|
Name |
Accession |
Description |
Interval |
E-value |
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
38-506 |
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: 844.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 38 VFQYIDLHQDEFVQTLKEWVAIESDSVQPvpRFRQELFRMMAVAADTLQRLGARVASVDMGPQQLPDGQSLPIPPVILAE 117
Cdd:cd05676 1 VFKYIDEHQDEFIERLREAVAIQSVSADP--EKRPELIRMMEWAAERLEKLGFKVELVDIGTQTLPDGEELPLPPVLLGR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 118 LGSDPTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEG 197
Cdd:cd05676 79 LGSDPSKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 198 MEEAGSVALEELVEKEKDRFFSGVDYIVISDNLWISQRKPAITYGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADLV 277
Cdd:cd05676 159 MEESGSEGLDELIEARKDTFFSDVDYVCISDNYWLGKKKPCLTYGLRGICYFFIEVEGPNKDLHSGVFGGSVHEPMTDLI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 278 ALLGSLVDSSGHILVPGIYDEVVPLTEEEINTYKAIHLDLEEYRNSSRVEKFLFDTKEEILMHLWRYPSLSIHGIEGAFD 357
Cdd:cd05676 239 ALMSSLVDSDGKILIPGIYDAVAPLTEEEWELYEKIDFDMEEYREDIGVRRLLYDNKEELLMHRWRYPSLSIHGIEGAFS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 358 EPGTKTVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKRNSSNKMVVSMTLGLHPWIANIDDTQYLAAKRAIRTV 437
Cdd:cd05676 319 GPGAKTVIPAKVIGKFSIRLVPNMDPEVVEKQVTDYLEKVFAELKSPNKLKVYMGHGGKPWVADPDHPNYKAARKATKRV 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21071039 438 FGTEPDMIRDGSTIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQNEKINRWNYIEGTKLFAAFFLEMAQL 506
Cdd:cd05676 399 FGVEPDLTREGGSIPITLTFQEATGKNVMLLPIGAADDGAHSQNEKINRRNYIEGTKLLAAYFHELSKL 467
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
50-502 |
0e+00 |
|
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: 578.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 50 VQTLKEWVAIESDSVQPVprFRQELFRMMAVAADTLQRLGARVASVDMGPqqlpdgqslpIPPVILAELGSDPTKGTVCF 129
Cdd:cd03893 1 LQTLAELVAIPSVSAQPD--RREELRRAAEWLADLLRRLGFTVEIVDTSN----------GAPVVFAEFPGAPGAPTVLL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 130 YGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEGMEEAGSVALEEL 209
Cdd:cd03893 69 YGHYDVQPAGDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEESGSPSLDQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 210 VEKEKDrfFSGVDYIVISDNLWISQRKPAITYGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADLVALLGSLVDSSGH 289
Cdd:cd03893 149 VEAHRD--LLAADAIVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLDHDLHSGLYGGVVPDPMTALAQLLASLRDETGR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 290 ILVPGIYDEVVPLTEEEINTYKAIhldLEEYRNSSRvekflfdTKEEILMHLWRYPSLSIHGIEGAFDEPGTKTVIPGRV 369
Cdd:cd03893 227 ILVPGLYDAVRELPEEEFRLDAGV---LEEVEIIGG-------TTGSVAERLWTRPALTVLGIDGGFPGEGSKTVIPPRA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 370 IGKFSIRLVPHMNVSAVEKQVTRHLEDVFSkrnSSNKMVVSMTLGLHPWIANIDDTQYLAAKRAIRTVFGTEPDMIRDGS 449
Cdd:cd03893 297 RAKISIRLVPGQDPEEASRLLEAHLEKHAP---SGAKVTVSYVEGGMPWRSDPSDPAYQAAKDALRTAYGVEPPLTREGG 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 21071039 450 TIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQNEKINRWNYIEGTKLFAAFFLE 502
Cdd:cd03893 374 SIPFISVLQEFPQAPVLLIGVGDPDDNAHSPNESLRLGNYKEGTQAEAALLYS 426
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
50-503 |
2.98e-110 |
|
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: 334.28 E-value: 2.98e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 50 VQTLKEWVAIESDSVQPVprFRQELFRMMAVAADTLQRLGARVASVdmgpqqLPDGQSlpipPVILAELGSDPTKGTVCF 129
Cdd:cd05680 1 LEELFELLRIPSVSADPA--HKGDVRRAAEWLADKLTEAGFEHTEV------LPTGGH----PLVYAEWLGAPGAPTVLV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 130 YGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEGMEEAGSVALEEL 209
Cdd:cd05680 69 YGHYDVQPPDPLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIGSPSLPAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 210 VEKEKDRFfsGVDYIVISDNLWISQRKPAITYGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADLVALLGSLVDSSGH 289
Cdd:cd05680 149 LEENAERL--AADVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNRDLHSGSYGGAVPNPANALARLLASLHDEDGR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 290 ILVPGIYDEVVPLTEEEINTYKAIHLDLEEYRNSSRVEKFL----FDTKEEilmhLWRYPSLSIHGIEGAFDEPGTKTVI 365
Cdd:cd05680 227 VAIPGFYDDVRPLTDAEREAWAALPFDEAAFKASLGVPALGgeagYTTLER----LWARPTLDVNGIWGGYQGEGSKTVI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 366 PGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKrnsSNKMVVSMTLGLHPWIANIDDTQYLAAKRAIRTVFGTEPDMI 445
Cdd:cd05680 303 PSKAHAKISMRLVPGQDPDAIADLLEAHLRAHAPP---GVTLSVKPLHGGRPYLVPTDHPALQAAERALEEAFGKPPVFV 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 21071039 446 RDGSTIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQNEKINRWNYIEGTKLFAAFFLEM 503
Cdd:cd05680 380 REGGSIPIVALFEKVLGIPTVLMGFGLPDDAIHAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
50-500 |
2.44e-104 |
|
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: 318.90 E-value: 2.44e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 50 VQTLKEWVAIESDSVQPVPRFRQELFRMMAVAADTLQRLGARvaSVDMGPqqLPDGQSlpipPVILAEL---GSDPTKGT 126
Cdd:cd05677 2 LNTLSEFIAFQTVSQSPTTENAEDSRRCAIFLRQLFKKLGAT--NCLLLP--SGPGTN----PIVLATFsgnSSDAKRKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 127 VCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVS-AFRalEQDLPVNIKFIIEGMEEAGSVA 205
Cdd:cd05677 74 ILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAeLFQ--EGELDNDVVFLIEGEEESGSPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 206 LEELVEKEKDRFFSgVDYIVISDNLWISQRKPAITYGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADLVALLGSLVD 285
Cdd:cd05677 152 FKEVLRKNKELIGD-IDWILLSNSYWLDDNIPCLNYGLRGVIHATIVVSSDKPDLHSGVDGGVLREPTADLIKLLSKLQD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 286 SSGHILVPGIYDEVVPLTEEEINTYKAIhldleeyrnSSRVEKFLFDTKEEiLMHLWRYPSLSIHGIEgaFDEPGTKTVI 365
Cdd:cd05677 231 PDGRILIPHFYDPVKPLTEAERARFTAI---------AETALIHEDTTVDS-LIAKWRKPSLTVHTVK--VSGPGNTTVI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 366 PGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKRNSSNKMVVSMTLGLHPWIANIDDTQYLAAKRAIRTVFGTEPDMI 445
Cdd:cd05677 299 PKSASASVSIRLVPDQDLDVIKQDLTDYIQSCFAELKSQNHLDIEVLNEAEPWLGDPDNPAYQILREAVTAAWGVEPLYI 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 21071039 446 RDGSTIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQNEKINRWNYIEGTKLFAAFF 500
Cdd:cd05677 379 REGGSIPTIRFLEKEFNAPAVQLPCGQSSDNAHLDNERLRIKNLYKMREILSRVF 433
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
34-506 |
2.12e-87 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 275.86 E-value: 2.12e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 34 LLEKVFQYIDLHQDEFVQTLKEWVAIESdsVQPVPRFRQELFRMMAVAADTLQRLG-ARVASVDMGPQqlpdgqslpipP 112
Cdd:PRK08201 1 MMQQVEAYLRERREAHLEELKEFLRIPS--ISALSEHKEDVRKAAEWLAGALEKAGlEHVEIMETAGH-----------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 113 VILAELGSDPTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIK 192
Cdd:PRK08201 68 IVYADWLHAPGKPTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 193 FIIEGMEEAGSVALEELVEKEKDRFFSgvDYIVISDNLWISQRKPAITYGTRGNSYFMVEVKCRDQDFHSGTFGGILHEP 272
Cdd:PRK08201 148 FCIEGEEEIGSPNLDSFVEEEKDKLAA--DVVLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLHSGLYGGAVPNA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 273 MADLVALLGSLVDSSGHILVPGIYDEVVPLTEEEINTYKAIHLDLEEYRNSSRVEKFLFDTKEEILMHLWRYPSLSIHGI 352
Cdd:PRK08201 226 LHALVQLLASLHDEHGTVAVEGFYDGVRPLTPEEREEFAALGFDEEKLKRELGVDELFGEEGYTALERTWARPTLELNGV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 353 EGAFDEPGTKTVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEdvfSKRNSSNKMVVSMTLGLHPWIANIDDTQYLAAKR 432
Cdd:PRK08201 306 YGGFQGEGTKTVIPAEAHAKITCRLVPDQDPQEILDLIEAHLQ---AHTPAGVRVTIRRFDKGPAFVAPIDHPAIQAAAR 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21071039 433 AIRTVFGTEPDMIRDGSTIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQNEKINRWNYIEGTKLFAAFFLEMAQL 506
Cdd:PRK08201 383 AYEAVYGTEAAFTRMGGSIPVVETFSSQLHIPIVLMGFGLPSENFHAPNEHFHLENFDKGLRTLVEYWHQLAEG 456
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
49-499 |
8.40e-86 |
|
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: 271.14 E-value: 8.40e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 49 FVQTLKEWVAIESDSVQpvprfrQELFRMMAVA-ADTLQRLGARVasvdmgpQQLPDgqslPIPPVILAELGSDPTKgTV 127
Cdd:cd05681 1 YLEDLRDLLKIPSVSAQ------GRGIPETADFlKEFLRRLGAEV-------EIFET----DGNPIVYAEFNSGDAK-TL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 128 CFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEGMEEAGSVALE 207
Cdd:cd05681 63 LFYNHYDVQPAEPLELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPNLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 208 ELVEKEKDRFFSgvDYIvisdnLWIS-----QRKPAITYGTRGNSYFMVEVKCRDQDFHSgTFGGILHEPMADLVALLGS 282
Cdd:cd05681 143 KFVAEHADLLKA--DGC-----IWEGggknpKGRPQISLGVKGIVYVELRVKTADFDLHS-SYGAIVENPAWRLVQALNS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 283 LVDSSGHILVPGIYDEVVPLTEEEINTYKAIHLDLEEYRNSSRVEKFLFDTKEEILMHLWRYPSLSIHGIEGAFDEPGTK 362
Cdd:cd05681 215 LRDEDGRVLIPGFYDDVRPLSEAERALIDTYDFDPEELRKTYGLKRPLQVEGKDPLRALFTEPTCNINGIYSGYTGEGSK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 363 TVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEdvfskRNSSNKMVVSMTLGLHPWIANIDDTQYLAAKRAIRTVFGTEP 442
Cdd:cd05681 295 TILPSEAFAKLDFRLVPDQDPAKILSLLRKHLD-----KNGFDDIEIHDLLGEKPFRTDPDAPFVQAVIESAKEVYGQDP 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 21071039 443 DMIRDGSTIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQNEKINRWNYIEGTKLFAAF 499
Cdd:cd05681 370 IVLPNSAGTGPMYPFYDALEVPVVAIGVGNAGSNAHAPNENIRIADYYKGIEHTEEL 426
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
36-505 |
1.26e-67 |
|
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: 222.45 E-value: 1.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 36 EKVFQYIDLHQDEFVQTLKEWVAIESDSvqpvprfRQELfRMMAVAADTLQRLGARVASVDMGPQQlpdgqslpipPVIL 115
Cdd:COG0624 1 AAVLAAIDAHLDEALELLRELVRIPSVS-------GEEA-AAAELLAELLEALGFEVERLEVPPGR----------PNLV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 116 AELGSDPTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFII 195
Cdd:COG0624 63 ARRPGDGGGPTLLLYGHLDVVPPGDLELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 196 EGMEEAGSVALEELVEKEKDRFfsGVDYIVISDnlwiSQRKPAITYGTRGNSYFMVEVKCRDQdfHSGTFGgilhepmad 275
Cdd:COG0624 143 TGDEEVGSPGARALVEELAEGL--KADAAIVGE----PTGVPTIVTGHKGSLRFELTVRGKAA--HSSRPE--------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 276 lvallgsLVDSSGHILVPGIydevvplteeeintykaihLDLEEYRNSSRVEKFLfdtkeeilmhlwRYPSLSIHGIEGa 355
Cdd:COG0624 206 -------LGVNAIEALARAL-------------------AALRDLEFDGRADPLF------------GRTTLNVTGIEG- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 356 fdepGTKT-VIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKRNSSnkmVVSMTLGLHPWIANIDDTQYLAAKRAI 434
Cdd:COG0624 247 ----GTAVnVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVEVE---VEVLGDGRPPFETPPDSPLVAAARAAI 319
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21071039 435 RTVFGTEPDMIRDGSTIPiAKMFQEIVHKSVVLipLGAVD-DGEHSQNEKINRWNYIEGTKLFAAFFLEMAQ 505
Cdd:COG0624 320 REVTGKEPVLSGVGGGTD-ARFFAEALGIPTVV--FGPGDgAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
32-483 |
1.73e-64 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 216.31 E-value: 1.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 32 PALLEKVFQYIDLHQDEFVQTLKEWVAIESDSVQPvpRFRQELFRMMAVAADTLQRLGARvASVdmgpqqlpdgQSLPIP 111
Cdd:PRK09104 2 MADLDPVLDHIDANLDASLERLFALLRIPSISTDP--AYAADCRKAADWLVADLASLGFE-ASV----------RDTPGH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 112 PVILAEL-GSDPTKGTVCFYGHLDVQPADRGDGWLTDPY--VLTEV-DGK--LYGRGATDNKGPVLAWINAVSAFRALEQ 185
Cdd:PRK09104 69 PMVVAHHeGPTGDAPHVLFYGHYDVQPVDPLDLWESPPFepRIKETpDGRkvIVARGASDDKGQLMTFVEACRAWKAVTG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 186 DLPVNIKFIIEGMEEAGSVALEELVEKEKDRFfsGVDYIVISD-NLWISQRkPAITYGTRGNSYFMVEVKCRDQDFHSGT 264
Cdd:PRK09104 149 SLPVRVTILFEGEEESGSPSLVPFLEANAEEL--KADVALVCDtGMWDRET-PAITTSLRGLVGEEVTITAADRDLHSGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 265 FGGILHEPMADLVALLGSLVDSSGHILVPGIYDEVVPLTEEEINTYKAIHLDleeyrnssrVEKFLFD---------TKE 335
Cdd:PRK09104 226 FGGAAANPIRVLTRILAGLHDETGRVTLPGFYDGVEELPPEILAQWKALGFT---------AEAFLGPvglsipageKGR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 336 EILMHLWRYPSLSIHGIEGAFDEPGTKTVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDvfskRNSSNKMVVSMTLGL 415
Cdd:PRK09104 297 SVLEQIWSRPTCEINGIWGGYTGEGFKTVIPAEASAKVSFRLVGGQDPAKIREAFRAYVRA----RLPADCSVEFHDHGG 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21071039 416 HPWIA-NIDDTQYLAAKRAIRTVFGTEPDMIRDGSTIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQNEK 483
Cdd:PRK09104 373 SPAIAlPYDSPALAAAKAALSDEWGKPAVLIGSGGSIPIVGDFKRILGMDSLLVGFGLDDDRIHSPNEK 441
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
112-506 |
3.00e-60 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 204.60 E-value: 3.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 112 PVILAELGSDPTKgTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVsaFRALEQD-LPVN 190
Cdd:PRK06446 51 PVVYGEINVGAKK-TLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAI--KHLIDKHkLNVN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 191 IKFIIEGMEEAGSVALEELVEKEKDRFFSgvDYIVISDNLWISQRKPAITYGTRGNSYFMVEVKCRDQDFHSgTFGGILH 270
Cdd:PRK06446 128 VKFLYEGEEEIGSPNLEDFIEKNKNKLKA--DSVIMEGAGLDPKGRPQIVLGVKGLLYVELVLRTGTKDLHS-SNAPIVR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 271 EPMADLVALLGSLVDSSGHILVPGIYDEVVPLTEEEINTYKAIHLDLEEYRNSSRVEKFLFDTKEEILMHLWRYPSLSIH 350
Cdd:PRK06446 205 NPAWDLVKLLSTLVDGEGRVLIPGFYDDVRELTEEERELLKKYDIDVEELRKALGFKELKYSDREKIAEALLTEPTCNID 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 351 GIEGAFDEPGTKTVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKrnssnkmVVSMTLGL-HPWIANIDDTQYLA 429
Cdd:PRK06446 285 GFYSGYTGKGSKTIVPSRAFAKLDFRLVPNQDPYKIFELLKKHLQKVGFN-------GEIIVHGFeYPVRTSVNSKVVKA 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21071039 430 AKRAIRTVFGTEPDMIRDGSTIPIAKMFQEI--VHKSVVLIPLGAVDDGEHSQNEKINRWNYIEGTKLFAAFFLEMAQL 506
Cdd:PRK06446 358 MIESAKRVYGTEPVVIPNSAGTQPMGLFVYKlgIRDIVSAIGVGGYYSNAHAPNENIRIDDYYKAIKHTEEFLKLYSTL 436
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
50-482 |
5.65e-58 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 198.59 E-value: 5.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 50 VQTLKEWVAIESdsVQPVPRFRQELFRMMAVAADTLQRLGAR-VASVDmgpqqlPDGQslpipPVILAELGSDPTKGTVC 128
Cdd:PRK07907 21 RADLEELVRIPS--VAADPFRREEVARSAEWVADLLREAGFDdVRVVS------ADGA-----PAVIGTRPAPPGAPTVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 129 FYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAwinAVSAFRALEQDLPVNIKFIIEGMEEAGSVALEE 208
Cdd:PRK07907 88 LYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAM---HLAALRALGGDLPVGVTVFVEGEEEMGSPSLER 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 209 LVEKEKDRFFSgvDYIVISDNLWISQRKPAITYGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADLVALLGSLVDSSG 288
Cdd:PRK07907 165 LLAEHPDLLAA--DVIVIADSGNWSVGVPALTTSLRGNADVVVTVRTLEHAVHSGQFGGAAPDALTALVRLLATLHDEDG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 289 HILVPGiydevvpLTEEEinTYKAIHLDLEEYRNSSRVekflFDTKEEI-----LMHLWRYPSLSIHGIegafDEPGTKT 363
Cdd:PRK07907 243 NVAVDG-------LDATE--PWLGVDYDEERFRADAGV----LDGVELIgtgsvADRLWAKPAITVIGI----DAPPVAG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 364 ---VIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEdvfskRNSSNKMVVSMTLGLH--PWIANIDDTQYLAAKRAIRTVF 438
Cdd:PRK07907 306 asnALPPSARARLSLRVAPGQDAAEAQDALVAHLE-----AHAPWGAHVTVERGDAgqPFAADASGPAYDAARAAMREAW 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 21071039 439 GTEPDMIRDGSTIPIAKMFQEIVHKSVVLipLGAVDDGE---HSQNE 482
Cdd:PRK07907 381 GKDPVDMGMGGSIPFIAELQEAFPQAEIL--VTGVEDPKtraHSPNE 425
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
112-498 |
9.79e-53 |
|
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: 185.38 E-value: 9.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 112 PVILAELGSDPTKGTVCFYGHLDVQPADRGDGWLTDPY--VLTEVDGK--------------------LYGRGATDNKGP 169
Cdd:cd05678 48 PLLLAEKPISDARKTVLFYMHLDGQPVDPSKWDQKSPYtpVLKRKDAAgnweeinwdaifsnldpewrVFARAAADDKGP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 170 VLAWINAVSAFRALEQDLPVNIKFIIEGMEEAGSVALEELVEKEKDRFFSgvDYIVISDNLWISQRKPAITYGTRGNSYF 249
Cdd:cd05678 128 IMMMLAALDALKAGGIAPKFNVKIILDSEEEKGSPSLPKAVKEYKELLAA--DALIIMDGPAHATNKPTLTFGCRGIATA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 250 MVEVKCRDQDFHSGTFGGILHEPMADLVALLGSLVDSSGHILVPGIYDEvVPLTEEEINTYKAIHLDLEEYRNS---SRV 326
Cdd:cd05678 206 TLTTYGAKVPQHSGHYGNYAPNPAFRLSSLLASMKDDTGKVTIPGFYDG-ISIDEETQKILAAVPDDEESINKRlgiAQT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 327 EKFLFDTKEEIlmhlwRYPSLSIHGIEGAFDEPGTKTVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLED----VFSK-- 400
Cdd:cd05678 285 DKVGRNYQEAL-----QYPSLNVRGMESGWKGDKVRTIIPEIAEAEIDIRLVPESDGPYLLDLVKAHIEKqgyfVTDRap 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 401 ----RNSSNKMV-VSMTLGLHPWIANIDDTQYLAAKRAIRTVFGTEPDMIRD-GSTIPIAKMFQEIvHKSVVLIPLGAVD 474
Cdd:cd05678 360 tdeeRLAHDKIAkFTYRNGADAFRTDINSPIGNWLRKALTDEFGEEPIQIRMmGGTVPIAPFVNVL-DIPAIIVPMVNMD 438
|
410 420
....*....|....*....|....
gi 21071039 475 DGEHSQNEKINRWNYIEGTKLFAA 498
Cdd:cd05678 439 NNQHSPNENLRIGNIRTGIRTCYA 462
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
128-502 |
1.27e-40 |
|
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: 148.65 E-value: 1.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 128 CFYGHLDVQPADRGDGWltdPYVLTEvDGKLYGRGATDNKGPVLAWINAVSAFRAlEQDLPVNIKFIIEGMEEAGSVALE 207
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKE-EGLKKGTVKLLFQPDEEGGMGGAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 208 ELVEKEKDRFFsGVDYIVISDN----LWISQRKPAITYGTRGNSYFMVEVKCRdqDFHSGTFgGILHEPMADLVALLGSL 283
Cdd:pfam01546 76 ALIEDGLLERE-KVDAVFGLHIgeptLLEGGIAIGVVTGHRGSLRFRVTVKGK--GGHASTP-HLGVNAIVAAARLILAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 284 VDSSGHILVPGIYDeVVPLTeeeintykaihldleeyrnssrvekflfdtkeeilmhlwrypslSIHGIEGAFdepgtkT 363
Cdd:pfam01546 152 QDIVSRNVDPLDPA-VVTVG--------------------------------------------NITGIPGGV------N 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 364 VIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKRNSSNKmvVSMTLGLHPWIANiDDTQYLAAKRAIRTVFGTEPD 443
Cdd:pfam01546 181 VIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVE--VEYVEGGAPPLVN-DSPLVAALREAAKELFGLKVE 257
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 444 MIRDGSTI-PIAKMFQEIVHKSVVLipLGAVDDGEHSQNEKINRWNYIEGTKLFAAFFLE 502
Cdd:pfam01546 258 LIVSGSMGgTDAAFFLLGVPPTVVF--FGPGSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
114-242 |
3.33e-34 |
|
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: 127.55 E-value: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 114 ILAELGSDPTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKF 193
Cdd:cd18669 2 VIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 21071039 194 IIEGMEEAGSVALEELVEKEKDRFFSGVDYIVISDNLWISQRKPAITYG 242
Cdd:cd18669 82 AFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTP 130
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
114-241 |
4.03e-34 |
|
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: 127.54 E-value: 4.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 114 ILAELGSDPTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKF 193
Cdd:cd03873 2 LIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 21071039 194 IIEGMEEAGSVALEELVEKEKDRFFSGVDYIVISDNLW--ISQRKPAITY 241
Cdd:cd03873 82 AFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDATAgpILQKGVVIRN 131
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
33-294 |
4.86e-33 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 131.19 E-value: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 33 ALLEKVFQYIDlhQDEFVQTLKEWVAI--ESDSVQPVPRFRQELFRMMAVAadtLQRLGARVASVDmgpqqLPDGQSlpi 110
Cdd:PRK07079 5 AAIARAAAYFD--SGAFFADLARRVAYrtESQNPDRAPALRAYLTDEIAPA---LAALGFTCRIVD-----NPVAGG--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 111 PPVILAELGSDPTKGTVCFYGHLDVQPADRG---DGwlTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSA-FRALEQD 186
Cdd:PRK07079 72 GPFLIAERIEDDALPTVLIYGHGDVVRGYDEqwrEG--LSPWTLTEEGDRWYGRGTADNKGQHTINLAALEQvLAARGGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 187 LPVNIKFIIEGMEEAGSVALEELVEKEKDRFFSgvDYIVISDNLWISQRKPAITYGTRGNSYFMVEVKCRDQDFHSGTFG 266
Cdd:PRK07079 150 LGFNVKLLIEMGEEIGSPGLAEVCRQHREALAA--DVLIASDGPRLSAERPTLFLGSRGAVNFRLRVNLRDGAHHSGNWG 227
|
250 260
....*....|....*....|....*...
gi 21071039 267 GILHEPMADLVALLGSLVDSSGHILVPG 294
Cdd:PRK07079 228 GLLRNPGTVLAHAIASLVDARGRIQVPG 255
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
46-301 |
3.86e-29 |
|
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: 119.53 E-value: 3.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 46 QDEFVQTLKEWVAIESDSVQP--VPRFRQELFRMMAVAadtLQRLGARVASVDMgpqqlpdgqslPIP---PVILAELGS 120
Cdd:cd05679 3 SGAFLAELARRVAVPTESQEParKPELRAYLDQEMRPR---FERLGFTVHIHDN-----------PVAgraPFLIAERIE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 121 DPTKGTVCFYGHLDVQPADRG---DGwlTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQ-DLPVNIKFIIE 196
Cdd:cd05679 69 DPSLPTLLIYGHGDVVPGYEGrwrDG--RDPWTVTVWGERWYGRGTADNKGQHSINMAALRQVLEARGgKLGFNVKFLIE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 197 GMEEAGSVALEELVEKEKDRFFSgvDYIVISDNLWISQRKPAITYGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADL 276
Cdd:cd05679 147 MGEEMGSPGLRAFCFSHREALKA--DLFIASDGPRLAADRPTMFLGSRGGLNFELRVNLREGGHHSGNWGGLLANPGIIL 224
|
250 260
....*....|....*....|....*
gi 21071039 277 VALLGSLVDSSGHILVPGIYDEVVP 301
Cdd:cd05679 225 ANAIASLVDGKGRIKLPALKPAHLP 249
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
111-459 |
8.04e-29 |
|
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: 118.59 E-value: 8.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 111 PPVILAEL-GSDPTKGTVCFYGHLDVQPadRGDGWLTD--PYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRalEQDL 187
Cdd:cd05682 59 TPLLFVEIpGTEQDDDTVLLYGHMDKQP--PFTGWDEGlgPTKPVIRGDKLYGRGGADDGYAIFASLTAIKALQ--EQGI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 188 P-VNIKFIIEGMEEAGSVALEELVEKEKDRfFSGVDYIVISDN-------LWisqrkpaITYGTRGNSYFMVEVKCRDQD 259
Cdd:cd05682 135 PhPRCVVLIEACEESGSADLPFYLDKLKER-IGNVDLVVCLDSgcgnyeqLW-------LTTSLRGVLGGDLTVQVLNEG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 260 FHSGTFGGILHEPMADLVALLGSLVDS-SGHILVPGIYDEVVPLTEEEINTYKAIHLD--LEEYRNSSRVEKFLFDTKEE 336
Cdd:cd05682 207 VHSGDASGIVPSSFRILRQLLSRIEDEnTGEVKLDEQHCDIPAHRYEQAKKIAEILGEavYEEFPFVSGVQPVTTDLVQL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 337 ILMHLWRyPSLSIHGIEGAfdePGTKT---VIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEdvfskRNSSNKMVVSMTL 413
Cdd:cd05682 287 YLNRTWK-PQLSVTGADGL---PPASTagnVLRPETTLKLSLRLPPTVDAEKASAALKKLLE-----TDPPYNAKVTFKS 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 21071039 414 ----------GLHPWIANIDDTqylaakrAIRTVFGTEPDMIRDGSTIPIAKMFQE 459
Cdd:cd05682 358 dgagsgwnapLLSPWLAKALNE-------ASQLFFGKPAAYQGEGGSIPFMNMLGE 406
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
47-442 |
5.65e-24 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 103.53 E-value: 5.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 47 DEFVQTLKEwvAIESDSVQPVPRFRQElfrMMAVAADTLQRLGARVaSVDMGPQQLPDgQSLPIPPVILAELGSDPTKgt 126
Cdd:PRK08651 6 FDIVEFLKD--LIKIPTVNPPGENYEE---IAEFLRDTLEELGFST-EIIEVPNEYVK-KHDGPRPNLIARRGSGNPH-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 127 VCFYGHLDVQPAdrGDGW-LTDPYVLTEVDGKLYGRGATDNKGPVLAWInavSAFRALEQDLPVNIKFIIEGMEEAGSVA 205
Cdd:PRK08651 77 LHFNGHYDVVPP--GEGWsVNVPFEPKVKDGKVYGRGASDMKGGIAALL---AAFERLDPAGDGNIELAIVPDEETGGTG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 206 LEELVEKEKDRffsgVDYIVI-----SDNLWIsqrkpaityGTRGNSYFMVEVKCRDQdfHSGTfggilhepmadlvALL 280
Cdd:PRK08651 152 TGYLVEEGKVT----PDYVIVgepsgLDNICI---------GHRGLVWGVVKVYGKQA--HAST-------------PWL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 281 GslvdssghilvpgiydevvplteeeINTYKAIHLDLEEYRNSSRVEKflfdTKEEILMHLWRYPSLSihgIEGAFDEPG 360
Cdd:PRK08651 204 G-------------------------INAFEAAAKIAERLKSSLSTIK----SKYEYDDERGAKPTVT---LGGPTVEGG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 361 TKT-VIPGRVigKFSI--RLVPHMNVSAVEKQVTRHLEDVFSKRNSsnKMVVSMTLGLHPWIANIDDTQYLAAKRAIRTV 437
Cdd:PRK08651 252 TKTnIVPGYC--AFSIdrRLIPEETAEEVRDELEALLDEVAPELGI--EVEFEITPFSEAFVTDPDSELVKALREAIREV 327
|
....*
gi 21071039 438 FGTEP 442
Cdd:PRK08651 328 LGVEP 332
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
40-214 |
3.07e-21 |
|
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: 96.16 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 40 QYIDLHQDEFVQTLKEWVAIESDSVQPVPR--FRQELFRMMAVAADTLQRLGARVASVD--MGpqqlpdgqslpippviL 115
Cdd:cd03888 1 EEIDKYKDEILEDLKELVAIPSVRDEATEGapFGEGPRKALDKFLDLAKRLGFKTKNIDnyAG----------------Y 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 116 AELGSDptKGTVCFYGHLDVQPAdrGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRalEQDLPVN--IKF 193
Cdd:cd03888 65 AEYGEG--EEVLGILGHLDVVPA--GEGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILK--DLGLPLKkkIRL 138
|
170 180
....*....|....*....|.
gi 21071039 194 IIEGMEEAGSVALEELVEKEK 214
Cdd:cd03888 139 IFGTDEETGWKCIEHYFEHEE 159
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
50-494 |
4.59e-21 |
|
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: 94.77 E-value: 4.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 50 VQTLKEWVAIesDSVQPVprfRQELFRMMAVAADTLQRLGARVASVDmgpqqLPDGQSLPIPPVILAELGSDPTKgTVCF 129
Cdd:TIGR01910 1 VELLKDLISI--PSVNPP---GGNEETIANYIKDLLREFGFSTDVIE-----ITDDRLKVLGKVVVKEPGNGNEK-SLIF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 130 YGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEGMEEAGSVALEEL 209
Cdd:TIGR01910 70 NGHYDVVPAGDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 210 VEKekdRFFSGVDYIVIS-----DNLWISQrkpaitYGTrgnsyfmvevkcrdQDFHSGTFGGILHEPMADLVAllgSLV 284
Cdd:TIGR01910 150 LQR---GYFKDADGVLIPepsggDNIVIGH------KGS--------------IWFKLRVKGKQAHASFPQFGV---NAI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 285 DSSGHILvpgiydevvplteEEINtykaihlDLEEYRNSSRVEKFLFDTkeeilmhlwryPSLSIHGIEGAfDEPGTktv 364
Cdd:TIGR01910 204 MKLAKLI-------------TELN-------ELEEHIYARNSYGFIPGP-----------ITFNPGVIKGG-DWVNS--- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 365 IPGRVIGKFSIRLVPHMNVSavekQVTRHLEDVFSKRNSSNKMvvsmtLGLHPWIANIDDTQYL--------AAKRAIRT 436
Cdd:TIGR01910 249 VPDYCEFSIDVRIIPEENLD----EVKQIIEDVVKALSKSDGW-----LYENEPVVKWSGPNETppdsrlvkALEAIIKK 319
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 21071039 437 VFGTEPDMIRDGSTIPIAkmfqEIVHKSVVLIPLGAVDDGE-HSQNEKINRWNYIEGTK 494
Cdd:TIGR01910 320 VRGIEPEVLVSTGGTDAR----FLRKAGIPSIVYGPGDLETaHQVNEYISIKNLVESTK 374
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
114-442 |
2.27e-18 |
|
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: 86.58 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 114 ILAELGSDPTKgTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKF 193
Cdd:cd08659 45 LVATVGGGDGP-VLLLNGHIDTVPPGDGDKWSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 194 IIEGMEEAGSVALEELVEKEKDRffsGVDYIVI---SDNlwisqrkpAITYGTRGNSYFMVEVKcrdqdfhsgtfgGIlh 270
Cdd:cd08659 124 LATVDEEVGSDGARALLEAGYAD---RLDALIVgepTGL--------DVVYAHKGSLWLRVTVH------------GK-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 271 epmadlvallgslvdsSGHILVPgiydevvpltEEEINtykAIHL------DLEEYRNSSRVEKFLFdtkeeilmhlwrY 344
Cdd:cd08659 179 ----------------AAHSSMP----------ELGVN---AIYAladflaELRTLFEELPAHPLLG------------P 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 345 PSLSIHGIEGafdepGTKT-VIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKRNssnkMVVSMTlGLHPWIANID 423
Cdd:cd08659 218 PTLNVGVING-----GTQVnSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLT----VEVSLD-GDPPFFTDPD 287
|
330
....*....|....*....
gi 21071039 424 DTQYLAAKRAIRTVFGTEP 442
Cdd:cd08659 288 HPLVQALQAAARALGGDPV 306
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
131-214 |
4.01e-17 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 83.74 E-value: 4.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 131 GHLDVQPAdrGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAwinavsAFRAL----EQDLPVN--IKFIIEGMEEAGSV 204
Cdd:PRK07318 86 GHLDVVPA--GDGWDTDPYEPVIKDGKIYARGTSDDKGPTMA------AYYALkiikELGLPLSkkVRFIVGTDEESGWK 157
|
90
....*....|
gi 21071039 205 ALEELVEKEK 214
Cdd:PRK07318 158 CMDYYFEHEE 167
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
114-225 |
7.74e-16 |
|
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: 79.09 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 114 ILAELGSDPTkgTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKF 193
Cdd:cd03891 46 LWARRGTGGP--HLCFAGHTDVVPPGDLEGWSSDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISF 123
|
90 100 110
....*....|....*....|....*....|....*..
gi 21071039 194 II----EGMEEAGSVALEELVEKEKDRFfsgvDY-IV 225
Cdd:cd03891 124 LItsdeEGPAIDGTKKVLEWLKARGEKI----DYcIV 156
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
114-226 |
5.16e-15 |
|
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: 76.48 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 114 ILAELGSDPtKGTVCFYGHLDVQPADrGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKF 193
Cdd:cd03894 48 LLATLGPGG-EGGLLLSGHTDVVPVD-GQKWSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAF 125
|
90 100 110
....*....|....*....|....*....|...
gi 21071039 194 IIEgmEEAGSVALEELVEKEKDRFFSgVDYIVI 226
Cdd:cd03894 126 SYD--EEVGCLGVRHLIAALAARGGR-PDAAIV 155
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
131-214 |
5.44e-15 |
|
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: 77.03 E-value: 5.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 131 GHLDVQPAdrGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEGMEEAGSVALEELV 210
Cdd:TIGR01887 74 GHLDVVPA--GDGWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEESGWKCIDYYF 151
|
....
gi 21071039 211 EKEK 214
Cdd:TIGR01887 152 EHEE 155
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
129-254 |
1.05e-14 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 75.50 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 129 FYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRA--LEQDLPVNIKFII--EGMEEAGSV 204
Cdd:cd08011 65 FNGHYDVVPAGDGEGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADakAPWDLPVVLTFVPdeETGGRAGTK 144
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 21071039 205 ALEELVEKEkdrffsgVDYIVISDnlwiSQRKPAITYGTRGNSYFMVEVK 254
Cdd:cd08011 145 YLLEKVRIK-------PNDVLIGE----PSGSDNIRIGEKGLVWVIIEIT 183
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
126-225 |
4.19e-14 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 73.58 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 126 TVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEGMEEA---- 201
Cdd:PRK13009 60 HLCFAGHTDVVPPGDLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGpain 139
|
90 100
....*....|....*....|....*
gi 21071039 202 GSVALEELVEKEKDRFfsgvDY-IV 225
Cdd:PRK13009 140 GTVKVLEWLKARGEKI----DYcIV 160
|
|
| PRK06915 |
PRK06915 |
peptidase; |
36-202 |
4.59e-14 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 73.96 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 36 EKVFQYIDLHQDEFVQTLKEWVaiESDSVQPvprfrQElFRMMAVAADTLQRLGARVASVDMGPQQLPDG-------QSL 108
Cdd:PRK06915 6 KQICDYIESHEEEAVKLLKRLI--QEKSVSG-----DE-SGAQAIVIEKLRELGLDLDIWEPSFKKLKDHpyfvsprTSF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 109 PIPPVILAELgsdptKGT-----VCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRAL 183
Cdd:PRK06915 78 SDSPNIVATL-----KGSgggksMILNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIES 152
|
170 180
....*....|....*....|.
gi 21071039 184 EQDLPVNIKF--IIEgmEEAG 202
Cdd:PRK06915 153 GIELKGDVIFqsVIE--EESG 171
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
125-211 |
1.96e-13 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 71.76 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 125 GTVCFYGHLDVQPADrGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEgmEEAGSV 204
Cdd:PRK07522 65 GGIVLSGHTDVVPVD-GQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYD--EEVGCL 141
|
90
....*....|.
gi 21071039 205 A----LEELVE 211
Cdd:PRK07522 142 GvpsmIARLPE 152
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
35-283 |
6.32e-13 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 70.45 E-value: 6.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 35 LEKVFQYIDLHQDEFVQTLKEWVAIESDSvqPVPRFRQELFRMMAvaaDTLQRLGArvaSVDMGpqqlpdgQSLPIPPVI 114
Cdd:PRK08596 1 VSQLLEQIELRKDELLELLKTLVRFETPA--PPARNTNEAQEFIA---EFLRKLGF---SVDKW-------DVYPNDPNV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 115 LAEL-GSDPTK-GTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIk 192
Cdd:PRK08596 66 VGVKkGTESDAyKSLIINGHMDVAEVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 193 fIIEGM--EEAGSVALEELVEKEKDrffsgVDYIVISD--NLWISQRKPAITyGtrgnsyfMVEVKcRDQDFHSGT---- 264
Cdd:PRK08596 145 -IFQSVigEEVGEAGTLQCCERGYD-----ADFAVVVDtsDLHMQGQGGVIT-G-------WITVK-SPQTFHDGTrrqm 209
|
250 260
....*....|....*....|....*.
gi 21071039 265 --FGGILH-----EPMADLVALLGSL 283
Cdd:PRK08596 210 ihAGGGLFgasaiEKMMKIIQSLQEL 235
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
45-200 |
7.39e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 70.49 E-value: 7.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 45 HQDEFVQTLKEWVAIES--DSVQPVPRFRQELFRMMAVAADTLQRLGARVaSVDmgpqqlPDGQslpippVILAELGS-D 121
Cdd:PRK07205 9 VQDACVAAIKTLVSYPSvlNEGENGTPFGQAIQDVLEATLDLCQGLGFKT-YLD------PKGY------YGYAEIGQgE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 122 PTKGTVCfygHLDVQPA-DRGDgWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEGMEE 200
Cdd:PRK07205 76 ELLAILC---HLDVVPEgDLSD-WQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGTDEE 151
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
114-225 |
1.32e-12 |
|
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: 69.70 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 114 ILAEL-GSDPTKGTVCFYGHLDVQPADRgDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIK 192
Cdd:cd05675 54 LVARIgGTDPSAGPLLLLGHIDVVPADA-SDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLV 132
|
90 100 110
....*....|....*....|....*....|....
gi 21071039 193 FIIEGMEEAGS-VALEELVEKEKDrFFSGVDYIV 225
Cdd:cd05675 133 FAFVADEEAGGeNGAKWLVDNHPE-LFDGATFAL 165
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
36-256 |
1.69e-12 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 69.02 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 36 EKVFQYIDLHQDEFVQTLKEWVAIESdsVQPVPRFRQELFRMMAvaadtlQRLGARVASVDMGPQQLPDGQSLPIPPVIL 115
Cdd:PRK13013 3 DRLFAAIEARRDDLVALTQDLIRIPT--LNPPGRAYREICEFLA------ARLAPRGFEVELIRAEGAPGDSETYPRWNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 116 AELGSDPTKGT-VCFYGHLDVQPAdrGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFI 194
Cdd:PRK13013 75 VARRQGARDGDcVHFNSHHDVVEV--GHGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEIS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21071039 195 IEGMEEAGSVA----LEELVEKEKDRffsgVDYIVISDNLwisqRKPAITYGTRGNSYFMVEVKCR 256
Cdd:PRK13013 153 GTADEESGGFGgvayLAEQGRFSPDR----VQHVIIPEPL----NKDRICLGHRGVWWAEVETRGR 210
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
112-228 |
2.60e-12 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 68.34 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 112 PVILAELGSDPTKGTVCFYGHLDVQPAdrGD--GWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPV 189
Cdd:PRK13983 64 PNIVAKIPGGDGKRTLWIISHMDVVPP--GDlsLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKY 141
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 21071039 190 NIKFIIEGMEEAGS-VALEELVEKEKDRFFSGvDYIVISD 228
Cdd:PRK13983 142 NLGLAFVSDEETGSkYGIQYLLKKHPELFKKD-DLILVPD 180
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
112-213 |
3.41e-12 |
|
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: 68.10 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 112 PVILAELGSDPTKG-TVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALeqdlpvn 190
Cdd:cd03895 61 PNVVGTHRPRGETGrSLILNGHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAA------- 133
|
90 100
....*....|....*....|...
gi 21071039 191 ikfiieGMEEAGSVALEELVEKE 213
Cdd:cd03895 134 ------GLQPAADVHFQSVVEEE 150
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
114-235 |
8.80e-12 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 66.89 E-value: 8.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 114 ILAELGSDPTKgtVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALeqDLPVNIKF 193
Cdd:PRK13004 61 VLGYIGHGKKL--IAFDAHIDTVGIGDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDL--GLDDEYTL 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 21071039 194 IIEG--MEEA--GsVALEELVEKEKDRffsgVDYIVI----SDNLWISQR 235
Cdd:PRK13004 137 YVTGtvQEEDcdG-LCWRYIIEEDKIK----PDFVVIteptDLNIYRGQR 181
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
114-209 |
1.31e-11 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 66.06 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 114 ILAELGSdpTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGP----VLAWINAVsafralEQDLPV 189
Cdd:PRK08588 51 LVAEIGS--GSPVLALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGlaalVIAMIELK------EQGQLL 122
|
90 100
....*....|....*....|....*
gi 21071039 190 N--IKFII---EGMEEAGSVALEEL 209
Cdd:PRK08588 123 NgtIRLLAtagEEVGELGAKQLTEK 147
|
|
| dipeptidase |
TIGR01886 |
dipeptidase PepV; This model represents a small clade of dipeptidase enzymes which are members ... |
130-213 |
1.62e-11 |
|
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: 66.45 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 130 YGHLDVQPAdrGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEGMEEAGSVALEEL 209
Cdd:TIGR01886 84 IGHMDVVPA--GEGWTRDPFEPEIDEGRIYARGASDDKGPSLAAYYAMKILKELGLPPSKKIRFVVGTNEETGWVDMDYY 161
|
....
gi 21071039 210 VEKE 213
Cdd:TIGR01886 162 FKHE 165
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
119-215 |
2.74e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 65.41 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 119 GSDPTKGTVcFYGHLDVQPADRGDgWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRAlEQDLPV-NIKFIIEG 197
Cdd:PRK09133 97 GTDPKKPIL-LLAHMDVVEAKRED-WTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKR-EGFKPKrDIILALTG 173
|
90
....*....|....*....
gi 21071039 198 MEEAGSVA-LEELVEKEKD 215
Cdd:PRK09133 174 DEEGTPMNgVAWLAENHRD 192
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
28-213 |
3.25e-11 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 65.02 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 28 PSPPPALLEKVFQYIDLHQDEFVQTLKEWVAIES--DSVQPVPRFRQELFRMMAVAADTLQrlgarVASVDMgpQQLPDG 105
Cdd:PRK06837 1 MMLTPDLTQRILAAVDAGFDAQVAFTQDLVRFPStrGAEAPCQDFLARAFRERGYEVDRWS-----IDPDDL--KSHPGA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 106 QSLPI-----PPVILAELGSDPTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAF 180
Cdd:PRK06837 74 GPVEIdysgaPNVVGTYRPAGKTGRSLILQGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDAL 153
|
170 180 190
....*....|....*....|....*....|...
gi 21071039 181 RALeqdlpvnikfiieGMEEAGSVALEELVEKE 213
Cdd:PRK06837 154 RAA-------------GLAPAARVHFQSVIEEE 173
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
112-215 |
7.08e-10 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 60.94 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 112 PVILAELGSDPTKgtVCFYGHLDVQPADRGDgWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRalEQDLPVNI 191
Cdd:PRK08554 53 YAVYGEIGEGKPK--LLFMAHFDVVPVNPEE-WNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELS--KEPLNGKV 127
|
90 100
....*....|....*....|....
gi 21071039 192 KFIIEGMEEAGSVALEELVEKEKD 215
Cdd:PRK08554 128 IFAFTGDEEIGGAMAMHIAEKLRE 151
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
30-256 |
1.32e-09 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 60.03 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 30 PPPALLEKVFQYidlhQDEFVQTLKEWVAIESDSVQpVPrfrqELFRMMAVAADTLQRLGARVASVDMGPQqlpdgqslp 109
Cdd:PRK06133 24 PDAELLAAAQQE----QPAYLDTLKELVSIESGSGD-AE----GLKQVAALLAERLKALGAKVERAPTPPS--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 110 IPPVILAELgsdptKGT----VCFYGHLD-VQPAdrgdGWLTD-PYvltEVDG-KLYGRGATDNKGPVLAWINAVSAFRA 182
Cdd:PRK06133 86 AGDMVVATF-----KGTgkrrIMLIAHMDtVYLP----GMLAKqPF---RIDGdRAYGPGIADDKGGVAVILHALKILQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21071039 183 LEQDLPVNIKFIIEGMEEAGSVALEELVEKEKDRFfsgvDYIVisdNLWISQRKPAITYGTRGNSYFMVEVKCR 256
Cdd:PRK06133 154 LGFKDYGTLTVLFNPDEETGSPGSRELIAELAAQH----DVVF---SCEPGRAKDALTLATSGIATALLEVKGK 220
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
131-228 |
6.47e-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. 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: 57.85 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 131 GHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEGMEEAGS-VALEEL 209
Cdd:cd05650 76 SHLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSeYGIQYL 155
|
90
....*....|....*....
gi 21071039 210 VEKEKdrFFSGVDYIVISD 228
Cdd:cd05650 156 LNKFD--LFKKDDLIIVPD 172
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
23-212 |
6.57e-09 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 58.06 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 23 GMFSSPSP----PPALleKVFQYIDLH-QDEFVQTLKEWVAIESDSVQPVP--------RFRQELfRMMAvaadtlQRLG 89
Cdd:PRK06156 19 SAATQAAAatltKPQL--DALLYARLKyGAAAIESLRELVAFPTVRVEGVPqhenpefiGFKKLL-KSLA------RDFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 90 ARVASVDMgpqqlpdgqslpippVILaELGSDPT-KGTVCFYGHLDVQPAD----RGDGWLTDPYVLTEVDGKLYGRGAT 164
Cdd:PRK06156 90 LDYRNVDN---------------RVL-EIGLGGSgSDKVGILTHADVVPANpelwVLDGTRLDPFKVTLVGDRLYGRGTE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21071039 165 DNKGPVLAWINAVSAFRalEQDLPVN--IKFIIEGMEEAGSVALEELVEK 212
Cdd:PRK06156 154 DDKGAIVTALYAMKAIK--DSGLPLArrIELLVYTTEETDGDPLKYYLER 201
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
49-213 |
1.35e-08 |
|
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: 56.83 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 49 FVQTLKEWVAIESDSVQPvprfrQELFRMMAVAADTLQRLGARVASVDMGPqqlpdgqslpIPPVILAELGSDPTKGtVC 128
Cdd:cd03885 1 MLDLLERLVNIESGTYDK-----EGVDRVAELLAEELEALGFTVERRPLGE----------FGDHLIATFKGTGGKR-VL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 129 FYGHLD-VQPAdrgdGWLTD-PYvlTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEGMEEAGSVAL 206
Cdd:cd03885 65 LIGHMDtVFPE----GTLAFrPF--TVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGS 138
|
....*..
gi 21071039 207 EELVEKE 213
Cdd:cd03885 139 RELIEEE 145
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
114-235 |
4.23e-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: 55.12 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 114 ILAELGSDPTKgtVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQdLPVNIKF 193
Cdd:cd05649 44 VIGYIGGGKKK--ILFDGHIDTVGIGNIDNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGL-RDFAYTI 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 21071039 194 IIEGM---EEAGSVALEELVEKEKDRffsgVDYIVISD----NLWISQR 235
Cdd:cd05649 121 LVAGTvqeEDCDGVCWQYISKADKIK----PDFVVSGEptdgNIYRGQR 165
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
121-200 |
1.62e-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: 53.08 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 121 DPTKGTVCFYGHLD-VQPadrGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRAlEQDLPVNIKFIIEGME 199
Cdd:cd05651 52 DEGKPTLLLNSHHDtVKP---NAGWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYS-EGPLNYNLIYAASAEE 127
|
.
gi 21071039 200 E 200
Cdd:cd05651 128 E 128
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
115-168 |
2.24e-07 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 52.90 E-value: 2.24e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 21071039 115 LAELGSDPtkGTVCFYGHLDVQPADRGdGWLTDPYVLTEVDGKLYGRGATDNKG 168
Cdd:PRK05111 64 LASLGSGE--GGLLLAGHTDTVPFDEG-RWTRDPFTLTEHDGKLYGLGTADMKG 114
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
119-168 |
2.75e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 52.93 E-value: 2.75e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 21071039 119 GSDPTKGTVCFYGHLDVQPADRGDgWLTDPYVLTEVDGKLYGRGATDNKG 168
Cdd:PRK07906 60 GADPSRPALLVHGHLDVVPAEAAD-WSVHPFSGEIRDGYVWGRGAVDMKD 108
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
118-262 |
9.65e-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: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 118 LGSDPTKGTVCFYGHLDVQPAD---RgdgwltdpyvltEVDGKLYGRGATDNKGPVLAWINAVSAFraleqDLPVNIKFI 194
Cdd:cd05653 48 GGAGSGPPDVLLLGHIDTVPGEipvR------------VEGGVLYGRGAVDAKGPLAAMILAASAL-----NEELGARVV 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21071039 195 IEGM--EEAGSVALEELVEKeKDRFfsgvDYIVISDnlwisqrkPA----ITYGTRGNsyFMVEVKCRDQDFHS 262
Cdd:cd05653 111 VAGLvdEEGSSKGARELVRR-GPRP----DYIIIGE--------PSgwdgITLGYRGS--LLVKIRCEGRSGHS 169
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
126-396 |
1.20e-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: 50.63 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 126 TVCFYGHLDVQPAdrGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEGMEEAGSVA 205
Cdd:cd02697 75 TVALNAHGDVVPP--GDGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 206 -----LEELVEKEKDRFFSGVDYIVIsdnlwisqrkpaitygTRGNSYFMVEVKCRDQDFHSGtFGGILHEPMADLVALL 280
Cdd:cd02697 153 gpgwlLRQGLTKPDLLIAAGFSYEVV----------------TAHNGCLQMEVTVHGKQAHAA-IPDTGVDALQGAVAIL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 281 GSLVDSSghilvpgiydevvplteeeiNTYKAIhldleeyrnSSRVEKFlfdtkeeilmhlwRYPSLSIHGIEGafdepG 360
Cdd:cd02697 216 NALYALN--------------------AQYRQV---------SSQVEGI-------------THPYLNVGRIEG-----G 248
|
250 260 270
....*....|....*....|....*....|....*..
gi 21071039 361 TKT-VIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLED 396
Cdd:cd02697 249 TNTnVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIAD 285
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
113-397 |
1.21e-06 |
|
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: 50.92 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 113 VILAELGSDPtKGTVCFYG-HLDVQPADRgDGWLTDPYVLTeVDG-KLYGRGATDNKGPVlAWINAVsaFRALEQDLP-- 188
Cdd:cd08012 67 IIVEYPGTVD-GKTVSFVGsHMDVVTANP-ETWEFDPFSLS-IDGdKLYGRGTTDCLGHV-ALVTEL--FRQLATEKPal 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 189 ---VNIKFIIEgmEEAGS---VALEELV-EKEKDRFFSGVDYivisdnlWI--SQRKPAItyGTRGNSYFMveVKCRDQD 259
Cdd:cd08012 141 krtVVAVFIAN--EENSEipgVGVDALVkSGLLDNLKSGPLY-------WVdsADSQPCI--GTGGMVTWK--LTATGKL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 260 FHSGTfggilhePMADLVALlgSLVDSSGHILVPGIYDEVVPLTEEeintykaihldleeyrnssrvEKFLFDTKEEILM 339
Cdd:cd08012 208 FHSGL-------PHKAINAL--ELVMEALAEIQKRFYIDFPPHPKE---------------------EVYGFATPSTMKP 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 21071039 340 HLWRYPSLSIHGIegafdePGTKTvIPGrvigkfSIRLVPHMNVSAVEKQVTRHLEDV 397
Cdd:cd08012 258 TQWSYPGGSINQI------PGECT-ICG------DCRLTPFYDVKEVREKLEEYVDDI 302
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
119-179 |
1.23e-06 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 50.71 E-value: 1.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21071039 119 GSDPTKGTVCFYGHLDVQPADRG--DGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSA 179
Cdd:PRK08262 106 GSDPSLKPIVLMAHQDVVPVAPGteGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEA 168
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
47-200 |
7.78e-06 |
|
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: 48.04 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 47 DEFVQTLKEWVAIesDSVQPVPRF---RQELFRMmavaADtlqRLGARVASVDMGPQQlpdgqslpiPPVILAELGSDPT 123
Cdd:cd05646 2 DPAVTRFREYLRI--NTVHPNPDYdacVEFLKRQ----AD---ELGLPVRVIEVVPGK---------PVVVLTWEGSNPE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 124 KGTVCFYGHLDVQPADRgDGWLTDPY--VLTEvDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLP--VNIKFI----- 194
Cdd:cd05646 64 LPSILLNSHTDVVPVFE-EKWTHDPFsaHKDE-DGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKrtIHLSFVpdeei 141
|
....*...
gi 21071039 195 --IEGMEE 200
Cdd:cd05646 142 ggHDGMEK 149
|
|
| dapE-lys-deAc |
TIGR01902 |
N-acetyl-ornithine/N-acetyl-lysine deacetylase; This clade of mainly archaeal and related ... |
156-327 |
1.03e-05 |
|
N-acetyl-ornithine/N-acetyl-lysine deacetylase; This clade of mainly archaeal and related bacterial species contains two characterized enzymes, an deacetylase with specificity for both N-acetyl-ornithine and N-acetyl-lysine from Thermus, which is found within a lysine biosynthesis operon, and a fusion protein with acetyl-glutamate kinase (an enzyme of ornithine biosynthesis) from Lactobacillus. It is possible that all of the sequences within this clade have dual specificity, or that a mix of specificities have evolved within this clade.
Pssm-ID: 130957 [Multi-domain] Cd Length: 336 Bit Score: 47.54 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 156 GKLYGRGATDNKGPVLAWINAVSAFRaleqdlPVNIKFIIEGM--EEAGSVALEELVEKEKDrffsgvDYIVISDNLWIS 233
Cdd:TIGR01902 73 GLLYGRGAVDAKGPLIAMIFATWLLN------EKGIKVIVSGLvdEESSSKGAREVIDKNYP------FYVIVGEPSGAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 234 QrkpaITYGTRGNsyFMVEVKCRDQDFHSGTFGGILHEPMADLVALLGSLVDSSGHI---LVPGIYDEVVplTEEEINTY 310
Cdd:TIGR01902 141 G----ITLGYKGS--LQLKIMCEGTPFHSSSAGNAAELLIDYSKKIIEVYKQPENYDkpsIVPTIIRFGE--SYNDTPAK 212
|
170
....*....|....*..
gi 21071039 311 KAIHLDLEEYRNSSRVE 327
Cdd:TIGR01902 213 LELHFDLRYPPNNKPEE 229
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
119-179 |
1.79e-05 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 47.25 E-value: 1.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21071039 119 GSDPTKGTVCFYGHLDVQPADRG--DGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSA 179
Cdd:cd05674 64 GSDPSLKPLLLMAHQDVVPVNPEteDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVEL 126
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
111-182 |
3.26e-05 |
|
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: 46.32 E-value: 3.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21071039 111 PPVILAELGSDPTKGTVCFYGHLDVQPADRgDGWLTDPY-VLTEVDGKLYGRGATDNKGPVLAWINAVSAFRA 182
Cdd:TIGR01880 58 PVVVLTWPGSNPELPSILLNSHTDVVPVFR-EHWTHPPFsAFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKA 129
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
47-216 |
4.75e-05 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 45.55 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 47 DEFVQTLKEWVAIESDSVQPVPrfrqeLFRMMAVAADTLQRLGARVASVDmGPQQLPDGQSLPIPpvilaelgsDPTKGT 126
Cdd:PRK07473 11 EAMLAGLRPWVECESPTWDAAA-----VNRMLDLAARDMAIMGATIERIP-GRQGFGDCVRARFP---------HPRQGE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 127 --VCFYGHLD-VQPAD-------RGDGwltdpyvltevdGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIE 196
Cdd:PRK07473 76 pgILIAGHMDtVHPVGtleklpwRREG------------NKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFT 143
|
170 180
....*....|....*....|
gi 21071039 197 GMEEAGSVALEELVEKEKDR 216
Cdd:PRK07473 144 PDEEVGTPSTRDLIEAEAAR 163
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
116-203 |
9.93e-04 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 41.48 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 116 AELGSDPTkgTVCFYGHLDVQPADrgdgwltdpyVLTEV-DGKLYGRGATDNKGPVLAWINAVsafRALEQDLPVNIKFI 194
Cdd:PRK04443 53 GPAGDGPP--LVLLLGHIDTVPGD----------IPVRVeDGVLWGRGSVDAKGPLAAFAAAA---ARLEALVRARVSFV 117
|
....*....
gi 21071039 195 IEGMEEAGS 203
Cdd:PRK04443 118 GAVEEEAPS 126
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
340-400 |
1.18e-03 |
|
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: 38.48 E-value: 1.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21071039 340 HLWRYPSLSIHGIEGAFDepgtKTVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSK 400
Cdd:pfam07687 49 FDFPRTTLNITGIEGGTA----TNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEKELPE 105
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
123-179 |
2.06e-03 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 40.57 E-value: 2.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 21071039 123 TKGT--VCFYGHLDVQPAdrGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSA 179
Cdd:PRK08737 60 VRGTpkYLFNVHLDTVPD--SPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANA 116
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
36-205 |
2.43e-03 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 40.33 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 36 EKVFQYIDLHQDEFVQTLKEWVAIESDSvqpvpRFRQELFRMMAVAADTLQRLGARVASVDMGPQQL--PDG--QSLPIP 111
Cdd:PRK07338 6 RAVLDLIDDRQAPMLEQLIAWAAINSGS-----RNLDGLARMAELLADAFAALPGEIELIPLPPVEVidADGrtLEQAHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21071039 112 PVILAELGSDPTKgTVCFYGHLD-VQPADRGDGWLTDpyvltEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVN 190
Cdd:PRK07338 81 PALHVSVRPEAPR-QVLLTGHMDtVFPADHPFQTLSW-----LDDGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLG 154
|
170
....*....|....*
gi 21071039 191 IKFIIEGMEEAGSVA 205
Cdd:PRK07338 155 YDVLINPDEEIGSPA 169
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
148-207 |
4.31e-03 |
|
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: 39.18 E-value: 4.31e-03
10 20 30 40 50 60
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gi 21071039 148 PYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLP--VNIKFII------EGMEEAGSVALE 207
Cdd:cd05652 75 PYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEgdLGLLFVVgeetggDGMKAFNDLGLN 142
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