|
Name |
Accession |
Description |
Interval |
E-value |
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
8-477 |
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: 799.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 8 VFQKIDSLKPQFFSRLTKAIQIPAVSSDESLRSKVFDKAKFISEQLSQSGFhDIKMVDLGIQPPPiSTPNLSLPPVILSR 87
Cdd:cd05676 1 VFKYIDEHQDEFIERLREAVAIQSVSADPEKRPELIRMMEWAAERLEKLGF-KVELVDIGTQTLP-DGEELPLPPVLLGR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 88 FGSDPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVidEAKGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCF 167
Cdd:cd05676 79 LGSDPSKKTVLIYGHLDVQPAKLEDGWDTDPFELT--EKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 168 EGMEESGSLKLDELIKKEANGYFKGVDAVCISDNYWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIFGGVVAEPMID 247
Cdd:cd05676 157 EGMEESGSEGLDELIEARKDTFFSDVDYVCISDNYWLGKKKPCLTYGLRGICYFFIEVEGPNKDLHSGVFGGSVHEPMTD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 248 LMQVLGSLVDSKGKILIDGIDEMVAPLTEKEKALYKDIEFSVEELNAATGSKTSLYDKKEDILMHRWRYPSLSIHGVEGA 327
Cdd:cd05676 237 LIALMSSLVDSDGKILIPGIYDAVAPLTEEEWELYEKIDFDMEEYREDIGVRRLLYDNKEELLMHRWRYPSLSIHGIEGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 328 FSAQGAKTVIPSKVFGKFSIRTVPDMDSEKLTSLVQKHCDAKFKSLNSPNKCRTELIHDGAYWVSDPFNAQFTAAKKATK 407
Cdd:cd05676 317 FSGPGAKTVIPAKVIGKFSIRLVPNMDPEVVEKQVTDYLEKVFAELKSPNKLKVYMGHGGKPWVADPDHPNYKAARKATK 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 408 LVYGVDPDFTREGGSIPITLTFQDALNTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKTMAAYLQYYSE 477
Cdd:cd05676 397 RVFGVEPDLTREGGSIPITLTFQEATGKNVMLLPIGAADDGAHSQNEKINRRNYIEGTKLLAAYFHELSK 466
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
23-473 |
1.35e-140 |
|
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: 410.57 E-value: 1.35e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 23 LTKAIQIPAVSSDESLRSKVFDKAKFISEQLSQSGFhDIKMVDlgiqpppistpNLSLPPVILSRFGSDPSKKTVLVYGH 102
Cdd:cd03893 4 LAELVAIPSVSAQPDRREELRRAAEWLADLLRRLGF-TVEIVD-----------TSNGAPVVFAEFPGAPGAPTVLLYGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 103 YDVQPAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEGMEESGSLKLDELI 182
Cdd:cd03893 72 YDVQPAGDEDGWDSDPFELTERD--GRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEESGSPSLDQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 183 KKEANgyFKGVDAVCISDNYWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIFGGVVAEPMIDLMQVLGSLVDSKGKI 262
Cdd:cd03893 150 EAHRD--LLAADAIVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLDHDLHSGLYGGVVPDPMTALAQLLASLRDETGRI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 263 LIDGIDEMVAPLTEKEKALYKDIefsVEELNAATGsktslydKKEDILMHRWRYPSLSIHGVEGAFSAQGAKTVIPSKVF 342
Cdd:cd03893 228 LVPGLYDAVRELPEEEFRLDAGV---LEEVEIIGG-------TTGSVAERLWTRPALTVLGIDGGFPGEGSKTVIPPRAR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 343 GKFSIRTVPDMDSEKLTSLVQKHCDAKFKslnSPNKCRTELIHDGAYWVSDPFNAQFTAAKKATKLVYGVDPDFTREGGS 422
Cdd:cd03893 298 AKISIRLVPGQDPEEASRLLEAHLEKHAP---SGAKVTVSYVEGGMPWRSDPSDPAYQAAKDALRTAYGVEPPLTREGGS 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 768801288 423 IPITLTFQDALNTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKTMAAYLQ 473
Cdd:cd03893 375 IPFISVLQEFPQAPVLLIGVGDPDDNAHSPNESLRLGNYKEGTQAEAALLY 425
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
21-475 |
8.59e-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: 331.97 E-value: 8.59e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 21 SRLTKAIQIPAVSSDESLRSKVFDKAKFISEQLSQSGFHDIKMVDlgiqpppisTPNLslpPVILSRFGSDPSKKTVLVY 100
Cdd:cd05680 2 EELFELLRIPSVSADPAHKGDVRRAAEWLADKLTEAGFEHTEVLP---------TGGH---PLVYAEWLGAPGAPTVLVY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 101 GHYDVQPAQLEDGWDTEPFKLVIDEAKgiMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEGMEESGSLKLDE 180
Cdd:cd05680 70 GHYDVQPPDPLELWTSPPFEPVVRDGR--LYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIGSPSLPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 181 LIkkEANGYFKGVDAVCISDNYWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIFGGVVAEPMIDLMQVLGSLVDSKG 260
Cdd:cd05680 148 FL--EENAERLAADVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNRDLHSGSYGGAVPNPANALARLLASLHDEDG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 261 KILIDGIDEMVAPLTEKEKALYKDIEFSVEELNAATGSKTSLYDKKEDILMHRWRYPSLSIHGVEGAFSAQGAKTVIPSK 340
Cdd:cd05680 226 RVAIPGFYDDVRPLTDAEREAWAALPFDEAAFKASLGVPALGGEAGYTTLERLWARPTLDVNGIWGGYQGEGSKTVIPSK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 341 VFGKFSIRTVPDMDSEKLTSLVQKHCDAKfkslnSPN--KCRTELIHDGAYWVSDPFNAQFTAAKKATKLVYGVDPDFTR 418
Cdd:cd05680 306 AHAKISMRLVPGQDPDAIADLLEAHLRAH-----APPgvTLSVKPLHGGRPYLVPTDHPALQAAERALEEAFGKPPVFVR 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 768801288 419 EGGSIPITLTFQDALNTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKTMAAYLQYY 475
Cdd:cd05680 381 EGGSIPIVALFEKVLGIPTVLMGFGLPDDAIHAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
82-460 |
8.79e-97 |
|
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: 298.87 E-value: 8.79e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 82 PVILSRF---GSDPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWI-NVVDAFKAsgQ 157
Cdd:cd05677 56 PIVLATFsgnSSDAKRKRILFYGHYDVIPAGETDGWDTDPFTLTCEN--GYLYGRGVSDNKGPLLAAIyAVAELFQE--G 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 158 EFPVNLVTCFEGMEESGSLKLDELIKKeaNGYFKG-VDAVCISDNYWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGI 236
Cdd:cd05677 132 ELDNDVVFLIEGEEESGSPGFKEVLRK--NKELIGdIDWILLSNSYWLDDNIPCLNYGLRGVIHATIVVSSDKPDLHSGV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 237 FGGVVAEPMIDLMQVLGSLVDSKGKILIDGIDEMVAPLTEKEKALYKDIefsVEELNAATgsktslyDKKEDILMHRWRY 316
Cdd:cd05677 210 DGGVLREPTADLIKLLSKLQDPDGRILIPHFYDPVKPLTEAERARFTAI---AETALIHE-------DTTVDSLIAKWRK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 317 PSLSIHGVEgaFSAQGAKTVIPSKVFGKFSIRTVPDMDSEKLTSLVQKHCDAKFKSLNSPNKCRTELIHDGAYWVSDPFN 396
Cdd:cd05677 280 PSLTVHTVK--VSGPGNTTVIPKSASASVSIRLVPDQDLDVIKQDLTDYIQSCFAELKSQNHLDIEVLNEAEPWLGDPDN 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768801288 397 AQFTAAKKATKLVYGVDPDFTREGGSIPITLTFQDALNTSVLLLPMGRGDDGAHSINEKLDISN 460
Cdd:cd05677 358 PAYQILREAVTAAWGVEPLYIREGGSIPTIRFLEKEFNAPAVQLPCGQSSDNAHLDNERLRIKN 421
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
23-477 |
1.50e-87 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 275.47 E-value: 1.50e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 23 LTKAIQIPAVSSDESLRSKVFDKAKFISEQLSQSGFHDIKMVDLGIQPppistpnlslppVILSRFGSDPSKKTVLVYGH 102
Cdd:PRK08201 20 LKEFLRIPSISALSEHKEDVRKAAEWLAGALEKAGLEHVEIMETAGHP------------IVYADWLHAPGKPTVLIYGH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 103 YDVQPAQLEDGWDTEPFKLVIDEAKgiMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEGMEESGSLKLDELI 182
Cdd:PRK08201 88 YDVQPVDPLNLWETPPFEPTIRDGK--LYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEEIGSPNLDSFV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 183 KKEANGYfkGVDAVCISDNYWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIFGGVVAEPMIDLMQVLGSLVDSKGKI 262
Cdd:PRK08201 166 EEEKDKL--AADVVLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLHSGLYGGAVPNALHALVQLLASLHDEHGTV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 263 LIDGIDEMVAPLTEKEKALYKDIEFSVEELNAATGSKTsLYDKKEDILMHR-WRYPSLSIHGVEGAFSAQGAKTVIPSKV 341
Cdd:PRK08201 244 AVEGFYDGVRPLTPEEREEFAALGFDEEKLKRELGVDE-LFGEEGYTALERtWARPTLELNGVYGGFQGEGTKTVIPAEA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 342 FGKFSIRTVPDMDSEKLTSLVQKHCDAkfkslNSPNKCRTELI-HDGAY-WVSDPFNAQFTAAKKATKLVYGVDPDFTRE 419
Cdd:PRK08201 323 HAKITCRLVPDQDPQEILDLIEAHLQA-----HTPAGVRVTIRrFDKGPaFVAPIDHPAIQAAARAYEAVYGTEAAFTRM 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 768801288 420 GGSIPITLTFQDALNTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKTMAAYLQYYSE 477
Cdd:PRK08201 398 GGSIPVVETFSSQLHIPIVLMGFGLPSENFHAPNEHFHLENFDKGLRTLVEYWHQLAE 455
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
19-472 |
4.55e-76 |
|
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: 244.94 E-value: 4.55e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 19 FFSRLTKAIQIPAVSSDESlrsKVFDKAKFISEQLSqsgfhdikmvDLGIQPPPISTPNlslPPVILSRFGSDpSKKTVL 98
Cdd:cd05681 1 YLEDLRDLLKIPSVSAQGR---GIPETADFLKEFLR----------RLGAEVEIFETDG---NPIVYAEFNSG-DAKTLL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 99 VYGHYDVQPAQLEDGWDTEPFKLVIDEAKgiMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEGMEESGSLKL 178
Cdd:cd05681 64 FYNHYDVQPAEPLELWTSDPFELTIRNGK--LYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPNL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 179 DELIKKEANgyFKGVDAvCISDNYWLGTK-KPVLTYGLRGCNYYQTIIEGPSADLHSGiFGGVVAEPMIDLMQVLGSLVD 257
Cdd:cd05681 142 EKFVAEHAD--LLKADG-CIWEGGGKNPKgRPQISLGVKGIVYVELRVKTADFDLHSS-YGAIVENPAWRLVQALNSLRD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 258 SKGKILIDGIDEMVAPLTEKEKALYKDIEFSVEELNAATGSKTSLYDKKEDILMHRWRYPSLSIHGVEGAFSAQGAKTVI 337
Cdd:cd05681 218 EDGRVLIPGFYDDVRPLSEAERALIDTYDFDPEELRKTYGLKRPLQVEGKDPLRALFTEPTCNINGIYSGYTGEGSKTIL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 338 PSKVFGKFSIRTVPDMDSEKLTSLVQKHCDAkfkslnsPNKCRTELIHDGAY--WVSDPFNAQFTAAKKATKLVYGVDPD 415
Cdd:cd05681 298 PSEAFAKLDFRLVPDQDPAKILSLLRKHLDK-------NGFDDIEIHDLLGEkpFRTDPDAPFVQAVIESAKEVYGQDPI 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 768801288 416 FTRE-GGSIPITlTFQDALNTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKTMAAYL 472
Cdd:cd05681 371 VLPNsAGTGPMY-PFYDALEVPVVAIGVGNAGSNAHAPNENIRIADYYKGIEHTEELL 427
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
1-469 |
1.46e-73 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 239.42 E-value: 1.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 1 MSHSLTSVFQKIDSLKPQFFSRLTKAIQIPAVSSDESLRSKVFDKAKFISEQLSQSGFhdikmvDLGIQPPPistpnlSL 80
Cdd:PRK09104 1 SMADLDPVLDHIDANLDASLERLFALLRIPSISTDPAYAADCRKAADWLVADLASLGF------EASVRDTP------GH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 81 PPVILSRFGSDPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDE-AKG--IMKGRGVTDDTGPLLSWINVVDAFKASGQ 157
Cdd:PRK09104 69 PMVVAHHEGPTGDAPHVLFYGHYDVQPVDPLDLWESPPFEPRIKEtPDGrkVIVARGASDDKGQLMTFVEACRAWKAVTG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 158 EFPVNLVTCFEGMEESGSLKLDELIkkEANGYFKGVDAVCISDNYWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIF 237
Cdd:PRK09104 149 SLPVRVTILFEGEEESGSPSLVPFL--EANAEELKADVALVCDTGMWDRETPAITTSLRGLVGEEVTITAADRDLHSGLF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 238 GGVVAEPMIDLMQVLGSLVDSKGKILIDGIDEMVAPLTEKEKALYKDIEFSVEELNAATGSKTSLYDKKEDILMHRWRYP 317
Cdd:PRK09104 227 GGAAANPIRVLTRILAGLHDETGRVTLPGFYDGVEELPPEILAQWKALGFTAEAFLGPVGLSIPAGEKGRSVLEQIWSRP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 318 SLSIHGVEGAFSAQGAKTVIPSKVFGKFSIRTVPDMDSEKLTSLVQKHCDAKFkslnsPNKCRTELI-HDGAYWVSDPFN 396
Cdd:PRK09104 307 TCEINGIWGGYTGEGFKTVIPAEASAKVSFRLVGGQDPAKIREAFRAYVRARL-----PADCSVEFHdHGGSPAIALPYD 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768801288 397 -AQFTAAKKATKLVYGVDPDFTREGGSIPITLTFQDALNTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKTMA 469
Cdd:PRK09104 382 sPALAAAKAALSDEWGKPAVLIGSGGSIPIVGDFKRILGMDSLLVGFGLDDDRIHSPNEKYDLESFHKGIRSWA 455
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
6-477 |
8.49e-59 |
|
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: 198.57 E-value: 8.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 6 TSVFQKIDSLKPQFFSRLTKAIQIPAVSSDESlrskvfDKAKFISEQLSQSGFHdikmVDlgIQPPPISTPNLslppviL 85
Cdd:COG0624 1 AAVLAAIDAHLDEALELLRELVRIPSVSGEEA------AAAELLAELLEALGFE----VE--RLEVPPGRPNL------V 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 86 SRFGSDPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVT 165
Cdd:COG0624 63 ARRPGDGGGPTLLLYGHLDVVPPGDLELWTSDPFEPTIED--GRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 166 CFEGMEESGSLKLDELIKKEANGYfkGVDAVCISDnywlGTKKPVLTYGLRGCNYYQTIIEGPSAdlHSGIFGGVVAePM 245
Cdd:COG0624 141 LFTGDEEVGSPGARALVEELAEGL--KADAAIVGE----PTGVPTIVTGHKGSLRFELTVRGKAA--HSSRPELGVN-AI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 246 IDLMQVLGSLvdskgkilidgidemvapltekekalyKDIEFSVEElNAATGsktslydkkedilmhrwrYPSLSIHGVE 325
Cdd:COG0624 212 EALARALAAL---------------------------RDLEFDGRA-DPLFG------------------RTTLNVTGIE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 326 GafsaqGAKT-VIPSKVFGKFSIRTVPDMDSEKLTSLVQKHCDAKFKSLnspnKCRTELIHDGAY-WVSDPFNAQFTAAK 403
Cdd:COG0624 246 G-----GTAVnVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGV----EVEVEVLGDGRPpFETPPDSPLVAAAR 316
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768801288 404 KATKLVYGVDPDFTREGGSIPITLtFQDALNTSVLLLPMGRGdDGAHSINEKLDISNFVGGMKTMAAYLQYYSE 477
Cdd:COG0624 317 AAIREVTGKEPVLSGVGGGTDARF-FAEALGIPTVVFGPGDG-AGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
63-477 |
1.12e-57 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 196.90 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 63 MVDLGIQPPPISTPNlslPPVILSRFGSDpSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEAKgiMKGRGVTDDTGPL 142
Cdd:PRK06446 35 MEKLGIKANIERTKG---HPVVYGEINVG-AKKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGR--IYARGASDNKGTL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 143 LS-WINVVDAFKASgqEFPVNLVTCFEGMEESGSLKLDELIKKEANgYFKGvDAVcISDNYWLGTK-KPVLTYGLRGCNY 220
Cdd:PRK06446 109 MArLFAIKHLIDKH--KLNVNVKFLYEGEEEIGSPNLEDFIEKNKN-KLKA-DSV-IMEGAGLDPKgRPQIVLGVKGLLY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 221 YQTIIEGPSADLHSgIFGGVVAEPMIDLMQVLGSLVDSKGKILIDGIDEMVAPLTEKEKALYKDIEFSVEELNAATGSKT 300
Cdd:PRK06446 184 VELVLRTGTKDLHS-SNAPIVRNPAWDLVKLLSTLVDGEGRVLIPGFYDDVRELTEEERELLKKYDIDVEELRKALGFKE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 301 SLYDKKEDILMHRWRYPSLSIHGVEGAFSAQGAKTVIPSKVFGKFSIRTVPDMDSEKLTSLVQKHCDakfkslnsPNKCR 380
Cdd:PRK06446 263 LKYSDREKIAEALLTEPTCNIDGFYSGYTGKGSKTIVPSRAFAKLDFRLVPNQDPYKIFELLKKHLQ--------KVGFN 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 381 TELIHDGA-YWVSDPFNAQFTAAK-KATKLVYGVDPD-FTREGGSIPITLtFQDALNTSVLLLPMGRGDDG--AHSINEK 455
Cdd:PRK06446 335 GEIIVHGFeYPVRTSVNSKVVKAMiESAKRVYGTEPVvIPNSAGTQPMGL-FVYKLGIRDIVSAIGVGGYYsnAHAPNEN 413
|
410 420
....*....|....*....|..
gi 768801288 456 LDISNFVGGMKTMAAYLQYYSE 477
Cdd:PRK06446 414 IRIDDYYKAIKHTEEFLKLYST 435
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
1-478 |
1.43e-54 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 188.96 E-value: 1.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 1 MSHSLTSVFQKIDSLKPQFFSRLTKAIQIPAVSSDESLRSKVFDKAKFISEQLSQSGFHDIKMVDLGiqpppistpnlSL 80
Cdd:PRK07907 2 TILTADDLRARVAELLPRVRADLEELVRIPSVAADPFRREEVARSAEWVADLLREAGFDDVRVVSAD-----------GA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 81 PPVILSRFGSdPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVidEAKGIMKGRGVTDDTGpllswiNVV---DAFKASGQ 157
Cdd:PRK07907 71 PAVIGTRPAP-PGAPTVLLYAHHDVQPPGDPDAWDSPPFELT--ERDGRLYGRGAADDKG------GIAmhlAALRALGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 158 EFPVNLVTCFEGMEESGSLKLDELIKKEANGYFKGVDAVCISDNYWLGTkkPVLTYGLRG---CNYYQTIIEGPsadLHS 234
Cdd:PRK07907 142 DLPVGVTVFVEGEEEMGSPSLERLLAEHPDLLAADVIVIADSGNWSVGV--PALTTSLRGnadVVVTVRTLEHA---VHS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 235 GIFGGVVAEPMIDLMQVLGSLVDSKGKILIDGID--EMVAPLTEKEKALYKD--IEFSVEElnAATGSKTslydkkeDIL 310
Cdd:PRK07907 217 GQFGGAAPDALTALVRLLATLHDEDGNVAVDGLDatEPWLGVDYDEERFRADagVLDGVEL--IGTGSVA-------DRL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 311 mhrWRYPSLSIHGVEgAFSAQGAKTVIPSKVFGKFSIRTVPDMDSEKLTSLVQKHCDAkfkslNSPNKCR--TELIHDGA 388
Cdd:PRK07907 288 ---WAKPAITVIGID-APPVAGASNALPPSARARLSLRVAPGQDAAEAQDALVAHLEA-----HAPWGAHvtVERGDAGQ 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 389 YWVSDPFNAQFTAAKKATKLVYGVDPDFTREGGSIPITLTFQDAL-NTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKT 467
Cdd:PRK07907 359 PFAADASGPAYDAARAAMREAWGKDPVDMGMGGSIPFIAELQEAFpQAEILVTGVEDPKTRAHSPNESVHLGELERAAVA 438
|
490
....*....|.
gi 768801288 468 MAAYLQYYSES 478
Cdd:PRK07907 439 EALLLARLAAA 449
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
82-473 |
7.17e-47 |
|
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: 168.82 E-value: 7.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 82 PVILSRFGSDPSKKTVLVYGHYDVQPA-----------------QLEDG-WDTEPFKLV---IDEAKGIMkGRGVTDDTG 140
Cdd:cd05678 48 PLLLAEKPISDARKTVLFYMHLDGQPVdpskwdqkspytpvlkrKDAAGnWEEINWDAIfsnLDPEWRVF-ARAAADDKG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 141 PLLSWINVVDAFKASGQEFPVNLVTCFEGMEESGSLKLDELIKKEANGYfkGVDAVCISDNYWLGTKKPVLTYGLRGCNY 220
Cdd:cd05678 127 PIMMMLAALDALKAGGIAPKFNVKIILDSEEEKGSPSLPKAVKEYKELL--AADALIIMDGPAHATNKPTLTFGCRGIAT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 221 YQTIIEGPSADLHSGIFGGVVAEPMIDLMQVLGSLVDSKGKILI----DGIDemvapLTEKEKALYKDIEFSVEELNAAT 296
Cdd:cd05678 205 ATLTTYGAKVPQHSGHYGNYAPNPAFRLSSLLASMKDDTGKVTIpgfyDGIS-----IDEETQKILAAVPDDEESINKRL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 297 GSKTSlyDKKEDILMHRWRYPSLSIHGVEGAFSAQGAKTVIPSKVFGKFSIRTVPDMDSEKLTSLVQKHCD--------- 367
Cdd:cd05678 280 GIAQT--DKVGRNYQEALQYPSLNVRGMESGWKGDKVRTIIPEIAEAEIDIRLVPESDGPYLLDLVKAHIEkqgyfvtdr 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 368 -------------AKFKSLNSPNKCRTELihdgaywvsDPFNAQFtaAKKATKLVYGVDPDFTR-EGGSIPITlTFQDAL 433
Cdd:cd05678 358 aptdeerlahdkiAKFTYRNGADAFRTDI---------NSPIGNW--LRKALTDEFGEEPIQIRmMGGTVPIA-PFVNVL 425
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 768801288 434 NTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKTMAAYLQ 473
Cdd:cd05678 426 DIPAIIVPMVNMDNNQHSPNENLRIGNIRTGIRTCYAILT 465
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
98-473 |
2.87e-37 |
|
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: 139.02 E-value: 2.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 98 LVYGHYDVQPAQLEDGWdtePFKLVIDeakGIMKGRGVTDDTGPLLSWINVVDAFKASGQEfPVNLVTCFEGMEES---G 174
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTED---GKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGgmgG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 175 SLKLDELIKKEANGyFKGVDAVCISD-NYWLGTKKPVLTYGLRGCNYYQTIIEGPSAdlHSGIFgGVVAEPMIDLMQVLG 253
Cdd:pfam01546 74 ARALIEDGLLEREK-VDAVFGLHIGEpTLLEGGIAIGVVTGHRGSLRFRVTVKGKGG--HASTP-HLGVNAIVAAARLIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 254 SLVDSKGKiLIDGIDEMVAPLTekekalykdiefsveelnaatgsktslydkkedilmhrwrypslSIHGVEGAFsaqga 333
Cdd:pfam01546 150 ALQDIVSR-NVDPLDPAVVTVG--------------------------------------------NITGIPGGV----- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 334 kTVIPSKVFGKFSIRTVPDMDSEKLTSLVQKHCDAKFKSLNSpnKCRTELIHDGAYWVSDpfNAQFT-AAKKATKLVYGV 412
Cdd:pfam01546 180 -NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGV--KVEVEYVEGGAPPLVN--DSPLVaALREAAKELFGL 254
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768801288 413 DPDFTREGgsIPITLTFQ---DALNTSVLLLpmGRGDDGAHSINEKLDISNFVGGMKTMAAYLQ 473
Cdd:pfam01546 255 KVELIVSG--SMGGTDAAfflLGVPPTVVFF--GPGSGLAHSPNEYVDLDDLEKGAKVLARLLL 314
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
80-472 |
1.51e-28 |
|
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: 117.43 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 80 LPPVILSRF-GSDPSKKTVLVYGHYDVQPAQleDGW--DTEPFKLVIDEAKgiMKGRGVTDDTGPLLSWINVVDAFKASG 156
Cdd:cd05682 58 RTPLLFVEIpGTEQDDDTVLLYGHMDKQPPF--TGWdeGLGPTKPVIRGDK--LYGRGGADDGYAIFASLTAIKALQEQG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 157 QEFPvNLVTCFEGMEESGSLKLDELIKKEANgYFKGVD-AVCI---SDNY---WlgtkkpvLTYGLRGCN----YYQTII 225
Cdd:cd05682 134 IPHP-RCVVLIEACEESGSADLPFYLDKLKE-RIGNVDlVVCLdsgCGNYeqlW-------LTTSLRGVLggdlTVQVLN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 226 EGpsadLHSGIFGGVVAEPMIDLMQVLGSLVDSK-GKILIDGIDEMVAPLTEKEKALYKDI--EFSVEELNAATGSKTSL 302
Cdd:cd05682 205 EG----VHSGDASGIVPSSFRILRQLLSRIEDENtGEVKLDEQHCDIPAHRYEQAKKIAEIlgEAVYEEFPFVSGVQPVT 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 303 YDKKEDILMHRWRyPSLSIHGVEGAFSAQGAKTVIPSKVFGKFSIRTVPDMDSEKLTSLVQK--------HCDAKFKSLN 374
Cdd:cd05682 281 TDLVQLYLNRTWK-PQLSVTGADGLPPASTAGNVLRPETTLKLSLRLPPTVDAEKASAALKKlletdppyNAKVTFKSDG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 375 SPNKCRTELIHDgayWVSDpfnaqftAAKKATKLVYGVDPDFTREGGSIPITLTFQDA------LNTSVLllpmgrG-DD 447
Cdd:cd05682 360 AGSGWNAPLLSP---WLAK-------ALNEASQLFFGKPAAYQGEGGSIPFMNMLGEKfpkaqfIVTGVL------GpKS 423
|
410 420
....*....|....*....|....*
gi 768801288 448 GAHSINEKLDIsNFVGGMKTMAAYL 472
Cdd:cd05682 424 NAHGPNEFLHI-PYTKKLTACVAYV 447
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
19-469 |
7.73e-20 |
|
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: 91.79 E-value: 7.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 19 FFSRLTKAIQIPAVSSDESLRSKVFDKA-KFISEQLSQSGFhDIKMVDlgiqpppisTPNLSLPPVILSRFGSDPSKKTV 97
Cdd:cd05679 6 FLAELARRVAVPTESQEPARKPELRAYLdQEMRPRFERLGF-TVHIHD---------NPVAGRAPFLIAERIEDPSLPTL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 98 LVYGHYDVQP---AQLEDGWDtePFKLVIDEAKgiMKGRGVTDDTGPLLswINVV---DAFKASGQEFPVNLVTCFEGME 171
Cdd:cd05679 76 LIYGHGDVVPgyeGRWRDGRD--PWTVTVWGER--WYGRGTADNKGQHS--INMAalrQVLEARGGKLGFNVKFLIEMGE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 172 ESGSLKLDELIkkEANGYFKGVDAVCISDNYWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIFGGVVAEPMIDLMQV 251
Cdd:cd05679 150 EMGSPGLRAFC--FSHREALKADLFIASDGPRLAADRPTMFLGSRGGLNFELRVNLREGGHHSGNWGGLLANPGIILANA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 252 LGSLVDSKGKILIDGIdeMVAPLTEKEKALYKDIEfsveelnAATGSKTSLYDKKedilmhrWRYPSLSI-HGVEG---- 326
Cdd:cd05679 228 IASLVDGKGRIKLPAL--KPAHLPNSVRSALADVE-------VGGGPDDPSIDPW-------WGEPGLTAaERVFGwntl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 327 ---AFSA---QGAKTVIPSKVFGKFSIRTVPDMDSEKLTSLVQKHCDAK-------FKSLNSPNKCRTELIHDGAYWVSD 393
Cdd:cd05679 292 evlAFKTgnpDAPVNAIPGHAEAICQIRFVVGTDPDTFIPAVRAHLDANgfdgvevTASQMVFAATRLDPDSPWVGWALA 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768801288 394 pfNAQFTAAKKATKLvygvdPDFtreGGSIPITLtFQDALNTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKTMA 469
Cdd:cd05679 372 --SLQKTTGKKPALL-----PNL---GGSLPNDV-FSEVLGLPTLWVPHSYPACSQHAPNEHILAPVMREALRVMA 436
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
17-286 |
1.22e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 88.05 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 17 PQFFSRLTKAIQIPAVS----SDESLRSKVFDkakFISEQLSQSGFhDIKMVDlgiqpppisTPNLSLPPVILSRFGSDP 92
Cdd:PRK07079 17 GAFFADLARRVAYRTESqnpdRAPALRAYLTD---EIAPALAALGF-TCRIVD---------NPVAGGGPFLIAERIEDD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 93 SKKTVLVYGHYDVQPAQlEDGWDT--EPFKLVIDEAKgiMKGRGVTDDTGPllSWINVV---DAFKASGQEFPVNLVTCF 167
Cdd:PRK07079 84 ALPTVLIYGHGDVVRGY-DEQWREglSPWTLTEEGDR--WYGRGTADNKGQ--HTINLAaleQVLAARGGRLGFNVKLLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 168 EGMEESGSLKLDELIKKEAngyfkgvDA----VCI-SDNYWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIFGGVVA 242
Cdd:PRK07079 159 EMGEEIGSPGLAEVCRQHR-------EAlaadVLIaSDGPRLSAERPTLFLGSRGAVNFRLRVNLRDGAHHSGNWGGLLR 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 768801288 243 EPMIDLMQVLGSLVDSKGKILIDGIdeMVAPLTEKEKALYKDIE 286
Cdd:PRK07079 232 NPGTVLAHAIASLVDARGRIQVPGL--RPPPLPAAVRAALADIT 273
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
84-215 |
7.25e-18 |
|
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 81.71 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 84 ILSRFGSDPSKKTVLVYGHYDVQPAQleDGWDTEPFKLVIDEAKGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNL 163
Cdd:cd18669 2 VIARYGGGGGGKRVLLGAHIDVVPAG--EGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 768801288 164 VTCFEGMEESGSLKLDELIKKEANGYFKGVDAVCISDNYWLGTKKPVLTYGL 215
Cdd:cd18669 80 VVAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTPL 131
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
23-462 |
2.78e-17 |
|
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: 83.22 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 23 LTKAIQIPAVSSDeslRSKVFDKAKFISEQLSQSGFhDIKMVDlgiqpPPISTPNlSLPPVILSRFGSDpSKKTVLVYGH 102
Cdd:TIGR01910 4 LKDLISIPSVNPP---GGNEETIANYIKDLLREFGF-STDVIE-----ITDDRLK-VLGKVVVKEPGNG-NEKSLIFNGH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 103 YDVQPAQLEDGWDTEPFKLVIDEAKgiMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEGMEESGSLKLDELI 182
Cdd:TIGR01910 73 YDVVPAGDLELWKTDPFKPVEKDGK--LYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 183 KKeanGYFKGVDAVCISDNywlgTKKPVLTYGLRGCNYYQTIIEGPSAdlHSGifggvvaepmidlMQVLGslvdskgki 262
Cdd:TIGR01910 151 QR---GYFKDADGVLIPEP----SGGDNIVIGHKGSIWFKLRVKGKQA--HAS-------------FPQFG--------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 263 lIDGIDEMvapltekekalYKDIefsvEELNAATGSKTSLYDKKEDilMHRWRYPSLSIHGVEGAfsaqgakTVIPSKVF 342
Cdd:TIGR01910 200 -VNAIMKL-----------AKLI----TELNELEEHIYARNSYGFI--PGPITFNPGVIKGGDWV-------NSVPDYCE 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 343 GKFSIRTVPDMDSEKLTSLVQKHCDAKFKSLNSPNKCRTELIHDGAYWVsDPFNAQFTAAKKATKLVYGVDPdftREGGS 422
Cdd:TIGR01910 255 FSIDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYENEPVVKWSGPNET-PPDSRLVKALEAIIKKVRGIEP---EVLVS 330
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 768801288 423 IPITLT--FQDALNTSVLLlpmGRGDDG-AHSINEKLDISNFV 462
Cdd:TIGR01910 331 TGGTDArfLRKAGIPSIVY---GPGDLEtAHQVNEYISIKNLV 370
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
84-213 |
7.20e-16 |
|
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: 75.92 E-value: 7.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 84 ILSRFGSDPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNL 163
Cdd:cd03873 2 LIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEE--GRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTI 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 768801288 164 VTCFEGMEESGSLKLDELIKKEANGYFKGVDAVCISD--NYWLGTKKPVLTY 213
Cdd:cd03873 80 VVAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDatAGPILQKGVVIRN 131
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
23-462 |
8.94e-15 |
|
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: 75.41 E-value: 8.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 23 LTKAIQIPAVSSDESlrskvfDKAKFISEQLSQSGFhdikmvdlGIQPPPIS-TPNLslppviLSRFGSDpSKKTVLVYG 101
Cdd:cd08659 3 LQDLVQIPSVNPPEA------EVAEYLAELLAKRGY--------GIESTIVEgRGNL------VATVGGG-DGPVLLLNG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 102 HYDVQPAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVN---LVTCFEGMEESGSLKL 178
Cdd:cd08659 62 HIDTVPPGDGDKWSFPPFSGRIRD--GRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRvalLATVDEEVGSDGARAL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 179 DElikkeaNGYFKGVDAVCI---SDNYwlgtkkpvLTYGLRGCNYYQTIIEGPSAdlHSGI-FGGVVA-EPMIDLMQVLG 253
Cdd:cd08659 140 LE------AGYADRLDALIVgepTGLD--------VVYAHKGSLWLRVTVHGKAA--HSSMpELGVNAiYALADFLAELR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 254 SLVDSKGKilidgiDEMVAPLTekekalykdieFSVEELNAATGSKtslydkkedilmhrwrypslsihgvegafsaqga 333
Cdd:cd08659 204 TLFEELPA------HPLLGPPT-----------LNVGVINGGTQVN---------------------------------- 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 334 ktVIPSKVFGKFSIRTVPDMDSEKLTSLVQKHCDAKFKSLNSpnkcrtELIHDG-AYWVSDPFNAQFTAAKKATKlVYGV 412
Cdd:cd08659 233 --SIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTV------EVSLDGdPPFFTDPDHPLVQALQAAAR-ALGG 303
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 768801288 413 DPDftrEGGSIPITltfqDAlntsVLLLPM--------GRGDDG-AHSINEKLDISNFV 462
Cdd:cd08659 304 DPV---VRPFTGTT----DA----SYFAKDlgfpvvvyGPGDLAlAHQPDEYVSLEDLL 351
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
21-207 |
2.16e-12 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 68.48 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 21 SRLTKAIQIPavsSDESLRSKVFDKAKFISEQLSQSGFHdikmvdLGIQPPPISTPNLSLPPVILSRFGSDPSKKTVLVY 100
Cdd:PRK08651 10 EFLKDLIKIP---TVNPPGENYEEIAEFLRDTLEELGFS------TEIIEVPNEYVKKHDGPRPNLIARRGSGNPHLHFN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 101 GHYDVQPAQleDGWD-TEPFKLVIDEakGIMKGRGVTDDTGPLLSWInvvDAFKASGQEFPVNLVTCFEGMEESGSL--- 176
Cdd:PRK08651 81 GHYDVVPPG--EGWSvNVPFEPKVKD--GKVYGRGASDMKGGIAALL---AAFERLDPAGDGNIELAIVPDEETGGTgtg 153
|
170 180 190
....*....|....*....|....*....|.
gi 768801288 177 KLDELIKKEANGYFKGVDAVciSDNYWLGTK 207
Cdd:PRK08651 154 YLVEEGKVTPDYVIVGEPSG--LDNICIGHR 182
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
13-200 |
4.85e-12 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 67.57 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 13 DSLKPQFFSRLTKAIQIPAVSSD-----EslrskvFDKAKFISEQLSQSGFHDIKMVDlgiqpppisTPNLSLP----PV 83
Cdd:PRK13983 1 DELRDEMIELLSELIAIPAVNPDfggegE------KEKAEYLESLLKEYGFDEVERYD---------APDPRVIegvrPN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 84 ILSRFGSDPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNL 163
Cdd:PRK13983 66 IVAKIPGGDGKRTLWIISHMDVVPPGDLSLWETDPFKPVVKD--GKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNL 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 768801288 164 VTCFEGMEESGSL-KLDELIKKEaNGYFKGVDAVCISD 200
Cdd:PRK13983 144 GLAFVSDEETGSKyGIQYLLKKH-PELFKKDDLILVPD 180
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
89-175 |
5.16e-11 |
|
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: 64.30 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 89 GSDPSKKTVLVYGHYDVQPAQLEDgWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFE 168
Cdd:cd05675 60 GTDPSAGPLLLLGHIDVVPADASD-WSVDPFSGEIKD--GYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFV 136
|
....*..
gi 768801288 169 GMEESGS 175
Cdd:cd05675 137 ADEEAGG 143
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
18-174 |
1.25e-09 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 59.71 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 18 QFFSRLtkaIQIPAVSSDESLRSKVfdkAKFISEQLSQSGFhdikmvDLGIQPPPISTPNLslPPVILSrfgsDPSKKTV 97
Cdd:cd08011 2 KLLQEL---VQIPSPNPPGDNTSAI---AAYIKLLLEDLGY------PVELHEPPEEIYGV--VSNIVG----GRKGKRL 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768801288 98 LVYGHYDVQPAQLEDGWDTEPFKLVIDEAKgiMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEGMEESG 174
Cdd:cd08011 64 LFNGHYDVVPAGDGEGWTVDPYSGKIKDGK--LYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETG 138
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
27-175 |
4.91e-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: 58.24 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 27 IQIPAVSSdESLRSKVFDKAKFISEQLSQSGFHDIKMVDLgIQPPPISTPNLslppVILSRFGSDpskKTVLVYGHYDVQ 106
Cdd:cd05650 11 IRIPAVNP-ESGGEGEKEKADYLEKKLREYGFYTLERYDA-PDERGIIRPNI----VAKIPGGND---KTLWIISHLDTV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768801288 107 PAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEGMEESGS 175
Cdd:cd05650 82 PPGDLSLWETDPWEPVVKD--GKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGS 148
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
5-255 |
7.12e-08 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 54.66 E-value: 7.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 5 LTSVFQKIDSLKPQFFSRLTKAIQIPAVS-----SDESlrskvfdkAKFISEQLSQSGFhDIKMVDLgiqpppisTPNLs 79
Cdd:PRK08596 1 VSQLLEQIELRKDELLELLKTLVRFETPApparnTNEA--------QEFIAEFLRKLGF-SVDKWDV--------YPND- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 80 lPPVILSRFGSDPSK-KTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASGQE 158
Cdd:PRK08596 63 -PNVVGVKKGTESDAyKSLIINGHMDVAEVSADEAWETNPFEPTIKD--GWLYGRGAADMKGGLAGALFAIQLLHEAGIE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 159 FPVNLVtcFEGM--EESGSLKLDELIKKEANGYFKGVdaVCISDNY----------WLGTKKPVlTY--GLRgcnyYQTI 224
Cdd:PRK08596 140 LPGDLI--FQSVigEEVGEAGTLQCCERGYDADFAVV--VDTSDLHmqgqggvitgWITVKSPQ-TFhdGTR----RQMI 210
|
250 260 270
....*....|....*....|....*....|.
gi 768801288 225 IEGpsadlhSGIFGGVVAEPMIDLMQVLGSL 255
Cdd:PRK08596 211 HAG------GGLFGASAIEKMMKIIQSLQEL 235
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
21-156 |
1.10e-07 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 54.18 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 21 SRLTKAIQIPAVSSDEslRSKvFDKAKFIseqlsqsGFHDIkMVDLGiqppPISTPNLSLPPVI-LSRF----GSDPSKK 95
Cdd:PRK08262 48 ERLSEAIRFRTISNRD--RAE-DDAAAFD-------ALHAH-LEESY----PAVHAALEREVVGgHSLLytwkGSDPSLK 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768801288 96 TVLVYGHYDVQPA--QLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASG 156
Cdd:PRK08262 113 PIVLMAHQDVVPVapGTEGDWTHPPFSGVIAD--GYVWGRGALDDKGSLVAILEAAEALLAQG 173
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
23-184 |
1.12e-07 |
|
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: 53.66 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 23 LTKA-IQIPAVSSDEslrskvfDKA-KFISEQLSQSGFHDIKMVDLGiqpppisTPNLslppviLSRFGSDPskkTVLVY 100
Cdd:cd03891 3 LAKElIRRPSVTPDD-------AGAqDLIAERLKALGFTCERLEFGG-------VKNL------WARRGTGG---PHLCF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 101 -GHYDVQPAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVtcF------EGMEES 173
Cdd:cd03891 60 aGHTDVVPPGDLEGWSSDPFSPTIKD--GMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSIS--FlitsdeEGPAID 135
|
170
....*....|..
gi 768801288 174 GSLK-LDELIKK 184
Cdd:cd03891 136 GTKKvLEWLKAR 147
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
10-143 |
1.33e-07 |
|
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: 53.79 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 10 QKIDSLKPQFFSRLTKAIQIPAVSsDESLR--------SKVFDKAKFISEQLsqsGF----HDIKMVDlgiqpppistpn 77
Cdd:cd03888 1 EEIDKYKDEILEDLKELVAIPSVR-DEATEgapfgegpRKALDKFLDLAKRL---GFktknIDNYAGY------------ 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768801288 78 lslppvilSRFGSDpsKKTVLVYGHYDVQPAQleDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLL 143
Cdd:cd03888 65 --------AEYGEG--EEVLGILGHLDVVPAG--EGWTTDPFKPVIKD--GKLYGRGTIDDKGPTI 116
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
8-170 |
1.57e-07 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 53.41 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 8 VFQKIDSL----KPQFFSRLTKAIQIPAVSSDESlrskvfDKAKFISEQLSQSGFHDIKMVDLGiqpppistpNlslppv 83
Cdd:PRK13004 2 PFKLILMLaekyKADMTRFLRDLIRIPSESGDEK------RVVKRIKEEMEKVGFDKVEIDPMG---------N------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 84 ILSRFGsdPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNL 163
Cdd:PRK13004 61 VLGYIG--HGKKLIAFDAHIDTVGIGDIKNWDFDPFEGEEDD--GRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTL 136
|
170
....*....|....
gi 768801288 164 -VT------CFEGM 170
Cdd:PRK13004 137 yVTgtvqeeDCDGL 150
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
81-160 |
3.72e-07 |
|
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: 52.27 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 81 PPVILSRFGSDPSKKTVLVYGHYDVQPAqLEDGWDTEPFKLVIDEaKGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFP 160
Cdd:cd05646 51 PVVVLTWEGSNPELPSILLNSHTDVVPV-FEEKWTHDPFSAHKDE-DGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPK 128
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
18-156 |
7.31e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 51.54 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 18 QFFSRLTKAIQIPAVSSdeslRSKVFDKAKFISEQLSQSGFHDikmVDLGIQPPPISTPNLSLppvilsRF-GSDPsKKT 96
Cdd:PRK09133 38 AARDLYKELIEINTTAS----TGSTTPAAEAMAARLKAAGFAD---ADIEVTGPYPRKGNLVA------RLrGTDP-KKP 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 97 VLVYGHYDVQPAQLEDgWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASG 156
Cdd:PRK09133 104 ILLLAHMDVVEAKRED-WTRDPFKLVEEN--GYFYGRGTSDDKADAAIWVATLIRLKREG 160
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
93-461 |
7.89e-07 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 51.04 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 93 SKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEAKgiMKGRGVTDDTGPL----LSWINVVDafkasgQEFPVN-----L 163
Cdd:PRK08588 58 GSPVLALSGHMDVVAAGDVDKWTYDPFELTEKDGK--LYGRGATDMKSGLaalvIAMIELKE------QGQLLNgtirlL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 164 VTCFEGMEESGSLKLDELikkeanGYFKGVDAVCI---SDNYwlgtkkpvLTYGLRGCNYYQTIIEGPSAdlHSGifggv 240
Cdd:PRK08588 130 ATAGEEVGELGAKQLTEK------GYADDLDALIIgepSGHG--------IVYAHKGSMDYKVTSTGKAA--HSS----- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 241 vaepmidlMQVLGslvdskgkilIDGIDEMVAPLTEkEKALYKDIEFSVEELNAATGSKTSLydkkedilmhrwrypsls 320
Cdd:PRK08588 189 --------MPELG----------VNAIDPLLEFYNE-QKEYFDSIKKHNPYLGGLTHVVTII------------------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 321 ihgvegafsaQGAKTV--IPSKVFGKFSIRTVPDMDSEKLTSLVQK---HCDAkfkslNSPNKCRTELIHDGAYWVSDPF 395
Cdd:PRK08588 232 ----------NGGEQVnsVPDEAELEFNIRTIPEYDNDQVISLLQEiinEVNQ-----NGAAQLSLDIYSNHRPVASDKD 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768801288 396 NAQFTAAKKATKLVYGVDPDFTregGSIPITltfqDAlntSVLL-----LPM---GRGD-DGAHSINEKLDISNF 461
Cdd:PRK08588 297 SKLVQLAKDVAKSYVGQDIPLS---AIPGAT----DA---SSFLkkkpdFPViifGPGNnLTAHQVDEYVEKDMY 361
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
94-159 |
1.16e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 50.85 E-value: 1.16e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768801288 94 KKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASGQEF 159
Cdd:PRK07205 75 EELLAILCHLDVVPEGDLSDWQTPPFEAVEKD--GCLFGRGTQDDKGPSMAALYAVKALLDAGVQF 138
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
94-141 |
2.57e-06 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 49.84 E-value: 2.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 768801288 94 KKTVLVYGHYDVQPAQleDGWDTEPFKLVIDEAKgiMKGRGVTDDTGP 141
Cdd:PRK07318 79 EEVLGILGHLDVVPAG--DGWDTDPYEPVIKDGK--IYARGTSDDKGP 122
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
22-138 |
5.74e-06 |
|
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: 48.79 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 22 RLTKAIQIPAVSSDESL------RSKVFDKakfISEQLSQSgFhdikmvdlgiqppPISTPNLSLppVILSRF------- 88
Cdd:cd05674 3 RLSGAVQIPTVSFDDMPpidedeRWDAFYK---FHDYLEKT-F-------------PLVHKTLKV--EVVNEYgllytwe 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 768801288 89 GSDPSKKTVLVYGHYDVQPAQ--LEDGWDTEPFKLVIDEakGIMKGRGVTDD 138
Cdd:cd05674 64 GSDPSLKPLLLMAHQDVVPVNpeTEDQWTHPPFSGHYDG--GYIWGRGALDD 113
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
97-185 |
1.65e-05 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 47.08 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 97 VLVYGHYDVQPAQLEDgWDTEPFKLVIDEAKGImkGRGVTDDTGPLLSwinVVDAFKASGQEfPVN--LVTCFEGMEESG 174
Cdd:PRK08554 66 LLFMAHFDVVPVNPEE-WNTEPFKLTVKGDKAY--GRGSADDKGNVAS---VMLALKELSKE-PLNgkVIFAFTGDEEIG 138
|
90
....*....|....
gi 768801288 175 ---SLKLDELIKKE 185
Cdd:PRK08554 139 gamAMHIAEKLREE 152
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
23-170 |
2.66e-05 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 46.26 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 23 LTKAIQIPAVSSDESlrskvfDKAKFISEQLSQSGFHDIKMVDLGiqpppistpNlslppvILSRFGSdpSKKTVLVYGH 102
Cdd:cd05649 4 LRDLIQIPSESGEEK------GVVERIEEEMEKLGFDEVEIDPMG---------N------VIGYIGG--GKKKILFDGH 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768801288 103 YDVQPAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFK------ASGQEFPVNLV--TCFEGM 170
Cdd:cd05649 61 IDTVGIGNIDNWKFDPYEGYETD--GKIYGRGTSDQKGGLASMVYAAKIMKdlglrdFAYTILVAGTVqeEDCDGV 134
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
89-175 |
3.58e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 46.00 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 89 GSDPSKKTVLVYGHYDVQPAQLEDgWDTEPFKLVIdeAKGIMKGRGVTD--DT-GPLLSwinVVDAFKASGQEFPVNLVT 165
Cdd:PRK07906 60 GADPSRPALLVHGHLDVVPAEAAD-WSVHPFSGEI--RDGYVWGRGAVDmkDMdAMMLA---VVRHLARTGRRPPRDLVF 133
|
90
....*....|
gi 768801288 166 CFEGMEESGS 175
Cdd:PRK07906 134 AFVADEEAGG 143
|
|
| PRK06915 |
PRK06915 |
peptidase; |
1-174 |
5.76e-05 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 45.45 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 1 MSHSLTSVFQKIDSLKPQFFSRLTKAIQIPAVSSDESLRSKVfdkakfISEQLSQSGFhDIKMVDLGI----QPPPISTP 76
Cdd:PRK06915 1 MEQLKKQICDYIESHEEEAVKLLKRLIQEKSVSGDESGAQAI------VIEKLRELGL-DLDIWEPSFkklkDHPYFVSP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 77 NLSL--PPVILSRFGSDPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIdeAKGIMKGRGVTDDTGPLLSWINVVDAFKA 154
Cdd:PRK06915 74 RTSFsdSPNIVATLKGSGGGKSMILNGHIDVVPEGDVNQWDHHPYSGEV--IGGRIYGRGTTDMKGGNVALLLAMEALIE 151
|
170 180
....*....|....*....|..
gi 768801288 155 SGQEFPVNLVtcFEGM--EESG 174
Cdd:PRK06915 152 SGIELKGDVI--FQSVieEESG 171
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
89-156 |
9.65e-05 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 44.61 E-value: 9.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768801288 89 GSDPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASG 156
Cdd:cd03895 69 PRGETGRSLILNGHIDVVPEGPVELWTRPPFEATIVD--GWMYGRGAGDMKAGLAANLFALDALRAAG 134
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
91-196 |
1.53e-04 |
|
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: 43.73 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 91 DPSKKTVLVYGHYD-VQPaqlEDGWDTEPFKlvIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEG 169
Cdd:cd03885 57 GTGGKRVLLIGHMDtVFP---EGTLAFRPFT--VDG--DRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNS 129
|
90 100
....*....|....*....|....*..
gi 768801288 170 MEESGSLKLDELIKKEAngyfKGVDAV 196
Cdd:cd03885 130 DEEIGSPGSRELIEEEA----KGADYV 152
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
81-174 |
1.98e-04 |
|
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: 43.63 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 81 PPVILSRFGSDPSKKTVLVYGHYDVQPAQLEDgWDTEPFKLVIDEaKGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFP 160
Cdd:TIGR01880 58 PVVVLTWPGSNPELPSILLNSHTDVVPVFREH-WTHPPFSAFKDE-DGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFK 135
|
90
....*....|....
gi 768801288 161 VNLVTCFEGMEESG 174
Cdd:TIGR01880 136 RTIHISFVPDEEIG 149
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
23-257 |
2.62e-04 |
|
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: 42.96 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 23 LTKAIQIPAVSSDESLRskVFDkakFISEQLSQSGF-HDIkmvdlgIQPPPISTPNLslppviLSRFGSDPSKKTVLVyG 101
Cdd:cd03894 3 LARLVAFDTVSRNSNLA--LIE---YVADYLAALGVkSRR------VPVPEGGKANL------LATLGPGGEGGLLLS-G 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 102 HYDVQPAqleDG--WDTEPFKLVIDEAKgiMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEgmEESGSLKLD 179
Cdd:cd03894 65 HTDVVPV---DGqkWSSDPFTLTERDGR--LYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYD--EEVGCLGVR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 180 ELIkkEANGYFKGVDAVCIsdnywLG--TK-KPVLtyGLRGCNYYQTIIEGPSAdlHS-GIFGGVVA-EPMIDLMQVLGS 254
Cdd:cd03894 138 HLI--AALAARGGRPDAAI-----VGepTSlQPVV--AHKGIASYRIRVRGRAA--HSsLPPLGVNAiEAAARLIGKLRE 206
|
...
gi 768801288 255 LVD 257
Cdd:cd03894 207 LAD 209
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
47-137 |
3.08e-04 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 42.77 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 47 KFISEQLSQSGFHDIKMVDLGiqpppisTPNLslppvILSRFGSDPskktVLVY-GHYDVQPAQLEDGWDTEPFKLVIDE 125
Cdd:PRK13009 26 DLLAERLEALGFTCERMDFGD-------VKNL-----WARRGTEGP----HLCFaGHTDVVPPGDLEAWTSPPFEPTIRD 89
|
90
....*....|..
gi 768801288 126 akGIMKGRGVTD 137
Cdd:PRK13009 90 --GMLYGRGAAD 99
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
83-183 |
4.65e-04 |
|
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: 42.45 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 83 VILSRFGSDPSKKTVLVYGHYDVQPAQLEDgWDTEPFKLVIDEAKgiMKGRGVTDDTGPLLSwinVVDAFKASGQEFPV- 161
Cdd:cd08012 67 IIVEYPGTVDGKTVSFVGSHMDVVTANPET-WEFDPFSLSIDGDK--LYGRGTTDCLGHVAL---VTELFRQLATEKPAl 140
|
90 100
....*....|....*....|....*..
gi 768801288 162 --NLVTCFEGMEESGSLK---LDELIK 183
Cdd:cd08012 141 krTVVAVFIANEENSEIPgvgVDALVK 167
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
101-176 |
4.95e-04 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 42.48 E-value: 4.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768801288 101 GHYDVQPAQlEDGWDTEPFKLVIDEAKgiMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEgmEESGSL 176
Cdd:PRK07522 71 GHTDVVPVD-GQAWTSDPFRLTERDGR--LYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYD--EEVGCL 141
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
91-156 |
8.76e-04 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 41.53 E-value: 8.76e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768801288 91 DPSKKT---VLVYGHYDVQPAQLEDGWDTEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASG 156
Cdd:PRK06837 91 RPAGKTgrsLILQGHIDVVPEGPLDLWSRPPFDPVIVD--GWMYGRGAADMKAGLAAMLFALDALRAAG 157
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
23-177 |
2.10e-03 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 40.16 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768801288 23 LTKAIQIPAVSSDESlrskvfDKAKFISEQLSQSGFHDIKMVDLGiqpppistpNlslppvILSRFGSDPSKKTVLVYGH 102
Cdd:cd03896 4 AIELGEIPAPTFREG------ARADLVAEWMADLGLGDVERDGRG---------N------VVGRLRGTGGGPALLFSAH 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768801288 103 YD-VQPAQledgwdtEPFKLVIDEakGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLV---TCfeGMEESGSLK 177
Cdd:cd03896 63 LDtVFPGD-------TPATVRHEG--GRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVfaaNV--GEEGLGDLR 130
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
300-371 |
2.16e-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: 37.71 E-value: 2.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768801288 300 TSLYDKKEDILmHRWRYPSLSIHGVEGAFsaqgAKTVIPSKVFGKFSIRTVPDMDSEKLTSLVQKHCDAKFK 371
Cdd:pfam07687 38 AELPAEYGDIG-FDFPRTTLNITGIEGGT----ATNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEKELP 104
|
|
| |
