|
Name |
Accession |
Description |
Interval |
E-value |
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
3-370 |
0e+00 |
|
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: 533.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 3 NQKRLLDCFLELVQINSETGHEETIQPYLKDTFKKMGLNVIEDEASKNDGLGANNLICTLKSNISHqnVPKIYFTSHMDT 82
Cdd:cd05683 1 NEDRLINTFLELVQIDSETLHEKEISKVLKKKFENLGLSVIEDDAGKTTGGGAGNLICTLKADKEE--VPKILFTSHMDT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 83 VVPGKNIQPVVKEDGYVYSDGTTILGADDKAGLAAIIEAIKQIKESNLPHGQIQIIITVGEESGLVGAKAIDTRLLDADF 162
Cdd:cd05683 79 VTPGINVKPPQIADGYIYSDGTTILGADDKAGIAAILEAIRVIKEKNIPHGQIQFVITVGEESGLVGAKALDPELIDADY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 163 GYAVDASKDVGTTVIGAPTQVKIYTTIKGKTAHAST-PKKGISAINIASKAISRMKLGQVDALTTANIGKFHGGSATNII 241
Cdd:cd05683 159 GYALDSEGDVGTIIVGAPTQDKINAKIYGKTAHAGTsPEKGISAINIAAKAISNMKLGRIDEETTANIGKFQGGTATNIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 242 ADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEVLVEKSYPGFEVNETDKVTQYAISSALALGLKGDTCIAG 321
Cdd:cd05683 239 TDEVNIEAEARSLDEEKLDAQVKHMKETFETTAKEKGAHAEVEVETSYPGFKINEDEEVVKLAKRAANNLGLEINTTYSG 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488388323 322 GGSDGNIMNQYGIPSVILGVGYENIHTTSERIAIKDMYMLTRQIIKIIE 370
Cdd:cd05683 319 GGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAVLVVEIIK 367
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
3-373 |
5.03e-143 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 409.83 E-value: 5.03e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 3 NQKRLLDCFLELVQINSETGHEETIQPYLKDTFKKMGLNVIEDEAskndglgaNNLICTLKSNISHqNVPKIYFTSHMDT 82
Cdd:COG2195 1 NPERLLERFLEYVKIPTPSDHEEALADYLVEELKELGLEVEEDEA--------GNVIATLPATPGY-NVPTIGLQAHMDT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 83 V--VPGKNIQPVVkEDGYVYSDGTTILGADDKAGLAAIIEAIKQIKESNLPHGQIQIIITVGEESGLVGAKAIDTRLLDA 160
Cdd:COG2195 72 VpqFPGDGIKPQI-DGGLITADGTTTLGADDKAGVAAILAALEYLKEPEIPHGPIEVLFTPDEEIGLRGAKALDVSKLGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 161 DFGYAVDASkDVGTTVIGAPTQVKIYTTIKGKTAHAST-PKKGISAINIASKAISRMKLGQVDALTTANIGKFHGGSATN 239
Cdd:COG2195 151 DFAYTLDGG-EEGELEYECAGAADAKITIKGKGGHSGDaKEKMINAIKLAARFLAALPLGRIPEETEGNEGFIHGGSATN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 240 IIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELG-GQAEVLVEKSYPGFEVNETDKVTQYAISSALALGLKGDTC 318
Cdd:COG2195 230 AIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGvGVVEVEIEDQYPNWKPEPDSPIVDLAKEAYEELGIEPKIK 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 488388323 319 IAGGGSDGNIMNQYGIPSVILGVGYENIHTTSERIAIKDMYMLTRQIIKIIELVA 373
Cdd:COG2195 310 PIRGGLDGGILSFKGLPTPNLGPGGHNFHSPDERVSIESMEKAWELLVEILKLIA 364
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
6-370 |
3.63e-127 |
|
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: 369.65 E-value: 3.63e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 6 RLLDCFLELVQINSETGHEETIQPYLKDTFKKMGLNVIEDEaSKNDGLGANNLICTLKSNIshqNVPKIYFTSHMDTVVP 85
Cdd:TIGR01883 1 RLKKYFLELIQIDSESGKEKAILTYLKKQITKLGIPVSLDE-VPAEVSNDNNLIARLPGTV---KFDTIFFCGHMDTVPP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 86 GKNIQPVVkEDGYVYSDGTTILGADDKAGLAAIIEAIKQIKESNLPHGQIQIIITVGEESGLVGAKAIDTRLLDADFGYA 165
Cdd:TIGR01883 77 GAGPEPVV-EDGIFTSLGGTILGADDKAGVAAMLEAMDVLSTEETPHGTIEFIFTVKEELGLIGMRLFDESKITAAYGYC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 166 VDASKDVGTTVIGAPTQVKIYTTIKGKTAHAS-TPKKGISAINIASKAISRMKLGQVDALTTANIGKFHGGSATNIIADE 244
Cdd:TIGR01883 156 LDAPGEVGNIQLAAPTQVKVDATIAGKDAHAGlVPEDGISAISVARMAIHAMRLGRIDEETTANIGSFSGGVNTNIVQDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 245 VTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEVLVEKSYPGFEVNETDKVTQYAISSALALGLKGDTCIAGGGS 324
Cdd:TIGR01883 236 QLIVAEARSLSFRKAEAQVQTMRERFEQAAEKYGATLEEETRLIYEGFKIHPQHPLMNIFKKAAKKIGLKTSEIFSGGGS 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 488388323 325 DGNIMNQYGIPSVILGVGYENIHTTSERIAIKDMYMLTRQIIKIIE 370
Cdd:TIGR01883 316 DANVLNEKGVPTVNLSAGYVHAHTEKETISIEQLVKLAELVIALAE 361
|
|
| M20_peptidase_T |
cd05645 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (PepT; ... |
7-371 |
1.11e-79 |
|
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: 249.99 E-value: 1.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 7 LLDCFLELVQINSETGHEETIQPY----------LKDTFKKMGL-NVIEDEASkndglganNLICTLKSNIShQNVPKIY 75
Cdd:cd05645 1 LLERFLEYVSLDTQSKAGVRQVPStegqwkllklLKKQLEELGLiNVTLSEKG--------TLIATLPANVD-GDIPAIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 76 FTSHMDTVVP--GKNIQPVVKED-----------------------------GYVYSDGTTILGADDKAGLAAIIEAIKQ 124
Cdd:cd05645 72 FISHVDTSPDgsGKNVNPQIVENyrggdialgigdevlspvmfpvlhqllgqTLITTDGKTLLGADDKAGLAEIFTALAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 125 IKESNLPHGQIQIIITVGEESGLvGAKAIDTRLLDADFGYAVDaSKDVGTTVIGAPTQVKIYTTIKGKTAHAST-PKKGI 203
Cdd:cd05645 152 LKEKNIPHGDIEVAFTPDEEVGK-GAKHFDVEAFTAKWAYTVD-GGGVGELEFENFNAASVNIKIVGNNVHPGTaKGVGV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 204 SAINIASKAISRMK-----LGQVDALTTANIGKFHGGsatniiADEVTLEAEARSHDDQSINKQVKHMKETFETTANEL- 277
Cdd:cd05645 230 NALSLAARIHAEVPadespEGTEGYEGFYHLASFKGT------VDRAQIHYIIRDFDRKQFEARKRK*KEIAKKVGKGLh 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 278 -GGQAEVLVEKSYPGFE--VNETDKVTQYAISSALALGLKGDTCIAGGGSDGNIMNQYGIPSVILGVGYENIHTTSERIA 354
Cdd:cd05645 304 pDCYIELVIEDSYYNFRekVVEHPHILDIAQQAARDCGITPELKPIRGGTDGAQLSFHGLPCPNLFTGGYNYHGKHEFVT 383
|
410
....*....|....*..
gi 488388323 355 IKDMYMLTRQIIKIIEL 371
Cdd:cd05645 384 LEGLEKAVQVIVRIAEL 400
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
3-374 |
4.35e-63 |
|
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: 206.27 E-value: 4.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 3 NQKRLLDCFLELVQINSETGHEETIQPYLKDTFKKMGLNVIEDEASKndglGANNLICTLKSNISHqnvPKIYFTSHMDT 82
Cdd:COG0624 10 HLDEALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPP----GRPNLVARRPGDGGG---PTLLLYGHLDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 83 VVPGKNIQ------PVVKEDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNL-PHGQIQIIITVGEESGLVGAKAI-- 153
Cdd:COG0624 83 VPPGDLELwtsdpfEPTIEDGRLYGRGA----ADMKGGLAAMLAALRALLAAGLrLPGNVTLLFTGDEEVGSPGARALve 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 154 -DTRLLDADFGYAVDASkDVGTTVIGAPTQVKIYTTIKGKTAHASTPKKGISAINIASKAISRMK----LGQVDAL---T 225
Cdd:COG0624 159 eLAEGLKADAAIVGEPT-GVPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRdlefDGRADPLfgrT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 226 TANIGKFHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELggQAEV-LVEKSYPGFEVNETDKVTQYA 304
Cdd:COG0624 238 TLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGV--EVEVeVLGDGRPPFETPPDSPLVAAA 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488388323 305 ISSALAL-GLKGDTCIAGGGSDGN-IMNQYGIPSVILGVG-YENIHTTSERIAIKDMYMLTRQIIKIIELVAE 374
Cdd:COG0624 316 RAAIREVtGKEPVLSGVGGGTDARfFAEALGIPTVVFGPGdGAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
11-373 |
7.99e-46 |
|
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: 160.54 E-value: 7.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 11 FLE-LVQINSETGHEETIQPYLKDTFKKMGLNvIEDEASKndglGANNLICTlksnISHQNVPKIYFTSHMDTVVPGKNI 89
Cdd:cd08659 2 LLQdLVQIPSVNPPEAEVAEYLAELLAKRGYG-IESTIVE----GRGNLVAT----VGGGDGPVLLLNGHIDTVPPGDGD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 90 Q------PVVKEDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNLPH-GQIQIIITVGEESGLVGAKAidtrLLDADF 162
Cdd:cd08659 73 KwsfppfSGRIRDGRLYGRGA----CDMKGGLAAMVAALIELKEAGALLgGRVALLATVDEEVGSDGARA----LLEAGY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 163 GYAVDAskdvgtTVIGAPTQVKIYT----------TIKGKTAHASTPKKGISAINIASKAISRM-----KLGQVDAL--T 225
Cdd:cd08659 145 ADRLDA------LIVGEPTGLDVVYahkgslwlrvTVHGKAAHSSMPELGVNAIYALADFLAELrtlfeELPAHPLLgpP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 226 TANIGKFHGGSATNIIADEVTLEAEARS---HDDQSINKQVKHMKETFETTANelggqAEVLVEKsYPGFEVNETDKVTQ 302
Cdd:cd08659 219 TLNVGVINGGTQVNSIPDEATLRVDIRLvpgETNEGVIARLEAILEEHEAKLT-----VEVSLDG-DPPFFTDPDHPLVQ 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488388323 303 YAISSALALGLKGDTCIAGGGSDG-NIMNQYGIPSVILGVG-YENIHTTSERIAIKDMymltRQIIKIIELVA 373
Cdd:cd08659 293 ALQAAARALGGDPVVRPFTGTTDAsYFAKDLGFPVVVYGPGdLALAHQPDEYVSLEDL----LRAAEIYKEII 361
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
76-370 |
3.36e-42 |
|
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: 149.80 E-value: 3.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 76 FTSHMDTVVPGKNIQP--VVKEDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNLPHGQIQIIITVGEESGLVGAKAI 153
Cdd:pfam01546 2 LRGHMDVVPDEETWGWpfKSTEDGKLYGRGH----DDMKGGLLAALEALRALKEEGLKKGTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 154 ------DTRLLDADFGYAVDASKD-VGTTVIG------APTQVKIytTIKGKTAHASTPKKGISAINIASKAISRMK--- 217
Cdd:pfam01546 78 iedgllEREKVDAVFGLHIGEPTLlEGGIAIGvvtghrGSLRFRV--TVKGKGGHASTPHLGVNAIVAAARLILALQdiv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 218 -----LGQVDALTTANIGKFHGGsaTNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEVLVEKSYPGF 292
Cdd:pfam01546 156 srnvdPLDPAVVTVGNITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEYVEGGAPP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 293 EVNeTDKVTQYAISSALAL-GLKGDTCIAG--GGSDGNIMNQyGIPS--VILGVGYENIHTTSERIAIKDMYMLTRQIIK 367
Cdd:pfam01546 234 LVN-DSPLVAALREAAKELfGLKVELIVSGsmGGTDAAFFLL-GVPPtvVFFGPGSGLAHSPNEYVDLDDLEKGAKVLAR 311
|
...
gi 488388323 368 IIE 370
Cdd:pfam01546 312 LLL 314
|
|
| PRK05469 |
PRK05469 |
tripeptide aminopeptidase PepT; |
5-374 |
3.25e-38 |
|
tripeptide aminopeptidase PepT;
Pssm-ID: 235484 [Multi-domain] Cd Length: 408 Bit Score: 141.42 E-value: 3.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 5 KRLLDCFLELVQINSETGHEETIQP----------YLKDTFKKMGL-NVIEDEASkndglganNLICTLKSNISHqNVPK 73
Cdd:PRK05469 2 DKLLERFLRYVKIDTQSDENSTTVPstegqwdlakLLVEELKELGLqDVTLDENG--------YVMATLPANVDK-DVPT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 74 IYFTSHMDTV--VPGKNIQP-----------VVKEDGYVYS------------------DGTTILGADDKAGLAAIIEAI 122
Cdd:PRK05469 73 IGFIAHMDTApdFSGKNVKPqiienydggdiALGDGNEVLSpaefpelknyigqtlittDGTTLLGADDKAGIAEIMTAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 123 KQIKES-NLPHGQIQIIITVGEESGLvGAKAIDTRLLDADFGYAVDASkdvgttVIG--------ApTQVKIytTIKGKT 193
Cdd:PRK05469 153 EYLIAHpEIKHGDIRVAFTPDEEIGR-GADKFDVEKFGADFAYTVDGG------PLGeleyenfnA-ASAKI--TIHGVN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 194 AHASTPK-KGISAINIASKAISRMKLGQVDALTTANIGKFHggsATNIIA--DEVTLEAEARSHDDQSINKQVKHMKETF 270
Cdd:PRK05469 223 VHPGTAKgKMVNALLLAADFHAMLPADETPETTEGYEGFYH---LTSIKGtvEEAELSYIIRDFDREGFEARKALMQEIA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 271 ETTANELGGQ-AEVLVEKSYPG-FEVNETDK-VTQYAISSALALGLKGDTCIAGGGSDGNIMNQYGIPSVILGVGYENIH 347
Cdd:PRK05469 300 KKVNAKYGEGrVELEIKDQYYNmREKIEPHPhIVDLAKQAMEDLGIEPIIKPIRGGTDGSQLSFMGLPCPNIFTGGHNFH 379
|
410 420
....*....|....*....|....*..
gi 488388323 348 TTSERIAIKDMYMLTRQIIKIIELVAE 374
Cdd:PRK05469 380 GKFEFVSLESMEKAVEVIVEIAELTAE 406
|
|
| M20_peptT |
cd03892 |
M20 Peptidase T specifically cleaves tripeptides; Peptidase M20 family, Peptidase T (peptT; ... |
7-371 |
3.44e-35 |
|
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: 133.05 E-value: 3.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 7 LLDCFLELVQINSETGHEETIQP----------YLKDTFKKMGL-NVIEDEASKndglgannLICTLKSNISHqNVPKIY 75
Cdd:cd03892 1 LLERFLRYVKIDTQSDESSETVPstegqlelakLLAKELKELGLeDVTLDEHGY--------VTATLPANVDK-DVPTIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 76 FTSHMDTV--VPGKNIQP-----------VVKEDGYVYS------------------DGTTILGADDKAGLAAIIEAIKQ 124
Cdd:cd03892 72 FIAHMDTApdNSGKNVKPqiienydggdiVLNESGIVLSpaefpelknykgqtlittDGTTLLGADDKAGIAEIMTALEY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 125 IKES-NLPHGQIQIIITVGEESGLvGAKAIDTRLLDADFGYAVDaskdvgttviGAP-----------TQVKIytTIKGK 192
Cdd:cd03892 152 LIEHpEIKHGDIRVGFTPDEEIGR-GADHFDVEKFGADFAYTLD----------GGElgeleyenfnaASATI--TITGV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 193 TAHASTPK-KGISAINIASKAISRMKLGQVDALTTANIGKFHggsATNIIA--DEVTLEAEARSHDDQSINKQVKHMKET 269
Cdd:cd03892 219 NVHPGTAKgKMVNALLLAADFHSMLPREETPEHTEGYEGFYH---LLSMEGtvEEAELSYIIRDFDRDGFEARKELIKEI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 270 FETTANELG-GQAEVLVEKSYPG-FEVNETD-KVTQYAISSALALGLKGDTCIAGGGSDGNIMNQYGIPSVILGVGYENI 346
Cdd:cd03892 296 AKKLNAKYGeGRVELEIKDQYYNmKEKIEPHmHIVDLAKEAMEALGIEPIVKPIRGGTDGARLSFMGLPTPNLFTGGHNF 375
|
410 420
....*....|....*....|....*
gi 488388323 347 HTTSERIAIKDMYMLTRQIIKIIEL 371
Cdd:cd03892 376 HGRYEFVPVESMEKAVEVIVKIAEL 400
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
7-365 |
4.33e-34 |
|
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.
Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 129.25 E-value: 4.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 7 LLDCFLELVQINSETGHEETI---QPYLKDTFKKMGLNViedEASKNDGLGaNNLICTLKsnisHQNVPKIYFTSHMDTV 83
Cdd:cd03885 1 MLDLLERLVNIESGTYDKEGVdrvAELLAEELEALGFTV---ERRPLGEFG-DHLIATFK----GTGGKRVLLIGHMDTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 84 VP-G-KNIQPVVKEDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESN-LPHGQIQIIITVGEESGLVGAKAIDTRLLD- 159
Cdd:cd03885 73 FPeGtLAFRPFTVDGDRAYGPGV----ADMKGGLVVILHALKALKAAGgRDYLPITVLLNSDEEIGSPGSRELIEEEAKg 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 160 ADFGYAVDASKDVGTTVIGAPTQVKIYTTIKGKTAHAST-PKKGISAIN-IASKAISRMKLGQVDALTTANIGKFHGGSA 237
Cdd:cd03885 149 ADYVLVFEPARADGNLVTARKGIGRFRLTVKGRAAHAGNaPEKGRSAIYeLAHQVLALHALTDPEKGTTVNVGVISGGTR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 238 TNIIADEVTLEAEAR---SHDDQSINKQVKHMKETFETTanelGGQAEVLVEKSYPGFEvnETDKVTQ-YAISSALA--L 311
Cdd:cd03885 229 VNVVPDHAEAQVDVRfatAEEADRVEEALRAIVATTLVP----GTSVELTGGLNRPPME--ETPASRRlLARAQEIAaeL 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 488388323 312 GLKGDTCIAGGGSDGNIMNQYGIPSVI-LGVGYENIHTTSERIAIKDM----YMLTRQI 365
Cdd:cd03885 303 GLTLDWEATGGGSDANFTAALGVPTLDgLGPVGGGAHTEDEYLELDSLvpriKLLARLL 361
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
7-374 |
3.18e-33 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 127.41 E-value: 3.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 7 LLDCFLELVQI---NSETGHEETIQPYLKDTFKKMGLN--VIE---DEASKNDGLGANNLICTLKSNishqnvPKIYFTS 78
Cdd:PRK08651 8 IVEFLKDLIKIptvNPPGENYEEIAEFLRDTLEELGFSteIIEvpnEYVKKHDGPRPNLIARRGSGN------PHLHFNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 79 HMDTVVPG---KNIQPV--VKEDGYVYSDGTTilgaDDKAGLAAIIEAIKQIKESNLphGQIQIIITVGEESGLVGAKAI 153
Cdd:PRK08651 82 HYDVVPPGegwSVNVPFepKVKDGKVYGRGAS----DMKGGIAALLAAFERLDPAGD--GNIELAIVPDEETGGTGTGYL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 154 DTRLLDADFGYAVDASKDVGTTVIGAPTQVKIYTTIKGKTAHASTPKKGISAINIASKAISRMKLGQVDALT-------- 225
Cdd:PRK08651 156 VEEGKVTPDYVIVGEPSGLDNICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSkyeydder 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 226 ----TANIGKF--HGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEVLVEKSYPGFEVNETD- 298
Cdd:PRK08651 236 gakpTVTLGGPtvEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFEITPFSEAFVTDPDSe 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488388323 299 --KVTQYAISSalALGLKGDTCIAGGGSDGNIMNQYGIPSVILGVG-YENIHTTSERIAIKDMymltRQIIKIIELVAE 374
Cdd:PRK08651 316 lvKALREAIRE--VLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGeLELAHAPDEYVEVKDV----EKAAKVYEEVLK 388
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
4-368 |
1.28e-29 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 117.81 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 4 QKRLLDCFLELVQINSETGHEE---TIQPYLKDTFKKMGLNViedEASKNDGLGANNLICTLKSNISHqnvpKIYFTSHM 80
Cdd:PRK06133 36 QPAYLDTLKELVSIESGSGDAEglkQVAALLAERLKALGAKV---ERAPTPPSAGDMVVATFKGTGKR----RIMLIAHM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 81 DTV-VPGK-NIQPVVKEDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNLP-HGQIQIIITVGEESGLVGAKAIDTRL 157
Cdd:PRK06133 109 DTVyLPGMlAKQPFRIDGDRAYGPGI----ADDKGGVAVILHALKILQQLGFKdYGTLTVLFNPDEETGSPGSRELIAEL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 158 L---DADFGYAVDASKD---VGTTVIGAptqvkIYTTIKGKTAHA-STPKKGISAINIASKAISRMK-LGQVDALTTANI 229
Cdd:PRK06133 185 AaqhDVVFSCEPGRAKDaltLATSGIAT-----ALLEVKGKASHAgAAPELGRNALYELAHQLLQLRdLGDPAKGTTLNW 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 230 GKFHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKetfETTANEL--GGQAEVLVEKSYPGFEVNET-DKVTQYA-- 304
Cdd:PRK06133 260 TVAKAGTNRNVIPASASAQADVRYLDPAEFDRLEADLQ---EKVKNKLvpDTEVTLRFERGRPPLEANAAsRALAEHAqg 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 305 ISSALALGLKGDTCIAGGGSDGNIMNQYGIPSVI--LGVGYENIHTTSERIAIKD----MYMLTRQIIKI 368
Cdd:PRK06133 337 IYGELGRRLEPIDMGTGGGTDAAFAAGSGKAAVLegFGLVGFGAHSNDEYIELNSivprLYLLTRMIMEL 406
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
13-359 |
5.91e-29 |
|
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: 115.57 E-value: 5.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 13 ELVQINSET---GHEETIQPYLKDTFKKMGLNVIEDEASKNDglgANNLICTLKSNISHQNVPKIYFTSHMDTVVPGKN- 88
Cdd:TIGR01910 6 DLISIPSVNppgGNEETIANYIKDLLREFGFSTDVIEITDDR---LKVLGKVVVKEPGNGNEKSLIFNGHYDVVPAGDLe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 89 ------IQPVVKeDGYVYSDGTTilgaDDKAGLAAIIEAIKQIKESNL-PHGQIQIIITVGEESGLVGAKAIDTRlldad 161
Cdd:TIGR01910 83 lwktdpFKPVEK-DGKLYGRGAT----DMKGGLVALLYALKAIREAGIkPNGNIILQSVVDEESGEAGTLYLLQR----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 162 fGYAVDAS-------KDVGTTVIGAPTQVKIYTTIKGKTAHASTPKKGISAINIASKAI-----------SRMKLGQVDA 223
Cdd:TIGR01910 153 -GYFKDADgvlipepSGGDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLItelneleehiyARNSYGFIPG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 224 LTTANIGKFHGGSATNIIADEVTLEAEARSHDDQSiNKQVKHMketFETTANELGGQAEVLVEKS--YPGFEVNETD--- 298
Cdd:TIGR01910 232 PITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEEN-LDEVKQI---IEDVVKALSKSDGWLYENEpvVKWSGPNETPpds 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488388323 299 ---KVTQYAISSalALGLKGDTCIAGGGSDGNIMNQYGIPSVILGVGY-ENIHTTSERIAIKDMY 359
Cdd:TIGR01910 308 rlvKALEAIIKK--VRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPGDlETAHQVNEYISIKNLV 370
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
14-277 |
6.43e-29 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 115.37 E-value: 6.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 14 LVQINSETGHEETIQPYLKDTFKKMGlnvIEDEASKNDGLGANnlictLKSNISHQNvPKIYFTSHMDTVVPGKNIQ--- 90
Cdd:PRK08588 11 IVKINSVNDNEIEVANYLQDLFAKHG---IESKIVKVNDGRAN-----LVAEIGSGS-PVLALSGHMDVVAAGDVDKwty 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 91 -P--VVKEDGYVYSDGTTilgaDDKAGLAAIIEAIKQIKESN-LPHGQIQIIITVGEESGLVGAKAIdtrlldADFGYAv 166
Cdd:PRK08588 82 dPfeLTEKDGKLYGRGAT----DMKSGLAALVIAMIELKEQGqLLNGTIRLLATAGEEVGELGAKQL------TEKGYA- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 167 dasKDVGTTVIGAPTQVKIY----------TTIKGKTAHASTPKKGISAINIASKAISRMK-----LGQVDAL---TTAN 228
Cdd:PRK08588 151 ---DDLDALIIGEPSGHGIVyahkgsmdykVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKeyfdsIKKHNPYlggLTHV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488388323 229 IGKFHGGSATNIIADEVTLEAEARS---HDdqsiNKQVKHmkeTFETTANEL 277
Cdd:PRK08588 228 VTIINGGEQVNSVPDEAELEFNIRTipeYD----NDQVIS---LLQEIINEV 272
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
57-358 |
1.68e-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: 111.15 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 57 NLICTLKSnishQNVPKIYFTSHMDTV-VPGKNIQ--P--VVKEDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNLp 131
Cdd:cd03894 47 NLLATLGP----GGEGGLLLSGHTDVVpVDGQKWSsdPftLTERDGRLYGRGT----CDMKGFLAAVLAAVPRLLAAKL- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 132 HGQIQIIITVGEESGLVGAKAIDTRLLDADFGYAVdaskdvgtTVIGAPTQVKIY----------TTIKGKTAHASTPKK 201
Cdd:cd03894 118 RKPLHLAFSYDEEVGCLGVRHLIAALAARGGRPDA--------AIVGEPTSLQPVvahkgiasyrIRVRGRAAHSSLPPL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 202 GISAINIASKAIS-------RMKLGQVDAL-----TTANIGKFHGGSATNIIADEVTLEAEAR---SHDDQSINKQVKhm 266
Cdd:cd03894 190 GVNAIEAAARLIGklreladRLAPGLRDPPfdppyPTLNVGLIHGGNAVNIVPAECEFEFEFRplpGEDPEAIDARLR-- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 267 keTF-ETTANELGGQAEVLVEKSYPGFEVNETDKVTQyaissaLALGLKGDTCIAG--GGSDGNIMNQYGIPSVILGVG- 342
Cdd:cd03894 268 --DYaEALLEFPEAGIEVEPLFEVPGLETDEDAPLVR------LAAALAGDNKVRTvaYGTEAGLFQRAGIPTVVCGPGs 339
|
330
....*....|....*.
gi 488388323 343 YENIHTTSERIAIKDM 358
Cdd:cd03894 340 IAQAHTPDEFVELEQL 355
|
|
| PRK13381 |
PRK13381 |
peptidase T; Provisional |
5-374 |
7.70e-27 |
|
peptidase T; Provisional
Pssm-ID: 237371 [Multi-domain] Cd Length: 404 Bit Score: 110.01 E-value: 7.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 5 KRLLDCFLELVQINSETGHEETIQP----------YLKDTFKKMGL-NVIEDEASkndglganNLICTLKSNIshQNVPK 73
Cdd:PRK13381 1 MQLTDRFFRYLKVNSQSDAASGTLPstpgqhelakLLADELRELGLeDIVIDEHA--------IVTAKLPGNT--PGAPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 74 IYFTSHMDTVVPGK--NIQPVV-----------KEDGYV------------------YSDGTTILGADDKAGLAAIIEAI 122
Cdd:PRK13381 71 IGFIAHLDTVDVGLspDIHPQIlrfdggdlclnAEQGIWlrtaehpellnyqgediiFSDGTSVLGADNKAAIAVVMTLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 123 KQIKESNLPHGQIQIIITVGEESGLVGAKAIDTRLLDADFGYAVDaSKDVGTTV---IGApTQVKIytTIKGKTAHASTP 199
Cdd:PRK13381 151 ENLTENEVEHGDIVVAFVPDEEIGLRGAKALDLARFPVDFAYTID-CCELGEVVyenFNA-ASAEI--TITGVTAHPMSA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 200 K-KGISAINIASKAISRMKLGQVDALTTANIG-----KFHGGsatniiADEVTLEAEARSHDdqsinkqvkhmKETFETT 273
Cdd:PRK13381 227 KgVLVNPILMANDFISHFPRQETPEHTEGREGyiwvnDLQGN------VNKAKLKLIIRDFD-----------LDGFEAR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 274 ANELGGQAEVLVEKsYP--GFEVNETDkvtQYA-ISSAL---------------ALGLKGDTCIAGGGSDGNIMNQYGIP 335
Cdd:PRK13381 290 KQFIEEVVAKINAK-YPtaRVSLTLTD---QYSnISNSIkddrravdlafdamkELGIEPKVIPMRGGTDGAALSAKGLP 365
|
410 420 430
....*....|....*....|....*....|....*....
gi 488388323 336 SVILGVGYENIHTTSERIAIKDMYMLTRQIIKIIELVAE 374
Cdd:PRK13381 366 TPNLFTGAHNFHSRFEFLPVSSFVKSYEVTITICLLAAK 404
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
5-288 |
3.35e-25 |
|
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: 106.07 E-value: 3.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 5 KRLLDCFLELVQINSETGHEETIQPYLKDTFKKMGLNVIEDEaskndglgANNLICTLKSNISHQNVPKIYFTSHMDtVV 84
Cdd:cd03890 2 KIVWKYFEEISKIPRPSGNEKQISDFLVKFAKKLGLEVIQDE--------VGNVIIRKPATPGYENAPPVILQGHMD-MV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 85 PGKN-----------IQPVVkEDGYVYSDGTTiLGADDKAGLAAIIeAIkqIKESNLPHGQIQIIITVGEESGLVGAKAI 153
Cdd:cd03890 73 CEKNadsehdfekdpIKLRI-DGDWLKATGTT-LGADNGIGVAYAL-AI--LEDKDIEHPPLEVLFTVDEETGMTGALGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 154 DTRLLDADFGYAVDaSKDVGTTVIGAPTQVKIYTTIKGKTAHASTPKKGI-----------SAINI------ASKAISRM 216
Cdd:cd03890 148 DPSLLKGKILLNLD-SEEEGELTVGCAGGIDVTITLPIEREEAEGGYTGLkitvkglkgghSGVDIhkgranANKLMARL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488388323 217 KLGQVDAlTTANIGKFHGGSATNIIAdevtLEAEAR-SHDDQSINKQVKHMKETFETTANELGGQ---AEVLVEKS 288
Cdd:cd03890 227 LYELAKE-LDFRLVSINGGTKRNAIP----REAVAViAVPAEDVEALKKLIKKLEKALKAEYAGTdpnLKIEVEKV 297
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
6-358 |
9.34e-25 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 103.30 E-value: 9.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 6 RLLDCFLELVQINSETGHEETIQPYLKDTFKKMGLNVIEDEasknDGLGANNLIctlksnishQNVPKIYFTSHMDTVVP 85
Cdd:PRK08652 3 RAKELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIES----DGEVINIVV---------NSKAELFVEVHYDTVPV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 86 gkNIQPVVkEDGYVYSDGTTilgaDDKAGLAAIIEAIKQIKESNLPHGqIQIIITVGEESGLVGAKAIDTRLldaDFGYA 165
Cdd:PRK08652 70 --RAEFFV-DGVYVYGTGAC----DAKGGVAAILLALEELGKEFEDLN-VGIAFVSDEEEGGRGSALFAERY---RPKMA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 166 VdaskdvgttvIGAPTQVKI----------YTTIKGKTAHASTPKKGISAINIASKAISRMK--LGQVDALTTANIG--K 231
Cdd:PRK08652 139 I----------VLEPTDLKVaiahygnleaYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKelLKALGKYFDPHIGiqE 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 232 FHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKETFEttanELGGQAEVLVEksYPGFEVNETDKVTQYAISSALAL 311
Cdd:PRK08652 209 IIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILD----EYTVKYEYTEI--WDGFELDEDEEIVQLLEKAMKEV 282
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 488388323 312 GLKGDTCIAGGGSDGNIMNQYGIPSVILGVGYENI-HTTSERIAIKDM 358
Cdd:PRK08652 283 GLEPEFTVMRSWTDAINFRYNGTKTVVWGPGELDLcHTKFERIDVREV 330
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
8-358 |
2.08e-24 |
|
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: 102.56 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 8 LDCFLELVQINSETGHEETIQPYLKDTFKKMGLNVIEdeaskNDGLGanNLICTLKSNISHqnvPKIYFTSHMDTVVPGK 87
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGLGDVE-----RDGRG--NVVGRLRGTGGG---PALLFSAHLDTVFPGD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 88 NIQPVVKEDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNLP-HGQIQIIITVGEE--SGLVGAKAIDTRLLD-ADFG 163
Cdd:cd03896 71 TPATVRHEGGRIYGPGI----GDNKGSLACLLAMARAMKEAGAAlKGDVVFAANVGEEglGDLRGARYLLSAHGArLDYF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 164 YAVDASKDVGTTVIGAPTQVKIytTIKGKTAHASTPKKGISAINIASKAISRMKLGQVDAL--TTANIGKFHGGSATNII 241
Cdd:cd03896 147 VVAEGTDGVPHTGAVGSKRFRI--TTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAPYVpkTTFAAIRGGGGTSVNRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 242 ADEVTLEAEARSH-DDQSINKQVKHMKETFETTANELGGQAEVLVEKSYPGFEVNETDKVTQYAISSALALGlkGDTCIA 320
Cdd:cd03896 225 ANLCSMYLDIRSNpDAELADVQREVEAVVSKLAAKHLRVKARVKPVGDRPGGEAQGTEPLVNAAVAAHREVG--GDPRPG 302
|
330 340 350
....*....|....*....|....*....|....*....
gi 488388323 321 GGGSDGNIMNQYGIPSVILGVGY-ENIHTTSERIAIKDM 358
Cdd:cd03896 303 SSSTDANPANSLGIPAVTYGLGRgGNAHRGDEYVLKDDM 341
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-373 |
9.78e-24 |
|
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: 100.54 E-value: 9.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 13 ELVQINSET---GHEETIQPYLKDTFKKMGL-NVIEDEASKNDGlgannlictlKSNISHQNV--PKIYFTSHMDTVVPG 86
Cdd:cd08011 6 ELVQIPSPNppgDNTSAIAAYIKLLLEDLGYpVELHEPPEEIYG----------VVSNIVGGRkgKRLLFNGHYDVVPAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 87 KNIQPVVK------EDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNLP-HGQIQIIITVGEES-GLVGAKaidtRLL 158
Cdd:cd08011 76 DGEGWTVDpysgkiKDGKLYGRGS----SDMKGGIAASIIAVARLADAKAPwDLPVVLTFVPDEETgGRAGTK----YLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 159 DADfgyavdaSKDVGTTVIGAPT-------------QVKIytTIKGKTAHASTPKKGISAINIASKAISRMKlgqvDALT 225
Cdd:cd08011 148 EKV-------RIKPNDVLIGEPSgsdnirigekglvWVII--EITGKPAHGSLPHRGESAVKAAMKLIERLY----ELEK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 226 TANIGKFHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKetfETTANELGGQAEVLVEKSYPGFEV-NETDKVTQYA 304
Cdd:cd08011 215 TVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRII---DHLDSIEEVSFEIKSFYSPTVSNPdSEIVKKTEEA 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 305 ISSalALGLKGDTCIAGGGSDGNIMNQYGIPSVILGVGY-ENIHTTSERIAIKDMYmltrQIIKIIELVA 373
Cdd:cd08011 292 ITE--VLGIRPKEVISVGASDARFYRNAGIPAIVYGPGRlGQMHAPNEYVEIDELI----KVIKVHALVA 355
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
18-345 |
1.92e-23 |
|
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: 99.98 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 18 NSETG-HEETIQPYLKDTFKKMGLNVIEdeaskndGLGANNLICTLKSnisHQNVPKIYFTSHMDTVvpgkniqPVVKED 96
Cdd:cd03886 11 HPELSfEEFRTAARIAEELRELGLEVRT-------GVGGTGVVATLKG---GGPGPTVALRADMDAL-------PIQEET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 97 GYVYS------------DG-TTILgaddkAGLAAIIEAIKQikesnLPHGQIQIIITVGEESGlVGAKA-IDTRLLDAD- 161
Cdd:cd03886 74 GLPFAskhegvmhacghDGhTAML-----LGAAKLLAERRD-----PLKGTVRFIFQPAEEGP-GGAKAmIEEGVLENPg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 162 ----FGYAVDASKDVGT------TVIGAPTQVKIytTIKGKTAHASTPKKGISAINIASKAI-------SRmklgQVDAL 224
Cdd:cd03886 143 vdaaFGLHVWPGLPVGTvgvrsgALMASADEFEI--TVKGKGGHGASPHLGVDPIVAAAQIVlalqtvvSR----ELDPL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 225 TTA--NIGKFHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEVLVEKSYPGFEVNE--TDKV 300
Cdd:cd03886 217 EPAvvTVGKFHAGTAFNVIPDTAVLEGTIRTFDPEVREALEARIKRLAEGIAAAYGATVELEYGYGYPAVINDPelTELV 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 488388323 301 TQYAIsSALALGLKGDTCIAGGGSD-GNIMNQygIPS--VILGVGYEN 345
Cdd:cd03886 297 REAAK-ELLGEEAVVEPEPVMGSEDfAYYLEK--VPGafFWLGAGEPD 341
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-294 |
3.29e-23 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal, and have been inferred by similarity as being related to both ArgE and DapE.
Pssm-ID: 349903 [Multi-domain] Cd Length: 340 Bit Score: 98.89 E-value: 3.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 13 ELVQINSETGHEETIQPYLKDTFKKMGLNVIEDEASKNDglgANNLICTLKSNIShqnvPKIYFTSHMDTVVPgkNIQPV 92
Cdd:cd05652 7 SLVEIPSISGNEAAVGDFLAEYLESLGFTVEKQPVENKD---RFNVYAYPGSSRQ----PRVLLTSHIDTVPP--FIPYS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 93 VKEDGyvysdgTTILG---ADDKAGLAAIIEAIKQIKESNL-PHGQIQIIITVGEESGLVGAKAIDTRLLdadfgyavda 168
Cdd:cd05652 78 ISDGG------DTIYGrgsVDAKGSVAAQIIAVEELLAEGEvPEGDLGLLFVVGEETGGDGMKAFNDLGL---------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 169 sKDVGTTVIGAPTQVKIYT----------TIKGKTAHASTPKKGISAINIASKA---ISRMKLGQVDAL--TTANIGKFH 233
Cdd:cd05652 142 -NTWDAVIFGEPTELKLASghkgmlgfklTAKGKAGHSGYPWLGISAIEILVEAlvkLIDADLPSSELLgpTTLNIGRIS 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488388323 234 GGSATNIIADEVTLEAEAR-SHDDQSINKQVK-----HMKETFETTANELGGQAEVLVEKSYPGFEV 294
Cdd:cd05652 221 GGVAANVVPAAAEASVAIRlAAGPPEVKDIVKeavagILTDTEDIEVTFTSGYGPVDLDCDVDGFET 287
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
13-361 |
2.37e-19 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 88.46 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 13 ELVQINSETGHEETIQPYLKDTFKKMGLNVIEdeaskNDGLGanNLICTLKSNishqnVPKIYFTSHMDTV-VPGKN--I 89
Cdd:PRK13004 23 DLIRIPSESGDEKRVVKRIKEEMEKVGFDKVE-----IDPMG--NVLGYIGHG-----KKLIAFDAHIDTVgIGDIKnwD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 90 QPVVK---EDGYVYSDGTTilgaDDKAGLAAIIEAIKQIKESNLP-HGQIQIIITVGEE--SGLVGAKAIDTRLLDADFg 163
Cdd:PRK13004 91 FDPFEgeeDDGRIYGRGTS----DQKGGMASMVYAAKIIKDLGLDdEYTLYVTGTVQEEdcDGLCWRYIIEEDKIKPDF- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 164 yavdaskdvgtTVIGAPTQVKIY----------TTIKGKTAHASTPKKGISAINIASKAISRMK-----------LGQvD 222
Cdd:PRK13004 166 -----------VVITEPTDLNIYrgqrgrmeirVETKGVSCHGSAPERGDNAIYKMAPILNELEelnpnlkedpfLGK-G 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 223 ALTTANIgKFHGGSAtNIIADEVT-------LEAEARshddQSINKQVKHMKEtfettANELGGQAEVLV--EKSY---- 289
Cdd:PRK13004 234 TLTVSDI-FSTSPSR-CAVPDSCAisidrrlTVGETW----ESVLAEIRALPA-----VKKANAKVSMYNydRPSYtglv 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 290 -------PGFEVNETDKVTQYAISSALAL-GLKGDT-----CIAGGGsdgnIMNQYGIPSVILGVGYENI-HTTSERIAI 355
Cdd:PRK13004 303 yptecyfPTWLYPEDHEFVKAAVEAYKGLfGKAPEVdkwtfSTNGVS----IAGRAGIPTIGFGPGKEPLaHAPNEYTWK 378
|
410
....*....|..
gi 488388323 356 KD------MYML 361
Cdd:PRK13004 379 EQlvkaaaMYAA 390
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
113-290 |
3.75e-19 |
|
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: 87.87 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 113 AGLAAIIEAIKQIKESnlPHGQIQIIITVGEEsGLVGAKA-IDTRLL-----DADFGYAVDASKDVGTTVIG------AP 180
Cdd:COG1473 107 AMLLGAAKALAELRDE--LKGTVRLIFQPAEE-GGGGAKAmIEDGLLdrpdvDAIFGLHVWPGLPVGTIGVRpgpimaAA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 181 TQVKIytTIKGKTAHASTPKKGISAINIASKAI-------SRmklgQVDALTTA--NIGKFHGGSATNIIADEVTLEAEA 251
Cdd:COG1473 184 DSFEI--TIKGKGGHAAAPHLGIDPIVAAAQIVtalqtivSR----NVDPLDPAvvTVGIIHGGTAPNVIPDEAELEGTV 257
|
170 180 190
....*....|....*....|....*....|....*....
gi 488388323 252 RSHDDQSINKQVKHMKETFETTANELGGQAEVLVEKSYP 290
Cdd:COG1473 258 RTFDPEVRELLEERIERIAEGIAAAYGATAEVEYLRGYP 296
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-374 |
2.68e-18 |
|
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: 85.44 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 13 ELVQINSETGHEETIQPYLKDTFKKMGLNV----IEDEASKN---------DGLGANNLICTLKSnisHQNVPK-IYFTS 78
Cdd:cd03895 5 DLVRFPSLRGEEAAAQDLVAAALRSRGYTVdrweIDVEKLKHhpgfspvavDYAGAPNVVGTHRP---RGETGRsLILNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 79 HMDTVVPGKN-------IQPVVKeDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNL-PHGQIQIIITVGEESGLVGA 150
Cdd:cd03895 82 HIDVVPEGPVelwtrppFEATIV-DGWMYGRGA----GDMKAGLAANLFALDALRAAGLqPAADVHFQSVVEEECTGNGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 151 KAIDTRlldadfGYAVDASkdvgttVIGAPTQVKIYT----------TIKGKTAHASTPKKGISAINIASKAISRMK--- 217
Cdd:cd03895 157 LAALMR------GYRADAA------LIPEPTELKLVRaqvgviwfrvKVRGTPAHVAEASEGVNAIEKAMHLIQALQele 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 218 ------------LGQVDALTTANIGKFHGGSATNIIADEVTLE-----------AEARSHDDQSINKQVKH---MKET-F 270
Cdd:cd03895 225 rewnarkkshphFSDHPHPINFNIGKIEGGDWPSSVPAWCVLDcrigiypgespEEARREIEECVADAAATdpwLSNHpP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 271 ETTANelGGQAEvlveksypGFEVNE-TDKVTQYAISSALALGLKGDTCIAGGGSDGNIMNQYG-IPSVILGVGYENIHT 348
Cdd:cd03895 305 EVEWN--GFQAE--------GYVLEPgSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGdIPALCYGPGSRDAHG 374
|
410 420
....*....|....*....|....*..
gi 488388323 349 TSERIAIKDMymltRQIIKIIEL-VAE 374
Cdd:cd03895 375 FDESVDLESL----RKITKTIALfIAE 397
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
14-364 |
3.47e-18 |
|
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: 84.80 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 14 LVQINSETGHEETIQPYLKDTFKKMG-LNVIEDeaskndglgANNLICTLKSNISHqnvpKIYFTSHMDTV-VPGkNIQP 91
Cdd:cd05647 8 LVDIPSVSGNEKPIADEIEAALRTLPhLEVIRD---------GNTVVARTERGLAS----RVILAGHLDTVpVAG-NLPS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 92 VVKEDGYVYSDGTTilgaDDKAGLAAIIEAIKQIKESNLPHGQIQIII----TVGEESGLVGAKAIDTRLLDADFGYAVD 167
Cdd:cd05647 74 RVEEDGVLYGCGAT----DMKAGDAVQLKLAATLAAATLKHDLTLIFYdceeVAAELNGLGRLAEEHPEWLAADFAVLGE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 168 ASKdvGTTVIGAPTQVKIYTTIKGKTAHASTPKKGISAINIASKAISRM-----KLGQVDALT---TANIGKFHGGSATN 239
Cdd:cd05647 150 PTD--GTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLaayepRTVNIDGLTyreGLNAVFISGGVAGN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 240 IIADEVTLEAEARSHDDQSINKQVKHMKETFEttanelGGQAEVLVEKSYPGFEVNETDKVTQYAISSalalgLKGDTCI 319
Cdd:cd05647 228 VIPDEARVNLNYRFAPDKSLAEAIAHVREVFE------GLGYEIEVTDLSPGALPGLDHPVARDLIEA-----VGGKVRA 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488388323 320 AGGGSDGNIMNQYGIPSVILGVGYENI-HTTSERIA---IKDMYMLTRQ 364
Cdd:cd05647 297 KYGWTDVARFSALGIPAVNFGPGDPLLaHKRDEQVPveqITACAAILRR 345
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
114-308 |
4.28e-18 |
|
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: 84.63 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 114 GLAAIIEAIKQ-IKesnlphGQIQIIITVGEESGLVGAKA-IDTRLL---DADFGYAVDASKDVGTTVI------GAPTQ 182
Cdd:cd08021 110 GAAKVLAENKDeIK------GTVRFIFQPAEEVPPGGAKPmIEAGVLegvDAVFGLHLWSTLPTGTIAVrpgaimAAPDE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 183 VKIytTIKGKTAHASTPKKGISAINIAS-------KAISRmklgQVDALTTA--NIGKFHGGSATNIIADEVTLEAEARS 253
Cdd:cd08021 184 FDI--TIKGKGGHGSMPHETVDPIVIAAqivtalqTIVSR----RVDPLDPAvvTIGTFQGGTSFNVIPDTVELKGTVRT 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488388323 254 HDDQSINKQVKHMKETFETTANELGGQAEVLVEKSYPgfEVNETDKVTQYAISSA 308
Cdd:cd08021 258 FDEEVREQVPKRIERIVKGICEAYGASYELEYQPGYP--VVYNDPEVTELVKKAA 310
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
116-290 |
4.63e-18 |
|
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: 84.70 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 116 AAIIEAIKQIKE-SNLPHGQIQIIITVGEESGLVGAKAIDTRLL---DADFGYAVDASKDVGTTVIGA-PT-----QVKI 185
Cdd:cd08019 94 AMLLGAAKILNEiKDTIKGTVKLIFQPAEEVGEGAKQMIEEGVLedvDAVFGIHLWSDVPAGKISVEAgPRmasadIFKI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 186 ytTIKGKTAHASTPKKGISAINIAS-------KAISRmklgQVDALTTA--NIGKFHGGSATNIIADEVTLEAEARSHDD 256
Cdd:cd08019 174 --EVKGKGGHGSMPHQGIDAVLAAAsivmnlqSIVSR----EIDPLEPVvvTVGKLNSGTRFNVIADEAKIEGTLRTFNP 247
|
170 180 190
....*....|....*....|....*....|....
gi 488388323 257 QSINKQVKHMKETFETTANELGGQAEVLVEKSYP 290
Cdd:cd08019 248 ETREKTPEIIERIAKHTAASYGAEAELTYGAATP 281
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
18-310 |
4.75e-17 |
|
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: 81.62 E-value: 4.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 18 NSETGHEE--TIQpYLKDTFKKMGLNViedeasKNDGLGANNLICTLKSnisHQNVPKIYFTSHMDTV-VPGKNIQPV-V 93
Cdd:TIGR01891 11 HPELSFEEfkTSS-LIAEALESLGIEV------RRGVGGATGVVATIGG---GKPGPVVALRADMDALpIQEQTDLPYkS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 94 KEDGYVYSDGTTILGAddkAGLAAiieAIKQIKESNLPHGQIQIIITVGEEsGLVGAKA-IDTRLL---DADFGYAVDAS 169
Cdd:TIGR01891 81 TNPGVMHACGHDLHTA---ILLGT---AKLLKKLADLLEGTVRLIFQPAEE-GGGGATKmIEDGVLddvDAILGLHPDPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 170 KDVGTTVIGAPTQV----KIYTTIKGKTAHASTPKKGISAINIASKAI-------SRmklgQVDALTTA--NIGKFHGGS 236
Cdd:TIGR01891 154 IPAGTVGLRPGTIMaaadKFEVTIHGKGAHAARPHLGRDALDAAAQLVvalqqivSR----NVDPSRPAvvSVGIIEAGG 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488388323 237 ATNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEVLVEKSYPGfeVNETDKVTQYAISSALA 310
Cdd:TIGR01891 230 APNVIPDKASMSGTVRSLDPEVRDQIIDRIERIVEGAAAMYGAKVELNYDRGLPA--VTNDPALTQILKEVARH 301
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
57-342 |
1.11e-16 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 80.62 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 57 NLICTlksnISHQNVPKIYFTSHMDtVVP--GkniQP-------VVKEDGYVYSDGTtilgADDKAGLAAIIEAIKQIKE 127
Cdd:PRK07522 54 NLFAT----IGPADRGGIVLSGHTD-VVPvdG---QAwtsdpfrLTERDGRLYGRGT----CDMKGFIAAALAAVPELAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 128 SNL--PhgqIQIIITVGEESGLVGAKAIDTRLldADFGYAVDASkdvgttVIGAPTQVKIYT----------TIKGKTAH 195
Cdd:PRK07522 122 APLrrP---LHLAFSYDEEVGCLGVPSMIARL--PERGVKPAGC------IVGEPTSMRPVVghkgkaayrcTVRGRAAH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 196 ASTPKKGISAINIASKAISRM--------KLGQVDAL-----TTANIGKFHGGSATNIIADEVTLEAEAR--SHDD-QSI 259
Cdd:PRK07522 191 SSLAPQGVNAIEYAARLIAHLrdladrlaAPGPFDALfdppySTLQTGTIQGGTALNIVPAECEFDFEFRnlPGDDpEAI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 260 NKQVKHM-KETFETTANELGGQAEVLVEK--SYPGFEVNETDKVTQyaissaLALGLKGDTCIAG--GGSDGNIMNQYGI 334
Cdd:PRK07522 271 LARIRAYaEAELLPEMRAVHPEAAIEFEPlsAYPGLDTAEDAAAAR------LVRALTGDNDLRKvaYGTEAGLFQRAGI 344
|
....*...
gi 488388323 335 PSVILGVG 342
Cdd:PRK07522 345 PTVVCGPG 352
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
30-360 |
2.06e-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: 76.73 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 30 YLKDTFKKMGLNVIEDEASKND-GLGANNLICTlksnISHQNVPKIYFTSHMDTVVPG------KNIQPVVKEDGYVYSD 102
Cdd:cd05650 31 YLEKKLREYGFYTLERYDAPDErGIIRPNIVAK----IPGGNDKTLWIISHLDTVPPGdlslweTDPWEPVVKDGKIYGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 103 GTTilgaDDKAGLAAIIEAIKQIKESNL-PHGQIQIIITVGEESG-------LVGAKAI---DTRLLDADFGyavdaSKD 171
Cdd:cd05650 107 GVE----DNQQGIVSSLLALKAIIKNGItPKYNFGLLFVADEEDGseygiqyLLNKFDLfkkDDLIIVPDFG-----TED 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 172 VGTTVIGAPTQVKIYTTIKGKTAHASTPKKGISAINIASKAISRM------KLGQVDALTTANIGKFHGGSA------TN 239
Cdd:cd05650 178 GEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFALELdellheKFDEKDDLFNPPYSTFEPTKKeanvpnVN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 240 IIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEVLVEKSYPGFEVNETDKVTQYAISSAL--ALGLKGDT 317
Cdd:cd05650 258 TIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDFENSYGAGITYEIVQKEQAPPATPEDSEIVVRLSKAIkkVRGREAKL 337
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 488388323 318 CIAGGGSDGNIMNQYGIPSVILGVGYENIHTTSERIAIKDMYM 360
Cdd:cd05650 338 IGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYIRISHIVK 380
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-358 |
2.85e-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. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 76.31 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 13 ELVQINSETGHEETIQPYLKDTFKKMGLnvieDEASKnDGLGanNLICTLKSNishqnVPKIYFTSHMDTV-VPGK---N 88
Cdd:cd05649 6 DLIQIPSESGEEKGVVERIEEEMEKLGF----DEVEI-DPMG--NVIGYIGGG-----KKKILFDGHIDTVgIGNIdnwK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 89 IQPV--VKEDGYVYSDGTTilgaDDKAGLAAIIEAIKQIKESNLPH--GQIQIIITVGEE--SGLVGAKAIDTRLLDADF 162
Cdd:cd05649 74 FDPYegYETDGKIYGRGTS----DQKGGLASMVYAAKIMKDLGLRDfaYTILVAGTVQEEdcDGVCWQYISKADKIKPDF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 163 gyavdaskdvgtTVIGAPTQVKIY----------TTIKGKTAHASTPKKGISAINIASKAISRMK-----------LGQv 221
Cdd:cd05649 150 ------------VVSGEPTDGNIYrgqrgrmeirVDTKGVSCHGSAPERGDNAVYKMADIIQDIRqlnpnfpeapfLGR- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 222 DALTTANIgkFHGGSATNIIADEVTLeaearshddqSINKQVKhMKETFETTANEL--------GGQAEVLV-------- 285
Cdd:cd05649 217 GTLTVTDI--FSTSPSRCAVPDSCRI----------SIDRRLT-VGETWEGCLEEIralpavkkYGDDVAVSmynydrps 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 286 --------EKSYPGFEVNETDKVTQYAISSALALGLKGDTC----IAGGGSdgNIMNQYGIPSVILGVGYENI-HTTSER 352
Cdd:cd05649 284 ytgevyesERYFPTWLLPEDHELVKALLEAYKALFGARPLIdkwtFSTNGV--SIMGRAGIPCIGFGPGAENQaHAPNEY 361
|
....*.
gi 488388323 353 IAIKDM 358
Cdd:cd05649 362 TWKEDL 367
|
|
| PRK06915 |
PRK06915 |
peptidase; |
13-371 |
2.42e-14 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 73.96 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 13 ELVQINSETGHEETIQPYLKDTFKKMGLNV---------IEDE----ASKNDGLGANNLICTLKSNISHQNvpkIYFTSH 79
Cdd:PRK06915 25 RLIQEKSVSGDESGAQAIVIEKLRELGLDLdiwepsfkkLKDHpyfvSPRTSFSDSPNIVATLKGSGGGKS---MILNGH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 80 MDTVVPGKNIQ----PV--VKEDGYVYSDGTTilgaDDKAGLAAIIEAIKQIKESNLP-HGQIQIIITVGEESGLVGAKA 152
Cdd:PRK06915 102 IDVVPEGDVNQwdhhPYsgEVIGGRIYGRGTT----DMKGGNVALLLAMEALIESGIElKGDVIFQSVIEEESGGAGTLA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 153 IDTRlldadfGYAVDASkdvgttVIGAPTQVKIYT----------TIKGKTAHASTPKKGISAINIASKAISRMK-LGQV 221
Cdd:PRK06915 178 AILR------GYKADGA------IIPEPTNMKFFPkqqgsmwfrlHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRkLEEK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 222 --DALTTA-----------NIGKFHGGSATNIIADEVTLEAEArshdDQSINKQVKHMKETFETTANELGGQAE------ 282
Cdd:PRK06915 246 rnDRITDPlykgipipipiNIGKIEGGSWPSSVPDSVILEGRC----GIAPNETIEAAKEEFENWIAELNDVDEwfvehp 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 283 VLVE----KSYPGfEVNETDKVTQyAISSALAlGLKGDTCI---AGGGSDGNIMNQYG-IPSVILGVG-YENIHTTSERI 353
Cdd:PRK06915 322 VEVEwfgaRWVPG-ELEENHPLMT-TLEHNFV-EIEGNKPIieaSPWGTDGGLLTQIAgVPTIVFGPGeTKVAHYPNEYI 398
|
410
....*....|....*...
gi 488388323 354 AIKDMYmltrQIIKIIEL 371
Cdd:PRK06915 399 EVDKMI----AAAKIIAL 412
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
113-325 |
4.33e-14 |
|
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349939 [Multi-domain] Cd Length: 365 Bit Score: 72.70 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 113 AGLAAIIEAIKQIKESNL-PHGQIQIIITVGEESGLvGAKA-IDTRLLD-ADFGYAV------DASKDVGTTVI--GAPT 181
Cdd:cd08018 90 AHMTMVLGAAELLKKIGLvKKGKLKFLFQPAEEKGT-GALKmIEDGVLDdVDYLFGVhlrpiqELPFGTAAPAIyhGAST 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 182 QVKIytTIKGKTAHASTPKKGISAINIASKAISRMKLGQVDAL--TTANIGKFH-GGSATNIIADEVTLEAEARSHDDQS 258
Cdd:cd08018 169 FLEG--TIKGKQAHGARPHLGINAIEAASAIVNAVNAIHLDPNipWSVKMTKLQaGGEATNIIPDKAKFALDLRAQSNEA 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488388323 259 INKQVKHMKETFETTANELGGQAEVLVEKSYPGFEVNE-TDKVTQYAISSALALGLKGDTCIAGGGSD 325
Cdd:cd08018 247 MEELKEKVEHAIEAAAALYGASIEITEKGGMPAAEYDEeAVELMEEAITEVLGEEKLAGPCVTPGGED 314
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
104-284 |
5.70e-14 |
|
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: 72.33 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 104 TTILGAddkaglaAIIeaIKQIkESNLPhGQIQIIITVGEESGLVGAKAIDTRLLD---ADFGYAVDASKDVGTTVI--G 178
Cdd:cd05669 98 ASLLGA-------AVL--LKER-EAELK-GTVRLIFQPAEETGAGAKKVIEAGALDdvsAIFGFHNKPDLPVGTIGLksG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 179 APT----QVKIytTIKGKTAHASTPKKGISAINIASKAI-------SRmklgQVDALTTA--NIGKFHGGSATNIIADEV 245
Cdd:cd05669 167 ALMaavdRFEI--EIAGKGAHAAKPENGVDPIVAASQIInalqtivSR----NISPLESAvvSVTRIHAGNTWNVIPDSA 240
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488388323 246 TLEAEARSHdDQSINKQVK-HMKETFETTANELGGQAEVL 284
Cdd:cd05669 241 ELEGTVRTF-DAEVRQLVKeRFEQIVEGIAAAFGAKIEFK 279
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
13-363 |
8.10e-14 |
|
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349886 [Multi-domain] Cd Length: 366 Bit Score: 71.77 E-value: 8.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 13 ELVQINSETGHEETIQPYLKDTFKKMGLNVIEDEASkndglGANNLICTLKSNishqnVPKIYFTSHMDTVVPGKNIQ-- 90
Cdd:cd03891 6 ELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFG-----GVKNLWARRGTG-----GPHLCFAGHTDVVPPGDLEGws 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 91 -----PVVKeDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNLPH-GQIQIIITVGEESglvgaKAID-TRlldadfg 163
Cdd:cd03891 76 sdpfsPTIK-DGMLYGRGA----ADMKGGIAAFVAAAERFVAKHPNHkGSISFLITSDEEG-----PAIDgTK------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 164 YAVDASKDVGTT----VIGAPTQ-------VKI--------YTTIKGKTAHASTPKKGISAINIASKAISR---MKLGQV 221
Cdd:cd03891 139 KVLEWLKARGEKidycIVGEPTSekklgdtIKIgrrgslngKLTIKGKQGHVAYPHLADNPIHLLAPILAEltaTVLDEG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 222 DAL---TTANIGKFHGGS-ATNIIADEVTLEAEAR---SHDDQSInkqvkhmKETFETTANELGGQAEVLVEKSYPGFeV 294
Cdd:cd03891 219 NEFfppSSLQITNIDVGNgATNVIPGELKAKFNIRfndEHTGESL-------KARIEAILDKHGLDYDLEWKLSGEPF-L 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 295 NETDKVTQYAISSALA-LGLKGDTCIAGGGSDGNIMNQYGIPSVILGVGYENIHTTSERIAIKDMYMLTR 363
Cdd:cd03891 291 TKPGKLVDAVSAAIKEvTGITPELSTSGGTSDARFIASYGCPVVEFGLVNATIHKVNERVSVADLEKLTD 360
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
17-351 |
2.85e-13 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 70.38 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 17 INSETGHE---ETIQPYLKDTFKKMGLNVIEDEASKNDGLGAN----------NLICTLKSNISHQnvpkIYFTSHMDTV 83
Cdd:PRK07338 29 INSGSRNLdglARMAELLADAFAALPGEIELIPLPPVEVIDADgrtleqahgpALHVSVRPEAPRQ----VLLTGHMDTV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 84 VP-GKNIQPVVkedgyvYSDGTTILG---ADDKAGLAAIIEAIKQIKESnlPHGQ---IQIIITVGEESGLVGAKAidtr 156
Cdd:PRK07338 105 FPaDHPFQTLS------WLDDGTLNGpgvADMKGGIVVMLAALLAFERS--PLADklgYDVLINPDEEIGSPASAP---- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 157 LLD-----ADFGYAVDASKDVGTTVIGAPTQVKIYTTIKGKTAHAS-TPKKGISAINIASKAISRMKL--GQVDALTTaN 228
Cdd:PRK07338 173 LLAelargKHAALTYEPALPDGTLAGARKGSGNFTIVVTGRAAHAGrAFDEGRNAIVAAAELALALHAlnGQRDGVTV-N 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 229 IGKFHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEVLVEKSYPGFEVNETDKVTQYAI-SS 307
Cdd:PRK07338 252 VAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHGVSLHLHGGFGRPPKPIDAAQQRLFEAVqAC 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 488388323 308 ALALGLKGDTCIAGGGSDGNIMNQYGIPSV-ILGVGYENIHTTSE 351
Cdd:PRK07338 332 GAALGLTIDWKDSGGVCDGNNLAAAGLPVVdTLGVRGGNIHSEDE 376
|
|
| FrvX |
COG1363 |
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ... |
5-167 |
2.89e-13 |
|
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];
Pssm-ID: 440974 [Multi-domain] Cd Length: 353 Bit Score: 70.16 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 5 KRLLDCFLELVQINSETGHEETIQPYLKDTFKKMGLNVIEDeaskndGLGanNLICTLKSNishQNVPKIYFTSHMDTV- 83
Cdd:COG1363 2 DYLLELLKELTEAPGPSGFEDEVREYIKEELEPLGDEVETD------RLG--NLIATKKGK---GDGPKVMLAAHMDEIg 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 84 --VpgKNIqpvvKEDGY--------------------VYSDGTTILGA-------------------------------- 109
Cdd:COG1363 71 fmV--KHI----TDNGFlrftplggwdprvlegqrvtIHTRDGDIPGVigskpphvltpeerkkpvdieelfidigassk 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 110 ----------------------------------DDKAGLAAIIEAIKQIKESNLPHgQIQIIITVGEESGLVGAKAIdT 155
Cdd:COG1363 145 eeaealgirvgdfvvfdpefeeltnsgfikskalDDRAGCAVLLELLKALKDEDLPV-TVYFVFTVQEEVGLRGASTA-A 222
|
250
....*....|..
gi 488388323 156 RLLDADFGYAVD 167
Cdd:COG1363 223 YDIKPDEAIAVD 234
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
188-274 |
4.43e-13 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 65.06 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 188 TIKGKTAHASTPKKGISAINIASKAISRMK-----LGQVDALTTANIGKFHGGSATNIIADEVTLEAEARSHDDQSINKQ 262
Cdd:pfam07687 12 TVKGKAGHSGAPGKGVNAIKLLARLLAELPaeygdIGFDFPRTTLNITGIEGGTATNVIPAEAEAKFDIRLLPGEDLEEL 91
|
90
....*....|..
gi 488388323 263 VKHMKETFETTA 274
Cdd:pfam07687 92 LEEIEAILEKEL 103
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
69-355 |
1.01e-12 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 68.66 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 69 QNVPKIYFTSHMDTVVPGKNIQ--PVVKEDGYVYSDGttILgaDDKAGLAAIIEAIKQIK----ESNLPhgqIQIIITVG 142
Cdd:PRK07473 73 QGEPGILIAGHMDTVHPVGTLEklPWRREGNKCYGPG--IL--DMKGGNYLALEAIRQLAragiTTPLP---ITVLFTPD 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 143 EESG------LVGAKAIDTRlldadFGYAVDASKDVGTTVIGAPTQVKIYTTIKGKTAHA-STPKKGISAIniasKAISR 215
Cdd:PRK07473 146 EEVGtpstrdLIEAEAARNK-----YVLVPEPGRPDNGVVTGRYAIARFNLEATGRPSHAgATLSEGRSAI----REMAR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 216 mKLGQVDALTTAN----IGKFHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMketFETTANELGGQAEVLVEKSYPG 291
Cdd:PRK07473 217 -QILAIDAMTTEDctfsVGIVHGGQWVNCVATTCTGEALSMAKRQADLDRGVARM---LALSGTEDDVTFTVTRGVTRPV 292
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488388323 292 FEVN-ETDKVTQYAISSALALGLKGDTCIAGGGSDGNIMNQYGIPSVI-LGVGYENIHTTSERIAI 355
Cdd:PRK07473 293 WEPDaGTMALYEKARAIAGQLGLSLPHGSAGGGSDGNFTGAMGIPTLDgLGVRGADYHTLNEHIEV 358
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
12-359 |
1.15e-12 |
|
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: 68.15 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 12 LELVQINSETGHEETIQPYLKDTFKKMGLNVIEDEaskndglgANNLICTLKSnishqNVPKIYFTSHMDTvVPGKniQP 91
Cdd:cd05653 8 LDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDE--------AGNAVGGAGS-----GPPDVLLLGHIDT-VPGE--IP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 92 VVKEDGYVYSDGTTilgaDDKAGLAAIIEAIKQIKESnlPHGQIQIIITVGEESGLVGAKAIDTRLLDADFgyavdaskd 171
Cdd:cd05653 72 VRVEGGVLYGRGAV----DAKGPLAAMILAASALNEE--LGARVVVAGLVDEEGSSKGARELVRRGPRPDY--------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 172 vgtTVIGAPT-----------QVKIYTTIKGKTAHASTPKKGisAINIASKAISRMKlgqvDALTTANIGKFHGGSAT-- 238
Cdd:cd05653 137 ---IIIGEPSgwdgitlgyrgSLLVKIRCEGRSGHSSSPERN--AAEDLIKKWLEVK----KWAEGYNVGGRDFDSVVpt 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 239 ----NIIADEVTLEAEARshddqsINKQVKHMKETFE--TTANELGGQAEVLVEKSYPGFEVNETDKVTQYAISSALALG 312
Cdd:cd05653 208 likgGESSNGLPQRAEAT------IDLRLPPRLSPEEaiALATALLPTCELEFIDDTEPVKVSKNNPLARAFRRAIRKQG 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488388323 313 LKGDTCIAGGGSDGNIM-NQYGIPSVILGVGYENI-HTTSERIAIKDMY 359
Cdd:cd05653 282 GKPRLKRKTGTSDMNVLaPLWTVPIVAYGPGDSTLdHTPNEHIELAEIE 330
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
103-283 |
1.33e-12 |
|
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: 68.07 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 103 GTTILGADDKAGLAAIIEAIKQIKESNLPHGQIQIIitvgEESGLVGAKAIdtrlldadFGYAVDASKDVGT--TVIGAP 180
Cdd:cd08014 99 GAALVLAALEEELPGRVRLIFQPAEETMPGGALDMI----RAGALDGVSAI--------FALHVDPRLPVGRvgVRYGPI 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 181 T----QVKIytTIKGKTAHASTPKKGISAINIASK-------AISRMklgqVDALTTANI--GKFHGGSATNIIADEVTL 247
Cdd:cd08014 167 TaaadSLEI--RIQGEGGHGARPHLTVDLVWAAAQvvtdlpqAISRR----IDPRSPVVLtwGSIEGGRAPNVIPDSVEL 240
|
170 180 190
....*....|....*....|....*....|....*.
gi 488388323 248 EAEARSHDDQSINKQVKHMKETFETTANELGGQAEV 283
Cdd:cd08014 241 SGTVRTLDPDTWAQLPDLVEEIVAGICAPYGAKYEL 276
|
|
| M20_Acy1-like |
cd05667 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
159-290 |
1.79e-11 |
|
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: 65.14 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 159 DADFGYAVDASKDVGTT------VIGAPTQVKIytTIKGKTAHASTPKKGISAINIASKAIS--------RMKLGQVDAL 224
Cdd:cd05667 168 EAIFGLHVGSGLPSGQLgyrsgpIMASADRFRI--TVKGKQTHGSRPWDGIDPIMASAQIIQglqtiisrRIDLTKEPAV 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488388323 225 TTanIGKFHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEVLVEKSYP 290
Cdd:cd05667 246 IS--IGKINGGTRGNIIPEDAEMVGTIRTFDPEMREDIFARLKTIAEHIAKAYGATAEVEFANGYP 309
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
13-235 |
2.70e-11 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 64.64 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 13 ELVQINSETGHEETIQPYLKDTFKKMGLNV----IEDEASKN---------DGLGANNLICTLKsniSHQNVPK-IYFTS 78
Cdd:PRK06837 28 DLVRFPSTRGAEAPCQDFLARAFRERGYEVdrwsIDPDDLKShpgagpveiDYSGAPNVVGTYR---PAGKTGRsLILQG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 79 HMDTVVPG-------KNIQPVVKeDGYVYSDGttilGADDKAGLAAIIEAIKQIKESNL-PHGQIQIIITVGEESGLVGA 150
Cdd:PRK06837 105 HIDVVPEGpldlwsrPPFDPVIV-DGWMYGRG----AADMKAGLAAMLFALDALRAAGLaPAARVHFQSVIEEESTGNGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 151 KAIDTRlldadfGYAVDAskdvgtTVIGAPTQVKIYTT----------IKGKTAHASTPKKGISAINIASKAISRMK--- 217
Cdd:PRK06837 180 LSTLQR------GYRADA------CLIPEPTGEKLVRAqvgviwfrlrVRGAPVHVREAGTGANAIDAAYHLIQALRele 247
|
250 260 270
....*....|....*....|....*....|
gi 488388323 218 ------------LGQVDALTTANIGKFHGG 235
Cdd:PRK06837 248 aewnarkasdphFEDVPHPINFNVGIIKGG 277
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
13-358 |
6.19e-11 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 63.10 E-value: 6.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 13 ELVQINSETGHEETIQPYLKDTFKKMGLNViedeaskndGLGANNLICTLKSniSHQNVPKIYFTSHMDTVVPGKN---- 88
Cdd:cd05651 8 SLIATPSFSREEHKTADLIENYLEQKGIPF---------KRKGNNVWAENGH--FDEGKPTLLLNSHHDTVKPNAGwtkd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 89 -IQPvVKEDGYVYSDGTTilgaDDKAGLAAIIEAIKQIKESNLPHGQIQIIITVGEE-SGLVGAKAIDTRLLDADFGyav 166
Cdd:cd05651 77 pFEP-VEKGGKLYGLGSN----DAGASVVSLLATFLHLYSEGPLNYNLIYAASAEEEiSGKNGIESLLPHLPPLDLA--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 167 daskdvgttVIGAPTQVKIYT----------TIKGKTAHASTPkKGISAINIASKAISRMK----------LGQVDALTT 226
Cdd:cd05651 149 ---------IVGEPTEMQPAIaekgllvldcTARGKAGHAARN-EGDNAIYKALDDIQWLRdfrfdkvsplLGPVKMTVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 227 anigKFHGGSATNIIADEVTLEAEARSHDDQSinkqvkhMKETFETTANELGGQAEVLVEKSYPGFeVNETDKVTQYAIs 306
Cdd:cd05651 219 ----QINAGTQHNVVPDSCTFVVDIRTTEAYT-------NEEIFEIIRGNLKSEIKPRSFRLNSSA-IPPDHPIVQAAI- 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 488388323 307 sALALGLKGDTCIagggSDGNIMNqygIPSVILGVG-YENIHTTSERIAIKDM 358
Cdd:cd05651 286 -AAGRTPFGSPTL----SDQALMP---FPSVKIGPGdSSRSHTADEFIELSEI 330
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
14-370 |
3.59e-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: 60.95 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 14 LVQINSET--------GHEETIQPYLKDTFKKMGLNVIEDEASKndglGANNLICTLKSNISHQNVpkiYFTSHMDTV-- 83
Cdd:cd08013 10 LVRINSSNpslsatggAGEAEIATYVAAWLAHRGIEAHRIEGTP----GRPSVVGVVRGTGGGKSL---MLNGHIDTVtl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 84 --VPGKNIQPVVKeDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNLpHGQIQIIITVGEESGLVGAKAIdtrlLDAd 161
Cdd:cd08013 83 dgYDGDPLSGEIA-DGRVYGRGT----LDMKGGLAACMAALADAKEAGL-RGDVILAAVADEEDASLGTQEV----LAA- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 162 fGYAVDASkdvgttVIGAPTQVKIYT----------TIKGKTAHASTPKKGISAINIASKAI-------SRMKLGQVDAL 224
Cdd:cd08013 152 -GWRADAA------IVTEPTNLQIIHahkgfvwfevDIHGRAAHGSRPDLGVDAILKAGYFLvaleeyqQELPERPVDPL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 225 T---TANIGKFHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGG-QAEVL-VEKSYPGFEVNETDK 299
Cdd:cd08013 225 LgraSVHASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTAILGELAQTVPNfSYREPrITLSRPPFEVPKEHP 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488388323 300 VTQyaISSALALGLKGDTCIAGGGS---DGNIMNQYGIPSVILGVGYENIHTTSERIAIKDMYMLTRQIIKIIE 370
Cdd:cd08013 305 FVQ--LVAAHAAKVLGEAPQIRSETfwtDAALLAEAGIPSVVFGPSGAGLHAKEEWVDVESIRQLREVLSAVVR 376
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
79-241 |
5.06e-10 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 60.22 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 79 HMDTVV--PGK-NIQP--VVKEDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNLPHgQIQIIITVGEESGLVGAKAI 153
Cdd:PRK05111 79 HTDTVPfdEGRwTRDPftLTEHDGKLYGLGT----ADMKGFFAFILEALRDIDLTKLKK-PLYILATADEETSMAGARAF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 154 -DTRLLDADfgYAvdaskdvgttVIGAPTQVK-IYT---------TIKGKTAHASTPKKGISAINIASKAISR-MKLGQV 221
Cdd:PRK05111 154 aEATAIRPD--CA----------IIGEPTSLKpVRAhkghmseaiRITGQSGHSSDPALGVNAIELMHDVIGElLQLRDE 221
|
170 180 190
....*....|....*....|....*....|.
gi 488388323 222 -------DALT----TANIGKFHGGSATNII 241
Cdd:PRK05111 222 lqeryhnPAFTvpypTLNLGHIHGGDAPNRI 252
|
|
| PRK15026 |
PRK15026 |
aminoacyl-histidine dipeptidase; Provisional |
7-171 |
1.73e-09 |
|
aminoacyl-histidine dipeptidase; Provisional
Pssm-ID: 184986 [Multi-domain] Cd Length: 485 Bit Score: 58.93 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 7 LLDCFLELVQINSETGHEETIQPYLKDTFKKMGLNVIEDEASkndglganNLICTLKSNISHQNVPKIYFTSHMDtVVPG 86
Cdd:PRK15026 12 LWDIFAKICSIPHPSYHEEQLAEYIVGWAKEKGFHVERDQVG--------NILIRKPATAGMENRKPVVLQAHLD-MVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 87 KN-----------IQPVVkeDG-YVYSDGTTiLGADDKAGLAAiieAIKQIKESNLPHGQIQIIITVGEESGLVGAKAID 154
Cdd:PRK15026 83 KNndtvhdftkdpIQPYI--DGeWVKARGTT-LGADNGIGMAS---ALAVLADENVVHGPLEVLLTMTEEAGMDGAFGLQ 156
|
170
....*....|....*..
gi 488388323 155 TRLLDADFGYAVDASKD 171
Cdd:PRK15026 157 SNWLQADILINTDSEEE 173
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
74-365 |
1.97e-09 |
|
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: 58.72 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 74 IYFTSHMDTVVPGK--NIQP--VVKEDGYVYSDGTTIlgadDKAGLAAIIEAIKQIKESNLP-HGQIQIIITVGEE-SGL 147
Cdd:cd02697 76 VALNAHGDVVPPGDgwTRDPygAVVEDGVMYGRAAAV----SKSDFASFTFAVRALESLGAPlRGAVELHFTYDEEfGGE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 148 VGAK-AIDTRLLDADFGYAVDASKDVGTTVIGAptqVKIYTTIKGKTAHASTPKKGISAINIASKAIS---------RMK 217
Cdd:cd02697 152 LGPGwLLRQGLTKPDLLIAAGFSYEVVTAHNGC---LQMEVTVHGKQAHAAIPDTGVDALQGAVAILNalyalnaqyRQV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 218 LGQVDALTTA--NIGKFHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQA----EVLVEKSY-- 289
Cdd:cd02697 229 SSQVEGITHPylNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAASMPGISvdirRLLLANSMrp 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 290 -PGFE--VNETDKVTQYAISSAL-ALGLKGDTciagggsDGNIMNQYGIPSVILGVG-----YENIHTTSERIAIKDMYM 360
Cdd:cd02697 309 lPGNAplVEAIQTHGEAVFGEPVpAMGTPLYT-------DVRLYAEAGIPGVIYGAGprtvlESHAKRADERLQLEDLRR 381
|
....*
gi 488388323 361 LTRQI 365
Cdd:cd02697 382 ATKVI 386
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
3-369 |
2.83e-09 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 58.13 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 3 NQKRLLDCFLELVQINSETG---HEETIQPYLKDTFKKMGLNVIEDEASKNDglgaNNLICTLK--SNISHQNvpkIYFT 77
Cdd:PRK08596 11 RKDELLELLKTLVRFETPAPparNTNEAQEFIAEFLRKLGFSVDKWDVYPND----PNVVGVKKgtESDAYKS---LIIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 78 SHMDTVVPGKN-------IQPVVKeDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNL-PHGQIQIIITVGEESGLVG 149
Cdd:PRK08596 84 GHMDVAEVSADeawetnpFEPTIK-DGWLYGRGA----ADMKGGLAGALFAIQLLHEAGIeLPGDLIFQSVIGEEVGEAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 150 AKAIDTRLLDADFGYAVDASK-------DVGTTVIGAPTQVKIYTTIKGKTAHASTPKKGISAINIASKAI--------- 213
Cdd:PRK08596 159 TLQCCERGYDADFAVVVDTSDlhmqgqgGVITGWITVKSPQTFHDGTRRQMIHAGGGLFGASAIEKMMKIIqslqelerh 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 214 -SRMKL--GQVDALTTANIGKFHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTAN------------ELG 278
Cdd:PRK08596 239 wAVMKSypGFPPGTNTINPAVIEGGRHAAFIADECRLWITVHFYPNETYEQVIKEIEEYIGKVAAadpwlrenppqfKWG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 279 GqAEVLVEKS--YPGFEVNET-DKVTQYAISSALALGLKGDTCIAGGGSDGNIMNQYGIPSVILGVG-YENIHTTSERIA 354
Cdd:PRK08596 319 G-ESMIEDRGeiFPSLEIDSEhPAVKTLSSAHESVLSKNAILDMSTTVTDGGWFAEFGIPAVIYGPGtLEEAHSVNEKVE 397
|
410
....*....|....*
gi 488388323 355 IKDMYMLTRQIIKII 369
Cdd:PRK08596 398 IEQLIEYTKVITAFI 412
|
|
| M20_IAA_Hyd |
cd08017 |
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ... |
96-290 |
2.92e-09 |
|
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: 58.10 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 96 DGYVysdgTTILGAddkaglAAIIEAIKQikesnLPHGQIQIIITVGEEsGLVGAKAI--DTRLLDADFGYAVDASKDVG 173
Cdd:cd08017 90 DAHV----AMLLGA------AKLLKARKH-----LLKGTVRLLFQPAEE-GGAGAKEMikEGALDDVEAIFGMHVSPALP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 174 TTVIGA---PTQ--VKIYT-TIKGKTAHASTPKKGISAINIASKAI-------SRmklgQVDALTTA--NIGKFHGGSAT 238
Cdd:cd08017 154 TGTIASrpgPFLagAGRFEvVIRGKGGHAAMPHHTVDPVVAASSAVlalqqlvSR----ETDPLDSQvvSVTRFNGGHAF 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488388323 239 NIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEV-LVEKSYP 290
Cdd:cd08017 230 NVIPDSVTFGGTLRALTTEGFYRLRQRIEEVIEGQAAVHRCNATVdFSEDERP 282
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
30-358 |
3.09e-09 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 57.94 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 30 YLKDTFKKMGLNVIEDEASKNDglganNLICTLKSNIshqnVPKIYFT---------SHMDTVVPG-------KNIQPVV 93
Cdd:PRK13983 35 YLESLLKEYGFDEVERYDAPDP-----RVIEGVRPNI----VAKIPGGdgkrtlwiiSHMDVVPPGdlslwetDPFKPVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 94 KeDGYVYSDGTTilgaDDKAGLAAIIEAIKQIKESNL-PHGQIQIIITVGEESG-------LVGAK----AIDTRLLDAD 161
Cdd:PRK13983 106 K-DGKIYGRGSE----DNGQGIVSSLLALKALMDLGIrPKYNLGLAFVSDEETGskygiqyLLKKHpelfKKDDLILVPD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 162 FGyavdaSKDvGTTVIGAPTQ---VKIytTIKGKTAHASTPKKGISAINIASKAISRM------KLGQVDALTTANIGKF 232
Cdd:PRK13983 181 AG-----NPD-GSFIEIAEKSilwLKF--TVKGKQCHASTPENGINAHRAAADFALELdealheKFNAKDPLFDPPYSTF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 233 ----HGGSATNI--IADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEV-LVEKSYPGFEVNETDKVTQyAI 305
Cdd:PRK13983 253 eptkKEANVDNIntIPGRDVFYFDCRVLPDYDLDEVLKDIKEIADEFEEEYGVKIEVeIVQREQAPPPTPPDSEIVK-KL 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 488388323 306 SSAL--ALGLKGDTCIAGGGSDGNIMNQYGIPSVILGVGYENIHTTSERIAIKDM 358
Cdd:PRK13983 332 KRAIkeVRGIEPKVGGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYAKISNL 386
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
72-199 |
1.01e-08 |
|
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: 54.75 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 72 PKIYFTSHMDTVVPGKN------IQPVVKEDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNL-PHGQIQIIITVGEE 144
Cdd:cd18669 13 KRVLLGAHIDVVPAGEGdprdppFFVDTVEEGRLYGRGA----LDDKGGVAAALEALKLLKENGFkLKGTVVVAFTPDEE 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488388323 145 SGLVGAKAIDTRLLDA-----DFGYAVD-ASKDVGTTVIGAPTQ---VKIYTTIKGKTAHASTP 199
Cdd:cd18669 89 VGSGAGKGLLSKDALEedlkvDYLFVGDaTPAPQKGVGIRTPLVdalSEAARKVFGKPQHAEGT 152
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
142-342 |
1.09e-08 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349914 [Multi-domain] Cd Length: 399 Bit Score: 56.19 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 142 GEESGLvGAKA-IDTRLLD----ADFGYAV----DASKDVGTT---VIGAPTQVKIytTIKGKTAHASTPKKGISAINIA 209
Cdd:cd05664 132 AEETGG-GAQAmVDDGLYDkipkPDVVLAQhvmpGPAGTVGTRpgrFLSAADSLDI--TIFGRGGHGSMPHLTIDPVVMA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 210 SKAISRMKL---GQVDALTTA--NIGKFHGGSATNIIADEVTLEAEARSHDDqSINKQVKHMKETF---ETTANELGGQA 281
Cdd:cd05664 209 ASIVTRLQTivsREVDPQEFAvvTVGSIQAGSAENIIPDEAELKLNVRTFDP-EVREKVLNAIKRIvraECAASGAPKPP 287
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488388323 282 EVLVEKSYPgFEVNETDKVTQYAISSALALGLKGDTCI-AGGGSD--GNIMNQYGIPSVILGVG 342
Cdd:cd05664 288 EFTYTDSFP-ATVNDEDATARLAAAFREYFGEDRVVEVpPVSASEdfSILATAFGVPSVFWFIG 350
|
|
| M42_Frv |
cd05656 |
M42 Peptidase, endoglucanases; Peptidase M42 family, Frv (Frv Operon Protein; Endo-1 ... |
99-201 |
1.10e-08 |
|
M42 Peptidase, endoglucanases; Peptidase M42 family, Frv (Frv Operon Protein; Endo-1 4-Beta-Glucanase; Cellulase Protein; Endoglucanase; Endo-1 4-Beta-Glucanase Homolog; Glucanase; EC. 3.2.1.4) subfamily. Frv is a co-catalytic metallopeptidase, found in archaea and bacteria, including Pyrococcus horikoshii tetrahedral shaped phTET1 (DAPPh1; FrvX; PhDAP aminopeptidase; PhTET aminopeptidase; deblocking aminopeptidase), phTET2 (DAPPh2) and phTET3 (DAPPh3), Haloarcula marismortui TET (HmTET) as well as Bacillus subtilis YsdC. All of these exhibit aminopeptidase and deblocking activities. The HmTET is a broad substrate aminopeptidase capable of degrading large peptides. PhTET2, which shares 24% identity with HmTET, is a cobalt-activated peptidase and possibly a deblocking aminopeptidase, assembled as a 12-subunit tetrahedral dodecamer, while PhTET1 can be alternatively assembled as a tetrahedral dodecamer or as an octahedral tetracosameric structure. The active site in such a self-compartmentalized complex is located on the inside such that substrate sizes are limited, indicating function as possible peptide scavengers. PhTET2 cleaves polypeptides by a nonprocessive mechanism, preferring N-terminal hydrophobic or uncharged polar amino acids. Streptococcus pneumoniae PepA (SpPepA) also forms dodecamer with tetrahedral architecture, and exhibits selective substrate specificity to acidic amino acids with the preference to glutamic acid, with the substrate binding S1 pocket containing an Arg allows electrostatic interactions with the N-terminal acidic residue in the substrate. The YsdC gene is conserved in a number of thermophiles, archaea and pathogenic bacterial species; the closest structural homolog is Thermotoga maritima FrwX (34% identity), which is annotated as either a cellulase or an endoglucanase, and is possibly involved in polysaccharide biosynthesis or degradation.
Pssm-ID: 349906 [Multi-domain] Cd Length: 337 Bit Score: 56.03 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 99 VYSDGTTILGA--------DDKAGLAAIIEAIKQIKESNLPHgQIQIIITVGEESGLVGAKAIdTRLLDADFGYAVDASK 170
Cdd:cd05656 154 VPDTEFTELGGnrvvgkalDNRAGCAVLLEVLRELKDEELPN-DLYFVATVQEEVGLRGAKTA-AFRIDPDIAIAVDVTI 231
|
90 100 110
....*....|....*....|....*....|...
gi 488388323 171 DVGTTVIGAPTQVKIY--TTIKGKTAHASTPKK 201
Cdd:cd05656 232 AGDTPGIKHKGEVKLGkgPVIRIGDRSLIPHPK 264
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
57-162 |
1.12e-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: 54.74 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 57 NLICTLKSNishQNVPKIYFTSHMDtVVPGKN-------IQPVVKEDGYVYSDGttilGADDKAGLAAIIEAIKQIKESN 129
Cdd:cd03873 1 NLIARLGGG---EGGKSVALGAHLD-VVPAGEgdnrdppFAEDTEEEGRLYGRG----ALDDKGGVAAALEALKRLKENG 72
|
90 100 110
....*....|....*....|....*....|....
gi 488388323 130 L-PHGQIQIIITVGEESGLVGAKAIDTRLLDADF 162
Cdd:cd03873 73 FkPKGTIVVAFTADEEVGSGGGKGLLSKFLLAED 106
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
188-311 |
2.19e-08 |
|
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: 55.23 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 188 TIKGKTAHASTPKKGISAINIASKAI-------SRmklgQVDALTTA--NIGKFHGGSATNIIADEVTLEAEARSHDDQS 258
Cdd:cd05666 178 TIRGKGGHAAMPHLGVDPIVAAAQLVqalqtivSR----NVDPLDAAvvSVTQIHAGDAYNVIPDTAELRGTVRAFDPEV 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488388323 259 INKQVKHMKETFETTANELGGQAEVLVEKSYPGFeVNeTDKVTQYAISSALAL 311
Cdd:cd05666 254 RDLIEERIREIADGIAAAYGATAEVDYRRGYPVT-VN-DAEETAFAAEVAREV 304
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
30-358 |
2.33e-08 |
|
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: 55.22 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 30 YLKDTFKKMGLNVIEDEAskndglGanNLICTLKSniSHQNVPKIYFTSHMDTVVPGKniqpvvKEDGyvysdgttILGA 109
Cdd:cd03884 34 LFVEWMEEAGLSVRVDAV------G--NLFGRLEG--TDPDAPPVLTGSHLDTVPNGG------RYDG--------ILGV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 110 ddkagLAAIiEAIKQIKESNL-PHGQIQIIITVGEE-----SGLVGAKAI----------------DTRLLDA--DFGYA 165
Cdd:cd03884 90 -----LAGL-EALRALKEAGIrPRRPIEVVAFTNEEgsrfpPSMLGSRAFagtldleellslrdadGVSLAEAlkAIGYD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 166 VD---------------------------ASKDVG-TTVIGAPTQVKIytTIKGKTAHA-STPKK-----GISAINIASK 211
Cdd:cd03884 164 GDrpasarrpgdikayvelhieqgpvleeEGLPIGvVTGIAGQRWLEV--TVTGEAGHAgTTPMAlrrdaLLAAAELILA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 212 AISRMKLGQVDALTTanIGKFHGG-SATNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEvlVEKSYp 290
Cdd:cd03884 242 VEEIALEHGDDLVAT--VGRIEVKpNAVNVIPGEVEFTLDLRHPDDAVLDAMVERIRAEAEAIAAERGVEVE--VERLW- 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488388323 291 GFEVNETDKVTQYAIS-SALALGLKGDTCIAGGGSDGNIMNQYG------IPSvILGVGyeniHTTSERIAIKDM 358
Cdd:cd03884 317 DSPPVPFDPELVAALEaAAEALGLSYRRMPSGAGHDAMFMARICptamifVPS-RDGIS----HNPAEYTSPEDL 386
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
1-336 |
3.01e-08 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 55.16 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 1 MINQKRLLDCFLELVQINSETGH--------EETIQ--PYLKDTFKKMGLNVIEDeaskndglGANNLICTLKSniSHQN 70
Cdd:PRK09290 3 RIDAERLWARLDELAKIGATPDGgvtrlalsPEDLQarDLFAEWMEAAGLTVRVD--------AVGNLFGRLEG--RDPD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 71 VPKIYFTSHMDTVVPGKNiqpvvkedgYvysDGttILGAddkagLAAiIEAIKQIKESN--LPHGqIQIIITVGEES--- 145
Cdd:PRK09290 73 APAVLTGSHLDTVPNGGR---------F---DG--PLGV-----LAG-LEAVRTLNERGirPRRP-IEVVAFTNEEGsrf 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 146 --GLVGAKAI-----DTRLLD-------------ADFGYAVDA-------SKDVGTTV----------------IGAPT- 181
Cdd:PRK09290 132 gpAMLGSRVFtgaltPEDALAlrdadgvsfaealAAIGYDGDEavgaaraRRDIKAFVelhieqgpvleaeglpIGVVTg 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 182 ---QVKIYTTIKGKTAHA-STPkkgisainiaskaisrMKLGQvDALTTA--------NIGKFHGGSA------------ 237
Cdd:PRK09290 212 ivgQRRYRVTFTGEANHAgTTP----------------MALRR-DALLAAaeiilaveRIAAAHGPDLvatvgrlevkpn 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 238 -TNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEVLVEKSYPGFEVNEtdKVTQYAISSALALGLKGD 316
Cdd:PRK09290 275 sVNVIPGEVTFTLDIRHPDDAVLDALVAELRAAAEAIAARRGVEVEIELISRRPPVPFDP--GLVAALEEAAERLGLSYR 352
|
410 420
....*....|....*....|
gi 488388323 317 TCIAGGGSDGNIMNQyGIPS 336
Cdd:PRK09290 353 RLPSGAGHDAQILAA-VVPT 371
|
|
| M20_Acy1L2 |
cd03887 |
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
113-337 |
4.25e-08 |
|
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: 54.50 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 113 AGLAAIIEAIKQIKESNLPhGQIQIIITVGEESGlvGAKAidtRLLDAdfGY--AVDASKDV---GTTVIGAPTQ--VKI 185
Cdd:cd03887 90 ASVAAALALKAALKALGLP-GTVVVLGTPAEEGG--GGKI---DLIKA--GAfdDVDIALMVhpgPKDVAGPKSLavSKL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 186 YTTIKGKTAHAST-PKKGISAIniaskaisrmklgqvDALTTA--NIG----------KFH-----GGSATNIIADEVTL 247
Cdd:cd03887 162 RVEFHGKAAHAAAaPWEGINAL---------------DAAVLAynNISalrqqlkptvRVHgiiteGGKAPNIIPDYAEA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 248 EAEARSHDDQSINKQVKHMKETFETTANELGGQAEVL-VEKSYPGFEVNET-DKVTQYAISSALALGLKGDTCIAGGGSD 325
Cdd:cd03887 227 EFYVRAPTLKELEELTERVIACFEGAALATGCEVEIEeLEGYYDELLPNKTlANIYAENMEALGEEVLDGDEGVGSGSTD 306
|
250
....*....|...
gi 488388323 326 -GNIMnqYGIPSV 337
Cdd:cd03887 307 fGNVS--YVVPGI 317
|
|
| M20_Acy1_IAAspH |
cd05665 |
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, ... |
102-264 |
1.09e-07 |
|
M20 Peptidases aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase; Peptidase M20 family, bacterial and archaeal aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349915 [Multi-domain] Cd Length: 415 Bit Score: 53.48 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 102 DGTTILGAddkaGLAaiiEAIKQIKESnlPHGQIQIIITVGEEsGLVGAKAIDTR--LLDADFGYAVDASKDV--GTTVI 177
Cdd:cd05665 139 DGHTAIGL----GLA---HALAQLKDS--LSGTIKLIFQPAEE-GVRGARAMAEAgvVDDVDYFLASHIGFGVpsGEVVC 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 178 G-----APTqvKIYTTIKGKTAHA-STPKKGISAINIASKA------ISRMKLGqvdaLTTANIGKFHGGSATNIIADEV 245
Cdd:cd05665 209 GpdnflATT--KLDARFTGVSAHAgAAPEDGRNALLAAATAalnlhaIPRHGEG----ATRINVGVLGAGEGRNVIPASA 282
|
170
....*....|....*....
gi 488388323 246 TLEAEARShDDQSINKQVK 264
Cdd:cd05665 283 ELQVETRG-ETTAINEYMF 300
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
4-215 |
1.36e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 53.08 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 4 QKRLLDCFLELVQINSETGHEETIQ--PYLKDTFKKMGLNViED----EASKNDGlganNLICTLksnisHQNVPK--IY 75
Cdd:PRK09133 36 QQAARDLYKELIEINTTASTGSTTPaaEAMAARLKAAGFAD-ADievtGPYPRKG----NLVARL-----RGTDPKkpIL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 76 FTSHMDtVVPGKN-------IQPVVkEDGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNL-PHGQIQIIITVGEESGL 147
Cdd:PRK09133 106 LLAHMD-VVEAKRedwtrdpFKLVE-ENGYFYGRGT----SDDKADAAIWVATLIRLKREGFkPKRDIILALTGDEEGTP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 148 V-GAKAIDTR---LLDADF-------GYAVDASKDVGTTVIGAPtqvKIYT----TIKGKTAHASTPKKGiSAINIASKA 212
Cdd:PRK09133 180 MnGVAWLAENhrdLIDAEFalnegggGTLDEDGKPVLLTVQAGE---KTYAdfrlEVTNPGGHSSRPTKD-NAIYRLAAA 255
|
...
gi 488388323 213 ISR 215
Cdd:PRK09133 256 LSR 258
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
5-370 |
1.50e-07 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 52.48 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 5 KRLLdcfLELVQINSETGHEETIQPYLKDTFKKMGLNVIEDEASKNDGLGAnnlictlksnishqnvPKIYFTSHMDTVv 84
Cdd:PRK00466 13 KELL---LDLLSIYTPSGNETNATKFFEKISNELNLKLEILPDSNSFILGE----------------GDILLASHVDTV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 85 PGKnIQPvvKEDGYV-YSDGttilGADDKAGLAAIIEAIKQIKESNLphgQIQIIITVGEESGLVGAKAIDTRllDADFG 163
Cdd:PRK00466 73 PGY-IEP--KIEGEViYGRG----AVDAKGPLISMIIAAWLLNEKGI---KVMVSGLADEESTSIGAKELVSK--GFNFK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 164 YAVDASKDVGT-TVIGAPTQVKIYTTIKGKTAHASTPKKGIsAINIASKAISRMKLGQVDALTTANIGKFHGGSATNIIA 242
Cdd:PRK00466 141 HIIVGEPSNGTdIVVEYRGSIQLDIMCEGTPEHSSSAKSNL-IVDISKKIIEVYKQPENYDKPSIVPTIIRAGESYNVTP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 243 DEVTLEAEARSHDDQSINKQVKHMKETFEttanelggQAEVLVEKSYPGFEVNETDKVTQYAISSALALGLKGDTCIAGG 322
Cdd:PRK00466 220 AKLYLHFDVRYAINNKRDDLISEIKDKFQ--------ECGLKIVDETPPVKVSINNPVVKALMRALLKQNIKPRLVRKAG 291
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488388323 323 GSDGNIMNQYGIPSVILGVGYENI-HTTSERIAIKDMYMLTRQIIKIIE 370
Cdd:PRK00466 292 TSDMNILQKITTSIATYGPGNSMLeHTNQEKITLDEIYIAVKTYMLAIE 340
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
76-215 |
1.77e-07 |
|
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: 52.64 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 76 FTSHMDTVvpgkniqPVVKE---------------DGYVYSDGTtilgADDKAGLAAIIEAIKQ-IKESNLPhgQIQIII 139
Cdd:cd05674 74 LMAHQDVV-------PVNPEtedqwthppfsghydGGYIWGRGA----LDDKNSLIGILEAVELlLKRGFKP--RRTIIL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 140 TVG---EESGLVGAKAIDTRLLDA----------DFGYAVDASKDVGTTVIGAPTQVKIYT----TIKGKTAHASTPKKG 202
Cdd:cd05674 141 AFGhdeEVGGERGAGAIAELLLERygvdglaailDEGGAVLEGVFLGVPFALPGVAEKGYMdveiTVHTPGGHSSVPPKH 220
|
170
....*....|...
gi 488388323 203 iSAINIASKAISR 215
Cdd:cd05674 221 -TGIGILSEAVAA 232
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
72-235 |
2.71e-07 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 52.07 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 72 PKIYFTSHMDtVVP---GKNIQPVVKE--DGYVYSDGTtilgADDKAGLAAIIEAIKQIKESNLP-HGQIQIIITVGEES 145
Cdd:PRK13013 85 DCVHFNSHHD-VVEvghGWTRDPFGGEvkDGRIYGRGA----CDMKGGLAASIIAAEAFLAVYPDfAGSIEISGTADEES 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 146 GLVGAKAidtrlLDADFGYAvdASKDVGTTVIGAPTQV-KIY----------TTIKGKTAHASTPKKGISAINIASKAIS 214
Cdd:PRK13013 160 GGFGGVA-----YLAEQGRF--SPDRVQHVIIPEPLNKdRIClghrgvwwaeVETRGRIAHGSMPFLGDSAIRHMGAVLA 232
|
170 180 190
....*....|....*....|....*....|....*..
gi 488388323 215 RMKLGQVDAL----------------TTANIGKFHGG 235
Cdd:PRK13013 233 EIEERLFPLLatrrtampvvpegarqSTLNINSIHGG 269
|
|
| Peptidase_M42 |
pfam05343 |
M42 glutamyl aminopeptidase; These peptidases are found in Archaea and Bacteria. The example ... |
110-358 |
6.38e-07 |
|
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: 50.26 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 110 DDKAGLAAIIEAIKQIKESNLPHgQIQIIITVGEESGLVGAKAIDTRLlDADFGYAVDaskdvgTTVIGAPTQVKIYTTI 189
Cdd:pfam05343 134 DDRAGVAVLLELLKELKDEDLPA-DVYFVATVQEEVGLRGAKTSAFKI-KPDEAIAVD------VTAAGDTPGSDEYEAP 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 190 KGKTAhastpkkgisainiaskaisrmklgqvdalttaNIGKFHGGSATNiiadevtleaearshddqsinkqvKHMKET 269
Cdd:pfam05343 206 LGKGP---------------------------------AIRVKDASGIYH------------------------PKLRKF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 270 FETTANELG--GQAEVLveksypgfevnetdkvtqyaissalalglkgdtciAGGGSDGNIM--NQYGIPSVILGVGYEN 345
Cdd:pfam05343 229 LVELAKKNNipYQVDVY-----------------------------------PGGGTDAGAAhlTGGGVPTALISIPTRY 273
|
250
....*....|...
gi 488388323 346 IHTTSERIAIKDM 358
Cdd:pfam05343 274 IHSPVEVAHLDDL 286
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
72-354 |
6.64e-07 |
|
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1L2 family contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.
Pssm-ID: 349945 [Multi-domain] Cd Length: 366 Bit Score: 50.70 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 72 PKIYFTSHMDT--VVPGKNIQPVVKEDGYVYSDGTTILGADDKAGLAAIIEAIKQIKesnlphGQIQIIITVGEESGLVG 149
Cdd:cd08660 57 PVIAIRADIDAlpIQEQTNLPFASKVDGT*HACGHDFHTTSIIGTA*LLNQRRAELK------GTVVFIFQPAEEGAAGA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 150 AKAIDTRLL---DADFGYAVDASKDVGT-TVIGAPTQVKI---YTTIKGKTAHASTPKKGISAINIASKAISrmKLGQVD 222
Cdd:cd08660 131 RKVLEAGVLngvSAIFGIHNKPDLPVGTiGVKEGPL*ASVdvfEIVIKGKGGHASIPNNSIDPIAAAGQIIS--GLQSVV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 223 ALTT-------ANIGKFHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEVLVEKSYPGFEVN 295
Cdd:cd08660 209 SRNIsslqnavVSITRVQGGTAWNVIPDQAE*EGTVRAFTKEARQAVPEH*RRVAEGIAAGYGCQAEFKWFPNGPSEVQN 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488388323 296 ETDKVTQYAISSALALGLKGDTCIAGGGSD-GNImnQYGIPSVI----LGVGYENIHTTSERIA 354
Cdd:cd08660 289 DGTLLNAFSKAAARLGYATVHAEQSPGSEDfALY--QEKIPGFFvw*gTNGRTEEWHHPAFRLD 350
|
|
| M20_ACY1L2-like |
cd05672 |
M20 Peptidase aminoacylase 1-like protein 2-like, amidohydrolase subfamily; Peptidase M20 ... |
113-336 |
7.65e-07 |
|
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: 50.64 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 113 AGLAAIIEAIKQIKESNLPhGQIQIIITVGEESGlvGAKAidtRLLDADFGYAVDASKDV---GTTVIGAPTQ--VKIYT 187
Cdd:cd05672 90 ASVAAALALKEALKALGLP-GKVVVLGTPAEEGG--GGKI---DLIKAGAFDDVDAALMVhpgPRDVAGVPSLavDKLTV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 188 TIKGKTAHAST-PKKGISAIniaskaisrmklgqvDALTTA--NIGKF---------------HGGSATNIIADEVTLEA 249
Cdd:cd05672 164 EFHGKSAHAAAaPWEGINAL---------------DAAVLAynAISALrqqlkptwrihgiitEGGKAPNIIPDYAEARF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 250 EARSHDDQSINKQVKHMKETFETTANELGGQAEVL-VEKSYPGFEVNET-DKVTQYAISSALALGLKGDTCIAGGGSD-G 326
Cdd:cd05672 229 YVRAPTRKELEELRERVIACFEGAALATGCTVEIEeDEPPYADLRPNKTlAEIYAENMEALGEEVIDDPEGVGTGSTDmG 308
|
250
....*....|
gi 488388323 327 NIMnqYGIPS 336
Cdd:cd05672 309 NVS--YVVPG 316
|
|
| Peptidase_M28 |
pfam04389 |
Peptidase family M28; |
57-212 |
8.19e-07 |
|
Peptidase family M28;
Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 48.82 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 57 NLICTLKSNiSHQNVpkIYFTSHMDTVVPGKniqpvvkedgyvysdgttilGADDKA-GLAAIIEAIKQIKESNLPHGQI 135
Cdd:pfam04389 1 NVIAKLPGK-APDEV--VLLSAHYDSVGTGP--------------------GADDNAsGVAALLELARVLAAGQRPKRSV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 136 QIIITVGEESGLVGAKAIDTR-----------LLDA--------DF-----------GYAVDASKDVGTTVIGAPTQvki 185
Cdd:pfam04389 58 RFLFFDAEEAGLLGSHHFAKShpplkkiraviNLDMigsggpalLFqsgpkgsslleKYLKAAAKPYGVTLAEDPFQ--- 134
|
170 180
....*....|....*....|....*..
gi 488388323 186 YTTIKGKTAHASTPKKGISAINIASKA 212
Cdd:pfam04389 135 ERGGPGRSDHAPFIKAGIPGLDLAFTD 161
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
143-306 |
8.48e-07 |
|
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: 50.34 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 143 EESGLVGAKAIDTRLL-----DADFGYAVDASKDVGT------TVIGAPTQVKIytTIKGKTAHASTPKKGISAINIASK 211
Cdd:cd05670 124 EEGPGGAKRMYESGVFgkwrpDEIYGLHVNPDLPVGTiatrsgTLFAGTSELHI--DFIGKSGHAAYPHNANDMVVAAAN 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 212 AISRMKL---GQVDALTTA--NIGKFHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKETFETTANELGGQAEVLVE 286
Cdd:cd05670 202 FVTQLQTivsRNVDPIDGAvvTIGKIHAGTARNVIAGTAHLEGTIRTLTQEMMELVKQRVRDIAEGIELAFDCEVKVDLG 281
|
170 180
....*....|....*....|
gi 488388323 287 KSYPgfEVNETDKVTQYAIS 306
Cdd:cd05670 282 QGYY--PVENDPDLTTEFID 299
|
|
| M42 |
cd05638 |
M42 Peptidases, also known as glutamyl aminopeptidase family; Peptidase M42 family proteins, ... |
81-169 |
3.05e-06 |
|
M42 Peptidases, also known as glutamyl aminopeptidase family; Peptidase M42 family proteins, also known as glutamyl aminopeptidases (GAP), are co-catalytic metallopeptidases, found in archaea and bacteria. They typically bind two zinc or cobalt atoms and include cellulase and endo-1,4-beta-glucanase (endoglucanase). 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. GAP removes glutamyl residues from the N-terminus of peptide substrates, but is also effective against aspartyl and, to a lesser extent, seryl residues. Lactococcus lactis glutamyl aminopeptidase (PepA; aminopeptidase A) has high thermal stability and aids growth of the organism in milk. Pyrococcus horikoshii contain a thermostable de-blocking aminopeptidase member of this family, used commercially for N-terminal protein sequencing.
Pssm-ID: 193517 [Multi-domain] Cd Length: 332 Bit Score: 48.61 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 81 DTVVPGKNIQpvVKEDGYVYSdgttiLGADDKAGLAAIIEAIKQIKESNLPhGQIQIIITVGEESGLVGAKAIdTRLLDA 160
Cdd:cd05638 151 DFVVFDPRFQ--VLESKYIKS-----RALDDRVSVYILLELIKRLQDAELP-AEVYFVASVQEEVGLRGASTS-TEAVEP 221
|
....*....
gi 488388323 161 DFGYAVDAS 169
Cdd:cd05638 222 DVALAVD*G 230
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
53-370 |
1.03e-05 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 47.25 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 53 LGANNLICTLKSniSHQNVPKIYFTSHMDtVVPgknIQP-------------VVKeDGYVYSDGTTilgaDDKAGLAAII 119
Cdd:PRK08262 95 VGGHSLLYTWKG--SDPSLKPIVLMAHQD-VVP---VAPgtegdwthppfsgVIA-DGYVWGRGAL----DDKGSLVAIL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 120 EAIkqikESNLPHGqIQ----IIITVG--EESGLVGAKAIdTRLLDA---------DFGYAVDASKDVGTT----VIGap 180
Cdd:PRK08262 164 EAA----EALLAQG-FQprrtIYLAFGhdEEVGGLGARAI-AELLKErgvrlafvlDEGGAITEGVLPGVKkpvaLIG-- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 181 TQVKIYTTIK----GKTAHASTPKKGiSAINIASKAISR------------------------MKLGQVDAL-------- 224
Cdd:PRK08262 236 VAEKGYATLEltarATGGHSSMPPRQ-TAIGRLARALTRlednplpmrlrgpvaemfdtlapeMSFAQRVVLanlwlfep 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 225 -----------------TTANIGKFHGGSATNIIADEVTLEAEARSHDDQSINKQVKHMKEtfetTANELGGQAEVLVEK 287
Cdd:PRK08262 315 lllrvlakspetaamlrTTTAPTMLKGSPKDNVLPQRATATVNFRILPGDSVESVLAHVRR----AVADDRVEIEVLGGN 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 288 SYPGfEVNETDKVtQYAISSALALGLKGDTCIA----GGGSDGNIMNQ-----YGIPSVILGV-GYENIHTTSERIAIKD 357
Cdd:PRK08262 391 SEPS-PVSSTDSA-AYKLLAATIREVFPDVVVApylvVGATDSRHYSGisdnvYRFSPLRLSPeDLARFHGTNERISVAN 468
|
410
....*....|...
gi 488388323 358 MYMLTRQIIKIIE 370
Cdd:PRK08262 469 YARMIRFYYRLIE 481
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
79-277 |
1.22e-05 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 46.86 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 79 HMDTVVPGKN-----IQPVVKeDGYVYSDGTTilgaDDKAGLAAIIEAIKQIKESNLP-HGQIQIIITVGEESglvGAKA 152
Cdd:cd03888 79 HLDVVPAGEGwttdpFKPVIK-DGKLYGRGTI----DDKGPTIAALYALKILKDLGLPlKKKIRLIFGTDEET---GWKC 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 153 IDTRLLD---ADFGYAVDASkdvgttvigaptqvkiYTTIKGktahastpKKGISAINIASKaisrmklgqVDALTTANI 229
Cdd:cd03888 151 IEHYFEHeeyPDFGFTPDAE----------------FPVING--------EKGIVTVDLTFK---------IDDDKGYRL 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488388323 230 GKFHGGSATNIIADEVTLEAEArSHDDQSINKQVKHMKETFETTANEL 277
Cdd:cd03888 198 ISIKGGEATNMVPDKAEAVIPG-KDKEELALSAATDLKGNIEIDDGGV 244
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
69-146 |
1.57e-05 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 46.56 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 69 QNVPKIYFTSHMDTVVPGKN-------IQPVVKeDGYVYSDGttilGADDK-AGLAAIIeAIKQIKESNLPHGQIQIIIT 140
Cdd:cd05682 71 QDDDTVLLYGHMDKQPPFTGwdeglgpTKPVIR-GDKLYGRG----GADDGyAIFASLT-AIKALQEQGIPHPRCVVLIE 144
|
....*.
gi 488388323 141 VGEESG 146
Cdd:cd05682 145 ACEESG 150
|
|
| M20_Acy1L2-like |
cd09849 |
M20 Peptidase aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
188-321 |
2.22e-05 |
|
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: 45.93 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 188 TIKGKTAHA-STPKKGISAINIASKAISRMKLgQVDALTTANIGKFH-----GGSATNIIADEVTLEAEARSHDDQSINK 261
Cdd:cd09849 195 KFTGKESHAgSAPFSGINALNAATLAINNVNA-QRETFKESDKVRFHpiitkGGDIVNVVPADVRVESYVRARSIDYMKE 273
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488388323 262 QVKHMKETFETTANELGGQAEVLVEKSY-PGFEVNETDKVTqyaISSALALGLKGDTCIAG 321
Cdd:cd09849 274 ANSKVNRALRASAMAVGAEVEIKELPGYlPILQDRDLDNFL---KENLQDLGLIERIIDGG 331
|
|
| M42_glucanase_like |
cd05657 |
M42 Peptidase, endoglucanase-like subfamily; Peptidase M42 family, glucanase (endo-1, ... |
6-153 |
2.70e-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: 45.73 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 6 RLLDCFLELVQINSETGHEETIQPYLKDTFKKMGLNVIEDEASkndglganNLICTLKSNISHqnvPKIYFTSHMDT--- 82
Cdd:cd05657 1 YLLDLLKELLAIPSPTGYTDEAVRYLKKELEGLGVETELTNKG--------ALIATIPGKDSR---KARALSAHVDTlga 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 83 ------------VVPGKNIQPVVKEDGYVY---SDGTTILGA-------------------------------------- 109
Cdd:cd05657 70 ivkeikpdgrlrLTPIGGFAWNSAEGENVTiitRDGKTYTGTvlplkasvhvygdapeaqertwdnmevrldekvksked 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488388323 110 -------------------------------DDKAGLAAIIEAIKQIKESNL-PHGQIQIIITVGEESGLVGAKAI 153
Cdd:cd05657 150 vlalgirvgdfvafdprpevtesgfiksrhlDDKASVAILLALARALKENKLkLPVDTHFLFSNYEEVGHGASFAP 225
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
72-369 |
2.73e-05 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 45.58 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 72 PKIYFTSHMDTV--VPGKNIQPVVKEDGyvySDGTTILGADDKAGLAAIIEAIkqikeSNLPHGQIQIIITVGEESGlvg 149
Cdd:PRK08737 64 PKYLFNVHLDTVpdSPHWSADPHVMRRT---DDRVIGLGVCDIKGAAAALLAA-----ANAGDGDAAFLFSSDEEAN--- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 150 akaiDTRLLdADFgyaVDASKDVGTTVIGAPTQVK-------IYT---TIKGKTAHASTPKK-GISAINIASKAISRmKL 218
Cdd:PRK08737 133 ----DPRCV-AAF---LARGIPYEAVLVAEPTMSEavlahrgISSvlmRFAGRAGHASGKQDpSASALHQAMRWGGQ-AL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 219 GQVDALTTA----------NIGKFHGGSATNIIADEVTLEAEAR---SHDdqsinkqVKHMKETFETTAnelGGQAEVLV 285
Cdd:PRK08737 204 DHVESLAHArfggltglrfNIGRVEGGIKANMIAPAAELRFGFRplpSMD-------VDGLLATFAGFA---EPAAATFE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 286 EK----SYPGFEVNETDKVTQYAISSALALGLKgdtciAGGGSD----GNIMNQYGIPSVILGVGyeNI---HTTSERIA 354
Cdd:PRK08737 274 ETfrgpSLPSGDIARAEERRLAARDVADALDLP-----IGNAVDfwteASLFSAAGYTALVYGPG--DIaqaHTADEFVT 346
|
330
....*....|....*
gi 488388323 355 IKDMYMLTRQIIKII 369
Cdd:PRK08737 347 LDQLQRYAESVHRII 361
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
13-157 |
3.41e-05 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 45.33 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 13 ELVQINSETGHEETIQPYLKDTFKKMGLNVIEDEaskndglgANNLICTLKSnishqNVPKIYFTSHMDTvVPGkNIqPV 92
Cdd:PRK04443 14 GLVEIPSPSGEEAAAAEFLVEFMESHGREAWVDE--------AGNARGPAGD-----GPPLVLLLGHIDT-VPG-DI-PV 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488388323 93 VKEDGYVYSDGTTilgaDDKAGLAAIIEAIKQIKEsnLPHGQIQIIITVGEE---SGlvGAKAIDTRL 157
Cdd:PRK04443 78 RVEDGVLWGRGSV----DAKGPLAAFAAAAARLEA--LVRARVSFVGAVEEEapsSG--GARLVADRE 137
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
13-146 |
3.63e-05 |
|
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a large variety of enzymes, including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase), canosinase, DUG2 type proteins, as well as many proteins inferred by homology to be dipeptidases. These enzymes have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. Substrates of CNDP are varied and not limited to Xaa-His dipeptides. DUG2 proteins contain a metallopeptidase domain and a large N-terminal WD40 repeat region, and are involved in the alternative pathway of glutathione degradation.
Pssm-ID: 349888 [Multi-domain] Cd Length: 426 Bit Score: 45.40 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 13 ELVQINSETGHEETIQ------PYLKDTFKKMGLNVIEDEASKndglGANNLICTLKSNISHqnvPKIYFTSHMDtVVPG 86
Cdd:cd03893 6 ELVAIPSVSAQPDRREelrraaEWLADLLRRLGFTVEIVDTSN----GAPVVFAEFPGAPGA---PTVLLYGHYD-VQPA 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488388323 87 KNIQ-------PVVKEDGYVYSDGttilGADDKAGLAAIIEAIKQIKE--SNLPHGqIQIIITVGEESG 146
Cdd:cd03893 78 GDEDgwdsdpfELTERDGRLYGRG----AADDKGPILAHLAALRALMQqgGDLPVN-VKFIIEGEEESG 141
|
|
| M28 |
cd02690 |
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ... |
57-218 |
5.25e-05 |
|
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y 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. 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. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases.
Pssm-ID: 349868 [Multi-domain] Cd Length: 202 Bit Score: 43.87 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 57 NLICTLKSNISHQnvPKIYFTSHMDTVVPGkniqpvvkedgyvysdgttiLGADDKA-GLAAIIEAIKQIKESNL-PHGQ 134
Cdd:cd02690 3 NVIATIKGSDKPD--EVILIGAHYDSVPLS--------------------PGANDNAsGVAVLLELARVLSKLQLkPKRS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 135 IQIIITVGEESGLVGAKAIDTRLLD----ADFGYAVD--ASKDVGTTVIGAP---------------------TQVKIYT 187
Cdd:cd02690 61 IRFAFWDAEELGLLGSKYYAEQLLSslknIRAALNLDmiGGAGPDLYLQTAPgndalvekllralahelenvvYTVVYKE 140
|
170 180 190
....*....|....*....|....*....|..
gi 488388323 188 TIK-GKTAHASTPKKGISAINIASKAISRMKL 218
Cdd:cd02690 141 DGGtGGSDHRPFLARGIPAASLIQSESYNFPY 172
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
72-249 |
1.36e-04 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 43.61 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 72 PKIYFTSHMDTVVPGKN------IQPVVKEDgYVYSDGTtilgADDKAGLAAIIEAIKQIKESNLpHGQIQIIITVGEES 145
Cdd:PRK08554 64 PKLLFMAHFDVVPVNPEewntepFKLTVKGD-KAYGRGS----ADDKGNVASVMLALKELSKEPL-NGKVIFAFTGDEEI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 146 GLVGAKAIDTRLLDADF--GYAVDAS-----------KDVGTTVIGAPTQVKIYTTIKGK----------TAHASTPKKG 202
Cdd:PRK08554 138 GGAMAMHIAEKLREEGKlpKYMINADgigmkpiirrrKGFGVTIRVPSEKVKVKGKLREQtfeirtpvveTRHAAYFLPG 217
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488388323 203 I-SAINIASKAISRMKlgqvDALTTANIGKFHGGsatNIIADEVTLEA 249
Cdd:PRK08554 218 VdTHPLIAASHFLRES----NVLAVSLEGKFLKG---NVVPGEVTLTY 258
|
|
| M28_like |
cd03877 |
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ... |
108-152 |
5.28e-04 |
|
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: 40.69 E-value: 5.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 488388323 108 GADDKA-GLAAIIEAIKQIKESNLPHGQIQIIITVGEESGLVGAKA 152
Cdd:cd03877 41 GADDNAsGVAAVLELARYFAKQKTPKRSIVFAAFTAEEKGLLGSKY 86
|
|
| M28_like_PA |
cd05660 |
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ... |
22-151 |
1.91e-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: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488388323 22 GHEETIQpYLKDTFKKMGLnviEDEASKNDGLGANNLICTLKSNISHQNVPK----------IYFTSHMDTVVPGKNIQp 91
Cdd:cd05660 18 GEKKTVD-YLAEQFKELGL---KPAGSDGSYLQAVPLVSKIEYSTSHNVVAIlpgsklpdeyIVLSAHWDHLGIGPPIG- 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488388323 92 vvkeDGYVYSdgttilGADDKA-GLAAIIEAIKQIKESNL-PHGQIQIIITVGEESGLVGAK 151
Cdd:cd05660 93 ----GDEIYN------GAVDNAsGVAAVLELARVFAAQDQrPKRSIVFLAVTAEEKGLLGSR 144
|
|
| PRK09961 |
PRK09961 |
aminopeptidase; |
110-185 |
4.38e-03 |
|
aminopeptidase;
Pssm-ID: 182170 Cd Length: 344 Bit Score: 38.58 E-value: 4.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488388323 110 DDKAGLAAIIEAIKQIKESNLPhGQIQIIITVGEESGLVGAKaIDTRLLDADFGYAVDASKDVGTTVIGAPTQVKI 185
Cdd:PRK09961 166 DDRLGCYLLVTLLRELHDAELP-AEVWLVASSSEEVGLRGGQ-TATRAVSPDVAIVLDTACWAKNFDYGAANHRQI 239
|
|
| |
