|
Name |
Accession |
Description |
Interval |
E-value |
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
10-479 |
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: 764.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 10 VFTKIDELKPEFIGMLSKAIAIPAVSSDESLRPRVVEKAHFLADHLKKLGFaDIQLKELGTQPPPvSDPNLQLPPIVLAR 89
Cdd:cd05676 1 VFKYIDEHQDEFIERLREAVAIQSVSADPEKRPELIRMMEWAAERLEKLGF-KVELVDIGTQTLP-DGEELPLPPVLLGR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 90 YGNDPAKKNVLVYGHYDVQPAKLEDGWDSEPFELVvdEKKQVLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITCF 169
Cdd:cd05676 79 LGSDPSKKTVLIYGHLDVQPAKLEDGWDTDPFELT--EKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 170 EGMEESGSLGLEELIGAEKDKYFKGVDAVCISDNYWLGTRKPVLTYGLRGCNYYQVTIEGPGADLHSGMFGGIIAEPMID 249
Cdd:cd05676 157 EGMEESGSEGLDELIEARKDTFFSDVDYVCISDNYWLGKKKPCLTYGLRGICYFFIEVEGPNKDLHSGVFGGSVHEPMTD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 250 LVQVMSTLVDSQGKILIEGVDAMVAKETEKEQELYKTIDFSVEELNAASGSETALYTKKEDILKHRWRYPSLSIHGVEGA 329
Cdd:cd05676 237 LIALMSSLVDSDGKILIPGIYDAVAPLTEEEWELYEKIDFDMEEYREDIGVRRLLYDNKEELLMHRWRYPSLSIHGIEGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 330 FYSQGAKTVIPAKVIGKFSIRTVPDIDSEKLTQIVVDHCHAAFKKLNSPNRCKAELIHDGNYWVSDPFNAQFQAAAKATK 409
Cdd:cd05676 317 FSGPGAKTVIPAKVIGKFSIRLVPNMDPEVVEKQVTDYLEKVFAELKSPNKLKVYMGHGGKPWVADPDHPNYKAARKATK 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 410 DVYGVEPDYTREGGSIPITLTFEEQLKTSVLLLPMGRGDDGAHSINEKLDISNFVNGMKLMAAYLHYYAE 479
Cdd:cd05676 397 RVFGVEPDLTREGGSIPITLTFQEATGKNVMLLPIGAADDGAHSQNEKINRRNYIEGTKLLAAYFHELSK 466
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
25-474 |
1.09e-137 |
|
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: 403.25 E-value: 1.09e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 25 LSKAIAIPAVSSDESLRPRVVEKAHFLADHLKKLGFADIQLkelgtqpppvsdPNLQLPPIVLARYGNDPAKKNVLVYGH 104
Cdd:cd03893 4 LAELVAIPSVSAQPDRREELRRAAEWLADLLRRLGFTVEIV------------DTSNGAPVVFAEFPGAPGAPTVLLYGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 105 YDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITCFEGMEESGSLGLEELI 184
Cdd:cd03893 72 YDVQPAGDEDGWDSDPFELTERDGR--LYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEESGSPSLDQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 185 GAEKDkyFKGVDAVCISDNYWLGTRKPVLTYGLRGCNYYQVTIEGPGADLHSGMFGGIIAEPMIDLVQVMSTLVDSQGKI 264
Cdd:cd03893 150 EAHRD--LLAADAIVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLDHDLHSGLYGGVVPDPMTALAQLLASLRDETGRI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 265 LIEGVDAMVAKETEKEQELYKTIDFSVEElnaasgsetaLYTKKEDILKHRWRYPSLSIHGVEGAFYSQGAKTVIPAKVI 344
Cdd:cd03893 228 LVPGLYDAVRELPEEEFRLDAGVLEEVEI----------IGGTTGSVAERLWTRPALTVLGIDGGFPGEGSKTVIPPRAR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 345 GKFSIRTVPDIDSEKLTQIVVDHCHAAFKklnSPNRCKAELIHDGNYWVSDPFNAQFQAAAKATKDVYGVEPDYTREGGS 424
Cdd:cd03893 298 AKISIRLVPGQDPEEASRLLEAHLEKHAP---SGAKVTVSYVEGGMPWRSDPSDPAYQAAKDALRTAYGVEPPLTREGGS 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1891256837 425 IPITLTFEEQLKTSVLLLPMGRGDDGAHSINEKLDISNFVNGMKLMAAYL 474
Cdd:cd03893 375 IPFISVLQEFPQAPVLLIGVGDPDDNAHSPNESLRLGNYKEGTQAEAALL 424
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
31-477 |
1.68e-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: 333.89 E-value: 1.68e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 31 IPAVSSDESLRPRVVEKAHFLADHLKKLGFADIQLKELGTQPppvsdpnlqlppIVLARYGNDPAKKNVLVYGHYDVQPA 110
Cdd:cd05680 10 IPSVSADPAHKGDVRRAAEWLADKLTEAGFEHTEVLPTGGHP------------LVYAEWLGAPGAPTVLVYGHYDVQPP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 111 KLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITCFEGMEESGSLGLEELIGAEKDK 190
Cdd:cd05680 78 DPLELWTSPPFEPVVRDGR--LYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIGSPSLPAFLEENAER 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 191 yFKGvDAVCISDNYWLGTRKPVLTYGLRGCNYYQVTIEGPGADLHSGMFGGIIAEPMIDLVQVMSTLVDSQGKILIEGVD 270
Cdd:cd05680 156 -LAA-DVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNRDLHSGSYGGAVPNPANALARLLASLHDEDGRVAIPGFY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 271 AMVAKETEKEQELYKTIDFSVEELNAASGSETAL----YTKKEdilkHRWRYPSLSIHGVEGAFYSQGAKTVIPAKVIGK 346
Cdd:cd05680 234 DDVRPLTDAEREAWAALPFDEAAFKASLGVPALGgeagYTTLE----RLWARPTLDVNGIWGGYQGEGSKTVIPSKAHAK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 347 FSIRTVPDIDSEKLTQIVVDHCHAafkklNSPNRCKAELI--HDGNYWVSDPFNAQFQAAAKATKDVYGVEPDYTREGGS 424
Cdd:cd05680 310 ISMRLVPGQDPDAIADLLEAHLRA-----HAPPGVTLSVKplHGGRPYLVPTDHPALQAAERALEEAFGKPPVFVREGGS 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1891256837 425 IPITLTFEEQLKTSVLLLPMGRGDDGAHSINEKLDISNFVNGMKLMAAYLHYY 477
Cdd:cd05680 385 IPIVALFEKVLGIPTVLMGFGLPDDAIHAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
25-466 |
4.01e-100 |
|
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: 307.35 E-value: 4.01e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 25 LSKAIAIPAVSSD------ESLRprvvEKAHFLADHLKKLGFADIQLkelgtqPPPVSDPNlqlpPIVLARY---GNDPA 95
Cdd:cd05677 5 LSEFIAFQTVSQSpttenaEDSR----RCAIFLRQLFKKLGATNCLL------LPSGPGTN----PIVLATFsgnSSDAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 96 KKNVLVYGHYDVQPAKLEDGWDSEPFELVVDEKkqVLRARGSSDDTGPLTGWLHVVqAHQAAGVELPVNLITCFEGMEES 175
Cdd:cd05677 71 RKRILFYGHYDVIPAGETDGWDTDPFTLTCENG--YLYGRGVSDNKGPLLAAIYAV-AELFQEGELDNDVVFLIEGEEES 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 176 GSLGLEELIgaEKDKYFKG-VDAVCISDNYWLGTRKPVLTYGLRGCNYYQVTIEGPGADLHSGMFGGIIAEPMIDLVQVM 254
Cdd:cd05677 148 GSPGFKEVL--RKNKELIGdIDWILLSNSYWLDDNIPCLNYGLRGVIHATIVVSSDKPDLHSGVDGGVLREPTADLIKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 255 STLVDSQGKILIEGVDAMVAKETEKEQELYKTIdfsveelnaASGSETALYTKKEDiLKHRWRYPSLSIHGVEgaFYSQG 334
Cdd:cd05677 226 SKLQDPDGRILIPHFYDPVKPLTEAERARFTAI---------AETALIHEDTTVDS-LIAKWRKPSLTVHTVK--VSGPG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 335 AKTVIPAKVIGKFSIRTVPDIDSEKLTQIVVDHCHAAFKKLNSPNRCKAELIHDGNYWVSDPFNAQFQAAAKATKDVYGV 414
Cdd:cd05677 294 NTTVIPKSASASVSIRLVPDQDLDVIKQDLTDYIQSCFAELKSQNHLDIEVLNEAEPWLGDPDNPAYQILREAVTAAWGV 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1891256837 415 EPDYTREGGSIPITLTFEEQLKTSVLLLPMGRGDDGAHSINEKLDISNFVNG 466
Cdd:cd05677 374 EPLYIREGGSIPTIRFLEKEFNAPAVQLPCGQSSDNAHLDNERLRIKNLYKM 425
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
25-479 |
2.54e-92 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 287.80 E-value: 2.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 25 LSKAIAIPAVSSDESLRPRVVEKAHFLADHLKKLGFADIQLKELGTQPppvsdpnlqlppIVLARYGNDPAKKNVLVYGH 104
Cdd:PRK08201 20 LKEFLRIPSISALSEHKEDVRKAAEWLAGALEKAGLEHVEIMETAGHP------------IVYADWLHAPGKPTVLIYGH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 105 YDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITCFEGMEESGSLGLEELI 184
Cdd:PRK08201 88 YDVQPVDPLNLWETPPFEPTIRDGK--LYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEEIGSPNLDSFV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 185 GAEKDKYfkGVDAVCISDNYWLGTRKPVLTYGLRGCNYYQVTIEGPGADLHSGMFGGIIAEPMIDLVQVMSTLVDSQGKI 264
Cdd:PRK08201 166 EEEKDKL--AADVVLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLHSGLYGGAVPNALHALVQLLASLHDEHGTV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 265 LIEGVDAMVAKETEKEQELYKTIDFSVEELNAASGSETALYTKKEDILKHRWRYPSLSIHGVEGAFYSQGAKTVIPAKVI 344
Cdd:PRK08201 244 AVEGFYDGVRPLTPEEREEFAALGFDEEKLKRELGVDELFGEEGYTALERTWARPTLELNGVYGGFQGEGTKTVIPAEAH 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 345 GKFSIRTVPDIDSEKLTQIVVDHCHAafkklNSPNRCKAELI-HDGNY-WVSDPFNAQFQAAAKATKDVYGVEPDYTREG 422
Cdd:PRK08201 324 AKITCRLVPDQDPQEILDLIEAHLQA-----HTPAGVRVTIRrFDKGPaFVAPIDHPAIQAAARAYEAVYGTEAAFTRMG 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1891256837 423 GSIPITLTFEEQLKTSVLLLPMGRGDDGAHSINEKLDISNFVNGMKLMAAYLHYYAE 479
Cdd:PRK08201 399 GSIPVVETFSSQLHIPIVLMGFGLPSENFHAPNEHFHLENFDKGLRTLVEYWHQLAE 455
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
3-468 |
5.41e-76 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 245.97 E-value: 5.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 3 STRAFDKVFTKIDELKPEFIGMLSKAIAIPAVSSDESLRPRVVEKAHFLADHLKKLGFadiqlkELGTQPPPvsdpnlqL 82
Cdd:PRK09104 1 SMADLDPVLDHIDANLDASLERLFALLRIPSISTDPAYAADCRKAADWLVADLASLGF------EASVRDTP-------G 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 83 PPIVLARY-GNDPAKKNVLVYGHYDVQPAKLEDGWDSEPFELVVDE---KKQVLRARGSSDDTGPLTGWLHVVQAHQAAG 158
Cdd:PRK09104 68 HPMVVAHHeGPTGDAPHVLFYGHYDVQPVDPLDLWESPPFEPRIKEtpdGRKVIVARGASDDKGQLMTFVEACRAWKAVT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 159 VELPVNLITCFEGMEESGSLGLEELIGAEKDKyFKGvDAVCISDNYWLGTRKPVLTYGLRGCNYYQVTIEGPGADLHSGM 238
Cdd:PRK09104 148 GSLPVRVTILFEGEEESGSPSLVPFLEANAEE-LKA-DVALVCDTGMWDRETPAITTSLRGLVGEEVTITAADRDLHSGL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 239 FGGIIAEPMIDLVQVMSTLVDSQGKILIEGVDAMVAKETEKEQELYKTIDFSVEE------LNAASGSetalytKKEDIL 312
Cdd:PRK09104 226 FGGAAANPIRVLTRILAGLHDETGRVTLPGFYDGVEELPPEILAQWKALGFTAEAflgpvgLSIPAGE------KGRSVL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 313 KHRWRYPSLSIHGVEGAFYSQGAKTVIPAKVIGKFSIRTVPDIDSEKLTQIVVDHCHAAFkklnsPNRCKAELI-HDGNY 391
Cdd:PRK09104 300 EQIWSRPTCEINGIWGGYTGEGFKTVIPAEASAKVSFRLVGGQDPAKIREAFRAYVRARL-----PADCSVEFHdHGGSP 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1891256837 392 WVSDPFN-AQFQAAAKATKDVYGVEPDYTREGGSIPITLTFEEQLKTSVLLLPMGRGDDGAHSINEKLDISNFVNGMK 468
Cdd:PRK09104 375 AIALPYDsPALAAAKAALSDEWGKPAVLIGSGGSIPIVGDFKRILGMDSLLVGFGLDDDRIHSPNEKYDLESFHKGIR 452
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
25-474 |
8.88e-70 |
|
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: 228.38 E-value: 8.88e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 25 LSKAIAIPAVSSDESlrpRVVEKAHFLADHLKKLGFADIQLKELGTqpppvsdpnlqlpPIVLARYGNDpAKKNVLVYGH 104
Cdd:cd05681 5 LRDLLKIPSVSAQGR---GIPETADFLKEFLRRLGAEVEIFETDGN-------------PIVYAEFNSG-DAKTLLFYNH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 105 YDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITCFEGMEESGSLGLEELI 184
Cdd:cd05681 68 YDVQPAEPLELWTSDPFELTIRNGK--LYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPNLEKFV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 185 GAEKDKYFkgVDAvCIsdnyW-LGTR----KPVLTYGLRGCNYYQVTIEGPGADLHSgMFGGIIAEPMIDLVQVMSTLVD 259
Cdd:cd05681 146 AEHADLLK--ADG-CI----WeGGGKnpkgRPQISLGVKGIVYVELRVKTADFDLHS-SYGAIVENPAWRLVQALNSLRD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 260 SQGKILIEGVDAMVAKETEKEQELYKTIDFSVEELNAASGSETALYTKKEDILKHRWRYPSLSIHGVEGAFYSQGAKTVI 339
Cdd:cd05681 218 EDGRVLIPGFYDDVRPLSEAERALIDTYDFDPEELRKTYGLKRPLQVEGKDPLRALFTEPTCNINGIYSGYTGEGSKTIL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 340 PAKVIGKFSIRTVPDIDSEKLTQIVVDHchaafkkLNSPNRCKAELIHDGNY--WVSDPFNAQFQAAAKATKDVYGVEPD 417
Cdd:cd05681 298 PSEAFAKLDFRLVPDQDPAKILSLLRKH-------LDKNGFDDIEIHDLLGEkpFRTDPDAPFVQAVIESAKEVYGQDPI 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1891256837 418 -YTREGGSIPITlTFEEQLKTSVLLLPMGRGDDGAHSINEKLDISNFVNGMKLMAAYL 474
Cdd:cd05681 371 vLPNSAGTGPMY-PFYDALEVPVVAIGVGNAGSNAHAPNENIRIADYYKGIEHTEELL 427
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
8-479 |
7.65e-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: 219.76 E-value: 7.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 8 DKVFTKIDELKPEFIGMLSKAIAIPAVSSDESlrprvvEKAHFLADHLKKLGFadiqlkELGTQPPPVSDPNlqlppiVL 87
Cdd:COG0624 1 AAVLAAIDAHLDEALELLRELVRIPSVSGEEA------AAAELLAELLEALGF------EVERLEVPPGRPN------LV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 88 ARYGNDPAKKNVLVYGHYDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLIT 167
Cdd:COG0624 63 ARRPGDGGGPTLLLYGHLDVVPPGDLELWTSDPFEPTIEDGR--LYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 168 CFEGMEESGSLGLEELIGAEKDKYfkGVDAVCISDnywlGTRKPVLTYGLRGCNYYQVTIEGPGAdlHSGMFGgiiaepm 247
Cdd:COG0624 141 LFTGDEEVGSPGARALVEELAEGL--KADAAIVGE----PTGVPTIVTGHKGSLRFELTVRGKAA--HSSRPE------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 248 idlvqvmstlvdsqgkiliEGVDAMvaketekeQELYKTIDfSVEELNAASGSETALYtkkedilkhrwrYPSLSIHGVE 327
Cdd:COG0624 206 -------------------LGVNAI--------EALARALA-ALRDLEFDGRADPLFG------------RTTLNVTGIE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 328 GafysqGAKT-VIPAKVIGKFSIRTVPDIDSEKLTQIVvdhcHAAFKKLNSPNRCKAELIHDGNY-WVSDPFNAQFQAAA 405
Cdd:COG0624 246 G-----GTAVnVIPDEAEAKVDIRLLPGEDPEEVLAAL----RALLAAAAPGVEVEVEVLGDGRPpFETPPDSPLVAAAR 316
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1891256837 406 KATKDVYGVEPDYTREGGSIPITLtFEEQLKTSVLLLPMGRGdDGAHSINEKLDISNFVNGMKLMAAYLHYYAE 479
Cdd:COG0624 317 AAIREVTGKEPVLSGVGGGTDARF-FAEALGIPTVVFGPGDG-AGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
8-480 |
1.82e-55 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 191.27 E-value: 1.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 8 DKVFTKIDELKPEFIGMLSKAIAIPAVSSDESLRPRVVEKAHFLADHLKKLGFADIQLKELGTQPPpvsdpnlqlppiVL 87
Cdd:PRK07907 7 DDLRARVAELLPRVRADLEELVRIPSVAADPFRREEVARSAEWVADLLREAGFDDVRVVSADGAPA------------VI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 88 ARYGNDPAKKNVLVYGHYDVQPAKLEDGWDSEPFELVvdEKKQVLRARGSSDDTGpltgwlHVVqAHQAA----GVELPV 163
Cdd:PRK07907 75 GTRPAPPGAPTVLLYAHHDVQPPGDPDAWDSPPFELT--ERDGRLYGRGAADDKG------GIA-MHLAAlralGGDLPV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 164 NLITCFEGMEESGSLGLEELIGAEKDKYFKGVDAVCISDNYWLGTrkPVLTYGLRGCNYYQVTIEGPGADLHSGMFGGII 243
Cdd:PRK07907 146 GVTVFVEGEEEMGSPSLERLLAEHPDLLAADVIVIADSGNWSVGV--PALTTSLRGNADVVVTVRTLEHAVHSGQFGGAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 244 AEPMIDLVQVMSTLVDSQGKILIEGVDAmvaketekeQELYKTIDFSVEELNAASG-----SETALYTKKEDIlkhrWRY 318
Cdd:PRK07907 224 PDALTALVRLLATLHDEDGNVAVDGLDA---------TEPWLGVDYDEERFRADAGvldgvELIGTGSVADRL----WAK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 319 PSLSI-----HGVEGAFysqgakTVIPAKVIGKFSIRTVPDIDSEKLTQIVVDHCHAafkklNSP--NRCKAELIHDGNY 391
Cdd:PRK07907 291 PAITVigidaPPVAGAS------NALPPSARARLSLRVAPGQDAAEAQDALVAHLEA-----HAPwgAHVTVERGDAGQP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 392 WVSDPFNAQFQAAAKATKDVYGVEPDYTREGGSIPITLTFEEQLKTSVLLLpMGRGDDG--AHSINEKLDISNFVNGMKL 469
Cdd:PRK07907 360 FAADASGPAYDAARAAMREAWGKDPVDMGMGGSIPFIAELQEAFPQAEILV-TGVEDPKtrAHSPNESVHLGELERAAVA 438
|
490
....*....|.
gi 1891256837 470 MAAYLHYYAES 480
Cdd:PRK07907 439 EALLLARLAAA 449
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
46-479 |
6.19e-54 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 186.88 E-value: 6.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 46 EKAHFLADHLKKLGfadIQLKELGTQPPPVSdpnlqlppivlarYG--NDPAKKNVLVYGHYDVQPAKLEDGWDSEPFEL 123
Cdd:PRK06446 26 ETANYLKDTMEKLG---IKANIERTKGHPVV-------------YGeiNVGAKKTLLIYNHYDVQPVDPLSEWKRDPFSA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 124 VVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGvELPVNLITCFEGMEESGSLGLEELIGAEKDKyFKGvDAVcISDN 203
Cdd:PRK06446 90 TIENGR--IYARGASDNKGTLMARLFAIKHLIDKH-KLNVNVKFLYEGEEEIGSPNLEDFIEKNKNK-LKA-DSV-IMEG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 204 YWLGTR-KPVLTYGLRGCNYYQVTIEGPGADLHSgMFGGIIAEPMIDLVQVMSTLVDSQGKILIEGVDAMVAKETEKEQE 282
Cdd:PRK06446 164 AGLDPKgRPQIVLGVKGLLYVELVLRTGTKDLHS-SNAPIVRNPAWDLVKLLSTLVDGEGRVLIPGFYDDVRELTEEERE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 283 LYKTIDFSVEELNAASGSETALYTKKEDILKHRWRYPSLSIHGVEGAFYSQGAKTVIPAKVIGKFSIRTVPDIDSEKLTQ 362
Cdd:PRK06446 243 LLKKYDIDVEELRKALGFKELKYSDREKIAEALLTEPTCNIDGFYSGYTGKGSKTIVPSRAFAKLDFRLVPNQDPYKIFE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 363 IVVDHChaafkklnSPNRCKAELI-HDGNYWVSDPFNAQF-QAAAKATKDVYGVEPDYT-REGGSIPITLtFEEQLKTSV 439
Cdd:PRK06446 323 LLKKHL--------QKVGFNGEIIvHGFEYPVRTSVNSKVvKAMIESAKRVYGTEPVVIpNSAGTQPMGL-FVYKLGIRD 393
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1891256837 440 LLLPMGRGDDG--AHSINEKLDISNFVNGMKLMAAYLHYYAE 479
Cdd:PRK06446 394 IVSAIGVGGYYsnAHAPNENIRIDDYYKAIKHTEEFLKLYST 435
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
29-474 |
2.88e-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: 169.97 E-value: 2.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 29 IAIPAVSSDESLRPRVVEkahFLADHLKKLGFaDIQLKELGTQPppvsdpnlqlppIVLARYGNDPAKKNVLVYGHYDVQ 108
Cdd:cd05678 9 VSIPNDATDEEEMRKNVD---WLEQAFRKRGF-KTSQLPTSGLP------------LLLAEKPISDARKTVLFYMHLDGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 109 PA-----------------KLEDG-W---DSEPFELVVDEKKQVLrARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLIT 167
Cdd:cd05678 73 PVdpskwdqkspytpvlkrKDAAGnWeeiNWDAIFSNLDPEWRVF-ARAAADDKGPIMMMLAALDALKAGGIAPKFNVKI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 168 CFEGMEESGSLGLEELIGAEKDKYfkGVDAVCISDNYWLGTRKPVLTYGLRGCNYYQVTIEGPGADLHSGMFGGIIAEPM 247
Cdd:cd05678 152 ILDSEEEKGSPSLPKAVKEYKELL--AADALIIMDGPAHATNKPTLTFGCRGIATATLTTYGAKVPQHSGHYGNYAPNPA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 248 IDLVQVMSTLVDSQGKILIEGVDAMVaKETEKEQELYKTIDFSVEELNAASG---SETALYTKKEDIlkhrwRYPSLSIH 324
Cdd:cd05678 230 FRLSSLLASMKDDTGKVTIPGFYDGI-SIDEETQKILAAVPDDEESINKRLGiaqTDKVGRNYQEAL-----QYPSLNVR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 325 GVEGAFYSQGAKTVIPAKVIGKFSIRTVPDIDSEKLTQIVVDHCHAAFKKLNSPNRCKAE-LIHD---------GNYWVS 394
Cdd:cd05678 304 GMESGWKGDKVRTIIPEIAEAEIDIRLVPESDGPYLLDLVKAHIEKQGYFVTDRAPTDEErLAHDkiakftyrnGADAFR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 395 DPFNAQF-QAAAKATKDVYGVEPDYTR-EGGSIPITlTFEEQLKTSVLLLPMGRGDDGAHSINEKLDISNFVNGMKLMAA 472
Cdd:cd05678 384 TDINSPIgNWLRKALTDEFGEEPIQIRmMGGTVPIA-PFVNVLDIPAIIVPMVNMDNNQHSPNENLRIGNIRTGIRTCYA 462
|
..
gi 1891256837 473 YL 474
Cdd:cd05678 463 IL 464
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
100-474 |
8.79e-41 |
|
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: 8.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 100 LVYGHYDVQPAKLEDGWdsePFELVVDEKkqvLRARGSSDDTGPLTGWLHVVQAHQAAGVeLPVNLITCFEGMEESGSLG 179
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTEDGK---LYGRGHDDMKGGLLAALEALRALKEEGL-KKGTVKLLFQPDEEGGMGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 180 LEELI--GAEKDKYFKGVDAVCISD-NYWLGTRKPVLTYGLRGCNYYQVTIEGPGAdlHSGMFgGIIAEPMIDLVQVMST 256
Cdd:pfam01546 74 ARALIedGLLEREKVDAVFGLHIGEpTLLEGGIAIGVVTGHRGSLRFRVTVKGKGG--HASTP-HLGVNAIVAAARLILA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 257 LVDsqgkiliegvdaMVAKETEKEQELYKTIdfsveelnaasgsetalytkkedilkhrwrypsLSIHGVEGAFysqgak 336
Cdd:pfam01546 151 LQD------------IVSRNVDPLDPAVVTV---------------------------------GNITGIPGGV------ 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 337 TVIPAKVIGKFSIRTVPDIDSEKLTQIVVDHCHAAFKKLNSpnRCKAELIHDGNYWVSDPfNAQFQAAAKATKDVYGVEP 416
Cdd:pfam01546 180 NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGV--KVEVEYVEGGAPPLVND-SPLVAALREAAKELFGLKV 256
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1891256837 417 DytREGGSIPITLTFE---EQLKTSVLLLpmGRGDDGAHSINEKLDISNFVNGMKLMAAYL 474
Cdd:pfam01546 257 E--LIVSGSMGGTDAAfflLGVPPTVVFF--GPGSGLAHSPNEYVDLDDLEKGAKVLARLL 313
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
25-479 |
3.82e-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: 119.36 E-value: 3.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 25 LSKAIAIPAVS---SDESLRPRVVEKA-HFLADHLKKLGFADIQLkELgtqpppVSDPNLqlPPIVLARY-GNDPAKKNV 99
Cdd:cd05682 6 LSDYIRIPNQSplfDPEWATNGLLEKAaNLIADWVKAQNIKGAKV-EV------VELEGR--TPLLFVEIpGTEQDDDTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 100 LVYGHYDVQPAKleDGWDSE--PFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITcFEGMEESGS 177
Cdd:cd05682 77 LLYGHMDKQPPF--TGWDEGlgPTKPVIRGDK--LYGRGGADDGYAIFASLTAIKALQEQGIPHPRCVVL-IEACEESGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 178 LGLEELIGAEKDKyFKGVD-AVCI---SDNY---WLgtrkpvlTYGLRGCNYYQVTIEGPGADLHSGMFGGIIAEPMIDL 250
Cdd:cd05682 152 ADLPFYLDKLKER-IGNVDlVVCLdsgCGNYeqlWL-------TTSLRGVLGGDLTVQVLNEGVHSGDASGIVPSSFRIL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 251 VQVMSTLVDSQ-GKILIEG----VDAMVAKETEKEQE-LYKTIdfsVEELNAASGSETALYTKKEDILKHRWRyPSLSIH 324
Cdd:cd05682 224 RQLLSRIEDENtGEVKLDEqhcdIPAHRYEQAKKIAEiLGEAV---YEEFPFVSGVQPVTTDLVQLYLNRTWK-PQLSVT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 325 GVEGAFYSQGAKTVIPAKVIGKFSIRTVPDIDSEKltqivvdhCHAAFKKL---NSPNRCK--AELIHDGNYWVSDPFNA 399
Cdd:cd05682 300 GADGLPPASTAGNVLRPETTLKLSLRLPPTVDAEK--------ASAALKKLletDPPYNAKvtFKSDGAGSGWNAPLLSP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 400 QF-QAAAKATKDVYGVEPDYTREGGSIPITLTFEEQ------LKTSVLllpmgrG-DDGAHSINEKLDIsNFvnGMKLMA 471
Cdd:cd05682 372 WLaKALNEASQLFFGKPAAYQGEGGSIPFMNMLGEKfpkaqfIVTGVL------GpKSNAHGPNEFLHI-PY--TKKLTA 442
|
....*...
gi 1891256837 472 AYLHYYAE 479
Cdd:cd05682 443 CVAYVLAD 450
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
20-269 |
8.96e-22 |
|
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: 97.57 E-value: 8.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 20 EFIGMLSKAIAIPAVSSDESLRPRVVEKAH-FLADHLKKLGF-ADIqlkelgtqpppVSDPNLQLPPIVLARYGNDPAKK 97
Cdd:cd05679 5 AFLAELARRVAVPTESQEPARKPELRAYLDqEMRPRFERLGFtVHI-----------HDNPVAGRAPFLIAERIEDPSLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 98 NVLVYGHYDVQP---AKLEDGWDsePFELVVDEKKqvLRARGSSDDTGPltgwlHVV------QAHQAAGVELPVNLITC 168
Cdd:cd05679 74 TLLIYGHGDVVPgyeGRWRDGRD--PWTVTVWGER--WYGRGTADNKGQ-----HSInmaalrQVLEARGGKLGFNVKFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 169 FEGMEESGSLGLEELIGAEKDKYfkGVDAVCISDNYWLGTRKPVLTYGLRGCNYYQVTIEGPGADLHSGMFGGIIAEPMI 248
Cdd:cd05679 145 IEMGEEMGSPGLRAFCFSHREAL--KADLFIASDGPRLAADRPTMFLGSRGGLNFELRVNLREGGHHSGNWGGLLANPGI 222
|
250 260
....*....|....*....|.
gi 1891256837 249 DLVQVMSTLVDSQGKILIEGV 269
Cdd:cd05679 223 ILANAIASLVDGKGRIKLPAL 243
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
22-468 |
7.77e-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: 94.00 E-value: 7.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 22 IGMLSKAIAIPAVSSDeslRPRVVEKAHFLADHLKKLGFaDIQLKElgtqpPPVSDPNlQLPPIVLARYGNDpAKKNVLV 101
Cdd:TIGR01910 1 VELLKDLISIPSVNPP---GGNEETIANYIKDLLREFGF-STDVIE-----ITDDRLK-VLGKVVVKEPGNG-NEKSLIF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 102 YGHYDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITCFEGMEESGSLGLE 181
Cdd:TIGR01910 70 NGHYDVVPAGDLELWKTDPFKPVEKDGK--LYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 182 ELIgaeKDKYFKGVDAVCISDNywlgTRKPVLTYGLRGCNYYQVTIEGPGAdlHSGMFGgiiaepmidlvqvmstlvdsq 261
Cdd:TIGR01910 148 YLL---QRGYFKDADGVLIPEP----SGGDNIVIGHKGSIWFKLRVKGKQA--HASFPQ--------------------- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 262 gkiliEGVDAMVAketekeqeLYKTIdfsvEELNAASGSETALYTKKEDILKhrwryPSLSIHGVEGafysqGAK-TVIP 340
Cdd:TIGR01910 198 -----FGVNAIMK--------LAKLI----TELNELEEHIYARNSYGFIPGP-----ITFNPGVIKG-----GDWvNSVP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 341 AKVIGKFSIRTVPDIDSEKLTQIVVDhchaAFKKLNSPNRCKAELIHD----GNYWVSD--PFNAQFQAAAkatKDVYGV 414
Cdd:TIGR01910 251 DYCEFSIDVRIIPEENLDEVKQIIED----VVKALSKSDGWLYENEPVvkwsGPNETPPdsRLVKALEAII---KKVRGI 323
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1891256837 415 EPDYTREGGSIPITLTFEEQLKTSVLllpmGRGDDG-AHSINEKLDISNFVNGMK 468
Cdd:TIGR01910 324 EPEVLVSTGGTDARFLRKAGIPSIVY----GPGDLEtAHQVNEYISIKNLVESTK 374
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
19-268 |
5.50e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 92.29 E-value: 5.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 19 PEFIGMLSKAIAIPAVSSDESLRPrvvEKAHFLADHLKKLgfadiqLKELGTQPPPVSDPNLQLPPIVLARYGNDPAKKN 98
Cdd:PRK07079 17 GAFFADLARRVAYRTESQNPDRAP---ALRAYLTDEIAPA------LAALGFTCRIVDNPVAGGGPFLIAERIEDDALPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 99 VLVYGHYDV---QPAKLEDGWDsePFELVVDEKKqvLRARGSSDDTGPltgwlHVV------QAHQAAGVELPVNLITCF 169
Cdd:PRK07079 88 VLIYGHGDVvrgYDEQWREGLS--PWTLTEEGDR--WYGRGTADNKGQ-----HTInlaaleQVLAARGGRLGFNVKLLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 170 EGMEESGSLGLEELIGAEKDKYfkGVDAVCISDNYWLGTRKPVLTYGLRGCNYYQVTIEGPGADLHSGMFGGIIAEPMID 249
Cdd:PRK07079 159 EMGEEIGSPGLAEVCRQHREAL--AADVLIASDGPRLSAERPTLFLGSRGAVNFRLRVNLRDGAHHSGNWGGLLRNPGTV 236
|
250
....*....|....*....
gi 1891256837 250 LVQVMSTLVDSQGKILIEG 268
Cdd:PRK07079 237 LAHAIASLVDARGRIQVPG 255
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
85-232 |
2.83e-16 |
|
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: 77.09 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 85 IVLARYGNDPAKKNVLVYGHYDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVN 164
Cdd:cd18669 1 NVIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGR--LYGRGALDDKGGVAAALEALKLLKENGFKLKGT 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1891256837 165 LITCFEGMEESGSLGLEELIGAEKDKYFKGVDAVCISDNYWLGTRKPVLTYGL--------RGCNYYQVTIEGPGA 232
Cdd:cd18669 79 VVVAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTPLvdalseaaRKVFGKPQHAEGTGG 154
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
14-474 |
2.82e-15 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 77.34 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 14 IDELKPEFIGMLSKAIAIPAVSSD-ESLRprvvEKAHFLADHLKKLGFaDIQLKElgtqpPPVSDPNLQLPPIVLARYGN 92
Cdd:PRK08651 1 VEAMMFDIVEFLKDLIKIPTVNPPgENYE----EIAEFLRDTLEELGF-STEIIE-----VPNEYVKKHDGPRPNLIARR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 93 DPAKKNVLVYGHYDVQPAKleDGWDS-EPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVqahQAAGVELPVNLITCFEG 171
Cdd:PRK08651 71 GSGNPHLHFNGHYDVVPPG--EGWSVnVPFEPKVKDGK--VYGRGASDMKGGIAALLAAF---ERLDPAGDGNIELAIVP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 172 MEESGSLGLEELIgaekDKYFKGVDAVCI-----SDNYWLGTRkpvltyGL-RGcnyyQVTIEGPGAdlHSGMfggiiae 245
Cdd:PRK08651 144 DEETGGTGTGYLV----EEGKVTPDYVIVgepsgLDNICIGHR------GLvWG----VVKVYGKQA--HAST------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 246 PmidlvqvmstlvdsqgkilIEGVDA--MVAKETEKEQELYKTIdfsveelnaasgsetalyTKKEDILKHRWRYPSLSI 323
Cdd:PRK08651 201 P-------------------WLGINAfeAAAKIAERLKSSLSTI------------------KSKYEYDDERGAKPTVTL 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 324 HG--VEGafysqGAKT-VIPAKVigKFSI--RTVPDIDSEKLTQIVVDHCHAAFKKLnsPNRCKAELIHDGNYWVSDPFN 398
Cdd:PRK08651 244 GGptVEG-----GTKTnIVPGYC--AFSIdrRLIPEETAEEVRDELEALLDEVAPEL--GIEVEFEITPFSEAFVTDPDS 314
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1891256837 399 AQFQAAAKATKDVYGVEPDYTREGGSIPITLTFEEQLKTSVLllpmGRGDDG-AHSINEKLDISNFVNGMKLMAAYL 474
Cdd:PRK08651 315 ELVKALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVY----GPGELElAHAPDEYVEVKDVEKAAKVYEEVL 387
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
25-464 |
3.04e-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: 76.95 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 25 LSKAIAIPAVSSDESlrprvvEKAHFLADHLKKLGFadiqlkelGTQPPPVSD-PNLqlppivLARYGNDPAKknVLVY- 102
Cdd:cd08659 3 LQDLVQIPSVNPPEA------EVAEYLAELLAKRGY--------GIESTIVEGrGNL------VATVGGGDGP--VLLLn 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 103 GHYDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITCFEGMEESGSLGLEE 182
Cdd:cd08659 61 GHIDTVPPGDGDKWSFPPFSGRIRDGR--LYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 183 LIgaeKDKYFKGVDAVCI---SDNYwlgtrkpvLTYGLRGCNYYQVTIEGPGAdlHSGM-FGGIIA-EPMIDLVQVMSTL 257
Cdd:cd08659 139 LL---EAGYADRLDALIVgepTGLD--------VVYAHKGSLWLRVTVHGKAA--HSSMpELGVNAiYALADFLAELRTL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 258 VDSQGKiliegvdamvaketekeqelyktidfsVEELNAasgsetalytkkedilkhrwryPSLSIHGVEGafysqGAKT 337
Cdd:cd08659 206 FEELPA---------------------------HPLLGP----------------------PTLNVGVING-----GTQV 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 338 -VIPAKVIGKFSIRTVPDIDSEKLTQIVVDHCHAAFKKLNspnrckAELIHDG-NYWVSDPFNAQFQAAAKATKDVYGVE 415
Cdd:cd08659 232 nSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLT------VEVSLDGdPPFFTDPDHPLVQALQAAARALGGDP 305
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1891256837 416 P----DYTREGGSIPITLTFEeqlktsVLLLpmGRGDDG-AHSINEKLDISNFV 464
Cdd:cd08659 306 VvrpfTGTTDASYFAKDLGFP------VVVY--GPGDLAlAHQPDEYVSLEDLL 351
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
15-189 |
3.94e-15 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 76.81 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 15 DELKPEFIGMLSKAIAIPAVSSD-----EslrprvVEKAHFLADHLKKLGFADIqlKELGTQPPPVSD---PNLqlppiv 86
Cdd:PRK13983 1 DELRDEMIELLSELIAIPAVNPDfggegE------KEKAEYLESLLKEYGFDEV--ERYDAPDPRVIEgvrPNI------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 87 LARYGNDPAKKNVLVYGHYDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLI 166
Cdd:PRK13983 67 VAKIPGGDGKRTLWIISHMDVVPPGDLSLWETDPFKPVVKDGK--IYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLG 144
|
170 180
....*....|....*....|....
gi 1891256837 167 TCFEGMEESGSL-GLEELIGAEKD 189
Cdd:PRK13983 145 LAFVSDEETGSKyGIQYLLKKHPE 168
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
85-205 |
1.01e-13 |
|
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: 69.76 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 85 IVLARYGNDPAKKNVLVYGHYDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVN 164
Cdd:cd03873 1 NLIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGR--LYGRGALDDKGGVAAALEALKRLKENGFKPKGT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1891256837 165 LITCFEGMEESGSLGLEELIGAEKDKYFKGVDAVCISDNYW 205
Cdd:cd03873 79 IVVAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDATA 119
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
8-179 |
1.08e-13 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 72.76 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 8 DKVFTKIDELKPEFIGMLSKAIAIPAVSsdeslrP--RVVEKAH-FLADHLKKLGFaDIQLKELgtQPppvSDPNlqlpp 84
Cdd:PRK08596 2 SQLLEQIELRKDELLELLKTLVRFETPA------PpaRNTNEAQeFIAEFLRKLGF-SVDKWDV--YP---NDPN----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 85 IVLARYGNDPAK-KNVLVYGHYDVQPAKLEDGWDSEPFELVVdeKKQVLRARGSSDDTGPLTGWLHVVQAHQAAGVELPV 163
Cdd:PRK08596 65 VVGVKKGTESDAyKSLIINGHMDVAEVSADEAWETNPFEPTI--KDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPG 142
|
170
....*....|....*...
gi 1891256837 164 NLItcFEGM--EESGSLG 179
Cdd:PRK08596 143 DLI--FQSVigEEVGEAG 158
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
64-460 |
1.98e-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: 65.84 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 64 QLKELGTQPPPVSDPNLQLPPIVLARY-GNDPAKKNVLVYGHYDVQPAKLEDgWDSEPFELVVDEKkqVLRARGSSDDTG 142
Cdd:cd05675 32 RLAEAGIQTEIFVVESHPGRANLVARIgGTDPSAGPLLLLGHIDVVPADASD-WSVDPFSGEIKDG--YVYGRGAVDMKN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 143 PLTGWLHVVQAHQAAGVELPVNLITCFEGMEESGS-LGLEELIgAEKDKYFKGVDAvCISDNYWL------GTRKPVLTY 215
Cdd:cd05675 109 MAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGeNGAKWLV-DNHPELFDGATF-ALNEGGGGslpvgkGRRLYPIQV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 216 GLRGCNYYQVTIEGPGAdlHSGMFGgiIAEPMIDLVQVMSTLVDSQGKILI----EGVDAMVAKETEKEQELYKTIDFSV 291
Cdd:cd05675 187 AEKGIAWMKLTVRGRAG--HGSRPT--DDNAITRLAEALRRLGAHNFPVRLtdetAYFAQMAELAGGEGGALMLTAVPVL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 292 EELNAASGSETALYtkkEDILKHrwrypSLSIHGVEGAFysqgAKTVIPAKVIGKFSIRTVPDiDSEkltQIVVDHCHAA 371
Cdd:cd05675 263 DPALAKLGPSAPLL---NAMLRN-----TASPTMLDAGY----ATNVLPGRATAEVDCRILPG-QSE---EEVLDTLDKL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 372 fkkLNSPnRCKAELIHDGNYWVSDPFNAQFQAAAKATKDVYgvePDytreGGSIPITLTFEEQLKT-----------SVL 440
Cdd:cd05675 327 ---LGDP-DVSVEAVHLEPATESPLDSPLVDAMEAAVQAVD---PG----APVVPYMSPGGTDAKYfrrlgipgygfAPL 395
|
410 420
....*....|....*....|.
gi 1891256837 441 LLPMGRGD-DGAHSINEKLDI 460
Cdd:cd05675 396 FLPPELDYtGLFHGVDERVPV 416
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
22-474 |
8.76e-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: 57.01 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 22 IGMLSKAIAIPAVS--SDESLrprvvEKAHFLADHLKKLGFaDIQLKElgtqpPPVSDPNLqLPPIVlarygNDPAKKNV 99
Cdd:cd08011 1 VKLLQELVQIPSPNppGDNTS-----AIAAYIKLLLEDLGY-PVELHE-----PPEEIYGV-VSNIV-----GGRKGKRL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 100 LVYGHYDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITCFEGMEES-GSL 178
Cdd:cd08011 64 LFNGHYDVVPAGDGEGWTVDPYSGKIKDGK--LYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETgGRA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 179 GLEELIgaekDKYFKGVDAVCISDNywlgTRKPVLTYGLRGcnYYQVTIEGPGADLHSGmfggiiaepmidLVQVMSTLV 258
Cdd:cd08011 142 GTKYLL----EKVRIKPNDVLIGEP----SGSDNIRIGEKG--LVWVIIEITGKPAHGS------------LPHRGESAV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 259 DSQGKILiegvdamvaketekeQELYKTIdfsveelnaasgsetalytkkedilkhrwryPSLSIHGVEGafysqGAK-T 337
Cdd:cd08011 200 KAAMKLI---------------ERLYELE-------------------------------KTVNPGVIKG-----GVKvN 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 338 VIPAKVIGKFSIRTVPDIDSEKLTQIVVDHChAAFKKLNSpnRCKAEliHDGNYwvSDPFNAQFQAAAKATKDVYGVEPD 417
Cdd:cd08011 229 LVPDYCEFSVDIRLPPGISTDEVLSRIIDHL-DSIEEVSF--EIKSF--YSPTV--SNPDSEIVKKTEEAITEVLGIRPK 301
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1891256837 418 YTREGGSIPITLTFEEQLKTSVLllpmGRGD-DGAHSINEKLDISNFVNGMKLMAAYL 474
Cdd:cd08011 302 EVISVGASDARFYRNAGIPAIVY----GPGRlGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
20-202 |
9.44e-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: 57.08 E-value: 9.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 20 EFIGMLSKAIAIPAVSSdESLRPRVVEKAHFLADHLKKLGFADIQLKElgtqpppVSDPNLQLPPIVLAR--YGNDpakK 97
Cdd:cd05650 2 EIIELERDLIRIPAVNP-ESGGEGEKEKADYLEKKLREYGFYTLERYD-------APDERGIIRPNIVAKipGGND---K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 98 NVLVYGHYDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITCFEGMEESGS 177
Cdd:cd05650 71 TLWIISHLDTVPPGDLSLWETDPWEPVVKDGK--IYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGS 148
|
170 180
....*....|....*....|....*.
gi 1891256837 178 -LGLEELIgaEKDKYFKGVDAVCISD 202
Cdd:cd05650 149 eYGIQYLL--NKFDLFKKDDLIIVPD 172
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
21-140 |
1.47e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 56.93 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 21 FIGMLSKAIAIPAVSSdeslRPRVVEKAHFLADHLKKLGFADIQLKELGTQPppvSDPNLqlppivLARY-GNDPaKKNV 99
Cdd:PRK09133 39 ARDLYKELIEINTTAS----TGSTTPAAEAMAARLKAAGFADADIEVTGPYP---RKGNL------VARLrGTDP-KKPI 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1891256837 100 LVYGHYDVQPAKLEDgWDSEPFELVvdEKKQVLRARGSSDD 140
Cdd:PRK09133 105 LLLAHMDVVEAKRED-WTRDPFKLV--EENGYFYGRGTSDD 142
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
20-183 |
6.98e-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. 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: 54.24 E-value: 6.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 20 EFIGMLSKAIAIPAVSSDESlrprvvEKAHFLADHLKKLGFadiqlkelgtqPPPVSDPNlqlppiVLARYGN-DPAKKN 98
Cdd:cd05651 1 EAIELLKSLIATPSFSREEH------KTADLIENYLEQKGI-----------PFKRKGNN------VWAENGHfDEGKPT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 99 VLVYGHYD-VQPAKledGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVqAHQAAGVELPVNLITCFEGMEE-SG 176
Cdd:cd05651 58 LLLNSHHDtVKPNA---GWTKDPFEPVEKGGK--LYGLGSNDAGASVVSLLATF-LHLYSEGPLNYNLIYAASAEEEiSG 131
|
....*..
gi 1891256837 177 SLGLEEL 183
Cdd:cd05651 132 KNGIESL 138
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
13-193 |
1.01e-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: 54.17 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 13 KIDELKPEFIGMLSKAIAIPAVSsDESLRP----RVVEKAhflADHLKKLGfadiqlKELGTQPppVSDPNLqlppIVLA 88
Cdd:cd03888 2 EIDKYKDEILEDLKELVAIPSVR-DEATEGapfgEGPRKA---LDKFLDLA------KRLGFKT--KNIDNY----AGYA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 89 RYGNDpaKKNVLVYGHYDVQPAKleDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELP--VNLI 166
Cdd:cd03888 66 EYGEG--EEVLGILGHLDVVPAG--EGWTTDPFKPVIKDGK--LYGRGTIDDKGPTIAALYALKILKDLGLPLKkkIRLI 139
|
170 180
....*....|....*....|....*..
gi 1891256837 167 tcFEGMEESGSLGLEeligaekdKYFK 193
Cdd:cd03888 140 --FGTDEETGWKCIE--------HYFE 156
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
24-252 |
1.94e-07 |
|
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: 52.98 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 24 MLSKAIAIPAVSSDESLrprvvEKAHFLADHLKKLGFAdiqlKELgTQPPPVSDPNLqlppivLARYGNDPAKKNVLVyG 103
Cdd:cd03894 2 LLARLVAFDTVSRNSNL-----ALIEYVADYLAALGVK----SRR-VPVPEGGKANL------LATLGPGGEGGLLLS-G 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 104 HYDVQPAkleDG--WDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITCFEgmEESGSLGLE 181
Cdd:cd03894 65 HTDVVPV---DGqkWSSDPFTLTERDGR--LYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYD--EEVGCLGVR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1891256837 182 ELIGAEKDKYFKgvDAVCIsdnywLG--TR-KPVLtyGLRGCNYYQVTIEGPGAdlHSGMFG-GIIA-EPMIDLVQ 252
Cdd:cd03894 138 HLIAALAARGGR--PDAAI-----VGepTSlQPVV--AHKGIASYRIRVRGRAA--HSSLPPlGVNAiEAAARLIG 202
|
|
| PRK06915 |
PRK06915 |
peptidase; |
8-179 |
2.08e-07 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 53.16 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 8 DKVFTKIDELKPEFIGMLSKAIAIPAVSSDES-LRPRVVEKahfladhLKKLGFA----DIQLKELGTQPPPVSD-PNLQ 81
Cdd:PRK06915 6 KQICDYIESHEEEAVKLLKRLIQEKSVSGDESgAQAIVIEK-------LRELGLDldiwEPSFKKLKDHPYFVSPrTSFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 82 LPPIVLARYGNDPAKKNVLVYGHYDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVEL 161
Cdd:PRK06915 79 DSPNIVATLKGSGGGKSMILNGHIDVVPEGDVNQWDHHPYSGEVIGGR--IYGRGTTDMKGGNVALLLAMEALIESGIEL 156
|
170 180
....*....|....*....|
gi 1891256837 162 PVNLItcFEGM--EESGSLG 179
Cdd:PRK06915 157 KGDVI--FQSVieEESGGAG 174
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
50-179 |
2.84e-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 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: 52.70 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 50 FLADHLKKLGFA----DIQLKELGTQP---PPVSDPNLQlpPIVLARYGNDPAKKNVLVY-GHYDVQPAKLEDGWDSEPF 121
Cdd:cd03895 22 LVAAALRSRGYTvdrwEIDVEKLKHHPgfsPVAVDYAGA--PNVVGTHRPRGETGRSLILnGHIDVVPEGPVELWTRPPF 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 122 ELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLItcFEGM--EESGSLG 179
Cdd:cd03895 100 EATIVDGW--MYGRGAGDMKAGLAANLFALDALRAAGLQPAADVH--FQSVveEECTGNG 155
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
7-142 |
4.56e-07 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 51.86 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 7 FDKVFTKIDELKPEFIGMLSKAIAIPAVSSDESlrprvvEKAHFLADHLKKLGFADIQLKELGTqpppvsdpnlqlppiV 86
Cdd:PRK13004 3 FKLILMLAEKYKADMTRFLRDLIRIPSESGDEK------RVVKRIKEEMEKVGFDKVEIDPMGN---------------V 61
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1891256837 87 LARYGNdpAKKNVLVYGHYDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTG 142
Cdd:PRK13004 62 LGYIGH--GKKLIAFDAHIDTVGIGDIKNWDFDPFEGEEDDGR--IYGRGTSDQKG 113
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
18-293 |
7.30e-07 |
|
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: 51.61 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 18 KPEFIGMLSKAIAIPAVSSDESLRPRV-----VEKA--HFLaDHLKKLGFADIQLKELGTQpppvsdpnlqlppivlARY 90
Cdd:TIGR01887 1 KDEILEDLKELIAIDSVEDLEKAKEGApfgegPRKAldKFL-EIAKRDGFTTENVDNYAGY----------------IEY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 91 GNDpaKKNVLVYGHYDVQPAKleDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELP--VNLItc 168
Cdd:TIGR01887 64 GQG--EEVLGILGHLDVVPAG--DGWTSPPFEPTIKDGR--IYGRGTLDDKGPTIAAYYAMKILKELGLKLKkkIRFI-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 169 FEGMEESGSLGLeeligaekDKYFKGV---DAVCISDNYWlgtrkPVlTYGLRGCNYYQVTIEGPG-ADLHSGMFGGIIA 244
Cdd:TIGR01887 136 FGTDEESGWKCI--------DYYFEHEempDIGFTPDAEF-----PI-IYGEKGITTLEIKFKDDTeGDVVLESFKAGEA 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1891256837 245 EPMidlvqvmstlVDSQGKILIEGVDAMVAKETEKEQELYKTIDFSVEE 293
Cdd:TIGR01887 202 YNM----------VPDHATAVISGKKLTEVEQLKFVFFIAKELEGDFEV 240
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
50-175 |
1.24e-06 |
|
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: 50.58 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 50 FLADHLKKLGFaDIQLKELGTqpppVsdPNLqlppivLARYGNDPakKNVLVYGHYDVQPAKLEDGWDSEPFELVVDEKK 129
Cdd:cd03891 23 LIAERLKALGF-TCERLEFGG----V--KNL------WARRGTGG--PHLCFAGHTDVVPPGDLEGWSSDPFSPTIKDGM 87
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1891256837 130 qvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVN---LITcfeGMEES 175
Cdd:cd03891 88 --LYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSisfLIT---SDEEG 131
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
25-179 |
3.63e-06 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 49.17 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 25 LSKAIAIPAVSSDEslrPRVVEKAHF--LADHLKKL---GFADIQLKELGTQPP----PVSDPnlQLPPIVLarygndpa 95
Cdd:PRK08262 50 LSEAIRFRTISNRD---RAEDDAAAFdaLHAHLEESypaVHAALEREVVGGHSLlytwKGSDP--SLKPIVL-------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 96 kknvlvYGHYDVQPA--KLEDGWDSEPFELVVDEkkQVLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITCFEGME 173
Cdd:PRK08262 117 ------MAHQDVVPVapGTEGDWTHPPFSGVIAD--GYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDE 188
|
....*.
gi 1891256837 174 ESGSLG 179
Cdd:PRK08262 189 EVGGLG 194
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
101-143 |
4.44e-06 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 49.07 E-value: 4.44e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1891256837 101 VYGHYDVQPAKleDGWDSEPFELVVDEKKqvLRARGSSDDTGP 143
Cdd:PRK07318 84 ILGHLDVVPAG--DGWDTDPYEPVIKDGK--IYARGTSDDKGP 122
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
48-198 |
7.85e-06 |
|
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: 47.97 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 48 AHFLADHLKKLGFAdiqlkelgtqppPVSDPNLQLPPIVLARYGnDPAKKNVLVYGHYD-VQPaklEDGWDSEPFElvVD 126
Cdd:cd03885 25 AELLAEELEALGFT------------VERRPLGEFGDHLIATFK-GTGGKRVLLIGHMDtVFP---EGTLAFRPFT--VD 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1891256837 127 EKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITCFEGMEESGSLGLEELIGaekdKYFKGVDAV 198
Cdd:cd03885 87 GDR--AYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRELIE----EEAKGADYV 152
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
101-161 |
3.69e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 45.84 E-value: 3.69e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1891256837 101 VYGHYDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVEL 161
Cdd:PRK07205 80 ILCHLDVVPEGDLSDWQTPPFEAVEKDGC--LFGRGTQDDKGPSMAALYAVKALLDAGVQF 138
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
25-146 |
6.16e-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: 45.10 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 25 LSKAIAIPAVSSDESlrprvvEKAHFLADHLKKLGFADIQLKELGTqpppvsdpnlqlppiVLARYGNdpAKKNVLVYGH 104
Cdd:cd05649 4 LRDLIQIPSESGEEK------GVVERIEEEMEKLGFDEVEIDPMGN---------------VIGYIGG--GKKKILFDGH 60
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1891256837 105 YDVQPAKLEDGWDSEPFE-LVVDEKkqvLRARGSSDDTGPLTG 146
Cdd:cd05649 61 IDTVGIGNIDNWKFDPYEgYETDGK---IYGRGTSDQKGGLAS 100
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
20-463 |
8.76e-05 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 44.49 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 20 EFIGMLSKAIAIPAVSSDEslrprvVEKAHFLADHLKKLGfadIQLKELgtqppPVSD--PNLqlppivLARYGNdpAKK 97
Cdd:PRK08588 3 EKIQILADIVKINSVNDNE------IEVANYLQDLFAKHG---IESKIV-----KVNDgrANL------VAEIGS--GSP 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 98 NVLVYGHYDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLtgwlhvvqahqAAGV---------ELPVN---- 164
Cdd:PRK08588 61 VLALSGHMDVVAAGDVDKWTYDPFELTEKDGK--LYGRGATDMKSGL-----------AALViamielkeqGQLLNgtir 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 165 -LITCFEGMEESGSLGLEELiGAEKDkyfkgVDAVCI---SDNYwlgtrkpvLTYGLRGCNYYQVTIEGPGAdlHSGM-F 239
Cdd:PRK08588 128 lLATAGEEVGELGAKQLTEK-GYADD-----LDALIIgepSGHG--------IVYAHKGSMDYKVTSTGKAA--HSSMpE 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 240 GGIIA-EPMIDLVQvmstlvdsqgkiliegvdamvaketeKEQELYKTIDFSVEELNAASGSETALytkkedilkhrwry 318
Cdd:PRK08588 192 LGVNAiDPLLEFYN--------------------------EQKEYFDSIKKHNPYLGGLTHVVTII-------------- 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 319 pslsihgvegafysQGAKTV--IPAKVIGKFSIRTVPDIDSEKltqiVVDHCHAAFKKLNSPNRCKAELIHDGNYW--VS 394
Cdd:PRK08588 232 --------------NGGEQVnsVPDEAELEFNIRTIPEYDNDQ----VISLLQEIINEVNQNGAAQLSLDIYSNHRpvAS 293
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1891256837 395 DPFNAQFQAAAKATKDVYGVEPDYTregGSIPITltfeeqlKTSVLL-----LPM---GRGD-DGAHSINEKLDISNF 463
Cdd:PRK08588 294 DKDSKLVQLAKDVAKSYVGQDIPLS---AIPGAT-------DASSFLkkkpdFPViifGPGNnLTAHQVDEYVEKDMY 361
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
50-139 |
9.65e-05 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 44.69 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 50 FLADHLKKLGFAdiqlkelgTQPPPVSD-PNLqlppivLARYGND-PakknVLVY-GHYDVQPAKLEDGWDSEPFELVVD 126
Cdd:PRK13009 27 LLAERLEALGFT--------CERMDFGDvKNL------WARRGTEgP----HLCFaGHTDVVPPGDLEAWTSPPFEPTIR 88
|
90
....*....|...
gi 1891256837 127 EKKqvLRARGSSD 139
Cdd:PRK13009 89 DGM--LYGRGAAD 99
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
19-139 |
1.30e-04 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 44.04 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 19 PEFIGMLSKAIAIPAVSS-----DESLRPrVVEKahfLADHLKKLGFA-DIQlkelgtqppPVSDP----NLqlppivLA 88
Cdd:PRK05111 5 PSFIEMYRALIATPSISAtdpalDQSNRA-VIDL---LAGWFEDLGFNvEIQ---------PVPGTrgkfNL------LA 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1891256837 89 RYGNDPAkkNVLVYGHYDVQPAKlEDGWDSEPFELVvdEKKQVLRARGSSD 139
Cdd:PRK05111 66 SLGSGEG--GLLLAGHTDTVPFD-EGRWTRDPFTLT--EHDGKLYGLGTAD 111
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
64-193 |
1.72e-04 |
|
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: 43.80 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 64 QLKELGTqPPPVSDPNLQLPPIVLARYGNDPAKKNVLVYGHYDVQPAkLEDGWDSEPFELVVDEKKQVLrARGSSDDTGP 143
Cdd:cd05646 33 QADELGL-PVRVIEVVPGKPVVVLTWEGSNPELPSILLNSHTDVVPV-FEEKWTHDPFSAHKDEDGNIY-ARGAQDMKCV 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1891256837 144 LTGWLHVVQAHQAAGVELPVNLITCFEGMEE-SGSLGLEELIgaeKDKYFK 193
Cdd:cd05646 110 GIQYLEAIRRLKASGFKPKRTIHLSFVPDEEiGGHDGMEKFV---KTEEFK 157
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
84-142 |
3.18e-04 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 43.22 E-value: 3.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1891256837 84 PIVLARYGNdpAKKNVLVYGHYDVQPAKLEDgWDSEPFELVVDEKKqvLRARGSSDDTG 142
Cdd:PRK08554 53 YAVYGEIGE--GKPKLLFMAHFDVVPVNPEE-WNTEPFKLTVKGDK--AYGRGSADDKG 106
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
8-179 |
3.38e-04 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 43.07 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 8 DKVFTKIDELKPEFIGMLSKAIAIPavssdeSLRPRVVEKAHFLADHLKKLGFA----DIQLKELGTQP--PPVSDPNLQ 81
Cdd:PRK06837 9 QRILAAVDAGFDAQVAFTQDLVRFP------STRGAEAPCQDFLARAFRERGYEvdrwSIDPDDLKSHPgaGPVEIDYSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 82 LPPIVLARYGNDPAKKNVLVYGHYDVQPAKLEDGWDSEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVEL 161
Cdd:PRK06837 83 APNVVGTYRPAGKTGRSLILQGHIDVVPEGPLDLWSRPPFDPVIVDGW--MYGRGAADMKAGLAAMLFALDALRAAGLAP 160
|
170 180
....*....|....*....|
gi 1891256837 162 --PVNLITCFEgmEESGSLG 179
Cdd:PRK06837 161 aaRVHFQSVIE--EESTGNG 178
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
103-184 |
3.44e-04 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 42.87 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 103 GHYDVQPAkleDG--WDSEPFELVVDEKKqvLRARGSSDdtgpLTGWLHVVQAH----QAAGVELPVNLitCFEGMEESG 176
Cdd:PRK07522 71 GHTDVVPV---DGqaWTSDPFRLTERDGR--LYGRGTCD----MKGFIAAALAAvpelAAAPLRRPLHL--AFSYDEEVG 139
|
....*...
gi 1891256837 177 SLGLEELI 184
Cdd:PRK07522 140 CLGVPSMI 147
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
25-148 |
5.14e-04 |
|
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: 42.24 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 25 LSKAIAIPAVSSDESLRPRVVE-KAHF--LADHLKK---LGFADIQLKELGT-------QPppvSDPNLQlpPIVLAryg 91
Cdd:cd05674 4 LSGAVQIPTVSFDDMPPIDEDErWDAFykFHDYLEKtfpLVHKTLKVEVVNEygllytwEG---SDPSLK--PLLLM--- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1891256837 92 ndpakknvlvyGHYDVQPA--KLEDGWDSEPFELVVDEKkqVLRARGSSDDTGPLTGWL 148
Cdd:cd05674 76 -----------AHQDVVPVnpETEDQWTHPPFSGHYDGG--YIWGRGALDDKNSLIGIL 121
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
22-258 |
5.33e-04 |
|
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: 42.08 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 22 IGMLSKAIAIPAVSSDESLRprvvekAHFLADHLKKLGFADIQLKELGTqpppvsdpnlqlppiVLARYGNDPAKKNVLV 101
Cdd:cd03896 1 VDTAIELGEIPAPTFREGAR------ADLVAEWMADLGLGDVERDGRGN---------------VVGRLRGTGGGPALLF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 102 YGHYD-VQPAKledgwdsEPFELVVDEKKqvLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLI---TCfeGMEESGS 177
Cdd:cd03896 60 SAHLDtVFPGD-------TPATVRHEGGR--IYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVfaaNV--GEEGLGD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 178 L-GLEELIGAEKDKyfkgVDAVCISDNYWLgtrkpVLTYGLRGCNYYQVTIEGPGAdlHS-GMFGGIIAepmidlVQVMS 255
Cdd:cd03896 129 LrGARYLLSAHGAR----LDYFVVAEGTDG-----VPHTGAVGSKRFRITTVGPGG--HSyGAFGSPSA------IVAMA 191
|
...
gi 1891256837 256 TLV 258
Cdd:cd03896 192 KLV 194
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
29-181 |
2.05e-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: 40.34 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 29 IAIPAVSSDESlrprvvEKAHFLADHLKKLGFAdiqlKELgtQPPPVSD-PNlqlppiVLARYGNDPAKKnVLVYGHYDV 107
Cdd:cd05652 9 VEIPSISGNEA------AVGDFLAEYLESLGFT----VEK--QPVENKDrFN------VYAYPGSSRQPR-VLLTSHIDT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1891256837 108 QPAKLedgwdsePFElvVDEKKQVLRARGSSDDTGPLTGWLHVVQAHQAAGVELPVNLITCF--------EGMEESGSLG 179
Cdd:cd05652 70 VPPFI-------PYS--ISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFvvgeetggDGMKAFNDLG 140
|
..
gi 1891256837 180 LE 181
Cdd:cd05652 141 LN 142
|
|
| |
