|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
1-459 |
0e+00 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 863.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 1 MAALKTVLDRIDANLEAALARLFKLVSIKSVSTDPAFADDCAAAAQFLSDELASLGFEASVRPTAGHPMVVAHAKAARPD 80
Cdd:PRK09104 2 MADLDPVLDHIDANLDASLERLFALLRIPSISTDPAYAADCRKAADWLVADLASLGFEASVRDTPGHPMVVAHHEGPTGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 81 VPHLLFYGHYDVQPPDPLELWESPPFEPKIVEAETGRR-IVGRGVADDKGQLMTFIEAVRAFKE-TGDLPCKITVLLEGE 158
Cdd:PRK09104 82 APHVLFYGHYDVQPVDPLDLWESPPFEPRIKETPDGRKvIVARGASDDKGQLMTFVEACRAWKAvTGSLPVRVTILFEGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 159 EETGSPSLPVFLAANKGELEADLALVCDTGMWDRRTPAITTMLRGLVTEEVIIRGADRDLHSGIFGSAAVNPIHALARVI 238
Cdd:PRK09104 162 EESGSPSLVPFLEANAEELKADVALVCDTGMWDRETPAITTSLRGLVGEEVTITAADRDLHSGLFGGAAANPIRVLTRIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 239 AGLHDADGKITLPGFYDAVAELPEEVAEQWRALKFDEAAFLGAVGLSVPAGEKGRSVLEMVWSRPSCDVNGIIGGYTGKG 318
Cdd:PRK09104 242 AGLHDETGRVTLPGFYDGVEELPPEILAQWKALGFTAEAFLGPVGLSIPAGEKGRSVLEQIWSRPTCEINGIWGGYTGEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 319 SKTVLPAQASAKFSFRLVGAQDPAKIAESFRAYVRKSLPQDCRVEFIPHGGSKALNLPFSSESLSRASRALQAEWDATPV 398
Cdd:PRK09104 322 FKTVIPAEASAKVSFRLVGGQDPAKIREAFRAYVRARLPADCSVEFHDHGGSPAIALPYDSPALAAAKAALSDEWGKPAV 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501585113 399 LAGCGGSIPIVGSFKSDLNMDTLMIGFGLEDDRVHSPNEKYELSSFHKGARSWARVLDALA 459
Cdd:PRK09104 402 LIGSGGSIPIVGDFKRILGMDSLLVGFGLDDDRIHSPNEKYDLESFHKGIRSWARILAALA 462
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
19-458 |
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: 349929 [Multi-domain] Cd Length: 437 Bit Score: 539.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 19 LARLFKLVSIKSVSTDPAFADDCAAAAQFLSDELASLGFE-ASVRPTAGHPMVVAHAKAArPDVPHLLFYGHYDVQPPDP 97
Cdd:cd05680 1 LEELFELLRIPSVSADPAHKGDVRRAAEWLADKLTEAGFEhTEVLPTGGHPLVYAEWLGA-PGAPTVLVYGHYDVQPPDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 98 LELWESPPFEPKIVEAetgrRIVGRGVADDKGQLMTFIEAVRAF-KETGDLPCKITVLLEGEEETGSPSLPVFLAANKGE 176
Cdd:cd05680 80 LELWTSPPFEPVVRDG----RLYARGASDDKGQVFIHIKAVEAWlAVEGALPVNVKFLIEGEEEIGSPSLPAFLEENAER 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 177 LEADLALVCDTGMWDRRTPAITTMLRGLVTEEVIIRGADRDLHSGIFGSAAVNPIHALARVIAGLHDADGKITLPGFYDA 256
Cdd:cd05680 156 LAADVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNRDLHSGSYGGAVPNPANALARLLASLHDEDGRVAIPGFYDD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 257 VAELPEEVAEQWRALKFDEAAFLGAVGLSVPAGEKGRSVLEMVWSRPSCDVNGIIGGYTGKGSKTVLPAQASAKFSFRLV 336
Cdd:cd05680 236 VRPLTDAEREAWAALPFDEAAFKASLGVPALGGEAGYTTLERLWARPTLDVNGIWGGYQGEGSKTVIPSKAHAKISMRLV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 337 GAQDPAKIAESFRAYVRKSLPQDCRVEFIPHGGSKALNLPFSSESLSRASRALQAEWDATPVLAGCGGSIPIVGSFKSDL 416
Cdd:cd05680 316 PGQDPDAIADLLEAHLRAHAPPGVTLSVKPLHGGRPYLVPTDHPALQAAERALEEAFGKPPVFVREGGSIPIVALFEKVL 395
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 501585113 417 NMDTLMIGFGLEDDRVHSPNEKYELSSFHKGARSWARVLDAL 458
Cdd:cd05680 396 GIPTVLMGFGLPDDAIHAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
16-459 |
8.09e-136 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 398.73 E-value: 8.09e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 16 EAALARLFKLVSIKSVSTDPAFADDCAAAAQFLSDELASLGFE-ASVRPTAGHPMVVA---HAKAArpdvPHLLFYGHYD 91
Cdd:PRK08201 14 EAHLEELKEFLRIPSISALSEHKEDVRKAAEWLAGALEKAGLEhVEIMETAGHPIVYAdwlHAPGK----PTVLIYGHYD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 92 VQPPDPLELWESPPFEPKIVEAetgrRIVGRGVADDKGQLMTFIEAVRA-FKETGDLPCKITVLLEGEEETGSPSLPVFL 170
Cdd:PRK08201 90 VQPVDPLNLWETPPFEPTIRDG----KLYARGASDDKGQVFMHLKAVEAlLKVEGTLPVNVKFCIEGEEEIGSPNLDSFV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 171 AANKGELEADLALVCDTGMWDRRTPAITTMLRGLVTEEVIIRGADRDLHSGIFGSAAVNPIHALARVIAGLHDADGKITL 250
Cdd:PRK08201 166 EEEKDKLAADVVLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLHSGLYGGAVPNALHALVQLLASLHDEHGTVAV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 251 PGFYDAVAELPEEVAEQWRALKFDEAAFLGAVGLSVPAGEKGRSVLEMVWSRPSCDVNGIIGGYTGKGSKTVLPAQASAK 330
Cdd:PRK08201 246 EGFYDGVRPLTPEEREEFAALGFDEEKLKRELGVDELFGEEGYTALERTWARPTLELNGVYGGFQGEGTKTVIPAEAHAK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 331 FSFRLVGAQDPAKIAESFRAYVRKSLPQDCRVEFIPHGGSKALNLPFSSESLSRASRALQAEWDATPVLAGCGGSIPIVG 410
Cdd:PRK08201 326 ITCRLVPDQDPQEILDLIEAHLQAHTPAGVRVTIRRFDKGPAFVAPIDHPAIQAAARAYEAVYGTEAAFTRMGGSIPVVE 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 501585113 411 SFKSDLNMDTLMIGFGLEDDRVHSPNEKYELSSFHKGARSWARVLDALA 459
Cdd:PRK08201 406 TFSSQLHIPIVLMGFGLPSENFHAPNEHFHLENFDKGLRTLVEYWHQLA 454
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
19-456 |
7.22e-117 |
|
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: 348.93 E-value: 7.22e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 19 LARLFKLVSIKSVSTDPAFADDCAAAAQFLSDELASLGFE-ASVRPTAGHPMVVAHAKAArPDVPHLLFYGHYDVQPPDP 97
Cdd:cd03893 1 LQTLAELVAIPSVSAQPDRREELRRAAEWLADLLRRLGFTvEIVDTSNGAPVVFAEFPGA-PGAPTVLLYGHYDVQPAGD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 98 LELWESPPFEPkiveAETGRRIVGRGVADDKGQLMTFIEAVRAFKETG-DLPCKITVLLEGEEETGSPSLPVFLAANKGE 176
Cdd:cd03893 80 EDGWDSDPFEL----TERDGRLYGRGAADDKGPILAHLAALRALMQQGgDLPVNVKFIIEGEEESGSPSLDQLVEAHRDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 177 LEADLALVCDTGMWDRRTPAITTMLRGLVTEEVIIRGADRDLHSGIFGSAAVNPIHALARVIAGLHDADGKITLPGFYDA 256
Cdd:cd03893 156 LAADAIVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLDHDLHSGLYGGVVPDPMTALAQLLASLRDETGRILVPGLYDA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 257 VAELPEEVAEQWRALKfDEAAFLGavglsvpaGEKGrSVLEMVWSRPSCDVNGIIGGYTGKGSKTVLPAQASAKFSFRLV 336
Cdd:cd03893 236 VRELPEEEFRLDAGVL-EEVEIIG--------GTTG-SVAERLWTRPALTVLGIDGGFPGEGSKTVIPPRARAKISIRLV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 337 GAQDPAKIAESFRAYVRKSLPQDCRVEFIPHGGSKALNLPFSSESLSRASRALQAEWDATPVLAGCGGSIPIVGSFKSDL 416
Cdd:cd03893 306 PGQDPEEASRLLEAHLEKHAPSGAKVTVSYVEGGMPWRSDPSDPAYQAAKDALRTAYGVEPPLTREGGSIPFISVLQEFP 385
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 501585113 417 NMDTLMIGFGLEDDRVHSPNEKYELSSFHKGARSWARVLD 456
Cdd:cd03893 386 QAPVLLIGVGDPDDNAHSPNESLRLGNYKEGTQAEAALLY 425
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
18-447 |
5.51e-105 |
|
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: 318.90 E-value: 5.51e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 18 ALARLFKLVSIKSVSTDPAFADDCAaaaQFLSDELASLGFEASVRPTAGHPMVVAHAKAARPdvPHLLFYGHYDVQPPDP 97
Cdd:cd05681 1 YLEDLRDLLKIPSVSAQGRGIPETA---DFLKEFLRRLGAEVEIFETDGNPIVYAEFNSGDA--KTLLFYNHYDVQPAEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 98 LELWESPPFEPKIveaeTGRRIVGRGVADDKGQLMTFIEAVRAFKET-GDLPCKITVLLEGEEETGSPSLPVFLAANKGE 176
Cdd:cd05681 76 LELWTSDPFELTI----RNGKLYARGVADDKGELMARLAALRALLQHlGELPVNIKFLVEGEEEVGSPNLEKFVAEHADL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 177 LEADlALVCDTGMWDRR-TPAITTMLRGLVTEEVIIRGADRDLHSGiFGSAAVNPIHALARVIAGLHDADGKITLPGFYD 255
Cdd:cd05681 152 LKAD-GCIWEGGGKNPKgRPQISLGVKGIVYVELRVKTADFDLHSS-YGAIVENPAWRLVQALNSLRDEDGRVLIPGFYD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 256 AVAELPEEVAEQWRALKFDEAAFLGAVGLSVPAGEKGRSVLEMVWSRPSCDVNGIIGGYTGKGSKTVLPAQASAKFSFRL 335
Cdd:cd05681 230 DVRPLSEAERALIDTYDFDPEELRKTYGLKRPLQVEGKDPLRALFTEPTCNINGIYSGYTGEGSKTILPSEAFAKLDFRL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 336 VGAQDPAKIAESFRAYVRKSLPQDcrVEFIPHGGSKALNLPFSSEsLSRASRALQAEWDATP--VLAGCGGSIPiVGSFK 413
Cdd:cd05681 310 VPDQDPAKILSLLRKHLDKNGFDD--IEIHDLLGEKPFRTDPDAP-FVQAVIESAKEVYGQDpiVLPNSAGTGP-MYPFY 385
|
410 420 430
....*....|....*....|....*....|....
gi 501585113 414 SDLNMDTLMIGFGLEDDRVHSPNEKYELSSFHKG 447
Cdd:cd05681 386 DALEVPVVAIGVGNAGSNAHAPNENIRIADYYKG 419
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
6-459 |
1.37e-96 |
|
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: 295.64 E-value: 1.37e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 6 TVLDRIDANLEAALARLFKLVSIKSVStdpafaDDCAAAAQFLSDELASLGFEASVRPTA-GHPMVVAHAKAARPDvPHL 84
Cdd:COG0624 2 AVLAAIDAHLDEALELLRELVRIPSVS------GEEAAAAELLAELLEALGFEVERLEVPpGRPNLVARRPGDGGG-PTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 85 LFYGHYDVQPPDPLELWESPPFEPKIVeaetGRRIVGRGVADDKGQLMTFIEAVRAFKETG-DLPCKITVLLEGEEETGS 163
Cdd:COG0624 75 LLYGHLDVVPPGDLELWTSDPFEPTIE----DGRLYGRGAADMKGGLAAMLAALRALLAAGlRLPGNVTLLFTGDEEVGS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 164 PSLPVFLAANKGELEADLALVCDTGMWDRrtpaITTMLRGLVTEEVIIRGADRdlHSGIFGsAAVNPIHALARVIAGLHD 243
Cdd:COG0624 151 PGARALVEELAEGLKADAAIVGEPTGVPT----IVTGHKGSLRFELTVRGKAA--HSSRPE-LGVNAIEALARALAALRD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 244 ADgkitlpgfydavaelpeevaeqwraLKFDEAAFLGavglsvpagekgrsvlemvwsRPSCDVNGIIGGYTGKgsktVL 323
Cdd:COG0624 224 LE-------------------------FDGRADPLFG---------------------RTTLNVTGIEGGTAVN----VI 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 324 PAQASAKFSFRLVGAQDPAKIAESFRAYVRKSLPqDCRVEF-IPHGGSKALNLPFSSESLSRASRALQAEWDATPVLAGC 402
Cdd:COG0624 254 PDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAP-GVEVEVeVLGDGRPPFETPPDSPLVAAARAAIREVTGKEPVLSGV 332
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 501585113 403 GGSIPIvGSFKSDLNMDTLMIGFGlEDDRVHSPNEKYELSSFHKGARSWARVLDALA 459
Cdd:COG0624 333 GGGTDA-RFFAEALGIPTVVFGPG-DGAGAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
9-459 |
8.81e-87 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 272.55 E-value: 8.81e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 9 DRIDANLEAALARLFKLVSIKSVSTDPAFADDCAAAAQFLSDELASLGF-EASVRPTAGHPMVVAHaKAARPDVPHLLFY 87
Cdd:PRK07907 11 ARVAELLPRVRADLEELVRIPSVAADPFRREEVARSAEWVADLLREAGFdDVRVVSADGAPAVIGT-RPAPPGAPTVLLY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 88 GHYDVQPPDPLELWESPPFEPkiveAETGRRIVGRGVADDKGQLMTFIEAVRAFkeTGDLPCKITVLLEGEEETGSPSLP 167
Cdd:PRK07907 90 AHHDVQPPGDPDAWDSPPFEL----TERDGRLYGRGAADDKGGIAMHLAALRAL--GGDLPVGVTVFVEGEEEMGSPSLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 168 VFLAANKGELEADLALVCDTGMWDRRTPAITTMLRGLVTEEVIIRGADRDLHSGIFGSAAVNPIHALARVIAGLHDADGK 247
Cdd:PRK07907 164 RLLAEHPDLLAADVIVIADSGNWSVGVPALTTSLRGNADVVVTVRTLEHAVHSGQFGGAAPDALTALVRLLATLHDEDGN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 248 ITLPGFydavaelpeEVAEQWRALKFDEAAFLGAVGLSVPAGEKGR-SVLEMVWSRPSCDVNGIIGGYTgKGSKTVLPAQ 326
Cdd:PRK07907 244 VAVDGL---------DATEPWLGVDYDEERFRADAGVLDGVELIGTgSVADRLWAKPAITVIGIDAPPV-AGASNALPPS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 327 ASAKFSFRLVGAQDPAKIAESFRAYVRKSLPQDCRVEFIPHGGSKALNLPFSSESLSRASRALQAEWDATPVLAGCGGSI 406
Cdd:PRK07907 314 ARARLSLRVAPGQDAAEAQDALVAHLEAHAPWGAHVTVERGDAGQPFAADASGPAYDAARAAMREAWGKDPVDMGMGGSI 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 501585113 407 PIVGSFKSDLNMDTLMIgFGLED--DRVHSPNEKYELSSFHKGARSWARVLDALA 459
Cdd:PRK07907 394 PFIAELQEAFPQAEILV-TGVEDpkTRAHSPNESVHLGELERAAVAEALLLARLA 447
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
47-452 |
2.84e-82 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 260.46 E-value: 2.84e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 47 FLSDELASLGFEASVRPTAGHPMVVAHAKAARPDVphLLFYGHYDVQPPDPLELWESPPFEPKIVeaetGRRIVGRGVAD 126
Cdd:PRK06446 30 YLKDTMEKLGIKANIERTKGHPVVYGEINVGAKKT--LLIYNHYDVQPVDPLSEWKRDPFSATIE----NGRIYARGASD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 127 DKGQLMTFIEAVRAFKETGDLPCKITVLLEGEEETGSPSLPVFLAANKGELEADLALVCDTGMWDRRTPAITTMLRGLVT 206
Cdd:PRK06446 104 NKGTLMARLFAIKHLIDKHKLNVNVKFLYEGEEEIGSPNLEDFIEKNKNKLKADSVIMEGAGLDPKGRPQIVLGVKGLLY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 207 EEVIIRGADRDLHSgIFGSAAVNPIHALARVIAGLHDADGKITLPGFYDAVAELPEEVAEQWRALKFDEAAFLGAVGLSV 286
Cdd:PRK06446 184 VELVLRTGTKDLHS-SNAPIVRNPAWDLVKLLSTLVDGEGRVLIPGFYDDVRELTEEERELLKKYDIDVEELRKALGFKE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 287 PAGEKGRSVLEMVWSRPSCDVNGIIGGYTGKGSKTVLPAQASAKFSFRLVGAQDPAKIAESFRAYVRKSLPqdcRVEFIP 366
Cdd:PRK06446 263 LKYSDREKIAEALLTEPTCNIDGFYSGYTGKGSKTIVPSRAFAKLDFRLVPNQDPYKIFELLKKHLQKVGF---NGEIIV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 367 HGGSKalnlPFSSESLSRASRAL--QAE--WDATP-VLAGCGGSIPIvGSFKSDLNMDTLM--IGFGLEDDRVHSPNEKY 439
Cdd:PRK06446 340 HGFEY----PVRTSVNSKVVKAMieSAKrvYGTEPvVIPNSAGTQPM-GLFVYKLGIRDIVsaIGVGGYYSNAHAPNENI 414
|
410
....*....|...
gi 501585113 440 ELSSFHKgARSWA 452
Cdd:PRK06446 415 RIDDYYK-AIKHT 426
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
7-447 |
4.00e-80 |
|
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: 255.99 E-value: 4.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 7 VLDRIDANLEAALARLFKLVSIKSVSTDPAFADDCAAAAQFLSDELASLGFEASVRPTAGHPM----VVAHAKA--AR-- 78
Cdd:cd05676 1 VFKYIDEHQDEFIERLREAVAIQSVSADPEKRPELIRMMEWAAERLEKLGFKVELVDIGTQTLpdgeELPLPPVllGRlg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 79 --PDVPHLLFYGHYDVQPPDPLELWESPPFEpkiVEAETGRrIVGRGVADDKGQLMTFIEAVRAFKETG-DLPCKITVLL 155
Cdd:cd05676 81 sdPSKKTVLIYGHLDVQPAKLEDGWDTDPFE---LTEKDGK-LYGRGSTDDKGPVLGWLNAIEAYQKLGqELPVNLKFCF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 156 EGEEETGSPSLPVFLAANKGELEADLALVC--DTGMWDRRTPAITTMLRGLVTEEVIIRGADRDLHSGIFGSAAVNPIHA 233
Cdd:cd05676 157 EGMEESGSEGLDELIEARKDTFFSDVDYVCisDNYWLGKKKPCLTYGLRGICYFFIEVEGPNKDLHSGVFGGSVHEPMTD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 234 LARVIAGLHDADGKITLPGFYDAVAELPEEVAEQWRALKFDEAAFLGAVGLSVPAGEKGRSVLEMVWSRPSCDVNGIIGG 313
Cdd:cd05676 237 LIALMSSLVDSDGKILIPGIYDAVAPLTEEEWELYEKIDFDMEEYREDIGVRRLLYDNKEELLMHRWRYPSLSIHGIEGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 314 YTGKGSKTVLPAQASAKFSFRLVGAQDPAKIAESFRAYV------RKSlPQDCRVEFIpHGGSkalnlPFSSESLSR--- 384
Cdd:cd05676 317 FSGPGAKTVIPAKVIGKFSIRLVPNMDPEVVEKQVTDYLekvfaeLKS-PNKLKVYMG-HGGK-----PWVADPDHPnyk 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501585113 385 -ASRALQAEWDATPVLAGCGGSIPIVGSFKSDLNMDTLMIGFGLEDDRVHSPNEKYELSSFHKG 447
Cdd:cd05676 390 aARKATKRVFGVEPDLTREGGSIPITLTFQEATGKNVMLLPIGAADDGAHSQNEKINRRNYIEG 453
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
19-458 |
3.65e-58 |
|
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: 197.57 E-value: 3.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 19 LARLFKLVSIKSVSTDPAFADDCAAA--AQFLSDELASLGFEAS---VRPTAGHPMVVAHAKAARPDVP--HLLFYGHYD 91
Cdd:cd05677 2 LNTLSEFIAFQTVSQSPTTENAEDSRrcAIFLRQLFKKLGATNClllPSGPGTNPIVLATFSGNSSDAKrkRILFYGHYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 92 VQPPDPLELWESPPFEpkiVEAETGRrIVGRGVADDKGQLMTFIEAVRAFKETGDLPCKITVLLEGEEETGSPSLPVFLA 171
Cdd:cd05677 82 VIPAGETDGWDTDPFT---LTCENGY-LYGRGVSDNKGPLLAAIYAVAELFQEGELDNDVVFLIEGEEESGSPGFKEVLR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 172 ANKGELEA-DLALVCDTGMWDRRTPAITTMLRGLVTEEVIIRGADRDLHSGIFGSAAVNPIHALARVIAGLHDADGKITL 250
Cdd:cd05677 158 KNKELIGDiDWILLSNSYWLDDNIPCLNYGLRGVIHATIVVSSDKPDLHSGVDGGVLREPTADLIKLLSKLQDPDGRILI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 251 PGFYDAVAELPEEVAEQWRALkfdeaaflgaVGLSVPAGEKGRSVLEMVWSRPSCDVNGIigGYTGKGSKTVLPAQASAK 330
Cdd:cd05677 238 PHFYDPVKPLTEAERARFTAI----------AETALIHEDTTVDSLIAKWRKPSLTVHTV--KVSGPGNTTVIPKSASAS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 331 FSFRLVGAQDPAKIAESFRAYVRKSL-----PQDCRVEfIPHGGSKALNLPfSSESLSRASRALQAEWDATPVLAGCGGS 405
Cdd:cd05677 306 VSIRLVPDQDLDVIKQDLTDYIQSCFaelksQNHLDIE-VLNEAEPWLGDP-DNPAYQILREAVTAAWGVEPLYIREGGS 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 501585113 406 IPIVGSFKSDLNMDTLMIGFGLEDDRVHSPNEKYELSSFHKGARSWARVLDAL 458
Cdd:cd05677 384 IPTIRFLEKEFNAPAVQLPCGQSSDNAHLDNERLRIKNLYKMREILSRVFNRL 436
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
22-455 |
4.37e-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.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 187.69 E-value: 4.37e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 22 LFKLVSIKSVSTDPAFADDCAAaaqFLSDELASLGFEASVRPTAGHPMVVAhAKAARPDVPHLLFYGHYDVQPPDPLELW 101
Cdd:cd05678 5 HRELVSIPNDATDEEEMRKNVD---WLEQAFRKRGFKTSQLPTSGLPLLLA-EKPISDARKTVLFYMHLDGQPVDPSKWD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 102 ESPPFEPkIVEAETGR-------------------RIVGRGVADDKGQLMTFIEAVRAFK-ETGDLPCKITVLLEGEEET 161
Cdd:cd05678 81 QKSPYTP-VLKRKDAAgnweeinwdaifsnldpewRVFARAAADDKGPIMMMLAALDALKaGGIAPKFNVKIILDSEEEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 162 GSPSLPVFLAANKGELEADLALVCDTGMWDRRTPAITTMLRGLVTEEVIIRGADRDLHSGIFGSAAVNPIHALARVIAGL 241
Cdd:cd05678 160 GSPSLPKAVKEYKELLAADALIIMDGPAHATNKPTLTFGCRGIATATLTTYGAKVPQHSGHYGNYAPNPAFRLSSLLASM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 242 HDADGKITLPGFYDAVaELPEEVAEQWRALKFDEAAFLGAVGLSVPagEK-GRSVLEMVwSRPSCDVNGIIGGYTGKGSK 320
Cdd:cd05678 240 KDDTGKVTIPGFYDGI-SIDEETQKILAAVPDDEESINKRLGIAQT--DKvGRNYQEAL-QYPSLNVRGMESGWKGDKVR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 321 TVLPAQASAKFSFRLVGAQDPAKIAESFRAYVRKS--------------LPQDCRVEFIPHGGSKALNLPFSSESLSRAS 386
Cdd:cd05678 316 TIIPEIAEAEIDIRLVPESDGPYLLDLVKAHIEKQgyfvtdraptdeerLAHDKIAKFTYRNGADAFRTDINSPIGNWLR 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 387 RALQAEWDATPV-LAGCGGSIPIVgSFKSDLNMDTLMIGFGLEDDRVHSPNEKYELSSFHKGARSWARVL 455
Cdd:cd05678 396 KALTDEFGEEPIqIRMMGGTVPIA-PFVNVLDIPAIIVPMVNMDNNQHSPNENLRIGNIRTGIRTCYAIL 464
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
85-455 |
5.63e-42 |
|
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: 151.35 E-value: 5.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 85 LFYGHYDVQPPDPLELWespPFEPKIVEaetgrRIVGRGVADDKGQLMTFIEAVRAFKETGDLPCKITVLLEGEEETGSP 164
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTEDG-----KLYGRGHDDMKGGLLAALEALRALKEEGLKKGTVKLLFQPDEEGGMG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 165 SLPVFLAA---NKGELEADLAL-VCDTGMWDRR-TPAITTMLRGLVTEEVIIRGADRdlHSGIFGsAAVNPIHALARVIA 239
Cdd:pfam01546 73 GARALIEDgllEREKVDAVFGLhIGEPTLLEGGiAIGVVTGHRGSLRFRVTVKGKGG--HASTPH-LGVNAIVAAARLIL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 240 GLHDADGKITLPGFYDAVaelpeevaeqwralkfdeaaflgavglsvpagekgrSVLEmvwsrpscdVNGIIGGYtgkgs 319
Cdd:pfam01546 150 ALQDIVSRNVDPLDPAVV------------------------------------TVGN---------ITGIPGGV----- 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 320 kTVLPAQASAKFSFRLVGAQDPAKIAESFRAYVRK-SLPQDCRVEFIPHGGSKALNLPfSSESLSRASRALQAEWDATPV 398
Cdd:pfam01546 180 -NVIPGEAELKGDIRLLPGEDLEELEERIREILEAiAAAYGVKVEVEYVEGGAPPLVN-DSPLVAALREAAKELFGLKVE 257
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501585113 399 LAGCGGSipivGSfkSDLNMDTL-----MIGFGLEDDRVHSPNEKYELSSFHKGARSWARVL 455
Cdd:pfam01546 258 LIVSGSM----GG--TDAAFFLLgvpptVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLARLL 313
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
68-410 |
3.46e-27 |
|
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: 113.20 E-value: 3.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 68 PMVVAHAKAARPDVPHLLFYGHYDVQPpdPLELWESP--PFEPKIVeaetGRRIVGRGVADDKGQLMTFIEAVRAFKETG 145
Cdd:cd05682 60 PLLFVEIPGTEQDDDTVLLYGHMDKQP--PFTGWDEGlgPTKPVIR----GDKLYGRGGADDGYAIFASLTAIKALQEQG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 146 dLP-CKITVLLEGEEETGSPSLPVFLAANKGEL-EADLALVCDTGMWDRRTPAITTMLRGLVTEEVIIRGADRDLHSGIF 223
Cdd:cd05682 134 -IPhPRCVVLIEACEESGSADLPFYLDKLKERIgNVDLVVCLDSGCGNYEQLWLTTSLRGVLGGDLTVQVLNEGVHSGDA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 224 GSAAVNPIHALARVIAGLHDAD-GKITLPGfydAVAELPEEVAEQWRALK-------FDEAAFLGavGLSVPAGEKGRSV 295
Cdd:cd05682 213 SGIVPSSFRILRQLLSRIEDENtGEVKLDE---QHCDIPAHRYEQAKKIAeilgeavYEEFPFVS--GVQPVTTDLVQLY 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 296 LEMVWsRPSCDVNGIIGGYTGKGSKTVLPAQASAKFSFRLVGAQDPAKIAESFRAYVRKSLPQDCRVEFIPHGGSKALNL 375
Cdd:cd05682 288 LNRTW-KPQLSVTGADGLPPASTAGNVLRPETTLKLSLRLPPTVDAEKASAALKKLLETDPPYNAKVTFKSDGAGSGWNA 366
|
330 340 350
....*....|....*....|....*....|....*.
gi 501585113 376 PFSSESLSRA-SRALQAEWDATPVLAGCGGSIPIVG 410
Cdd:cd05682 367 PLLSPWLAKAlNEASQLFFGKPAAYQGEGGSIPFMN 402
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
2-437 |
8.43e-27 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 112.32 E-value: 8.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 2 AALKTVLDRIDAN-LEAALARLfklVSIKSVSTDPAFADDCAAaaqFLSDE----LASLGFEASV--RPTAGH-PMVVAH 73
Cdd:PRK07079 5 AAIARAAAYFDSGaFFADLARR---VAYRTESQNPDRAPALRA---YLTDEiapaLAALGFTCRIvdNPVAGGgPFLIAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 74 aKAARPDVPHLLFYGHYDVQPPDPlELWeSPPFEP-KIVEAetGRRIVGRGVADDKGQL---MTFIEAVRAFKEtGDLPC 149
Cdd:PRK07079 79 -RIEDDALPTVLIYGHGDVVRGYD-EQW-REGLSPwTLTEE--GDRWYGRGTADNKGQHtinLAALEQVLAARG-GRLGF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 150 KITVLLEGEEETGSPSLPVFLAANKGELEADLALVCDTGMWDRRTPAITTMLRGLVTEEVIIRGADRDLHSGIFGSAAVN 229
Cdd:PRK07079 153 NVKLLIEMGEEIGSPGLAEVCRQHREALAADVLIASDGPRLSAERPTLFLGSRGAVNFRLRVNLRDGAHHSGNWGGLLRN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 230 PIHALARVIAGLHDADGKITLPGFYDavAELPEEVAEQWRALKFDEAAflGAVGLSVPAGEKGRSVLEMVWSRPSCDVNG 309
Cdd:PRK07079 233 PGTVLAHAIASLVDARGRIQVPGLRP--PPLPAAVRAALADITVGGGP--GDPAIDPDWGEPGLTPAERVFGWNTLEVLA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 310 IIggyTGKGSKTV--LPAQASAKFSFRLVGAQDPAKIAESFRAYV-RKSLPQdcrVEFIPHGGSKALNLPFSSESLSRAS 386
Cdd:PRK07079 309 FK---TGNPDAPVnaIPGSARAVCQLRFVVGTDWENLAPHLRAHLdAHGFPM---VEVTVERGSPATRLDPDDPWVRWAL 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 501585113 387 RALQAEWDATP-VLAGCGGSIPiVGSFKSDLNMDTLMIGFGLEDDRVHSPNE 437
Cdd:PRK07079 383 ASIARTTGKKPaLLPNLGGSLP-NDVFADILGLPTLWVPHSYPACSQHAPNE 433
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
46-437 |
5.73e-26 |
|
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: 109.51 E-value: 5.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 46 QFLSDELASLGFEASV--RPTAGH-PMVVAHAKAArPDVPHLLFYGHYDVQP------PDPLELWesppfepKIVEAetG 116
Cdd:cd05679 35 QEMRPRFERLGFTVHIhdNPVAGRaPFLIAERIED-PSLPTLLIYGHGDVVPgyegrwRDGRDPW-------TVTVW--G 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 117 RRIVGRGVADDKGQLMTFIEAVRAFKET--GDLPCKITVLLEGEEETGSPSLPVFLAANKGELEADLALVCDTGMWDRRT 194
Cdd:cd05679 105 ERWYGRGTADNKGQHSINMAALRQVLEArgGKLGFNVKFLIEMGEEMGSPGLRAFCFSHREALKADLFIASDGPRLAADR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 195 PAITTMLRGLVTEEVIIRGADRDLHSGIFGSAAVNPIHALARVIAGLHDADGKITLPGFydavaeLPEEVAEQWRALKFD 274
Cdd:cd05679 185 PTMFLGSRGGLNFELRVNLREGGHHSGNWGGLLANPGIILANAIASLVDGKGRIKLPAL------KPAHLPNSVRSALAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 275 EAAFLGAVGLSVPA--GEKGRSVLEMVWSRPSCDVNGIIGGYTGKGSKTVlPAQASAKFSFRLVGAQDPAKIAESFRAY- 351
Cdd:cd05679 259 VEVGGGPDDPSIDPwwGEPGLTAAERVFGWNTLEVLAFKTGNPDAPVNAI-PGHAEAICQIRFVVGTDPDTFIPAVRAHl 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 352 VRKSLPQdcrVEFIPHGGS-KALNLPFSSESLSRASRALQAEWDATP-VLAGCGGSIPiVGSFKSDLNMDTLMIGFGLED 429
Cdd:cd05679 338 DANGFDG---VEVTASQMVfAATRLDPDSPWVGWALASLQKTTGKKPaLLPNLGGSLP-NDVFSEVLGLPTLWVPHSYPA 413
|
....*...
gi 501585113 430 DRVHSPNE 437
Cdd:cd05679 414 CSQHAPNE 421
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
24-455 |
4.46e-24 |
|
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: 102.76 E-value: 4.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 24 KLVSIKSVStdpafaDDCAAAAQFLSDELASLGFEASVRPTAGHPMVVAHAKAARPdvPHLLFYGHYDVQPPDPLELWES 103
Cdd:cd08659 5 DLVQIPSVN------PPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVATVGGGDG--PVLLLNGHIDTVPPGDGDKWSF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 104 PPFEPKIVEAetgrRIVGRGVADDKGQLMTFIEAVRAFKETGDLPC-KITVLLEGEEETGSpslpvflaanKGeleadLA 182
Cdd:cd08659 77 PPFSGRIRDG----RLYGRGACDMKGGLAAMVAALIELKEAGALLGgRVALLATVDEEVGS----------DG-----AR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 183 LVCDTGMWDRRTPAIT---TML------RGLVTEEVIIRGADRdlHSGIfGSAAVNPIHALARVIAGLHdadgkitlpgf 253
Cdd:cd08659 138 ALLEAGYADRLDALIVgepTGLdvvyahKGSLWLRVTVHGKAA--HSSM-PELGVNAIYALADFLAELR----------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 254 yDAVAELPEEVaeqwralkfdeaaFLGAVGLSVpagekgrsvlemvwsrpscdvnGIIGGytGKGSKTVlPAQASAKFSF 333
Cdd:cd08659 204 -TLFEELPAHP-------------LLGPPTLNV----------------------GVING--GTQVNSI-PDEATLRVDI 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 334 RLVGAQDPAKIAESFRAYVRKSlPQDCRVEFIPHGGSKALNLPfSSE---SLSRASRALQAEWDATPVLAGCGGSipivg 410
Cdd:cd08659 245 RLVPGETNEGVIARLEAILEEH-EAKLTVEVSLDGDPPFFTDP-DHPlvqALQAAARALGGDPVVRPFTGTTDAS----- 317
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 501585113 411 SFKSDLNMDTLMIGFGlEDDRVHSPNEKYELSSFHKGARSWARVL 455
Cdd:cd08659 318 YFAKDLGFPVVVYGPG-DLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
46-455 |
7.32e-20 |
|
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: 90.73 E-value: 7.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 46 QFLSDELASLGFEASVRPTAGH-PMVVAHAKAarPDVPHLLFYGHYD-VQPPDPLELWespPFEpkiveaETGRRIVGRG 123
Cdd:cd03885 26 ELLAEELEALGFTVERRPLGEFgDHLIATFKG--TGGKRVLLIGHMDtVFPEGTLAFR---PFT------VDGDRAYGPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 124 VADDKGQLMTFIEAVRAFKETGDLP-CKITVLLEGEEETGSP-SLPVFLAANKGeleADLALVCDTGmwdRRTPAITTML 201
Cdd:cd03885 95 VADMKGGLVVILHALKALKAAGGRDyLPITVLLNSDEEIGSPgSRELIEEEAKG---ADYVLVFEPA---RADGNLVTAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 202 RGLVTEEVIIRGadRDLHSGIFGSAAVNPIHALARVIAGLHDADGKitlpgfydavaelpeevaeqwralkfdeaaflgA 281
Cdd:cd03885 169 KGIGRFRLTVKG--RAAHAGNAPEKGRSAIYELAHQVLALHALTDP---------------------------------E 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 282 VGLSVpagekgrSVlemvwsrpscdvnGIIGGYTGkgsKTVLPAQASAKFSFRLVGAQDPAKIAESFRAYVRKSLPQDCR 361
Cdd:cd03885 214 KGTTV-------NV-------------GVISGGTR---VNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTLVPGTS 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 362 VEFipHGGSKALNLPFS--SESLSRASRALQAE--WDATPVLAGcGGSipiVGSFKSDLNMDTLMiGFGLEDDRVHSPNE 437
Cdd:cd03885 271 VEL--TGGLNRPPMEETpaSRRLLARAQEIAAElgLTLDWEATG-GGS---DANFTAALGVPTLD-GLGPVGGGAHTEDE 343
|
410
....*....|....*...
gi 501585113 438 KYELSSFHKGARSWARVL 455
Cdd:cd03885 344 YLELDSLVPRIKLLARLL 361
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
18-255 |
3.45e-19 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 88.89 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 18 ALARLFKLVSIKSVstdPAFADDCAAAAQFLSDELASLGFEASV------RPTAGHPMVVAHAKAARPDVPHLLFYGHYD 91
Cdd:PRK08651 8 IVEFLKDLIKIPTV---NPPGENYEEIAEFLRDTLEELGFSTEIievpneYVKKHDGPRPNLIARRGSGNPHLHFNGHYD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 92 VQPPDplELWES-PPFEPKIVEAetgrRIVGRGVADDKGQLMTFIEAVRAFKETGDLPckITVLLEGEEETGSPSLPVFl 170
Cdd:PRK08651 85 VVPPG--EGWSVnVPFEPKVKDG----KVYGRGASDMKGGIAALLAAFERLDPAGDGN--IELAIVPDEETGGTGTGYL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 171 aANKGELEADLALVC-DTGMWDrrtpaITTMLRGLVTEEVIIRGadRDLHSGiFGSAAVNPIHALARVIAGLHDADGKIT 249
Cdd:PRK08651 156 -VEEGKVTPDYVIVGePSGLDN-----ICIGHRGLVWGVVKVYG--KQAHAS-TPWLGINAFEAAAKIAERLKSSLSTIK 226
|
....*.
gi 501585113 250 LPGFYD 255
Cdd:PRK08651 227 SKYEYD 232
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
46-442 |
1.42e-18 |
|
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: 86.79 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 46 QFLSDELASLGFEAsvrptagHPMVVAHAK---AAR-PDVPHLLFYGHYDVQPPDPLELWESPPFEPKIVEAetgrRIVG 121
Cdd:cd03891 22 DLIAERLKALGFTC-------ERLEFGGVKnlwARRgTGGPHLCFAGHTDVVPPGDLEGWSSDPFSPTIKDG----MLYG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 122 RGVADDKGQLMTFIEAVRAF-KETGDLPCKITVLLEGEEET----GSPSLPVFLAAnKGELeADLALV----CDTGMWDr 192
Cdd:cd03891 91 RGAADMKGGIAAFVAAAERFvAKHPNHKGSISFLITSDEEGpaidGTKKVLEWLKA-RGEK-IDYCIVgeptSEKKLGD- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 193 rtpAITTMLRGLVTEEVIIRGadRDLHsgifgSA----AVNPIHALARVIAGLhdadgkitlpgfydavaelpeevaeqw 268
Cdd:cd03891 168 ---TIKIGRRGSLNGKLTIKG--KQGH-----VAyphlADNPIHLLAPILAEL--------------------------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 269 RALKFDEaaflgavglsvpaGEKgrsvlemvWSRPS-CDVNGIiggYTGKGSKTVLPAQASAKFSFRLVGAQDPAKIAES 347
Cdd:cd03891 211 TATVLDE-------------GNE--------FFPPSsLQITNI---DVGNGATNVIPGELKAKFNIRFNDEHTGESLKAR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 348 FRAYVRKSLPqDCRVEFIPHGgskalnLPFSSES---LSRASRALQAEWDATPVLAGCGGSipivgsfkSD----LNMDT 420
Cdd:cd03891 267 IEAILDKHGL-DYDLEWKLSG------EPFLTKPgklVDAVSAAIKEVTGITPELSTSGGT--------SDarfiASYGC 331
|
410 420
....*....|....*....|..
gi 501585113 421 LMIGFGLEDDRVHSPNEKYELS 442
Cdd:cd03891 332 PVVEFGLVNATIHKVNERVSVA 353
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
46-456 |
7.10e-17 |
|
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: 82.41 E-value: 7.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 46 QFLSDELASLGFEASVRPTAGHP---MVVAHAKAARPDVPHLLFYGHYDVQPPDPLElWESPPFEPkiveAETGRRIVGR 122
Cdd:cd05675 27 EVLAARLAEAGIQTEIFVVESHPgraNLVARIGGTDPSAGPLLLLGHIDVVPADASD-WSVDPFSG----EIKDGYVYGR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 123 GVADDKGQLMTFIEAVRAFKETGDLPCK-ITVLLEGEEETGSPSLPVFLAANKGEL--EADLALvCDTGMWD------RR 193
Cdd:cd05675 102 GAVDMKNMAAMMLAVLRHYKREGFKPKRdLVFAFVADEEAGGENGAKWLVDNHPELfdGATFAL-NEGGGGSlpvgkgRR 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 194 TPAITTMLRGLVTEEVIIRGadRDLHSGIFGSAavNPIHALARVIAGLHDADGKITL---PGFYDAVAELPEEvaEQWRA 270
Cdd:cd05675 181 LYPIQVAEKGIAWMKLTVRG--RAGHGSRPTDD--NAITRLAEALRRLGAHNFPVRLtdeTAYFAQMAELAGG--EGGAL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 271 LKFDEAAFLGAVGLSVPAGEKGRSVLemvwsRPSCDVNGIIGGYTGkgskTVLPAQASAKFSFRLVgaqdPAKIAESFRA 350
Cdd:cd05675 255 MLTAVPVLDPALAKLGPSAPLLNAML-----RNTASPTMLDAGYAT----NVLPGRATAEVDCRIL----PGQSEEEVLD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 351 YVRKSL-PQDCRVEFIPHggSKALNLPFSSESLSRASRALQAEWDATPVlagcggsIPIVGSFKSDLN-MDTLMI-GFGL 427
Cdd:cd05675 322 TLDKLLgDPDVSVEAVHL--EPATESPLDSPLVDAMEAAVQAVDPGAPV-------VPYMSPGGTDAKyFRRLGIpGYGF 392
|
410 420 430
....*....|....*....|....*....|....*....
gi 501585113 428 ----------EDDRVHSPNEKYELSSFHKGARSWARVLD 456
Cdd:cd05675 393 aplflppeldYTGLFHGVDERVPVESLYFGVRFLDRLVK 431
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
22-249 |
1.55e-16 |
|
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: 80.91 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 22 LFKLVSIKSVStdpAFADDCAAAAQFLSDELASLGFEASV-RPTAGHPMVVAHAKAARPDV---PHLLFYGHYDVQPPDP 97
Cdd:TIGR01910 4 LKDLISIPSVN---PPGGNEETIANYIKDLLREFGFSTDViEITDDRLKVLGKVVVKEPGNgneKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 98 LELWESPPFEPKIVEAetgrRIVGRGVADDKGQLMTFIEAVRAFKETGDLPCKITVLLE--GEEETGSPSLpvFLAANKG 175
Cdd:TIGR01910 81 LELWKTDPFKPVEKDG----KLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSvvDEESGEAGTL--YLLQRGY 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501585113 176 ELEADLALVCDTGMWDRrtpaITTMLRGLVTEEVIIRGadRDLHSGiFGSAAVNPIHALARVIAGLHDADGKIT 249
Cdd:TIGR01910 155 FKDADGVLIPEPSGGDN----IVIGHKGSIWFKLRVKG--KQAHAS-FPQFGVNAIMKLAKLITELNELEEHIY 221
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
4-253 |
9.18e-16 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 78.93 E-value: 9.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 4 LKTVLDRIDANLEAALARLFKLVSIKSVSTDPAFADDCAaaaQFLSDELASLGFEA---SVRPtaGHPMVVAHAKAARPD 80
Cdd:PRK08596 1 VSQLLEQIELRKDELLELLKTLVRFETPAPPARNTNEAQ---EFIAEFLRKLGFSVdkwDVYP--NDPNVVGVKKGTESD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 81 VPH-LLFYGHYDVQPPDPLELWESPPFEPKIVEaetgRRIVGRGVADDKGQLMTFIEAVRAFKETG-DLPCKITVL-LEG 157
Cdd:PRK08596 76 AYKsLIINGHMDVAEVSADEAWETNPFEPTIKD----GWLYGRGAADMKGGLAGALFAIQLLHEAGiELPGDLIFQsVIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 158 EE--ETGSpslpvfLAANKGELEADLALVCDTGmwDRRTPAITTMLRGLVT---EEVIIRGADRDL-HSG--IFGSAAvn 229
Cdd:PRK08596 152 EEvgEAGT------LQCCERGYDADFAVVVDTS--DLHMQGQGGVITGWITvksPQTFHDGTRRQMiHAGggLFGASA-- 221
|
250 260
....*....|....*....|....*....
gi 501585113 230 pIHALARVIAGL-----HDADGKiTLPGF 253
Cdd:PRK08596 222 -IEKMMKIIQSLqelerHWAVMK-SYPGF 248
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
22-456 |
2.73e-15 |
|
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349889 [Multi-domain] Cd Length: 367 Bit Score: 76.86 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 22 LFKLVSIKSVStdpafADDCAAAAQFLSDELASLGFEASV--RPTAGHPMVVAhaKAARPDVPHLLFYGHYDVQPPDPlE 99
Cdd:cd03894 3 LARLVAFDTVS-----RNSNLALIEYVADYLAALGVKSRRvpVPEGGKANLLA--TLGPGGEGGLLLSGHTDVVPVDG-Q 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 100 LWESPPFEPKiveaETGRRIVGRGVADDKGQLMTFIEAVRAFKETgDLPCKITVLLEGEEETGSPSLPVFLAANKGELE- 178
Cdd:cd03894 75 KWSSDPFTLT----ERDGRLYGRGTCDMKGFLAAVLAAVPRLLAA-KLRKPLHLAFSYDEEVGCLGVRHLIAALAARGGr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 179 ADLALVCD-TGMwdrrTPAIttMLRGLVTEEVIIRGadRDLHSGIfGSAAVNPIHALARVIAGLhdadgkitlpgfydav 257
Cdd:cd03894 150 PDAAIVGEpTSL----QPVV--AHKGIASYRIRVRG--RAAHSSL-PPLGVNAIEAAARLIGKL---------------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 258 aelpEEVAEQWRALKFDEaaflgavGLSVPAgekgrsvlemvwsrPSCDVNGIIGGytgkGSKTVLPAQASAKFSFRLVG 337
Cdd:cd03894 205 ----RELADRLAPGLRDP-------PFDPPY--------------PTLNVGLIHGG----NAVNIVPAECEFEFEFRPLP 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 338 AQDPAKIAESFRAYVRKSLPQD-CRVEFIPHGGSKALNLPFSSESLSRASRAlqaewdatpvlagCGGSIPIV------G 410
Cdd:cd03894 256 GEDPEAIDARLRDYAEALLEFPeAGIEVEPLFEVPGLETDEDAPLVRLAAAL-------------AGDNKVRTvaygteA 322
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 501585113 411 SFKSDLNMDTLMIGFGlEDDRVHSPNEKYELSSFHKGARSWARVLD 456
Cdd:cd03894 323 GLFQRAGIPTVVCGPG-SIAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
46-241 |
7.68e-15 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 75.89 E-value: 7.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 46 QFLSDELASLGFEAsvrptagHPMVVAHAK---AARP-DVPHLLFYGHYDVQPPDPLELWESPPFEPKIVEaetGrRIVG 121
Cdd:PRK13009 26 DLLAERLEALGFTC-------ERMDFGDVKnlwARRGtEGPHLCFAGHTDVVPPGDLEAWTSPPFEPTIRD---G-MLYG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 122 RGVADDKGQLMTFIEAVRAF-KETGDLPCKITVLLEGEEET----GSPSLPVFLAAnKGELeADLALV----CDTGMWD- 191
Cdd:PRK13009 95 RGAADMKGSLAAFVVAAERFvAAHPDHKGSIAFLITSDEEGpainGTVKVLEWLKA-RGEK-IDYCIVgeptSTERLGDv 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501585113 192 ----RrtpaittmlRGLVTEEVIIRgadrdlhsGIFGSAA-----VNPIHALARVIAGL 241
Cdd:PRK13009 173 ikngR---------RGSLTGKLTVK--------GVQGHVAyphlaDNPIHLAAPALAEL 214
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
65-241 |
1.63e-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: 75.04 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 65 AGHPMVVAHAKAARPDVPHLLFYGHYDVQPPDPLELWESPPFEPKIVEAetgrRIVGRGVADDKGQLMTFIEAVRAFKET 144
Cdd:cd03895 58 AGAPNVVGTHRPRGETGRSLILNGHIDVVPEGPVELWTRPPFEATIVDG----WMYGRGAGDMKAGLAANLFALDALRAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 145 GDLPcKITVLLE---GEEETGSPSLPVFLAANKgeleADLALVCDTgmwdrRTPAITTMLRGLVTEEVIIRGADrdlHSG 221
Cdd:cd03895 134 GLQP-AADVHFQsvvEEECTGNGALAALMRGYR----ADAALIPEP-----TELKLVRAQVGVIWFRVKVRGTP---AHV 200
|
170 180
....*....|....*....|
gi 501585113 222 IFGSAAVNPIHALARVIAGL 241
Cdd:cd03895 201 AEASEGVNAIEKAMHLIQAL 220
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
77-258 |
8.64e-14 |
|
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: 69.77 E-value: 8.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 77 ARPDVPHLLFYGHYDVQPPDPLELWESPPFEPKIVEAetgrRIVGRGVADDKGQLMTFIEAVRAFKETG-DLPCKITVLL 155
Cdd:cd18669 8 GGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEG----RLYGRGALDDKGGVAAALEALKLLKENGfKLKGTVVVAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 156 EGEEETGSPSLPVFLA--ANKGELEADLALVCDTGMWDRRTPAITT--------MLRGLVTEEVIIRGADRDLHSGIFGS 225
Cdd:cd18669 84 TPDEEVGSGAGKGLLSkdALEEDLKVDYLFVGDATPAPQKGVGIRTplvdalseAARKVFGKPQHAEGTGGGTDGRYLQE 163
|
170 180 190
....*....|....*....|....*....|...
gi 501585113 226 AAVNPIHALARVIAGLHDADGKITLPGFYDAVA 258
Cdd:cd18669 164 LGIPGVTLGAGGGKGAHSPNERVNLEDLESALA 196
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
22-162 |
1.17e-13 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 72.50 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 22 LFKLVSIKSVSTDPAFADDCAAAAQFLSDELASLGFEASVRPTAGHPMVVAHAKAARPdvpHLLFYGHYDVQPPDPlELW 101
Cdd:PRK08554 7 LSSLVSFETVNDPSKGIKPSKECPKFIKDTLESWGIESELIEKDGYYAVYGEIGEGKP---KLLFMAHFDVVPVNP-EEW 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501585113 102 ESPPFEPKIveaeTGRRIVGRGVADDKGQLMTFIEAVRAFKETgDLPCKITVLLEGEEETG 162
Cdd:PRK08554 83 NTEPFKLTV----KGDKAYGRGSADDKGNVASVMLALKELSKE-PLNGKVIFAFTGDEEIG 138
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
5-459 |
1.36e-13 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 72.30 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 5 KTVLDRIDANLEAALARLFKLVSIKSVSTDPAFADDCAaaaQFLSDELASLGFEASVRPTA--------GHPMVVAHAKA 76
Cdd:PRK07338 6 RAVLDLIDDRQAPMLEQLIAWAAINSGSRNLDGLARMA---ELLADAFAALPGEIELIPLPpvevidadGRTLEQAHGPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 77 ----ARPDVP-HLLFYGHYD-VQPPDPlelwespPFEPkiVEAETGRRIVGRGVADDKGQLMTFIEAVRAFkETGDLPCK 150
Cdd:PRK07338 83 lhvsVRPEAPrQVLLTGHMDtVFPADH-------PFQT--LSWLDDGTLNGPGVADMKGGIVVMLAALLAF-ERSPLADK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 151 I--TVLLEGEEETGSP-SLPVFLAANKGeleADLALVCDTGMWD------RRTPAITTmlrglvteeVIIRG----ADRD 217
Cdd:PRK07338 153 LgyDVLINPDEEIGSPaSAPLLAELARG---KHAALTYEPALPDgtlagaRKGSGNFT---------IVVTGraahAGRA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 218 LHSGIfgsaavNPIHALARVIAGLHDADGKitlpgfydavaelpeevaeqwralkfdeaaflgavglsvpagekgrsvle 297
Cdd:PRK07338 221 FDEGR------NAIVAAAELALALHALNGQ-------------------------------------------------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 298 mvwsRPSCDVNgiIGGYTGKGSKTVLPAQASAKFSFRLVGAQDPAKIAESFRAYVrKSLPQDCRVEFIPHGGSKALNLPF 377
Cdd:PRK07338 245 ----RDGVTVN--VAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLI-AQVNQRHGVSLHLHGGFGRPPKPI 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 378 SS------ESLSRASRALQAEWDATPVLAGCGGSipivGSFKSDL-NMDTLmigfGLEDDRVHSPNEKYELSSFHKGARS 450
Cdd:PRK07338 318 DAaqqrlfEAVQACGAALGLTIDWKDSGGVCDGN----NLAAAGLpVVDTL----GVRGGNIHSEDEFVILDSLVERAQL 389
|
....*....
gi 501585113 451 WARVLDALA 459
Cdd:PRK07338 390 SALILMRLA 398
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
77-191 |
5.96e-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: 67.45 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 77 ARPDVPHLLFYGHYDVQPPDPLELWESPPFEPKIVEaetgRRIVGRGVADDKGQLMTFIEAVRAFKETG-DLPCKITVLL 155
Cdd:cd03873 8 GGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEE----GRLYGRGALDDKGGVAAALEALKRLKENGfKPKGTIVVAF 83
|
90 100 110
....*....|....*....|....*....|....*...
gi 501585113 156 EGEEETGSPSLPVFLA--ANKGELEADLALVCDTGMWD 191
Cdd:cd03873 84 TADEEVGSGGGKGLLSkfLLAEDLKVDAAFVIDATAGP 121
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
199-360 |
6.19e-12 |
|
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: 61.98 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 199 TMLRGLVTEEVIIRGadRDLHSGiFGSAAVNPIHALARVIAGLHDADGKITLpgfydavaelpeevaeqwralkfdeaaf 278
Cdd:pfam07687 1 IGHKGLAGGHLTVKG--KAGHSG-APGKGVNAIKLLARLLAELPAEYGDIGF---------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 279 lgavglsvpagekgrsvlemVWSRPSCDVNGIIGGYtgkgSKTVLPAQASAKFSFRLVGAQDPAKIAESFRAYVRKSLPQ 358
Cdd:pfam07687 50 --------------------DFPRTTLNITGIEGGT----ATNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEKELPE 105
|
..
gi 501585113 359 DC 360
Cdd:pfam07687 106 GE 107
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
1-166 |
6.94e-12 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 66.95 E-value: 6.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 1 MAALKTVLDRIDANLEAALARLFKLVSIKSVSTDPAFADdcaaaaQFLSDELASLGFEA---SVRPTA------------ 65
Cdd:PRK06837 5 PDLTQRILAAVDAGFDAQVAFTQDLVRFPSTRGAEAPCQ------DFLARAFRERGYEVdrwSIDPDDlkshpgagpvei 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 66 ---GHPMVVAHAKAARPDVPHLLFYGHYDVQPPDPLELWESPPFEPKIVEAetgrRIVGRGVADDKGQLMTFIEAVRAFK 142
Cdd:PRK06837 79 dysGAPNVVGTYRPAGKTGRSLILQGHIDVVPEGPLDLWSRPPFDPVIVDG----WMYGRGAADMKAGLAAMLFALDALR 154
|
170 180
....*....|....*....|....*..
gi 501585113 143 ETGDLPcKITVLLEG---EEETGSPSL 166
Cdd:PRK06837 155 AAGLAP-AARVHFQSvieEESTGNGAL 180
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
68-260 |
1.44e-11 |
|
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: 65.94 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 68 PMVVAHAKAARPDVPHLLfyGHYDVQPPDPLELWESPPFEPKIveaeTGRRIVGRGVADDKGQLMTFIEAVRAFKETGDL 147
Cdd:cd05650 58 PNIVAKIPGGNDKTLWII--SHLDTVPPGDLSLWETDPWEPVV----KDGKIYGRGVEDNQQGIVSSLLALKAIIKNGIT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 148 P-CKITVLLEGEEETGSPSLPVFLaANKGEL--EADLALVCDTGMWDRRTPAITTmlRGLVTEEVIIRGadRDLHsgifG 224
Cdd:cd05650 132 PkYNFGLLFVADEEDGSEYGIQYL-LNKFDLfkKDDLIIVPDFGTEDGEFIEIAE--KSILWIKVNVKG--KQCH----A 202
|
170 180 190
....*....|....*....|....*....|....*....
gi 501585113 225 SAAVNPIHAL---ARVIAGLHDADGKitlpgFYDAVAEL 260
Cdd:cd05650 203 STPENGINAFvaaSNFALELDELLHE-----KFDEKDDL 236
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
47-252 |
2.27e-11 |
|
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: 65.10 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 47 FLSDELASLGFEASVRPTA-GHPMVVAHAKAARPDvPHLLFYGHYDVQPPDPLELWESPPFEPKIVEAetgrRIVGRGVA 125
Cdd:cd08011 26 YIKLLLEDLGYPVELHEPPeEIYGVVSNIVGGRKG-KRLLFNGHYDVVPAGDGEGWTVDPYSGKIKDG----KLYGRGSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 126 DDKGQLMTFIEAVRAFKETG---DLPCKITvlLEGEEETGSPSLPVFLaANKGELEADLALVC-DTGmwdrrTPAITTML 201
Cdd:cd08011 101 DMKGGIAASIIAVARLADAKapwDLPVVLT--FVPDEETGGRAGTKYL-LEKVRIKPNDVLIGePSG-----SDNIRIGE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 501585113 202 RGLVteEVIIRGADRDLHSGiFGSAAVNPIHALARVIAGLHDADgKITLPG 252
Cdd:cd08011 173 KGLV--WVIIEITGKPAHGS-LPHRGESAVKAAMKLIERLYELE-KTVNPG 219
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
88-245 |
2.97e-11 |
|
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: 65.09 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 88 GHYDVQPPDplELWESPPFEPKIVEAetgrRIVGRGVADDKGQLMTFIEAVRAFKETG-DLPCKITVLLEGEEETGSPSL 166
Cdd:TIGR01887 74 GHLDVVPAG--DGWTSPPFEPTIKDG----RIYGRGTLDDKGPTIAAYYAMKILKELGlKLKKKIRFIFGTDEESGWKCI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 167 PVFLaanKGELEADLALVCDTGMwdrrtpAITTMLRGLVTEEVIIRGADRD---LHSGIFGSAA-VNPIHALArVIAGLH 242
Cdd:TIGR01887 148 DYYF---EHEEMPDIGFTPDAEF------PIIYGEKGITTLEIKFKDDTEGdvvLESFKAGEAYnMVPDHATA-VISGKK 217
|
...
gi 501585113 243 DAD 245
Cdd:TIGR01887 218 LTE 220
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
46-145 |
3.08e-11 |
|
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: 64.99 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 46 QFLSDELASLGFEA-SVRPTAGHPMVVAHAKAARPDVPHLLFYGHYDVQPPDPlELWESPPFEPKIveAETGRrIVGRGV 124
Cdd:cd05646 28 EFLKRQADELGLPVrVIEVVPGKPVVVLTWEGSNPELPSILLNSHTDVVPVFE-EKWTHDPFSAHK--DEDGN-IYARGA 103
|
90 100
....*....|....*....|.
gi 501585113 125 ADDKGQLMTFIEAVRAFKETG 145
Cdd:cd05646 104 QDMKCVGIQYLEAIRRLKASG 124
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
88-191 |
1.48e-10 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 62.56 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 88 GHYDVQPPDPLELWESPPFEPkIVEaetGRRIVGRGVADDKGQLMTFIEAVRAFKETGDLPcKITV--LLEGEEETGSPS 165
Cdd:PRK13983 83 SHMDVVPPGDLSLWETDPFKP-VVK---DGKIYGRGSEDNGQGIVSSLLALKALMDLGIRP-KYNLglAFVSDEETGSKY 157
|
90 100
....*....|....*....|....*...
gi 501585113 166 LPVFLAANKGEL--EADLALVCDTGMWD 191
Cdd:PRK13983 158 GIQYLLKKHPELfkKDDLILVPDAGNPD 185
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
88-174 |
3.13e-10 |
|
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: 61.88 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 88 GHYDVQPPDplELWESPPFEPKIveaeTGRRIVGRGVADDKGQLMTFIEAVRAFKETG-DLPCKITVLLEGEEETGSPSL 166
Cdd:cd03888 78 GHLDVVPAG--EGWTTDPFKPVI----KDGKLYGRGTIDDKGPTIAALYALKILKDLGlPLKKKIRLIFGTDEETGWKCI 151
|
....*...
gi 501585113 167 PVFLAANK 174
Cdd:cd03888 152 EHYFEHEE 159
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
79-354 |
1.51e-09 |
|
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: 59.96 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 79 PDVPHLLFYGHYDVQP--PDPLELWESPPFEpkivEAETGRRIVGRGVADDKGQLMTFIEAVRAFKETGDLPcKITVLLE 156
Cdd:cd05674 67 PSLKPLLLMAHQDVVPvnPETEDQWTHPPFS----GHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKP-RRTIILA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 157 --GEEETGSPSLPVFLAAnkgELEA-----DLALVCDTGM-----WDRRTPA--ITTMLRGLVTEEVIIRGAdrdlhsGi 222
Cdd:cd05674 142 fgHDEEVGGERGAGAIAE---LLLErygvdGLAAILDEGGavlegVFLGVPFalPGVAEKGYMDVEITVHTP------G- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 223 fGSAAVNPIH----ALARVIAGLHDA--DGKITLP----GFYDAVAELPEEVAEQWRALkFDEAAFLGAVGLSVPAGEKG 292
Cdd:cd05674 212 -GHSSVPPKHtgigILSEAVAALEANpfPPKLTPGnpyyGMLQCLAEHSPLPPRSLKSN-LWLASPLLKALLASELLSTS 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501585113 293 RSVLEMVWSRPSCDvngIIGGytgkGSKT-VLPAQASAKFSFRLVGAQDPAKIAESFRAYVRK 354
Cdd:cd05674 290 PLTRALLRTTQAVD---IING----GVKInALPETATATVNHRIAPGSSVEEVLEHVKNLIAD 345
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
10-189 |
5.03e-09 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 58.42 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 10 RIDANLEAALARLFKLVSIKSVSTDPAFADDCAAAAQF---LSDELASLGFEASVRPTAGHPMVVaHAKAARPDVPHLLF 86
Cdd:PRK08262 38 PVAVDEDAAAERLSEAIRFRTISNRDRAEDDAAAFDALhahLEESYPAVHAALEREVVGGHSLLY-TWKGSDPSLKPIVL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 87 YGHYDVQPPDP--LELWESPPFEPKIVEAetgrRIVGRGVADDKGQLMTFIEAVRAFKETGDLPcKITVLLE--GEEETG 162
Cdd:PRK08262 117 MAHQDVVPVAPgtEGDWTHPPFSGVIADG----YVWGRGALDDKGSLVAILEAAEALLAQGFQP-RRTIYLAfgHDEEVG 191
|
170 180 190
....*....|....*....|....*....|
gi 501585113 163 SPSLPVfLAAnkgELEA---DLALVCDTGM 189
Cdd:PRK08262 192 GLGARA-IAE---LLKErgvRLAFVLDEGG 217
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
46-460 |
6.33e-09 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 57.51 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 46 QFLSDELASLGFEASVRPTAGHPmvvahaKA---AR--P-DVPHLLFYGHYDVQPPDPLElWESPPFEPKiveaETGRRI 119
Cdd:PRK07522 29 EWVRDYLAAHGVESELIPDPEGD------KAnlfATigPaDRGGIVLSGHTDVVPVDGQA-WTSDPFRLT----ERDGRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 120 VGRGVADDKGQLMTFIEAVRAFKETG-DLPckITVLLEGEEETGSPSLPVFLAANKGELE-ADLALVcdtgmwdrrtpai 197
Cdd:PRK07522 98 YGRGTCDMKGFIAAALAAVPELAAAPlRRP--LHLAFSYDEEVGCLGVPSMIARLPERGVkPAGCIV------------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 198 ttmlrGLVTEEVIIRGadrdlHSGIF-------GSAA--------VNPIHALARVIAGLHDADGKITLPGFYDAVaelpe 262
Cdd:PRK07522 163 -----GEPTSMRPVVG-----HKGKAayrctvrGRAAhsslapqgVNAIEYAARLIAHLRDLADRLAAPGPFDAL----- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 263 evaeqwralkFDeaaflgavglsVPagekgrsvlemvWSrpSCDVNGIIGGytgkgskTVL---PAQASAKFSFRLVGAQ 339
Cdd:PRK07522 228 ----------FD-----------PP------------YS--TLQTGTIQGG-------TALnivPAECEFDFEFRNLPGD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 340 DPAKIAESFRAYVRKSL-PQ------DCRVEFIPHGGSKALNLPFSSEsLSRASRALQAEWDATPVLAGCGGsipivGSF 412
Cdd:PRK07522 266 DPEAILARIRAYAEAELlPEmravhpEAAIEFEPLSAYPGLDTAEDAA-AARLVRALTGDNDLRKVAYGTEA-----GLF 339
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 501585113 413 kSDLNMDTLMIGFGlEDDRVHSPNEKYELSSFHKGARSWARVLDALAL 460
Cdd:PRK07522 340 -QRAGIPTVVCGPG-SIEQAHKPDEFVELAQLAACEAFLRRLLASLAA 385
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
47-162 |
1.52e-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: 56.34 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 47 FLSDELASLGFEA-SVRPTAGHPMVVAHAKAARPDVPHLLFYGHYDVQPPDPlELWESPPFEPKIveAETGRrIVGRGVA 125
Cdd:TIGR01880 36 FLIKQADELGLARkTIEFVPGKPVVVLTWPGSNPELPSILLNSHTDVVPVFR-EHWTHPPFSAFK--DEDGN-IYARGAQ 111
|
90 100 110
....*....|....*....|....*....|....*...
gi 501585113 126 DDKGQLMTFIEAVRAFKETGDLPCK-ITVLLEGEEETG 162
Cdd:TIGR01880 112 DMKCVGVQYLEAVRNLKASGFKFKRtIHISFVPDEEIG 149
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
88-161 |
5.58e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 54.70 E-value: 5.58e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501585113 88 GHYDVQPPDPLELWESPPFEPKIVEAetgrRIVGRGVADDKGQLMTFIEAVRAFKETG-DLPCKITVLLEGEEET 161
Cdd:PRK07205 82 CHLDVVPEGDLSDWQTPPFEAVEKDG----CLFGRGTQDDKGPSMAALYAVKALLDAGvQFNKRIRFIFGTDEET 152
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
88-163 |
2.76e-07 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 52.54 E-value: 2.76e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501585113 88 GHYDVQPPDplELWESPPFEPKIVEAetgrRIVGRGVADDKGQLMTFIEAVRAFKETG-DLPCKITVLLEGEEETGS 163
Cdd:PRK07318 86 GHLDVVPAG--DGWDTDPYEPVIKDG----KIYARGTSDDKGPTMAAYYALKIIKELGlPLSKKVRFIVGTDEESGW 156
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
46-183 |
5.84e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 51.54 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 46 QFLSDELASLGFEAS-VRPTAGHPM---VVAHAKAARPDVPhLLFYGHYDVQPPDPlELWESPPFEPkiveAETGRRIVG 121
Cdd:PRK09133 63 EAMAARLKAAGFADAdIEVTGPYPRkgnLVARLRGTDPKKP-ILLLAHMDVVEAKR-EDWTRDPFKL----VEENGYFYG 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501585113 122 RGVADDKGQLMTFIEAVRAFKETGDLPCK-ITVLLEGEEETGSPSLPVFLAANKGEL-EADLAL 183
Cdd:PRK09133 137 RGTSDDKADAAIWVATLIRLKREGFKPKRdIILALTGDEEGTPMNGVAWLAENHRDLiDAEFAL 200
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
2-164 |
6.29e-07 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 51.56 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 2 AALKTVLDRIDANLEAALARLFKLVSIKSVStdpAFADDCAAAAQFLSDELASLGFEASVRPTAGH--PMVVAHAKA--- 76
Cdd:PRK06133 23 APDAELLAAAQQEQPAYLDTLKELVSIESGS---GDAEGLKQVAALLAERLKALGAKVERAPTPPSagDMVVATFKGtgk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 77 ARpdvphLLFYGHYD-VQPPDPLElweSPPFEpkiveaETGRRIVGRGVADDKGQLMTFIEAV-----RAFKETGdlpcK 150
Cdd:PRK06133 100 RR-----IMLIAHMDtVYLPGMLA---KQPFR------IDGDRAYGPGIADDKGGVAVILHALkilqqLGFKDYG----T 161
|
170
....*....|....
gi 501585113 151 ITVLLEGEEETGSP 164
Cdd:PRK06133 162 LTVLFNPDEETGSP 175
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
79-286 |
7.10e-07 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349902 [Multi-domain] Cd Length: 341 Bit Score: 51.16 E-value: 7.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 79 PDVPHLLFYGHYDVQPPDplELWESPPFEPKiveaETGRRIVGRGVADDKGQLMTFIEAVRAFKETGDLPCKITVLLEGE 158
Cdd:cd05651 53 EGKPTLLLNSHHDTVKPN--AGWTKDPFEPV----EKGGKLYGLGSNDAGASVVSLLATFLHLYSEGPLNYNLIYAASAE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 159 EETGS--------PSLPvflaankgelEADLALVCD-TGMwdrrTPAITTmlRGLVTEEVIIRGADrdlhsgifGSAA-- 227
Cdd:cd05651 127 EEISGkngiesllPHLP----------PLDLAIVGEpTEM----QPAIAE--KGLLVLDCTARGKA--------GHAArn 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501585113 228 --VNPIHALARVIAGLhdadgkitlpgfydavaelpeevaeqwRALKFDEAA-FLGAVGLSV 286
Cdd:cd05651 183 egDNAIYKALDDIQWL---------------------------RDFRFDKVSpLLGPVKMTV 217
|
|
| PRK06915 |
PRK06915 |
peptidase; |
1-162 |
1.89e-06 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 50.08 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 1 MAALKT-VLDRIDANLEAALARLFKLVSIKSVStdpafaDDCAAAAQFLSDELASLGFE-----------------ASVR 62
Cdd:PRK06915 1 MEQLKKqICDYIESHEEEAVKLLKRLIQEKSVS------GDESGAQAIVIEKLRELGLDldiwepsfkklkdhpyfVSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 63 PT-AGHPMVVAHAKAArPDVPHLLFYGHYDVQPPDPLELWESPPFEPKIVeaetGRRIVGRGVADDKGQLMTFIEAVRAF 141
Cdd:PRK06915 75 TSfSDSPNIVATLKGS-GGGKSMILNGHIDVVPEGDVNQWDHHPYSGEVI----GGRIYGRGTTDMKGGNVALLLAMEAL 149
|
170 180
....*....|....*....|...
gi 501585113 142 KETGdLPCKITVLLEG--EEETG 162
Cdd:PRK06915 150 IESG-IELKGDVIFQSviEEESG 171
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
89-173 |
2.21e-06 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 49.97 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 89 HYDVQPPDPlELW--ESPPFEPKIVEaETGRRIVGRGVADDKGQLMTFIEAVRAFKETGdLPCK--ITVLLEGEEETGSP 164
Cdd:PRK06156 117 HADVVPANP-ELWvlDGTRLDPFKVT-LVGDRLYGRGTEDDKGAIVTALYAMKAIKDSG-LPLArrIELLVYTTEETDGD 193
|
....*....
gi 501585113 165 SLPVFLAAN 173
Cdd:PRK06156 194 PLKYYLERY 202
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
84-160 |
3.70e-06 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 48.78 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 84 LLFYGHYDVQPPDPLELWESPPFEPKIVEAetgrRIVGRGVADDKGQLMTFIEAVRAFKETGdLPCKITVLLEG---EEE 160
Cdd:PRK13004 72 IAFDAHIDTVGIGDIKNWDFDPFEGEEDDG----RIYGRGTSDQKGGMASMVYAAKIIKDLG-LDDEYTLYVTGtvqEED 146
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
56-165 |
7.37e-06 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 47.86 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 56 GFEASVRPTAGHPmvvahakaaRPDVPHLLFYGHYD-VQPPDPLELWespPFEpkiveaETGRRIVGRGVADDKGQLMTF 134
Cdd:PRK07473 59 GFGDCVRARFPHP---------RQGEPGILIAGHMDtVHPVGTLEKL---PWR------REGNKCYGPGILDMKGGNYLA 120
|
90 100 110
....*....|....*....|....*....|..
gi 501585113 135 IEAVRAFKETG-DLPCKITVLLEGEEETGSPS 165
Cdd:PRK07473 121 LEAIRQLARAGiTTPLPITVLFTPDEEVGTPS 152
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
84-160 |
2.68e-05 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 46.26 E-value: 2.68e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501585113 84 LLFYGHYDVQPPDPLELWESPPFEPKIVEAEtgrrIVGRGVADDKGQLMTFIEAVRAFKETGDLPCKITVLLEG--EEE 160
Cdd:cd05649 55 ILFDGHIDTVGIGNIDNWKFDPYEGYETDGK----IYGRGTSDQKGGLASMVYAAKIMKDLGLRDFAYTILVAGtvQEE 129
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
52-392 |
4.38e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 45.61 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 52 LASLGFEAS-VRPTAGHPMVVAHAKAARPDVPHLLFYGHYDVQPPDPLElWESPPFEPKIVEAetgrRIVGRGVADDKGQ 130
Cdd:PRK07906 35 LAEVGLEPTyLESAPGRANVVARLPGADPSRPALLVHGHLDVVPAEAAD-WSVHPFSGEIRDG----YVWGRGAVDMKDM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 131 LMTFIEAVRAFKETGDLPCK-ITVLLEGEEETGSPSLPVFLAANKGEL-----EAdlalVCDTGMW------DRRTPAIT 198
Cdd:PRK07906 110 DAMMLAVVRHLARTGRRPPRdLVFAFVADEEAGGTYGAHWLVDNHPELfegvtEA----ISEVGGFsltvpgRDRLYLIE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 199 TMLRGLVTEEVIIRGadRDLHsgifGSA--AVNPIHALARVIAGLHDADGKITLPgfyDAVAELPEEVAEQWrALKFDE- 275
Cdd:PRK07906 186 TAEKGLAWMRLTARG--RAGH----GSMvnDDNAVTRLAEAVARIGRHRWPLVLT---PTVRAFLDGVAELT-GLEFDPd 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 276 --AAFLGAVGlsvPAGEKGRSVLemvwsRPSCDVNGIIGGYtgkgsKT-VLPAQASAKFSFR-LVGAQdpakiaESFRAY 351
Cdd:PRK07906 256 dpDALLAKLG---PAARMVGATL-----RNTANPTMLKAGY-----KVnVIPGTAEAVVDGRfLPGRE------EEFLAT 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 501585113 352 VRKSLPQDCRVEFIPHggSKALNLPFSSESLSRASRALQAE 392
Cdd:PRK07906 317 VDELLGPDVEREWVHR--DPALETPFDGPLVDAMNAALLAE 355
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
11-212 |
4.39e-05 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 45.33 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 11 IDANLEAALARLFKLVSIKSVSTDPAFADdcaaaaQFLSDELASLGFEASVrPTAGHpmVVAHAKAARPDVphlLFYGHY 90
Cdd:PRK04443 1 MTISALEARELLKGLVEIPSPSGEEAAAA------EFLVEFMESHGREAWV-DEAGN--ARGPAGDGPPLV---LLLGHI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 91 DVQPPD-PlelwesppfepkiVEAETGrRIVGRGVADDKGQLMTFIEAVRAFKETgdLPCKITVLLEGEEETGSpSLPVF 169
Cdd:PRK04443 69 DTVPGDiP-------------VRVEDG-VLWGRGSVDAKGPLAAFAAAAARLEAL--VRARVSFVGAVEEEAPS-SGGAR 131
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 501585113 170 LAANKgeLEADLALVCDTGMWDRrtpaITTMLRGLVTEEVIIR 212
Cdd:PRK04443 132 LVADR--ERPDAVIIGEPSGWDG----ITLGYKGRLLVTYVAT 168
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
47-243 |
4.35e-04 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 42.47 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 47 FLSDELASLGFEASVRPTAGHPMVVAHAKAARPdvpHLLFYGHYDVQPP--DPLELWESppfepkiveaetGRRIVGRGV 124
Cdd:cd03896 23 LVAEWMADLGLGDVERDGRGNVVGRLRGTGGGP---ALLFSAHLDTVFPgdTPATVRHE------------GGRIYGPGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 125 ADDKGQLMTFIEAVRAFKETGdlpckitVLLEGeeetgspslPVFLAANKGELEadlaLVCDTGMwdRRtpaITTMLRGL 204
Cdd:cd03896 88 GDNKGSLACLLAMARAMKEAG-------AALKG---------DVVFAANVGEEG----LGDLRGA--RY---LLSAHGAR 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501585113 205 VTEEVIIRGADRDLHSGIFGS------------------AAVNPIHALARVIAGLHD 243
Cdd:cd03896 143 LDYFVVAEGTDGVPHTGAVGSkrfrittvgpgghsygafGSPSAIVAMAKLVEALYE 199
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
18-163 |
1.83e-03 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal, and have been inferred by similarity as being related to both ArgE and DapE.
Pssm-ID: 349903 [Multi-domain] Cd Length: 340 Bit Score: 40.34 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 18 ALARLFKLVSIKSVStdpafaDDCAAAAQFLSDELASLGF--EASVRPTAGHPMVVAHAKAARPdvPHLLFYGHYDVqpp 95
Cdd:cd05652 1 LLSLHKSLVEIPSIS------GNEAAVGDFLAEYLESLGFtvEKQPVENKDRFNVYAYPGSSRQ--PRVLLTSHIDT--- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 96 dplelweSPPFEPKIVEaETGRRIVGRGVADDKGQLMTFIEAVRAFKETGDLPCKITVLL--EGEEETGS 163
Cdd:cd05652 70 -------VPPFIPYSIS-DGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLfvVGEETGGD 131
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
47-164 |
2.20e-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: 40.03 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 47 FLSDELASLGFEASVrPTAGHpmVVAHAKAARPDVphlLFYGHYDVQPPDplelwesppFEPKIVeaetGRRIVGRGVAD 126
Cdd:cd05653 26 FLEEIMKELGLEAWV-DEAGN--AVGGAGSGPPDV---LLLGHIDTVPGE---------IPVRVE----GGVLYGRGAVD 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 501585113 127 DKGQLMTFIEAVRAFKEtgDLPCKITVLLEGEEETGSP 164
Cdd:cd05653 87 AKGPLAAMILAASALNE--ELGARVVVAGLVDEEGSSK 122
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
47-241 |
2.27e-03 |
|
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349932 [Multi-domain] Cd Length: 368 Bit Score: 40.13 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 47 FLSDELASLGFE-----ASVRPTAGHPMVVAHAKAARPDVPHLLFYGHYD-VQPPDPLelwesppfePKIVEAE-----T 115
Cdd:cd05683 28 VLKKKFENLGLSvieddAGKTTGGGAGNLICTLKADKEEVPKILFTSHMDtVTPGINV---------KPPQIADgyiysD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501585113 116 GRRIVGrgvADDKGQLMTFIEAVRAFKE----TGDLPCKITVlleGEEE--TGSPSLpvflaaNKGELEADLALVCDTGm 189
Cdd:cd05683 99 GTTILG---ADDKAGIAAILEAIRVIKEknipHGQIQFVITV---GEESglVGAKAL------DPELIDADYGYALDSE- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501585113 190 wdrrTPAITTMLRGLVTEEV--IIRGadRDLHSGIFGSAAVNPIHALARVIAGL 241
Cdd:cd05683 166 ----GDVGTIIVGAPTQDKInaKIYG--KTAHAGTSPEKGISAINIAAKAISNM 213
|
|
| |
