|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
1-469 |
0e+00 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 924.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 1 MTTPQVIQQALAYFDSGRFRDVLARRVAIASESQRTDRDAALQQYLSEEIIPALQALGFELQQIDNPAAANRPFLIASRI 80
Cdd:PRK07079 1 MTREAAIARAAAYFDSGAFFADLARRVAYRTESQNPDRAPALRAYLTDEIAPALAALGFTCRIVDNPVAGGGPFLIAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 81 EDAALPTVLCYGHGDVVFGDDEHWSEGLSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQVFQARQGRLGFNCKWLFEM 160
Cdd:PRK07079 81 EDDALPTVLIYGHGDVVRGYDEQWREGLSPWTLTEEGDRWYGRGTADNKGQHTINLAALEQVLAARGGRLGFNVKLLIEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 161 GEEISSPGLAEVCRQHAQALQADLFIASDGPRLNAERPTLFLGSRGCVNFRLTIRARERDYHSGNWGGLLSNPGTQLANA 240
Cdd:PRK07079 161 GEEIGSPGLAEVCRQHREALAADVLIASDGPRLSAERPTLFLGSRGAVNFRLRVNLRDGAHHSGNWGGLLRNPGTVLAHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 241 IASLVNQHGQMQVAALKPPRLTPALRTILADIAPGGQATDPAIDPQWGEAGLSPSERLFGWNTLEVLSFLTGNPQRPMNA 320
Cdd:PRK07079 241 IASLVDARGRIQVPGLRPPPLPAAVRAALADITVGGGPGDPAIDPDWGEPGLTPAERVFGWNTLEVLAFKTGNPDAPVNA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 321 IPGHATAVCQLRFVVGTDWQQLAQHLRHHLDEHGFTMVEISDVRGTPATRLDPTDPLVNWTLDLMRQTSDKKPALLPNLG 400
Cdd:PRK07079 321 IPGSARAVCQLRFVVGTDWENLAPHLRAHLDAHGFPMVEVTVERGSPATRLDPDDPWVRWALASIARTTGKKPALLPNLG 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742461296 401 GSLPNEVFAEILGLPTLWIPHSYPACGQHAVDEHMLVSVAREGLQIMTRLFWELGEQGHAVLAQHRAHR 469
Cdd:PRK07079 401 GSLPNDVFADILGLPTLWVPHSYPACSQHAPNEHLLASVAREGLQIMAGLFWDLGEQGPALLAARRAHA 469
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
14-458 |
0e+00 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 686.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 14 FDSGRFRDVLARRVAIASESQRTDRDAALQQYLSEEIIPALQALGFELQQIDNPAAANRPFLIASRIEDAALPTVLCYGH 93
Cdd:cd05679 1 FDSGAFLAELARRVAVPTESQEPARKPELRAYLDQEMRPRFERLGFTVHIHDNPVAGRAPFLIAERIEDPSLPTLLIYGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 94 GDVVFGDDEHWSEGLSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQVFQARQGRLGFNCKWLFEMGEEISSPGLAEVC 173
Cdd:cd05679 81 GDVVPGYEGRWRDGRDPWTVTVWGERWYGRGTADNKGQHSINMAALRQVLEARGGKLGFNVKFLIEMGEEMGSPGLRAFC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 174 RQHAQALQADLFIASDGPRLNAERPTLFLGSRGCVNFRLTIRARERDYHSGNWGGLLSNPGTQLANAIASLVNQHGQMQV 253
Cdd:cd05679 161 FSHREALKADLFIASDGPRLAADRPTMFLGSRGGLNFELRVNLREGGHHSGNWGGLLANPGIILANAIASLVDGKGRIKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 254 AALKPPRLTPALRTILADIAPGGQATDPAIDPQWGEAGLSPSERLFGWNTLEVLSFLTGNPQRPMNAIPGHATAVCQLRF 333
Cdd:cd05679 241 PALKPAHLPNSVRSALADVEVGGGPDDPSIDPWWGEPGLTAAERVFGWNTLEVLAFKTGNPDAPVNAIPGHAEAICQIRF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 334 VVGTDWQQLAQHLRHHLDEHGFTMVEISDVRGT-PATRLDPTDPLVNWTLDLMRQTSDKKPALLPNLGGSLPNEVFAEIL 412
Cdd:cd05679 321 VVGTDPDTFIPAVRAHLDANGFDGVEVTASQMVfAATRLDPDSPWVGWALASLQKTTGKKPALLPNLGGSLPNDVFSEVL 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 742461296 413 GLPTLWIPHSYPACGQHAVDEHMLVSVAREGLQIMTRLFWELGEQG 458
Cdd:cd05679 401 GLPTLWVPHSYPACSQHAPNEHILAPVMREALRVMAGLFWDLGEDG 446
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
22-453 |
1.09e-114 |
|
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: 343.93 E-value: 1.09e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 22 VLARRVAIASESQRTDRDAALQqYLSEEIIPALQALGFELQQIDNPAAAnrPFLIASRIEDAALPTVLCYGHGDVVFGDD 101
Cdd:cd03893 3 TLAELVAIPSVSAQPDRREELR-RAAEWLADLLRRLGFTVEIVDTSNGA--PVVFAEFPGAPGAPTVLLYGHYDVQPAGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 102 EhWSEGLSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQVFQARQGrLGFNCKWLFEMGEEISSPGLAEVCRQHAQALQ 181
Cdd:cd03893 80 E-DGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGD-LPVNVKFIIEGEEESGSPSLDQLVEAHRDLLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 182 ADLFIASDGPRLNAERPTLFLGSRGCVNFRLTIRARERDYHSGNWGGLLSNPGTQLANAIASLVNQHGQMQVAALKPPrl 261
Cdd:cd03893 158 ADAIVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLDHDLHSGLYGGVVPDPMTALAQLLASLRDETGRILVPGLYDA-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 262 tpalrtiLADIAPGGQATDPAIDPQWGEAGL---SPSERLFGWNTLEVLSFLTG-NPQRPMNAIPGHATAVCQLRFVVGT 337
Cdd:cd03893 236 -------VRELPEEEFRLDAGVLEEVEIIGGttgSVAERLWTRPALTVLGIDGGfPGEGSKTVIPPRARAKISIRLVPGQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 338 DWQQLAQHLRHHLDEHG--FTMVEISDVRGTPATRLDPTDPLVNWTLDLMRQTSDKKPaLLPNLGGSLPN-EVFAEILGL 414
Cdd:cd03893 309 DPEEASRLLEAHLEKHApsGAKVTVSYVEGGMPWRSDPSDPAYQAAKDALRTAYGVEP-PLTREGGSIPFiSVLQEFPQA 387
|
410 420 430
....*....|....*....|....*....|....*....
gi 742461296 415 PTLWIPHSYPACGQHAVDEHMLVSVAREGLQIMTRLFWE 453
Cdd:cd03893 388 PVLLIGVGDPDDNAHSPNESLRLGNYKEGTQAEAALLYS 426
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
8-456 |
6.76e-76 |
|
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: 242.87 E-value: 6.76e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 8 QQALAYFDSGR--FRDVLARRVAIASESqrtDRDAALQQYLSEEiipaLQALGFELQQIDNPAaaNRPFLIASRIEDAAL 85
Cdd:COG0624 1 AAVLAAIDAHLdeALELLRELVRIPSVS---GEEAAAAELLAEL----LEALGFEVERLEVPP--GRPNLVARRPGDGGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 86 PTVLCYGHGDVVF-GDDEHWSEGlsPWQLVEQAGRWYGRGSADNKGQHSINIAALEQvFQARQGRLGFNCKWLFEMGEEI 164
Cdd:COG0624 72 PTLLLYGHLDVVPpGDLELWTSD--PFEPTIEDGRLYGRGAADMKGGLAAMLAALRA-LLAAGLRLPGNVTLLFTGDEEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 165 SSPGLAEVCRQHAQALQADLFIASDGPRLnaerPTLFLGSRGCVNFRLTIRARERdyHSGNWgGLLSNPGTQLANAIASL 244
Cdd:COG0624 149 GSPGARALVEELAEGLKADAAIVGEPTGV----PTIVTGHKGSLRFELTVRGKAA--HSSRP-ELGVNAIEALARALAAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 245 vnqhgqmqvAALKPPRltpalrtiladiapggqatdpaidpqwgeaglsPSERLFGWNTLEVLSFLTGNpqrPMNAIPGH 324
Cdd:COG0624 222 ---------RDLEFDG---------------------------------RADPLFGRTTLNVTGIEGGT---AVNVIPDE 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 325 ATAVCQLRFVVGTDWQQLAQHLRHHLDEHGF-TMVEISDV-RGTPATRLDPTDPLVNWTLDLMRQTSDKKPALLPnLGGS 402
Cdd:COG0624 257 AEAKVDIRLLPGEDPEEVLAALRALLAAAAPgVEVEVEVLgDGRPPFETPPDSPLVAAARAAIREVTGKEPVLSG-VGGG 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 742461296 403 LPNEVFAEILGLPTLWIPHSYPAcGQHAVDEHMLVSVAREGLQIMTRLFWELGE 456
Cdd:COG0624 336 TDARFFAEALGIPTVVFGPGDGA-GAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
29-454 |
1.75e-56 |
|
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: 193.68 E-value: 1.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 29 IASESQRTD--RDAAlqqylsEEIIPALQALGFELQQIDNPAAAnrPFLIASRIEDAALPTVLCYGHGDVVFGDDEH-WS 105
Cdd:cd05680 13 VSADPAHKGdvRRAA------EWLADKLTEAGFEHTEVLPTGGH--PLVYAEWLGAPGAPTVLVYGHYDVQPPDPLElWT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 106 EGlsPWQLVEQAGRWYGRGSADNKGQHSINIAALEQVFQARqGRLGFNCKWLFEMGEEISSPGLAEVCRQHAQALQADLF 185
Cdd:cd05680 85 SP--PFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVE-GALPVNVKFLIEGEEEIGSPSLPAFLEENAERLAADVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 186 IASDGPRLNAERPTLFLGSRGCVNFRLTIRARERDYHSGNWGGLLSNPGTQLANAIASLVNQHGQMQVAALKPP--RLTP 263
Cdd:cd05680 162 LVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNRDLHSGSYGGAVPNPANALARLLASLHDEDGRVAIPGFYDDvrPLTD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 264 ALRTILADIaPGGQAT---DPAIDPQWGEAGLSPSERLFGWNTLEVlSFLTGNPQRP--MNAIPGHATAVCQLRFVVGTD 338
Cdd:cd05680 242 AEREAWAAL-PFDEAAfkaSLGVPALGGEAGYTTLERLWARPTLDV-NGIWGGYQGEgsKTVIPSKAHAKISMRLVPGQD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 339 WQQLAQHLRHHLDEH---GFTmVEISDVRGTPATRLDPTDPLVNWTLDLMRQTSDKKPALLPNlGGSLP-NEVFAEILGL 414
Cdd:cd05680 320 PDAIADLLEAHLRAHappGVT-LSVKPLHGGRPYLVPTDHPALQAAERALEEAFGKPPVFVRE-GGSIPiVALFEKVLGI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 742461296 415 PTLWIPHSYPACGQHAVDEHMLVSVAREGLQIMTRLFWEL 454
Cdd:cd05680 398 PTVLMGFGLPDDAIHAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
53-437 |
8.58e-54 |
|
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: 186.39 E-value: 8.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 53 ALQALGFELQQIDNPAAanrPFLIASrIEDAALPTVLCYGHGDVVFGD-DEHWSEglSPWQLVEQAGRWYGRGSADNKGQ 131
Cdd:cd05681 31 FLRRLGAEVEIFETDGN---PIVYAE-FNSGDAKTLLFYNHYDVQPAEpLELWTS--DPFELTIRNGKLYARGVADDKGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 132 HSINIAALEQVfQARQGRLGFNCKWLFEMGEEISSPGLAEVCRQHAQALQADLFIASDGPRLNAERPTLFLGSRGCVNFR 211
Cdd:cd05681 105 LMARLAALRAL-LQHLGELPVNIKFLVEGEEEVGSPNLEKFVAEHADLLKADGCIWEGGGKNPKGRPQISLGVKGIVYVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 212 LTIRARERDYHSgNWGGLLSNPGTQLANAIASLVNQHGQMQVAAL----KPPrlTPALRTILADIAPGGQA--TDPAIDP 285
Cdd:cd05681 184 LRVKTADFDLHS-SYGAIVENPAWRLVQALNSLRDEDGRVLIPGFyddvRPL--SEAERALIDTYDFDPEElrKTYGLKR 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 286 QWGEAGLSPSERLFGWNTLEVLSFLTG-NPQRPMNAIPGHATAVCQLRFVVGTDWQQLAQHLRHHLDEHGFTMVEISDVR 364
Cdd:cd05681 261 PLQVEGKDPLRALFTEPTCNINGIYSGyTGEGSKTILPSEAFAKLDFRLVPDQDPAKILSLLRKHLDKNGFDDIEIHDLL 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742461296 365 GTPATRLDPTDPLVNWTLDLMRQTSDKKPALLPNLGGSLPNEVFAEILGLPTLWIPHSYPACGQHAVDEHMLV 437
Cdd:cd05681 341 GEKPFRTDPDAPFVQAVIESAKEVYGQDPIVLPNSAGTGPMYPFYDALEVPVVAIGVGNAGSNAHAPNENIRI 413
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
31-456 |
1.53e-44 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 162.22 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 31 SESQRTDRDAAlqqylsEEIIPALQALGFElqQIDNPAAANRPFLIASRIEDAALPTVLCYGHGDVVFGDDEHWSEGlSP 110
Cdd:PRK08201 33 SEHKEDVRKAA------EWLAGALEKAGLE--HVEIMETAGHPIVYADWLHAPGKPTVLIYGHYDVQPVDPLNLWET-PP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 111 WQLVEQAGRWYGRGSADNKGQHSINIAALEQVFQArQGRLGFNCKWLFEMGEEISSPGLAEVCRQHAQALQADLFIASDG 190
Cdd:PRK08201 104 FEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKV-EGTLPVNVKFCIEGEEEIGSPNLDSFVEEEKDKLAADVVLISDT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 191 PRLNAERPTLFLGSRGCVNFRLTIRARERDYHSGNWGGLLSNPGTQLANAIASLVNQHGQMQVAAL--KPPRLTPALRTI 268
Cdd:PRK08201 183 TLLGPGKPAICYGLRGLAALEIDVRGAKGDLHSGLYGGAVPNALHALVQLLASLHDEHGTVAVEGFydGVRPLTPEEREE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 269 LADIAPGGQA--TDPAIDPQWGEAGLSPSERLFGWNTLEVLSFLTG-NPQRPMNAIPGHATAVCQLRFVVGTDWQQLAQH 345
Cdd:PRK08201 263 FAALGFDEEKlkRELGVDELFGEEGYTALERTWARPTLELNGVYGGfQGEGTKTVIPAEAHAKITCRLVPDQDPQEILDL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 346 LRHHLDEHGFTMVEISDVR--GTPATRLDPTDPLVNWTLDLMRQTSDkKPALLPNLGGSLP-NEVFAEILGLPTLWIPHS 422
Cdd:PRK08201 343 IEAHLQAHTPAGVRVTIRRfdKGPAFVAPIDHPAIQAAARAYEAVYG-TEAAFTRMGGSIPvVETFSSQLHIPIVLMGFG 421
|
410 420 430
....*....|....*....|....*....|....
gi 742461296 423 YPACGQHAVDEHMLVSVAREGLQIMTRLFWELGE 456
Cdd:PRK08201 422 LPSENFHAPNEHFHLENFDKGLRTLVEYWHQLAE 455
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
53-450 |
1.84e-39 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 148.40 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 53 ALQALGFELQQIDNpaaANRPFLIASRIEDAALPTVLCYGHGDVVFGDDEHWSEGlSPWQLV----EQAGRW-------- 120
Cdd:cd05678 31 AFRKRGFKTSQLPT---SGLPLLLAEKPISDARKTVLFYMHLDGQPVDPSKWDQK-SPYTPVlkrkDAAGNWeeinwdai 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 121 ----------YGRGSADNKGQHSINIAALEqVFQARQGRLGFNCKWLFEMGEEISSPGLAEVCRQHAQALQADLFIASDG 190
Cdd:cd05678 107 fsnldpewrvFARAAADDKGPIMMMLAALD-ALKAGGIAPKFNVKIILDSEEEKGSPSLPKAVKEYKELLAADALIIMDG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 191 PRLNAERPTLFLGSRGCVNFRLTIRARERDYHSGNWGGLLSNPGTQLANAIASLVNQHGQMQVAALKPP-RLTPALRTIL 269
Cdd:cd05678 186 PAHATNKPTLTFGCRGIATATLTTYGAKVPQHSGHYGNYAPNPAFRLSSLLASMKDDTGKVTIPGFYDGiSIDEETQKIL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 270 ADIAPGGQATDPAIdpqwgeaGLSPSERLfGWNTLEVLSFLTGNPQ---------RPMNAIPGHATAVCQLRFVVGTDWQ 340
Cdd:cd05678 266 AAVPDDEESINKRL-------GIAQTDKV-GRNYQEALQYPSLNVRgmesgwkgdKVRTIIPEIAEAEIDIRLVPESDGP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 341 QLAQHLRHHLDEHGF----------------TMVEISDVRGTPATRLDPTDPLVNWTLDLMRQTSDKKPALLPNLGGSLP 404
Cdd:cd05678 338 YLLDLVKAHIEKQGYfvtdraptdeerlahdKIAKFTYRNGADAFRTDINSPIGNWLRKALTDEFGEEPIQIRMMGGTVP 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 742461296 405 NEVFAEILGLPTLWIPHSYPACGQHAVDEHMLVSVAREGLQIMTRL 450
Cdd:cd05678 418 IAPFVNVLDIPAIIVPMVNMDNNQHSPNENLRIGNIRTGIRTCYAI 463
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
18-433 |
2.37e-34 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 133.88 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 18 RFRDVLARRVAIASESQRTDRDAALQQyLSEEIIPALQALGF-ELQQIDNPAAanrPFLIASRIEDAALPTVLCYGHGDV 96
Cdd:PRK07907 19 RVRADLEELVRIPSVAADPFRREEVAR-SAEWVADLLREAGFdDVRVVSADGA---PAVIGTRPAPPGAPTVLLYAHHDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 97 V-FGDDEHWSEglSPWQLVEQAGRWYGRGSADNKGQHSINIAALeqvfQARQGRLGFNCKWLFEMGEEISSPGLAEVCRQ 175
Cdd:PRK07907 95 QpPGDPDAWDS--PPFELTERDGRLYGRGAADDKGGIAMHLAAL----RALGGDLPVGVTVFVEGEEEMGSPSLERLLAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 176 HAQALQADLFIASDGPRLNAERPTLFLGSRGCVNFRLTIRARERDYHSGNWGGLLSNPGTQLANAIASLVNQHGQMQVAA 255
Cdd:PRK07907 169 HPDLLAADVIVIADSGNWSVGVPALTTSLRGNADVVVTVRTLEHAVHSGQFGGAAPDALTALVRLLATLHDEDGNVAVDG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 256 LkpprltpalrtiladiAPGGQATDPAIDPQW--GEAGL----------SPSERLFGWNTLEVLSFLTGNPQRPMNAIPG 323
Cdd:PRK07907 249 L----------------DATEPWLGVDYDEERfrADAGVldgveligtgSVADRLWAKPAITVIGIDAPPVAGASNALPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 324 HATAVCQLRFVVGTDWQQLAQHLRHHLDEH---GfTMVEISDVRGTPATRLDPTDPLVNWTLDLMRQTSDKKPALLpNLG 400
Cdd:PRK07907 313 SARARLSLRVAPGQDAAEAQDALVAHLEAHapwG-AHVTVERGDAGQPFAADASGPAYDAARAAMREAWGKDPVDM-GMG 390
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 742461296 401 GSLP-----NEVF--AEIL--GLptlwiphSYPACGQHAVDE 433
Cdd:PRK07907 391 GSIPfiaelQEAFpqAEILvtGV-------EDPKTRAHSPNE 425
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
19-272 |
8.62e-26 |
|
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: 109.61 E-value: 8.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 19 FRDVLARRVAIASESQRTDRDAALQ---QYLSEEiipaLQALGF--ELQQI------DNPAAANRPFLIASRIEDAALPT 87
Cdd:cd05676 12 FIERLREAVAIQSVSADPEKRPELIrmmEWAAER----LEKLGFkvELVDIgtqtlpDGEELPLPPVLLGRLGSDPSKKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 88 VLCYGHGDVVFGDDE-HW-SEglsPWQLVEQAGRWYGRGSADNKGQHSINIAALEqVFQARQGRLGFNCKWLFEMGEEIS 165
Cdd:cd05676 88 VLIYGHLDVQPAKLEdGWdTD---PFELTEKDGKLYGRGSTDDKGPVLGWLNAIE-AYQKLGQELPVNLKFCFEGMEESG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 166 SPGLAEVCRQHAQALQADL-FIA-SDGPRLNAERPTLFLGSRGCVNFRLTIRARERDYHSGNWGGLLSNPGTQLANAIAS 243
Cdd:cd05676 164 SEGLDELIEARKDTFFSDVdYVCiSDNYWLGKKKPCLTYGLRGICYFFIEVEGPNKDLHSGVFGGSVHEPMTDLIALMSS 243
|
250 260 270
....*....|....*....|....*....|...
gi 742461296 244 LVNQHGQMQVA----ALKPprLTPALRTILADI 272
Cdd:cd05676 244 LVDSDGKILIPgiydAVAP--LTEEEWELYEKI 274
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
87-454 |
1.82e-25 |
|
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: 108.20 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 87 TVLCYGHGDVVFGDDE-HWSEglSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQVFQarQGRLGFNCKWLFEMGEEIS 165
Cdd:cd05677 73 RILFYGHYDVIPAGETdGWDT--DPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQ--EGELDNDVVFLIEGEEESG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 166 SPGLAEVCRQHAQALQA-DLFIASDGPRLNAERPTLFLGSRGCVNFRLTIRARERDYHSGNWGGLLSNPGTQLANAIASL 244
Cdd:cd05677 149 SPGFKEVLRKNKELIGDiDWILLSNSYWLDDNIPCLNYGLRGVIHATIVVSSDKPDLHSGVDGGVLREPTADLIKLLSKL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 245 VNQHGQMQV----AALKPprLTPALRTILADIAPGGQatdpaIDPQWgeaglsPSERLFGWNTLEVLSFLTGNPQRPMNA 320
Cdd:cd05677 229 QDPDGRILIphfyDPVKP--LTEAERARFTAIAETAL-----IHEDT------TVDSLIAKWRKPSLTVHTVKVSGPGNT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 321 --IPGHATAVCQLRFVVGTDWQQLAQHLRHHLDEHGFTM-----VEISdVRGTPATRL-DPTDPLVNWTLDLMRQTSDKK 392
Cdd:cd05677 296 tvIPKSASASVSIRLVPDQDLDVIKQDLTDYIQSCFAELksqnhLDIE-VLNEAEPWLgDPDNPAYQILREAVTAAWGVE 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742461296 393 PaLLPNLGGSLPNEVFAE-ILGLPTLWIPhsypaCGQ-----HAVDEHMLVSVAREGLQIMTRLFWEL 454
Cdd:cd05677 375 P-LYIREGGSIPTIRFLEkEFNAPAVQLP-----CGQssdnaHLDNERLRIKNLYKMREILSRVFNRL 436
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
7-419 |
2.34e-24 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 105.37 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 7 IQQALAYFDSGrFRDVLARRVA---IASESqrTD-------RDAAlqQYLSEEiipaLQALGFELQQIDNPAaanRPFLI 76
Cdd:PRK09104 5 LDPVLDHIDAN-LDASLERLFAllrIPSIS--TDpayaadcRKAA--DWLVAD----LASLGFEASVRDTPG---HPMVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 77 A-SRIEDAALPTVLCYGHGDVVFGDD-EHW-SEGLSPwQLVEQA-GR--WYGRGSADNKGQHSINIAALeQVFQARQGRL 150
Cdd:PRK09104 73 AhHEGPTGDAPHVLFYGHYDVQPVDPlDLWeSPPFEP-RIKETPdGRkvIVARGASDDKGQLMTFVEAC-RAWKAVTGSL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 151 GFNCKWLFEMGEEISSPGLAEVCRQHAQALQADLFIASDGPRLNAERPTLFLGSRGCVNFRLTIRARERDYHSGNWGGLL 230
Cdd:PRK09104 151 PVRVTILFEGEEESGSPSLVPFLEANAEELKADVALVCDTGMWDRETPAITTSLRGLVGEEVTITAADRDLHSGLFGGAA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 231 SNPGTQLANAIASLVNQHGqmqvaalkpprltpalRTILADIAPGGQATDPAIDPQW-----------GEAGLS-PS-ER 297
Cdd:PRK09104 231 ANPIRVLTRILAGLHDETG----------------RVTLPGFYDGVEELPPEILAQWkalgftaeaflGPVGLSiPAgEK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 298 lfGWNTLEVLSfltgnpQRP---MNA-------------IPGHATAVCQLRFVVGTDWQQLAQHLRHHLDEH--GFTMVE 359
Cdd:PRK09104 295 --GRSVLEQIW------SRPtceINGiwggytgegfktvIPAEASAKVSFRLVGGQDPAKIREAFRAYVRARlpADCSVE 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742461296 360 ISDVRGTPATRLDPTDPLVNWTLDLMrqtSDK--KPALLPNLGGSLP-NEVFAEILGLPTLWI 419
Cdd:PRK09104 367 FHDHGGSPAIALPYDSPALAAAKAAL---SDEwgKPAVLIGSGGSIPiVGDFKRILGMDSLLV 426
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
91-453 |
2.19e-23 |
|
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: 100.11 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 91 YGHGDVVF-GDDEHWseglsPWQLVEqAGRWYGRGSADNKGQHSINIAALEQVfqARQGRLGFNCKWLFEMGEEISSPGL 169
Cdd:pfam01546 3 RGHMDVVPdEETWGW-----PFKSTE-DGKLYGRGHDDMKGGLLAALEALRAL--KEEGLKKGTVKLLFQPDEEGGMGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 170 AEVCRQHA-QALQADLFIA---SDGPRLNAE-RPTLFLGSRGCVNFRLTIRARERdyHSGNWgGLLSNPGTQLANAIASL 244
Cdd:pfam01546 75 RALIEDGLlEREKVDAVFGlhiGEPTLLEGGiAIGVVTGHRGSLRFRVTVKGKGG--HASTP-HLGVNAIVAAARLILAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 245 VNQHGQmQVAALKPPRLTpalrTILADIAPGGQatdpaidpqwgeaglspserlfgwntlevlsfltgnpqrpmNAIPGH 324
Cdd:pfam01546 152 QDIVSR-NVDPLDPAVVT----VGNITGIPGGV-----------------------------------------NVIPGE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 325 ATAVCQLRFVVGTDWQQLAQHLRHHLDEHG---FTMVEISDVRGTPATRLDpTDPLVNWTLDLMRQTSDKKPALLPnlGG 401
Cdd:pfam01546 186 AELKGDIRLLPGEDLEELEERIREILEAIAaayGVKVEVEYVEGGAPPLVN-DSPLVAALREAAKELFGLKVELIV--SG 262
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 742461296 402 SLPNEVFAEIL-GLPT---LWIPHSYPAcgqHAVDEHMLVSVAREGLQIMTRLFWE 453
Cdd:pfam01546 263 SMGGTDAAFFLlGVPPtvvFFGPGSGLA---HSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
54-414 |
4.12e-22 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 98.29 E-value: 4.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 54 LQALGFELQQIDNPAaanRPFLIAsRIEDAALPTVLCYGHGDVVFGDD-EHWSEglSPWQLVEQAGRWYGRGSADNKGQH 132
Cdd:PRK06446 35 MEKLGIKANIERTKG---HPVVYG-EINVGAKKTLLIYNHYDVQPVDPlSEWKR--DPFSATIENGRIYARGASDNKGTL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 133 SINIAALEQVFqaRQGRLGFNCKWLFEMGEEISSPGLAEVCRQHAQALQADLFIASDGPRLNAERPTLFLGSRGCVNFRL 212
Cdd:PRK06446 109 MARLFAIKHLI--DKHKLNVNVKFLYEGEEEIGSPNLEDFIEKNKNKLKADSVIMEGAGLDPKGRPQIVLGVKGLLYVEL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 213 TIRARERDYHSGNwGGLLSNPGTQLANAIASLVNQHGQMQVAAL--KPPRLTPALRTILADIAPGGQATDPAI--DPQWG 288
Cdd:PRK06446 187 VLRTGTKDLHSSN-APIVRNPAWDLVKLLSTLVDGEGRVLIPGFydDVRELTEEERELLKKYDIDVEELRKALgfKELKY 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 289 EAGLSPSERLFGWNTLEVLSFLTG-NPQRPMNAIPGHATAVCQLRFVVGTDWQQLAQHLRHHLDEHGFTmVEISDVRGTP 367
Cdd:PRK06446 266 SDREKIAEALLTEPTCNIDGFYSGyTGKGSKTIVPSRAFAKLDFRLVPNQDPYKIFELLKKHLQKVGFN-GEIIVHGFEY 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 742461296 368 ATRLDPTDPLVNWTLDLMRQTSDKKPALLPNLGGSLPNEVFAEILGL 414
Cdd:PRK06446 345 PVRTSVNSKVVKAMIESAKRVYGTEPVVIPNSAGTQPMGLFVYKLGI 391
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
20-450 |
3.09e-19 |
|
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: 89.73 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 20 RDVLARRVAIASE--SQRTDRDAALQQYLSEEiipaLQALGFELQQIDNPAAANRPFLIAsRIE--DAALPTVLCYGHGD 95
Cdd:cd05675 1 VDLLQELIRIDTTnsGDGTGSETRAAEVLAAR----LAEAGIQTEIFVVESHPGRANLVA-RIGgtDPSAGPLLLLGHID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 96 VVFGDDEHWSEglSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQVfqARQG-RLGFNCKWLFEMGEEISSPGLAEVCR 174
Cdd:cd05675 76 VVPADASDWSV--DPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHY--KREGfKPKRDLVFAFVADEEAGGENGAKWLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 175 QHAQAL--QADLFIA-SDGPRLNAERPTLFL----GSRGCVNFRLTIRARerdyhsgnwGGLLSNPGTQlaNAIASL--- 244
Cdd:cd05675 152 DNHPELfdGATFALNeGGGGSLPVGKGRRLYpiqvAEKGIAWMKLTVRGR---------AGHGSRPTDD--NAITRLaea 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 245 VNQHGQMQVaalkPPRLTP--ALRTILADIAPG--GQATDPAIDPQWGE-AGLSPSERLfgwntLEVLSFLTGNPQ---- 315
Cdd:cd05675 221 LRRLGAHNF----PVRLTDetAYFAQMAELAGGegGALMLTAVPVLDPAlAKLGPSAPL-----LNAMLRNTASPTmlda 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 316 -RPMNAIPGHATAVCQLRFVVGTDWQQLAQHLRHHLdehGFTMVEISDVRGTPATRLDPTDPLVNwTLDLMRQTSDKKPA 394
Cdd:cd05675 292 gYATNVLPGRATAEVDCRILPGQSEEEVLDTLDKLL---GDPDVSVEAVHLEPATESPLDSPLVD-AMEAAVQAVDPGAP 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742461296 395 LLPN-LGGSLPNEVFAEiLGLPT-----LWIPHSYPACGQ-HAVDEHMLVSVAREGLQIMTRL 450
Cdd:cd05675 368 VVPYmSPGGTDAKYFRR-LGIPGygfapLFLPPELDYTGLfHGVDERVPVESLYFGVRFLDRL 429
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
21-451 |
5.79e-19 |
|
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: 88.13 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 21 DVLARRVAIASESqrtDRDAALQQYLSEEiipaLQALGFelqQIDNPAAANRPFLIASRiEDAALPTVLCYGHGDVV-FG 99
Cdd:cd08659 1 SLLQDLVQIPSVN---PPEAEVAEYLAEL----LAKRGY---GIESTIVEGRGNLVATV-GGGDGPVLLLNGHIDTVpPG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 100 DDEHWSegLSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQVFQAR---QGRLGFnckwLFEMGEEISSPGLAEVCrQH 176
Cdd:cd08659 70 DGDKWS--FPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGallGGRVAL----LATVDEEVGSDGARALL-EA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 177 AQALQADLFIasdgprlNAErPT---LFLGSRGCVNFRLTIRARERdyHSgnwggllSNPGTQlANAIASLVnqhgqmqv 253
Cdd:cd08659 143 GYADRLDALI-------VGE-PTgldVVYAHKGSLWLRVTVHGKAA--HS-------SMPELG-VNAIYALA-------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 254 aalkppRLTPALRTILADIAPggqatdpaiDPQWGEAGLSPSERLFGWNTlevlsfltgnpqrpmNAIPGHATAVCQLRF 333
Cdd:cd08659 197 ------DFLAELRTLFEELPA---------HPLLGPPTLNVGVINGGTQV---------------NSIPDEATLRVDIRL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 334 VVGTDWQQLAQHLRHHLDEHG--FTMVEISDvrGTPATRLDPTDPLVNWTLDLMRQTSdkKPALLPNLGGSLPNEVFAEI 411
Cdd:cd08659 247 VPGETNEGVIARLEAILEEHEakLTVEVSLD--GDPPFFTDPDHPLVQALQAAARALG--GDPVVRPFTGTTDASYFAKD 322
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 742461296 412 LGLPTL-WIPhsYPACGQHAVDEHMLVSVAREGLQIMTRLF 451
Cdd:cd08659 323 LGFPVVvYGP--GDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
15-454 |
8.37e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 70.03 E-value: 8.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 15 DSGRFRDVLARRVAI---ASESQRTDrdaalqqyLSEEIIPALQALGFELQQID-NPAAANRPFLIAS-RIEDAALPTVL 89
Cdd:PRK09133 35 DQQAARDLYKELIEInttASTGSTTP--------AAEAMAARLKAAGFADADIEvTGPYPRKGNLVARlRGTDPKKPILL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 90 CyGHGDVVFGDDEHWSEglSPWQLVEQAGRWYGRGSADNKGQHSINIAALeqvfqARQGRLGF----NCKWLFEMGEE-- 163
Cdd:PRK09133 107 L-AHMDVVEAKREDWTR--DPFKLVEENGYFYGRGTSDDKADAAIWVATL-----IRLKREGFkpkrDIILALTGDEEgt 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 164 --ISSPGLAEvcrQHAQALQADLFI--ASDGPRLNAERPTLF---LGSRGCVNFRLTIRarerdyhsgNWGGLLSNPGTQ 236
Cdd:PRK09133 179 pmNGVAWLAE---NHRDLIDAEFALneGGGGTLDEDGKPVLLtvqAGEKTYADFRLEVT---------NPGGHSSRPTKD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 237 laNAIASLVNqhGQMQVAALK-PPRLTPALRTILADIAP--GGQ--------ATDPAiDPQwgEAGLSPSERLfgWN--- 302
Cdd:PRK09133 247 --NAIYRLAA--ALSRLAAYRfPVMLNDVTRAYFKQSAAieTGPlaaamrafAANPA-DEA--AIALLSADPS--YNaml 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 303 -TLEVLSFLTGNpqRPMNAIPGHATAVCQLRFVVGTDWQQLAQHLRHHLDEHGFTMVEISDVRGTPATRLDPtdplvnwt 381
Cdd:PRK09133 318 rTTCVATMLEGG--HAENALPQRATANVNCRIFPGDTIEAVRATLKQVVADPAIKITRIGDPSPSPASPLRP-------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 382 lDLMRQTSDKKPALLPNL--------GGSlpNEVFAEILGLPTLWIPHSYPACGQ---HAVDEHMLVSVAREGLQIMTRL 450
Cdd:PRK09133 388 -DIMKAVEKLTAAMWPGVpvipsmstGAT--DGRYLRAAGIPTYGVSGLFGDPDDtfaHGLNERIPVASFYEGRDFLYEL 464
|
....
gi 742461296 451 FWEL 454
Cdd:PRK09133 465 VKDL 468
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
21-241 |
1.18e-12 |
|
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: 69.16 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 21 DVLARRVAIASESQRTDrdAALQQYLSEEiipaLQALGFELQQIDNPAAaNRPFLIAsRIEDAALPTVLCYGHGDVVFGD 100
Cdd:cd03894 1 ELLARLVAFDTVSRNSN--LALIEYVADY----LAALGVKSRRVPVPEG-GKANLLA-TLGPGGEGGLLLSGHTDVVPVD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 101 DEHWSEglSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQVFQARQGR-LGFnckwLFEMGEEIS---SPGLAEvcRQH 176
Cdd:cd03894 73 GQKWSS--DPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKpLHL----AFSYDEEVGclgVRHLIA--ALA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 742461296 177 AQALQADLFIAsdgprlnAErPTLF---LGSRGCVNFRLTIRARERdyHSgnwggllSNPgTQLANAI 241
Cdd:cd03894 145 ARGGRPDAAIV-------GE-PTSLqpvVAHKGIASYRIRVRGRAA--HS-------SLP-PLGVNAI 194
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
21-225 |
9.47e-12 |
|
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: 66.46 E-value: 9.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 21 DVLARRVAIASESqrtdRDAALQQYLSEEIIPALQALGFELQQIDNPAAANRpfLIAsRIEDAALPTVLCYGHGDVVFGD 100
Cdd:cd03885 3 DLLERLVNIESGT----YDKEGVDRVAELLAEELEALGFTVERRPLGEFGDH--LIA-TFKGTGGKRVLLIGHMDTVFPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 101 DEHWSEGLSpwqlvEQAGRWYGRGSADNKGQHSINIAALEQvFQARQGRLGFNCKWLFEMGEEISSPGLAEVCRQHAQal 180
Cdd:cd03885 76 GTLAFRPFT-----VDGDRAYGPGVADMKGGLVVILHALKA-LKAAGGRDYLPITVLLNSDEEIGSPGSRELIEEEAK-- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 742461296 181 QADLFIASDGPRLNAErptLFLGSRGCVNFRLTIRARERdyHSGN 225
Cdd:cd03885 148 GADYVLVFEPARADGN---LVTARKGIGRFRLTVKGRAA--HAGN 187
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
36-440 |
1.04e-09 |
|
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE; aspartyl dipeptidase; succinyl-diaminopimelate desuccinylase) subfamily. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from Escherichia coli and Haemophilus influenzae, while the genes that encode for DapEs have been sequenced from several bacterial sources such as Corynebacterium glutamicum, Helicobacter pylori, Neisseria meningitidis and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme that requires two zinc atoms per molecule for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349886 [Multi-domain] Cd Length: 366 Bit Score: 59.83 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 36 TDRDAALQQYLSEeiipALQALGFELQQIDNPAAANrpfLIASRIEDaalPTVLCY-GHGDVV-FGDDEHWSegLSPWQL 113
Cdd:cd03891 14 TPDDAGAQDLIAE----RLKALGFTCERLEFGGVKN---LWARRGTG---GPHLCFaGHTDVVpPGDLEGWS--SDPFSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 114 VEQAGRWYGRGSADNKGQHSINIAALEQVFQAR---QGRLGFnckwLFEMGEEISSP-GLAEVCrqhaQALQAdlfiasd 189
Cdd:cd03891 82 TIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHpnhKGSISF----LITSDEEGPAIdGTKKVL----EWLKA------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 190 gprlNAERPTLFL----------------GSRGCVNFRLTIRarerdyhsgnwggllsnpGTQ-------LA-NAIaslv 245
Cdd:cd03891 147 ----RGEKIDYCIvgeptsekklgdtikiGRRGSLNGKLTIK------------------GKQghvayphLAdNPI---- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 246 nqhgqmqvaalkpPRLTPALRTILAdiapggqatdpaidPQW--GEAGLSPSerlfgwnTLEVLSFLTGNPQRpmNAIPG 323
Cdd:cd03891 201 -------------HLLAPILAELTA--------------TVLdeGNEFFPPS-------SLQITNIDVGNGAT--NVIPG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 324 HATAVCQLRFVVGTDWQQLAQHLRHHLDEHGFTM-VEISdVRGTPAtrLDPTDPLVNWTLDLMRQTSDKKPALLpNLGG- 401
Cdd:cd03891 245 ELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYdLEWK-LSGEPF--LTKPGKLVDAVSAAIKEVTGITPELS-TSGGt 320
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 742461296 402 -------SLPNEVfAEiLGLPTLWIphsypacgqHAVDEHmlVSVA 440
Cdd:cd03891 321 sdarfiaSYGCPV-VE-FGLVNATI---------HKVNER--VSVA 353
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
20-130 |
1.17e-07 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 53.65 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 20 RDVLARRVAIASESQRTDRD--AALQQYLseeiipalQALGFELQQIDNPAA--ANrpfLIAsRIEDAALPTVLCYGHGD 95
Cdd:PRK07522 7 LDILERLVAFDTVSRDSNLAliEWVRDYL--------AAHGVESELIPDPEGdkAN---LFA-TIGPADRGGIVLSGHTD 74
|
90 100 110
....*....|....*....|....*....|....*
gi 742461296 96 VVFGDDEHWSegLSPWQLVEQAGRWYGRGSADNKG 130
Cdd:PRK07522 75 VVPVDGQAWT--SDPFRLTERDGRLYGRGTCDMKG 107
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
71-233 |
1.98e-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: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 71 NRPFLIASRIE--DAALPTVLCYGHGDvvfgDDEH---WSEGLSPWQLVEQAGRWYGRGSADNKgqHSI--NIAALE--Q 141
Cdd:cd05682 57 GRTPLLFVEIPgtEQDDDTVLLYGHMD----KQPPftgWDEGLGPTKPVIRGDKLYGRGGADDG--YAIfaSLTAIKalQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 142 VFQARQGRlgfnCKWLFEMGEEISS---PGLAEVCRQHAQALqaDLFIASDGPRLNAErpTLFLGS--RGCVNFRLTIRA 216
Cdd:cd05682 131 EQGIPHPR----CVVLIEACEESGSadlPFYLDKLKERIGNV--DLVVCLDSGCGNYE--QLWLTTslRGVLGGDLTVQV 202
|
170
....*....|....*..
gi 742461296 217 RERDYHSGNWGGLLSNP 233
Cdd:cd05682 203 LNEGVHSGDASGIVPSS 219
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
36-152 |
2.10e-07 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 52.78 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 36 TDRDAALQQYLSEeiipALQALGFELQ-----QIDNpaaanrpfLIASRIEDAalpTVLCY-GHGDVV-FGDDEHWSEGl 108
Cdd:PRK13009 18 TPDDAGCQDLLAE----RLEALGFTCErmdfgDVKN--------LWARRGTEG---PHLCFaGHTDVVpPGDLEAWTSP- 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 742461296 109 sPWQLVEQAGRWYGRGSADNKGqhSIN--IAALEQVFQAR---QGRLGF 152
Cdd:PRK13009 82 -PFEPTIRDGMLYGRGAADMKG--SLAafVVAAERFVAAHpdhKGSIAF 127
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
19-142 |
1.29e-06 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 50.59 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 19 FRDVLARRVAIASESqrtDRDAALQQYlSEEIIPALQ----ALGF--ELQQIdnPAAANRPFLIASRIE-DAALptVLCy 91
Cdd:PRK05111 7 FIEMYRALIATPSIS---ATDPALDQS-NRAVIDLLAgwfeDLGFnvEIQPV--PGTRGKFNLLASLGSgEGGL--LLA- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 742461296 92 GHGDVVFGDDEHWSEglSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQV 142
Cdd:PRK05111 78 GHTDTVPFDEGRWTR--DPFTLTEHDGKLYGLGTADMKGFFAFILEALRDI 126
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
21-184 |
8.47e-06 |
|
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: 47.77 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 21 DVLARRVAIASESQRTDRDAALQQYLSEeiipALQALGF--ELQQIDNPAAANRPFLIASRiedaALPTVLCYGHGDVV- 97
Cdd:cd08011 2 KLLQELVQIPSPNPPGDNTSAIAAYIKL----LLEDLGYpvELHEPPEEIYGVVSNIVGGR----KGKRLLFNGHYDVVp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 98 FGDDEHWSegLSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQVFQARQ-----------------GRLGfnCKWLFEM 160
Cdd:cd08011 74 AGDGEGWT--VDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKApwdlpvvltfvpdeetgGRAG--TKYLLEK 149
|
170 180 190
....*....|....*....|....*....|.
gi 742461296 161 GEE------ISSP-GLAEVCRQHAQALQADL 184
Cdd:cd08011 150 VRIkpndvlIGEPsGSDNIRIGEKGLVWVII 180
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
92-215 |
2.27e-05 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 46.53 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 92 GHGDVV-FGDDEHWSEglSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQVFQAR---QGRLgfnckwLFE--MGEEIS 165
Cdd:cd03895 81 GHIDVVpEGPVELWTR--PPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGlqpAADV------HFQsvVEEECT 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 742461296 166 SPG-LAEVCRQHAqalqADLFIASDgprlnAERPTLFLGSRGCVNFRLTIR 215
Cdd:cd03895 153 GNGaLAALMRGYR----ADAALIPE-----PTELKLVRAQVGVIWFRVKVR 194
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
68-450 |
2.82e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 46.38 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 68 AAANRPFLIAsRIE--DAALPTVLCYGHGDVVFGDDEHWSegLSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQVfqA 145
Cdd:PRK07906 47 SAPGRANVVA-RLPgaDPSRPALLVHGHLDVVPAEAADWS--VHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHL--A 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 146 RQGR-------LGF----------NCKWLFEmgeeiSSPGLAEVCRQHAQALQADLFIASDGPRL----NAERPTLFLgs 204
Cdd:PRK07906 122 RTGRrpprdlvFAFvadeeaggtyGAHWLVD-----NHPELFEGVTEAISEVGGFSLTVPGRDRLylieTAEKGLAWM-- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 205 rgcvnfRLTirARERDYHsgnwGGLLS--NPGTQLANAIASLvnqhGQMQVaalkPPRLTPALRTILADIApggQATDPA 282
Cdd:PRK07906 195 ------RLT--ARGRAGH----GSMVNddNAVTRLAEAVARI----GRHRW----PLVLTPTVRAFLDGVA---ELTGLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 283 IDPQWGE---AGLSPSERLFGwNTLEVlsflTGNPQR-----PMNAIPGHATAVCQLRFVVGTDWQQLAQhlrhhLDEHG 354
Cdd:PRK07906 252 FDPDDPDallAKLGPAARMVG-ATLRN----TANPTMlkagyKVNVIPGTAEAVVDGRFLPGREEEFLAT-----VDELL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 355 FTMVEISDVRGTPATRLDPTDPLVnwtlDLMR---QTSDKKPALLP-NLGGSLPNEVFAEI----LGLPTLWIPHSYPAC 426
Cdd:PRK07906 322 GPDVEREWVHRDPALETPFDGPLV----DAMNaalLAEDPGARVVPyMLSGGTDAKAFSRLgircYGFAPLRLPPDLDFA 397
|
410 420
....*....|....*....|....*
gi 742461296 427 GQ-HAVDEHMLVSVAREGLQIMTRL 450
Cdd:PRK07906 398 ALfHGVDERVPVDALRFGVRVLDRF 422
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
54-401 |
2.86e-05 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 46.14 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 54 LQALGFELQQIDNP------AAANRPFLIASRIEDAalPTVLCYGHGDVVFGDDEhWSEgLSPWQLVEQAGRWYGRGSAD 127
Cdd:PRK08651 39 LEELGFSTEIIEVPneyvkkHDGPRPNLIARRGSGN--PHLHFNGHYDVVPPGEG-WSV-NVPFEPKVKDGKVYGRGASD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 128 NKGQHSINIAALEQVFQARQGRLGFNckwlFEMGEEISSPG---LAEVCRqhaqaLQADLFIASDGPRLNaerpTLFLGS 204
Cdd:PRK08651 115 MKGGIAALLAAFERLDPAGDGNIELA----IVPDEETGGTGtgyLVEEGK-----VTPDYVIVGEPSGLD----NICIGH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 205 RGcvNFRLTIRARERDYHSGN-WGGLlsnpgtqlaNAIASLVnqhgqmqvaalkppRLTPALRTILADIAPGGQATDPA- 282
Cdd:PRK08651 182 RG--LVWGVVKVYGKQAHASTpWLGI---------NAFEAAA--------------KIAERLKSSLSTIKSKYEYDDERg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 283 --IDPQWGEAGLSPSERlfgwntlevlsfltgnpqrpMNAIPGHATAVCQLRFVVGTDWQQLAQHLRHHLDEHGFTMVEI 360
Cdd:PRK08651 237 akPTVTLGGPTVEGGTK--------------------TNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIE 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 742461296 361 SDVRGTP---ATRLDPTDPLVNWTLDLMRQTSDKKPALLPNLGG 401
Cdd:PRK08651 297 VEFEITPfseAFVTDPDSELVKALREAIREVLGVEPKKTISLGG 340
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
47-190 |
5.35e-05 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and 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: 45.53 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 47 SEEIIPALQALGF-ELQQID--NPAAANRPFLIAsRIEDAALPTVLCYGHGDVV-FGDDEHWseGLSPWQLVEQAGRWYG 122
Cdd:cd05650 29 ADYLEKKLREYGFyTLERYDapDERGIIRPNIVA-KIPGGNDKTLWIISHLDTVpPGDLSLW--ETDPWEPVVKDGKIYG 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 742461296 123 RGSADNKGQHSINIAALEQVFQarqgrLG----FNCKWLFEMGEEISSP-GLAEVCRQHAQALQADLFIASDG 190
Cdd:cd05650 106 RGVEDNQQGIVSSLLALKAIIK-----NGitpkYNFGLLFVADEEDGSEyGIQYLLNKFDLFKKDDLIIVPDF 173
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
1-145 |
5.40e-05 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 45.38 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 1 MTTPQVIQQALAYFDSGRFRDV--LARRVAIASesQRTDrDAALQQYLSEeiipALQALGFELQ--QIDNPAAANRPFLI 76
Cdd:PRK06837 2 MLTPDLTQRILAAVDAGFDAQVafTQDLVRFPS--TRGA-EAPCQDFLAR----AFRERGYEVDrwSIDPDDLKSHPGAG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 77 ASRIEDAALPTVLCY--------------GHGDVV-FGDDEHWSEglSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQ 141
Cdd:PRK06837 75 PVEIDYSGAPNVVGTyrpagktgrslilqGHIDVVpEGPLDLWSR--PPFDPVIVDGWMYGRGAADMKAGLAAMLFALDA 152
|
....
gi 742461296 142 VFQA 145
Cdd:PRK06837 153 LRAA 156
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
82-375 |
6.90e-05 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 45.32 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 82 DAALPTVLCYGHGDVV---FGDDEHWSEGlsPWQLVEQAGRWYGRGSADNKGQ-HSINIAA---LEQVFQARQG-RLGFN 153
Cdd:PRK08262 108 DPSLKPIVLMAHQDVVpvaPGTEGDWTHP--PFSGVIADGYVWGRGALDDKGSlVAILEAAealLAQGFQPRRTiYLAFG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 154 CKwlfemgEEISSPG---LAEVCRQH----AQALQADLFIASDG-PRLNAERPTLFLGSRGCVNFRLTIRARerdyhsgn 225
Cdd:PRK08262 186 HD------EEVGGLGaraIAELLKERgvrlAFVLDEGGAITEGVlPGVKKPVALIGVAEKGYATLELTARAT-------- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 226 wGGLLSNPGTQ-----LANAIASLVNQhgQMqvaalkPPRLTPALRTILADIAP---GGQ--------ATDPAIDpqwGE 289
Cdd:PRK08262 252 -GGHSSMPPRQtaigrLARALTRLEDN--PL------PMRLRGPVAEMFDTLAPemsFAQrvvlanlwLFEPLLL---RV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 290 AGLSPSERLFgWNTLEVLSFLTGNPQRpmNAIPGHATAVCQLRFVVGTDWQQLAQHLRHHLDEHGftmVEISDVRG-TPA 368
Cdd:PRK08262 320 LAKSPETAAM-LRTTTAPTMLKGSPKD--NVLPQRATATVNFRILPGDSVESVLAHVRRAVADDR---VEIEVLGGnSEP 393
|
....*..
gi 742461296 369 TRLDPTD 375
Cdd:PRK08262 394 SPVSSTD 400
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
75-168 |
8.02e-05 |
|
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: 43.57 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 75 LIASRIEDAALPTVLCYGHGDVVFGDDEHWSEgLSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQVFQAR---QGRLG 151
Cdd:cd03873 2 LIARLGGGEGGKSVALGAHLDVVPAGEGDNRD-PPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGfkpKGTIV 80
|
90
....*....|....*..
gi 742461296 152 FnckwLFEMGEEISSPG 168
Cdd:cd03873 81 V----AFTADEEVGSGG 93
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
85-139 |
8.91e-05 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 44.76 E-value: 8.91e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 742461296 85 LPTVLCYGHGDVVFGDDEHWSEglSPWQLVEQAGRWYGRGSADNKGqhsiNIAAL 139
Cdd:PRK08554 63 KPKLLFMAHFDVVPVNPEEWNT--EPFKLTVKGDKAYGRGSADDKG----NVASV 111
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
86-190 |
2.03e-04 |
|
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: 42.42 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 86 PTVLCYGHGDVVFGDDEHWSEgLSPWQLVEQAGRWYGRGSADNKGQHSINIAALEQVFQAR---QGRLGFnckwLFEMGE 162
Cdd:cd18669 13 KRVLLGAHIDVVPAGEGDPRD-PPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGfklKGTVVV----AFTPDE 87
|
90 100 110
....*....|....*....|....*....|
gi 742461296 163 EISSPGLAE--VCRQHAQALQADLFIASDG 190
Cdd:cd18669 88 EVGSGAGKGllSKDALEEDLKVDYLFVGDA 117
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
21-257 |
6.04e-04 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 42.26 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 21 DVLARRVAIasesqRTDRDAALQQYLSEEII---PALQAL--GFELQQIDNpaaANRPFLIASRIEDAALPTVLCygHGD 95
Cdd:PRK06156 50 ESLRELVAF-----PTVRVEGVPQHENPEFIgfkKLLKSLarDFGLDYRNV---DNRVLEIGLGGSGSDKVGILT--HAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 96 VVFGDDEHW---SEGLSPWQLVEQAGRWYGRGSADNKGqhSInIAAL--------EQVFQARQGRLgfnckwLFEMGEEI 164
Cdd:PRK06156 120 VVPANPELWvldGTRLDPFKVTLVGDRLYGRGTEDDKG--AI-VTALyamkaikdSGLPLARRIEL------LVYTTEET 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 165 SSPGLAEVcRQHAQalQADLFIASDG--PRLNAERptlflGSrGCVNFRLTIRArerdyHSGNWGGLLSNPGTQLANAI- 241
Cdd:PRK06156 191 DGDPLKYY-LERYT--PPDYNITLDAeyPVVTAEK-----GW-GTIMATFPKRA-----ADGKGAEIVAMTGGAFANQIp 256
|
250 260
....*....|....*....|
gi 742461296 242 ----ASLVNQHGQMQVAALK 257
Cdd:PRK06156 257 qtavATLSGGDPAALAAALQ 276
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
21-176 |
6.14e-04 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 41.93 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 21 DVLARRVAIASESQRTDRDAALQQYLSEEiipaLQALGFELQQIDNPAAANRpfLIASRIEDAALPTVLCYGHGDVVFGd 100
Cdd:PRK06133 41 DTLKELVSIESGSGDAEGLKQVAALLAER----LKALGAKVERAPTPPSAGD--MVVATFKGTGKRRIMLIAHMDTVYL- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 101 dehwsEGLSPWQ-LVEQAGRWYGRGSADNKGQHSINIAALeQVFQARQ----GRLGFnckwLFEMGEEISSPG----LAE 171
Cdd:PRK06133 114 -----PGMLAKQpFRIDGDRAYGPGIADDKGGVAVILHAL-KILQQLGfkdyGTLTV----LFNPDEETGSPGsrelIAE 183
|
....*
gi 742461296 172 VCRQH 176
Cdd:PRK06133 184 LAAQH 188
|
|
| PRK06915 |
PRK06915 |
peptidase; |
23-140 |
6.64e-04 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 41.99 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 23 LARRVAIASESQRTDRDAALQQYLSEE------------IIPALQALGFELQ--QIDNPAAANRPFLIASRIEDAALPTV 88
Cdd:PRK06915 4 LKKQICDYIESHEEEAVKLLKRLIQEKsvsgdesgaqaiVIEKLRELGLDLDiwEPSFKKLKDHPYFVSPRTSFSDSPNI 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742461296 89 -------------LCYGHGDVV-FGDDEHWSEglSPWQLVEQAGRWYGRGSADNKGQHSINIAALE 140
Cdd:PRK06915 84 vatlkgsgggksmILNGHIDVVpEGDVNQWDH--HPYSGEVIGGRIYGRGTTDMKGGNVALLLAME 147
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
20-290 |
1.16e-03 |
|
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: 41.18 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 20 RDVLARRVAIASESQRtdrDAALQQYLsEEIipaLQALGFELQqIDNpaaANRPFLIAsrieDAALPTVLCYGHGDVVFG 99
Cdd:cd05653 4 VELLLDLLSIYSPSGE---EARAAKFL-EEI---MKELGLEAW-VDE---AGNAVGGA----GSGPPDVLLLGHIDTVPG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 100 DDEHWSEGlspwqlveqaGRWYGRGSADNKGQhsinIAALeqVFQARQGRLGFNCKWLFE--MGEEISSPGLAEVCRQHa 177
Cdd:cd05653 69 EIPVRVEG----------GVLYGRGAVDAKGP----LAAM--ILAASALNEELGARVVVAglVDEEGSSKGARELVRRG- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 178 qaLQADLFIAsdGPRLNAERPTlfLGSRGCVnfRLTIRARERDYHSgnwggllSNPGT----QLANAIASLVNQHGQMQV 253
Cdd:cd05653 132 --PRPDYIII--GEPSGWDGIT--LGYRGSL--LVKIRCEGRSGHS-------SSPERnaaeDLIKKWLEVKKWAEGYNV 196
|
250 260 270
....*....|....*....|....*....|....*..
gi 742461296 254 AALKPPRLTPalrTILAdiapGGqaTDPAIDPQWGEA 290
Cdd:cd05653 197 GGRDFDSVVP---TLIK----GG--ESSNGLPQRAEA 224
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
92-139 |
4.16e-03 |
|
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: 39.54 E-value: 4.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 742461296 92 GHGDVV-FGDDehWSegLSPWQLVEQAGRWYGRGSADNKGQHSINIAAL 139
Cdd:cd03888 78 GHLDVVpAGEG--WT--TDPFKPVIKDGKLYGRGTIDDKGPTIAALYAL 122
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
92-190 |
4.37e-03 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 39.45 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742461296 92 GHGDVV-FGDDEHWSEglSPWQLVEQAGRWYGRGSADNkgQHSI--NIAALEQVFQaRQGRLGFNCKWLFEMGEEISSP- 167
Cdd:PRK13983 83 SHMDVVpPGDLSLWET--DPFKPVVKDGKIYGRGSEDN--GQGIvsSLLALKALMD-LGIRPKYNLGLAFVSDEETGSKy 157
|
90 100
....*....|....*....|....
gi 742461296 168 GLAEVCRQHAQAL-QADLFIASDG 190
Cdd:PRK13983 158 GIQYLLKKHPELFkKDDLILVPDA 181
|
|
| |
