|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
1-451 |
0e+00 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 701.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 1 MSSNPVAETVASLMPRAKEELTELVAFRSVAdFDQFPRSESEGAARWVADALAAEGFQDVALLDtPDGTQSVYGYLPGPE 80
Cdd:PRK07907 4 LTADDLRARVAELLPRVRADLEELVRIPSVA-ADPFRREEVARSAEWVADLLREAGFDDVRVVS-ADGAPAVIGTRPAPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 81 GAKTVLLYAHYDVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALkaNGGVPVHVKVIAEGSEEQGT 160
Cdd:PRK07907 82 GAPTVLLYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRAL--GGDLPVGVTVFVEGEEEMGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 161 GGLERYAEEHPGLLEADTIVIGDAGNFRVGLPTVTATLRGMTLVRVRIDTLAGNLHSGQFGGAAPDALAALIRVLDSLRA 240
Cdd:PRK07907 160 PSLERLLAEHPDLLAADVIVIADSGNWSVGVPALTTSLRGNADVVVTVRTLEHAVHSGQFGGAAPDALTALVRLLATLHD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 241 EDGSTTVDGLTGDTAWDGLQYDEERFRQDAKVLDGVGLIGSGTVADRIWARPAVTVLGIDCPPVVGATPSVQASARALIS 320
Cdd:PRK07907 240 EDGNVAVDGLDATEPWLGVDYDEERFRADAGVLDGVELIGTGSVADRLWAKPAITVIGIDAPPVAGASNALPPSARARLS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 321 LRVPPGVDAAEATKLLQAHLEARTPWGARVSTEQIGQGQAFRADTTSPAYQAMADAMAVAYpGQEMQYAGQGGSIPLCNT 400
Cdd:PRK07907 320 LRVAPGQDAAEAQDALVAHLEAHAPWGAHVTVERGDAGQPFAADASGPAYDAARAAMREAW-GKDPVDMGMGGSIPFIAE 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1752498394 401 LAALYPRAEILLIGLSEPEAQIHAVNESVSPEELERLSVAEALFLRNYAAS 451
Cdd:PRK07907 399 LQEAFPQAEILVTGVEDPKTRAHSPNESVHLGELERAAVAEALLLARLAAA 449
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
18-447 |
1.13e-172 |
|
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: 491.07 E-value: 1.13e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 18 KEELTELVAFRSVADFDQFpRSESEGAARWVADALAAEGFqDVALLDTPDGTQSVYGYLPGPEGAKTVLLYAHYDVQPPL 97
Cdd:cd03893 1 LQTLAELVAIPSVSAQPDR-REELRRAAEWLADLLRRLGF-TVEIVDTSNGAPVVFAEFPGAPGAPTVLLYGHYDVQPAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 98 DEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGG-VPVHVKVIAEGSEEQGTGGLERYAEEHPGLLEA 176
Cdd:cd03893 79 DEDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGdLPVNVKFIIEGEEESGSPSLDQLVEAHRDLLAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 177 DTIVIGDAGNFRVGLPTVTATLRGMTLVRVRIDTLAGNLHSGQFGGAAPDALAALIRVLDSLRAEDGSTTVDGLTGDTAw 256
Cdd:cd03893 159 DAIVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLDHDLHSGLYGGVVPDPMTALAQLLASLRDETGRILVPGLYDAVR- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 257 dglQYDEERFRQDAKVLDGVGLIGS--GTVADRIWARPAVTVLGIDCPPVV-GATPSVQASARALISLRVPPGVDAAEAT 333
Cdd:cd03893 238 ---ELPEEEFRLDAGVLEEVEIIGGttGSVAERLWTRPALTVLGIDGGFPGeGSKTVIPPRARAKISIRLVPGQDPEEAS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 334 KLLQAHLEARTPWGARVSTEQIGQGQAFRADTTSPAYQAMADAMAVAYpGQEMQYAGQGGSIPLCNTLAAlYPRAEILLI 413
Cdd:cd03893 315 RLLEAHLEKHAPSGAKVTVSYVEGGMPWRSDPSDPAYQAAKDALRTAY-GVEPPLTREGGSIPFISVLQE-FPQAPVLLI 392
|
410 420 430
....*....|....*....|....*....|....
gi 1752498394 414 GLSEPEAQIHAVNESVSPEELERLSVAEALFLRN 447
Cdd:cd03893 393 GVGDPDDNAHSPNESLRLGNYKEGTQAEAALLYS 426
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
19-448 |
2.36e-100 |
|
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: 306.93 E-value: 2.36e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 19 EELTELVAFRSV-ADFDQfpRSESEGAARWVADALAAEGFQDVALLDTPdGTQSVYGYLPGPEGAKTVLLYAHYDVQPPL 97
Cdd:cd05680 2 EELFELLRIPSVsADPAH--KGDVRRAAEWLADKLTEAGFEHTEVLPTG-GHPLVYAEWLGAPGAPTVLVYGHYDVQPPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 98 DEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRA-LKANGGVPVHVKVIAEGSEEQGTGGLERYAEEHPGLLEA 176
Cdd:cd05680 79 PLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAwLAVEGALPVNVKFLIEGEEEIGSPSLPAFLEENAERLAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 177 DTIVIGDAGNFRVGLPTVTATLRGMTLVRVRIDTLAGNLHSGQFGGAAPDALAALIRVLDSLRAEDGSTTVDGLTGDT-- 254
Cdd:cd05680 159 DVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNRDLHSGSYGGAVPNPANALARLLASLHDEDGRVAIPGFYDDVrp 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 255 -------AWDGLQYDEERFRQDAKVLDGVGLIGSGTVaDRIWARPAVTVLGIDCPPV-VGATPSVQASARALISLRVPPG 326
Cdd:cd05680 239 ltdaereAWAALPFDEAAFKASLGVPALGGEAGYTTL-ERLWARPTLDVNGIWGGYQgEGSKTVIPSKAHAKISMRLVPG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 327 VDAAEATKLLQAHLEARTPWGARVSTEQIGQGQAFRADTTSPAYQAMADAMAVAYpGQEMQYAGQGGSIPLCNTLAALYp 406
Cdd:cd05680 318 QDPDAIADLLEAHLRAHAPPGVTLSVKPLHGGRPYLVPTDHPALQAAERALEEAF-GKPPVFVREGGSIPIVALFEKVL- 395
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1752498394 407 RAEILLIGLSEPEAQIHAVNESVSPEELERLSVAEALFLRNY 448
Cdd:cd05680 396 GIPTVLMGFGLPDDAIHAPNEKFRLECFHKGIEAIAHLLARL 437
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
19-450 |
3.96e-87 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 273.54 E-value: 3.96e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 19 EELTELVAFRSVADFDQFpRSESEGAARWVADALAAEGFQDVALLDTPdGTQSVYGYLPGPEGAKTVLLYAHYDVQP--P 96
Cdd:PRK08201 18 EELKEFLRIPSISALSEH-KEDVRKAAEWLAGALEKAGLEHVEIMETA-GHPIVYADWLHAPGKPTVLIYGHYDVQPvdP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 97 LDEagWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRA-LKANGGVPVHVKVIAEGSEEQGTGGLERYAEEHPGLLE 175
Cdd:PRK08201 96 LNL--WETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEAlLKVEGTLPVNVKFCIEGEEEIGSPNLDSFVEEEKDKLA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 176 ADTIVIGDAGNFRVGLPTVTATLRGMTLVRVRIDTLAGNLHSGQFGGAAPDALAALIRVLDSLRAEDGSTTVDGLTGDT- 254
Cdd:PRK08201 174 ADVVLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLHSGLYGGAVPNALHALVQLLASLHDEHGTVAVEGFYDGVr 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 255 --------AWDGLQYDEERFRQDAKVLDGVGLIGSgTVADRIWARPAVTVLGIDCPPVVGATPSV-QASARALISLRVPP 325
Cdd:PRK08201 254 pltpeereEFAALGFDEEKLKRELGVDELFGEEGY-TALERTWARPTLELNGVYGGFQGEGTKTViPAEAHAKITCRLVP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 326 GVDAAEATKLLQAHLEARTPWGARVSTEQIGQGQAFRADTTSPAYQAMADAMAVAYpGQEMQYAGQGGSIPLCNTLAALY 405
Cdd:PRK08201 333 DQDPQEILDLIEAHLQAHTPAGVRVTIRRFDKGPAFVAPIDHPAIQAAARAYEAVY-GTEAAFTRMGGSIPVVETFSSQL 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1752498394 406 pRAEILLIGLSEPEAQIHAVNESVSPEELERLSVAEALFLRNYAA 450
Cdd:PRK08201 412 -HIPIVLMGFGLPSENFHAPNEHFHLENFDKGLRTLVEYWHQLAE 455
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
5-450 |
5.13e-81 |
|
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: 255.58 E-value: 5.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 5 PVAETVASLMPRAKEELTELVAFRSVadfdqfPRSEsEGAARWVADALAAEGFqDVALLDTPDGTQSVYGYLPGPEGAKT 84
Cdd:COG0624 2 AVLAAIDAHLDEALELLRELVRIPSV------SGEE-AAAAELLAELLEALGF-EVERLEVPPGRPNLVARRPGDGGGPT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 85 VLLYAHYDVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVP-VHVKVIAEGSEEQGTGGL 163
Cdd:COG0624 74 LLLYGHLDVVPPGDLELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLpGNVTLLFTGDEEVGSPGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 164 ERYAEEHPGLLEADTIVIGDAGnfrvGLPTVTATLRGMTLVRVRIDTLAGnlHSGQFgGAAPDALAALIRVLDSLRAEDG 243
Cdd:COG0624 154 RALVEELAEGLKADAAIVGEPT----GVPTIVTGHKGSLRFELTVRGKAA--HSSRP-ELGVNAIEALARALAALRDLEF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 244 STTVDGLTGdtawdglqydeerfrqdakvldgvgligsgtvadriwaRPAVTVLGIDCPPVVGATPsvqASARALISLRV 323
Cdd:COG0624 227 DGRADPLFG--------------------------------------RTTLNVTGIEGGTAVNVIP---DEAEAKVDIRL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 324 PPGVDAAEATKLLQAHLEARTPwGARVSTEQIG-QGQAFRADTTSPAYQAMADAMAVAYpGQEMQYAGQGGSIPLCNTLA 402
Cdd:COG0624 266 LPGEDPEEVLAALRALLAAAAP-GVEVEVEVLGdGRPPFETPPDSPLVAAARAAIREVT-GKEPVLSGVGGGTDARFFAE 343
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1752498394 403 ALypRAEILLIGLSEPeAQIHAVNESVSPEELERLSVAEALFLRNYAA 450
Cdd:COG0624 344 AL--GIPTVVFGPGDG-AGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
1-427 |
3.12e-58 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 198.20 E-value: 3.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 1 MSSNPVAETVASLMPRAKEELTELVAFRSVADfDQFPRSESEGAARWVADALAAEGFqDVALLDTPdGTQSVYGYLPGPE 80
Cdd:PRK09104 3 ADLDPVLDHIDANLDASLERLFALLRIPSIST-DPAYAADCRKAADWLVADLASLGF-EASVRDTP-GHPMVVAHHEGPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 81 G-AKTVLLYAHYDVQP--PLDEagWATPPFE--LTER-DGR--WYGRGAADCKGGVIMHLLALRALKA-NGGVPVHVKVI 151
Cdd:PRK09104 80 GdAPHVLFYGHYDVQPvdPLDL--WESPPFEprIKETpDGRkvIVARGASDDKGQLMTFVEACRAWKAvTGSLPVRVTIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 152 AEGSEEQGTGGLERYAEEHPGLLEADTIVIGDAGNFRVGLPTVTATLRGMTLVRVRIDTLAGNLHSGQFGGAAPDALAAL 231
Cdd:PRK09104 158 FEGEEESGSPSLVPFLEANAEELKADVALVCDTGMWDRETPAITTSLRGLVGEEVTITAADRDLHSGLFGGAAANPIRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 232 IRVLDSLRAEDGSTTVDGLTGDTA---------WDGLQYDEERFrqdakvLDGVGL-IGSG----TVADRIWARPAVTVL 297
Cdd:PRK09104 238 TRILAGLHDETGRVTLPGFYDGVEelppeilaqWKALGFTAEAF------LGPVGLsIPAGekgrSVLEQIWSRPTCEIN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 298 GIdcppVVGAT--------PSvQASARalISLRVPPGVDAAEATKLLQAHLEARTPWGARVSTEQIGQGQAFRADTTSPA 369
Cdd:PRK09104 312 GI----WGGYTgegfktviPA-EASAK--VSFRLVGGQDPAKIREAFRAYVRARLPADCSVEFHDHGGSPAIALPYDSPA 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752498394 370 YQAMADAMAVAYpGQEMQYAGQGGSIPlcntLAALYPRA---EILLIGLSEPEAQIHAVNE 427
Cdd:PRK09104 385 LAAAKAALSDEW-GKPAVLIGSGGSIP----IVGDFKRIlgmDSLLVGFGLDDDRIHSPNE 440
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
19-429 |
4.58e-56 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 191.78 E-value: 4.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 19 EELTELVAFRSVADFDqfprSESEGAARWVADALAAEGFQdVALLDTpDGTQSVYGYLpGPEGAKTVLLYAHYDVQP--P 96
Cdd:cd05681 3 EDLRDLLKIPSVSAQG----RGIPETADFLKEFLRRLGAE-VEIFET-DGNPIVYAEF-NSGDAKTLLFYNHYDVQPaeP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 97 LDEagWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKA-NGGVPVHVKVIAEGSEEQGTGGLERYAEEHPGLLE 175
Cdd:cd05681 76 LEL--WTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQhLGELPVNIKFLVEGEEEVGSPNLEKFVAEHADLLK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 176 ADTIVIGDAGNFRVGLPTVTATLRGMTLVRVRIDTLAGNLHSgQFGGAAPDALAALIRVLDSLRAEDGSTTVDGLTGDTA 255
Cdd:cd05681 154 ADGCIWEGGGKNPKGRPQISLGVKGIVYVELRVKTADFDLHS-SYGAIVENPAWRLVQALNSLRDEDGRVLIPGFYDDVR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 256 W---------DGLQYDEERFRQDAKVLDGVGLIGsGTVADRIWARPAVTVLGIDCppvvGATPS-----VQASARALISL 321
Cdd:cd05681 233 PlseaeraliDTYDFDPEELRKTYGLKRPLQVEG-KDPLRALFTEPTCNINGIYS----GYTGEgsktiLPSEAFAKLDF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 322 RVPPGVDAAEATKLLQAHLEArtPWGARVSTEQIGQGQAFRADTTSPAYQAMADAMAVAYpGQEMQY----AGQGGSIPL 397
Cdd:cd05681 308 RLVPDQDPAKILSLLRKHLDK--NGFDDIEIHDLLGEKPFRTDPDAPFVQAVIESAKEVY-GQDPIVlpnsAGTGPMYPF 384
|
410 420 430
....*....|....*....|....*....|..
gi 1752498394 398 CNTLaalypRAEILLIGLSEPEAQIHAVNESV 429
Cdd:cd05681 385 YDAL-----EVPVVAIGVGNAGSNAHAPNENI 411
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
19-430 |
1.68e-52 |
|
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: 183.19 E-value: 1.68e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 19 EELTELVAFRSV-ADFDQfpRSESEGAARWVADALAAEGFQdVALLDTPDGTQS----------VYGYLPGPEGAKTVLL 87
Cdd:cd05676 14 ERLREAVAIQSVsADPEK--RPELIRMMEWAAERLEKLGFK-VELVDIGTQTLPdgeelplppvLLGRLGSDPSKKTVLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 88 YAHYDVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGG-VPVHVKVIAEGSEEQGTGGLERY 166
Cdd:cd05676 91 YGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQeLPVNLKFCFEGMEESGSEGLDEL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 167 AEEHPG--LLEADTIVIGDagNFRVG--LPTVTATLRGMTLVRVRIDTLAGNLHSGQFGGAAPDALAALIRVLDSLRAED 242
Cdd:cd05676 171 IEARKDtfFSDVDYVCISD--NYWLGkkKPCLTYGLRGICYFFIEVEGPNKDLHSGVFGGSVHEPMTDLIALMSSLVDSD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 243 GSTTVDGLTGDTA---------WDGLQYDEERFRQDAkvldGVGLIGSGTVAD---RIWARPAVTVLGI---DCPPvvGA 307
Cdd:cd05676 249 GKILIPGIYDAVAplteeewelYEKIDFDMEEYREDI----GVRRLLYDNKEEllmHRWRYPSLSIHGIegaFSGP--GA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 308 TPSVQASARALISLRVPPGVDAAEATKLLQAHLEA-----RTPwgARVSTEQIGQGQAFRADTTSPAYQAMADAMAVAYp 382
Cdd:cd05676 323 KTVIPAKVIGKFSIRLVPNMDPEVVEKQVTDYLEKvfaelKSP--NKLKVYMGHGGKPWVADPDHPNYKAARKATKRVF- 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1752498394 383 GQEMQYAGQGGSIPLCNTLAALyPRAEILLIGLSEPEAQIHAVNESVS 430
Cdd:cd05676 400 GVEPDLTREGGSIPITLTFQEA-TGKNVMLLPIGAADDGAHSQNEKIN 446
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
80-428 |
7.64e-45 |
|
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: 162.12 E-value: 7.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 80 EGAKTVLLYAHYDVQPPLDeaGWA--TPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGgVPvHVK--VIAEGS 155
Cdd:cd05682 71 QDDDTVLLYGHMDKQPPFT--GWDegLGPTKPVIRGDKLYGRGGADDGYAIFASLTAIKALQEQG-IP-HPRcvVLIEAC 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 156 EEQGTGGLERYAEE-HPGLLEADTIVIGDAGNFRVGLPTVTATLRGMTLVRVRIDTLAGNLHSGQFGGAAPDALAALIRV 234
Cdd:cd05682 147 EESGSADLPFYLDKlKERIGNVDLVVCLDSGCGNYEQLWLTTSLRGVLGGDLTVQVLNEGVHSGDASGIVPSSFRILRQL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 235 LDslRAEDGsttvdgLTGDTAWDGLQYD--EERFRQDAKV--------------LDGVGLIGSGTVA---DRIWaRPAVT 295
Cdd:cd05682 227 LS--RIEDE------NTGEVKLDEQHCDipAHRYEQAKKIaeilgeavyeefpfVSGVQPVTTDLVQlylNRTW-KPQLS 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 296 VLGIDCPPVVGATPSVQASARAL-ISLRVPPGVDAAEATKLLQAHLEARTPWGARVSTEQIGQGQAFRADTTSPAYQAMA 374
Cdd:cd05682 298 VTGADGLPPASTAGNVLRPETTLkLSLRLPPTVDAEKASAALKKLLETDPPYNAKVTFKSDGAGSGWNAPLLSPWLAKAL 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1752498394 375 DAMAVAYPGQEMQYAGQGGSIPLCNTLAALYPRAEILLIGLSEPEAQIHAVNES 428
Cdd:cd05682 378 NEASQLFFGKPAAYQGEGGSIPFMNMLGEKFPKAQFIVTGVLGPKSNAHGPNEF 431
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
19-396 |
2.64e-42 |
|
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: 154.81 E-value: 2.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 19 EELTELVAFRSV-ADFDQFPRSESEGAARWVADALAAEGFQDVALLDTPDGTQS-VYGYLPGP---EGAKTVLLYAHYDV 93
Cdd:cd05677 3 NTLSEFIAFQTVsQSPTTENAEDSRRCAIFLRQLFKKLGATNCLLLPSGPGTNPiVLATFSGNssdAKRKRILFYGHYDV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 94 QPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEGSEEQGTGGLERYAEEHPGL 173
Cdd:cd05677 83 IPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQEGELDNDVVFLIEGEEESGSPGFKEVLRKNKEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 174 LEA-DTIVIGDAGNFRVGLPTVTATLRGMTLVRVRIDTLAGNLHSGQFGGAAPDALAALIRVLDSLRAEDGSTTVDGLTg 252
Cdd:cd05677 163 IGDiDWILLSNSYWLDDNIPCLNYGLRGVIHATIVVSSDKPDLHSGVDGGVLREPTADLIKLLSKLQDPDGRILIPHFY- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 253 DTAWDGLQYDEERFRQDAKVLDgvgLIGSGTVADRI--WARPAVTV--LGIDCPpvvGATPSVQASARALISLRVPPGVD 328
Cdd:cd05677 242 DPVKPLTEAERARFTAIAETAL---IHEDTTVDSLIakWRKPSLTVhtVKVSGP---GNTTVIPKSASASVSIRLVPDQD 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752498394 329 AAEATKLLQAHLEA-----RTPwgARVSTEQIGQGQAFRADTTSPAYQAMADAMAVAYpGQEMQYAGQGGSIP 396
Cdd:cd05677 316 LDVIKQDLTDYIQScfaelKSQ--NHLDIEVLNEAEPWLGDPDNPAYQILREAVTAAW-GVEPLYIREGGSIP 385
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
19-429 |
1.22e-35 |
|
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: 137.23 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 19 EELTELVAFRSVADFDQfprsESEGAARWVADALAAEGFQDVALldtPDGTQSV-YGYLPGPEGAKTVLLYAHYDVQPpL 97
Cdd:cd05678 3 REHRELVSIPNDATDEE----EMRKNVDWLEQAFRKRGFKTSQL---PTSGLPLlLAEKPISDARKTVLFYMHLDGQP-V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 98 DEAGWA-----TPPFELTERDGRW------------------YGRGAADCKGGVIMHLLALRALKANGGVP-VHVKVIAE 153
Cdd:cd05678 75 DPSKWDqkspyTPVLKRKDAAGNWeeinwdaifsnldpewrvFARAAADDKGPIMMMLAALDALKAGGIAPkFNVKIILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 154 GSEEQGTGGLERYAEEHPGLLEADTIVIGDAGNFRVGLPTVTATLRGMTlvRVRIDTLAGNL--HSGQFGGAAPDALAAL 231
Cdd:cd05678 155 SEEEKGSPSLPKAVKEYKELLAADALIIMDGPAHATNKPTLTFGCRGIA--TATLTTYGAKVpqHSGHYGNYAPNPAFRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 232 IRVLDSLRAEDGSTTVDGLtgdtaWDGLQYDEERFRQDAKVLDGvgligsgtvADRIWARpavtvLGIDCPPVVGAT--- 308
Cdd:cd05678 233 SSLLASMKDDTGKVTIPGF-----YDGISIDEETQKILAAVPDD---------EESINKR-----LGIAQTDKVGRNyqe 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 309 ----PS------------------VQASARALISLRVPPGVDAAEATKLLQAHLE-------ARTPWGA-RVSTEQI--- 355
Cdd:cd05678 294 alqyPSlnvrgmesgwkgdkvrtiIPEIAEAEIDIRLVPESDGPYLLDLVKAHIEkqgyfvtDRAPTDEeRLAHDKIakf 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752498394 356 ---GQGQAFRADTTSPAYQAMADAMAVAYPGQEMQYAGQGGSIPLCNTLAALYPRAEIllIGLSEPEAQIHAVNESV 429
Cdd:cd05678 374 tyrNGADAFRTDINSPIGNWLRKALTDEFGEEPIQIRMMGGTVPIAPFVNVLDIPAII--VPMVNMDNNQHSPNENL 448
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
28-429 |
2.39e-35 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 136.04 E-value: 2.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 28 RSVADFDQFPRSESEGA--------ARWVADALAAEGFQdvALLDTPDGTQSVYGYLpGPEGAKTVLLYAHYDVQP--PL 97
Cdd:PRK06446 3 EELYTLIEFLKKPSISAtgegieetANYLKDTMEKLGIK--ANIERTKGHPVVYGEI-NVGAKKTLLIYNHYDVQPvdPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 98 DEagWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEGSEEQGTGGLERYAEEHPGLLEAD 177
Cdd:PRK06446 80 SE--WKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKHKLNVNVKFLYEGEEEIGSPNLEDFIEKNKNKLKAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 178 TIVIGDAGNFRVGLPTVTATLRGMTLVRVRIDTLAGNLHSgQFGGAAPDALAALIRVLDSLRAEDGSTTVDGLTGDTAW- 256
Cdd:PRK06446 158 SVIMEGAGLDPKGRPQIVLGVKGLLYVELVLRTGTKDLHS-SNAPIVRNPAWDLVKLLSTLVDGEGRVLIPGFYDDVREl 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 257 --------DGLQYDEERFRqDAKVLDGVGLIGSGTVADRIWARPAVTVLGIDCPPV-VGATPSVQASARALISLRVPPGV 327
Cdd:PRK06446 237 teeerellKKYDIDVEELR-KALGFKELKYSDREKIAEALLTEPTCNIDGFYSGYTgKGSKTIVPSRAFAKLDFRLVPNQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 328 DAAEATKLLQAHLEartPWGARVSTEQIGQGQAFRADTTSPAYQAMADAMAVAYPGQEMQYAGQGGSIPLCNTLAALYPR 407
Cdd:PRK06446 316 DPYKIFELLKKHLQ---KVGFNGEIIVHGFEYPVRTSVNSKVVKAMIESAKRVYGTEPVVIPNSAGTQPMGLFVYKLGIR 392
|
410 420
....*....|....*....|..
gi 1752498394 408 AEILLIGLSEPEAQIHAVNESV 429
Cdd:PRK06446 393 DIVSAIGVGGYYSNAHAPNENI 414
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
86-447 |
4.48e-35 |
|
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: 132.47 E-value: 4.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 86 LLYAHYDVQPPLDEAGWatpPFELTErDGRWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEGSEEQGTGGLER 165
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLKKGTVKLLFQPDEEGGMGGARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 166 YAEEhpGLLEADTI------VIGDAGNF-RVGLPTVTATLRGMTLVRVRIDTLAGnlHSGQFgGAAPDALAALIRVLDSL 238
Cdd:pfam01546 77 LIED--GLLEREKVdavfglHIGEPTLLeGGIAIGVVTGHRGSLRFRVTVKGKGG--HASTP-HLGVNAIVAAARLILAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 239 RAEDgSTTVDGLTGDTawdglqydeerfrqdakvldgvgligsgtvadriwarpaVTVLGIDCPPvvGATPSVQASARAL 318
Cdd:pfam01546 152 QDIV-SRNVDPLDPAV---------------------------------------VTVGNITGIP--GGVNVIPGEAELK 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 319 ISLRVPPGVDAAEATKLLQAHLEARTP-WGARVSTEQIGQGQAFRADtTSPAYQAMADAMAVAYPGQEMQYA-GQGGSIP 396
Cdd:pfam01546 190 GDIRLLPGEDLEELEERIREILEAIAAaYGVKVEVEYVEGGAPPLVN-DSPLVAALREAAKELFGLKVELIVsGSMGGTD 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1752498394 397 LCNTLAALYPraEILLIGLSepEAQIHAVNESVSPEELERLSVAEALFLRN 447
Cdd:pfam01546 269 AAFFLLGVPP--TVVFFGPG--SGLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
18-444 |
1.46e-25 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 108.46 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 18 KEELTELVAFRSvadfdqfprsESEGAARW----------VADALAAEGFqDVALLDTPDGTQsvygylpGP-------- 79
Cdd:PRK07079 20 FADLARRVAYRT----------ESQNPDRApalrayltdeIAPALAALGF-TCRIVDNPVAGG-------GPfliaerie 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 80 -EGAKTVLLYAHYDVQPPlDEAGWATP--PFELTERDGRWYGRGAADCKGGVIMHLLALRA-LKANGG-VPVHVKVIAEG 154
Cdd:PRK07079 82 dDALPTVLIYGHGDVVRG-YDEQWREGlsPWTLTEEGDRWYGRGTADNKGQHTINLAALEQvLAARGGrLGFNVKLLIEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 155 SEEQGTGGLERYAEEHPGLLEADTIVIGDAGNFRVGLPTVTATLRGMTLVRVRIDTLAGNLHSGQFGG--AAP-----DA 227
Cdd:PRK07079 161 GEEIGSPGLAEVCRQHREALAADVLIASDGPRLSAERPTLFLGSRGAVNFRLRVNLRDGAHHSGNWGGllRNPgtvlaHA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 228 LAALI--------------RVLDSLRAEDGSTTVDGLTGDTAWDGlQYDEErfrqdakvldgvGLigsgTVADRIWARPA 293
Cdd:PRK07079 241 IASLVdargriqvpglrppPLPAAVRAALADITVGGGPGDPAIDP-DWGEP------------GL----TPAERVFGWNT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 294 VTVLGI-----DCPpvVGATPsvqASARALISLRVPPGVDAAEATKLLQAHLEARtpwG-ARVSTEQIGQGQAFRADTTS 367
Cdd:PRK07079 304 LEVLAFktgnpDAP--VNAIP---GSARAVCQLRFVVGTDWENLAPHLRAHLDAH---GfPMVEVTVERGSPATRLDPDD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 368 PAYQAMADAMAvaypgqemQYAGQ--------GGSIPlcNTLAalyprAEILliGL-------SEPEAQIHAVNESV-SP 431
Cdd:PRK07079 376 PWVRWALASIA--------RTTGKkpallpnlGGSLP--NDVF-----ADIL--GLptlwvphSYPACSQHAPNEHLlAS 438
|
490
....*....|...
gi 1752498394 432 EELERLSVAEALF 444
Cdd:PRK07079 439 VAREGLQIMAGLF 451
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
21-437 |
8.77e-25 |
|
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: 104.69 E-value: 8.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 21 LTELVAFRSVADfdqfprsESEGAARWVADALAAEGFQdvaLLDTPD-GTQSVYGYLPGpEGAKTVLLYAHYDVQPPLDE 99
Cdd:cd08659 3 LQDLVQIPSVNP-------PEAEVAEYLAELLAKRGYG---IESTIVeGRGNLVATVGG-GDGPVLLLNGHIDTVPPGDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 100 AGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVP-VHVKVIAEGSEEQGTGGLERYAeEHPGLLEADT 178
Cdd:cd08659 72 DKWSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLgGRVALLATVDEEVGSDGARALL-EAGYADRLDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 179 IVIGDAGNFRVglptVTATlRGMTLVRVRIDTLAGnlHSGQFGGAApDALAALIRVLDSLRAEDGSTTVDGLTGDTAWDg 258
Cdd:cd08659 151 LIVGEPTGLDV----VYAH-KGSLWLRVTVHGKAA--HSSMPELGV-NAIYALADFLAELRTLFEELPAHPLLGPPTLN- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 259 lqydeerfrqdakvldgVGLIGSGTvadriwarpavtvlgidcppvvgATPSVQASARALISLRVPPGVDAAEATKLLQA 338
Cdd:cd08659 222 -----------------VGVINGGT-----------------------QVNSIPDEATLRVDIRLVPGETNEGVIARLEA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 339 HLEARtpwGARVSTEQIG-QGQAFRADTTSPAYQAMADAMAVAYPGQEMqyagqGGSIPLCNtlAALYPR---AEILLIG 414
Cdd:cd08659 262 ILEEH---EAKLTVEVSLdGDPPFFTDPDHPLVQALQAAARALGGDPVV-----RPFTGTTD--ASYFAKdlgFPVVVYG 331
|
410 420
....*....|....*....|...
gi 1752498394 415 LSEPeAQIHAVNESVSPEELERL 437
Cdd:cd08659 332 PGDL-ALAHQPDEYVSLEDLLRA 353
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
72-198 |
2.24e-23 |
|
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: 97.12 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 72 VYGYLPGPEGAKTVLLYAHYDVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVP-VHVKV 150
Cdd:cd18669 2 VIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLkGTVVV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1752498394 151 IAEGSEEQGTGGLERYA--EEHPGLLEADTIVIGDAGNFRVGLPTVTATL 198
Cdd:cd18669 82 AFTPDEEVGSGAGKGLLskDALEEDLKVDYLFVGDATPAPQKGVGIRTPL 131
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
20-444 |
6.49e-22 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 97.57 E-value: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 20 ELTELVAFRSVAdfdQFPRSESEGAA---RWVADALAAEGFqDVALLDTPDGTQSVYGYLPGPEGAK--TVLLYAHYDVQ 94
Cdd:cd05679 9 ELARRVAVPTES---QEPARKPELRAyldQEMRPRFERLGF-TVHIHDNPVAGRAPFLIAERIEDPSlpTLLIYGHGDVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 95 PPLdEAGW--ATPPFELTERDGRWYGRGAADCKGGVIMHLLALRA-LKANGG-VPVHVKVIAEGSEEQGTGGLERYAEEH 170
Cdd:cd05679 85 PGY-EGRWrdGRDPWTVTVWGERWYGRGTADNKGQHSINMAALRQvLEARGGkLGFNVKFLIEMGEEMGSPGLRAFCFSH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 171 PGLLEADTIVIGDAGNFRVGLPTVTATLRGMTLVRVRIDTLAGNLHSGQFGGAAPDALAALIRVLDSLRAEDGSTTVDGL 250
Cdd:cd05679 164 REALKADLFIASDGPRLAADRPTMFLGSRGGLNFELRVNLREGGHHSGNWGGLLANPGIILANAIASLVDGKGRIKLPAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 251 TGDtawdGLQYDEERFRQDAKVLDGVG--LIGSG------TVADRIWARPAVTVLG-----IDCPpvVGATPsvqASARA 317
Cdd:cd05679 244 KPA----HLPNSVRSALADVEVGGGPDdpSIDPWwgepglTAAERVFGWNTLEVLAfktgnPDAP--VNAIP---GHAEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 318 LISLRVPPGVDAAEATKLLQAHLEARTPWGARVSTEQIgQGQAFRADTTSPAYQAMADAMAVAYPGQEMQYAGQGGSIPl 397
Cdd:cd05679 315 ICQIRFVVGTDPDTFIPAVRAHLDANGFDGVEVTASQM-VFAATRLDPDSPWVGWALASLQKTTGKKPALLPNLGGSLP- 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1752498394 398 cNTLAALYPRAEILLIGLSEPEAQIHAVNESV-SPEELERLSVAEALF 444
Cdd:cd05679 393 -NDVFSEVLGLPTLWVPHSYPACSQHAPNEHIlAPVMREALRVMAGLF 439
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
21-238 |
8.28e-22 |
|
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: 96.31 E-value: 8.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 21 LTELVAFRSVAdfdqFPRSESEGAARWVADALAAEGFqDVALLDTPDGTQSVYG----YLPGPEGAKTVLLYAHYDVQPP 96
Cdd:TIGR01910 4 LKDLISIPSVN----PPGGNEETIANYIKDLLREFGF-STDVIEITDDRLKVLGkvvvKEPGNGNEKSLIFNGHYDVVPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 97 LDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEGSEEQGTGGLERYAEEHPGLLEA 176
Cdd:TIGR01910 79 GDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLLQRGYFKDA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752498394 177 DTIVIGDAGNFrvglPTVTATLRGMTLVRVRIDTLAGNLHSGQFGGAAPDALAALIRVLDSL 238
Cdd:TIGR01910 159 DGVLIPEPSGG----DNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNEL 216
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
21-446 |
1.25e-21 |
|
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: 95.74 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 21 LTELVAFRSVAdfdqfprSESEGA-ARWVADALAAEGFQDVALLDTPDGTQSVYGYLpGPEGAKTVLLYAHYDVQPpLDE 99
Cdd:cd03894 3 LARLVAFDTVS-------RNSNLAlIEYVADYLAALGVKSRRVPVPEGGKANLLATL-GPGGEGGLLLSGHTDVVP-VDG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 100 AGWATPPFELTERDGRWYGRGAADCKGG--VIMHLLAlRALKANGGVPVHVKVIAEgsEEQGTGGLERYAEEHPGLLEAD 177
Cdd:cd03894 74 QKWSSDPFTLTERDGRLYGRGTCDMKGFlaAVLAAVP-RLLAAKLRKPLHLAFSYD--EEVGCLGVRHLIAALAARGGRP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 178 TIVIgdagnfrVGLPT----VTATlRGMTLVRVRIDTLAGnlHSGQ--FGGAAPDALAALIRVLDSLRAEDGSTTVDGlt 251
Cdd:cd03894 151 DAAI-------VGEPTslqpVVAH-KGIASYRIRVRGRAA--HSSLppLGVNAIEAAARLIGKLRELADRLAPGLRDP-- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 252 gdtawdglqydeeRFRQDAKVLDgVGLIGSGTVADRIwarPAVTVLGIDCppvvgatpsvqasaralislRVPPGVDAAE 331
Cdd:cd03894 219 -------------PFDPPYPTLN-VGLIHGGNAVNIV---PAECEFEFEF--------------------RPLPGEDPEA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 332 ATKLLQAHLEART-PWGARVSTEQIGQGQAFRADTTSPAYQAMADA------MAVAYPGQEMQYAGQG--------GSIp 396
Cdd:cd03894 262 IDARLRDYAEALLeFPEAGIEVEPLFEVPGLETDEDAPLVRLAAALagdnkvRTVAYGTEAGLFQRAGiptvvcgpGSI- 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1752498394 397 lcntlaalypraeilliglsepeAQIHAVNESVSPEELERlsvAEALFLR 446
Cdd:cd03894 341 -----------------------AQAHTPDEFVELEQLDR---CEEFLRR 364
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
21-249 |
1.27e-21 |
|
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: 95.53 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 21 LTELVAFRSvadfDQFPRSESEGAARWVADALAAEGFQdVALLDTPDGTQSVYGYLPGPEGAKTVLLYAHYDVQPPLDEA 100
Cdd:cd08011 4 LQELVQIPS----PNPPGDNTSAIAAYIKLLLEDLGYP-VELHEPPEEIYGVVSNIVGGRKGKRLLFNGHYDVVPAGDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 101 GWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGvPVHVKVI--AEGSEEqgTGGLE--RYAEEHPGLLEA 176
Cdd:cd08011 79 GWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKA-PWDLPVVltFVPDEE--TGGRAgtKYLLEKVRIKPN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1752498394 177 DTIVIGDAG--NFRVGlptvtatLRGmtLVRVRIDTLAGNLHSG--QFGGAAPDALAALIRVLDSLRAEDGSTTVDG 249
Cdd:cd08011 156 DVLIGEPSGsdNIRIG-------EKG--LVWVIIEITGKPAHGSlpHRGESAVKAAMKLIERLYELEKTVNPGVIKG 223
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
19-171 |
4.19e-21 |
|
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: 95.39 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 19 EELTELVAFRSVADFDQFPRSESEG---AARWVADALAAEGFQdVALLDTpdgtqsVYGYLPGPEGAKTVLLYAHYDVQP 95
Cdd:cd03888 12 EDLKELVAIPSVRDEATEGAPFGEGprkALDKFLDLAKRLGFK-TKNIDN------YAGYAEYGEGEEVLGILGHLDVVP 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752498394 96 PLDeaGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKaNGGVPVHVKV--IAEGSEEQGTGGLERYAEEHP 171
Cdd:cd03888 85 AGE--GWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILK-DLGLPLKKKIrlIFGTDEETGWKCIEHYFEHEE 159
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
12-186 |
7.65e-21 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 93.76 E-value: 7.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 12 SLMPRAKEELTELVAFRSVAdfdqfPRSESEG---AARWVADALAAEGFQDVALLDTPD-----GTQS-VYGYLPGPEGA 82
Cdd:PRK13983 2 ELRDEMIELLSELIAIPAVN-----PDFGGEGekeKAEYLESLLKEYGFDEVERYDAPDprvieGVRPnIVAKIPGGDGK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 83 KTVLLYAHYDVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVP-VHVKVIAEGSEEQG-T 160
Cdd:PRK13983 77 RTLWIISHMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPkYNLGLAFVSDEETGsK 156
|
170 180
....*....|....*....|....*..
gi 1752498394 161 GGLERYAEEHPGLL-EADTIVIGDAGN 186
Cdd:PRK13983 157 YGIQYLLKKHPELFkKDDLILVPDAGN 183
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
72-223 |
1.16e-20 |
|
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: 89.41 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 72 VYGYLPGPEGAKTVLLYAHYDVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVP-VHVKV 150
Cdd:cd03873 2 LIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPkGTIVV 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1752498394 151 IAEGSEEQGTGGLERYA--EEHPGLLEADTIVIGDAGNFRVGLPTVTATLRGMTLVRVRIDTLAGNL-HSGQFGGA 223
Cdd:cd03873 82 AFTADEEVGSGGGKGLLskFLLAEDLKVDAAFVIDATAGPILQKGVVIRNPLVDALRKAAREVGGKPqRASVIGGG 157
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
21-435 |
2.12e-18 |
|
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: 87.03 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 21 LTELVAFRSVADFDQFPrSESEgAARWVADALAAEGFQ-DVALLDTPDGTQSVYGYLPGPE-GAKTVLLYAHYDVQPPlD 98
Cdd:cd05675 4 LQELIRIDTTNSGDGTG-SETR-AAEVLAARLAEAGIQtEIFVVESHPGRANLVARIGGTDpSAGPLLLLGHIDVVPA-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 99 EAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEGSEEQGTG--GLERYAEEHPGLLEA 176
Cdd:cd05675 81 ASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGenGAKWLVDNHPELFDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 177 DTIVIGDAGNF-------RVGLPTVTATlRGMTLVRVRIDTLAGnlHSGQFGgaAPDALAALIRVLDSLRAEDGSTTVDg 249
Cdd:cd05675 161 ATFALNEGGGGslpvgkgRRLYPIQVAE-KGIAWMKLTVRGRAG--HGSRPT--DDNAITRLAEALRRLGAHNFPVRLT- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 250 ltgdtawdglqyDEERFRQDAKVLDGvgliGSGTVADriwaRPAVTVLGIDCPPVVGATPSVQASARALISlrvPPGVDA 329
Cdd:cd05675 235 ------------DETAYFAQMAELAG----GEGGALM----LTAVPVLDPALAKLGPSAPLLNAMLRNTAS---PTMLDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 330 AEATKLL----QAHLEARTPWGA----------------RVSTEQIGQGQAFRADTTSPAYQAMADAMAVAYPGqemqya 389
Cdd:cd05675 292 GYATNVLpgraTAEVDCRILPGQseeevldtldkllgdpDVSVEAVHLEPATESPLDSPLVDAMEAAVQAVDPG------ 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752498394 390 gqGGSIPLCN---TLAALYPRAEILLIGLS----EPE----AQIHAVNESVSPEELE 435
Cdd:cd05675 366 --APVVPYMSpggTDAKYFRRLGIPGYGFAplflPPEldytGLFHGVDERVPVESLY 420
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
37-186 |
4.24e-18 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 85.59 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 37 PRSESEGA---ARWVADALAAEGFQDVALLDTPDG----TQSVYGYLPGPEGaKTVLLYAHYDVQPPLDEAGWATPPFEL 109
Cdd:cd05650 18 PESGGEGEkekADYLEKKLREYGFYTLERYDAPDErgiiRPNIVAKIPGGND-KTLWIISHLDTVPPGDLSLWETDPWEP 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752498394 110 TERDGRWYGRGAADCKGGVIMHLLALRALKANGGVPVH-VKVIAEGSEEQGTG-GLERYAEEHPGLLEADTIVIGDAGN 186
Cdd:cd05650 97 VVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYnFGLLFVADEEDGSEyGIQYLLNKFDLFKKDDLIIVPDFGT 175
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
6-163 |
2.36e-17 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 83.90 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 6 VAETVASLMPRAKEELTELVAFRSVadfdqfpRSESEGAARWVADALAAEGFQ-------DVALLDTP---------DGT 69
Cdd:PRK06837 11 ILAAVDAGFDAQVAFTQDLVRFPST-------RGAEAPCQDFLARAFRERGYEvdrwsidPDDLKSHPgagpveidySGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 70 QSVYG-YLPGPEGAKTVLLYAHYDVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVP--- 145
Cdd:PRK06837 84 PNVVGtYRPAGKTGRSLILQGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPaar 163
|
170
....*....|....*...
gi 1752498394 146 VHVKVIAEgSEEQGTGGL 163
Cdd:PRK06837 164 VHFQSVIE-EESTGNGAL 180
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
12-443 |
2.79e-17 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 83.12 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 12 SLMPRAKEELTELVAFRSVADfdqfPRSESEGAARWVADALAAEGFqDVALLDTPDGTQS-VYGYLP-----GPEGAKTV 85
Cdd:PRK08651 3 AMMFDIVEFLKDLIKIPTVNP----PGENYEEIAEFLRDTLEELGF-STEIIEVPNEYVKkHDGPRPnliarRGSGNPHL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 86 LLYAHYDVQPPLDeaGWA-TPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIaeGSEEQGTGGLE 164
Cdd:PRK08651 78 HFNGHYDVVPPGE--GWSvNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAGDGNIELAIV--PDEETGGTGTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 165 RYAEEhpGLLEADTIVIGDAGnfrvGLPTVTATLRGMTLVRVRIdtlagnlHSGQFGGAAP----DALAALIRVLDSLRA 240
Cdd:PRK08651 154 YLVEE--GKVTPDYVIVGEPS----GLDNICIGHRGLVWGVVKV-------YGKQAHASTPwlgiNAFEAAAKIAERLKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 241 EDGSTTVDgltgdtawdgLQYDEERfrqdakvldgvgligsGTVADRIWARPAVTvlgidCPpvvGATPSVQASARALIS 320
Cdd:PRK08651 221 SLSTIKSK----------YEYDDER----------------GAKPTVTLGGPTVE-----GG---TKTNIVPGYCAFSID 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 321 LRVPPGVDAAEATKLLQAHLEARTP-WGARVSTEQIGQGQAFRADTTSPAYQAMADAmavaypgqemqYAGQGGSIplcn 399
Cdd:PRK08651 267 RRLIPEETAEEVRDELEALLDEVAPeLGIEVEFEITPFSEAFVTDPDSELVKALREA-----------IREVLGVE---- 331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 400 tlaalyPRAEILLIGLS--------EP--------EAQIHAVNESVSPEELERlsVAEAL 443
Cdd:PRK08651 332 ------PKKTISLGGTDarffgakgIPtvvygpgeLELAHAPDEYVEVKDVEK--AAKVY 383
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
21-444 |
4.95e-17 |
|
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: 82.74 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 21 LTELVAFRSVadfdqfpRSESEGAARWVADALAAEGFQ------DVALL----------DTPDGTQSVYG-YLPGPEGAK 83
Cdd:cd03895 3 LQDLVRFPSL-------RGEEAAAQDLVAAALRSRGYTvdrweiDVEKLkhhpgfspvaVDYAGAPNVVGtHRPRGETGR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 84 TVLLYAHYDVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANG---GVPVHVK-VIAEGSEEQG 159
Cdd:cd03895 76 SLILNGHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGlqpAADVHFQsVVEEECTGNG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 160 T-GGLER-YAeehpglleADTIVIGDAGNFRVglptVTATLrGMTLVRVRIDTLAGNLHSGQFGGAAPDALAALIRVLDS 237
Cdd:cd03895 156 AlAALMRgYR--------ADAALIPEPTELKL----VRAQV-GVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 238 LRAEdgsttvdgltgdtaWDGLQYDEERFRQDAKVLD-GVGLIGSGTvadriWARPAVTVLGIDCppvvgatpsvqasaR 316
Cdd:cd03895 223 LERE--------------WNARKKSHPHFSDHPHPINfNIGKIEGGD-----WPSSVPAWCVLDC--------------R 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 317 ALISlrvpPGVDAAEATKLLQAHL---EARTPWGAR--VSTEQIG-QGQAFRADTTSPAYQAMADAMAVAYPGQEMQYAg 390
Cdd:cd03895 270 IGIY----PGESPEEARREIEECVadaAATDPWLSNhpPEVEWNGfQAEGYVLEPGSDAEQVLAAAHQAVFGTPPVQSA- 344
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752498394 391 qggSIPLCNT-LAALYPRAEILLIGlsePEAQ-IHAVNESVSPEELERLSVAEALF 444
Cdd:cd03895 345 ---MTATTDGrFFVLYGDIPALCYG---PGSRdAHGFDESVDLESLRKITKTIALF 394
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
16-186 |
5.59e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 82.74 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 16 RAKEELTELVAFRSVADFDQFPRsesegAARWVADALAAEGFQ--DVALLDTPDGTQSVYGYLPGPEGAKTVLLYAHYDV 93
Cdd:PRK09133 38 AARDLYKELIEINTTASTGSTTP-----AAEAMAARLKAAGFAdaDIEVTGPYPRKGNLVARLRGTDPKKPILLLAHMDV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 94 QPPLDEaGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEGSEEQGTG--GLERYAEEHP 171
Cdd:PRK09133 113 VEAKRE-DWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDIILALTGDEEGTPmnGVAWLAENHR 191
|
170
....*....|....*
gi 1752498394 172 GLLEADtIVIGDAGN 186
Cdd:PRK09133 192 DLIDAE-FALNEGGG 205
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
19-241 |
6.84e-17 |
|
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: 82.43 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 19 EELTELVAFRSVADFDqfprSESEGA--ARWVADALaaEGFQDVALLD-----TPDGtqsVYGYLPGPEGAKTVLLYAHY 91
Cdd:TIGR01887 6 EDLKELIAIDSVEDLE----KAKEGApfGEGPRKAL--DKFLEIAKRDgftteNVDN---YAGYIEYGQGEEVLGILGHL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 92 DVQPPLDeaGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKaNGGVPVHVKV--IAEGSEEQGTGGLERY--A 167
Cdd:TIGR01887 77 DVVPAGD--GWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILK-ELGLKLKKKIrfIFGTDEESGWKCIDYYfeH 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752498394 168 EEHPGL-LEADT---IVIGDAGNFRVGLptvtaTLRGMTLVRVRIDTLAGnlhsGQFGGAAPDALAALIRVLDSLRAE 241
Cdd:TIGR01887 154 EEMPDIgFTPDAefpIIYGEKGITTLEI-----KFKDDTEGDVVLESFKA----GEAYNMVPDHATAVISGKKLTEVE 222
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
18-160 |
1.11e-16 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 81.62 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 18 KEEL----TELVAFRSVADfdqfPRSESEGAARWVADALAAEGFqDVALLDTPDGTQSVYGYLPG--PEGAKTVLLYAHY 91
Cdd:PRK08596 12 KDELlellKTLVRFETPAP----PARNTNEAQEFIAEFLRKLGF-SVDKWDVYPNDPNVVGVKKGteSDAYKSLIINGHM 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752498394 92 DVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANG----GVPVHVKVIAEGSEEQGT 160
Cdd:PRK08596 87 DVAEVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGielpGDLIFQSVIGEEVGEAGT 159
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
14-126 |
1.81e-15 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 77.54 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 14 MPRAKEELTELVAFRSVADfdqfprsESEGA-ARWVADALAAEGFQdVALLDTPDGTQS-VYGYLpGPEGAKTVLLYAHY 91
Cdd:PRK07522 3 SMSSLDILERLVAFDTVSR-------DSNLAlIEWVRDYLAAHGVE-SELIPDPEGDKAnLFATI-GPADRGGIVLSGHT 73
|
90 100 110
....*....|....*....|....*....|....*
gi 1752498394 92 DVQPpLDEAGWATPPFELTERDGRWYGRGAADCKG 126
Cdd:PRK07522 74 DVVP-VDGQAWTSDPFRLTERDGRLYGRGTCDMKG 107
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
80-182 |
2.21e-15 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 77.23 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 80 EGAKTVLLYAHYDVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVPV-HVKVIAEGSEEQ 158
Cdd:PRK08588 57 SGSPVLALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNgTIRLLATAGEEV 136
|
90 100
....*....|....*....|....*
gi 1752498394 159 GTGGLERYAEEhpGLLE-ADTIVIG 182
Cdd:PRK08588 137 GELGAKQLTEK--GYADdLDALIIG 159
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
20-160 |
9.49e-14 |
|
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: 72.15 E-value: 9.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 20 ELT-ELVAFRSVAdfdqfPrsESEGAARWVADALAAEGFqDVALLDTpDGTQSVYGYLpGPEGakTVLLYA-HYDVQPPL 97
Cdd:cd03891 2 ELAkELIRRPSVT-----P--DDAGAQDLIAERLKALGF-TCERLEF-GGVKNLWARR-GTGG--PHLCFAgHTDVVPPG 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752498394 98 DEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLA-LRALKANGGVPVHVKVI----AEGSEEQGT 160
Cdd:cd03891 70 DLEGWSSDPFSPTIKDGMLYGRGAADMKGGIAAFVAAaERFVAKHPNHKGSISFLitsdEEGPAIDGT 137
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
17-157 |
1.86e-13 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 71.29 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 17 AKEELTELVAFRSVAdfdqfprSESEGAARWVADALAAEGFQ-------DVALLDTPDGTqsvygylpgpeGAKTVLLYA 89
Cdd:TIGR01246 1 VTELAKELISRPSVT-------PNDAGCQDIIAERLEKLGFEiewmhfgDTKNLWATRGT-----------GEPVLAFAG 62
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752498394 90 HYDVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGV-IMHLLALRALKANGGVPVHVKVIAEGSEE 157
Cdd:TIGR01246 63 HTDVVPAGPEEQWSSPPFEPVERDGKLYGRGAADMKGSLaAFIVAAERFVKKNPDHKGSISLLITSDEE 131
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
83-217 |
4.50e-13 |
|
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: 70.75 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 83 KTVLLYAHYDVQP--PLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEGSEEQGT 160
Cdd:cd05674 70 KPLLLMAHQDVVPvnPETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTIILAFGHDEEVG 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752498394 161 GG----------LERYAEEHPGLL--EADTIVIGDAGNFRVGLPTVTAtlRGMTLVRVRIDTLAGnlHS 217
Cdd:cd05674 150 GErgagaiaellLERYGVDGLAAIldEGGAVLEGVFLGVPFALPGVAE--KGYMDVEITVHTPGG--HS 214
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
20-128 |
4.88e-13 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 70.11 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 20 ELT-ELVAFRSVAdfdqfPrsESEGAARWVADALAAEGFQdvalLDTPD--GTQSVYGYLpGPEGakTVLLYA-HYDVQP 95
Cdd:PRK13009 6 ELAqDLIRRPSVT-----P--DDAGCQDLLAERLEALGFT----CERMDfgDVKNLWARR-GTEG--PHLCFAgHTDVVP 71
|
90 100 110
....*....|....*....|....*....|...
gi 1752498394 96 PLDEAGWATPPFELTERDGRWYGRGAADCKGGV 128
Cdd:PRK13009 72 PGDLEAWTSPPFEPTIRDGMLYGRGAADMKGSL 104
|
|
| PRK06915 |
PRK06915 |
peptidase; |
68-162 |
5.80e-13 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 70.11 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 68 GTQSVYGYLPGPEGAKTVLLYAHYDVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANgGVPVH 147
Cdd:PRK06915 79 DSPNIVATLKGSGGGKSMILNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIES-GIELK 157
|
90
....*....|....*
gi 1752498394 148 VKVIAEGSEEQGTGG 162
Cdd:PRK06915 158 GDVIFQSVIEEESGG 172
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
44-192 |
7.88e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 69.88 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 44 AARWVADALAAEGFqDVALLDTPDGTQSVYGYLPGPE-GAKTVLLYAHYDVQPPlDEAGWATPPFELTERDGRWYGRGAA 122
Cdd:PRK07906 27 AAEYVAEKLAEVGL-EPTYLESAPGRANVVARLPGADpSRPALLVHGHLDVVPA-EAADWSVHPFSGEIRDGYVWGRGAV 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752498394 123 DCKGGVIMHLLALRALKANGGVPVHVKVIAEGSEEQ--GTGGLERYAEEHPGLLEADTIVIGDAGNFRVGLP 192
Cdd:PRK07906 105 DMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEagGTYGAHWLVDNHPELFEGVTEAISEVGGFSLTVP 176
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
19-159 |
8.99e-13 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 69.80 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 19 EELTELVAFRSVADFDQFPRSESEgAARWVADALAAEGFqDVALLDTpDGTQSVYGYLPgpEGAKTVLLYAHYDVQPPLD 98
Cdd:PRK08554 5 ELLSSLVSFETVNDPSKGIKPSKE-CPKFIKDTLESWGI-ESELIEK-DGYYAVYGEIG--EGKPKLLFMAHFDVVPVNP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752498394 99 EAgWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANggvPVHVKVI--AEGSEEQG 159
Cdd:PRK08554 80 EE-WNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKE---PLNGKVIfaFTGDEEIG 138
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
66-168 |
1.36e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 69.34 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 66 PDGtqsVYGYLPGPEGAKTVLLYAHYDVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGgvp 145
Cdd:PRK07205 62 PKG---YYGYAEIGQGEELLAILCHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAG--- 135
|
90 100
....*....|....*....|....*..
gi 1752498394 146 VH----VKVIAEGSEEQGTGGLERYAE 168
Cdd:PRK07205 136 VQfnkrIRFIFGTDEETLWRCMNRYNE 162
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
19-171 |
2.62e-12 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 68.33 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 19 EELTELVAFRSVADfDQFPRSES---EGaarwVADALAA-------EGFQDVALldtpDGtqsVYGYLPGPEGAKTVLLY 88
Cdd:PRK07318 18 EDLQELLRINSVRD-DSKAKEGApfgPG----PVKALEKfleiaerDGFKTKNV----DN---YAGHIEYGEGEEVLGIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 89 AHYDVQPPLDeaGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANgGVPVHVKV--IAEGSEEQGTGGLERY 166
Cdd:PRK07318 86 GHLDVVPAGD--GWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIKEL-GLPLSKKVrfIVGTDEESGWKCMDYY 162
|
....*
gi 1752498394 167 AEEHP 171
Cdd:PRK07318 163 FEHEE 167
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
39-227 |
8.22e-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 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: 63.21 E-value: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 39 SESeGAARWVADALAAE----GFQDVALldtpDGTQSVYGYLPGpeGAKTVLLYAHYDVQPPLDEAGWATPPFELTERDG 114
Cdd:cd05649 12 SES-GEEKGVVERIEEEmeklGFDEVEI----DPMGNVIGYIGG--GKKKILFDGHIDTVGIGNIDNWKFDPYEGYETDG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 115 RWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEGS--EEQGTGGLERYAEEHPGlLEADTIVIGDA--GNFRVG 190
Cdd:cd05649 85 KIYGRGTSDQKGGLASMVYAAKIMKDLGLRDFAYTILVAGTvqEEDCDGVCWQYISKADK-IKPDFVVSGEPtdGNIYRG 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1752498394 191 lptvtatLRGMtlVRVRIDTLAGNLHsgqfgGAAPDA 227
Cdd:cd05649 164 -------QRGR--MEIRVDTKGVSCH-----GSAPER 186
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
80-173 |
1.32e-10 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 62.33 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 80 EGAKTVLLYAHYDVQPPldEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEGSEE-Q 158
Cdd:cd05651 53 EGKPTLLLNSHHDTVKP--NAGWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGPLNYNLIYAASAEEEiS 130
|
90
....*....|....*
gi 1752498394 159 GTGGLERYAEEHPGL 173
Cdd:cd05651 131 GKNGIESLLPHLPPL 145
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
13-139 |
1.86e-10 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 62.26 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 13 LMPRAKEELTELVAFRSvaDFDQFPrSESeGAARWVADALAAE----GFQDValldTPDGTQSVYGYLPGpeGAKTVLLY 88
Cdd:PRK13004 6 ILMLAEKYKADMTRFLR--DLIRIP-SES-GDEKRVVKRIKEEmekvGFDKV----EIDPMGNVLGYIGH--GKKLIAFD 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1752498394 89 AHYDVQPPLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALK 139
Cdd:PRK13004 76 AHIDTVGIGDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIK 126
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
15-182 |
6.68e-10 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 60.61 E-value: 6.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 15 PRAKEELTELVAFRSV----ADFDQFPRSESEGAARWVADAlaaeGFQ-DV-ALLDTPDGTQSVYGYLPGPEGaktVLLY 88
Cdd:PRK05111 5 PSFIEMYRALIATPSIsatdPALDQSNRAVIDLLAGWFEDL----GFNvEIqPVPGTRGKFNLLASLGSGEGG---LLLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 89 AHYD-VqpPLDEAGWATPPFELTERDGRWYGRGAADCKGgviMHLLALRALKangGVPVH-----VKVIAEGSEEQGTGG 162
Cdd:PRK05111 78 GHTDtV--PFDEGRWTRDPFTLTEHDGKLYGLGTADMKG---FFAFILEALR---DIDLTklkkpLYILATADEETSMAG 149
|
170 180
....*....|....*....|
gi 1752498394 163 LERYAEEHPglLEADTIVIG 182
Cdd:PRK05111 150 ARAFAEATA--IRPDCAIIG 167
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
48-170 |
3.19e-09 |
|
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: 58.37 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 48 VADALAAEGFQdVALLDTPDGTQSVYGYLPGPEGAKtVLLYAHYDVQPPLDEAgwATPPFelTERDGRWYGRGAADCKGG 127
Cdd:cd03885 28 LAEELEALGFT-VERRPLGEFGDHLIATFKGTGGKR-VLLIGHMDTVFPEGTL--AFRPF--TVDGDRAYGPGVADMKGG 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1752498394 128 VIMHLLALRALKANGGVPVH-VKVIAEGSEEQGTGG----LERYAEEH 170
Cdd:cd03885 102 LVVILHALKALKAAGGRDYLpITVLLNSDEEIGSPGsrelIEEEAKGA 149
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
3-163 |
4.59e-09 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 58.42 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 3 SNPVAETVASLMPRAKEELTELVAFRSVADFDqfPRSESEGAARWVADALAAEgFQDV--ALLDTPDGTQSVYGYLPGP- 79
Cdd:PRK08262 32 DVPAVAPVAVDEDAAAERLSEAIRFRTISNRD--RAEDDAAAFDALHAHLEES-YPAVhaALEREVVGGHSLLYTWKGSd 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 80 EGAKTVLLYAHYDVQP--PLDEAGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEGSEE 157
Cdd:PRK08262 109 PSLKPIVLMAHQDVVPvaPGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDE 188
|
....*.
gi 1752498394 158 QgTGGL 163
Cdd:PRK08262 189 E-VGGL 193
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
84-168 |
2.04e-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: 55.95 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 84 TVLLYAHYDVQPPLDEAgWATPPFE-LTERDGRWYGRGAADCKGGVIMHLLALRALKANGGVP---VHVKVIAEgSEEQG 159
Cdd:TIGR01880 73 SILLNSHTDVVPVFREH-WTHPPFSaFKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFkrtIHISFVPD-EEIGG 150
|
....*....
gi 1752498394 160 TGGLERYAE 168
Cdd:TIGR01880 151 HDGMEKFAK 159
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
80-176 |
7.54e-08 |
|
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.
Pssm-ID: 349869 [Multi-domain] Cd Length: 394 Bit Score: 54.10 E-value: 7.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 80 EGAKTVLLYAHYDVQPPLDeaGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKA-----NGGVPVHVKVIAEG 154
Cdd:cd02697 71 DGGRTVALNAHGDVVPPGD--GWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESlgaplRGAVELHFTYDEEF 148
|
90 100
....*....|....*....|..
gi 1752498394 155 SEEQGTGGLERYAEEHPGLLEA 176
Cdd:cd02697 149 GGELGPGWLLRQGLTKPDLLIA 170
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
17-196 |
1.22e-07 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 53.82 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 17 AKEELTELVAFRSVADFDQFPRSESEGAArwVADALA--AEGFQdvalLDTPDGTQSVYGYLPGPEGAKTVLLYAHYDVQ 94
Cdd:PRK06156 48 AIESLRELVAFPTVRVEGVPQHENPEFIG--FKKLLKslARDFG----LDYRNVDNRVLEIGLGGSGSDKVGILTHADVV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 95 PpLDEAGWATP-----PFELTERDGRWYGRGAADCKGGVIMHLLALRALKANgGVPV--HVKVIAEGSEEQGTGGLERYA 167
Cdd:PRK06156 122 P-ANPELWVLDgtrldPFKVTLVGDRLYGRGTEDDKGAIVTALYAMKAIKDS-GLPLarRIELLVYTTEETDGDPLKYYL 199
|
170 180
....*....|....*....|....*....
gi 1752498394 168 EEHPglLEADTIVIgDAgnfrvGLPTVTA 196
Cdd:PRK06156 200 ERYT--PPDYNITL-DA-----EYPVVTA 220
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
83-142 |
1.32e-07 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 53.43 E-value: 1.32e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1752498394 83 KTVLLYAHYDVQPPLDEAgWATPPFE-LTERDGRWYGRGAADCKGGVIMHLLALRALKANG 142
Cdd:cd05646 65 PSILLNSHTDVVPVFEEK-WTHDPFSaHKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASG 124
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
37-238 |
2.19e-06 |
|
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: 49.40 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 37 PRSESEGAARWVADALAAEGFQDVALldtpDGTQSVYGYLPGPEGAKTVLLYAHYDVQPPLDEagwatpPFELTERDGRW 116
Cdd:cd03896 13 PTFREGARADLVAEWMADLGLGDVER----DGRGNVVGRLRGTGGGPALLFSAHLDTVFPGDT------PATVRHEGGRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 117 YGRGAADCKGGVIMHLLALRALKaNGGVPVHVKVIAE---GSEEQGTGGLERYAEEHPGLLeADTIVIGDAGNFRvglpt 193
Cdd:cd03896 83 YGPGIGDNKGSLACLLAMARAMK-EAGAALKGDVVFAanvGEEGLGDLRGARYLLSAHGAR-LDYFVVAEGTDGV----- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1752498394 194 vtATLRGMTLVRVRIDTLAGNLHS-GQFGgaAPDALAALIRVLDSL 238
Cdd:cd03896 156 --PHTGAVGSKRFRITTVGPGGHSyGAFG--SPSAIVAMAKLVEAL 197
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
17-325 |
2.99e-06 |
|
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: 48.89 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 17 AKEELTELVAFRSVadfdqfPRSESEGAARWVadalaaEGFQDVALLDTPDGTQSVYGylPGPEGAKTVLLYAHYDvqpp 96
Cdd:cd05653 3 AVELLLDLLSIYSP------SGEEARAAKFLE------EIMKELGLEAWVDEAGNAVG--GAGSGPPDVLLLGHID---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 97 ldeagwaTPPFELTER--DGRWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEgsEEQGTGGLERYAEEHPgll 174
Cdd:cd05653 65 -------TVPGEIPVRveGGVLYGRGAVDAKGPLAAMILAASALNEELGARVVVAGLVD--EEGSSKGARELVRRGP--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 175 EADTIVIGDAGnfrvGLPTVTATLRGMTLVRVRIDtlAGNLHS-GQFGGAAPDALAALIRVLDSLRA------EDGSTTV 247
Cdd:cd05653 133 RPDYIIIGEPS----GWDGITLGYRGSLLVKIRCE--GRSGHSsSPERNAAEDLIKKWLEVKKWAEGynvggrDFDSVVP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 248 DGLTGDTAWDGLqYDEERFRQDAKVLDGVGLIGSGTVADRIWARPAVTVLGiDCPPVVGA--TPSVQASARALISLRVPP 325
Cdd:cd05653 207 TLIKGGESSNGL-PQRAEATIDLRLPPRLSPEEAIALATALLPTCELEFID-DTEPVKVSknNPLARAFRRAIRKQGGKP 284
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
44-145 |
4.08e-06 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 48.42 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 44 AARWVADALAAEGF----QDValldTPDGTQSVYGYLPGPEGAKtVLLYAHYDVQPPLdeagwatPPFELTERDGRWYGR 119
Cdd:cd05652 21 VGDFLAEYLESLGFtvekQPV----ENKDRFNVYAYPGSSRQPR-VLLTSHIDTVPPF-------IPYSISDGGDTIYGR 88
|
90 100
....*....|....*....|....*.
gi 1752498394 120 GAADCKGGVIMHLLALRALKANGGVP 145
Cdd:cd05652 89 GSVDAKGSVAAQIIAVEELLAEGEVP 114
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
82-251 |
5.07e-06 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 48.21 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 82 AKTVLLYAHYDVQPPLDEagwaTPPfeLTERDGRWYGRGAADCKGGVIMHLLALRALKANgGVPVHVKVIAEGSEEQGT- 160
Cdd:cd05647 53 ASRVILAGHLDTVPVAGN----LPS--RVEEDGVLYGCGATDMKAGDAVQLKLAATLAAA-TLKHDLTLIFYDCEEVAAe 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 161 -GGLERYAEEHPGLLEADTIVIGDAGNfrvglPTVTATLRGMTLVRVRIDTLAGnlHSGQ--FGGAAPDALAALIRVLDS 237
Cdd:cd05647 126 lNGLGRLAEEHPEWLAADFAVLGEPTD-----GTIEGGCQGTLRFKVTTHGVRA--HSARswLGENAIHKLAPILARLAA 198
|
170
....*....|....
gi 1752498394 238 LRAEdgSTTVDGLT 251
Cdd:cd05647 199 YEPR--TVNIDGLT 210
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
45-142 |
5.72e-06 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly fungal and bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349935 [Multi-domain] Cd Length: 379 Bit Score: 48.24 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 45 ARWVADALAAEGFQDVALLDTPdGTQSVYGYLPGPEGAKTVLLYAHYDVqppLDEAGWATPPFELTERDGRWYGRGAADC 124
Cdd:cd08013 32 ATYVAAWLAHRGIEAHRIEGTP-GRPSVVGVVRGTGGGKSLMLNGHIDT---VTLDGYDGDPLSGEIADGRVYGRGTLDM 107
|
90
....*....|....*...
gi 1752498394 125 KGGVIMHLLALRALKANG 142
Cdd:cd08013 108 KGGLAACMAALADAKEAG 125
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
14-171 |
7.43e-06 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 47.83 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 14 MPRAKEELTELVAFRSvadfdqfpRSESEGA-ARWVADALAAEGFqDVALldTPDGtqSVYGYLPGPEGakTVLLYAHYD 92
Cdd:PRK08652 1 TERAKELLKQLVKIPS--------PSGQEDEiALHIMEFLESLGY-DVHI--ESDG--EVINIVVNSKA--ELFVEVHYD 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752498394 93 VQPPLdeagwaTPPFElteRDGRWYGRGAADCKGGVIMHLLALRALKANGGVPVhVKVIAEGSEEQGTGGLERYAEEHP 171
Cdd:PRK08652 66 TVPVR------AEFFV---DGVYVYGTGACDAKGGVAAILLALEELGKEFEDLN-VGIAFVSDEEEGGRGSALFAERYR 134
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
17-373 |
1.55e-05 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 46.87 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 17 AKEELTELVAFRSVAdfdqfprSESEGAARWVADALAAEGFQdvALLDTPDGTQSVYGylpgpEGAKTVLLYAHYDvqpp 96
Cdd:PRK04443 8 ARELLKGLVEIPSPS-------GEEAAAAEFLVEFMESHGRE--AWVDEAGNARGPAG-----DGPPLVLLLGHID---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 97 ldeagwaTPPFELTER--DGRWYGRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEgsEEQGTGGLERYAEEHpglL 174
Cdd:PRK04443 70 -------TVPGDIPVRveDGVLWGRGSVDAKGPLAAFAAAAARLEALVRARVSFVGAVE--EEAPSSGGARLVADR---E 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 175 EADTIVIGDAGnfrvGLPTVTATLRGMTLVRVRIDTLAGnlHS-GQFGGAAPDALAALIRVLDSLRAEDGsttvdgltGD 253
Cdd:PRK04443 138 RPDAVIIGEPS----GWDGITLGYKGRLLVTYVATSESF--HSaGPEPNAAEDAIEWWLAVEAWFEANDG--------RE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 254 TAWDGLQYDEERFRQDAkvlDGVgligsgtvadriwarpavtvlgidcppvvgatpSVQASARalISLRVPPGVDAAEAT 333
Cdd:PRK04443 204 RVFDQVTPKLVDFDSSS---DGL---------------------------------TVEAEMT--VGLRLPPGLSPEEAR 245
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1752498394 334 KLLQAHLEartpwGARVSTEqiGQGQAFRADTTSPAYQAM 373
Cdd:PRK04443 246 EILDALLP-----TGTVTFT--GAVPAYMVSKRTPLARAF 278
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
48-170 |
2.56e-05 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 46.16 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 48 VADALAAEGFQdVALLDT-PDGTQSVYGYLPGpEGAKTVLLYAHYD-VQPPldeAGWATPPFEltERDGRWYGRGAADCK 125
Cdd:PRK06133 66 LAERLKALGAK-VERAPTpPSAGDMVVATFKG-TGKRRIMLIAHMDtVYLP---GMLAKQPFR--IDGDRAYGPGIADDK 138
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1752498394 126 GGVIMHLLALRALKANG----GvpvHVKVIAEGSEEQGTGG----LERYAEEH 170
Cdd:PRK06133 139 GGVAVILHALKILQQLGfkdyG---TLTVLFNPDEETGSPGsrelIAELAAQH 188
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
78-185 |
3.18e-05 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 45.91 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 78 GPEGAKTVLLYAHYDVQPPLDeaGWATPPFELTERDGRWYGRGAADCKGGVIMHLLALRALKANgGVPVH--VKVIAEGS 155
Cdd:PRK13013 80 GARDGDCVHFNSHHDVVEVGH--GWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAV-YPDFAgsIEISGTAD 156
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1752498394 156 EEQG-------TGGLERYAEEH------PGLLEADTIVIGDAG 185
Cdd:PRK13013 157 EESGgfggvayLAEQGRFSPDRvqhviiPEPLNKDRICLGHRG 199
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
198-347 |
1.92e-04 |
|
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: 40.79 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 198 LRGMTLVRVRIDTLAGnlHSGqFGGAAPDALAALIRVLDSLRAEDGSTTvdgltgdtawdglqydeerfrqdakvldgvg 277
Cdd:pfam07687 3 HKGLAGGHLTVKGKAG--HSG-APGKGVNAIKLLARLLAELPAEYGDIG------------------------------- 48
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 278 ligsgtvadRIWARPAVTVLGIDCPPVVGATPsvqASARALISLRVPPGVDAAEATKLLQAHLEARTPWG 347
Cdd:pfam07687 49 ---------FDFPRTTLNITGIEGGTATNVIP---AEAEAKFDIRLLPGEDLEELLEEIEAILEKELPEG 106
|
|
| Iap |
COG2234 |
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ... |
35-175 |
2.28e-04 |
|
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];
Pssm-ID: 441835 [Multi-domain] Cd Length: 257 Bit Score: 42.81 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 35 QFPRSESEGAARWVADALAAEGFQDVALLDTPDGTQSVYGYLPGPEGA-KTVLLYAHYDvqppldeaGWATppfelterd 113
Cdd:COG2234 12 TAGAAAAAAAAAAAAAGLALLKLKGLLLEAAGGDSRNVIAEIPGTDPPdEVVVLGAHYD--------SVGS--------- 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752498394 114 grwYGRGAADCKGGVIMhLLAL-RALKANGGVPVH-VKVIAEGSEEQGTGGLERYAEEHPGLLE 175
Cdd:COG2234 75 ---IGPGADDNASGVAA-LLELaRALAALGPKPKRtIRFVAFGAEEQGLLGSRYYAENLKAPLE 134
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
61-170 |
4.08e-04 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 42.72 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 61 ALLDTPDGTQSVYGYLPGPEGAK-TVLLYAHYDVQPpLDEAG----WATPPFELTE--------------RD---GRW-Y 117
Cdd:cd05654 49 LLPPDDLGRRNVTALVKGKKPSKrTIILISHFDTVG-IEDYGelkdIAFDPDELTKafseyveeldeevrEDllsGEWlF 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 118 GRGAADCKGGVIMHLLALRALKANGGVPVHVKVIAEGSEEQGTGG-------LERYAEEH 170
Cdd:cd05654 128 GRGTMDMKSGLAVHLALLEQASEDEDFDGNLLLMAVPDEEVNSRGmraavpaLLELKKKH 187
|
|
| M28_like |
cd08015 |
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ... |
69-269 |
5.72e-04 |
|
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.
Pssm-ID: 349937 [Multi-domain] Cd Length: 218 Bit Score: 41.04 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 69 TQSVYGYLPGPEGA-KTVLLYAHYDvqppldeaGWATppfelterdgrwyGRGAADCKGGVIMHLLALRALKANGGVPVH 147
Cdd:cd08015 1 TYNVIAEIPGSDKKdEVVILGAHLD--------SWHG-------------ATGATDNGAGTAVMMEAMRILKAIGSKPKR 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 148 -VKVIAEGSEEQGTGGLERYAEEHPG-----LLEADTIVIGDAGNFRVGlptvTATLRGMtlvrvridTLAGNLHSGqfg 221
Cdd:cd08015 60 tIRVALWGSEEQGLHGSRAYVEKHFGdpptmQLQRDHKKISAYFNLDNG----TGRIRGI--------YLQGNLAAY--- 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1752498394 222 gaapDALAALIRVLDSLRAEDGSTTVDGLTGDTAWDGLQYDEERFRQD 269
Cdd:cd08015 125 ----PIFSAWLYPFHDLGATTVIERNTGGTDHAAFDAVGIPAFQFIQD 168
|
|
| Peptidase_M28 |
pfam04389 |
Peptidase family M28; |
72-171 |
7.69e-04 |
|
Peptidase family M28;
Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 40.35 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 72 VYGYLPGPEGAKTVLLYAHYDvqppldeaGWATPPfelterdgrwygrGAADCKGGVIMHLLALRALKANGGVPVHVKVI 151
Cdd:pfam04389 2 VIAKLPGKAPDEVVLLSAHYD--------SVGTGP-------------GADDNASGVAALLELARVLAAGQRPKRSVRFL 60
|
90 100
....*....|....*....|
gi 1752498394 152 AEGSEEQGTGGLERYAEEHP 171
Cdd:pfam04389 61 FFDAEEAGLLGSHHFAKSHP 80
|
|
| M28 |
cd02690 |
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ... |
70-185 |
1.31e-03 |
|
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; 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. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases.
Pssm-ID: 349868 [Multi-domain] Cd Length: 202 Bit Score: 40.02 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 70 QSVYGYLPGPEGAK-TVLLYAHYDvqppldeagwaTPPFelterdgrwyGRGAADCKGGVIMHLLALRALKANGGVP-VH 147
Cdd:cd02690 2 YNVIATIKGSDKPDeVILIGAHYD-----------SVPL----------SPGANDNASGVAVLLELARVLSKLQLKPkRS 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1752498394 148 VKVIAEGSEEQGTGGLERYAEEHP-------GLLEADTIVIGDAG 185
Cdd:cd02690 61 IRFAFWDAEELGLLGSKYYAEQLLsslknirAALNLDMIGGAGPD 105
|
|
| PRK12892 |
PRK12892 |
allantoate amidohydrolase; Reviewed |
44-157 |
1.60e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 183817 [Multi-domain] Cd Length: 412 Bit Score: 40.46 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498394 44 AARWVADALAAEGfqdvaLLDTPDGTQSVYGYLPGPEGAKTVLLYAHYDVQPPldeAGWAtppfelterDGRWygrgaad 123
Cdd:PRK12892 41 ARRRLAAWCEAAG-----LAVRIDGIGNVFGRLPGPGPGPALLVGSHLDSQNL---GGRY---------DGAL------- 96
|
90 100 110
....*....|....*....|....*....|....*
gi 1752498394 124 ckgGVIMHLLALRALKANGG-VPVHVKVIAEGSEE 157
Cdd:PRK12892 97 ---GVVAGLEAARALNEHGIaTRHPLDVVAWCDEE 128
|
|
| M28_Pgcp_like |
cd03883 |
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate ... |
118-188 |
7.56e-03 |
|
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate carboxypeptidase (PGCP; blood plasma glutamate carboxypeptidase; EC 3.4.17.21) subfamily. PGCP is a 56kDa glutamate carboxypeptidase that is mainly produced in mammalian placenta and kidney, the majority of which is thought to be secreted into the bloodstream. Similar proteins are also found in other species, including bacteria. These proteins contain protease-associated (PA) domain inserts between the first and second strands of the central beta sheet in the protease-like domain. The PA domains may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. The exact physiological substrates of PGCP are unknown, although this enzyme may play an important role in the hydrolysis of circulating peptides. Its closest homolog encodes an important brain glutamate carboxypeptidase II (NAALADase) identical to the prostate-specific membrane antigen (PSMA), which serves as a marker for prostatic cancer metastasis. Hypermethylation of PGCP gene has been associated with human bronchial epithelial (HBE) cell immortalization and lung cancer. PGCP also provides an attractive target for serological analysis in hepatitis C virus (HCV)-induced hepatocellular carcinoma (HCC) patients.
Pssm-ID: 349879 [Multi-domain] Cd Length: 425 Bit Score: 38.44 E-value: 7.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752498394 118 GRGAADCKGGVIMHLLALRALKANGGVPVH-VKVIAEGSEEQGTGGLERYAEEHPGLLEADTIVI-GDAGNFR 188
Cdd:cd03883 255 GTGAMDDGGGVAISWEALKLIKDLGLKPKRtIRVVLWTGEEQGLVGAKAYAEAHKDELENHVFAMeSDIGTFT 327
|
|
| |
