|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
2-468 |
0e+00 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 787.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 2 SAINWTEEVAKRKDDLIRDTQQFLQIKSVWEEESAKEGAPFGEGVEKALSFMLHKGETEGFTSKNLEGYAGHLEMGQGEE 81
Cdd:PRK07318 1 MTIDWKKEVEKRKDDLIEDLQELLRINSVRDDSKAKEGAPFGPGPVKALEKFLEIAERDGFKTKNVDNYAGHIEYGEGEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 82 LVGILCHVDVVPEGDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEESNWKCVD 161
Cdd:PRK07318 81 VLGILGHLDVVPAGDGWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRFIVGTDEESGWKCMD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 162 HYFKNEEMPTIGFAPDADFPIINAEKGISDIQVVqNGSEEKKGTYELVSFESGRRLNMVPDFAEAVVTGEDVNTLTVAYE 241
Cdd:PRK07318 161 YYFEHEEAPDFGFSPDAEFPIINGEKGITTFDLV-HFEGENEGDYVLVSFKSGLRENMVPDSAEAVITGDDLDDLIAAFE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 242 EYLQTAKKIGEAIVEGNTVTLQIKGISAHGSTPEKGENAGLLLANFLTTVALDGKANAFATFATETFTGDIFGEKATIAY 321
Cdd:PRK07318 240 AFLAENGLKGELEEEGGKLVLTVIGKSAHGSTPEKGVNAATYLAKFLNQLNLDGDAKAFLDFAAEYLHEDTRGEKLGIAY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 322 KDEVSGPLTVNVGRLSYTKENGGNLGLNVRYPVTTNFEEMIAKLKEYVGTHGFAVADYSNSRPHHVDKDHVLIRTLQRVY 401
Cdd:PRK07318 320 EDDVMGDLTMNVGVFSFDEEKGGTLGLNFRYPVGTDFEKIKAKLEKLIGVTGVELSEHEHQKPHYVPKDDPLVKTLLKVY 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300378381 402 EEQTGEKAELLAIGGGTYARSLKAGVAFGPLFPGKEELAHQKDEYIEIEDLLKATAIYAQAIHELAK 468
Cdd:PRK07318 400 EKQTGLKGEEQVIGGGTYARLLKRGVAFGAMFPGSEDTMHQANEYIEIDDLIKAAAIYAEAIYELAK 466
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
8-466 |
0e+00 |
|
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: 579.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 8 EEVAKRKDDLIRDTQQFLQIKSVWEEesAKEGAPFGEGVEKALSFMLHKGETEGFTSKNLEGYAGHLEMGQGEELVGILC 87
Cdd:cd03888 1 EEIDKYKDEILEDLKELVAIPSVRDE--ATEGAPFGEGPRKALDKFLDLAKRLGFKTKNIDNYAGYAEYGEGEEVLGILG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 88 HVDVVPEGDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEESNWKCVDHYFKNE 167
Cdd:cd03888 79 HLDVVPAGEGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGWKCIEHYFEHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 168 EMPTIGFAPDADFPIINAEKGISDIQVVQNGseEKKGTYELVSFESGRRLNMVPDFAEAVVTGEDVNTLTVAYEEYLQta 247
Cdd:cd03888 159 EYPDFGFTPDAEFPVINGEKGIVTVDLTFKI--DDDKGYRLISIKGGEATNMVPDKAEAVIPGKDKEELALSAATDLK-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 248 kkiGEAIVEGNTVTLQIKGISAHGSTPEKGENAGLLLANFLTTVALDGKANAFATFATETFTGDIFGEKATIAYKDEVSG 327
Cdd:cd03888 235 ---GNIEIDDGGVELTVTGKSAHASAPEKGVNAITLLAKFLAELNKDGNDKDFIKFLAKNLHEDYNGKKLGINFEDEVMG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 328 PLTVNVGRLSYtKENGGNLGLNVRYPVTTNFEEMIAKLKEYVGTHGFAVADYSNSRPHHVDKDHVLIRTLQRVYEEQTGE 407
Cdd:cd03888 312 ELTLNPGIITL-DDGKLELGLNVRYPVGTSAEDIIKQIEEALEKYGVEVEGHKHQKPLYVPKDSPLVKTLLKVYEEQTGK 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 300378381 408 KAELLAIGGGTYARSLKAGVAFGPLFPGKEELAHQKDEYIEIEDLLKATAIYAQAIHEL 466
Cdd:cd03888 391 EGEPVAIGGGTYARELPNGVAFGPEFPGQKDTMHQANEFIPIDDLIKALAIYAEAIYEL 449
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
14-463 |
0e+00 |
|
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: 573.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 14 KDDLIRDTQQFLQIKSVWEEESAKEGAPFGEGVEKALSFMLHKGETEGFTSKNLEGYAGHLEMGQGEELVGILCHVDVVP 93
Cdd:TIGR01887 1 KDEILEDLKELIAIDSVEDLEKAKEGAPFGEGPRKALDKFLEIAKRDGFTTENVDNYAGYIEYGQGEEVLGILGHLDVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 94 EGDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEESNWKCVDHYFKNEEMPTIG 173
Cdd:TIGR01887 81 AGDGWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEESGWKCIDYYFEHEEMPDIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 174 FAPDADFPIINAEKGISDIQVvqNGSEEKKGTYELVSFESGRRLNMVPDFAEAVVTGEDVNTLTVAYEEYLQTAKKIGEA 253
Cdd:TIGR01887 161 FTPDAEFPIIYGEKGITTLEI--KFKDDTEGDVVLESFKAGEAYNMVPDHATAVISGKKLTEVEQLKFVFFIAKELEGDF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 254 IVEGNTVTLQIKGISAHGSTPEKGENAGLLLANFLTTVALDGKANAFATFATETFTGDIFGEKATIAYKDEVSGPLTVNV 333
Cdd:TIGR01887 239 EVNDGTLTITLEGKSAHGSAPEKGINAATYLALFLAQLNLAGGAKAFLQFLAEYLHEDHYGEKLGIKFHDDVSGDLTMNV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 334 GRLSYTKENGGNLGLNVRYPVTTNFEEMIAKLKEYVGThGFAVADYSNSRPHHVDKDHVLIRTLQRVYEEQTGEKAELLA 413
Cdd:TIGR01887 319 GVIDYENAEAGLIGLNVRYPVGNDPDTMLKNELAKESG-VVEVTLNGYLKPLYVPKDDPLVQTLMKVYEKQTGDEGEPVA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 300378381 414 IGGGTYARSLKAGVAFGPLFPGKEELAHQKDEYIEIEDLLKATAIYAQAI 463
Cdd:TIGR01887 398 IGGGTYARLMPNGVAFGALFPGEEDTMHQANEYIMIDDLLLATAIYAEAI 447
|
|
| dipeptidase |
TIGR01886 |
dipeptidase PepV; This model represents a small clade of dipeptidase enzymes which are members ... |
4-468 |
4.06e-151 |
|
dipeptidase PepV; This model represents a small clade of dipeptidase enzymes which are members of the larger M25 subfamily of metalloproteases. Two characterized enzymes are included in the seed. One, from Lactococcus lactis has been shown to act on a wide range of dipeptides, but not larger peptides. The enzyme from Lactobacillus delbrueckii was originally characterized as a Xaa-His dipeptidase, specifically a carnosinase (beta-Ala-His) by complementation of an E. coli mutant. Further study, including the crystallization of the enzyme, has shown it to also be a non-specific dipeptidase. This group also includes enzymes from Streptococcus and Enterococcus. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 130941 [Multi-domain] Cd Length: 466 Bit Score: 438.16 E-value: 4.06e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 4 INWTEEVAKRKDDLIRDTQQFLQIKSVWEEESAKEGAPFGEGVEKALSFMLHKGETEGFTSKNLEGYAGHLEMGQGEELV 83
Cdd:TIGR01886 2 IDFKEEVEARKDALLEDLEELLRIDSSEDLENATEEYPFGPGPVDALTKFLSFAERDGFTTKNFDNYAGHVEYGAGDERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 84 GILCHVDVVPEGDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEESNWKCVDHY 163
Cdd:TIGR01886 82 GIIGHMDVVPAGEGWTRDPFEPEIDEGRIYARGASDDKGPSLAAYYAMKILKELGLPPSKKIRFVVGTNEETGWVDMDYY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 164 FKNEEMPTIGFAPDADFPIINAEKGISDIQVVQNGseEKKGTYELVSFESGRRLNMVPDFAEAVVTGEDVNTLTVAYEEY 243
Cdd:TIGR01886 162 FKHEETPDFGFSPDAEFPIINGEKGNFTLELSFKG--DNKGDYVLDSFKAGLAENMVPQVARAVISGPDAEALKAAYESF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 244 L-QTAKKIGEAIVEGNTVTLQIKGISAHGSTPEKGENAGLLLANFLTTVALDGKANAFATFATETFTGDIFGEKATIAYK 322
Cdd:TIGR01886 240 LaDKASLDGSFEINDESATIVLIGKGAHGAAPQVGINSATFLALFLNQYAFAGGAKNFIHFLAEVEHEDFYGEKLGIAFH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 323 DEVSGPLTVNVGRLSYTKENG-GNLGLNVRYPVTTNFEEMIAKLKEYVGTHGFAVADYSNSRPHHVDKDHVLIRTLQRVY 401
Cdd:TIGR01886 320 DELMGDLAMNAGMFDFDHANKeSKLLLNFRYPQGTSPETMQKQVLDKFGGIVDVTYNGHFEEPHYVPGSDPLVQTLLKVY 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300378381 402 EEQTGEKAELLAIGGGTYARSLKAGVAFGPLFPGKEELAHQKDEYIEIEDLLKATAIYAQAIHELAK 468
Cdd:TIGR01886 400 EKHTGKKGHEVIIGGGTYGRLLERGVAYGAMFEGGPDVMHQANEFMMLDDLILAAAIYAEAIYELAK 466
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
7-468 |
2.23e-117 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 351.30 E-value: 2.23e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 7 TEEVakrKDDLIRDTQQFLQIKSVWEEesAKEGAPFGEGVEKALSFMLHKGETEGF-TSKNLEGYAGHLEMGQGEELVGI 85
Cdd:PRK07205 6 TEKV---QDACVAAIKTLVSYPSVLNE--GENGTPFGQAIQDVLEATLDLCQGLGFkTYLDPKGYYGYAEIGQGEELLAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 86 LCHVDVVPEGD--GWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEESNWKCVDHY 163
Cdd:PRK07205 81 LCHLDVVPEGDlsDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGTDEETLWRCMNRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 164 FKNEEMPTIGFAPDADFPIINAEKGISDIQVVQNGSEEkkgtyelVSFESGRRLNMVPdfAEAVVTGEdvntltvaYEEY 243
Cdd:PRK07205 161 NEVEEQATMGFAPDSSFPLTYAEKGLLQAKLVGPGSDQ-------LELEVGQAFNVVP--AKASYQGP--------KLEA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 244 LQTA-KKIG-EAIVEGNTVTlqIKGISAHGSTPEKGENAGLLLAnflttVALDgkanAFATFATETFTGDIFGEKATIAY 321
Cdd:PRK07205 224 VKKElDKLGfEYVVKENEVT--VLGKSVHAKDAPQGINAVIRLA-----KALV----VLEPHPALDFLANVIGEDATGLN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 322 -----KDEVSGPLTVNVGRLSYTKENgGNLGLNVRYPVTTNFEEMIAKLKEYVGTHGFAVADYSNSRPHHVDKDHVLIRT 396
Cdd:PRK07205 293 ifgdiEDEPSGKLSFNIAGLTITKEK-SEIRIDIRIPVLADKEKLVQQLSQKAQEYGLTYEEFDYLAPLYVPLDSELVST 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300378381 397 LQRVYEEQTGEKAELLAIGGGTYARSLKAGVAFGPLFPGKEELAHQKDEYIEIEDLLKATAIYAQAIHELAK 468
Cdd:PRK07205 372 LMSVYQEKTGDDSPAQSSGGATFARTMPNCVAFGALFPGAPQTEHQANEHIVLEDLYRAMDIYAEAIYRLTT 443
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
77-468 |
4.71e-68 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 226.00 E-value: 4.71e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 77 GQGEELVGILCHVDVVP-------EGDGWTTPaYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMIL 149
Cdd:PRK06156 106 GSGSDKVGILTHADVVPanpelwvLDGTRLDP-FKVTLVGDRLYGRGTEDDKGAIVTALYAMKAIKDSGLPLARRIELLV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 150 GTDEESNWKCVDHYFKNEEMPTIGFAPDADFPIINAEKGISDIQVVQNGSEEKKGTYELVSFESGRRLNMVPDFAEAVVT 229
Cdd:PRK06156 185 YTTEETDGDPLKYYLERYTPPDYNITLDAEYPVVTAEKGWGTIMATFPKRAADGKGAEIVAMTGGAFANQIPQTAVATLS 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 230 GEDVNTLTVAyeeyLQTA-----KKIG-----EAIVEGNTVTLQIKGISAHGSTPEKGENAGLLLANFLTTVALDGKANA 299
Cdd:PRK06156 265 GGDPAALAAA----LQAAaaaqvKRHGggfsiDFKRDGKDVTITVTGKSAHSSTPESGVNPVTRLALFLQSLDGDLPHNH 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 300 F---ATFATETFTGDIFGEKATIAYKDEVSGPLTVNvgrLSYTKENGG--NLGLNVRYPVTTNFE----EMIAKLKEYVG 370
Cdd:PRK06156 341 AadaARYINDLVGLDYLGEKFGVAYKDDFMGPLTLS---PTVVGQDDKgtEVTVNLRRPVGKTPEllkgEIADALAAWQA 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 371 THGFAVA-DYSNSRPHHVDKDHVLIRTLQRVYEEQTGEKAELLAIGGGTYARSLKAGVAFGPLFPGKEELAHQKDEYIEI 449
Cdd:PRK06156 418 KHQVALDiDYYWGEPMVRDPKGPWLKTLLDVFGHFTGLDAKPVAIAGSTNAKLFPNAVSFGPAMPGVKYTGHTENEFKTV 497
|
410
....*....|....*....
gi 300378381 450 EDLLKATAIYAQAIHELAK 468
Cdd:PRK06156 498 EQFMLDLQMYTEMLIRIGN 516
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
7-468 |
5.39e-48 |
|
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: 169.68 E-value: 5.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 7 TEEVAKRKDDLIRDTQQFLQIKSVweeesAKEGAPFGEGVEKALsfmlhkgETEGFTSKNLEGYAGH------LEMGQGE 80
Cdd:COG0624 4 LAAIDAHLDEALELLRELVRIPSV-----SGEEAAAAELLAELL-------EALGFEVERLEVPPGRpnlvarRPGDGGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 81 ELVGILCHVDVVPEGD--GWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEESNWK 158
Cdd:COG0624 72 PTLLLYGHLDVVPPGDleLWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 159 CVDHYFKNEEmptIGFAPDAdfpiinaekgisdiqvvqngseekkgtyeLVSFESGRRLNmvpdfaeaVVTGEdvntltv 238
Cdd:COG0624 152 GARALVEELA---EGLKADA-----------------------------AIVGEPTGVPT--------IVTGH------- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 239 ayeeylqtaKKIGeaivegnTVTLQIKGISAHGSTPEKGENAGLLLANFLTTValdgKANAFATFATETFtgdifgekat 318
Cdd:COG0624 185 ---------KGSL-------RFELTVRGKAAHSSRPELGVNAIEALARALAAL----RDLEFDGRADPLF---------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 319 iaykdevsGPLTVNVGRLsytkeNGGN----------LGLNVRYPVTTNFEEMIAKLKEYVGTHGFAV-----ADYSNSR 383
Cdd:COG0624 235 --------GRTTLNVTGI-----EGGTavnvipdeaeAKVDIRLLPGEDPEEVLAALRALLAAAAPGVeveveVLGDGRP 301
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 384 PHHVDKDHVLIRTLQRVYEEQTGEKAELLAIGGGTYARSLKAG-----VAFGPlfpGKEELAHQKDEYIEIEDLLKATAI 458
Cdd:COG0624 302 PFETPPDSPLVAAARAAIREVTGKEPVLSGVGGGTDARFFAEAlgiptVVFGP---GDGAGAHAPDEYVELDDLEKGARV 378
|
490
....*....|
gi 300378381 459 YAQAIHELAK 468
Cdd:COG0624 379 LARLLERLAG 388
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
21-463 |
1.82e-42 |
|
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: 153.99 E-value: 1.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 21 TQQFLQIKSVWEEES------AKEGAPFGEGVEkalsfmlhkgETEGFTSKNLEGYAGhlemGQGEELVGILCHVDVVPE 94
Cdd:cd08659 3 LQDLVQIPSVNPPEAevaeylAELLAKRGYGIE----------STIVEGRGNLVATVG----GGDGPVLLLNGHIDTVPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 95 GDG--WTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEESNWKCVDHYFKNeempti 172
Cdd:cd08659 69 GDGdkWSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLEA------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 173 GFAPDADFPIInAEKGISDIQVVQngseekKGTYELvsfesgrrlnmvpdfaeavvtgedvntltvayeeylqtakkige 252
Cdd:cd08659 143 GYADRLDALIV-GEPTGLDVVYAH------KGSLWL-------------------------------------------- 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 253 aivegntvTLQIKGISAHGSTPEKGENAGLLLANFLttvaldGKANAFatfatetftgdiFGEKAtiayKDEVSGPLTVN 332
Cdd:cd08659 172 --------RVTVHGKAAHSSMPELGVNAIYALADFL------AELRTL------------FEELP----AHPLLGPPTLN 221
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 333 VGRLsytkeNGGN----------LGLNVRYPVTTNFEEMIAKLKEYVGTHGFAV-ADYSNSRPH--HVDKDHVLIRTLQR 399
Cdd:cd08659 222 VGVI-----NGGTqvnsipdeatLRVDIRLVPGETNEGVIARLEAILEEHEAKLtVEVSLDGDPpfFTDPDHPLVQALQA 296
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300378381 400 VYEEqTGEKAELLAIGGGTYARSLKAG-----VAFGPlfpGKEELAHQKDEYIEIEDLLKATAIYAQAI 463
Cdd:cd08659 297 AARA-LGGDPVVRPFTGTTDASYFAKDlgfpvVVYGP---GDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
88-465 |
3.21e-31 |
|
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: 122.07 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 88 HVDVVPEGDGWTTPaYSADIrDGKIFARGAIDDKGPTMAAYYAMKIVKELGlPLSKRVRMILGTDEESNWKCVDHYFKNE 167
Cdd:pfam01546 5 HMDVVPDEETWGWP-FKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEG-LKKGTVKLLFQPDEEGGMGGARALIEDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 168 EMptIGFAPDADFPIINAEkgisdiqvvqNGSEEKKGTYELVSFESGRRlnmvpdfaeavvtgedvntltvayeeylqta 247
Cdd:pfam01546 82 LL--EREKVDAVFGLHIGE----------PTLLEGGIAIGVVTGHRGSL------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 248 kkigeaivegnTVTLQIKGISAHGSTPEKGENAGLLLANFLTTValdgkanafatfatetftgdifgeKATIAYKDEVSG 327
Cdd:pfam01546 119 -----------RFRVTVKGKGGHASTPHLGVNAIVAAARLILAL------------------------QDIVSRNVDPLD 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 328 PLTVNVGRLSYtKENGGN-------LGLNVRYPVTTNFEEMIAKLKEYVGTHGFA------VADYSNSRPHHVDkDHVLI 394
Cdd:pfam01546 164 PAVVTVGNITG-IPGGVNvipgeaeLKGDIRLLPGEDLEELEERIREILEAIAAAygvkveVEYVEGGAPPLVN-DSPLV 241
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300378381 395 RTLQRVYEEQTGEKAELLAIG--GGTYARSLKAGVA-----FGPlfpgKEELAHQKDEYIEIEDLLKATAIYAQAIHE 465
Cdd:pfam01546 242 AALREAAKELFGLKVELIVSGsmGGTDAAFFLLGVPptvvfFGP----GSGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
14-468 |
5.70e-30 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 120.48 E-value: 5.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 14 KDDLIRDTQQFLQIKSVweeesakegAPFGEGVEKALSFMLHKGETEGF------------TSKNLEGYAGHLEMGQGEE 81
Cdd:PRK08651 5 MFDIVEFLKDLIKIPTV---------NPPGENYEEIAEFLRDTLEELGFsteiievpneyvKKHDGPRPNLIARRGSGNP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 82 LVGILCHVDVVPEGDGW-TTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGlplskRVRmilgtdeesnwkcv 160
Cdd:PRK08651 76 HLHFNGHYDVVPPGEGWsVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAG-----DGN-------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 161 dhyfkneemPTIGFAPDadfpiinaekgisdiqvvqngsEE--KKGTYELVsfesgRRLNMVPDfaeAVVTGEDvntltv 238
Cdd:PRK08651 137 ---------IELAIVPD----------------------EEtgGTGTGYLV-----EEGKVTPD---YVIVGEP------ 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 239 AYEEYLQTAKKigeAIVEGntvTLQIKGISAHGSTPEKGENAGLLLANFLttvaldgkanafatfatETFTGDIFGEKAT 318
Cdd:PRK08651 172 SGLDNICIGHR---GLVWG---VVKVYGKQAHASTPWLGINAFEAAAKIA-----------------ERLKSSLSTIKSK 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 319 IAYKDEVSGPLTVNVGRLSytkENGGN----------LGLNVRYPVTTNFEEMIAKLKEYVGT------HGFAVADYSNS 382
Cdd:PRK08651 229 YEYDDERGAKPTVTLGGPT---VEGGTktnivpgycaFSIDRRLIPEETAEEVRDELEALLDEvapelgIEVEFEITPFS 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 383 RPHHVDKDHVLIRTLQRVYEEQTGEKAELLAIGGGTYARSL-KAG---VAFGPlfpGKEELAHQKDEYIEIEDLLKATAI 458
Cdd:PRK08651 306 EAFVTDPDSELVKALREAIREVLGVEPKKTISLGGTDARFFgAKGiptVVYGP---GELELAHAPDEYVEVKDVEKAAKV 382
|
490
....*....|
gi 300378381 459 YAQAIHELAK 468
Cdd:PRK08651 383 YEEVLKRLAK 392
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
18-458 |
3.15e-29 |
|
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences contains annotations for both acetylornithine deacetylase and succinyl-diaminopimelate desuccinylase, but does not contain any members with experimental characterization. Bacillus, Staphylococcus and Sulfolobus species contain multiple hits to this subfamily and each may have a separate activity. Determining which is which must await further laboratory research. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273870 [Multi-domain] Cd Length: 375 Bit Score: 117.89 E-value: 3.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 18 IRDTQQFLQIKSVweeesakegAPFGEGVEKALSFMLHKGETEGFTSKNLEGYAGHL---------EMGQGEELVGIL-C 87
Cdd:TIGR01910 1 VELLKDLISIPSV---------NPPGGNEETIANYIKDLLREFGFSTDVIEITDDRLkvlgkvvvkEPGNGNEKSLIFnG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 88 HVDVVPEGD--GWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEESN-----WKCV 160
Cdd:TIGR01910 72 HYDVVPAGDleLWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGeagtlYLLQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 161 DHYFKNEEMPTIGFAPDADFpIINAEKGISDiqvvqngseekkgtyelvsfesgrrlnmvpdfaeavvtgedvntltvay 240
Cdd:TIGR01910 152 RGYFKDADGVLIPEPSGGDN-IVIGHKGSIW------------------------------------------------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 241 eeylqtakkigeaivegntVTLQIKGISAHGSTPEKGENAGLLLANFLTTValdgkanafatfatetftGDIFGEKATIA 320
Cdd:TIGR01910 182 -------------------FKLRVKGKQAHASFPQFGVNAIMKLAKLITEL------------------NELEEHIYARN 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 321 YKDEVSGPLTVNVGRLsytkeNGGN----------LGLNVRYPVTTNFEEMIAKLKEYV----GTHGFAV---ADYSNSR 383
Cdd:TIGR01910 225 SYGFIPGPITFNPGVI-----KGGDwvnsvpdyceFSIDVRIIPEENLDEVKQIIEDVVkalsKSDGWLYenePVVKWSG 299
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300378381 384 PHHVDKDHVLIRTLQRVYEEQTGEKAELLAIGGGTYARSL-KAGVAFGPLFPGKEELAHQKDEYIEIEDLLKATAI 458
Cdd:TIGR01910 300 PNETPPDSRLVKALEAIIKKVRGIEPEVLVSTGGTDARFLrKAGIPSIVYGPGDLETAHQVNEYISIKNLVESTKV 375
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
8-460 |
3.15e-27 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 112.73 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 8 EEVAKRKDDLIRDTQQFLQIKSvweeESAKEgapfgEGVEKALS-FMlhkgETEGFTSKNLEGYAGHL-EMGQGEELVGI 85
Cdd:PRK13004 8 MLAEKYKADMTRFLRDLIRIPS----ESGDE-----KRVVKRIKeEM----EKVGFDKVEIDPMGNVLgYIGHGKKLIAF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 86 LCHVDVVPEGD--GWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVrMILGTDEEsnwKCVDhy 163
Cdd:PRK13004 75 DAHIDTVGIGDikNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTL-YVTGTVQE---EDCD-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 164 fkneemptiGFAPDAdfpIINAEKgisdIQvvqngseekkgtyelvsfesgrrlnmvPDFaeaVVTGEDVNtltvayeey 243
Cdd:PRK13004 149 ---------GLCWRY---IIEEDK----IK---------------------------PDF---VVITEPTD--------- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 244 LQTakKIG-----EAIVEgntvtlqIKGISAHGSTPEKGENAGLLLANFLTTV-ALDGKanafatFATETFTGdifgeKA 317
Cdd:PRK13004 174 LNI--YRGqrgrmEIRVE-------TKGVSCHGSAPERGDNAIYKMAPILNELeELNPN------LKEDPFLG-----KG 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 318 TIAYKDEVSGPLTVNV----GRLSYTKEnggnlgLNVRYPVTTNFEEmIAKLKEyVGTHGFAVADYSNSRPHH------- 386
Cdd:PRK13004 234 TLTVSDIFSTSPSRCAvpdsCAISIDRR------LTVGETWESVLAE-IRALPA-VKKANAKVSMYNYDRPSYtglvypt 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 387 --------VDKDHVLIRTLQRVYEEQTGEKAELlaiggGTYARSLK----AGVA------FGplfPGKEELAHQKDEYIE 448
Cdd:PRK13004 306 ecyfptwlYPEDHEFVKAAVEAYKGLFGKAPEV-----DKWTFSTNgvsiAGRAgiptigFG---PGKEPLAHAPNEYTW 377
|
490
....*....|..
gi 300378381 449 IEDLLKATAIYA 460
Cdd:PRK13004 378 KEQLVKAAAMYA 389
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
75-463 |
1.52e-25 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 107.66 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 75 EMGQGEELVGILCHVDVVPEGD--GWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTD 152
Cdd:PRK08588 54 EIGSGSPVLALSGHMDVVAAGDvdKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 153 EEsnwkcvdhyfKNEE----MPTIGFAPDADFPIInAEKGISDIQVVQNGSEekkgTYELVSfesgrrlnmvpdfaeavv 228
Cdd:PRK08588 134 EE----------VGELgakqLTEKGYADDLDALII-GEPSGHGIVYAHKGSM----DYKVTS------------------ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 229 tgedvntltvayeeylqtakkigeaivegntvtlqiKGISAHGSTPEKGENAgllLANFLTtvaldgkanaFATFATETF 308
Cdd:PRK08588 181 ------------------------------------TGKAAHSSMPELGVNA---IDPLLE----------FYNEQKEYF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 309 tgdifgekATIAYKDEVSGPLTVNVgrlsyTKENGGN----------LGLNVR----YP---VTTNFEEMIAKLKEyVGT 371
Cdd:PRK08588 212 --------DSIKKHNPYLGGLTHVV-----TIINGGEqvnsvpdeaeLEFNIRtipeYDndqVISLLQEIINEVNQ-NGA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 372 HGFAVADYSNSRPHHVDKDHVLIRTLQRVYEEQTGEKAELLAIGGGTYARSL-KAG-----VAFGPlfpGKEELAHQKDE 445
Cdd:PRK08588 278 AQLSLDIYSNHRPVASDKDSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFlKKKpdfpvIIFGP---GNNLTAHQVDE 354
|
410
....*....|....*...
gi 300378381 446 YIEIEDLLKATAIYAQAI 463
Cdd:PRK08588 355 YVEKDMYLKFIDIYKEII 372
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
88-463 |
1.18e-20 |
|
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: 92.84 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 88 HVDVVP--EGDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEEsnwkcvdhyfk 165
Cdd:cd08011 68 HYDVVPagDGEGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEE----------- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 166 neempTIGFApdadfpiinaekgisdiqvvqngseekkGTYELVsfESGRrlnMVPDFaeaVVTGEDVNTLTVAYEEylq 245
Cdd:cd08011 137 -----TGGRA----------------------------GTKYLL--EKVR---IKPND---VLIGEPSGSDNIRIGE--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 246 taKKIGEAIVEgntvtlqIKGISAHGSTPEKGENAGLLLANFLTTValdgkANAFATFATETFTGdifGEKATIaykdeV 325
Cdd:cd08011 173 --KGLVWVIIE-------ITGKPAHGSLPHRGESAVKAAMKLIERL-----YELEKTVNPGVIKG---GVKVNL-----V 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 326 SGPLTVNVGRlsytkenggnlglnvRYPVTTNFEEMIAKLKEYVGT-HGFAVADYSNSRPHHVDKDHVLIRTLQRVYEEQ 404
Cdd:cd08011 231 PDYCEFSVDI---------------RLPPGISTDEVLSRIIDHLDSiEEVSFEIKSFYSPTVSNPDSEIVKKTEEAITEV 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300378381 405 TGEKAELLAIGGGTYARSLKA----GVAFGplfPGKEELAHQKDEYIEIEDLLKATAIYAQAI 463
Cdd:cd08011 296 LGIRPKEVISVGASDARFYRNagipAIVYG---PGRLGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
9-466 |
1.69e-18 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 87.51 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 9 EVAKRKDDLIRDTQQFLQIKSVweeesakegAPFGEGVEKALSFMLHKGETEGFTSKNL--EGYAGH------------L 74
Cdd:PRK13013 8 AIEARRDDLVALTQDLIRIPTL---------NPPGRAYREICEFLAARLAPRGFEVELIraEGAPGDsetyprwnlvarR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 75 EMGQGEELVGILCHVDVVPEGDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEE 154
Cdd:PRK13013 79 QGARDGDCVHFNSHHDVVEVGHGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 155 SNwkcvdhyfkneemptiGFAPDADFpiinAEKGISDIQVVQngseekkgtyelvsfesgrrlnmvpdfaeAVVTGEDVN 234
Cdd:PRK13013 159 SG----------------GFGGVAYL----AEQGRFSPDRVQ-----------------------------HVIIPEPLN 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 235 TLTVAyeeylqtakkIGEAIVEGNTVtlQIKGISAHGSTPEKGENA----GLLLANFLTTV--ALDGKANAF------AT 302
Cdd:PRK13013 190 KDRIC----------LGHRGVWWAEV--ETRGRIAHGSMPFLGDSAirhmGAVLAEIEERLfpLLATRRTAMpvvpegAR 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 303 FATETFTGDIFGEKATIAYKDEVSGPLTVNVGRLSYTKenggnlglnvRYPVTTNFEE-------MIAKLKEYVGTHGFA 375
Cdd:PRK13013 258 QSTLNINSIHGGEPEQDPDYTGLPAPCVADRCRIVIDR----------RFLIEEDLDEvkaeitaLLERLKRARPGFAYE 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 376 VADYSNSRPHHVDKDHVLIRTLQRVYEEQTGEKAElLAIGGGTYAR-------SLKAGVAFGplfPGKEELAHQKDEYIE 448
Cdd:PRK13013 328 IRDLFEVLPTMTDRDAPVVRSVAAAIERVLGRQAD-YVVSPGTYDQkhidrigKLKNCIAYG---PGILDLAHQPDEWVG 403
|
490
....*....|....*...
gi 300378381 449 IEDLLKATAIYAQAIHEL 466
Cdd:PRK13013 404 IADMVDSAKVMALVLADL 421
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
66-460 |
3.50e-18 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 85.94 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 66 NLEGYaghleMGQGEELVGILCHVDVVPEGD--GWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSK 143
Cdd:cd05649 43 NVIGY-----IGGGKKKILFDGHIDTVGIGNidNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLRDFA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 144 RVRMILGTDEEsnwKCVDhyfkneemptiGFAPDAdfpIINAEKgisdIQvvqngseekkgtyelvsfesgrrlnmvPDF 223
Cdd:cd05649 118 YTILVAGTVQE---EDCD-----------GVCWQY---ISKADK----IK---------------------------PDF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 224 aeaVVTGE--DVNTltvayeeylqtakKIG-----EAIVEgntvtlqIKGISAHGSTPEKGENAGLLLANFLTTV-ALDg 295
Cdd:cd05649 150 ---VVSGEptDGNI-------------YRGqrgrmEIRVD-------TKGVSCHGSAPERGDNAVYKMADIIQDIrQLN- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 296 kanafatfatETFTGDIFGEKATIAYKDEVSGPLTVNV----GRLSY--------TKENG----GNLGLNVRYPVTTNFE 359
Cdd:cd05649 206 ----------PNFPEAPFLGRGTLTVTDIFSTSPSRCAvpdsCRISIdrrltvgeTWEGCleeiRALPAVKKYGDDVAVS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 360 EMIAKLKEYVGTHgFAVADYSnsrPHHV-DKDHVLIRTLQRVYEEQTGEKAEL----LAIGGGTYARslKAG---VAFGp 431
Cdd:cd05649 276 MYNYDRPSYTGEV-YESERYF---PTWLlPEDHELVKALLEAYKALFGARPLIdkwtFSTNGVSIMG--RAGipcIGFG- 348
|
410 420
....*....|....*....|....*....
gi 300378381 432 lfPGKEELAHQKDEYIEIEDLLKATAIYA 460
Cdd:cd05649 349 --PGAENQAHAPNEYTWKEDLVRCAAGYA 375
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
65-463 |
1.00e-16 |
|
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349886 [Multi-domain] Cd Length: 366 Bit Score: 81.40 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 65 KNLegYAGHlemGQGEELVGILCHVDVVPEGD--GWTTPAYSADIRDGKIFARGAIDDKGpTMAAYYAM--KIVKELGLP 140
Cdd:cd03891 44 KNL--WARR---GTGGPHLCFAGHTDVVPPGDleGWSSDPFSPTIKDGMLYGRGAADMKG-GIAAFVAAaeRFVAKHPNH 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 141 lSKRVRMILGTDEEsnwkcvdhyfkneemptigfapdadfpiinaekgisdiqvvqngSEEKKGTYELVSFESGRrlNMV 220
Cdd:cd03891 118 -KGSISFLITSDEE--------------------------------------------GPAIDGTKKVLEWLKAR--GEK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 221 PDFAeavVTGEDVNTltvayeeylqtaKKIGEAIVEGN----TVTLQIKGISAHGSTPEKGENAGLLLANF---LTTVAL 293
Cdd:cd03891 151 IDYC---IVGEPTSE------------KKLGDTIKIGRrgslNGKLTIKGKQGHVAYPHLADNPIHLLAPIlaeLTATVL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 294 DgKANAFatFATETFtgdifgEKATIAykdevSGPLTVNV--GRLsytkenggNLGLNVRYPVTTNFEEMIAKLKEYVGT 371
Cdd:cd03891 216 D-EGNEF--FPPSSL------QITNID-----VGNGATNVipGEL--------KAKFNIRFNDEHTGESLKARIEAILDK 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 372 HGFavaDYS-----NSRPHHVDKDhVLIRTLQRVYEEQTGEKAElLAIGGGT----YARSLKAGVA-FGPlfPGKEelAH 441
Cdd:cd03891 274 HGL---DYDlewklSGEPFLTKPG-KLVDAVSAAIKEVTGITPE-LSTSGGTsdarFIASYGCPVVeFGL--VNAT--IH 344
|
410 420
....*....|....*....|..
gi 300378381 442 QKDEYIEIEDLLKATAIYAQAI 463
Cdd:cd03891 345 KVNERVSVADLEKLTDIYERIL 366
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
85-460 |
4.31e-15 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 76.81 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 85 ILCHVDVVPEGD--GWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEE--SNWKcv 160
Cdd:PRK13983 81 IISHMDVVPPGDlsLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEEtgSKYG-- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 161 dhyfkneemptIGFapdadfpIINAEKGIsdiqvvqngseekkgtyelvsFESGrRLNMVPDFAEavvtgEDVNTLTVAY 240
Cdd:PRK13983 159 -----------IQY-------LLKKHPEL---------------------FKKD-DLILVPDAGN-----PDGSFIEIAE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 241 EEYLQtakkigeaivegntVTLQIKGISAHGSTPEKGENAGLLLANFLTTV--ALDGKANA--------FATFAtetftg 310
Cdd:PRK13983 194 KSILW--------------LKFTVKGKQCHASTPENGINAHRAAADFALELdeALHEKFNAkdplfdppYSTFE------ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 311 difgekATIAYKDeVSGPLTVNvgrlsytkengGNLGLNV------RYPVttnfEEMIAKLKEYVgtHGFAVADY----- 379
Cdd:PRK13983 254 ------PTKKEAN-VDNINTIP-----------GRDVFYFdcrvlpDYDL----DEVLKDIKEIA--DEFEEEYGvkiev 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 380 ----SNSRPHHVDKDHVLIRTLQRVYEEQTGEKAELLAIGGGTYARSL-KAG---VAFGPLfpgkEELAHQKDEYIEIED 451
Cdd:PRK13983 310 eivqREQAPPPTPPDSEIVKKLKRAIKEVRGIEPKVGGIGGGTVAAFLrKKGypaVVWSTL----DETAHQPNEYAKISN 385
|
....*....
gi 300378381 452 LLKATAIYA 460
Cdd:PRK13983 386 LIEDAKVFA 394
|
|
| PRK06915 |
PRK06915 |
peptidase; |
88-460 |
8.88e-15 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 75.88 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 88 HVDVVPEGD--GWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKrvrmilgtdeesnwkcvDHYFK 165
Cdd:PRK06915 101 HIDVVPEGDvnQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKG-----------------DVIFQ 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 166 NeemptigfapdadfpiinaekgisdiqVVQngsEEKKGTYELVSFESGRRlnmvpdfAEAVVTGEDVNTltvayeeylq 245
Cdd:PRK06915 164 S---------------------------VIE---EESGGAGTLAAILRGYK-------ADGAIIPEPTNM---------- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 246 takKIGEAIVEGNTVTLQIKGISAHGSTPEKGENA---GLLLANFLTtvALDGKANAFATfatetftgDIFGEKATIayk 322
Cdd:PRK06915 197 ---KFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAiekSMFVIDHLR--KLEEKRNDRIT--------DPLYKGIPI--- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 323 devsgPLTVNVGRLsytkeNGGN--------LGLNVRYPVTTN---------FEEMIAKLK---EYVGTHGFAVaDYSNS 382
Cdd:PRK06915 261 -----PIPINIGKI-----EGGSwpssvpdsVILEGRCGIAPNetieaakeeFENWIAELNdvdEWFVEHPVEV-EWFGA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 383 R--PHHVDKDHVLIRTLQRVYEEQTGEKAELLAIGGGTYARSL-KAG----VAFGplfPGKEELAHQKDEYIEIEDLLKA 455
Cdd:PRK06915 330 RwvPGELEENHPLMTTLEHNFVEIEGNKPIIEASPWGTDGGLLtQIAgvptIVFG---PGETKVAHYPNEYIEVDKMIAA 406
|
....*
gi 300378381 456 TAIYA 460
Cdd:PRK06915 407 AKIIA 411
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
66-464 |
7.21e-14 |
|
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: 72.63 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 66 NLegYAGHLEMGQGeelvGIL--CHVDVVP-EGDGWTTPAYSADIRDGKIFARGAIDDKGpTMAAYYAMkiVKELGL-PL 141
Cdd:cd03894 47 NL--LATLGPGGEG----GLLlsGHTDVVPvDGQKWSSDPFTLTERDGRLYGRGTCDMKG-FLAAVLAA--VPRLLAaKL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 142 SKRVRMILGTDEESNWKCVDHYFknEEMPTIGFAPDA-------DFPIINAEKGISdiqvvqngseekkgtyelvsfesg 214
Cdd:cd03894 118 RKPLHLAFSYDEEVGCLGVRHLI--AALAARGGRPDAaivgeptSLQPVVAHKGIA------------------------ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 215 rrlnmvpdfaeavvtgedvntltvayeeylqtakkigeaivegnTVTLQIKGISAHGSTPEKGENAGLLLANFLTtvALD 294
Cdd:cd03894 172 --------------------------------------------SYRIRVRGRAAHSSLPPLGVNAIEAAARLIG--KLR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 295 GKAnafATFATETFTGDiFGEKATiaykdevsgplTVNVGRLSytkenGGN----------LGLNVRYPVTTNFEEMIAK 364
Cdd:cd03894 206 ELA---DRLAPGLRDPP-FDPPYP-----------TLNVGLIH-----GGNavnivpaeceFEFEFRPLPGEDPEAIDAR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 365 LKEYVGTHG-FAVADYSNSRPHHV-----DKDHVLIRTLQRVYEEQTGEKAellAIG--GGTYARSLKAGVAFGplfPGK 436
Cdd:cd03894 266 LRDYAEALLeFPEAGIEVEPLFEVpgletDEDAPLVRLAAALAGDNKVRTV---AYGteAGLFQRAGIPTVVCG---PGS 339
|
410 420
....*....|....*....|....*...
gi 300378381 437 EELAHQKDEYIEIEDLLKATAIYAQAIH 464
Cdd:cd03894 340 IAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
88-465 |
9.93e-14 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 72.73 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 88 HVDVVPEG--DGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVrmilgtdeesnwkcvdhYFK 165
Cdd:cd03895 82 HIDVVPEGpvELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADV-----------------HFQ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 166 NeemptigfapdadfpiinaekgisdiqVVQngsEEKKGTYELVSFESGRRlnmvpdfAEAVVTGEdvntltvayeeylQ 245
Cdd:cd03895 145 S---------------------------VVE---EECTGNGALAALMRGYR-------ADAALIPE-------------P 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 246 TAKKIGEAIVEGNTVTLQIKGISAHGSTPEKGENAgLLLANFLTTV--ALDGKANAFAtfatetftgdifgeKATIAYKD 323
Cdd:cd03895 175 TELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNA-IEKAMHLIQAlqELEREWNARK--------------KSHPHFSD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 324 eVSGPLTVNVGRLSytkenGGN--------LGLNVR---YPVTTnFEEMIAKLKEYVGTHGFAVADYSN----------- 381
Cdd:cd03895 240 -HPHPINFNIGKIE-----GGDwpssvpawCVLDCRigiYPGES-PEEARREIEECVADAAATDPWLSNhppevewngfq 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 382 SRPHHVDKDHVLIRTLQRVYEEQTGEKAELLAIGGGTYAR--SLKAG---VAFGPlfpgKEELAHQKDEYIEIEDLLKAT 456
Cdd:cd03895 313 AEGYVLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRffVLYGDipaLCYGP----GSRDAHGFDESVDLESLRKIT 388
|
....*....
gi 300378381 457 AIYAQAIHE 465
Cdd:cd03895 389 KTIALFIAE 397
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
85-460 |
4.48e-13 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and 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: 70.56 E-value: 4.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 85 ILCHVDVVPEGDG--WTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEE--SNWKcV 160
Cdd:cd05650 74 IISHLDTVPPGDLslWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEdgSEYG-I 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 161 DHYFKNEEMptigFAPDadfpiinaekgisdiqvvqngseekkgtyelvsfesgrRLNMVPDFAEavvtgEDVNTLTVAY 240
Cdd:cd05650 153 QYLLNKFDL----FKKD--------------------------------------DLIIVPDFGT-----EDGEFIEIAE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 241 EEYLQtakkigeaivegntVTLQIKGISAHGSTPEKGENAGLLLANFLTTvaLDGKANAFATFATETFTGDIFGEKATIA 320
Cdd:cd05650 186 KSILW--------------IKVNVKGKQCHASTPENGINAFVAASNFALE--LDELLHEKFDEKDDLFNPPYSTFEPTKK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 321 YKDeVSGPLTVNvgrlsytkengGNLGLNV------RYPVTTNFEEMIAKLKEYVGTHGFAVA---DYSNSRPHHVDKDH 391
Cdd:cd05650 250 EAN-VPNVNTIP-----------GYDVFYFdcrvlpTYKLDEVLKFVNKIISDFENSYGAGITyeiVQKEQAPPATPEDS 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300378381 392 VLIRTLQRVYEEQTGEKAELLAIGGGTYARSLKA----GVAFGPLfpgkEELAHQKDEYIEIEDLLKATAIYA 460
Cdd:cd05650 318 EIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKkgypAVVWSTL----DETAHQPNEYIRISHIVKDAKVFA 386
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
77-189 |
9.30e-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: 67.07 E-value: 9.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 77 GQGEELVGILCHVDVVP--EGDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEE 154
Cdd:cd03873 9 GEGGKSVALGAHLDVVPagEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 300378381 155 SNWK-----CVDHYFKNEEMPTIGFAPDAdFPIINAEKGI 189
Cdd:cd03873 89 VGSGggkglLSKFLLAEDLKVDAAFVIDA-TAGPILQKGV 127
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
77-158 |
3.38e-12 |
|
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: 65.15 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 77 GQGEELVGILCHVDVVPEGDGWTT--PAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEE 154
Cdd:cd18669 9 GGGGKRVLLGAHIDVVPAGEGDPRdpPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEE 88
|
....
gi 300378381 155 SNWK 158
Cdd:cd18669 89 VGSG 92
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
88-155 |
3.86e-12 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 67.72 E-value: 3.86e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 88 HVDVVPEG--DGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEES 155
Cdd:PRK06837 105 HIDVVPEGplDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEES 174
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
88-466 |
5.50e-12 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 67.03 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 88 HVDVVPEGD--GWTTPAYSADIRDGKIFARGAIDDKGpTMAAYYAMkivkelglplskrvrmilgtdeesnwkCVDHYFK 165
Cdd:PRK13009 66 HTDVVPPGDleAWTSPPFEPTIRDGMLYGRGAADMKG-SLAAFVVA---------------------------AERFVAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 166 NEEMP-TIGFapdadfpIINaekgiSDiqvvqngsEE---KKGTYELVsfESGRRLNMVPDFAeavVTGEDVNTltvaye 241
Cdd:PRK13009 118 HPDHKgSIAF-------LIT-----SD--------EEgpaINGTVKVL--EWLKARGEKIDYC---IVGEPTST------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 242 eylqtaKKIGEAIVEGN----TVTLQIKGISAHGSTPEKGEN-----AGLLLAnfLTTVALDgKANAFatFATETFtgdi 312
Cdd:PRK13009 167 ------ERLGDVIKNGRrgslTGKLTVKGVQGHVAYPHLADNpihlaAPALAE--LAATEWD-EGNEF--FPPTSL---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 313 fgekatiaykdEVSgplTVNVGrlsytkeNGGN--------LGLNVRYPVTTNFEEMIAKLKEYVGTHGFavaDYS---- 380
Cdd:PRK13009 232 -----------QIT---NIDAG-------TGATnvipgeleAQFNFRFSTEHTAESLKARVEAILDKHGL---DYTlewt 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 381 -NSRPHHVDKDHvLIRTLQRVYEEQTGEKAELLAiGGGTY-ARSLKA-G---VAFGPLfpgkEELAHQKDEYIEIEDLLK 454
Cdd:PRK13009 288 lSGEPFLTPPGK-LVDAVVAAIEAVTGITPELST-SGGTSdARFIADyGaqvVEFGPV----NATIHKVNECVSVADLEK 361
|
410
....*....|..
gi 300378381 455 ATAIYAQAIHEL 466
Cdd:PRK13009 362 LTRIYERILERL 373
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
77-466 |
6.90e-12 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 66.61 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 77 GQGEELVGILCHVDVVPeGDgwttpaYSADIRDGKIFARGAIDDKGPtMAAYyamkIVKELGLPLSKRVRMILG--TDEE 154
Cdd:cd05653 51 GSGPPDVLLLGHIDTVP-GE------IPVRVEGGVLYGRGAVDAKGP-LAAM----ILAASALNEELGARVVVAglVDEE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 155 SNwkcvdhyfkneemptigfapdadfpiinaekgisdiqvvqngseeKKGTYELVsfESGRRlnmvPDFaeaVVTGEDVN 234
Cdd:cd05653 119 GS---------------------------------------------SKGARELV--RRGPR----PDY---IIIGEPSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 235 T--LTVAYEEYLQtakkiGEAIVEGNtvtlqikgiSAHGSTPEkgENAGLLLANFLTTV--ALDGKANAFATFATETFTG 310
Cdd:cd05653 145 WdgITLGYRGSLL-----VKIRCEGR---------SGHSSSPE--RNAAEDLIKKWLEVkkWAEGYNVGGRDFDSVVPTL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 311 DIFGEkatiaYKDEVSGPLTVNvgrlsytkenggnlgLNVRYPVTTNFEEMIAKLKEYVGTHGFAVADysNSRPHHVDKD 390
Cdd:cd05653 209 IKGGE-----SSNGLPQRAEAT---------------IDLRLPPRLSPEEAIALATALLPTCELEFID--DTEPVKVSKN 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 391 HVLIRTLQRVYEEQtgekaellaigGGTYARSLKAG---------------VAFGplfPGKEELAHQKDEYIEIEDLLKA 455
Cdd:cd05653 267 NPLARAFRRAIRKQ-----------GGKPRLKRKTGtsdmnvlaplwtvpiVAYG---PGDSTLDHTPNEHIELAEIERA 332
|
410
....*....|.
gi 300378381 456 TAIYAQAIHEL 466
Cdd:cd05653 333 AAVLKGALEEL 343
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
8-155 |
1.03e-11 |
|
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: 66.86 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 8 EEVAKRKDDLIRDTQQFLQIKSVWEEESAKegapfGEgVEKALSFMLHKGETEGFTSKNLegYAGHLEMGQGEEL----- 82
Cdd:cd05676 3 KYIDEHQDEFIERLREAVAIQSVSADPEKR-----PE-LIRMMEWAAERLEKLGFKVELV--DIGTQTLPDGEELplppv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 83 -------------VGILCHVDVVP--EGDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRM 147
Cdd:cd05676 75 llgrlgsdpskktVLIYGHLDVQPakLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKF 154
|
....*...
gi 300378381 148 ILGTDEES 155
Cdd:cd05676 155 CFEGMEES 162
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
60-463 |
9.33e-11 |
|
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130947 [Multi-domain] Cd Length: 364 Bit Score: 63.30 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 60 EGFTSKNLEGYAGHLEMGqGEELVGilcHVDVVP-EGDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELg 138
Cdd:TIGR01892 42 DGAEKSNLVAVIGPSGAG-GLALSG---HTDVVPyDDAAWTRDPFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAE- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 139 lPLSKRVRMILGTDEESNWKCVDHYFKNeemptigFAPDADFPIInaekgisdiqvvqngseekkgtyelvsfesGRRLN 218
Cdd:TIGR01892 117 -QLKKPLHLALTADEEVGCTGAPKMIEA-------GAGRPRHAII------------------------------GEPTR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 219 MVPdfaeavvtgedvntltvayeeyLQTAKKIGEAIVEgntvtlqIKGISAHGSTPEKGENAGLLLANFLT-TVALdgka 297
Cdd:TIGR01892 159 LIP----------------------VRAHKGYASAEVT-------VRGRSGHSSYPDSGVNAIFRAGRFLQrLVHL---- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 298 nafatfaTETFTGDIFGEKATIAYKdevsgplTVNVGRLsytkeNGGN----------LGLNVRYP-------VTTNFEE 360
Cdd:TIGR01892 206 -------ADTLLREDLDEGFTPPYT-------TLNIGVI-----QGGKavniipgaceFVFEWRPIpgmdpeeLLQLLET 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 361 MIAKLKEyvGTHGFAVAD--YSNSRPHHVDKDHVLIRTLqrvyEEQTGEKAELLAIG--GGTYARSLKAGVAFGPlfpGK 436
Cdd:TIGR01892 267 IAQALVR--DEPGFEVQIevVSTDPGVNTEPDAELVAFL----EELSGNAPEVVSYGteAPQFQELGAEAVVCGP---GD 337
|
410 420
....*....|....*....|....*..
gi 300378381 437 EELAHQKDEYIEIEDLLKATAIYAQAI 463
Cdd:TIGR01892 338 IRQAHQPDEYVEIEDLVRCRAVLARLV 364
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
15-165 |
1.46e-10 |
|
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: 63.13 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 15 DDLIRdtqqFLQIKSVweeeSAKegapfGEGVEKALSFMLHKGETEGFTSKNLEGYAGHLEMG----QGEELVGILCHVD 90
Cdd:cd05681 3 EDLRD----LLKIPSV----SAQ-----GRGIPETADFLKEFLRRLGAEVEIFETDGNPIVYAefnsGDAKTLLFYNHYD 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300378381 91 VVPEgDG---WTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEESNWKCVDHYFK 165
Cdd:cd05681 70 VQPA-EPlelWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPNLEKFVA 146
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
88-155 |
1.63e-10 |
|
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: 62.73 E-value: 1.63e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 88 HVDVVPEGD--GWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEES 155
Cdd:cd03893 71 HYDVQPAGDedGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEES 140
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
44-452 |
3.48e-10 |
|
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: 61.45 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 44 EGVEKALSFMLHKGETEGFTSK--NLEGYAGHLEM---GQGEELVGILCHVDVV-PEGDGWTTPaYSadIRDGKIFARGA 117
Cdd:cd03885 19 EGVDRVAELLAEELEALGFTVErrPLGEFGDHLIAtfkGTGGKRVLLIGHMDTVfPEGTLAFRP-FT--VDGDRAYGPGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 118 IDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEEsnwkcvdhyfkneemptIGfAPDADfpiinaekgisdiQVVQN 197
Cdd:cd03885 96 ADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEE-----------------IG-SPGSR-------------ELIEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 198 gsEEKKGTYELVsFESGRrlnmvPDfaEAVVTGedvntltvayeeylqtAKKIGeaivegnTVTLQIKGISAH-GSTPEK 276
Cdd:cd03885 145 --EAKGADYVLV-FEPAR-----AD--GNLVTA----------------RKGIG-------RFRLTVKGRAAHaGNAPEK 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 277 GENAGLLLANFLTTVAldgkanafatfatetftgdifgekatiAYKDEVSGpLTVNVGRLSytkenGGN----------L 346
Cdd:cd03885 192 GRSAIYELAHQVLALH---------------------------ALTDPEKG-TTVNVGVIS-----GGTrvnvvpdhaeA 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 347 GLNVRYPVTTNFEEMIAKLKEYVGTHgfAVADYSNS------RPHHVDKDHV--LIRTLQRVYEEQtGEKAELLAIGGGT 418
Cdd:cd03885 239 QVDVRFATAEEADRVEEALRAIVATT--LVPGTSVEltgglnRPPMEETPASrrLLARAQEIAAEL-GLTLDWEATGGGS 315
|
410 420 430
....*....|....*....|....*....|....*....
gi 300378381 419 ---YARSLKAGV--AFGPlfPGKeeLAHQKDEYIEIEDL 452
Cdd:cd03885 316 danFTAALGVPTldGLGP--VGG--GAHTEDEYLELDSL 350
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
75-154 |
3.79e-10 |
|
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.
Pssm-ID: 349869 [Multi-domain] Cd Length: 394 Bit Score: 61.42 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 75 EMGQGEELVGILCHVDVVPEGDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEE 154
Cdd:cd02697 68 RYGDGGRTVALNAHGDVVPPGDGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEE 147
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
15-465 |
6.17e-10 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349935 [Multi-domain] Cd Length: 379 Bit Score: 60.95 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 15 DDLIRDTQQFLQIKSVWEEESAKEGAPFGEGVEKALSFMLHKGetegFTSKNLEGYAGHLEM-------GQGEELVgILC 87
Cdd:cd08013 1 DDPVSLTQTLVRINSSNPSLSATGGAGEAEIATYVAAWLAHRG----IEAHRIEGTPGRPSVvgvvrgtGGGKSLM-LNG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 88 HVDVVPEgDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLplskRVRMILG--TDEEsnwkcvdhyfk 165
Cdd:cd08013 76 HIDTVTL-DGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGL----RGDVILAavADEE----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 166 neemptigfapdadfpiiNAEKGISDIqvvqngseekkgtyelvsFESGRRlnmvpdfAEAVVTGEDVN-TLTVAYEeyl 244
Cdd:cd08013 140 ------------------DASLGTQEV------------------LAAGWR-------ADAAIVTEPTNlQIIHAHK--- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 245 qtakkiGEAIVEgntvtLQIKGISAHGSTPEKGENAGLLLANFLttVALDGKANAFATFATETFTGDIFGEKATIAYKDE 324
Cdd:cd08013 174 ------GFVWFE-----VDIHGRAAHGSRPDLGVDAILKAGYFL--VALEEYQQELPERPVDPLLGRASVHASLIKGGEE 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 325 VSG-P--LTVNVGRLSytkenggnlglnvrYPVTTNfEEMIAKLKEYVGTHGFAVADYS-------NSR-PHHVDKDHVL 393
Cdd:cd08013 241 PSSyParCTLTIERRT--------------IPGETD-ESVLAELTAILGELAQTVPNFSyrepritLSRpPFEVPKEHPF 305
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300378381 394 IRTLQRVYEEQTGEKAELLAIGGGTYARSLKA----GVAFGPLFPGkeelAHQKDEYIEIEDLLKATAIYAQAIHE 465
Cdd:cd08013 306 VQLVAAHAAKVLGEAPQIRSETFWTDAALLAEagipSVVFGPSGAG----LHAKEEWVDVESIRQLREVLSAVVRE 377
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
250-456 |
7.06e-10 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 60.45 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 250 IGEAIVE---GNTVTLQIKGISAH-GSTPEKGENAGLLLANFLTTVALDGkanafatfATETFT---GDIFGEKATIAYK 322
Cdd:COG2195 161 EGELEYEcagAADAKITIKGKGGHsGDAKEKMINAIKLAARFLAALPLGR--------IPEETEgneGFIHGGSATNAIP 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 323 DEVSgpltvnvgrlsytkenggnLGLNVRYPVTTNFEE----MIAKLKEYVGTHGFAVA------DYSNSRPhhvDKDHV 392
Cdd:COG2195 233 REAE-------------------AVYIIRDHDREKLEArkaeLEEAFEEENAKYGVGVVeveiedQYPNWKP---EPDSP 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300378381 393 LIRTLQRVYEEQtGEKAELLAIGGGTYARSLKA-GVafgP---LFPGKEElAHQKDEYIEIEDLLKAT 456
Cdd:COG2195 291 IVDLAKEAYEEL-GIEPKIKPIRGGLDGGILSFkGL---PtpnLGPGGHN-FHSPDERVSIESMEKAW 353
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
24-156 |
8.69e-10 |
|
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: 60.40 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 24 FLQIKSVweeeSAKegAPFGEGVEKALSFMLHKGETEGFTSKNL---EG----YAGHLeMGQGEELVGILCHVDVVPEG- 95
Cdd:cd05680 7 LLRIPSV----SAD--PAHKGDVRRAAEWLADKLTEAGFEHTEVlptGGhplvYAEWL-GAPGAPTVLVYGHYDVQPPDp 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300378381 96 -DGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEESN 156
Cdd:cd05680 80 lELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIG 141
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
85-463 |
9.69e-10 |
|
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: 60.45 E-value: 9.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 85 ILCHVDVVP-EGDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEESnwkcvdhy 163
Cdd:cd05675 70 LLGHIDVVPaDASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEA-------- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 164 fkneemptigfapdadfpiiNAEKGISDIqvvqngSEEKKGTYELVSFEsgrrLNMVPDFAEAVVTGedvntlTVAYEey 243
Cdd:cd05675 142 --------------------GGENGAKWL------VDNHPELFDGATFA----LNEGGGGSLPVGKG------RRLYP-- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 244 LQTAKKIgeaIVEgntVTLQIKGISAHGSTPEKgENAGLLLANFLTTVAldgkANAFA---TFATETFT--GDIFGEKAT 318
Cdd:cd05675 184 IQVAEKG---IAW---MKLTVRGRAGHGSRPTD-DNAITRLAEALRRLG----AHNFPvrlTDETAYFAqmAELAGGEGG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 319 IAYKD--EVSGPLTVNVGRL------------SYTKENGGNLG----------LNVRY-PVTTNfEEMIAKLKEYVGTHG 373
Cdd:cd05675 253 ALMLTavPVLDPALAKLGPSapllnamlrntaSPTMLDAGYATnvlpgrataeVDCRIlPGQSE-EEVLDTLDKLLGDPD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 374 FAVADYSNSRPHHVDKDHVLIRTLQRVYEEQTGEkAELLAI--GGGTYARSLKA--GVAFG--PLFPGKEE----LAHQK 443
Cdd:cd05675 332 VSVEAVHLEPATESPLDSPLVDAMEAAVQAVDPG-APVVPYmsPGGTDAKYFRRlgIPGYGfaPLFLPPELdytgLFHGV 410
|
410 420
....*....|....*....|
gi 300378381 444 DEYIEIEDLLKATAIYAQAI 463
Cdd:cd05675 411 DERVPVESLYFGVRFLDRLV 430
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
14-170 |
6.68e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 57.84 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 14 KDDLIRDTQQFLQIKSVweeeSAKegapfGEGVEKALSFMLHKGETEGFTSkNLEGYAGHlEMGQGEELVG------ILC 87
Cdd:PRK06446 1 MDEELYTLIEFLKKPSI----SAT-----GEGIEETANYLKDTMEKLGIKA-NIERTKGH-PVVYGEINVGakktllIYN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 88 HVDVVPEG--DGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMK-IVKELGLPLSkrVRMILGTDEESNWKCVDHYF 164
Cdd:PRK06446 70 HYDVQPVDplSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKhLIDKHKLNVN--VKFLYEGEEEIGSPNLEDFI 147
|
....*..
gi 300378381 165 K-NEEMP 170
Cdd:PRK06446 148 EkNKNKL 154
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
88-154 |
7.51e-09 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 57.65 E-value: 7.51e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300378381 88 HVDVVPEGDG----WTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEE 154
Cdd:PRK08262 119 HQDVVPVAPGtegdWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEE 189
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
11-124 |
1.75e-08 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 56.68 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 11 AKRKDDLIRDTQQFLQIKSVWEEESAKEGapfgegVEKALSFMLHKGETEGF-------TSKNLEGYAGHLEmGQGEELV 83
Cdd:PRK08201 10 RERREAHLEELKEFLRIPSISALSEHKED------VRKAAEWLAGALEKAGLehveimeTAGHPIVYADWLH-APGKPTV 82
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 300378381 84 GILCHVDVVPEG--DGWTTPAYSADIRDGKIFARGAIDDKGPT 124
Cdd:PRK08201 83 LIYGHYDVQPVDplNLWETPPFEPTIRDGKLYARGASDDKGQV 125
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
87-145 |
8.24e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 54.53 E-value: 8.24e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300378381 87 CHVDVVPEGD--GWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKElGLPLSKRV 145
Cdd:PRK07907 90 AHHDVQPPGDpdAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRALGG-DLPVGVTV 149
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
1-154 |
8.28e-08 |
|
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: 54.03 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 1 MSAINWTEevakrkDDLIRDTQQFLQIKSVweeESAKEGAPfgegvekALSFMLHKGETEGFTSKNLEGYAGHLEM---- 76
Cdd:TIGR01880 1 MSSSKWEE------DIAVTRFREYLRINTV---QPNPDYAA-------CVDFLIKQADELGLARKTIEFVPGKPVVvltw 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 77 -GQGEELVGIL--CHVDVVP-EGDGWTTPAYSADI-RDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGT 151
Cdd:TIGR01880 65 pGSNPELPSILlnSHTDVVPvFREHWTHPPFSAFKdEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVP 144
|
...
gi 300378381 152 DEE 154
Cdd:TIGR01880 145 DEE 147
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
88-164 |
2.32e-07 |
|
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: 53.11 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 88 HVDVVPEGDGW------TTPAysadIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPlSKRVRMILGTDEESNWKCVD 161
Cdd:cd05682 81 HMDKQPPFTGWdeglgpTKPV----IRGDKLYGRGGADDGYAIFASLTAIKALQEQGIP-HPRCVVLIEACEESGSADLP 155
|
...
gi 300378381 162 HYF 164
Cdd:cd05682 156 FYL 158
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
88-131 |
3.35e-07 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 52.64 E-value: 3.35e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 300378381 88 HVDVVP----EGDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAM 131
Cdd:cd05674 77 HQDVVPvnpeTEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAV 124
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
47-187 |
4.55e-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: 51.89 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 47 EKALSFMLHKGETEGFTSKNLEGYAGHLE-----MGQGEELVGIL--CHVDVVP-EGDGWTTPAYSADI-RDGKIFARGA 117
Cdd:cd05646 24 DACVEFLKRQADELGLPVRVIEVVPGKPVvvltwEGSNPELPSILlnSHTDVVPvFEEKWTHDPFSAHKdEDGNIYARGA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 118 IDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEE-----SNWKCVDH-YFKNEempTIGFA-------PDADFPIIN 184
Cdd:cd05646 104 QDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEigghdGMEKFVKTeEFKKL---NVGFAldeglasPTEEYRVFY 180
|
...
gi 300378381 185 AEK 187
Cdd:cd05646 181 GER 183
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
392-459 |
1.34e-06 |
|
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: 48.96 E-value: 1.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300378381 392 VLIRTLQRVYEEQTGEKAELLAIGGGTYARSLK-AGVAFGPLFPGKEELAHQKDEYIEIEDLLKATAIY 459
Cdd:cd03873 132 PLVDALRKAAREVGGKPQRASVIGGGTDGRLFAeLGIPGVTLGPPGDKGAHSPNEFLNLDDLEKATKVY 200
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
70-468 |
2.02e-06 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 49.77 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 70 YAGHLEMGQGEELVGILCHVDVVPEGDG-WTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMK-IVKElglPLSKRVRM 147
Cdd:PRK08554 53 YAVYGEIGEGKPKLLFMAHFDVVPVNPEeWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKeLSKE---PLNGKVIF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 148 ILGTDEESNWKCVDHYfkNEEMPTIGFAPD----AD----FPIINAEKGISDIQVVQNGSEEKKGTYELVSFESgrRLNM 219
Cdd:PRK08554 130 AFTGDEEIGGAMAMHI--AEKLREEGKLPKyminADgigmKPIIRRRKGFGVTIRVPSEKVKVKGKLREQTFEI--RTPV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 220 VPD-FAEAVVTGEDVNTLtVAYEEYLQT----AKKIGEAIVEGNTV--TLQIKGIS-AHGSTPEKGENAGLLLANFLTTV 291
Cdd:PRK08554 206 VETrHAAYFLPGVDTHPL-IAASHFLREsnvlAVSLEGKFLKGNVVpgEVTLTYLEpGEGEEVEVDLGLTRLLKAIVPLV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 292 ALDGKANAFATFATeTFTGDIFgekatiAYKDEvSGPLTVNVGRLSYTKEnggnlglNVRYPVTTNFEEMIAKLKEYVGT 371
Cdd:PRK08554 285 RAPIKAEKYSDYGV-SITPNVY------SFAEG-KHVLKLDIRAMSYSKE-------DIERTLKEVLEFNLPEAEVEIRT 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 372 HGFAVADYSnsrphhvDKDHVLIRTLQRVYEEqTGEKAELLAIGGGTYAR-----SLKAgVAFGPlfpgKEELAHQKDEY 446
Cdd:PRK08554 350 NEKAGYLFT-------PPDEEIVKVALRVLKE-LGEDAEPVEGPGASDSRyftpyGVKA-IDFGP----KGGNIHGPNEY 416
|
410 420
....*....|....*....|..
gi 300378381 447 IEIEDLLKATAIYAQAIHELAK 468
Cdd:PRK08554 417 VEIDSLKKMPEVYKRIALRLLG 438
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
88-141 |
3.55e-06 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 49.27 E-value: 3.55e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 300378381 88 HVDV--VPEGDGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYAMKIVKELGLPL 141
Cdd:PRK08596 85 HMDVaeVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIEL 140
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
88-154 |
4.24e-06 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 48.65 E-value: 4.24e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300378381 88 HVDVVP-EGDGWTTPAYSADIRDGKIFARGAIDDKGpTMAAYYAMkIVKELGLPLSKRVRMILGTDEE 154
Cdd:PRK07522 72 HTDVVPvDGQAWTSDPFRLTERDGRLYGRGTCDMKG-FIAAALAA-VPELAAAPLRRPLHLAFSYDEE 137
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
392-459 |
4.86e-06 |
|
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: 47.04 E-value: 4.86e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300378381 392 VLIRTLQRVYEEQTGEKAELLAIGGGTYARSLKA----GVAFGPlfpGKEELAHQKDEYIEIEDLLKATAIY 459
Cdd:cd18669 130 PLVDALSEAARKVFGKPQHAEGTGGGTDGRYLQElgipGVTLGA---GGGKGAHSPNERVNLEDLESALAVL 198
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
76-466 |
3.45e-05 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 45.93 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 76 MGQGEELvgILCHVDVVPegdGWTTPAYSADIrdgkIFARGAIDDKGPTMAayyamkivkelglplskrvrMILGTdees 155
Cdd:PRK00466 58 LGEGDIL--LASHVDTVP---GYIEPKIEGEV----IYGRGAVDAKGPLIS--------------------MIIAA---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 156 nWkcvdhyfkneemptigfapdadfpIINaEKGISdIQVVQNGSEEKK--GTYELVSfeSGRRLNMVpdfaeavVTGEDV 233
Cdd:PRK00466 105 -W------------------------LLN-EKGIK-VMVSGLADEESTsiGAKELVS--KGFNFKHI-------IVGEPS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 234 NTLTVAYEEYlqtakkigeaivegNTVTLQI--KGISAHGSTPEkgENAGLLLANFLTTVAldgkanafatfatetftgd 311
Cdd:PRK00466 149 NGTDIVVEYR--------------GSIQLDImcEGTPEHSSSAK--SNLIVDISKKIIEVY------------------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 312 ifgeKATIAYKDEVSGPLTVNVGRLSYTKENGGNLGLNVRYPVTTNFEEMIAKLKEYVgtHGFAVADYSNSRPHHVDKDH 391
Cdd:PRK00466 194 ----KQPENYDKPSIVPTIIRAGESYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKF--QECGLKIVDETPPVKVSINN 267
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300378381 392 VLIRTLQRVYEEQtGEKAELLAIGGGTYARSLKAG----VAFGPlfpGKEELAHQKDEYIEIEDLLKATAIYAQAIHEL 466
Cdd:PRK00466 268 PVVKALMRALLKQ-NIKPRLVRKAGTSDMNILQKIttsiATYGP---GNSMLEHTNQEKITLDEIYIAVKTYMLAIEEL 342
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
88-122 |
5.45e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 45.23 E-value: 5.45e-05
10 20 30
....*....|....*....|....*....|....*.
gi 300378381 88 HVDVVP-EGDGWTTPAYSADIRDGKIFARGAIDDKG 122
Cdd:PRK07906 73 HLDVVPaEAADWSVHPFSGEIRDGYVWGRGAVDMKD 108
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
88-130 |
9.97e-05 |
|
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: 44.64 E-value: 9.97e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 300378381 88 HVDVVPEG--DGWTTPAYSADIRDGKIFARGAIDDKGPTMAAYYA 130
Cdd:cd05677 79 HYDVIPAGetDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYA 123
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
77-466 |
1.06e-03 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 41.09 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 77 GQGEELVGILCHVDVVPeGDgwtTPAysaDIRDGKIFARGAIDDKGP--TMAAyyamkIVKELGLPLSKRVRMILGTDEE 154
Cdd:PRK04443 56 GDGPPLVLLLGHIDTVP-GD---IPV---RVEDGVLWGRGSVDAKGPlaAFAA-----AAARLEALVRARVSFVGAVEEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 155 SnwkcvdhyfkneemptigfapdadfpiinAEKGisdiqvvqngseekkgtyelvsfesGRRLNMVPDFAEAVVTGE--D 232
Cdd:PRK04443 124 A-----------------------------PSSG-------------------------GARLVADRERPDAVIIGEpsG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 233 VNTLTVAYEEYLqtakkigeaivegnTVTLQIKGISAHGSTPEkgENAGLLLANFLTTVAldgkanafATFATETFTGDI 312
Cdd:PRK04443 150 WDGITLGYKGRL--------------LVTYVATSESFHSAGPE--PNAAEDAIEWWLAVE--------AWFEANDGRERV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 313 FgekatiaykDEVSG-PLTVNVGRLSYTKEngGNLGLNVRYPVTTNFEEMIAKLKEYVGTHGFAVADysNSRPHHVDKDH 391
Cdd:PRK04443 206 F---------DQVTPkLVDFDSSSDGLTVE--AEMTVGLRLPPGLSPEEAREILDALLPTGTVTFTG--AVPAYMVSKRT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 392 VLIRTLQRVYEEQtgekaellaigGGTYARSLKAGVA----FGPLF--------PGKEELAHQKDEYIEIEDLLKATAIY 459
Cdd:PRK04443 273 PLARAFRVAIREA-----------GGTPRLKRKTGTSdmnvVAPAWgcpmvaygPGDSDLDHTPDEHLPLAEYLRAIAVL 341
|
....*..
gi 300378381 460 AQAIHEL 466
Cdd:PRK04443 342 TDVLERL 348
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
260-458 |
1.46e-03 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 40.50 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 260 VTLQIKGISAHGSTPEKGENAGLLLANFLTTVAldgkanafatfatetftgdifgekatiAYKdevsgPLTVNVGRLSY- 338
Cdd:cd05647 165 FKVTTHGVRAHSARSWLGENAIHKLAPILARLA---------------------------AYE-----PRTVNIDGLTYr 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 339 --------TKENGGN-------LGLNVRYPVTTNFEEMIAKLKEYVGTHG--FAVADYSNS-RPhhvDKDHVLIRTLQRV 400
Cdd:cd05647 213 eglnavfiSGGVAGNvipdearVNLNYRFAPDKSLAEAIAHVREVFEGLGyeIEVTDLSPGaLP---GLDHPVARDLIEA 289
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300378381 401 YEEQTGEK------AELLAIGggtyarslKAGVAFGPlfpGKEELAHQKDEYIEIEDLLKATAI 458
Cdd:cd05647 290 VGGKVRAKygwtdvARFSALG--------IPAVNFGP---GDPLLAHKRDEQVPVEQITACAAI 342
|
|
| M28_Pgcp_like |
cd03883 |
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate ... |
116-180 |
7.30e-03 |
|
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate carboxypeptidase (PGCP; blood plasma glutamate carboxypeptidase; EC 3.4.17.21) subfamily. PGCP is a 56kDa glutamate carboxypeptidase that is mainly produced in mammalian placenta and kidney, the majority of which is thought to be secreted into the bloodstream. Similar proteins are also found in other species, including bacteria. These proteins contain protease-associated (PA) domain inserts between the first and second strands of the central beta sheet in the protease-like domain. The PA domains may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. The exact physiological substrates of PGCP are unknown, although this enzyme may play an important role in the hydrolysis of circulating peptides. Its closest homolog encodes an important brain glutamate carboxypeptidase II (NAALADase) identical to the prostate-specific membrane antigen (PSMA), which serves as a marker for prostatic cancer metastasis. Hypermethylation of PGCP gene has been associated with human bronchial epithelial (HBE) cell immortalization and lung cancer. PGCP also provides an attractive target for serological analysis in hepatitis C virus (HCV)-induced hepatocellular carcinoma (HCC) patients.
Pssm-ID: 349879 [Multi-domain] Cd Length: 425 Bit Score: 38.44 E-value: 7.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300378381 116 GAIDDKGPTMAAYYAMKIVKELGLPLSKRVRMILGTDEESNWKCVDHYFKN--EEMPTIGFAPDADF 180
Cdd:cd03883 257 GAMDDGGGVAISWEALKLIKDLGLKPKRTIRVVLWTGEEQGLVGAKAYAEAhkDELENHVFAMESDI 323
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
259-373 |
8.64e-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: 35.78 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300378381 259 TVTLQIKGISAHGSTPEKGENAGLLLANFLTTVALDGKANAFATFATETFTGDIFGEKATiaykdevsgplTVNVGRLSy 338
Cdd:pfam07687 8 GGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGFDFPRTTLNITGIEGGTAT-----------NVIPAEAE- 75
|
90 100 110
....*....|....*....|....*....|....*
gi 300378381 339 tkenggnLGLNVRYPVTTNFEEMIAKLKEYVGTHG 373
Cdd:pfam07687 76 -------AKFDIRLLPGEDLEELLEEIEAILEKEL 103
|
|
| |
