMEA---IEITFKGKKAHaGIEPEKGINAIVVAS-------KAISKMhigrID-YET-TSNIGHI 229
Cdd:cd08019 149 wsDVPAgkisveAGPRMASadiFKIEVKGKGGH-GSMPHQGIDAVLAAAsivmnlqSIVSRE----IDpLEPvVVTVGKL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 230 EGGSATNIVTDEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPVLSLEEDCELI-QDTVNAMAEE 308
Cdd:cd08019 224 NSGTRFNVIADEAKIEGTLRTFNPETREKTPEIIERIAKHTAASYGAEAELTYGAATPPVINDEKLSKIaRQAAIKIFGE 303
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
106-149 |
1.19e-07 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 53.41 E-value: 1.19e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 547812054 106 DDKAGISAIMEAVEDIIESGV-PHRDIYLVFTCSEEISMMGTKHM 149
Cdd:PRK08262 154 DDKGSLVAILEAAEALLAQGFqPRRTIYLAFGHDEEVGGLGARAI 198
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
162-319 |
1.88e-07 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 52.27 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 162 VDATGGAETLAYKAPAM----EAIEITFKGKKAHAGIePEKGINAIVVASKAISKM-HI--GRIDYETTS--NIGHIEGG 232
Cdd:cd08021 161 LWSTLPTGTIAVRPGAImaapDEFDITIKGKGGHGSM-PHETVDPIVIAAQIVTALqTIvsRRVDPLDPAvvTIGTFQGG 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 233 SATNIVTDEV-------TFTAEIRSHSMEKlaaevthMEQCCKEAVEEMGACYEMKHEMAYPVL-SLEEDCELIQDTVN- 303
Cdd:cd08021 240 TSFNVIPDTVelkgtvrTFDEEVREQVPKR-------IERIVKGICEAYGASYELEYQPGYPVVyNDPEVTELVKKAAKe 312
|
170
....*....|....*.
gi 547812054 304 AMAEERITANKMIIGG 319
Cdd:cd08021 313 VLIGVENVEPQLMMGG 328
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
57-143 |
1.89e-07 |
|
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: 50.89 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 57 NIVAFVKGNTKERPLGFAAHMDQ--IEPCRNVNPVINGNIISTDKTTTLGG-DDKAGISAIMEAVEDIIESG-VPHRDIY 132
Cdd:cd18669 1 NVIARYGGGGGGKRVLLGAHIDVvpAGEGDPRDPPFFVDTVEEGRLYGRGAlDDKGGVAAALEALKLLKENGfKLKGTVV 80
|
90
....*....|.
gi 547812054 133 LVFTCSEEISM 143
Cdd:cd18669 81 VAFTPDEEVGS 91
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
177-289 |
2.45e-07 |
|
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349919 [Multi-domain] Cd Length: 371 Bit Score: 51.91 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 177 AMEAIEITFKGKKAHAGIePEKGINAIVVASKAISKMH------IGRIDYETTSnIGHIEGGSATNIVTDEVTFTAEIRS 250
Cdd:cd05669 171 AVDRFEIEIAGKGAHAAK-PENGVDPIVAASQIINALQtivsrnISPLESAVVS-VTRIHAGNTWNVIPDSAELEGTVRT 248
|
90 100 110
....*....|....*....|....*....|....*....
gi 547812054 251 HSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPVL 289
Cdd:cd05669 249 FDAEVRQLVKERFEQIVEGIAAAFGAKIEFKWHSGPPAV 287
|
|
| PRK15026 |
PRK15026 |
aminoacyl-histidine dipeptidase; Provisional |
2-273 |
2.86e-07 |
|
aminoacyl-histidine dipeptidase; Provisional
Pssm-ID: 184986 [Multi-domain] Cd Length: 485 Bit Score: 51.99 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 2 LSRERLQERFIEMIKIYSPSKGEKEMADWIENWLRERNIPFQSDHAGeayggngrNIV---AFVKGNTKERPLGFAAHMD 78
Cdd:PRK15026 7 LSPQPLWDIFAKICSIPHPSYHEEQLAEYIVGWAKEKGFHVERDQVG--------NILirkPATAGMENRKPVVLQAHLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 79 QIePCRN-----------VNPVINGNIISTdKTTTLGGDDKAGISAIMEAVEDiieSGVPHRDIYLVFTCSEEISMMGTK 147
Cdd:PRK15026 79 MV-PQKNndtvhdftkdpIQPYIDGEWVKA-RGTTLGADNGIGMASALAVLAD---ENVVHGPLEVLLTMTEEAGMDGAF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 148 HMDMSMLPCKELVVVDA----------TGGAETLA------YKAPA-MEAIEITFKG-KKAHAGIEPEKGINAivvASKA 209
Cdd:PRK15026 154 GLQSNWLQADILINTDSeeegeiymgcAGGIDFTSnlhldrEAVPAgFETFKLTLKGlKGGHSGGEIHVGLGN---ANKL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 547812054 210 ISKMHIGRIDyETTSNIGHIEGGSATNIVTDEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEE 273
Cdd:PRK15026 231 LVRFLAGHAE-ELDLRLIDFNGGTLRNAIPREAFATIAVAADKVDALKSLVNTYQEILKNELAE 293
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
181-364 |
3.53e-07 |
|
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: 51.79 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 181 IEITFKGKKAHAGIePEKGINAIVVASKAISKMHIGRIDYETTS-----------NIGHIEGGSATNIVTDEVTFTAEiR 249
Cdd:cd02697 187 MEVTVHGKQAHAAI-PDTGVDALQGAVAILNALYALNAQYRQVSsqvegithpylNVGRIEGGTNTNVVPGKVTFKLD-R 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 250 SHSMEKLAAEV-THMEQCCKEAVEEM-GACYEMKH-EMAYPVLSLEED---CELIQDTVNAMAEERITAnkMIIGGGSDA 323
Cdd:cd02697 265 RMIPEENPVEVeAEIRRVIADAAASMpGISVDIRRlLLANSMRPLPGNaplVEAIQTHGEAVFGEPVPA--MGTPLYTDV 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 547812054 324 NVLAGHGYKSVILGCGMINV-----HTVEEALDTDETWKVTKVLRR 364
Cdd:cd02697 343 RLYAEAGIPGVIYGAGPRTVleshaKRADERLQLEDLRRATKVIAR 388
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
181-319 |
4.58e-07 |
|
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349939 [Multi-domain] Cd Length: 365 Bit Score: 51.13 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 181 IEITFKGKKAHaGIEPEKGINAIVVASKAISKMHIGRIDYETTSNIGHIE---GGSATNIVTDEVTFTAEIRSHS---ME 254
Cdd:cd08018 170 LEGTIKGKQAH-GARPHLGINAIEAASAIVNAVNAIHLDPNIPWSVKMTKlqaGGEATNIIPDKAKFALDLRAQSneaME 248
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 547812054 255 KLAAEVTHmeqcckeAVEEMGACY------EMKHEMAYPVLSlEEDCELIQDTV-NAMAEERITANKMIIGG 319
Cdd:cd08018 249 ELKEKVEH-------AIEAAAALYgasieiTEKGGMPAAEYD-EEAVELMEEAItEVLGEEKLAGPCVTPGG 312
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
181-322 |
5.59e-07 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of uncharacterized bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349936 [Multi-domain] Cd Length: 371 Bit Score: 50.74 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 181 IEITFKGKKAHaGIEPEKGINAIVVASKAISKMH--IGR-IDYETTSNI--GHIEGGSATNIVTDEVTFTAEIRSHSMEK 255
Cdd:cd08014 173 LEIRIQGEGGH-GARPHLTVDLVWAAAQVVTDLPqaISRrIDPRSPVVLtwGSIEGGRAPNVIPDSVELSGTVRTLDPDT 251
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 547812054 256 LAAEVTHMEqcckEAVEEMGACYEMKHEMAY-----PVLSLEEDCELIQDTVNAM-AEERITANKMIIGGGSD 322
Cdd:cd08014 252 WAQLPDLVE----EIVAGICAPYGAKYELEYrrgvpPVINDPASTALLEAAVREIlGEDNVVALAEPSMGGED 320
|
|
| PRK06915 |
PRK06915 |
peptidase; |
57-362 |
8.30e-07 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 50.46 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 57 NIVAFVKGNTKERPLGFAAHMDQIePCRNVNP---------VINGNIISTDKTttlggDDKAGISAIMEAVEDIIESGVP 127
Cdd:PRK06915 82 NIVATLKGSGGGKSMILNGHIDVV-PEGDVNQwdhhpysgeVIGGRIYGRGTT-----DMKGGNVALLLAMEALIESGIE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 128 HR-DIYLvftcseeismmgtkhmdmsmlpckELVVVDATGGAETLA-----YKAPAMEAIE-----------------IT 184
Cdd:PRK06915 156 LKgDVIF------------------------QSVIEEESGGAGTLAailrgYKADGAIIPEptnmkffpkqqgsmwfrLH 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 185 FKGKKAHAGIEPEkGINAI------VVASKAISKMHIGRID---YETTS-----NIGHIEGGSATNIVTDEVTFTAEIRS 250
Cdd:PRK06915 212 VKGKAAHGGTRYE-GVSAIeksmfvIDHLRKLEEKRNDRITdplYKGIPipipiNIGKIEGGSWPSSVPDSVILEGRCGI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 251 HSMEKLAAEVTHMEQCCKE-------------AVEEMGACYEMKhemaypvlSLEEDCELIQDTVNAMaeERITANKMII 317
Cdd:PRK06915 291 APNETIEAAKEEFENWIAElndvdewfvehpvEVEWFGARWVPG--------ELEENHPLMTTLEHNF--VEIEGNKPII 360
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 547812054 318 GG---GSDANVL-AGHGYKSVILGCGMINV-HTVEEALDTDETWKVTKVL 362
Cdd:PRK06915 361 EAspwGTDGGLLtQIAGVPTIVFGPGETKVaHYPNEYIEVDKMIAAAKII 410
|
|
| FrvX |
COG1363 |
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ... |
4-80 |
8.83e-07 |
|
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];
Pssm-ID: 440974 [Multi-domain] Cd Length: 353 Bit Score: 50.13 E-value: 8.83e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 547812054 4 RERLQERFIEMIKIYSPSKGEKEMADWIENWLRERNIPFQSDHAGeayggngrNIVAFVKGNTKERPLGFAAHMDQI 80
Cdd:COG1363 1 MDYLLELLKELTEAPGPSGFEDEVREYIKEELEPLGDEVETDRLG--------NLIATKKGKGDGPKVMLAAHMDEI 69
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
176-289 |
2.28e-06 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349916 [Multi-domain] Cd Length: 373 Bit Score: 49.06 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 176 PAMEA---IEITFKGKKAHAGIePEKGINAIVVAS------KAISKMHIGRIDYETTSnIGHIEGGSATNIVTDEVTFTA 246
Cdd:cd05666 167 PMMASadtFEITIRGKGGHAAM-PHLGVDPIVAAAqlvqalQTIVSRNVDPLDAAVVS-VTQIHAGDAYNVIPDTAELRG 244
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 547812054 247 EIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPVL 289
Cdd:cd05666 245 TVRAFDPEVRDLIEERIREIADGIAAAYGATAEVDYRRGYPVT 287
|
|
| PRK12893 |
PRK12893 |
Zn-dependent hydrolase; |
181-362 |
2.48e-06 |
|
Zn-dependent hydrolase;
Pssm-ID: 237250 [Multi-domain] Cd Length: 412 Bit Score: 49.11 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 181 IEITFKGKKAHAGIEP-EKGINAIVVASKAISKMH--IGRIDYETTSNIGHI--EGGSAtNIVTDEVTFTAEIRSHSMEK 255
Cdd:PRK12893 217 LEVTVEGQAAHAGTTPmAMRRDALVAAARIILAVEriAAALAPDGVATVGRLrvEPNSR-NVIPGKVVFTVDIRHPDDAR 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 256 LAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPVLSLEEDCeliQDTVNAMAEER-ITANKMIIGGGSDANVLAGHgyksv 334
Cdd:PRK12893 296 LDAMEAALRAACAKIAAARGVQVTVETVWDFPPVPFDPAL---VALVEAAAEALgLSHMRMVSGAGHDAMFLARV----- 367
|
170 180 190
....*....|....*....|....*....|....*
gi 547812054 335 iLGCGMINV-------HTVEEALDTDETWKVTKVL 362
Cdd:PRK12893 368 -APAAMIFVpcrggisHNEAEDTEPADLAAGANVL 401
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
133-254 |
4.36e-06 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349914 [Multi-domain] Cd Length: 399 Bit Score: 48.10 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 133 LVFTCSEEiSMMGTKHM--D--MSMLPCKELVVVDATGG--AETLAYKA----PAMEAIEITFKGKKAHaGIEPEKGINA 202
Cdd:cd05664 127 AVFQPAEE-TGGGAQAMvdDglYDKIPKPDVVLAQHVMPgpAGTVGTRPgrflSAADSLDITIFGRGGH-GSMPHLTIDP 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 203 IVVASKAISKMH--IGRidyETTSN------IGHIEGGSATNIVTDEVTFTAEIRSHSME 254
Cdd:cd05664 205 VVMAASIVTRLQtiVSR---EVDPQefavvtVGSIQAGSAENIIPDEAELKLNVRTFDPE 261
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
181-308 |
5.28e-06 |
|
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349920 [Multi-domain] Cd Length: 367 Bit Score: 48.03 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 181 IEITFKGKKAHAGIePEKGINAIVVASKAISKMH------IGRIDYETTSnIGHIEGGSATNIVTDEVTFTAEIRSHSME 254
Cdd:cd05670 175 LHIDFIGKSGHAAY-PHNANDMVVAAANFVTQLQtivsrnVDPIDGAVVT-IGKIHAGTARNVIAGTAHLEGTIRTLTQE 252
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 547812054 255 KLaaevTHMEQCCKEAVEEMGACYEMKHEMA-----YPVlslEEDCELIQDTVNAMAEE 308
Cdd:cd05670 253 MM----ELVKQRVRDIAEGIELAFDCEVKVDlgqgyYPV---ENDPDLTTEFIDFMKKA 304
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
69-142 |
1.91e-05 |
|
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: 46.48 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 69 RPLGFAAHMDqiepcrnVNPV------------INGNIistdKTTTLGG----DDKAGISAIMEAVEDIIESG-VPHRDI 131
Cdd:cd05674 70 KPLLLMAHQD-------VVPVnpetedqwthppFSGHY----DGGYIWGrgalDDKNSLIGILEAVELLLKRGfKPRRTI 138
|
90
....*....|.
gi 547812054 132 YLVFTCSEEIS 142
Cdd:cd05674 139 ILAFGHDEEVG 149
|
|
| M42_glucanase_like |
cd05657 |
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ... |
6-141 |
3.29e-05 |
|
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1,4-beta-glucanase or endoglucanase)-like subfamily. Proteins in this subfamily are co-catalytic metallopeptidases, found in archaea and bacteria. They show similarity to cellulase and endo-1,4-beta-glucanase (endoglucanase) which typically bind two zinc or cobalt atoms. Some of the enzymes exhibit typical aminopeptidase specificity, whereas others are also capable of N-terminal deblocking activity, i.e. hydrolyzing acylated N-terminal residues. Many of these enzymes are assembled either as tetrahedral dodecamers or as octahedral tetracosameric structures, with the active site located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers.
Pssm-ID: 349907 [Multi-domain] Cd Length: 337 Bit Score: 45.34 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 6 RLQERFIEMIKIYSPSKGEKEMADWIENWLRERNIPFQSDHAGeayggngrNIVAFVKGNTKERPLGFAAHMDQI----- 80
Cdd:cd05657 1 YLLDLLKELLAIPSPTGYTDEAVRYLKKELEGLGVETELTNKG--------ALIATIPGKDSRKARALSAHVDTLgaivk 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 81 -----------------------EPC-----------------------------------RNVNPVINGNIISTDKTTT 102
Cdd:cd05657 73 eikpdgrlrltpiggfawnsaegENVtiitrdgktytgtvlplkasvhvygdapeaqertwDNMEVRLDEKVKSKEDVLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547812054 103 LG---G----------------------DDKAGISAIMEAVEDIIESGV-PHRDIYLVFTCSEEI 141
Cdd:cd05657 153 LGirvGdfvafdprpevtesgfiksrhlDDKASVAILLALARALKENKLkLPVDTHFLFSNYEEV 217
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
73-323 |
8.15e-05 |
|
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: 44.19 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 73 FAAHMDqiepcrnvnpvINGNIISTdktttlgG--DDKA-GISaIMEAVEDIIESGV-PHRDIYLVFTCSEEI----SMM 144
Cdd:cd05646 88 FSAHKD-----------EDGNIYAR-------GaqDMKCvGIQ-YLEAIRRLKASGFkPKRTIHLSFVPDEEIgghdGME 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 145 G-TKHMDMsmlpcKEL---VVVD---ATGGAE-TLAYKAPAMEAIEITFKGKKAH--------AGIEPEKGINAI----- 203
Cdd:cd05646 149 KfVKTEEF-----KKLnvgFALDeglASPTEEyRVFYGERSPWWVVITAPGTPGHgskllentAGEKLRKVIESImefre 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 204 --VVASKAISKMHIGRIdyeTTSNIGHIEGGSATNIVTDEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMK 281
Cdd:cd05646 224 sqKQRLKSNPNLTLGDV---TTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGRGVTYEFEQK 300
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 547812054 282 HeMAYPVLSLEED---CELIQDTVNAMaeeRITANKMIIGGGSDA 323
Cdd:cd05646 301 S-PEKDPTSLDDSnpwWAAFKKAVKEM---GLKLKPEIFPAATDS 341
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
105-362 |
8.66e-05 |
|
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: 44.22 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 105 GDDKAGISAIMEAVEDIIESGV-PHRDIYLVFTCSEEISMMGTK-------HMDMSMLP-CKELVVVDATGGAETlayka 175
Cdd:cd03895 114 GDMKAGLAANLFALDALRAAGLqPAADVHFQSVVEEECTGNGALaalmrgyRADAALIPePTELKLVRAQVGVIW----- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 176 pameaIEITFKGKKAHAGiEPEKGINAIVVASKAI---------------SKMHIGRIDYETTSNIGHIEGGSATNIVTD 240
Cdd:cd03895 189 -----FRVKVRGTPAHVA-EASEGVNAIEKAMHLIqalqelerewnarkkSHPHFSDHPHPINFNIGKIEGGDWPSSVPA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 241 EVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAY-----PVLSLEEDCELIQdtVNAMAEERITANKM 315
Cdd:cd03895 263 WCVLDCRIGIYPGESPEEARREIEECVADAAATDPWLSNHPPEVEWngfqaEGYVLEPGSDAEQ--VLAAAHQAVFGTPP 340
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 547812054 316 IIGG---GSDANVLA-GHGYKSVILGCGMINVHTVEEALDTDETWKVTKVL 362
Cdd:cd03895 341 VQSAmtaTTDGRFFVlYGDIPALCYGPGSRDAHGFDESVDLESLRKITKTI 391
|
|
| M20_Acy1-like |
cd05667 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
170-288 |
1.23e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349917 [Multi-domain] Cd Length: 403 Bit Score: 43.57 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 170 TLAYKA-PAMEA---IEITFKGKKAHaGIEPEKGINAIVVASKAISKM-HI--GRIDYETTS---NIGHIEGGSATNIVT 239
Cdd:cd05667 183 QLGYRSgPIMASadrFRITVKGKQTH-GSRPWDGIDPIMASAQIIQGLqTIisRRIDLTKEPaviSIGKINGGTRGNIIP 261
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 547812054 240 DEVTFTAEIRSHSMEKLAAEVTHMEQCCKEAVEEMGACYEMKHEMAYPV 288
Cdd:cd05667 262 EDAEMVGTIRTFDPEMREDIFARLKTIAEHIAKAYGATAEVEFANGYPV 310
|
|
| Peptidase_M28 |
pfam04389 |
Peptidase family M28; |
57-149 |
1.71e-04 |
|
Peptidase family M28;
Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 42.27 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 57 NIVAFVKGNTKERPLGFAAHMDqiepcrnvnpvingniiSTDKTTtlG-GDDKAGISAIMEAVEDIIESGVPHRDIYLVF 135
Cdd:pfam04389 1 NVIAKLPGKAPDEVVLLSAHYD-----------------SVGTGP--GaDDNASGVAALLELARVLAAGQRPKRSVRFLF 61
|
90
....*....|....
gi 547812054 136 TCSEEISMMGTKHM 149
Cdd:pfam04389 62 FDAEEAGLLGSHHF 75
|
|
| Peptidase_M42 |
pfam05343 |
M42 glutamyl aminopeptidase; These peptidases are found in Archaea and Bacteria. The example ... |
92-174 |
4.28e-04 |
|
M42 glutamyl aminopeptidase; These peptidases are found in Archaea and Bacteria. The example in Lactococcus lactis, PepA, aids growth on milk. Pyrococcus horikoshii contain a thermostable de-blocking aminopeptidase member of this family used commercially for N-terminal protein sequencing.
Pssm-ID: 428431 [Multi-domain] Cd Length: 292 Bit Score: 41.79 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 92 GNIISTDKTTT-LGG--------DDKAGISAIMEAVEDIIESGVPHrDIYLVFTCSEEISMMGTKhMDMSMLPCKELVVV 162
Cdd:pfam05343 111 GDFVVFDPEFVeLGNgrikskalDDRAGVAVLLELLKELKDEDLPA-DVYFVATVQEEVGLRGAK-TSAFKIKPDEAIAV 188
|
90
....*....|..
gi 547812054 163 DATGGAETLAYK 174
Cdd:pfam05343 189 DVTAAGDTPGSD 200
|
|
| M28_like_PA_PDZ_associated |
cd05663 |
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ... |
21-155 |
5.14e-04 |
|
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ domain; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.
Pssm-ID: 349913 [Multi-domain] Cd Length: 266 Bit Score: 41.28 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 21 SKGEKEMADWIENWLRERNI--------PFQSdhaGEAYGGNGRNIVAF--VKGNTKERPLGFAAHMDQIEpcrnvnpvi 90
Cdd:cd05663 16 TKGEKLAADYIAQRFEELGLepgldngtYFQP---FEFTTGTGRNVIGVlpGKGDVADETVVVGAHYDHLG--------- 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547812054 91 NGNIISTDKTTTL----GGDDKA-GISAIMEAVEDIIESGVP---HRDIYLVFTCSEEISMMGTKHM--DMSMLP 155
Cdd:cd05663 84 YGGEGSLARGDESlihnGADDNAsGVAAMLELAAKLVDSDTSlalSRNLVFIAFSGEELGLLGSKHFvkNPPFPI 158
|
|
| PRK12892 |
PRK12892 |
allantoate amidohydrolase; Reviewed |
183-367 |
5.18e-04 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 183817 [Multi-domain] Cd Length: 412 Bit Score: 41.62 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 183 ITFKGKKAHAGIEP-EKGINAIVVASKAISKM--HIGRIDYETTSNIGHI--EGGSAtNIVTDEVTFTAEIRSHSMEKLA 257
Cdd:PRK12892 220 ITVTGEAGHAGTTPmALRRDAGLAAAEMIAAIdeHFPRVCGPAVVTVGRValDPGSP-SIIPGRVEFSFDARHPSPPVLQ 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 258 AEVTHMEQCCKEAVEEMGACYEMKHEMAYPVLSLEEDCeliQDTVNAMAEER-ITANKMIIGGGSDANVLAghgyksVIL 336
Cdd:PRK12892 299 RLVALLEALCREIARRRGCRVSVDRIAEYAPAPCDAAL---VDALRAAAEAAgGPYLEMPSGAGHDAQNMA------RIA 369
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 547812054 337 GCGMINV-------HTVEEALDTDETWKVTKVL----RRLMG 367
Cdd:PRK12892 370 PSAMLFVpskggisHNPAEDTSPADLAQGARVLadtlRRLAR 411
|
|
| M28_like_PA |
cd05660 |
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ... |
21-148 |
2.10e-03 |
|
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.
Pssm-ID: 349910 [Multi-domain] Cd Length: 290 Bit Score: 39.65 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 21 SKGEKEMADWIENWLRE-------------RNIPFQSDHAGEayggNGRNIVAFVKGNT-KERPLGFAAHMDQIepcrnv 86
Cdd:cd05660 16 SEGEKKTVDYLAEQFKElglkpagsdgsylQAVPLVSKIEYS----TSHNVVAILPGSKlPDEYIVLSAHWDHL------ 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 547812054 87 npvinGNIISTDKTTTLGG--DDKAGISAIMEAVEDI-IESGVPHRDIYLVFTCSEEISMMGTKH 148
Cdd:cd05660 86 -----GIGPPIGGDEIYNGavDNASGVAAVLELARVFaAQDQRPKRSIVFLAVTAEEKGLLGSRY 145
|
|
| M28_like |
cd03877 |
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ... |
55-148 |
2.58e-03 |
|
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Some proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.
Pssm-ID: 349874 [Multi-domain] Cd Length: 206 Bit Score: 38.76 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 55 GRNIVAFVKGNT-KERPLGFAAHMDQIepcrnvnpvingNIISTDKTTTL--GGDDKA-GISAIMEAVEDIIESGVPHRD 130
Cdd:cd03877 1 GHNVVGVLEGSDlPDETIVIGAHYDHL------------GIGGGDSGDKIynGADDNAsGVAAVLELARYFAKQKTPKRS 68
|
90
....*....|....*...
gi 547812054 131 IYLVFTCSEEISMMGTKH 148
Cdd:cd03877 69 IVFAAFTAEEKGLLGSKY 86
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
177-281 |
4.03e-03 |
|
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1L2 family contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.
Pssm-ID: 349945 [Multi-domain] Cd Length: 366 Bit Score: 38.76 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 177 AMEAIEITFKGKKAHAGIePEKGINAIVVASKAISKMHiGRIDYETTS------NIGHIEGGSATNIVTDEVTFTAEIRS 250
Cdd:cd08660 169 SVDVFEIVIKGKGGHASI-PNNSIDPIAAAGQIISGLQ-SVVSRNISSlqnavvSITRVQGGTAWNVIPDQAE*EGTVRA 246
|
90 100 110
....*....|....*....|....*....|.
gi 547812054 251 HSMEKLAAEVTHMEQCCKEAVEEMGACYEMK 281
Cdd:cd08660 247 FTKEARQAVPEH*RRVAEGIAAGYGCQAEFK 277
|
|
| M20_IAA_Hyd |
cd08017 |
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ... |
182-294 |
4.32e-03 |
|
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349938 [Multi-domain] Cd Length: 376 Bit Score: 38.84 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 547812054 182 EITFKGKKAHAGIePEKGINAIVVASKAISKMH--IGR----IDYETTSnIGHIEGGSATNIVTDEVTFTAEIRSHSMEK 255
Cdd:cd08017 172 EVVIRGKGGHAAM-PHHTVDPVVAASSAVLALQqlVSRetdpLDSQVVS-VTRFNGGHAFNVIPDSVTFGGTLRALTTEG 249
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 547812054 256 LAaevtHMEQCCKEAVEEMGACY---------EMKHEMaYPVLSLEED 294
Cdd:cd08017 250 FY----RLRQRIEEVIEGQAAVHrcnatvdfsEDERPP-YPPTVNDER 292
|
|
| |
