|
Name |
Accession |
Description |
Interval |
E-value |
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
8-474 |
0e+00 |
|
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.
Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 826.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 8 LYEVIDKKKDEFVTRLSRAVSIPSVSADVTLRPKVVEMADFVVSEFTKLGAKMEKRDIGYHQM-DGQDVPLPPIVLGQYG 86
Cdd:cd05676 1 VFKYIDEHQDEFIERLREAVAIQSVSADPEKRPELIRMMEWAAERLEKLGFKVELVDIGTQTLpDGEELPLPPVLLGRLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 87 NDPSKKTVLIYNHFDVQPASLEDGWSTDPFTLTvDNKGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGM 166
Cdd:cd05676 81 SDPSKKTVLIYGHLDVQPAKLEDGWDTDPFELT-EKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEGM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 167 EEYGSEGLEDLIRAEAEKYFAKADCVCISDTYWLGTKKPVLTYGLRGVCYFNITVEGPSADLHSGVFGGTVHEPMTDLVA 246
Cdd:cd05676 160 EESGSEGLDELIEARKDTFFSDVDYVCISDNYWLGKKKPCLTYGLRGICYFFIEVEGPNKDLHSGVFGGSVHEPMTDLIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 247 IMSTLVKPNGEILIPGIMDQVAELTPTEDSIYDGIDYTMEDLKEAVGADISIYPDPKRTLQHRWRYPTLSLHGIEGAFSG 326
Cdd:cd05676 240 LMSSLVDSDGKILIPGIYDAVAPLTEEEWELYEKIDFDMEEYREDIGVRRLLYDNKEELLMHRWRYPSLSIHGIEGAFSG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 327 SGAKTVIPAKVIGKFSIRTVPNMESETVERLVKEHVTKVFNSLNSKNKLAFNNMHSGSWWISSPDHWHYDVGKKATERVY 406
Cdd:cd05676 320 PGAKTVIPAKVIGKFSIRLVPNMDPEVVEKQVTDYLEKVFAELKSPNKLKVYMGHGGKPWVADPDHPNYKAARKATKRVF 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429239506 407 GITPDFVREGGSIPVTVTFEQSLKKNVLLLPMGRGDDGAHSINEKLDLDNFLKGIKLFCTYVHELASV 474
Cdd:cd05676 400 GVEPDLTREGGSIPITLTFQEATGKNVMLLPIGAADDGAHSQNEKINRRNYIEGTKLLAAYFHELSKL 467
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
27-467 |
1.02e-151 |
|
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: 438.69 E-value: 1.02e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 27 VSIPSVSADVTLRPKVVEMADFVVSEFTKLGAKMEKRDIGyhqmdgqdvPLPPIVLGQYGNDPSKKTVLIYNHFDVQPAS 106
Cdd:cd03893 8 VAIPSVSAQPDRREELRRAAEWLADLLRRLGFTVEIVDTS---------NGAPVVFAEFPGAPGAPTVLLYGHYDVQPAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 107 LEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEYGSEGLEDLIraEAEKYF 186
Cdd:cd03893 79 DEDGWDSDPFELTERD-GRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEESGSPSLDQLV--EAHRDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 187 AKADCVCISDTYWLGTKKPVLTYGLRGVCYFNITVEGPSADLHSGVFGGTVHEPMTDLVAIMSTLVKPNGEILIPGIMDQ 266
Cdd:cd03893 156 LAADAIVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLDHDLHSGLYGGVVPDPMTALAQLLASLRDETGRILVPGLYDA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 267 VAELTPTEDSIYDGIDYTMEDLKEAVGADisiypdpkrtLQHRWRYPTLSLHGIEGAFSGSGAKTVIPAKVIGKFSIRTV 346
Cdd:cd03893 236 VRELPEEEFRLDAGVLEEVEIIGGTTGSV----------AERLWTRPALTVLGIDGGFPGEGSKTVIPPRARAKISIRLV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 347 PNMESETVERLVKEHVTKVFnslNSKNKLAFNNMHSGSWWISSPDHWHYDVGKKATERVYGITPDFVREGGSIPVTVTFE 426
Cdd:cd03893 306 PGQDPEEASRLLEAHLEKHA---PSGAKVTVSYVEGGMPWRSDPSDPAYQAAKDALRTAYGVEPPLTREGGSIPFISVLQ 382
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 429239506 427 QSLKKNVLLLPMGRGDDGAHSINEKLDLDNFLKGIKLFCTY 467
Cdd:cd03893 383 EFPQAPVLLIGVGDPDDNAHSPNESLRLGNYKEGTQAEAAL 423
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
20-471 |
4.37e-123 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 365.86 E-value: 4.37e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 20 VTRLSRAVSIPSVSADVTLRPKVVEMADFVVSEFTKLGA-KMEKRDIGYHqmdgqdvplpPIVLGQYGNDPSKKTVLIYN 98
Cdd:cd05680 1 LEELFELLRIPSVSADPAHKGDVRRAAEWLADKLTEAGFeHTEVLPTGGH----------PLVYAEWLGAPGAPTVLVYG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 99 HFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEYGSEGLEDLI 178
Cdd:cd05680 71 HYDVQPPDPLELWTSPPFEPVVRD-GRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIGSPSLPAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 179 RAEAEKYfaKADCVCISDTYWLGTKKPVLTYGLRGVCYFNITVEGPSADLHSGVFGGTVHEPMTDLVAIMSTLVKPNGEI 258
Cdd:cd05680 150 EENAERL--AADVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNRDLHSGSYGGAVPNPANALARLLASLHDEDGRV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 259 LIPGIMDQVAELTPTEDSIYDGIDYTMEDLKEAVGADISIYPDPKRTLQHRWRYPTLSLHGIEGAFSGSGAKTVIPAKVI 338
Cdd:cd05680 228 AIPGFYDDVRPLTDAEREAWAALPFDEAAFKASLGVPALGGEAGYTTLERLWARPTLDVNGIWGGYQGEGSKTVIPSKAH 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 339 GKFSIRTVPNMESETVERLVKEHVTKVfnsLNSKNKLAFNNMHSGSWWISSPDHWHYDVGKKATERVYGITPDFVREGGS 418
Cdd:cd05680 308 AKISMRLVPGQDPDAIADLLEAHLRAH---APPGVTLSVKPLHGGRPYLVPTDHPALQAAERALEEAFGKPPVFVREGGS 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 429239506 419 IPVTVTFEQSLKKNVLLLPMGRGDDGAHSINEKLDLDNFLKGIKLFCTYVHEL 471
Cdd:cd05680 385 IPIVALFEKVLGIPTVLMGFGLPDDAIHAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
14-472 |
7.05e-100 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 307.06 E-value: 7.05e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 14 KKKDEFVTRLSRAVSIPSVSADVTLRPKVVEMADFVVSEFTKLGakMEKRDIgyHQMDGQdvplpPIVLGQYGNDPSKKT 93
Cdd:PRK08201 11 ERREAHLEELKEFLRIPSISALSEHKEDVRKAAEWLAGALEKAG--LEHVEI--METAGH-----PIVYADWLHAPGKPT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 94 VLIYNHFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEYGSEG 173
Cdd:PRK08201 82 VLIYGHYDVQPVDPLNLWETPPFEPTIRD-GKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEEIGSPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 174 LEDLIRAEAEKYfaKADCVCISDTYWLGTKKPVLTYGLRGVCYFNITVEGPSADLHSGVFGGTVHEPMTDLVAIMSTLVK 253
Cdd:PRK08201 161 LDSFVEEEKDKL--AADVVLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLHSGLYGGAVPNALHALVQLLASLHD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 254 PNGEILIPGIMDQVAELTPTEDSIYDGIDYTMEDLKEAVGADiSIYPDPKRTLQHR-WRYPTLSLHGIEGAFSGSGAKTV 332
Cdd:PRK08201 239 EHGTVAVEGFYDGVRPLTPEEREEFAALGFDEEKLKRELGVD-ELFGEEGYTALERtWARPTLELNGVYGGFQGEGTKTV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 333 IPAKVIGKFSIRTVPNMESETVERLVKEHVTKvfnSLNSKNKLAFNNMHSGSWWISSPDHWHYDVGKKATERVYGITPDF 412
Cdd:PRK08201 318 IPAEAHAKITCRLVPDQDPQEILDLIEAHLQA---HTPAGVRVTIRRFDKGPAFVAPIDHPAIQAAARAYEAVYGTEAAF 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 413 VREGGSIPVTVTFEQSLKKNVLLLPMGRGDDGAHSINEKLDLDNFLKGIKLFCTYVHELA 472
Cdd:PRK08201 395 TRMGGSIPVVETFSSQLHIPIVLMGFGLPSENFHAPNEHFHLENFDKGLRTLVEYWHQLA 454
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
46-460 |
1.12e-99 |
|
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase M20 family, Defective in Utilization of Glutathione (DUG2) subfamily. DUG2-type proteins are metallopeptidases containing WD repeats at the N-terminus. DUG2 proteins are involved in the alternative pathway of glutathione (GSH) degradation. GSH, the major low-molecular-weight thiol compound in most eukaryotic cells, is normally degraded through the gamma-glutamyl cycle initiated by gamma-glutamyl transpeptidase. However, a novel pathway for the degradation of GSH has been characterized; it requires the participation of three genes identified in Saccharomyces cerevisiae as "defective in utilization of glutathione" genes including DUG1, DUG2, and DUG3. DUG1 encodes a probable di- or tri-peptidase identified as M20 metallopeptidase, DUG2 gene encodes a protein with a metallopeptidase domain and a large N-terminal WD40 repeat region, while DUG3 encodes a protein with a glutamine amidotransferase domain. Although dipeptides and tripeptides with a normal peptide bond, such as cys-gly or glu-cys-gly, can be hydrolyzed by the DUG1 protein, the presence of an unusual peptide bond, like in GSH, requires the participation of the DUG2 and DUG3 proteins as well. These three proteins form a GSH degradosomal complex.
Pssm-ID: 349926 [Multi-domain] Cd Length: 436 Bit Score: 305.81 E-value: 1.12e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 46 ADFVVSEFTKLGAKmekrdigyhqmDGQDVPLP----PIVLGQY---GNDPSKKTVLIYNHFDVQPASLEDGWSTDPFTL 118
Cdd:cd05677 30 AIFLRQLFKKLGAT-----------NCLLLPSGpgtnPIVLATFsgnSSDAKRKRILFYGHYDVIPAGETDGWDTDPFTL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 119 TVDNkGRMFGRGATDDKGPLIGWI-SAIEAH--KELGIDfpvnLLMCFEGMEEYGSEGLEDLIRAEAEKyFAKADCVCIS 195
Cdd:cd05677 99 TCEN-GYLYGRGVSDNKGPLLAAIyAVAELFqeGELDND----VVFLIEGEEESGSPGFKEVLRKNKEL-IGDIDWILLS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 196 DTYWLGTKKPVLTYGLRGVCYFNITVEGPSADLHSGVFGGTVHEPMTDLVAIMSTLVKPNGEILIPGIMDQVAELTPTED 275
Cdd:cd05677 173 NSYWLDDNIPCLNYGLRGVIHATIVVSSDKPDLHSGVDGGVLREPTADLIKLLSKLQDPDGRILIPHFYDPVKPLTEAER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 276 SIYDGIdytmedlkeAVGADIsIYPDPKRTLQHRWRYPTLSLHGIEgaFSGSGAKTVIPAKVIGKFSIRTVPNMESETVE 355
Cdd:cd05677 253 ARFTAI---------AETALI-HEDTTVDSLIAKWRKPSLTVHTVK--VSGPGNTTVIPKSASASVSIRLVPDQDLDVIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 356 RLVKEHVTKVFNSLNSKNKLAFNNMHSGSWWISSPDHWHYDVGKKATERVYGITPDFVREGGSIPVTVTFEQSLKKNVLL 435
Cdd:cd05677 321 QDLTDYIQSCFAELKSQNHLDIEVLNEAEPWLGDPDNPAYQILREAVTAAWGVEPLYIREGGSIPTIRFLEKEFNAPAVQ 400
|
410 420
....*....|....*....|....*
gi 429239506 436 LPMGRGDDGAHSINEKLDLDNFLKG 460
Cdd:cd05677 401 LPCGQSSDNAHLDNERLRIKNLYKM 425
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
23-463 |
1.22e-83 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 264.20 E-value: 1.22e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 23 LSRAVSIPSVSA-DVTLRpkvvEMADFVVSEFTKLGAKMEKrdigyHQMDGQdvplpPIVLGQYGNDpSKKTVLIYNHFD 101
Cdd:cd05681 5 LRDLLKIPSVSAqGRGIP----ETADFLKEFLRRLGAEVEI-----FETDGN-----PIVYAEFNSG-DAKTLLFYNHYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 102 VQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEYGSEGLEDLIRAE 181
Cdd:cd05681 70 VQPAEPLELWTSDPFELTIRN-GKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPNLEKFVAEH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 182 AEKYFAKAdcvCISDTYWLGTK-KPVLTYGLRGVCYFNITVEGPSADLHSGvFGGTVHEPMTDLVAIMSTLVKPNGEILI 260
Cdd:cd05681 149 ADLLKADG---CIWEGGGKNPKgRPQISLGVKGIVYVELRVKTADFDLHSS-YGAIVENPAWRLVQALNSLRDEDGRVLI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 261 PGIMDQVAELTPTEDSIYDGIDYTMEDLKEAVGADISIY---PDPKRTLqhrWRYPTLSLHGIEGAFSGSGAKTVIPAKV 337
Cdd:cd05681 225 PGFYDDVRPLSEAERALIDTYDFDPEELRKTYGLKRPLQvegKDPLRAL---FTEPTCNINGIYSGYTGEGSKTILPSEA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 338 IGKFSIRTVPNMESETVERLVKEHVTKvfnslNSKNKLAFNNMHSGSWWISSPDHWHYDVGKKATERVYGITPDFVRE-G 416
Cdd:cd05681 302 FAKLDFRLVPDQDPAKILSLLRKHLDK-----NGFDDIEIHDLLGEKPFRTDPDAPFVQAVIESAKEVYGQDPIVLPNsA 376
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 429239506 417 GSIPVTvTFEQSLKKNVLLLPMGRGDDGAHSINEKLDLDNFLKGIKL 463
Cdd:cd05681 377 GTGPMY-PFYDALEVPVVAIGVGNAGSNAHAPNENIRIADYYKGIEH 422
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
1-462 |
2.78e-82 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 261.76 E-value: 2.78e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 1 MKMSLDKLYEVIDKKKDEFVTRLSRAVSIPSVSADVTLRPKVVEMADFVVSEFTKLGAKMEKRDIGYHqmdgqdvplpPI 80
Cdd:PRK09104 1 SMADLDPVLDHIDANLDASLERLFALLRIPSISTDPAYAADCRKAADWLVADLASLGFEASVRDTPGH----------PM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 81 VLGQY-GNDPSKKTVLIYNHFDVQPASLEDGWSTDPFT--LTVDNKGRMF--GRGATDDKGPLIGWISAIEAHKELGIDF 155
Cdd:PRK09104 71 VVAHHeGPTGDAPHVLFYGHYDVQPVDPLDLWESPPFEprIKETPDGRKVivARGASDDKGQLMTFVEACRAWKAVTGSL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 156 PVNLLMCFEGMEEYGSEGLEDLIRAEAEKYfaKADCVCISDTYWLGTKKPVLTYGLRGVCYFNITVEGPSADLHSGVFGG 235
Cdd:PRK09104 151 PVRVTILFEGEEESGSPSLVPFLEANAEEL--KADVALVCDTGMWDRETPAITTSLRGLVGEEVTITAADRDLHSGLFGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 236 TVHEPMTDLVAIMSTLVKPNGEILIPGIMDQVAELTPTEDSIYDGIDYTMEDLKEAVGADISIYPDPKRTLQHRWRYPTL 315
Cdd:PRK09104 229 AAANPIRVLTRILAGLHDETGRVTLPGFYDGVEELPPEILAQWKALGFTAEAFLGPVGLSIPAGEKGRSVLEQIWSRPTC 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 316 SLHGIEGAFSGSGAKTVIPAKVIGKFSIRTVPNMESETVERLVKEHVTkvfNSLNSKNKLAFNNmHSGSWWISSP-DHWH 394
Cdd:PRK09104 309 EINGIWGGYTGEGFKTVIPAEASAKVSFRLVGGQDPAKIREAFRAYVR---ARLPADCSVEFHD-HGGSPAIALPyDSPA 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429239506 395 YDVGKKATERVYGITPDFVREGGSIPVTVTFEQSLKKNVLLLPMGRGDDGAHSINEKLDLDNFLKGIK 462
Cdd:PRK09104 385 LAAAKAALSDEWGKPAVLIGSGGSIPIVGDFKRILGMDSLLVGFGLDDDRIHSPNEKYDLESFHKGIR 452
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
6-472 |
3.33e-73 |
|
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: 235.93 E-value: 3.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 6 DKLYEVIDKKKDEFVTRLSRAVSIPSVSADVTlrpkvvEMADFVVSEFTKLGAKMEKRDIGyhqmdgqdvPLPPIVLGQY 85
Cdd:COG0624 1 AAVLAAIDAHLDEALELLRELVRIPSVSGEEA------AAAELLAELLEALGFEVERLEVP---------PGRPNLVARR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 86 GNDPSKKTVLIYNHFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEG 165
Cdd:COG0624 66 PGDGGGPTLLLYGHLDVVPPGDLELWTSDPFEPTIED-GRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 166 MEEYGSEGLEDLIRAEAEKYfaKADCVCISDtywlGTKKPVLTYGLRGVCYFNITVEGPSAdlHSGVFgGTVHEPMTDLV 245
Cdd:COG0624 145 DEEVGSPGARALVEELAEGL--KADAAIVGE----PTGVPTIVTGHKGSLRFELTVRGKAA--HSSRP-ELGVNAIEALA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 246 AIMSTLvkpngeilipgimdqvaeltptedsiydgidytmEDLKEAVGADISIYPdpkrtlqhrwryPTLSLHGIEGafs 325
Cdd:COG0624 216 RALAAL----------------------------------RDLEFDGRADPLFGR------------TTLNVTGIEG--- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 326 GSGAKtVIPAKVIGKFSIRTVPNMESETVERLVKEHVTKVFNSLNSKNKLAFNNMHSgswWISSPDHWHYDVGKKATERV 405
Cdd:COG0624 247 GTAVN-VIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVEVEVLGDGRPP---FETPPDSPLVAAARAAIREV 322
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429239506 406 YGITPDFVREGGSIPVTVtFEQSLKKNVLLLPMGRGdDGAHSINEKLDLDNFLKGIKLFCTYVHELA 472
Cdd:COG0624 323 TGKEPVLSGVGGGTDARF-FAEALGIPTVVFGPGDG-AGAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
1-454 |
1.19e-68 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 225.94 E-value: 1.19e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 1 MKMSLDKLYEVIDKKKDEFVTRLSRAVSIPSVSADVTLRPKVVEMADFVVSEFTKLGAkmekRDIGYHQMDGQdvplpPI 80
Cdd:PRK07907 2 TILTADDLRARVAELLPRVRADLEELVRIPSVAADPFRREEVARSAEWVADLLREAGF----DDVRVVSADGA-----PA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 81 VLGQYGNDPSKKTVLIYNHFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAhkeLGIDFPVNLL 160
Cdd:PRK07907 73 VIGTRPAPPGAPTVLLYAHHDVQPPGDPDAWDSPPFELTERD-GRLYGRGAADDKGGIAMHLAALRA---LGGDLPVGVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 161 MCFEGMEEYGSEGLEDLIRAEAEkyFAKADCVCISDTYWLGTKKPVLTYGLRGVCYFNITVEGPSADLHSGVFGGTVHEP 240
Cdd:PRK07907 149 VFVEGEEEMGSPSLERLLAEHPD--LLAADVIVIADSGNWSVGVPALTTSLRGNADVVVTVRTLEHAVHSGQFGGAAPDA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 241 MTDLVAIMSTLVKPNGEILIPGImdqvaeltpTEDSIYDGIDYTMEDLKEAVGA--DISIYPDpKRTLQHRWRYPTLSLH 318
Cdd:PRK07907 227 LTALVRLLATLHDEDGNVAVDGL---------DATEPWLGVDYDEERFRADAGVldGVELIGT-GSVADRLWAKPAITVI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 319 GIEgAFSGSGAKTVIPAKVIGKFSIRTVPNMESETVERLVKEHVTK--VFNSlnsknKLAFNNMHSGSWWISSPDHWHYD 396
Cdd:PRK07907 297 GID-APPVAGASNALPPSARARLSLRVAPGQDAAEAQDALVAHLEAhaPWGA-----HVTVERGDAGQPFAADASGPAYD 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 397 VGKKATERVYGITPDFVREGGSIPVTVTFeQSLKKNVLLLPMGRGDDG--AHSINEKLDL 454
Cdd:PRK07907 371 AARAAMREAWGKDPVDMGMGGSIPFIAEL-QEAFPQAEILVTGVEDPKtrAHSPNESVHL 429
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
16-474 |
1.55e-64 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 215.00 E-value: 1.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 16 KDEFVTRLSRAVSIPSVSADvtlRPKVVEMADFVVSEFTKLGAKMEKRDIGYHqmdgqdvplpPIVLGQYgNDPSKKTVL 95
Cdd:PRK06446 1 MDEELYTLIEFLKKPSISAT---GEGIEETANYLKDTMEKLGIKANIERTKGH----------PVVYGEI-NVGAKKTLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 96 IYNHFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGiDFPVNLLMCFEGMEEYGSEGLE 175
Cdd:PRK06446 67 IYNHYDVQPVDPLSEWKRDPFSATIEN-GRIYARGASDNKGTLMARLFAIKHLIDKH-KLNVNVKFLYEGEEEIGSPNLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 176 DLIRAEAEKYfaKADCVcISDTYWLGTK-KPVLTYGLRGVCYFNITVEGPSADLHSgVFGGTVHEPMTDLVAIMSTLVKP 254
Cdd:PRK06446 145 DFIEKNKNKL--KADSV-IMEGAGLDPKgRPQIVLGVKGLLYVELVLRTGTKDLHS-SNAPIVRNPAWDLVKLLSTLVDG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 255 NGEILIPGIMDQVAELTPTEDSIYDGIDYTMEDLKEAVGADISIYPDPKRTLQHRWRYPTLSLHGIEGAFSGSGAKTVIP 334
Cdd:PRK06446 221 EGRVLIPGFYDDVRELTEEERELLKKYDIDVEELRKALGFKELKYSDREKIAEALLTEPTCNIDGFYSGYTGKGSKTIVP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 335 AKVIGKFSIRTVPNMESETVERLVKEHVTKVFNSLNSKnklafnnMHSGSWWI-SSPDHwhyDVGK---KATERVYGITP 410
Cdd:PRK06446 301 SRAFAKLDFRLVPNQDPYKIFELLKKHLQKVGFNGEII-------VHGFEYPVrTSVNS---KVVKamiESAKRVYGTEP 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429239506 411 DFV-REGGSIPVTVtFEQSLKKNVLLLPMGRGDDG--AHSINEKLDLDNFLKGIKLFCTYVHELASV 474
Cdd:PRK06446 371 VVIpNSAGTQPMGL-FVYKLGIRDIVSAIGVGGYYsnAHAPNENIRIDDYYKAIKHTEEFLKLYSTL 436
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
27-464 |
6.27e-52 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 182.30 E-value: 6.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 27 VSIPSVSADVTLRPKVVemaDFVVSEFTKLGAKMEKrdigyhqmdgqdvpLP----PIVLGQYGNDPSKKTVLIYNHFDV 102
Cdd:cd05678 9 VSIPNDATDEEEMRKNV---DWLEQAFRKRGFKTSQ--------------LPtsglPLLLAEKPISDARKTVLFYMHLDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 103 QPASL-----------------EDG-WST---DPFTLTVDNKGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLM 161
Cdd:cd05678 72 QPVDPskwdqkspytpvlkrkdAAGnWEEinwDAIFSNLDPEWRVFARAAADDKGPIMMMLAALDALKAGGIAPKFNVKI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 162 CFEGMEEYGSEGLEDLIRAEAEKYfaKADCVCISDTYWLGTKKPVLTYGLRGVCYFNITVEGPSADLHSGVFGGTVHEPM 241
Cdd:cd05678 152 ILDSEEEKGSPSLPKAVKEYKELL--AADALIIMDGPAHATNKPTLTFGCRGIATATLTTYGAKVPQHSGHYGNYAPNPA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 242 TDLVAIMSTLVKPNGEILIPGimdqvaeltptedsIYDGIDYTMEDLK---------EAVGADISIYPDPK--RTLQHRW 310
Cdd:cd05678 230 FRLSSLLASMKDDTGKVTIPG--------------FYDGISIDEETQKilaavpddeESINKRLGIAQTDKvgRNYQEAL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 311 RYPTLSLHGIEGAFSGSGAKTVIPAKVIGKFSIRTVPNMESETVERLVKEHVTKVFNSLNSKN-----KLAFNNMHSGSw 385
Cdd:cd05678 296 QYPSLNVRGMESGWKGDKVRTIIPEIAEAEIDIRLVPESDGPYLLDLVKAHIEKQGYFVTDRAptdeeRLAHDKIAKFT- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 386 WISSPDHWHYD----VGKKATE---RVYGITPDFVR-EGGSIPVTvTFEQSLKKNVLLLPMGRGDDGAHSINEKLDLDNF 457
Cdd:cd05678 375 YRNGADAFRTDinspIGNWLRKaltDEFGEEPIQIRmMGGTVPIA-PFVNVLDIPAIIVPMVNMDNNQHSPNENLRIGNI 453
|
....*..
gi 429239506 458 LKGIKLF 464
Cdd:cd05678 454 RTGIRTC 460
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
95-470 |
5.56e-47 |
|
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: 164.83 E-value: 5.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 95 LIYNHFDVQPASLEDGWstdPFTLTVDnkGRMFGRGATDDKGPLIGWISAIEAHKELGIDfPVNLLMCFEGMEEYGSEGL 174
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTED--GKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGGMGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 175 EDLIRAEAEKYFaKADCV---CISD-TYWLGTKKPVLTYGLRGVCYFNITVEGPSAdlHSGVFgGTVHEPMTDLVAIMST 250
Cdd:pfam01546 75 RALIEDGLLERE-KVDAVfglHIGEpTLLEGGIAIGVVTGHRGSLRFRVTVKGKGG--HASTP-HLGVNAIVAAARLILA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 251 LVKPNGEILIPGImdqvaeltptedsiydgidytmedlkeavGADISIypdpkrtlqhrwryptLSLHGIEGAFsgsgak 330
Cdd:pfam01546 151 LQDIVSRNVDPLD-----------------------------PAVVTV----------------GNITGIPGGV------ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 331 TVIPAKVIGKFSIRTVPNMESETVERLVKEHVTKVFNSLNSKNKLAFnnMHSGSWWISSPDHWhYDVGKKATERVYGITP 410
Cdd:pfam01546 180 NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVEVEY--VEGGAPPLVNDSPL-VAALREAAKELFGLKV 256
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429239506 411 DFVREGGS-----------IPVTVTFeqslkknvlllpMGRGDDGAHSINEKLDLDNFLKGIKLFCTYVHE 470
Cdd:pfam01546 257 ELIVSGSMggtdaaffllgVPPTVVF------------FGPGSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
86-468 |
1.87e-26 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 111.27 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 86 GNDPSKKTVLIYNHFDVQPASleDGWSTD--PFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPvNLLMCF 163
Cdd:cd05682 68 GTEQDDDTVLLYGHMDKQPPF--TGWDEGlgPTKPVIRG-DKLYGRGGADDGYAIFASLTAIKALQEQGIPHP-RCVVLI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 164 EGMEEYGSEGLEDLIRAEAEKYFAKADCVCIS------DTYWLgtkkpvlTYGLRGVCYFNITVEGPSADLHSGVFGGTV 237
Cdd:cd05682 144 EACEESGSADLPFYLDKLKERIGNVDLVVCLDsgcgnyEQLWL-------TTSLRGVLGGDLTVQVLNEGVHSGDASGIV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 238 HEPMTDLVAIMSTLVKPN-GEIL-------IPG--------IMDQVAELTPTEDSIYDGIDYTMEDLKEAVgadisiypd 301
Cdd:cd05682 217 PSSFRILRQLLSRIEDENtGEVKldeqhcdIPAhryeqakkIAEILGEAVYEEFPFVSGVQPVTTDLVQLY--------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 302 pkrtLQHRWRyPTLSLHGIEGAFSGSGAKTVIPAKVIGKFSIRTVPNMESETVERLVKEHVTK--VFNSlnsknKLAFNN 379
Cdd:cd05682 288 ----LNRTWK-PQLSVTGADGLPPASTAGNVLRPETTLKLSLRLPPTVDAEKASAALKKLLETdpPYNA-----KVTFKS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 380 MHSGSWWiSSPD--HWHYDVGKKATERVYGITPDFVREGGSIPVTVTF-EQSLKKNVLLLPMGRGDDGAHSINEKLDLdN 456
Cdd:cd05682 358 DGAGSGW-NAPLlsPWLAKALNEASQLFFGKPAAYQGEGGSIPFMNMLgEKFPKAQFIVTGVLGPKSNAHGPNEFLHI-P 435
|
410
....*....|..
gi 429239506 457 FLKGIKLFCTYV 468
Cdd:cd05682 436 YTKKLTACVAYV 447
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
18-452 |
4.39e-25 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 107.20 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 18 EFVTRLSRAVSIPSVSADVTLRPKVVE-MADFVVSEFTKLGakmekrdigyHQMDGQDVPLP---PIVLGQYGNDPSKKT 93
Cdd:cd05679 5 AFLAELARRVAVPTESQEPARKPELRAyLDQEMRPRFERLG----------FTVHIHDNPVAgraPFLIAERIEDPSLPT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 94 VLIYNHFDVQPAslEDG-WST--DPFTLTVDNKgRMFGRGATDDKGPLIGWISAIEAHKEL---GIDFPVNLLMcfEGME 167
Cdd:cd05679 75 LLIYGHGDVVPG--YEGrWRDgrDPWTVTVWGE-RWYGRGTADNKGQHSINMAALRQVLEArggKLGFNVKFLI--EMGE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 168 EYGSEGLEDLIRAEAEKYfaKADCVCISDTYWLGTKKPVLTYGLRGVCYFNITVEGPSADLHSGVFGGTVHEPMTDLVAI 247
Cdd:cd05679 150 EMGSPGLRAFCFSHREAL--KADLFIASDGPRLAADRPTMFLGSRGGLNFELRVNLREGGHHSGNWGGLLANPGIILANA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 248 MSTLVKPNGEILIPGIMDqvAELTPTedsiydgIDYTMEDLKEAVGADisiypDPkrTLQHRWRYPTLSLHgiEGAF--- 324
Cdd:cd05679 228 IASLVDGKGRIKLPALKP--AHLPNS-------VRSALADVEVGGGPD-----DP--SIDPWWGEPGLTAA--ERVFgwn 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 325 --------SGSGAKTV--IPAKVIGKFSIRTVPNMESETVERLVKEH-VTKVFNSLN---SKNKLAFNNMHSGSWWISsp 390
Cdd:cd05679 290 tlevlafkTGNPDAPVnaIPGHAEAICQIRFVVGTDPDTFIPAVRAHlDANGFDGVEvtaSQMVFAATRLDPDSPWVG-- 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 429239506 391 dhWHYDVGKKATERVYGITPDFvreGGSIPVTVtFEQSLKKNVLLLPMGRGDDGAHSINEKL 452
Cdd:cd05679 368 --WALASLQKTTGKKPALLPNL---GGSLPNDV-FSEVLGLPTLWVPHSYPACSQHAPNEHI 423
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
18-361 |
3.23e-24 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 105.00 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 18 EFVTRLSRAVSIPSVSADVTLRPKVVE-MADFVVSEFTKLGAKMEkrdigyhQMDGQDVPLPPIVLGQYGNDPSKKTVLI 96
Cdd:PRK07079 18 AFFADLARRVAYRTESQNPDRAPALRAyLTDEIAPALAALGFTCR-------IVDNPVAGGGPFLIAERIEDDALPTVLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 97 YNHFDVQPAsLEDGWST--DPFTLTVDNkGRMFGRGATDDKGP-LIGwISAIEAHKE-----LGidFPVNLLmcFEGMEE 168
Cdd:PRK07079 91 YGHGDVVRG-YDEQWREglSPWTLTEEG-DRWYGRGTADNKGQhTIN-LAALEQVLAarggrLG--FNVKLL--IEMGEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 169 YGSEGLEDLIRAEAEKYfaKADCVCISDTYWLGTKKPVLTYGLRGVCYFNITVEGPSADLHSGVFGGTVHEPMTDLVAIM 248
Cdd:PRK07079 164 IGSPGLAEVCRQHREAL--AADVLIASDGPRLSAERPTLFLGSRGAVNFRLRVNLRDGAHHSGNWGGLLRNPGTVLAHAI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 249 STLVKPNGEIlipgimdQVAELTPteDSIYDGIDYTMEDLKEAVGADisiypDPkrTLQHRWRYPTLS----LHG---IE 321
Cdd:PRK07079 242 ASLVDARGRI-------QVPGLRP--PPLPAAVRAALADITVGGGPG-----DP--AIDPDWGEPGLTpaerVFGwntLE 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 429239506 322 G-AF-SGSGAKTV--IPAKVIGKFSIRTVPNMESETVERLVKEH 361
Cdd:PRK07079 306 VlAFkTGNPDAPVnaIPGSARAVCQLRFVVGTDWENLAPHLRAH 349
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
12-473 |
5.40e-23 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 100.45 E-value: 5.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 12 IDKKKDEFVTRLSRAVSIPSVsadVTLRPKVVEMADFVVSEFTKLGAKMEKRDIGYHQMDGQDVPLPPIVLGQYgndpSK 91
Cdd:PRK08651 1 VEAMMFDIVEFLKDLIKIPTV---NPPGENYEEIAEFLRDTLEELGFSTEIIEVPNEYVKKHDGPRPNLIARRG----SG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 92 KTVLIYN-HFDVQPASleDGW-STDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGidfPVNLLMCFEGMEEY 169
Cdd:PRK08651 74 NPHLHFNgHYDVVPPG--EGWsVNVPFEPKVKD-GKVYGRGASDMKGGIAALLAAFERLDPAG---DGNIELAIVPDEET 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 170 GSEGLEDLiraeAEKYFAKADCVCI-----SDTYWlgtkkpvltYGLRGVCYFNITVEGPSAdlHSGvfggtvhEPMTDL 244
Cdd:PRK08651 148 GGTGTGYL----VEEGKVTPDYVIVgepsgLDNIC---------IGHRGLVWGVVKVYGKQA--HAS-------TPWLGI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 245 VAIMstlvkpngeilipgimdqvaeltptedsiydGIDYTMEDLKEAVGADISIYPDPkrtlQHRWRYPTLSLHG--IEG 322
Cdd:PRK08651 206 NAFE-------------------------------AAAKIAERLKSSLSTIKSKYEYD----DERGAKPTVTLGGptVEG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 323 afsgsGAKT-VIPAKVigKFSI--RTVPNMESETVERLVKEHVTKVFNSLNSKNKLAFNNMHSGSWwiSSPDHWHYDVGK 399
Cdd:PRK08651 251 -----GTKTnIVPGYC--AFSIdrRLIPEETAEEVRDELEALLDEVAPELGIEVEFEITPFSEAFV--TDPDSELVKALR 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 400 KATERVYGITPD------------FVREGgsIPvTVTFeqslkknvlllpmGRGDDG-AHSINEKLDLDNFLKGIKLFCT 466
Cdd:PRK08651 322 EAIREVLGVEPKktislggtdarfFGAKG--IP-TVVY-------------GPGELElAHAPDEYVEVKDVEKAAKVYEE 385
|
....*..
gi 429239506 467 YVHELAS 473
Cdd:PRK08651 386 VLKRLAK 392
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
23-464 |
1.48e-22 |
|
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: 98.53 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 23 LSRAVSIPSVSadvtlrPKVVEMADFVVSEFTKLGAKMEkrdigyhqmdgqdvplpPIVLGQYGN-----DPSKKTVLIY 97
Cdd:cd08659 3 LQDLVQIPSVN------PPEAEVAEYLAELLAKRGYGIE-----------------STIVEGRGNlvatvGGGDGPVLLL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 98 N-HFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEYGSEGLED 176
Cdd:cd08659 60 NgHIDTVPPGDGDKWSFPPFSGRIRD-GRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 177 LIraeAEKYFAKADCVCISD-TYwlgtkkPVLTYGLRGVCYFNITVEGPSAdlHSGvfggtvhEPMTDLVAImstlvkpn 255
Cdd:cd08659 139 LL---EAGYADRLDALIVGEpTG------LDVVYAHKGSLWLRVTVHGKAA--HSS-------MPELGVNAI-------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 256 gEILIPGImdqvaeltptedsiydgidYTMEDLKEAVGADISIYPdpkrtlqhrwryPTLSLHGIEGafsGSGAKtVIPA 335
Cdd:cd08659 193 -YALADFL-------------------AELRTLFEELPAHPLLGP------------PTLNVGVING---GTQVN-SIPD 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 336 KVIGKFSIRTVPNMESETVERLVKEHVTKVFNSLNSKnklafNNMHSGSWWISSPDHWHYDVGKKATERVYGITPdfVRe 415
Cdd:cd08659 237 EATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVE-----VSLDGDPPFFTDPDHPLVQALQAAARALGGDPV--VR- 308
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 429239506 416 ggsiPVTVTFEQSL---KKNVLLLPMGRGDDG-AHSINEKLDLDNFLKGIKLF 464
Cdd:cd08659 309 ----PFTGTTDASYfakDLGFPVVVYGPGDLAlAHQPDEYVSLEDLLRAAEIY 357
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
23-462 |
2.81e-20 |
|
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: 92.08 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 23 LSRAVSIPSVSADvtlRPKVVEMADFVVSEFTKLGAKMEKRDIGyhqmDGQDVPLPPIVLGQYGNDPSKktVLIYN-HFD 101
Cdd:TIGR01910 4 LKDLISIPSVNPP---GGNEETIANYIKDLLREFGFSTDVIEIT----DDRLKVLGKVVVKEPGNGNEK--SLIFNgHYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 102 VQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEYGSEGLEDLIrae 181
Cdd:TIGR01910 75 VVPAGDLELWKTDPFKPVEKD-GKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLL--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 182 AEKYFAKADCVCISDTywlgTKKPVLTYGLRGVCYFNITVEGPSAdlHSGVfggtvhePMTDLVAIMSTlvkpngeilip 261
Cdd:TIGR01910 151 QRGYFKDADGVLIPEP----SGGDNIVIGHKGSIWFKLRVKGKQA--HASF-------PQFGVNAIMKL----------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 262 giMDQVAELTPTEDSIYDGIDYTMEDLKeavgadISIYPdpkrtlqhrwryptlslhgieGAFSGSGAKTVIPAKVIGKF 341
Cdd:TIGR01910 207 --AKLITELNELEEHIYARNSYGFIPGP------ITFNP---------------------GVIKGGDWVNSVPDYCEFSI 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 342 SIRTVPNMESETverlVKEHVTKVFNSLNSKNKLAFNN---MHSGSWWISSPDHWHYDVGKKATERVYGITPdfvrEGGS 418
Cdd:TIGR01910 258 DVRIIPEENLDE----VKQIIEDVVKALSKSDGWLYENepvVKWSGPNETPPDSRLVKALEAIIKKVRGIEP----EVLV 329
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 429239506 419 IPVTVTFEQSLKKNVLLLPMGRGDDG-AHSINEKLDLDNFLKGIK 462
Cdd:TIGR01910 330 STGGTDARFLRKAGIPSIVYGPGDLEtAHQVNEYISIKNLVESTK 374
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
80-211 |
9.59e-18 |
|
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: 81.32 E-value: 9.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 80 IVLGQYGNDPSKKTVLIYNHFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNL 159
Cdd:cd18669 1 NVIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEE-GRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 429239506 160 LMCFEGMEEYGSEGLEDLIRAEAEKYFAKADCVCISDTYWLGTKKPVLTYGL 211
Cdd:cd18669 80 VVAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTPL 131
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
10-188 |
1.43e-17 |
|
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: 84.60 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 10 EVIDKKKDEFVTRLSRAVSIPSVSADVT----LRPKVVEMADFVVSEFTKLGAKMEKRD--IGYhqmdgqdvplppivlG 83
Cdd:cd03888 1 EEIDKYKDEILEDLKELVAIPSVRDEATegapFGEGPRKALDKFLDLAKRLGFKTKNIDnyAGY---------------A 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 84 QYGNDpsKKTVLIYNHFDVQPASleDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCF 163
Cdd:cd03888 66 EYGEG--EEVLGILGHLDVVPAG--EGWTTDPFKPVIKD-GKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIF 140
|
170 180
....*....|....*....|....*
gi 429239506 164 EGMEEYGSEGLedliraeaEKYFAK 188
Cdd:cd03888 141 GTDEETGWKCI--------EHYFEH 157
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
86-461 |
2.87e-17 |
|
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.
Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 83.56 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 86 GNDPSKKTVLIYNHFDVQPASLEDgWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEG 165
Cdd:cd05675 60 GTDPSAGPLLLLGHIDVVPADASD-WSVDPFSGEIKD-GYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 166 MEEYGSE-GLEDLIRaEAEKYFAKADcVCISDTYW--LGTKKPVLTY----GLRGVCYFNITVEGPSAdlHsgvfGGTVH 238
Cdd:cd05675 138 DEEAGGEnGAKWLVD-NHPELFDGAT-FALNEGGGgsLPVGKGRRLYpiqvAEKGIAWMKLTVRGRAG--H----GSRPT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 239 EP--MTDLVAIMSTL------VKPNGEiliPGIMDQVAELTPTEDSIYDgiDYTMEDLKEAVGADISIYPDPKRTLQHrw 310
Cdd:cd05675 210 DDnaITRLAEALRRLgahnfpVRLTDE---TAYFAQMAELAGGEGGALM--LTAVPVLDPALAKLGPSAPLLNAMLRN-- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 311 rypTLSLHGIEGAFsgsgAKTVIPAKVIGKFSIRTVPnmesETVERLVKEHVTKVFNSLNSKNKLAfnnmHSGSWWISSP 390
Cdd:cd05675 283 ---TASPTMLDAGY----ATNVLPGRATAEVDCRILP----GQSEEEVLDTLDKLLGDPDVSVEAV----HLEPATESPL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 391 DHWHYDVGKKATERVYgitPDfvreGGSIPVTVTFEQSLKK-----------NVLLLPMGRGD-DGAHSINEKLDLDNFL 458
Cdd:cd05675 348 DSPLVDAMEAAVQAVD---PG----APVVPYMSPGGTDAKYfrrlgipgygfAPLFLPPELDYtGLFHGVDERVPVESLY 420
|
...
gi 429239506 459 KGI 461
Cdd:cd05675 421 FGV 423
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
20-472 |
1.37e-16 |
|
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: 80.89 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 20 VTRLSRAVSIPSVS--ADVTLrpkvvEMADFVVSEFTKLGAKMEKRDIGyHQMDGQDvplPPIVLGQygndpsKKTVLIY 97
Cdd:cd08011 1 VKLLQELVQIPSPNppGDNTS-----AIAAYIKLLLEDLGYPVELHEPP-EEIYGVV---SNIVGGR------KGKRLLF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 98 N-HFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEE----YGSE 172
Cdd:cd08011 66 NgHYDVVPAGDGEGWTVDPYSGKIKD-GKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEEtggrAGTK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 173 GLedliraeAEKYFAKADCVCISDTywlgTKKPVLTYGLRGVCYFNITVEGPSAdlHsgvfGGTVHEPMTDLVAIMSTLv 252
Cdd:cd08011 145 YL-------LEKVRIKPNDVLIGEP----SGSDNIRIGEKGLVWVIIEITGKPA--H----GSLPHRGESAVKAAMKLI- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 253 kpngeilipgimdqvaeltptedsiydgidytmEDLKEAVgadisiypdpkrtlqhrwryPTLSLHGIEGafsGSGAKTV 332
Cdd:cd08011 207 ---------------------------------ERLYELE--------------------KTVNPGVIKG---GVKVNLV 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 333 iPAKVIGKFSIRTVPNMESETVERLVKEHVTKVfnslnSKNKLAFNNMHSGSWwiSSPDHWHYDVGKKATERVYGITPdf 412
Cdd:cd08011 231 -PDYCEFSVDIRLPPGISTDEVLSRIIDHLDSI-----EEVSFEIKSFYSPTV--SNPDSEIVKKTEEAITEVLGIRP-- 300
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429239506 413 vregGSIPVTVTFEQSL--KKNVLLLPMGRGD-DGAHSINEKLDLDNFLKGIKlfctyVHELA 472
Cdd:cd08011 301 ----KEVISVGASDARFyrNAGIPAIVYGPGRlGQMHAPNEYVEIDELIKVIK-----VHALV 354
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
16-227 |
4.23e-16 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 80.11 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 16 KDEFVTRLSRAVSIPSV------SADVTLRPKVVEMADFVVSEFTKLGAKMEKRD--IGYHQMdGQDvplppivlgqygn 87
Cdd:TIGR01887 1 KDEILEDLKELIAIDSVedlekaKEGAPFGEGPRKALDKFLEIAKRDGFTTENVDnyAGYIEY-GQG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 88 dpsKKTVLIYNHFDVQPASleDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGME 167
Cdd:TIGR01887 67 ---EEVLGILGHLDVVPAG--DGWTSPPFEPTIKD-GRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDE 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429239506 168 EYGSEGLEDLIRAEAEKYFAKA-DCvcisdtywlgtKKPVlTYGLRGVCYFNITVEGPSAD 227
Cdd:TIGR01887 141 ESGWKCIDYYFEHEEMPDIGFTpDA-----------EFPI-IYGEKGITTLEIKFKDDTEG 189
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
80-216 |
1.92e-15 |
|
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 74.77 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 80 IVLGQYGNDPSKKTVLIYNHFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNL 159
Cdd:cd03873 1 NLIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEE-GRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTI 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 429239506 160 LMCFEGMEEYGSEGLEDLIRAEAEKYFAKADCVCISDTYWlgTKKPVLTYGLRGVCY 216
Cdd:cd03873 80 VVAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDATA--GPILQKGVVIRNPLV 134
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
13-196 |
1.27e-14 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 75.27 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 13 DKKKDEFVTRLSRAVSIPSVSADVTlRPKVVEMADFVVSEFTKLGAKMEKRdigYHQMDgQDVPL---PPIVLGQYGNDP 89
Cdd:PRK13983 1 DELRDEMIELLSELIAIPAVNPDFG-GEGEKEKAEYLESLLKEYGFDEVER---YDAPD-PRVIEgvrPNIVAKIPGGDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 90 sKKTVLIYNHFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEY 169
Cdd:PRK13983 76 -KRTLWIISHMDVVPPGDLSLWETDPFKPVVKD-GKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEET 153
|
170 180
....*....|....*....|....*...
gi 429239506 170 GSE-GLEDLIRAEAEkYFAKADCVCISD 196
Cdd:PRK13983 154 GSKyGIQYLLKKHPE-LFKKDDLILVPD 180
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
79-227 |
1.16e-13 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 72.34 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 79 PIVLGQYGNDPSKKTVLIYN-HFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPV 157
Cdd:cd03895 61 PNVVGTHRPRGETGRSLILNgHIDVVPEGPVELWTRPPFEATIVD-GWMYGRGAGDMKAGLAANLFALDALRAAGLQPAA 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429239506 158 NLLmcFEGM--EEYGSEG-LEDLIRAeaekYfaKADCVCISDTYwlgtkKPVLTYGLRGVCYFNITVEGPSAD 227
Cdd:cd03895 140 DVH--FQSVveEECTGNGaLAALMRG----Y--RADAALIPEPT-----ELKLVRAQVGVIWFRVKVRGTPAH 199
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
5-251 |
2.31e-13 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 71.61 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 5 LDKLYEVIDKKKDEFVTRLSRAVSIPSVS--ADVTlrpkvVEMADFVVSEFTKLGAKMEKRDIgYhqmdgqdvPLPPIVL 82
Cdd:PRK08596 1 VSQLLEQIELRKDELLELLKTLVRFETPAppARNT-----NEAQEFIAEFLRKLGFSVDKWDV-Y--------PNDPNVV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 83 GQY-GNDPSKKTVLIYN-HFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLL 160
Cdd:PRK08596 67 GVKkGTESDAYKSLIINgHMDVAEVSADEAWETNPFEPTIKD-GWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 161 mcFEGM--EEYGSEGLEdliraEAEKYFAKADCVCISDTYWLGTKkpvltyGLRGVCYFNITVEGP--------SADLHS 230
Cdd:PRK08596 146 --FQSVigEEVGEAGTL-----QCCERGYDADFAVVVDTSDLHMQ------GQGGVITGWITVKSPqtfhdgtrRQMIHA 212
|
250 260
....*....|....*....|...
gi 429239506 231 G--VFGGTVHEPMTDLVAIMSTL 251
Cdd:PRK08596 213 GggLFGASAIEKMMKIIQSLQEL 235
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
23-359 |
3.40e-13 |
|
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: 70.70 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 23 LSRAVSIPSVSADVTLrpkvvEMADFVVSEFTKLGAKMEkrdIGYHQMDGQdvplpPIVLGQYGNDPSKKTVLiYNHFDV 102
Cdd:cd03894 3 LARLVAFDTVSRNSNL-----ALIEYVADYLAALGVKSR---RVPVPEGGK-----ANLLATLGPGGEGGLLL-SGHTDV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 103 QPAsleDG--WSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEgmEEYGSEGLEDLIRA 180
Cdd:cd03894 69 VPV---DGqkWSSDPFTLTERD-GRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYD--EEVGCLGVRHLIAA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 181 EAEKYFaKADCVCISDTYWLgtkKPVLtyGLRGVCYFNITVEGP---SADLHSGVfggTVHEPMTDlvaimstlvkpnge 257
Cdd:cd03894 143 LAARGG-RPDAAIVGEPTSL---QPVV--AHKGIASYRIRVRGRaahSSLPPLGV---NAIEAAAR-------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 258 iLIPGIMDQVAELTPTE-DSIYDGidytmedlkeavgadisiyPdpkrtlqhrwrYPTLSLHGIEGafsGSgAKTVIPAK 336
Cdd:cd03894 200 -LIGKLRELADRLAPGLrDPPFDP-------------------P-----------YPTLNVGLIHG---GN-AVNIVPAE 244
|
330 340
....*....|....*....|...
gi 429239506 337 VIGKFSIRTVPNMESETVERLVK 359
Cdd:cd03894 245 CEFEFEFRPLPGEDPEAIDARLR 267
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
17-230 |
4.42e-12 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 68.05 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 17 DEFVTRLSRAVSIPSVSADvtLRPKV-----VEMADFVVSEFTKLGAKMEKRDIGYHQmdgqdvplppIVLGQYGNDPSK 91
Cdd:PRK08262 44 DAAAERLSEAIRFRTISNR--DRAEDdaaafDALHAHLEESYPAVHAALEREVVGGHS----------LLYTWKGSDPSL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 92 KTVLIYNHFDVQPA--SLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEY 169
Cdd:PRK08262 112 KPIVLMAHQDVVPVapGTEGDWTHPPFSGVIAD-GYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEV 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429239506 170 GSEG---LEDLIRAEAEkyfaKADCVC-----ISDTYWLGTKKPVLTYGLRGVCYFNITVEGPSADLHS 230
Cdd:PRK08262 191 GGLGaraIAELLKERGV----RLAFVLdeggaITEGVLPGVKKPVALIGVAEKGYATLELTARATGGHS 255
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
22-147 |
4.94e-12 |
|
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: 67.67 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 22 RLSRAVSIPSVSADVTLRP-------KVVEMADFVVSEFTKLGAKMEKRDIGYHQmdgqdvplppIVLGQYGNDPSKKTV 94
Cdd:cd05674 3 RLSGAVQIPTVSFDDMPPIdederwdAFYKFHDYLEKTFPLVHKTLKVEVVNEYG----------LLYTWEGSDPSLKPL 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 429239506 95 LIYNHFDVQPA--SLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEA 147
Cdd:cd05674 73 LLMAHQDVVPVnpETEDQWTHPPFSGHYDG-GYIWGRGALDDKNSLIGILEAVEL 126
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
1-155 |
6.22e-12 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 67.56 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 1 MKMSLDKLyevIDKKKDEFVTRLSRAVSIPSV------SADVTLRPKVVEMADFvvseFTKLGakmeKRDiGY--HQMDG 72
Cdd:PRK07318 1 MTIDWKKE---VEKRKDDLIEDLQELLRINSVrddskaKEGAPFGPGPVKALEK----FLEIA----ERD-GFktKNVDN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 73 qdvplppiVLG--QYGNdpSKKTVLIYNHFDVQPASleDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKE 150
Cdd:PRK07318 69 --------YAGhiEYGE--GEEVLGILGHLDVVPAG--DGWDTDPYEPVIKD-GKIYARGTSDDKGPTMAAYYALKIIKE 135
|
....*
gi 429239506 151 LGIDF 155
Cdd:PRK07318 136 LGLPL 140
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
14-155 |
7.52e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 67.03 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 14 KKKDEFVTRLSRAVSIPSVSADVTLRPKVVEMADFVVSEFTKLGakmekRDIGYHQMDGQDvplppivlGQYGN---DPS 90
Cdd:PRK07205 8 KVQDACVAAIKTLVSYPSVLNEGENGTPFGQAIQDVLEATLDLC-----QGLGFKTYLDPK--------GYYGYaeiGQG 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429239506 91 KKTVLIYNHFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDF 155
Cdd:PRK07205 75 EELLAILCHLDVVPEGDLSDWQTPPFEAVEKD-GCLFGRGTQDDKGPSMAALYAVKALLDAGVQF 138
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
17-474 |
1.41e-11 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 65.97 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 17 DEFVTRLSRAVSIPSVSADvtlrPKVVEMADFVVSEFTKLGAKMEKRDIgyhqmdgqdVPLPPIVLGQY-GNDPSKKTVL 95
Cdd:TIGR01880 9 DIAVTRFREYLRINTVQPN----PDYAACVDFLIKQADELGLARKTIEF---------VPGKPVVVLTWpGSNPELPSIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 96 IYNHFDVQPASLEDgWSTDPFTLTVDNKGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEE-YGSEGL 174
Cdd:TIGR01880 76 LNSHTDVVPVFREH-WTHPPFSAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEiGGHDGM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 175 EDLirAEAEKYfaKADCVCISDTYWLGTKKPVLT--YGLRGVCYFNITVEGPSAdlHSGVFggtvhepmtdlvaimstlv 252
Cdd:TIGR01880 155 EKF--AKTDEF--KALNLGFALDEGLASPDDVYRvfYAERVPWWVVVTAPGNPG--HGSKL------------------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 253 kpngeilipgiMDQVAeltptedsiydgidytMEDLKEAVGADISIYPDPKRTLQHRWRYPTLSLHGIEGAFSGSGAKT- 331
Cdd:TIGR01880 210 -----------MENTA----------------MEKLEKSVESIRRFRESQFQLLQSNPDLAIGDVTSVNLTKLKGGVQSn 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 332 VIPAKVIGKFSIRTVPNMESETVE-RLVK------EHVTKVFNSLNSKNKLAFNNmHSGSWWISSPDHWHyDVGKKATER 404
Cdd:TIGR01880 263 VIPSEAEAGFDIRLAPSVDFEEMEnRLDEwcadagEGVTYEFSQHSGKPLVTPHD-DSNPWWVAFKDAVK-EMGCTFKPE 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 429239506 405 VYGITPD--FVREGGsIPvTVTFEqslkknvlllPMGRGDDGAHSINEKLDLDNFLKGIKLFCTYVHELASV 474
Cdd:TIGR01880 341 ILPGSTDsrYIRAAG-VP-ALGFS----------PMNNTPVLLHDHNEFLNEAVFLRGIEIYQTLISALASV 400
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
17-181 |
2.41e-11 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 65.37 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 17 DEFVTRLSRAVSIPSVSADVTLRPKVvemaDFVVSEFTKLGAKMEKRDIgyhqmdgqdVPLPPIVLGQY-GNDPSKKTVL 95
Cdd:cd05646 2 DPAVTRFREYLRINTVHPNPDYDACV----EFLKRQADELGLPVRVIEV---------VPGKPVVVLTWeGSNPELPSIL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 96 IYNHFDVQPAsLEDGWSTDPFTLTVDNKGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEYGS-EGL 174
Cdd:cd05646 69 LNSHTDVVPV-FEEKWTHDPFSAHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGhDGM 147
|
....*..
gi 429239506 175 EDLIRAE 181
Cdd:cd05646 148 EKFVKTE 154
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
6-156 |
2.70e-11 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 65.17 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 6 DKLYEVIDKKKDEFVTRLSRAVSIPsvsadvTLRP---KVVEMADFvvseftkLGAKMEKRD--IGYHQMDGQ--DVPLP 78
Cdd:PRK13013 3 DRLFAAIEARRDDLVALTQDLIRIP------TLNPpgrAYREICEF-------LAARLAPRGfeVELIRAEGApgDSETY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 79 PI--VLGQYGNDPSKKTVLIYNHFDVQPASleDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFP 156
Cdd:PRK13013 70 PRwnLVARRQGARDGDCVHFNSHHDVVEVG--HGWTRDPFGGEVKD-GRIYGRGACDMKGGLAASIIAAEAFLAVYPDFA 146
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
17-196 |
1.18e-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. 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: 63.25 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 17 DEFVTRLSRAVSIPSVSADVTlRPKVVEMADFVVSEFtklgakmekRDIGYHQMDGQDVP------LPPIVLG-QYGNDp 89
Cdd:cd05650 1 EEIIELERDLIRIPAVNPESG-GEGEKEKADYLEKKL---------REYGFYTLERYDAPdergiiRPNIVAKiPGGND- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 90 skKTVLIYNHFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEY 169
Cdd:cd05650 70 --KTLWIISHLDTVPPGDLSLWETDPWEPVVKD-GKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEED 146
|
170 180
....*....|....*....|....*...
gi 429239506 170 GSE-GLEDLIraEAEKYFAKADCVCISD 196
Cdd:cd05650 147 GSEyGIQYLL--NKFDLFKKDDLIIVPD 172
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
3-231 |
4.08e-10 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 61.49 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 3 MSLDKLYEVIDKKKDEFVTRLSRAVSIPSVSADVTlrpkvvEMADFVVSEFTKLG-AKMEKRDIGYhqmdgqdvplppiV 81
Cdd:PRK13004 1 IPFKLILMLAEKYKADMTRFLRDLIRIPSESGDEK------RVVKRIKEEMEKVGfDKVEIDPMGN-------------V 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 82 LGQYGNdpSKKTVLIYNHFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLM 161
Cdd:PRK13004 62 LGYIGH--GKKLIAFDAHIDTVGIGDIKNWDFDPFEGEEDD-GRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429239506 162 -------CFEGME-EYGSEglEDLIraeaekyfaKADCVCISDTYWLGTKKpvltyGLRGVCYFNITVEGPSAdlHSG 231
Cdd:PRK13004 139 tgtvqeeDCDGLCwRYIIE--EDKI---------KPDFVVITEPTDLNIYR-----GQRGRMEIRVETKGVSC--HGS 198
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
79-172 |
8.97e-10 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 60.56 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 79 PIVLGQYGNDPSKktVLIYNHFDVQPASLEDgWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVn 158
Cdd:PRK08554 53 YAVYGEIGEGKPK--LLFMAHFDVVPVNPEE-WNTEPFKLTVKG-DKAYGRGSADDKGNVASVMLALKELSKEPLNGKV- 127
|
90
....*....|....
gi 429239506 159 lLMCFEGMEEYGSE 172
Cdd:PRK08554 128 -IFAFTGDEEIGGA 140
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
5-152 |
1.02e-09 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 60.40 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 5 LDKLYEVIDKKKDEFVTRLSRAVSIPSvsadvtLRPKVVEMADFVVSEFTKLGAKME---------KRDIGY----HQMD 71
Cdd:PRK06837 8 TQRILAAVDAGFDAQVAFTQDLVRFPS------TRGAEAPCQDFLARAFRERGYEVDrwsidpddlKSHPGAgpveIDYS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 72 GQdvplpPIVLGQYgnDPSKKT--VLIYN-HFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAH 148
Cdd:PRK06837 82 GA-----PNVVGTY--RPAGKTgrSLILQgHIDVVPEGPLDLWSRPPFDPVIVD-GWMYGRGAADMKAGLAAMLFALDAL 153
|
....
gi 429239506 149 KELG 152
Cdd:PRK06837 154 RAAG 157
|
|
| dipeptidase |
TIGR01886 |
dipeptidase PepV; This model represents a small clade of dipeptidase enzymes which are members ... |
84-153 |
1.68e-09 |
|
dipeptidase PepV; This model represents a small clade of dipeptidase enzymes which are members of the larger M25 subfamily of metalloproteases. Two characterized enzymes are included in the seed. One, from Lactococcus lactis has been shown to act on a wide range of dipeptides, but not larger peptides. The enzyme from Lactobacillus delbrueckii was originally characterized as a Xaa-His dipeptidase, specifically a carnosinase (beta-Ala-His) by complementation of an E. coli mutant. Further study, including the crystallization of the enzyme, has shown it to also be a non-specific dipeptidase. This group also includes enzymes from Streptococcus and Enterococcus. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 130941 [Multi-domain] Cd Length: 466 Bit Score: 59.90 E-value: 1.68e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 84 QYGNdpSKKTVLIYNHFDVQPASleDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGI 153
Cdd:TIGR01886 73 EYGA--GDERLGIIGHMDVVPAG--EGWTRDPFEPEIDE-GRIYARGASDDKGPSLAAYYAMKILKELGL 137
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
19-232 |
1.80e-09 |
|
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: 59.14 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 19 FVTRLSRAVSIPSVSADVTLrpkVVEMADFVVSEFTKLGAKMEKRDIGYHQmdgqdvplpPIVLGQYGNDPSKKTVLIyN 98
Cdd:cd03885 1 MLDLLERLVNIESGTYDKEG---VDRVAELLAEELEALGFTVERRPLGEFG---------DHLIATFKGTGGKRVLLI-G 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 99 HFD-VQPA-SLEDgwstDPFtlTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEYGSEGLED 176
Cdd:cd03885 68 HMDtVFPEgTLAF----RPF--TVDG-DRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRE 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 177 LIRAEAekyfAKADCVcisdtywLGTKKPV----LTYGLRGVCYFNITVEGPSAdlHSGV 232
Cdd:cd03885 141 LIEEEA----KGADYV-------LVFEPARadgnLVTARKGIGRFRLTVKGRAA--HAGN 187
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
99-417 |
7.01e-09 |
|
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: 57.51 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 99 HFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLlmCF------EGMEEYGSE 172
Cdd:cd03891 62 HTDVVPPGDLEGWSSDPFSPTIKD-GMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSI--SFlitsdeEGPAIDGTK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 173 GLEDLIRAEAEkyfaKADCvCI----SDTYWLGTkkpVLTYGLRGVCYFNITVEgpsadlhsGVFGgtvHepmtdlVAIM 248
Cdd:cd03891 139 KVLEWLKARGE----KIDY-CIvgepTSEKKLGD---TIKIGRRGSLNGKLTIK--------GKQG---H------VAYP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 249 STLVKPngeilIPGIMDQVAELTPTEdsiydgIDYTMEDLkeavgadisiypdPKRTLQhrwryptlslhgIEGAFSGSG 328
Cdd:cd03891 194 HLADNP-----IHLLAPILAELTATV------LDEGNEFF-------------PPSSLQ------------ITNIDVGNG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 329 AKTVIPAKVIGKFSIRTvpNMESeTVERLvKEHVTKVFNSLNSKNKLAFNnmHSGSWWISSPDHwHYDVGKKATERVYGI 408
Cdd:cd03891 238 ATNVIPGELKAKFNIRF--NDEH-TGESL-KARIEAILDKHGLDYDLEWK--LSGEPFLTKPGK-LVDAVSAAIKEVTGI 310
|
....*....
gi 429239506 409 TPDFVREGG 417
Cdd:cd03891 311 TPELSTSGG 319
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
54-181 |
7.40e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 57.70 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 54 TKLGAKMEKR--DIGYHQMDGQDVPLPP----IVLGQYGNDPsKKTVLIYNHFDVQPASLEDgWSTDPFTLTVDNkGRMF 127
Cdd:PRK09133 59 TPAAEAMAARlkAAGFADADIEVTGPYPrkgnLVARLRGTDP-KKPILLLAHMDVVEAKRED-WTRDPFKLVEEN-GYFY 135
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 429239506 128 GRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEYGS--------EGLEDLIRAE 181
Cdd:PRK09133 136 GRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEGTPmngvawlaENHRDLIDAE 197
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
17-226 |
9.53e-09 |
|
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: 57.10 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 17 DEFVTRLSRAVSIPSVSADVTLRPKV--VEMADFVVseftklgAKMEKRDIGYHQMDGqdVPLPPIVLGQYGNDPSKKTV 94
Cdd:cd08013 1 DDPVSLTQTLVRINSSNPSLSATGGAgeAEIATYVA-------AWLAHRGIEAHRIEG--TPGRPSVVGVVRGTGGGKSL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 95 LIYNHFDVqpASLeDGWSTDPFTLTVdNKGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEgmEEYGSEGL 174
Cdd:cd08013 72 MLNGHIDT--VTL-DGYDGDPLSGEI-ADGRVYGRGTLDMKGGLAACMAALADAKEAGLRGDVILAAVAD--EEDASLGT 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 429239506 175 EDLIRAEaekyfAKADCVCISDTYWLgtkkpVLTYGLRGVCYFNITVEGPSA 226
Cdd:cd08013 146 QEVLAAG-----WRADAAIVTEPTNL-----QIIHAHKGFVWFEVDIHGRAA 187
|
|
| PRK06915 |
PRK06915 |
peptidase; |
95-239 |
4.88e-08 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 55.08 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 95 LIYN-HFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLmcFEGM--EEYGS 171
Cdd:PRK06915 96 MILNgHIDVVPEGDVNQWDHHPYSGEVIG-GRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVI--FQSVieEESGG 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429239506 172 EG-LEDLIRAeaekYfaKADCVCISD--TYWLGTKKpvltyglRGVCYFNITVEGPSAdlHsgvfGGTVHE 239
Cdd:PRK06915 173 AGtLAAILRG----Y--KADGAIIPEptNMKFFPKQ-------QGSMWFRLHVKGKAA--H----GGTRYE 224
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
99-194 |
5.08e-08 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 54.81 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 99 HFDVQPAsleDG--WSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEgmEEYGSEGLED 176
Cdd:PRK07522 72 HTDVVPV---DGqaWTSDPFRLTERD-GRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYD--EEVGCLGVPS 145
|
90
....*....|....*...
gi 429239506 177 LIrAEAEKYFAKADcVCI 194
Cdd:PRK07522 146 MI-ARLPERGVKPA-GCI 161
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
23-166 |
5.82e-08 |
|
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: 54.73 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 23 LSRAVSIPSVSADvtlRPKVVEmadfvvseftKLGAKMEKrdIGYhqmdgQDVPLPPI--VLGQYGNdpSKKTVLIYNHF 100
Cdd:cd05649 4 LRDLIQIPSESGE---EKGVVE----------RIEEEMEK--LGF-----DEVEIDPMgnVIGYIGG--GKKKILFDGHI 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 429239506 101 DVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELG-IDFPVNLLM-------CFEGM 166
Cdd:cd05649 62 DTVGIGNIDNWKFDPYEGYETD-GKIYGRGTSDQKGGLASMVYAAKIMKDLGlRDFAYTILVagtvqeeDCDGV 134
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
90-464 |
1.41e-07 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 53.35 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 90 SKKTVLIYNHFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGW-ISAIEAHKElgiDFPVN---LLMCFEG 165
Cdd:PRK08588 58 GSPVLALSGHMDVVAAGDVDKWTYDPFELTEKD-GKLYGRGATDMKSGLAALvIAMIELKEQ---GQLLNgtiRLLATAG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 166 mEEYGSEG------------LEDLIRAEAEKYFakadcvcisdtywlgtkkpvLTYGLRGVCYFNITVEGPSAdlHSGV- 232
Cdd:PRK08588 134 -EEVGELGakqltekgyaddLDALIIGEPSGHG--------------------IVYAHKGSMDYKVTSTGKAA--HSSMp 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 233 -FGGTVHEPMTDLVAIMSTLVKPngeilIPGIMDQVAELTPTEDSIydgidytmedlkeavgadisiypdpkrtlqhrwr 311
Cdd:PRK08588 191 eLGVNAIDPLLEFYNEQKEYFDS-----IKKHNPYLGGLTHVVTII---------------------------------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 312 yptlslhgiegafsgSGAKTV--IPAKVIGKFSIRTVPNMESETVERLVKEHVTKVfNSlNSKNKLAFNNMHSGSWWISS 389
Cdd:PRK08588 232 ---------------NGGEQVnsVPDEAELEFNIRTIPEYDNDQVISLLQEIINEV-NQ-NGAAQLSLDIYSNHRPVASD 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 429239506 390 PDHWHYDVGKKATERVYGITPDFVreggSIPVTVTFEQSLKK--NVLLLPMGRGD-DGAHSINEKLDLDNFLKGIKLF 464
Cdd:PRK08588 295 KDSKLVQLAKDVAKSYVGQDIPLS----AIPGATDASSFLKKkpDFPVIIFGPGNnLTAHQVDEYVEKDMYLKFIDIY 368
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
99-156 |
1.77e-07 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 53.17 E-value: 1.77e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 429239506 99 HFDVQPASLEDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFP 156
Cdd:PRK13009 66 HTDVVPPGDLEAWTSPPFEPTIRD-GMLYGRGAADMKGSLAAFVVAAERFVAAHPDHK 122
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
8-153 |
2.51e-07 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 53.05 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 8 LYEVIdKKKDEFVTRLSRAVSIPSVSAD-VTL--RPKVVEMADFVVSEFTKLGAKMekRDIGYHQMDgqdvplppIVLGQ 84
Cdd:PRK06156 38 LYARL-KYGAAAIESLRELVAFPTVRVEgVPQheNPEFIGFKKLLKSLARDFGLDY--RNVDNRVLE--------IGLGG 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429239506 85 YGndpsKKTVLIYNHFDVQPASLE----DGWSTDPFTLTVDNKgRMFGRGATDDKGPLIGWISAIEAHKELGI 153
Cdd:PRK06156 107 SG----SDKVGILTHADVVPANPElwvlDGTRLDPFKVTLVGD-RLYGRGTEDDKGAIVTALYAMKAIKDSGL 174
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
6-184 |
6.72e-07 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 51.56 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 6 DKLYEVIDKKKDEFVTRLSRAVSIPSVSADVtlrPKVVEMADFVVSEFTKLGAKMEKrdigyhqmdgqdVPLPP----IV 81
Cdd:PRK06133 26 AELLAAAQQEQPAYLDTLKELVSIESGSGDA---EGLKQVAALLAERLKALGAKVER------------APTPPsagdMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 82 LGQYGNDPSKKTVLIYnHFDV--QPASLedgwSTDPFTLtvdNKGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNL 159
Cdd:PRK06133 91 VATFKGTGKRRIMLIA-HMDTvyLPGML----AKQPFRI---DGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTL 162
|
170 180
....*....|....*....|....*
gi 429239506 160 LMCFEGMEEYGSEGLEDLIRAEAEK 184
Cdd:PRK06133 163 TVLFNPDEETGSPGSRELIAELAAQ 187
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
18-177 |
8.34e-07 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 50.77 E-value: 8.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 18 EFVTRLSRAVSIPSVSADVTlrpkvvEMADFVVSEFTKLGAKMEKRdigyhqmdGQDVplpPIVLGQYgnDPSKKTVLIY 97
Cdd:cd05651 1 EAIELLKSLIATPSFSREEH------KTADLIENYLEQKGIPFKRK--------GNNV---WAENGHF--DEGKPTLLLN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 98 NHFD-VQPASledGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGiDFPVNLLMCFEGMEEY-GSEGLE 175
Cdd:cd05651 62 SHHDtVKPNA---GWTKDPFEPVEKG-GKLYGLGSNDAGASVVSLLATFLHLYSEG-PLNYNLIYAASAEEEIsGKNGIE 136
|
..
gi 429239506 176 DL 177
Cdd:cd05651 137 SL 138
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
23-230 |
9.57e-07 |
|
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: 50.81 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 23 LSRAVSIPSVSADVTlrpkvvEMADFVVSEFTKLGAKMEKRDIGYhqmdgqdvplppiVLGQYGNDPskKTVLIYNHFDV 102
Cdd:cd05653 7 LLDLLSIYSPSGEEA------RAAKFLEEIMKELGLEAWVDEAGN-------------AVGGAGSGP--PDVLLLGHIDT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 103 QPASLEdgwstdpftLTVDNkGRMFGRGATDDKGPLIGWI-SAIEAHKELGIDFPVNLLMcfegMEEYGSEGLEDLIRAe 181
Cdd:cd05653 66 VPGEIP---------VRVEG-GVLYGRGAVDAKGPLAAMIlAASALNEELGARVVVAGLV----DEEGSSKGARELVRR- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 429239506 182 aekyFAKADCVCISD-TYWLGtkkpvLTYGLRGVCYFNITVEGPSAdlHS 230
Cdd:cd05653 131 ----GPRPDYIIIGEpSGWDG-----ITLGYRGSLLVKIRCEGRSG--HS 169
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
80-172 |
2.55e-06 |
|
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: 49.48 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 80 IVLGQYGNDPskKTVLIYNHFDVQPASleDGWSTDPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNL 159
Cdd:cd02697 64 IVRRRYGDGG--RTVALNAHGDVVPPG--DGWTRDPYGAVVED-GVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAV 138
|
90
....*....|...
gi 429239506 160 LMCFEGMEEYGSE 172
Cdd:cd02697 139 ELHFTYDEEFGGE 151
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
86-136 |
9.29e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 44.84 E-value: 9.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 429239506 86 GNDPSKKTVLIYNHFDVQPASLEDgWSTDPFTLTVDNkGRMFGRGATDDKG 136
Cdd:PRK07906 60 GADPSRPALLVHGHLDVVPAEAAD-WSVHPFSGEIRD-GYVWGRGAVDMKD 108
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
27-231 |
1.43e-04 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 43.80 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 27 VSIPSVSADVtlrpkvVEMADFVVSEFTKLGAKMEKrdigyhqmdgQDVPLPPI--VLGQYGNDPSKKtVLIYNHFDVQP 104
Cdd:cd05652 9 VEIPSISGNE------AAVGDFLAEYLESLGFTVEK----------QPVENKDRfnVYAYPGSSRQPR-VLLTSHIDTVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 105 ASLedgwstdPFTLTVDNkGRMFGRGATDDKGPLIGWISAIEAHKELGIDFPVNLLMCFEGMEEYGSEGLedliraeaeK 184
Cdd:cd05652 72 PFI-------PYSISDGG-DTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGDGM---------K 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 429239506 185 YFAKadcvcisdtywLGTKKP-----------VLTYGLRGVCYFNITVEGPSAdlHSG 231
Cdd:cd05652 135 AFND-----------LGLNTWdavifgeptelKLASGHKGMLGFKLTAKGKAG--HSG 179
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
16-144 |
1.66e-04 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 43.79 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429239506 16 KDEFVTRLSRAVSIPSVSADVTlrpkvvEMADFVVSEFTKLGAKMEKRDIGYhqmdgqdvplppiVLGQYGNDPskKTVL 95
Cdd:PRK04443 5 ALEARELLKGLVEIPSPSGEEA------AAAEFLVEFMESHGREAWVDEAGN-------------ARGPAGDGP--PLVL 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 429239506 96 IYNHFD----VQPASLEDGwstdpftltvdnkgRMFGRGATDDKGPLIGWISA 144
Cdd:PRK04443 64 LLGHIDtvpgDIPVRVEDG--------------VLWGRGSVDAKGPLAAFAAA 102
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
300-366 |
1.78e-04 |
|
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: 40.79 E-value: 1.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429239506 300 PDPKRTLQHRWRYPTLSLHGIEGAFsgsgAKTVIPAKVIGKFSIRTVPNMESETVERLVKEHVTKVF 366
Cdd:pfam07687 41 PAEYGDIGFDFPRTTLNITGIEGGT----ATNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEKEL 103
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
99-171 |
1.16e-03 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 40.95 E-value: 1.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429239506 99 HFDVQPASleDGWSTDPFTLTVDNKgRMFGRGATDDKGPLIGWISAIEAHkelgiDFPVNLLmcFEGMEEYGS 171
Cdd:PRK08737 71 HLDTVPDS--PHWSADPHVMRRTDD-RVIGLGVCDIKGAAAALLAAANAG-----DGDAAFL--FSSDEEAND 133
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
57-133 |
7.02e-03 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 38.59 E-value: 7.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 429239506 57 GAKMEKRDIGYHQMDGQdvplppIVLGQYGNDPSKKTVLIYNHFDVQPASLEDgWSTDPFTLTVDNKgRMFGRGATD 133
Cdd:cd08012 50 GGPLVIDHVSYVKGRGN------IIVEYPGTVDGKTVSFVGSHMDVVTANPET-WEFDPFSLSIDGD-KLYGRGTTD 118
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
108-151 |
9.82e-03 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 38.27 E-value: 9.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 429239506 108 EDGWSTDPFTLTVDNkGRMFGRGATDDKG--PLIgwisaIEAHKEL 151
Cdd:PRK05111 87 EGRWTRDPFTLTEHD-GKLYGLGTADMKGffAFI-----LEALRDI 126
|
|
| |
