|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
21-440 |
0e+00 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 869.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 21 ISQLLKQIDSRKEELLELTKTLIRFETPAPPARNTNEAQEFVADFLRKRNFSIDKWDVYPNDPNVVGVKKGTESGTYKSL 100
Cdd:PRK08596 1 VSQLLEQIELRKDELLELLKTLVRFETPAPPARNTNEAQEFIAEFLRKLGFSVDKWDVYPNDPNVVGVKKGTESDAYKSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 101 IINGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGEAGTL 180
Cdd:PRK08596 81 IINGHMDVAEVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEVGEAGTL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 181 QCCKRGYDADFAVVVDTSNLHMQGQGGVITGWITVKSPRTFHDATRRQMIHAGGRLFGASAIEKMMKIVQSLQELERHWA 260
Cdd:PRK08596 161 QCCERGYDADFAVVVDTSDLHMQGQGGVITGWITVKSPQTFHDGTRRQMIHAGGGLFGASAIEKMMKIIQSLQELERHWA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 261 VMKTYEGYPSGTTTINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAADPWLSENPPQFKWGGE 340
Cdd:PRK08596 241 VMKSYPGFPPGTNTINPAVIEGGRHAAFIADECRLWITVHFYPNETYEQVIKEIEEYIGKVAAADPWLRENPPQFKWGGE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 341 SMIVDRGEIFPSLEVDSEHVAVKTLSAVHESILSKNAILDMSATVTDGGWFSEFHIPAIIYGPGTLEEAHSVNEKVEVEQ 420
Cdd:PRK08596 321 SMIEDRGEIFPSLEIDSEHPAVKTLSSAHESVLSKNAILDMSTTVTDGGWFAEFGIPAVIYGPGTLEEAHSVNEKVEIEQ 400
|
410 420
....*....|....*....|
gi 1586368115 421 LIEFTKVITAFIYEWCHTKK 440
Cdd:PRK08596 401 LIEYTKVITAFIYEWCHTKK 420
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
37-437 |
7.99e-134 |
|
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: 390.52 E-value: 7.99e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 37 ELTKTLIRFetpapPARNTNE--AQEFVADFLRKRNFSIDKWDV-----------------YPNDPNVVGVKKGTeSGTY 97
Cdd:cd03895 1 AFLQDLVRF-----PSLRGEEaaAQDLVAAALRSRGYTVDRWEIdveklkhhpgfspvavdYAGAPNVVGTHRPR-GETG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 98 KSLIINGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGEA 177
Cdd:cd03895 75 RSLILNGHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 178 GTLQCCKRGYDADFAVVVDTSNLHM-QGQGGVItgWITVKSPRTFHdatrrqmiHAGGRLFGASAIEKMMKIVQSLQELE 256
Cdd:cd03895 155 GALAALMRGYRADAALIPEPTELKLvRAQVGVI--WFRVKVRGTPA--------HVAEASEGVNAIEKAMHLIQALQELE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 257 RHWAVMKT----YEGYPsGTTTINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAADPWLSENP 332
Cdd:cd03895 225 REWNARKKshphFSDHP-HPINFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVADAAATDPWLSNHP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 333 PQFKWGGESmivdrgeiFPSLEVDSEHVAVKTLSAVHESILSKNAILDMSATVTDGGWFSEFH-IPAIIYGPGTlEEAHS 411
Cdd:cd03895 304 PEVEWNGFQ--------AEGYVLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGdIPALCYGPGS-RDAHG 374
|
410 420
....*....|....*....|....*.
gi 1586368115 412 VNEKVEVEQLIEFTKVITAFIYEWCH 437
Cdd:cd03895 375 FDESVDLESLRKITKTIALFIAEWCG 400
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
36-427 |
7.59e-133 |
|
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: 387.14 E-value: 7.59e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 36 LELTKTLIRFETPAPPARNTNEAQEFVADFLRKRNFSIDKWDVYPNDPNVVG--VKKGTESGTYKSLIINGHMDVAEVSI 113
Cdd:TIGR01910 1 VELLKDLISIPSVNPPGGNEETIANYIKDLLREFGFSTDVIEITDDRLKVLGkvVVKEPGNGNEKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 114 DEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGEAGTLQCCKRGYDAdfav 193
Cdd:TIGR01910 81 LELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTLYLLQRGYFK---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 194 vvDTSNLHMQGQGGVITGWITVKSPRTFHDATRRQMIHAGGRLFGASAIEKMMKIVQSLQELERHWAVMKTYEGYPsGTT 273
Cdd:TIGR01910 157 --DADGVLIPEPSGGDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEEHIYARNSYGFIP-GPI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 274 TINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAADPWLSENPPQFKWGGesmivdrgeifpSL 353
Cdd:TIGR01910 234 TFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYENEPVVKWSG------------PN 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586368115 354 EVDSEHVAVKTLSAVHESILSKNAILDMSATVTDGGWFSEFHIPAIIYGPGTLEEAHSVNEKVEVEQLIEFTKV 427
Cdd:TIGR01910 302 ETPPDSRLVKALEAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPGDLETAHQVNEYISIKNLVESTKV 375
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
22-436 |
2.07e-104 |
|
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: 315.29 E-value: 2.07e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 22 SQLLKQIDSRKEELLELTKTLIRFETPAPPARntnEAQEFVADFLRKRNFSIDKWDVYPNDPNVVGVKKGTESGtyKSLI 101
Cdd:COG0624 1 AAVLAAIDAHLDEALELLRELVRIPSVSGEEA---AAAELLAELLEALGFEVERLEVPPGRPNLVARRPGDGGG--PTLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 102 INGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGEAGTLQ 181
Cdd:COG0624 76 LYGHLDVVPPGDLELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGSPGARA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 182 CCKR---GYDADFAVVVDTSNLHM--QGQGGVITGWITVKSPRTfhdatrrqmiHAGGRLFGASAIEKMMKIVQSLQELE 256
Cdd:COG0624 156 LVEElaeGLKADAAIVGEPTGVPTivTGHKGSLRFELTVRGKAA----------HSSRPELGVNAIEALARALAALRDLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 257 RHWAVMKTYegypsGTTTINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAadpwlsenPPQFK 336
Cdd:COG0624 226 FDGRADPLF-----GRTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAP--------GVEVE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 337 WggeSMIVDRgeiFPSLEVDSEHVAVKTLSAVHESILSKNAILDMSATVTDGGWFSEFH-IPAIIYGPGTLEEAHSVNEK 415
Cdd:COG0624 293 V---EVLGDG---RPPFETPPDSPLVAAARAAIREVTGKEPVLSGVGGGTDARFFAEALgIPTVVFGPGDGAGAHAPDEY 366
|
410 420
....*....|....*....|.
gi 1586368115 416 VEVEQLIEFTKVITAFIYEWC 436
Cdd:COG0624 367 VELDDLEKGARVLARLLERLA 387
|
|
| PRK06915 |
PRK06915 |
peptidase; |
17-440 |
2.71e-80 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 254.23 E-value: 2.71e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 17 MNPEiSQLLKQIDSRKEELLELTKTLIRFETPAPPARNtneAQEFVADFLRKRNFSIDKWDV-----------------Y 79
Cdd:PRK06915 2 EQLK-KQICDYIESHEEEAVKLLKRLIQEKSVSGDESG---AQAIVIEKLRELGLDLDIWEPsfkklkdhpyfvsprtsF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 80 PNDPNVVGVKKGTESGtyKSLIINGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIE 159
Cdd:PRK06915 78 SDSPNIVATLKGSGGG--KSMILNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 160 LPGNLIFQSVIGEEVGEAGTLQCCKRGYDADFAVVVDTSNLHM--QGQGGVitgW--ITVKSPRTfhdatrrqmiHAGGR 235
Cdd:PRK06915 156 LKGDVIFQSVIEEESGGAGTLAAILRGYKADGAIIPEPTNMKFfpKQQGSM---WfrLHVKGKAA----------HGGTR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 236 LFGASAIEKMMKIVQSLQELERHWAVMKT---YEGYPSgTTTINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIE 312
Cdd:PRK06915 223 YEGVSAIEKSMFVIDHLRKLEEKRNDRITdplYKGIPI-PIPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 313 EIEAYIRKVAAADPWLSENPPQFKWGGESMIvdrgeifPSlEVDSEHVAVKTLSAVHESILSKNAILDMSATVTDGGWFS 392
Cdd:PRK06915 302 EFENWIAELNDVDEWFVEHPVEVEWFGARWV-------PG-ELEENHPLMTTLEHNFVEIEGNKPIIEASPWGTDGGLLT 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1586368115 393 EF-HIPAIIYGPGTLEEAHSVNEKVEVEQLIEFTKVITAFIYEWCHTKK 440
Cdd:PRK06915 374 QIaGVPTIVFGPGETKVAHYPNEYIEVDKMIAAAKIIALTLLDWCEVKK 422
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
15-436 |
2.77e-78 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 249.15 E-value: 2.77e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 15 LAMNPEISQ-LLKQIDSRKEELLELTKTLIRFetpapPARNTNEA--QEFVADFLRKRNFSIDKWDVYPND--------- 82
Cdd:PRK06837 1 MMLTPDLTQrILAAVDAGFDAQVAFTQDLVRF-----PSTRGAEApcQDFLARAFRERGYEVDRWSIDPDDlkshpgagp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 83 --------PNVVGVKKGtESGTYKSLIINGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLE 154
Cdd:PRK06837 76 veidysgaPNVVGTYRP-AGKTGRSLILQGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 155 EAGIELPGNLIFQSVIGEEVGEAGTLQCCKRGYDADFAVVVD-TSNLHMQGQGGVItgWITVKsprtfhdaTRRQMIHAG 233
Cdd:PRK06837 155 AAGLAPAARVHFQSVIEEESTGNGALSTLQRGYRADACLIPEpTGEKLVRAQVGVI--WFRLR--------VRGAPVHVR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 234 GRLFGASAIEKMMKIVQSLQELERHWAVMKT----YEGYPSgTTTINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQ 309
Cdd:PRK06837 225 EAGTGANAIDAAYHLIQALRELEAEWNARKAsdphFEDVPH-PINFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAAD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 310 IIEEIEAYIRKVAAADPWLSENPPQFKWGGesmivdrgeiF--PSLEVDSEHVAVKTLSAVHESILSKNAILDMSATVTD 387
Cdd:PRK06837 304 AQAEIEACLAAAARDDRFLSNNPPEVVWSG----------FlaEGYVLEPGSEAEAALARAHAAVFGGPLRSFVTTAYTD 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1586368115 388 GGWFS-EFHIPAIIYGPgTLEEAHSVNEKVEVEQLIEFTKVITAFIYEWC 436
Cdd:PRK06837 374 TRFYGlYYGIPALCYGP-SGEGIHGFDERVDLESVRKVTKTIALFVAEWC 422
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
37-432 |
1.77e-70 |
|
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: 226.80 E-value: 1.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 37 ELTKTLIRFETPAPPARntnEAQEFVADFLRKRNFSIDkWDVYPNDPNVVgVKKGTESGtyKSLIINGHMDVAEVSIDEA 116
Cdd:cd08659 1 SLLQDLVQIPSVNPPEA---EVAEYLAELLAKRGYGIE-STIVEGRGNLV-ATVGGGDG--PVLLLNGHIDTVPPGDGDK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 117 WETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGEAGTLQCCKRGY--DADFAVV 194
Cdd:cd08659 74 WSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLEAGYadRLDALIV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 195 VDTSNLHMQ-GQGGviTGWITVksprTFHDATRrqmiHAGGRLFGASAIEKMMKIVQSLQELERHWAVMKTYegypsGTT 273
Cdd:cd08659 154 GEPTGLDVVyAHKG--SLWLRV----TVHGKAA----HSSMPELGVNAIYALADFLAELRTLFEELPAHPLL-----GPP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 274 TINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKvaaadpwlSENPPQFKWggesmivdRGEIFPSL 353
Cdd:cd08659 219 TLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEE--------HEAKLTVEV--------SLDGDPPF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 354 EVDSEHVAVKTLSAVHESiLSKNAILDMSATVTDGGWFSEF-HIPAIIYGPGTLEEAHSVNEKVEVEQLIEFTKVITAFI 432
Cdd:cd08659 283 FTDPDHPLVQALQAAARA-LGGDPVVRPFTGTTDASYFAKDlGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
28-432 |
1.34e-54 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 186.35 E-value: 1.34e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 28 IDSRKEELLELTKTLIRFETPAPPARNTNEAQEFVADFLRKRNFSIDKWDV--------YPNDPNVVGVKKGTEsgtyKS 99
Cdd:PRK08651 1 VEAMMFDIVEFLKDLIKIPTVNPPGENYEEIAEFLRDTLEELGFSTEIIEVpneyvkkhDGPRPNLIARRGSGN----PH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 100 LIINGHMDVaeVSIDEAW-ETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGielPGNLIFQSVIGEEVGEAG 178
Cdd:PRK08651 77 LHFNGHYDV--VPPGEGWsVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAG---DGNIELAIVPDEETGGTG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 179 TLQCCKRGYD-ADFAVVVDTSNLHMQGQG--GVITGWITVKSprtfhdatrRQmIHAGGRLFGASAIEKMMKIVQSLQEL 255
Cdd:PRK08651 152 TGYLVEEGKVtPDYVIVGEPSGLDNICIGhrGLVWGVVKVYG---------KQ-AHASTPWLGINAFEAAAKIAERLKSS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 256 ERHWAVMKTYEGYPSGTTTIN--PAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAADPWLSENPP 333
Cdd:PRK08651 222 LSTIKSKYEYDDERGAKPTVTlgGPTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVEFEI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 334 QfkwggesmivdrgEIFPSLEVDSEHVAVKTLSAVHESILSKNAILDMSATVTDGGWFSEFHIPAIIYGPGTLEEAHSVN 413
Cdd:PRK08651 302 T-------------PFSEAFVTDPDSELVKALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGELELAHAPD 368
|
410
....*....|....*....
gi 1586368115 414 EKVEVEQLIEFTKVITAFI 432
Cdd:PRK08651 369 EYVEVKDVEKAAKVYEEVL 387
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
36-432 |
1.37e-46 |
|
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: 164.10 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 36 LELTKTLIRFETPAPPARNTNEAQEFVADFLRKRNFSIDKWDVYPNDPNVVGVKKGTESGtyKSLIINGHMDVAEVSIDE 115
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDNTSAIAAYIKLLLEDLGYPVELHEPPEEIYGVVSNIVGGRKG--KRLLFNGHYDVVPAGDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 116 AWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEE-VGEAGTLQCCKRGYDA-DFAV 193
Cdd:cd08011 79 GWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEEtGGRAGTKYLLEKVRIKpNDVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 194 VV-DTSNLHMQ-GQGGVItgWITVKSPRTfhdatrrqMIHAGGRLFGASAIEKMMKIVQSLQELERhwavmktyegypsg 271
Cdd:cd08011 159 IGePSGSDNIRiGEKGLV--WVIIEITGK--------PAHGSLPHRGESAVKAAMKLIERLYELEK-------------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 272 ttTINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAADPwlsenppqfkwggesmiVDRGEIFP 351
Cdd:cd08011 215 --TVNPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSIEEVSF-----------------EIKSFYSP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 352 SLEVDSEHVAVKTLSAVHEsILSKNAILDMSATVTDGGWFSEFHIPAIIYGPGTLEEAHSVNEKVEVEQLIEFTKVITAF 431
Cdd:cd08011 276 TVSNPDSEIVKKTEEAITE-VLGIRPKEVISVGASDARFYRNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVHALV 354
|
.
gi 1586368115 432 I 432
Cdd:cd08011 355 A 355
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
33-436 |
3.75e-46 |
|
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: 163.80 E-value: 3.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 33 EELLELTKTLIRFETPAPPARNTNEAQE-----FVADFLRKRNFSIDKWDVYPNDPNVVGVKKGTESGtyKSLIINGHMD 107
Cdd:cd08013 1 DDPVSLTQTLVRINSSNPSLSATGGAGEaeiatYVAAWLAHRGIEAHRIEGTPGRPSVVGVVRGTGGG--KSLMLNGHID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 108 VaeVSIDeAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGieLPGNLIFQSVIGEEVGEAGTLQCCKRGY 187
Cdd:cd08013 79 T--VTLD-GYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAG--LRGDVILAAVADEEDASLGTQEVLAAGW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 188 DADFAVVVDTSNLHMqgqggvitgwITVKSPRTFHDATrrqmIHA----GGR-LFGASAIEKMMKIvqsLQELERHWAVM 262
Cdd:cd08013 154 RADAAIVTEPTNLQI----------IHAHKGFVWFEVD----IHGraahGSRpDLGVDAILKAGYF---LVALEEYQQEL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 263 KTYEGYPS-GTTTINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAADPWLSENPPQfkwgges 341
Cdd:cd08013 217 PERPVDPLlGRASVHASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTAILGELAQTVPNFSYREPR------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 342 MIVDRgeifPSLEVDSEHVAVKTLSAVHESILSKNAILDMSATVTDGGWFSEFHIPAIIYGP-GTleEAHSVNEKVEVEQ 420
Cdd:cd08013 290 ITLSR----PPFEVPKEHPFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPsGA--GLHAKEEWVDVES 363
|
410
....*....|....*.
gi 1586368115 421 LIEFTKVITAFIYEWC 436
Cdd:cd08013 364 IRQLREVLSAVVREFC 379
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
37-421 |
3.57e-43 |
|
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: 155.44 E-value: 3.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 37 ELTKTLIRFETPAppaRNTNEAQ-EFVADFLRKRNFSIDKwdVYPND---PNVVGVKKGTESGTyksLIINGHMDVaeVS 112
Cdd:cd03894 1 ELLARLVAFDTVS---RNSNLALiEYVADYLAALGVKSRR--VPVPEggkANLLATLGPGGEGG---LLLSGHTDV--VP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 113 IDE-AWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPgnLIFQSVIGEEVGEAG------TLQccKR 185
Cdd:cd03894 71 VDGqKWSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKP--LHLAFSYDEEVGCLGvrhliaALA--AR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 186 GYDADFAVVVD-TSnlhMQ---GQGGVITGWITVKSpRTFHDATRRQmihaggrlfGASAIEKMMKIVQSLQELERHWAV 261
Cdd:cd03894 147 GGRPDAAIVGEpTS---LQpvvAHKGIASYRIRVRG-RAAHSSLPPL---------GVNAIEAAARLIGKLRELADRLAP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 262 MKTYEGYPSGTTTINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAADPwlsenppqfkwGGes 341
Cdd:cd03894 214 GLRDPPFDPPYPTLNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPE-----------AG-- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 342 MIVDRGEIFPSLEVDSEHVAVKTLSAVHESilsknailDMSATV---TDGGWFSEFHIPAIIYGPGTLEEAHSVNEKVEV 418
Cdd:cd03894 281 IEVEPLFEVPGLETDEDAPLVRLAAALAGD--------NKVRTVaygTEAGLFQRAGIPTVVCGPGSIAQAHTPDEFVEL 352
|
...
gi 1586368115 419 EQL 421
Cdd:cd03894 353 EQL 355
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
101-434 |
4.52e-39 |
|
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: 142.87 E-value: 4.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 101 IINGHMDVaeVSIDEAWeTNPFEPFIkDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIeLPGNLIFQSVIGEEVGEAGTL 180
Cdd:pfam01546 1 LLRGHMDV--VPDEETW-GWPFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGL-KKGTVKLLFQPDEEGGMGGAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 181 QCCKRGY------DADFAVVV-DTSNLHMQ-------GQGGVITGWITVKSpRTFHdATRRQMihaggrlfGASAIEKMM 246
Cdd:pfam01546 76 ALIEDGLlerekvDAVFGLHIgEPTLLEGGiaigvvtGHRGSLRFRVTVKG-KGGH-ASTPHL--------GVNAIVAAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 247 KIVQSLQELERHWAVmktyEGYPSGTTTINPAVIEGGRHAafIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAADP 326
Cdd:pfam01546 146 RLILALQDIVSRNVD----PLDPAVVTVGNITGIPGGVNV--IPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 327 WLSEnppqfkwggesmiVDRGEIFPSLEVDSEHVaVKTLSAVHESILSKNAILDMSATV--TDGGWFSEfHIPA--IIYG 402
Cdd:pfam01546 220 VKVE-------------VEYVEGGAPPLVNDSPL-VAALREAAKELFGLKVELIVSGSMggTDAAFFLL-GVPPtvVFFG 284
|
330 340 350
....*....|....*....|....*....|..
gi 1586368115 403 PGTlEEAHSVNEKVEVEQLIEFTKVITAFIYE 434
Cdd:pfam01546 285 PGS-GLAHSPNEYVDLDDLEKGAKVLARLLLK 315
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
21-428 |
5.18e-38 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 142.98 E-value: 5.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 21 ISQLLKQIDSRKEELLELTKTLIRFETPAPPARNTNEAQEFVADFLRKRNFSID---------KWDVYPNdPNVVGVKKG 91
Cdd:PRK13013 2 DDRLFAAIEARRDDLVALTQDLIRIPTLNPPGRAYREICEFLAARLAPRGFEVEliraegapgDSETYPR-WNLVARRQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 92 TESGtyKSLIINGHMDVAEVSidEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIG 171
Cdd:PRK13013 81 ARDG--DCVHFNSHHDVVEVG--HGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 172 EEVGE-AGTLQCCKRGYDADFAV--VVDTSNLHMQ----GQGGVItgWITVKsprtfhdaTRRQMIHAGGRLFGASAIEK 244
Cdd:PRK13013 157 EESGGfGGVAYLAEQGRFSPDRVqhVIIPEPLNKDriclGHRGVW--WAEVE--------TRGRIAHGSMPFLGDSAIRH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 245 MMKIvqsLQELE---------RHWAVMKTYEGYPSGTTTINPavIEGGR----------HAAFIADECRLWITVHFYPNE 305
Cdd:PRK13013 227 MGAV---LAEIEerlfpllatRRTAMPVVPEGARQSTLNINS--IHGGEpeqdpdytglPAPCVADRCRIVIDRRFLIEE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 306 THEQIIEEIEAYIRKVAAADPwlsenppqfkwGGESMIVDRGEIFPSLeVDSEHVAVKTLSAVHESILSKNAILdmsatV 385
Cdd:PRK13013 302 DLDEVKAEITALLERLKRARP-----------GFAYEIRDLFEVLPTM-TDRDAPVVRSVAAAIERVLGRQADY-----V 364
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1586368115 386 TDGGWFSEFHIP-------AIIYGPGTLEEAHSVNEKVEVEQLIEFTKVI 428
Cdd:PRK13013 365 VSPGTYDQKHIDrigklknCIAYGPGILDLAHQPDEWVGIADMVDSAKVM 414
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
23-422 |
1.69e-33 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 129.67 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 23 QLLKQIDSRKEELLELTKTLIRFetpapPARNTNEAQ--EFVADFLRKRNFsiDKWDVypnDP--NVVGVKKGTEsgtyK 98
Cdd:PRK13004 5 LILMLAEKYKADMTRFLRDLIRI-----PSESGDEKRvvKRIKEEMEKVGF--DKVEI---DPmgNVLGYIGHGK----K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 99 SLIINGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEvgeag 178
Cdd:PRK13004 71 LIAFDAHIDTVGIGDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEE----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 179 tlqCC----------KRGYDADFAVVVDTSNLHM-QGQGGVITGWITVKSpRTFHDATRRQmihaggrlfGASAIEKMMK 247
Cdd:PRK13004 146 ---DCdglcwryiieEDKIKPDFVVITEPTDLNIyRGQRGRMEIRVETKG-VSCHGSAPER---------GDNAIYKMAP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 248 IVQSLQELERHWavmKTYEGYPSGTTTIN------PaviegGRHAafIADECRLWITVHFYPNETHEQIIEEIEAyIRKV 321
Cdd:PRK13004 213 ILNELEELNPNL---KEDPFLGKGTLTVSdifstsP-----SRCA--VPDSCAISIDRRLTVGETWESVLAEIRA-LPAV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 322 AAADPWLS----ENPpqfKWGGESMIVDRgeIFPSLEVDSEHVAVKTLSAVHESILSKNAILDMSATVTDG-GWFSEFHI 396
Cdd:PRK13004 282 KKANAKVSmynyDRP---SYTGLVYPTEC--YFPTWLYPEDHEFVKAAVEAYKGLFGKAPEVDKWTFSTNGvSIAGRAGI 356
|
410 420
....*....|....*....|....*.
gi 1586368115 397 PAIIYGPGTLEEAHSVNEKVEVEQLI 422
Cdd:PRK13004 357 PTIGFGPGKEPLAHAPNEYTWKEQLV 382
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
69-431 |
3.79e-31 |
|
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: 122.91 E-value: 3.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 69 RNFSIDKWDVypnDP--NVVGVKKGTEsgtyKSLIINGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGS 146
Cdd:cd05649 29 EKLGFDEVEI---DPmgNVIGYIGGGK----KKILFDGHIDTVGIGNIDNWKFDPYEGYETDGKIYGRGTSDQKGGLASM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 147 LFAIQLLEEAG-IELPGNLIFQSVIGEEVGEAGTLQ--CCKRGYDADFAVVVDTSNLHM-QGQGGVITGWITVKSpRTFH 222
Cdd:cd05649 102 VYAAKIMKDLGlRDFAYTILVAGTVQEEDCDGVCWQyiSKADKIKPDFVVSGEPTDGNIyRGQRGRMEIRVDTKG-VSCH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 223 DAtrrqmihAGGRlfGASAIEKMMKIVQSLQELERHWaVMKTYEGYPSGTTTinpAVIEGGRHAAFIADECRLWITVHFY 302
Cdd:cd05649 181 GS-------APER--GDNAVYKMADIIQDIRQLNPNF-PEAPFLGRGTLTVT---DIFSTSPSRCAVPDSCRISIDRRLT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 303 PNETHEQIIEEIEA-----YIRKVAAADPWLSENPpqfKWGGESMIVDRgeIFPSLEVDSEHVAVKTLSAVHESILSKNA 377
Cdd:cd05649 248 VGETWEGCLEEIRAlpavkKYGDDVAVSMYNYDRP---SYTGEVYESER--YFPTWLLPEDHELVKALLEAYKALFGARP 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1586368115 378 ILDMSATVTDG-GWFSEFHIPAIIYGPGTLEEAHSVNEKVEVEQLIEFTKVITAF 431
Cdd:cd05649 323 LIDKWTFSTNGvSIMGRAGIPCIGFGPGAENQAHAPNEYTWKEDLVRCAAGYAAI 377
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
100-432 |
6.60e-27 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 111.13 E-value: 6.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 100 LIINGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGEAGT 179
Cdd:PRK08588 62 LALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGELGA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 180 LQCCKRGY--DADFAVVVDTSN-----LHMqgqgGVITgwITVKSprtfhdatRRQMIHAGGRLFGASAIEKMMKIVQSL 252
Cdd:PRK08588 142 KQLTEKGYadDLDALIIGEPSGhgivyAHK----GSMD--YKVTS--------TGKAAHSSMPELGVNAIDPLLEFYNEQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 253 QELerhWAVMKTYEGYpSGTTTINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAAdpwlsenp 332
Cdd:PRK08588 208 KEY---FDSIKKHNPY-LGGLTHVVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNQN-------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 333 pqfkwGGESMivdrgeifpSLEVDSEHVAV---------KTLSAVHESILSKNAILDMSATVTDGgwfSEF-----HIPA 398
Cdd:PRK08588 276 -----GAAQL---------SLDIYSNHRPVasdkdsklvQLAKDVAKSYVGQDIPLSAIPGATDA---SSFlkkkpDFPV 338
|
330 340 350
....*....|....*....|....*....|....
gi 1586368115 399 IIYGPGTLEEAHSVNEKVEVEQLIEFTKVITAFI 432
Cdd:PRK08588 339 IIFGPGNNLTAHQVDEYVEKDMYLKFIDIYKEII 372
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
40-434 |
6.05e-26 |
|
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: 108.95 E-value: 6.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 40 KTLIRFETPAPPARNTNE---AQEFVADFLRKRNFSIDKWDVYPNDPNVVGVKKGteSGTYKSLIINGHMDVAEVSIDEA 116
Cdd:cd03893 5 AELVAIPSVSAQPDRREElrrAAEWLADLLRRLGFTVEIVDTSNGAPVVFAEFPG--APGAPTVLLYGHYDVQPAGDEDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 117 WETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGEAGTLQCC---KRGYDADFAV 193
Cdd:cd03893 83 WDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEESGSPSLDQLVeahRDLLAADAIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 194 VVDTSnlhMQGQG---------GVITGWITVKsprtfhdaTRRQMIHAGgrLFG---ASAIEKMMKIVQSLQELERHWAV 261
Cdd:cd03893 163 ISDST---WVGQEqptltyglrGNANFDVEVK--------GLDHDLHSG--LYGgvvPDPMTALAQLLASLRDETGRILV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 262 --------------MKTYEGYPSGTTTIN-------------PAV----IEGGRHAA----FIADECRLWITVHFYPNET 306
Cdd:cd03893 230 pglydavrelpeeeFRLDAGVLEEVEIIGgttgsvaerlwtrPALtvlgIDGGFPGEgsktVIPPRARAKISIRLVPGQD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 307 HEQIIEEIEAYIRKVAAAD------------PWLSE-NPPQFKWGGESMivdrgeifpslevdsehvavKTLSAVHESIl 373
Cdd:cd03893 310 PEEASRLLEAHLEKHAPSGakvtvsyveggmPWRSDpSDPAYQAAKDAL--------------------RTAYGVEPPL- 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586368115 374 sknaildmsatVTDGG------WFSEF-HIPAIIYGPGTLEE-AHSVNEKVEVEQLIEFTKVITAFIYE 434
Cdd:cd03893 369 -----------TREGGsipfisVLQEFpQAPVLLIGVGDPDDnAHSPNESLRLGNYKEGTQAEAALLYS 426
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
36-421 |
2.11e-25 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 106.81 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 36 LELTKTLIRFETPAppaRNTN-EAQEFVADFLRKRNFSIDkwdVYPNDpnvvgvkKGTESGTYKSL--------IINGHM 106
Cdd:PRK07522 7 LDILERLVAFDTVS---RDSNlALIEWVRDYLAAHGVESE---LIPDP-------EGDKANLFATIgpadrggiVLSGHT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 107 DVaeVSIDE-AWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQsvIGEEVGEAGT------ 179
Cdd:PRK07522 74 DV--VPVDGqAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFS--YDEEVGCLGVpsmiar 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 180 LQccKRGYDADFAVVVDTSNlhMQgqggVITGwitvksprtfhdatrrqmiHAGGRLF----------------GASAIE 243
Cdd:PRK07522 150 LP--ERGVKPAGCIVGEPTS--MR----PVVG-------------------HKGKAAYrctvrgraahsslapqGVNAIE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 244 KMMKIVQSLQELERHWAVMKTYEG-----YpsgtTTINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYI 318
Cdd:PRK07522 203 YAARLIAHLRDLADRLAAPGPFDAlfdppY----STLQTGTIQGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 319 R-----KVAAADPwlsenppqfkwggESMI-VDRGEIFPSLEVDSEHVAVKTLSAVHESilsknailDMSATV---TDGG 389
Cdd:PRK07522 279 EaellpEMRAVHP-------------EAAIeFEPLSAYPGLDTAEDAAAARLVRALTGD--------NDLRKVaygTEAG 337
|
410 420 430
....*....|....*....|....*....|..
gi 1586368115 390 WFSEFHIPAIIYGPGTLEEAHSVNEKVEVEQL 421
Cdd:PRK07522 338 LFQRAGIPTVVCGPGSIEQAHKPDEFVELAQL 369
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
41-427 |
2.57e-22 |
|
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: 97.55 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 41 TLIRF-ETPAPPARNTNEAqEFVADFLRKRNFSidkwDVYPNDP-NVVGVKKGTesGTYKSLIINGHMDVAeVSIDEAWE 118
Cdd:cd03896 3 TAIELgEIPAPTFREGARA-DLVAEWMADLGLG----DVERDGRgNVVGRLRGT--GGGPALLFSAHLDTV-FPGDTPAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 119 tnpfePFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEvgEAGTLQCCKR-----GYDADFAV 193
Cdd:cd03896 75 -----VRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEE--GLGDLRGARYllsahGARLDYFV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 194 VVDtsnlhmqGQGGVITgWITVKSPRtfhdaTRRQMIHAGGRLFGA----SAIEKMMKIVQSLQELERHWAvmktyegyP 269
Cdd:cd03896 148 VAE-------GTDGVPH-TGAVGSKR-----FRITTVGPGGHSYGAfgspSAIVAMAKLVEALYEWAAPYV--------P 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 270 SgtTTINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAADPWLSenpPQFKWggesmIVDRgei 349
Cdd:cd03896 207 K--TTFAAIRGGGGTSVNRIANLCSMYLDIRSNPDAELADVQREVEAVVSKLAAKHLRVK---ARVKP-----VGDR--- 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586368115 350 fPSLEVDSEHVAVKTLSAVHEsilSKNAILDMSATVTDGGWFSEFHIPAIIYGPGTLEEAHSVNEKVEVEQLIEFTKV 427
Cdd:cd03896 274 -PGGEAQGTEPLVNAAVAAHR---EVGGDPRPGSSSTDANPANSLGIPAVTYGLGRGGNAHRGDEYVLKDDMLKGAKA 347
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
35-432 |
3.34e-22 |
|
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: 97.13 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 35 LLELTKTLIRFETPAppaRNTNEAQEFVADFLRKRNfsidKWDVYPNDPNVVGvkkGTESGTYKSLIINGHMDVAEV--S 112
Cdd:cd05647 1 PIELTAALVDIPSVS---GNEKPIADEIEAALRTLP----HLEVIRDGNTVVA---RTERGLASRVILAGHLDTVPVagN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 113 IDEAWEtnpfepfiKDDWLVGRGAADMKGGLAGSLFAIQLLEEAgiELPGNLIFQSVIGEEV-GEAGTLQCCKRGY---- 187
Cdd:cd05647 71 LPSRVE--------EDGVLYGCGATDMKAGDAVQLKLAATLAAA--TLKHDLTLIFYDCEEVaAELNGLGRLAEEHpewl 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 188 DADFAVVVDTSNLHMQ-GQGGVITGWITVKSPRTfhdatrrqmiHAGGRLFGASAIEKMMKIVQSLQELERHWAVMK--T 264
Cdd:cd05647 141 AADFAVLGEPTDGTIEgGCQGTLRFKVTTHGVRA----------HSARSWLGENAIHKLAPILARLAAYEPRTVNIDglT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 265 Y-EGypsgtttINPAVIEGGRHAAFIADECRLWITVHFYPNETheqiIEEIEAYIRKVAAADpwlsenppqfkwGGESMI 343
Cdd:cd05647 211 YrEG-------LNAVFISGGVAGNVIPDEARVNLNYRFAPDKS----LAEAIAHVREVFEGL------------GYEIEV 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 344 VD-RGEIFPSLevdSEHVAVKTLSAVHESILSKNAILDMSAtvtdggwFSEFHIPAIIYGPGTLEEAHSVNEKVEVEQLI 422
Cdd:cd05647 268 TDlSPGALPGL---DHPVARDLIEAVGGKVRAKYGWTDVAR-------FSALGIPAVNFGPGDPLLAHKRDEQVPVEQIT 337
|
410
....*....|
gi 1586368115 423 EFTKVITAFI 432
Cdd:cd05647 338 ACAAILRRWL 347
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
36-432 |
4.64e-22 |
|
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: 96.80 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 36 LELTKTLIRFE--TPapparNTNEAQEFVADFLRKRNFSIDKwdvypndPNVVGVK-----KGTESGTyksLIINGHMDV 108
Cdd:cd03891 1 LELAKELIRRPsvTP-----DDAGAQDLIAERLKALGFTCER-------LEFGGVKnlwarRGTGGPH---LCFAGHTDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 109 AEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFqsVI-GEEVGEA--GTLQCC-- 183
Cdd:cd03891 66 VPPGDLEGWSSDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISF--LItSDEEGPAidGTKKVLew 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 184 --KRGYDADFAVVVD-TSNLHM-----QGQGGVITGWITVKSprtfhdatrRQmihaggrlfGASA--------IEKMMK 247
Cdd:cd03891 144 lkARGEKIDYCIVGEpTSEKKLgdtikIGRRGSLNGKLTIKG---------KQ---------GHVAyphladnpIHLLAP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 248 IVQSLqeLERHWAvmKTYEGYPSgtTTINPAVIEGGRHAA-FIADECRLWITVHFYPNETHEQIIEEIEAYIRKVaaadp 326
Cdd:cd03891 206 ILAEL--TATVLD--EGNEFFPP--SSLQITNIDVGNGATnVIPGELKAKFNIRFNDEHTGESLKARIEAILDKH----- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 327 wlsENPPQFKW--GGESMIVDRGEIfpslevdsehvaVKTLSAVHESILSKNAILDMSATVTDGGWFSEFHIPAIIYGP- 403
Cdd:cd03891 275 ---GLDYDLEWklSGEPFLTKPGKL------------VDAVSAAIKEVTGITPELSTSGGTSDARFIASYGCPVVEFGLv 339
|
410 420 430
....*....|....*....|....*....|
gi 1586368115 404 -GTleeAHSVNEKVEVEQLIEFTKVITAFI 432
Cdd:cd03891 340 nAT---IHKVNERVSVADLEKLTDIYERIL 366
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
35-432 |
1.01e-21 |
|
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: 95.74 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 35 LLELTKTLIRFETPAPPARNTNEAQEFVADFLRKRNFSIDKWDVYPNDPNVVGVKKGTESgtyKSLIINGHMD-VAEVSi 113
Cdd:cd03885 1 MLDLLERLVNIESGTYDKEGVDRVAELLAEELEALGFTVERRPLGEFGDHLIATFKGTGG---KRVLLIGHMDtVFPEG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 114 deaweTNPFEPF-IKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGEAGTLQCCKR-GYDADF 191
Cdd:cd03885 77 -----TLAFRPFtVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSRELIEEeAKGADY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 192 AVVVDTSNLHmqgqGGVITG-------WITVKSprtfhdatrrQMIHAGGRLF-GASAIEKMMKIVQSLQELerhwavmk 263
Cdd:cd03885 152 VLVFEPARAD----GNLVTArkgigrfRLTVKG----------RAAHAGNAPEkGRSAIYELAHQVLALHAL-------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 264 tyEGYPSGtTTINPAVIEGGRHAAFIADECRLWITVHFYPNEthEQiiEEIEAYIRKVAAADPwlsenppqfkWGGESMI 343
Cdd:cd03885 210 --TDPEKG-TTVNVGVISGGTRVNVVPDHAEAQVDVRFATAE--EA--DRVEEALRAIVATTL----------VPGTSVE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 344 VDRGEIFPSLEvdsEHVAVKTLSAVHESILSKNAI-LDMSAT--VTDGGWFSEFHIPAI----IYGPGtleeAHSVNEKV 416
Cdd:cd03885 273 LTGGLNRPPME---ETPASRRLLARAQEIAAELGLtLDWEATggGSDANFTAALGVPTLdglgPVGGG----AHTEDEYL 345
|
410
....*....|....*.
gi 1586368115 417 EVEQLIEFTKVITAFI 432
Cdd:cd03885 346 ELDSLVPRIKLLARLL 361
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
36-432 |
2.66e-21 |
|
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: 95.50 E-value: 2.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 36 LELTKTLIRFETPAPPARNTNEAQ--EFVADFLRKRNFSIDKWDV--YPNDPNVVGVKKGTESGTyKSLIINGHMDVAEV 111
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTGSETRaaEVLAARLAEAGIQTEIFVVesHPGRANLVARIGGTDPSA-GPLLLLGHIDVVPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 112 SIDEaWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEV-GEAGTLQCCKRGYD-- 188
Cdd:cd05675 80 DASD-WSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAgGENGAKWLVDNHPElf 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 189 --ADFAV---------VVDTSNLHMQGQGGVITGWITVKS-------------------------------PRTFHDAT- 225
Cdd:cd05675 159 dgATFALneggggslpVGKGRRLYPIQVAEKGIAWMKLTVrgraghgsrptddnaitrlaealrrlgahnfPVRLTDETa 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 226 -RRQMIHAGGRLFGA---SAIEKMMKIVQSLQELERHWAVMKtyegypsgTTTINPAVIEGGRHAAFIADECRLWITVHF 301
Cdd:cd05675 239 yFAQMAELAGGEGGAlmlTAVPVLDPALAKLGPSAPLLNAML--------RNTASPTMLDAGYATNVLPGRATAEVDCRI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 302 YPnethEQIIEEIEAYIRKvAAADP-----WLSENPPqfkwggesmivdrgeifPSLEVDSEHVAVKTlSAVHESILSKN 376
Cdd:cd05675 311 LP----GQSEEEVLDTLDK-LLGDPdvsveAVHLEPA-----------------TESPLDSPLVDAME-AAVQAVDPGAP 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586368115 377 AILDMSATVTDGGWFSEFHIPAiiYG------PGTLEE---AHSVNEKVEVEQLIEFTKVITAFI 432
Cdd:cd05675 368 VVPYMSPGGTDAKYFRRLGIPG--YGfaplflPPELDYtglFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
35-423 |
1.91e-20 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 91.95 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 35 LLELTKTLIRFETPAPparNTNEAQEFVADFLRKRNFSIDKWDVYPNDPNVVGVKKGTESGTykSLIINGHMDVaevsid 114
Cdd:cd05652 1 LLSLHKSLVEIPSISG---NEAAVGDFLAEYLESLGFTVEKQPVENKDRFNVYAYPGSSRQP--RVLLTSHIDT------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 115 eaweTNPFEPF---IKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGEAGTLQCCKRGYDADF 191
Cdd:cd05652 70 ----VPPFIPYsisDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGDGMKAFNDLGLNTWD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 192 AVVVD--TSNLHMQGQGGVITGWITVKSprtfhdatrrQMIHAGGRLFGASAIEKMMKIVQSLQELerHWAVMKTYegyp 269
Cdd:cd05652 146 AVIFGepTELKLASGHKGMLGFKLTAKG----------KAGHSGYPWLGISAIEILVEALVKLIDA--DLPSSELL---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 270 sGTTTINPAVIEGGRHAAFIADEC--RLWITVHFYPNETHEQIIEEI-EAYIRKVAAADPWLSENPPQfkwggesmivdr 346
Cdd:cd05652 210 -GPTTLNIGRISGGVAANVVPAAAeaSVAIRLAAGPPEVKDIVKEAVaGILTDTEDIEVTFTSGYGPV------------ 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 347 geifpSLEVDSE-----HVAVKT----LSAVHESILsknaildmsatvtdggwfsefhipaiiYGPGTLEEAHSVNEKVE 417
Cdd:cd05652 277 -----DLDCDVDgfetdVVAYGTdipyLKGDHKRYL---------------------------YGPGSILVAHGPDEAIT 324
|
....*.
gi 1586368115 418 VEQLIE 423
Cdd:cd05652 325 VSELEE 330
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
26-434 |
5.44e-19 |
|
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: 88.84 E-value: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 26 KQIDSRKEELLELTKTLIRFET-------PAPPARNTNEAQEFVADFLRKRNFsidkwDVYpNDPNVVGVkkgTESGTYK 98
Cdd:cd03888 1 EEIDKYKDEILEDLKELVAIPSvrdeateGAPFGEGPRKALDKFLDLAKRLGF-----KTK-NIDNYAGY---AEYGEGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 99 SLI-INGHMDVaeVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGN--LIFQS------- 168
Cdd:cd03888 72 EVLgILGHLDV--VPAGEGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKirLIFGTdeetgwk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 169 ------------------------VIGEE-------------------------------------VGEAGTLQC----C 183
Cdd:cd03888 150 ciehyfeheeypdfgftpdaefpvINGEKgivtvdltfkidddkgyrlisikggeatnmvpdkaeaVIPGKDKEElalsA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 184 KRGYDADFAVVVDTSNLHMQGQGGvitgwitvksprtfHDATRRQMIHAGGRLFGA----SAIEKMMKIVQSLQELERHW 259
Cdd:cd03888 230 ATDLKGNIEIDDGGVELTVTGKSA--------------HASAPEKGVNAITLLAKFlaelNKDGNDKDFIKFLAKNLHED 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 260 AVMKT----YEGYPSGTTTINPAVIEggrhaaFIADECRLWITVHfYPNETH-EQIIEEIEAYIrkvaaadpwlsenppq 334
Cdd:cd03888 296 YNGKKlginFEDEVMGELTLNPGIIT------LDDGKLELGLNVR-YPVGTSaEDIIKQIEEAL---------------- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 335 FKWGGEsmiVDRGEIFPSLEVDSEHVAVKTLSAVHESILSKNAildmSATVTDGGWFSEFHIPAIIYG---PGTLEEAHS 411
Cdd:cd03888 353 EKYGVE---VEGHKHQKPLYVPKDSPLVKTLLKVYEEQTGKEG----EPVAIGGGTYARELPNGVAFGpefPGQKDTMHQ 425
|
490 500
....*....|....*....|...
gi 1586368115 412 VNEKVEVEQLIEFTKVITAFIYE 434
Cdd:cd03888 426 ANEFIPIDDLIKALAIYAEAIYE 448
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
32-432 |
8.17e-19 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 87.41 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 32 KEELLELTKTLIRFETPApparnTNEAQ--EFVADFLRKRNFsidkwDVYPND-PNVVGVKKGTESGTYKSLIINGHMDV 108
Cdd:COG2195 2 PERLLERFLEYVKIPTPS-----DHEEAlaDYLVEELKELGL-----EVEEDEaGNVIATLPATPGYNVPTIGLQAHMDT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 109 AEVSideawETNPFEPFIKDDWLVGRGA----ADMKGGLAGSLFAIQLLEEAGIELpGNL--IFqsVIGEEVGEAGTlqc 182
Cdd:COG2195 72 VPQF-----PGDGIKPQIDGGLITADGTttlgADDKAGVAAILAALEYLKEPEIPH-GPIevLF--TPDEEIGLRGA--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 183 ckRGYD-----ADFAVVVDTSNLhmqgqGGVITG-------WITVKSprtfhdatrrQMIHAG----GRlfgASAIEKMM 246
Cdd:COG2195 141 --KALDvsklgADFAYTLDGGEE-----GELEYEcagaadaKITIKG----------KGGHSGdakeKM---INAIKLAA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 247 KIVQSLQELERhwavmktyegypSGTTTINPAVIEGG--RHAafIADECRLWITVH-FYPNEThEQIIEEIEAYIRKVAA 323
Cdd:COG2195 201 RFLAALPLGRI------------PEETEGNEGFIHGGsaTNA--IPREAEAVYIIRdHDREKL-EARKAELEEAFEEENA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 324 adpwlsenppqfKWGGESMIVDRGEIFPSLEVDSEHVAVKTLSAVHESilsknaiLDMSATV------TDGGWFSEFHIP 397
Cdd:COG2195 266 ------------KYGVGVVEVEIEDQYPNWKPEPDSPIVDLAKEAYEE-------LGIEPKIkpirggLDGGILSFKGLP 326
|
410 420 430
....*....|....*....|....*....|....*
gi 1586368115 398 AIIYGPGtLEEAHSVNEKVEVEQLIEFTKVITAFI 432
Cdd:COG2195 327 TPNLGPG-GHNFHSPDERVSIESMEKAWELLVEIL 360
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
36-421 |
1.35e-18 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 87.06 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 36 LELTKTLIRFE--TPapparNTNEAQEFVADFLRKRNFSIDKwdvypndPNVVGVK-----KGTESgtyKSLIINGHMDV 108
Cdd:PRK13009 5 LELAQDLIRRPsvTP-----DDAGCQDLLAERLEALGFTCER-------MDFGDVKnlwarRGTEG---PHLCFAGHTDV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 109 AEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFqsVI-GEEVGEA--GT------ 179
Cdd:PRK13009 70 VPPGDLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAF--LItSDEEGPAinGTvkvlew 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 180 LQccKRGYDADFAVVVD-TSNLHM-----QGQGGVITGWITVKSprtfhdatrRQmihaggrlfGASA--------IEKM 245
Cdd:PRK13009 148 LK--ARGEKIDYCIVGEpTSTERLgdvikNGRRGSLTGKLTVKG---------VQ---------GHVAyphladnpIHLA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 246 MKIvqsLQEL-ERHWAvmktyEGY----PS---------GTTTINpaVIEGgrhaafiadECRLWITVHFYPNETHEQII 311
Cdd:PRK13009 208 APA---LAELaATEWD-----EGNeffpPTslqitnidaGTGATN--VIPG---------ELEAQFNFRFSTEHTAESLK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 312 EEIEAYIRKVAAadpwlsenPPQFKW--GGESMIVDRGEIfpslevdsehvaVKTLSAVHESILSKNAILDMSATVTDGG 389
Cdd:PRK13009 269 ARVEAILDKHGL--------DYTLEWtlSGEPFLTPPGKL------------VDAVVAAIEAVTGITPELSTSGGTSDAR 328
|
410 420 430
....*....|....*....|....*....|....
gi 1586368115 390 WFSEFHIPAIIYGP--GTleeAHSVNEKVEVEQL 421
Cdd:PRK13009 329 FIADYGAQVVEFGPvnAT---IHKVNECVSVADL 359
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
24-434 |
1.57e-18 |
|
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: 87.66 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 24 LLKQIDSRKEELLELTKTLIRFET-PAPPAR--NTNEAQEFVADFLRKRNFSIDKWDVYPND---------PNVVGVKKG 91
Cdd:cd05676 1 VFKYIDEHQDEFIERLREAVAIQSvSADPEKrpELIRMMEWAAERLEKLGFKVELVDIGTQTlpdgeelplPPVLLGRLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 92 tESGTYKSLIINGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNL--IFQSV 169
Cdd:cd05676 81 -SDPSKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLkfCFEGM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 170 igEEVGEAG---TLQCCKRGY--DADFAVVVDTSNLH------MQGQGGVITGWITVKSPrtfhdatrRQMIHAGgrLFG 238
Cdd:cd05676 160 --EESGSEGldeLIEARKDTFfsDVDYVCISDNYWLGkkkpclTYGLRGICYFFIEVEGP--------NKDLHSG--VFG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 239 ASAIEKMMKIVQSLQEL--------------------ERHWAV-------MKTYEGYPSGTTTIN-------------PA 278
Cdd:cd05676 228 GSVHEPMTDLIALMSSLvdsdgkilipgiydavapltEEEWELyekidfdMEEYREDIGVRRLLYdnkeellmhrwryPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 279 V----IEGgrhaAFIADECRLWI-----------TVhfyPNETHEQIIEEIEAYIRKVAA---------------ADPWL 328
Cdd:cd05676 308 LsihgIEG----AFSGPGAKTVIpakvigkfsirLV---PNMDPEVVEKQVTDYLEKVFAelkspnklkvymghgGKPWV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 329 SE-NPPQFKWGGESMivdrGEIF---PSL--EVDSEHVAVKTLSAVHESILsknaILDMSAtVTDGgwfsefhipaiiyg 402
Cdd:cd05676 381 ADpDHPNYKAARKAT----KRVFgvePDLtrEGGSIPITLTFQEATGKNVM----LLPIGA-ADDG-------------- 437
|
490 500 510
....*....|....*....|....*....|..
gi 1586368115 403 pgtleeAHSVNEKVEVEQLIEFTKVITAFIYE 434
Cdd:cd05676 438 ------AHSQNEKINRRNYIEGTKLLAAYFHE 463
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
36-175 |
1.52e-17 |
|
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: 84.31 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 36 LELTKTLIRFETPAPPARNTNEAQEFVADFLRKRNFSIDKWDVYPNdPNVVGVKKgteSGTYKSLIINGHMDVAEVSIDE 115
Cdd:cd05681 2 LEDLRDLLKIPSVSAQGRGIPETADFLKEFLRRLGAEVEIFETDGN-PIVYAEFN---SGDAKTLLFYNHYDVQPAEPLE 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 116 AWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVG 175
Cdd:cd05681 78 LWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVG 137
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
84-242 |
2.74e-17 |
|
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: 79.78 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 84 NVVGVKKGTESGtyKSLIINGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGN 163
Cdd:cd18669 1 NVIARYGGGGGG--KRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 164 LIFQSVIGEEVG-EAGTLQCCK----RGYDADFAVVVDTSNLHMQGQGGVITGWITVKS--PRTFHDATRRQMIHAG--G 234
Cdd:cd18669 79 VVVAFTPDEEVGsGAGKGLLSKdaleEDLKVDYLFVGDATPAPQKGVGIRTPLVDALSEaaRKVFGKPQHAEGTGGGtdG 158
|
....*...
gi 1586368115 235 RLFGASAI 242
Cdd:cd18669 159 RYLQELGI 166
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
204-326 |
3.49e-17 |
|
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: 77.00 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 204 GQGGVITGWITVKSprtfHDAtrrqmiHAGGRLFGASAIEKMMKIVQSLQELERHWavmktyeGYPSGTTTINPAVIEGG 283
Cdd:pfam07687 2 GHKGLAGGHLTVKG----KAG------HSGAPGKGVNAIKLLARLLAELPAEYGDI-------GFDFPRTTLNITGIEGG 64
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1586368115 284 RHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAADP 326
Cdd:pfam07687 65 TATNVIPAEAEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
33-421 |
6.97e-17 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 81.79 E-value: 6.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 33 EELLELTKTLIRFETPAPPaRNTNEAQEFvaDFLRKR--NFSIDKWDVYPNDPNVVGVKkgtesGTYKSLIiNGHMDVAE 110
Cdd:PRK08737 6 ESTLDHLQALVSFDTRNPP-RAITTGGIF--DYLRAQlpGFQVEVIDHGAGAVSLYAVR-----GTPKYLF-NVHLDTVP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 111 VSidEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIqlleEAGiELPGNLIFQSvigEEvgEAGTLQCCK----RG 186
Cdd:PRK08737 77 DS--PHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAA----NAG-DGDAAFLFSS---DE--EANDPRCVAaflaRG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 187 YDADFAVVVD-TSNLHMQGQGGVITGWITVkSPRTFHDATRRQMihaggrlfGASAIEKMMKIVQslQELERHWAVMKTY 265
Cdd:PRK08737 145 IPYEAVLVAEpTMSEAVLAHRGISSVLMRF-AGRAGHASGKQDP--------SASALHQAMRWGG--QALDHVESLAHAR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 266 EGYPSGTTtINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYirkvaaADPWLSENPPQFkwggesmivd 345
Cdd:PRK08737 214 FGGLTGLR-FNIGRVEGGIKANMIAPAAELRFGFRPLPSMDVDGLLATFAGF------AEPAAATFEETF---------- 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1586368115 346 RGEIFPSleVDSEHVAVKTLSAVHesiLSKNAILDMSATV---TDGGWFSEFHIPAIIYGPGTLEEAHSVNEKVEVEQL 421
Cdd:PRK08737 277 RGPSLPS--GDIARAEERRLAARD---VADALDLPIGNAVdfwTEASLFSAAGYTALVYGPGDIAQAHTADEFVTLDQL 350
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
84-231 |
6.84e-16 |
|
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: 75.92 E-value: 6.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 84 NVVGVKKGTESGtyKSLIINGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGN 163
Cdd:cd03873 1 NLIARLGGGEGG--KSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGT 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586368115 164 LIFQSVIGEEVG-----EAGTLQCCKRGYDADFAVVVDTSNLHMQGQGGVITGwitvKSPRTFHDATRRQMIH 231
Cdd:cd03873 79 IVVAFTADEEVGsgggkGLLSKFLLAEDLKVDAAFVIDATAGPILQKGVVIRN----PLVDALRKAAREVGGK 147
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
49-435 |
1.00e-15 |
|
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: 78.89 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 49 APPARNT--NEAQEFVADFLRKRNFsiDKWDVYPND--PNVVGVKKGTESGtyKSLIINGHMDVAEVSIDEAWETNPFEP 124
Cdd:cd05680 15 ADPAHKGdvRRAAEWLADKLTEAGF--EHTEVLPTGghPLVYAEWLGAPGA--PTVLVYGHYDVQPPDPLELWTSPPFEP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 125 FIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGEAGT---LQCCKRGYDADFAVVVDTSNLH 201
Cdd:cd05680 91 VVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIGSPSLpafLEENAERLAADVVLVSDTSMWS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 202 MQ------GQGGVITGWITVKSPRtfHDatrrqmIHAGgrLFG---ASAIEKMMKIVQSLQELERHWAVMKTYEGY---- 268
Cdd:cd05680 171 PDtptityGLRGLAYLEISVTGPN--RD------LHSG--SYGgavPNPANALARLLASLHDEDGRVAIPGFYDDVrplt 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 269 ----------------------------PSGTTT-----INPAV----IEGGRHAA----FIADECRLWITVHFYPNETH 307
Cdd:cd05680 241 daereawaalpfdeaafkaslgvpalggEAGYTTlerlwARPTLdvngIWGGYQGEgsktVIPSKAHAKISMRLVPGQDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 308 EQIIEEIEAYIRKVAaadpwlsenPPQFKWGgesmiVDRGEIFPSLEVDSEHVAVKTLSAVHESILSKNAILdmsatVTD 387
Cdd:cd05680 321 DAIADLLEAHLRAHA---------PPGVTLS-----VKPLHGGRPYLVPTDHPALQAAERALEEAFGKPPVF-----VRE 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1586368115 388 GG------WFSE-FHIPAIIYGPGTLEEA-HSVNEKVEVEQlieFTKVITAFIYEW 435
Cdd:cd05680 382 GGsipivaLFEKvLGIPTVLMGFGLPDDAiHAPNEKFRLEC---FHKGIEAIAHLL 434
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
33-428 |
1.31e-15 |
|
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: 77.98 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 33 EELLELTKTLIRFETPAPPARNTNEAqEFVADFLRKRNFSIDKWDVypndPNVVGVKKGTESGTY-----------KSLI 101
Cdd:cd02697 3 DEEVRFLQKLVRVPTDTPPGNNAPHA-ERTAALLQGFGFEAERHPV----PEAEVRAYGMESITNlivrrrygdggRTVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 102 INGHMDVaeVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEV-GEAGTL 180
Cdd:cd02697 78 LNAHGDV--VPPGDGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFgGELGPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 181 QCCKRGY-DADFAVVVDTSNLHMQGQGGVITGWITVksprtfhdatRRQMIHAGGRLFGASAIEKMMKIVQSLQELERHW 259
Cdd:cd02697 156 WLLRQGLtKPDLLIAAGFSYEVVTAHNGCLQMEVTV----------HGKQAHAAIPDTGVDALQGAVAILNALYALNAQY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 260 -AVMKTYEGYPSgtTTINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAADPwlsenppqfkwg 338
Cdd:cd02697 226 rQVSSQVEGITH--PYLNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAASMP------------ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 339 GESMIVDRGEIFPSLEVDSEHVAVKTLSAVHESILSKNAILDMSATV-TDGGWFSEFHIPAIIY--GPGTLEEAHS--VN 413
Cdd:cd02697 292 GISVDIRRLLLANSMRPLPGNAPLVEAIQTHGEAVFGEPVPAMGTPLyTDVRLYAEAGIPGVIYgaGPRTVLESHAkrAD 371
|
410
....*....|....*
gi 1586368115 414 EKVEVEQLIEFTKVI 428
Cdd:cd02697 372 ERLQLEDLRRATKVI 386
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
34-423 |
5.01e-14 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 72.73 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 34 ELLELTKTLIrfETPAPpARNTNEAQEFVADFLRKRNFSIDKwdvypNDPNVVGVKKGTESGTYkSLIINGHMDVaeVSI 113
Cdd:cd05651 1 EAIELLKSLI--ATPSF-SREEHKTADLIENYLEQKGIPFKR-----KGNNVWAENGHFDEGKP-TLLLNSHHDT--VKP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 114 DEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFA-IQLLEEAgiELPGNLIFQSVIGEEVGEAGTLQC--CKRGyDAD 190
Cdd:cd05651 70 NAGWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATfLHLYSEG--PLNYNLIYAASAEEEISGKNGIESllPHLP-PLD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 191 FAVVVDTSNLHMQ-GQGGVITGWITVKSpRTFHDAtrrqmihaggRLFGASAIEKMMKIVQSLQELErhWAVMKTYEGYP 269
Cdd:cd05651 147 LAIVGEPTEMQPAiAEKGLLVLDCTARG-KAGHAA----------RNEGDNAIYKALDDIQWLRDFR--FDKVSPLLGPV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 270 SGTTTInpavIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRkvaaadpwlsenppqfkwggeSMIVDRGEI 349
Cdd:cd05651 214 KMTVTQ----INAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLK---------------------SEIKPRSFR 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586368115 350 FPSLEVDSEHVAVKTLSAVHESILSknaildmSATVTDggwFSEFHIPAIIYGPGTLEEAHSVNEKVEVEQLIE 423
Cdd:cd05651 269 LNSSAIPPDHPIVQAAIAAGRTPFG-------SPTLSD---QALMPFPSVKIGPGDSSRSHTADEFIELSEIEE 332
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
31-178 |
8.00e-14 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 73.35 E-value: 8.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 31 RKEELLELTKTLIRFetpapPARNTNEAQEFVADFLRKRNFSIDKWDVYP---------NDP----NVVGVKKGTESGTy 97
Cdd:COG4187 6 TKEQLEELLCELVSI-----PSVTGTEGEKEVAEFIYEKLSELPYFQENPehlglhplpDDPlgrkNVTALVKGKGESK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 98 KSLIINGHMDVaeVSID----------------EAWETNPFEPFIKDD-----WLVGRGAADMKGGLAGSLfaiQLLEEA 156
Cdd:COG4187 80 KTVILISHFDV--VDVEdygslkplafdpeeltEALKEIKLPEDVRKDlesgeWLFGRGTMDMKAGLALHL---ALLEEA 154
|
170 180
....*....|....*....|....
gi 1586368115 157 GI--ELPGNLIFQSVIGEEVGEAG 178
Cdd:COG4187 155 SEneEFPGNLLLLAVPDEEVNSAG 178
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
33-431 |
9.19e-14 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 72.10 E-value: 9.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 33 EELLELTKTLIRFETPAPparNTNEAQEFVADFLRKRNFSidkWDVYPNDP--NVVgVKKGTEsgtyksLIINGHMDVAE 110
Cdd:PRK08652 2 ERAKELLKQLVKIPSPSG---QEDEIALHIMEFLESLGYD---VHIESDGEviNIV-VNSKAE------LFVEVHYDTVP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 111 VSIdeawetnpfEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSviGEEVGEAGTLQCCKRgYDAD 190
Cdd:PRK08652 69 VRA---------EFFVDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVS--DEEEGGRGSALFAER-YRPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 191 FAVVVDTSNLHMQ-GQGGVITGWITVKSPRTfhdatrrqmiHAGGRLFGASAIEKMMKIVQSLQELERhwAVMKTYEGYp 269
Cdd:PRK08652 137 MAIVLEPTDLKVAiAHYGNLEAYVEVKGKPS----------HGACPESGVNAIEKAFEMLEKLKELLK--ALGKYFDPH- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 270 sgtttINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIeayirkvaaaDPWLSENPPQFKWGgesmivdrgEI 349
Cdd:PRK08652 204 -----IGIQEIIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEI----------DPILDEYTVKYEYT---------EI 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 350 FPSLEVDSEHVAVKTLSAVHesilsKNAILDMSATV----TDGGWFSEFHIPAIIYGPGTLEEAHSVNEKVEVEQLIEFT 425
Cdd:PRK08652 260 WDGFELDEDEEIVQLLEKAM-----KEVGLEPEFTVmrswTDAINFRYNGTKTVVWGPGELDLCHTKFERIDVREVEKAK 334
|
....*.
gi 1586368115 426 KVITAF 431
Cdd:PRK08652 335 EFLKAL 340
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
29-175 |
1.02e-13 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 72.19 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 29 DSRKEELLELTKTLIRFetPAPPARNTNEAQEFVADFLRK--RNFSIDKWDVY--PND-------PNVVGVKKGTEsgTY 97
Cdd:PRK13983 1 DELRDEMIELLSELIAI--PAVNPDFGGEGEKEKAEYLESllKEYGFDEVERYdaPDPrviegvrPNIVAKIPGGD--GK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586368115 98 KSLIINGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVG 175
Cdd:PRK13983 77 RTLWIISHMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETG 154
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
33-175 |
4.28e-13 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349901 [Multi-domain] Cd Length: 389 Bit Score: 70.56 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 33 EELLELTKTLIRFETPAPPARNTNEAQ--EFVADFLRKRNFS-IDKWDVyPND-----PNVVGVKKGtesGTYKSLIING 104
Cdd:cd05650 1 EEIIELERDLIRIPAVNPESGGEGEKEkaDYLEKKLREYGFYtLERYDA-PDErgiirPNIVAKIPG---GNDKTLWIIS 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586368115 105 HMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVG 175
Cdd:cd05650 77 HLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDG 147
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
32-160 |
1.12e-12 |
|
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: 69.33 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 32 KEELLELTKTLIRFETPAPPARNTNE---------AQEFVADFLRKRNFSIDKWDvypndpNVVG---VKKGTESgtyks 99
Cdd:TIGR01887 1 KDEILEDLKELIAIDSVEDLEKAKEGapfgegprkALDKFLEIAKRDGFTTENVD------NYAGyieYGQGEEV----- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1586368115 100 LIINGHMDVaeVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIEL 160
Cdd:TIGR01887 70 LGILGHLDV--VPAGDGWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKL 128
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
26-199 |
1.94e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 68.78 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 26 KQIDSRKEELleltKTLIRFETPAP---PARNTNEAQEFVADFLRKRNFsiDKWDVYPND--PNVVGVKKGTESgtYKSL 100
Cdd:PRK07907 15 ELLPRVRADL----EELVRIPSVAAdpfRREEVARSAEWVADLLREAGF--DDVRVVSADgaPAVIGTRPAPPG--APTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 101 IINGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLeeaGIELPGNL-IFqsVIGEEvgEAGT 179
Cdd:PRK07907 87 LLYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRAL---GGDLPVGVtVF--VEGEE--EMGS 159
|
170 180
....*....|....*....|....*.
gi 1586368115 180 ------LQCCKRGYDADFAVVVDTSN 199
Cdd:PRK07907 160 pslerlLAEHPDLLAADVIVIADSGN 185
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
36-144 |
1.94e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 68.87 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 36 LELTKTLIRFETPAPPARNTnEAQEFVADFLRKRNFS---IDKWDVYPNDPNVVGVKKGTesGTYKSLIINGHMDVAEvS 112
Cdd:PRK09133 40 RDLYKELIEINTTASTGSTT-PAAEAMAARLKAAGFAdadIEVTGPYPRKGNLVARLRGT--DPKKPILLLAHMDVVE-A 115
|
90 100 110
....*....|....*....|....*....|..
gi 1586368115 113 IDEAWETNPFEPFIKDDWLVGRGAADMKGGLA 144
Cdd:PRK09133 116 KREDWTRDPFKLVEENGYFYGRGTSDDKADAA 147
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
84-434 |
2.58e-12 |
|
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349932 [Multi-domain] Cd Length: 368 Bit Score: 67.86 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 84 NVVGVKKGTESGTYKsLIINGHMDVAEVSIdeawetNPFEPFIKDDWLVGRG----AADMKGGLAGSLFAIQLLEEAGIE 159
Cdd:cd05683 55 NLICTLKADKEEVPK-ILFTSHMDTVTPGI------NVKPPQIADGYIYSDGttilGADDKAGIAAILEAIRVIKEKNIP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 160 lPGNLIFQSVIGEEVGEAGTLQCCKRGYDADFAVVVDtsnlhmqgqGGVITGWITVKSPR--TFHDATRRQMIHAGGR-- 235
Cdd:cd05683 128 -HGQIQFVITVGEESGLVGAKALDPELIDADYGYALD---------SEGDVGTIIVGAPTqdKINAKIYGKTAHAGTSpe 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 236 ------LFGASAIEKmMKIVQSLQElerhwavmktyegypsgtTTINPAVIEGGRHAAFIADECRLWitvhfypNETHEQ 309
Cdd:cd05683 198 kgisaiNIAAKAISN-MKLGRIDEE------------------TTANIGKFQGGTATNIVTDEVNIE-------AEARSL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 310 IIEEIEAYIRKVAAAdpwLSENPPQFkwgGESMIVDRGEIFPSLEVDS-EHV---AVKTLSAvhesiLSKNAILDMSATV 385
Cdd:cd05683 252 DEEKLDAQVKHMKET---FETTAKEK---GAHAEVEVETSYPGFKINEdEEVvklAKRAANN-----LGLEINTTYSGGG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1586368115 386 TDGGWFSEFHIPAIIYGPGtLEEAHSVNEKVEVEQLIEFTKVITAFIYE 434
Cdd:cd05683 321 SDANIINGLGIPTVNLGIG-YENIHTTNERIPIEDLYDTAVLVVEIIKE 368
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
34-175 |
4.43e-12 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 67.49 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 34 ELLELTKTLIRFETPAPPARN---TNEAQEFVADFLRkrNFSIDKwDVYPND--PNVVGVkkgTESGTYKSLIInGHMDV 108
Cdd:PRK08554 2 DVLELLSSLVSFETVNDPSKGikpSKECPKFIKDTLE--SWGIES-ELIEKDgyYAVYGE---IGEGKPKLLFM-AHFDV 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586368115 109 AEVSIDEaWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAgiELPGNLIFQSVIGEEVG 175
Cdd:PRK08554 75 VPVNPEE-WNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKE--PLNGKVIFAFTGDEEIG 138
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
33-434 |
6.95e-12 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 66.22 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 33 EELLELTKTLIRFETPAppaRNTNEAQEFVADFLRKRNfsidkWDVYPNDP-NVVGVKKGTESGtyksLIINGHMDvaev 111
Cdd:cd05653 1 QDAVELLLDLLSIYSPS---GEEARAAKFLEEIMKELG-----LEAWVDEAgNAVGGAGSGPPD----VLLLGHID---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 112 sideaweTNP--FEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEagiELPGNLIFQSVIGEEVGEAGTLQCCKRGYDA 189
Cdd:cd05653 65 -------TVPgeIPVRVEGGVLYGRGAVDAKGPLAAMILAASALNE---ELGARVVVAGLVDEEGSSKGARELVRRGPRP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 190 DFAVVVDTSNLH--MQGQGGVITGWITVKSpRTFHDATRrqmihaggrlfGASAIEKMMKIVQSLQELERHWAVmkTYEG 267
Cdd:cd05653 135 DYIIIGEPSGWDgiTLGYRGSLLVKIRCEG-RSGHSSSP-----------ERNAAEDLIKKWLEVKKWAEGYNV--GGRD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 268 YPSGTTTInpavIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRkvaaadpwlsenPPQFKWGGESmivdrg 347
Cdd:cd05653 201 FDSVVPTL----IKGGESSNGLPQRAEATIDLRLPPRLSPEEAIALATALLP------------TCELEFIDDT------ 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 348 eifPSLEVDSEHVAVKTLSA------VHESILSKNAILDMSATVtdggwfSEFHIPAIIYGPGTLEEAHSVNEKVEVEQL 421
Cdd:cd05653 259 ---EPVKVSKNNPLARAFRRairkqgGKPRLKRKTGTSDMNVLA------PLWTVPIVAYGPGDSTLDHTPNEHIELAEI 329
|
410
....*....|...
gi 1586368115 422 IEFTKVITAFIYE 434
Cdd:cd05653 330 ERAAAVLKGALEE 342
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
98-434 |
1.79e-11 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 65.54 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 98 KSLIINGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGEA 177
Cdd:PRK08201 80 PTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEEIGSP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 178 GTLQCCKRGYD---ADFAVVVDTSnLHMQGQGGVITGW-------ITVKSPRTfhDatrrqmIHAGgrLFGAS---AIEK 244
Cdd:PRK08201 160 NLDSFVEEEKDklaADVVLISDTT-LLGPGKPAICYGLrglaaleIDVRGAKG--D------LHSG--LYGGAvpnALHA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 245 MMKIVQSLQELERHWAVmktyEGYPSGTTTINPAVIEGGRHAAFIADEC-------------------RLW--------- 296
Cdd:PRK08201 229 LVQLLASLHDEHGTVAV----EGFYDGVRPLTPEEREEFAALGFDEEKLkrelgvdelfgeegytaleRTWarptlelng 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 297 ---------------------ITVHFYPNETHEQIIEEIEAYIRKvaaadpwlseNPPQfkwgGESMIVDRGEIFPSLEV 355
Cdd:PRK08201 305 vyggfqgegtktvipaeahakITCRLVPDQDPQEILDLIEAHLQA----------HTPA----GVRVTIRRFDKGPAFVA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 356 DSEHVAVKTLSAVHESIL-SKNAILDMSATVTDGGWFSE-FHIPAIIYGPGTLEEA-HSVNEKVEVEQLIEFTKVITAFI 432
Cdd:PRK08201 371 PIDHPAIQAAARAYEAVYgTEAAFTRMGGSIPVVETFSSqLHIPIVLMGFGLPSENfHAPNEHFHLENFDKGLRTLVEYW 450
|
..
gi 1586368115 433 YE 434
Cdd:PRK08201 451 HQ 452
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
40-173 |
2.80e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 65.16 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 40 KTLIRF---ETPAPPARNTNEAQEFVADFLRKR--NFSIDKwdvYPNDPNVVGvkkGTESGTYKSLIINGHMDVAEVSID 114
Cdd:PRK06446 6 YTLIEFlkkPSISATGEGIEETANYLKDTMEKLgiKANIER---TKGHPVVYG---EINVGAKKTLLIYNHYDVQPVDPL 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 115 EAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAI-QLLEEAGIELPGNLIFQsviGEE 173
Cdd:PRK06446 80 SEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIkHLIDKHKLNVNVKFLYE---GEE 136
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
43-424 |
1.07e-10 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 63.42 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 43 IRFETPAPPARNTNEAQEFVA--DFLRkrnfsidkwDVYPN-----DPNVVGVK------KGTESGTyKSLIINGHMDVa 109
Cdd:PRK08262 54 IRFRTISNRDRAEDDAAAFDAlhAHLE---------ESYPAvhaalEREVVGGHsllytwKGSDPSL-KPIVLMAHQDV- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 110 eVSIDEA----WETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGE------AGT 179
Cdd:PRK08262 123 -VPVAPGtegdWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVGGlgaraiAEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 180 LQccKRGYDADFavVVDtsnlhmqgQGGVIT-------------------GWITVK------------SPRtfHDATrrq 228
Cdd:PRK08262 202 LK--ERGVRLAF--VLD--------EGGAITegvlpgvkkpvaligvaekGYATLEltaratgghssmPPR--QTAI--- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 229 mihagGRLfgASAIEKM------MKIVQSLQELERH----------------W-------AVM-KTYEGYPSGTTTINPA 278
Cdd:PRK08262 265 -----GRL--ARALTRLednplpMRLRGPVAEMFDTlapemsfaqrvvlanlWlfeplllRVLaKSPETAAMLRTTTAPT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 279 VIEGGRHAAFIADECRLWITVHFYPNETheqiIEEIEAYIRKVAAADPWLSEnppqfkwggesmiVDRGEIFPSLEVDSE 358
Cdd:PRK08262 338 MLKGSPKDNVLPQRATATVNFRILPGDS----VESVLAHVRRAVADDRVEIE-------------VLGGNSEPSPVSSTD 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586368115 359 HVAVKTLSAVHESIlSKNAI----LDMSAtvTDGGWFSE-----FHIPAIIYGPGTLEEAHSVNEKVEVE---QLIEF 424
Cdd:PRK08262 401 SAAYKLLAATIREV-FPDVVvapyLVVGA--TDSRHYSGisdnvYRFSPLRLSPEDLARFHGTNERISVAnyaRMIRF 475
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
33-206 |
1.28e-10 |
|
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: 63.13 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 33 EELLELTKTLIRFetpapPARNTNEAQEFVADFLRK--------RNFSIDKWDVYPNDP----NVVGVKKGTESGTyKSL 100
Cdd:cd05654 1 ERLEQLLKSLVSW-----PSVTGTEGERSFADFLKEilkelpyfKENPSHVWQLLPPDDlgrrNVTALVKGKKPSK-RTI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 101 IINGHMDVaeVSIDE--AWETNPFEP------FI-----------KD----DWLVGRGAADMKGGLAgslFAIQLLEEAG 157
Cdd:cd05654 75 ILISHFDT--VGIEDygELKDIAFDPdeltkaFSeyveeldeevrEDllsgEWLFGRGTMDMKSGLA---VHLALLEQAS 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1586368115 158 I--ELPGNLIFQSVIGEEVGEAG------TLQCCKRGYDADFAVVVDTSNLHMQGQG 206
Cdd:cd05654 150 EdeDFDGNLLLMAVPDEEVNSRGmraavpALLELKKKHDLEYKLAINSEPIFPQYDG 206
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
64-283 |
2.05e-10 |
|
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: 62.29 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 64 DFLRKRNFSID----KWDVYPNDPNVVGVKKGTESgTYKSLIINGHMDVAEVsIDEAWETNPFEPFIKDD-WLVGRGAAD 138
Cdd:cd05646 28 EFLKRQADELGlpvrVIEVVPGKPVVVLTWEGSNP-ELPSILLNSHTDVVPV-FEEKWTHDPFSAHKDEDgNIYARGAQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 139 MKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGeagtlqcckrGYD--ADFAVVVDTSNLHM-----QGQ------ 205
Cdd:cd05646 106 MKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIG----------GHDgmEKFVKTEEFKKLNVgfaldEGLasptee 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 206 -----GGVITGWITVKSP-RTFHdatrrqmihaGGRLFGASAIEKMMKIVQSLQEL-ERHWAVMKTYEGYPSG-TTTINP 277
Cdd:cd05646 176 yrvfyGERSPWWVVITAPgTPGH----------GSKLLENTAGEKLRKVIESIMEFrESQKQRLKSNPNLTLGdVTTVNL 245
|
....*.
gi 1586368115 278 AVIEGG 283
Cdd:cd05646 246 TMLKGG 251
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
37-175 |
3.64e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 61.41 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 37 ELTKTLIRFETP---APPARNTNEAQEFVADFLRKRNFSIDKWDVYPNDPNVVGVKKGTESGTyKSLIINGHMDVaeVSI 113
Cdd:PRK07906 3 DLCSELIRIDTTntgDGTGKGEREAAEYVAEKLAEVGLEPTYLESAPGRANVVARLPGADPSR-PALLVHGHLDV--VPA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1586368115 114 DEA-WETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVG 175
Cdd:PRK07906 80 EAAdWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGRRPPRDLVFAFVADEEAG 142
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
26-160 |
4.51e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 61.25 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 26 KQIDSR-KEELLELTKTLIRF-------ETPAPPARNTNEAQEFVADFLRKRNFSIDKwdvypnDPNvvGVKKGTESGTY 97
Cdd:PRK07205 3 SYITEKvQDACVAAIKTLVSYpsvlnegENGTPFGQAIQDVLEATLDLCQGLGFKTYL------DPK--GYYGYAEIGQG 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1586368115 98 KSLI-INGHMDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIEL 160
Cdd:PRK07205 75 EELLaILCHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQF 138
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
100-438 |
6.49e-10 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 60.61 E-value: 6.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 100 LIINGHMDVaeVSIDEA-WETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPgnLIFQSVIGEEVGEAG 178
Cdd:PRK05111 74 LLLAGHTDT--VPFDEGrWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTKLKKP--LYILATADEETSMAG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 179 TLQCCKRG-YDADFAVVVDTSNL--------HMqGQGGVITGwitvkspRTFH--DATRrqmihaggrlfGASAIEKMMK 247
Cdd:PRK05111 150 ARAFAEATaIRPDCAIIGEPTSLkpvrahkgHM-SEAIRITG-------QSGHssDPAL-----------GVNAIELMHD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 248 IVQSLQELERHWAVMKTYEGYPSGTTTINPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAadpw 327
Cdd:PRK05111 211 VIGELLQLRDELQERYHNPAFTVPYPTLNLGHIHGGDAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSE---- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 328 lsenppqfKWGGesmIVDRGEIF---PSLEVDSEHVAVKtlsaVHESILSKNAildmsATV---TDGGWFSEFHIPAIIY 401
Cdd:PRK05111 287 --------RWPG---RITVAPLHppiPGYECPADHQLVR----VVEKLLGHKA-----EVVnycTEAPFIQQLGCPTLVL 346
|
330 340 350
....*....|....*....|....*....|....*..
gi 1586368115 402 GPGTLEEAHSVNEKVEVEQLIEFTKVITAFIYEWCHT 438
Cdd:PRK05111 347 GPGSIEQAHQPDEYLELSFIKPTRELLRQLIHHFCLH 383
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
26-160 |
9.26e-09 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 57.16 E-value: 9.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 26 KQIDSRKEELLELTKTLIRFET---------PAPPARNTNEAQEFVADFLRKRNFSIDKWDvypndpNVVGvkkGTESGT 96
Cdd:PRK07318 7 KEVEKRKDDLIEDLQELLRINSvrddskakeGAPFGPGPVKALEKFLEIAERDGFKTKNVD------NYAG---HIEYGE 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586368115 97 YKSLI-INGHMDVaeVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIEL 160
Cdd:PRK07318 78 GEEVLgILGHLDV--VPAGDGWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIKELGLPL 140
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
17-198 |
1.36e-08 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 56.83 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 17 MNPEISQLLKQIDSRKEELLELTKTLIRFET-PAPPARNTN--EAQEFVADFLRKRNFSIDKWDVyPNDPNVVGvKKGTE 93
Cdd:PRK09104 1 SMADLDPVLDHIDANLDASLERLFALLRIPSiSTDPAYAADcrKAADWLVADLASLGFEASVRDT-PGHPMVVA-HHEGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 94 SGTYKSLIINGHMDVAEVSIDEAWETNPFEPFIKDD-----WLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFqs 168
Cdd:PRK09104 79 TGDAPHVLFYGHYDVQPVDPLDLWESPPFEPRIKETpdgrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTI-- 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1586368115 169 VI-GEEvgEAGT------LQCCKRGYDADFAVVVDTS 198
Cdd:PRK09104 157 LFeGEE--ESGSpslvpfLEANAEELKADVALVCDTG 191
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
23-179 |
5.82e-08 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 54.64 E-value: 5.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 23 QLLKQIDSRKEELLELTKTLIRFETPAPPARNTNEAQEFVADFLRKRNFSIDKWDVYP-NDPNVVGVKKGTesGTYKSLI 101
Cdd:PRK06133 27 ELLAAAQQEQPAYLDTLKELVSIESGSGDAEGLKQVAALLAERLKALGAKVERAPTPPsAGDMVVATFKGT--GKRRIML 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1586368115 102 InGHMDVaeVSIDEAWETNPFEpfIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPGNLIFQSVIGEEVGEAGT 179
Cdd:PRK06133 105 I-AHMDT--VYLPGMLAKQPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGSPGS 177
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
98-435 |
1.50e-07 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 53.41 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 98 KSLIINGHMDVAEVSID--EAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGielpgnliFQ---SVI-- 170
Cdd:cd05674 70 KPLLLMAHQDVVPVNPEteDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRG--------FKprrTIIla 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 171 -G--EEV-GEAGTLQCC-----KRGYDAdFAVVVDTSNLHMQGQG-------------GVITGWITVKS----------- 217
Cdd:cd05674 142 fGhdEEVgGERGAGAIAellleRYGVDG-LAAILDEGGAVLEGVFlgvpfalpgvaekGYMDVEITVHTpgghssvppkh 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 218 ------------------PRTFHDATR-RQMIHAGGRlFGASAIEKMMKIVQSLQELERHWAVMKTYEGYPSG----TTT 274
Cdd:cd05674 221 tgigilseavaaleanpfPPKLTPGNPyYGMLQCLAE-HSPLPPRSLKSNLWLASPLLKALLASELLSTSPLTrallRTT 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 275 INPAVIEGGRHAAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAA-DPWLSENPPQFKWGGESMIVDRGEIF--- 350
Cdd:cd05674 300 QAVDIINGGVKINALPETATATVNHRIAPGSSVEEVLEHVKNLIADIAVKyGLGLSAFGGDVIYSTNGTKLLTSLLSpep 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 351 -PSLEVDSEhvAVKTLS-AVHESILSKNAILDMSATV----TDGGWFSE-----FHIPAIIYGPGTLEEAHSVNEKVEVE 419
Cdd:cd05674 380 sPVSSTSSP--VWQLLAgTIRQVFEQFGEDLVVAPGImtgnTDTRHYWNltkniYRFTPIRLNPEDLGRIHGVNERISID 457
|
410
....*....|....*.
gi 1586368115 420 QLIEftkvITAFIYEW 435
Cdd:cd05674 458 DYLE----TVAFYYQL 469
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
35-185 |
1.43e-06 |
|
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: 50.42 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 35 LLELTKTLIRFETPA--PPARNTNEAQEfVADFLRK--RNFSIDKWDVYP----NDPNVVGVKKGTESGTY-KSLIINGH 105
Cdd:cd05677 1 MLNTLSEFIAFQTVSqsPTTENAEDSRR-CAIFLRQlfKKLGATNCLLLPsgpgTNPIVLATFSGNSSDAKrKRILFYGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 106 MDVAEVSIDEAWETNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGiELPGNLIFQSVIGEEVGEAGTLQCCKR 185
Cdd:cd05677 80 YDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQEG-ELDNDVVFLIEGEEESGSPGFKEVLRK 158
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
100-326 |
1.10e-04 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 44.18 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 100 LIINGHMDVAeVSIDEAWETNPFepfIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAgiELPGNLIFQSVIG--EEVG-- 175
Cdd:PRK07338 95 VLLTGHMDTV-FPADHPFQTLSW---LDDGTLNGPGVADMKGGIVVMLAALLAFERS--PLADKLGYDVLINpdEEIGsp 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 176 -----------------------EAGTLQCCKRGydadfavvvdTSNLHMqgqggVITGwitvkspRTFHdatrrqmiha 232
Cdd:PRK07338 169 asapllaelargkhaaltyepalPDGTLAGARKG----------SGNFTI-----VVTG-------RAAH---------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 233 GGRLF--GASAIEKMMKIVQSLQELERHwavmktyegypSGTTTINPAVIEGGRHAAFIADECRLWITVHFyPNETHEQI 310
Cdd:PRK07338 217 AGRAFdeGRNAIVAAAELALALHALNGQ-----------RDGVTVNVAKIDGGGPLNVVPDNAVLRFNIRP-PTPEDAAW 284
|
250
....*....|....*..
gi 1586368115 311 IE-EIEAYIRKVAAADP 326
Cdd:PRK07338 285 AEaELKKLIAQVNQRHG 301
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
93-183 |
1.77e-04 |
|
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: 43.64 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 93 ESGTYKSLIINGHMDVAEvSIDEAWET--NPFEPFIKDDWLVGRGAADMKGGLAGSLFAI-QLLEEAGIELPGNLIFQSV 169
Cdd:cd05679 68 EDPSLPTLLIYGHGDVVP-GYEGRWRDgrDPWTVTVWGERWYGRGTADNKGQHSINMAALrQVLEARGGKLGFNVKFLIE 146
|
90
....*....|....
gi 1586368115 170 IGEEVGEAGTLQCC 183
Cdd:cd05679 147 MGEEMGSPGLRAFC 160
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
147-324 |
2.91e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 42.71 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 147 LFAIQLLEEAGIELPGN--LIFQSviGEEVGEaGTLQCCKRGY----DADFAVvvdtsnlHMQGQggVITGWITVKSPRT 220
Cdd:cd08019 97 LGAAKILNEIKDTIKGTvkLIFQP--AEEVGE-GAKQMIEEGVledvDAVFGI-------HLWSD--VPAGKISVEAGPR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 221 F---------------HDATRRQMIHAggrLFGASAIekmmkiVQSLQElerhwavMKTYEGYPSGTTTINPAVIEGGRH 285
Cdd:cd08019 165 MasadifkievkgkggHGSMPHQGIDA---VLAAASI------VMNLQS-------IVSREIDPLEPVVVTVGKLNSGTR 228
|
170 180 190
....*....|....*....|....*....|....*....
gi 1586368115 286 AAFIADECRLWITVHFYPNETHEQIIEEIEAYIRKVAAA 324
Cdd:cd08019 229 FNVIADEAKIEGTLRTFNPETREKTPEIIERIAKHTAAS 267
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
51-135 |
1.19e-03 |
|
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.
Pssm-ID: 349885 [Multi-domain] Cd Length: 474 Bit Score: 40.97 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 51 PARNTNEAQEFVADFLRKRNFsidkwDVYPNDP-NVVGVKKGTESG-TYKSLIINGHMDV-----AEVSIDeaWETNPFE 123
Cdd:cd03890 17 PSGNEKQISDFLVKFAKKLGL-----EVIQDEVgNVIIRKPATPGYeNAPPVILQGHMDMvceknADSEHD--FEKDPIK 89
|
90
....*....|..
gi 1586368115 124 PFIKDDWLVGRG 135
Cdd:cd03890 90 LRIDGDWLKATG 101
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
91-216 |
1.69e-03 |
|
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: 40.39 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 91 GTESGTyKSLIINGHMD-VAEVSideAWE--TNPFEPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIELPG-NLIF 166
Cdd:cd05682 68 GTEQDD-DTVLLYGHMDkQPPFT---GWDegLGPTKPVIRGDKLYGRGGADDGYAIFASLTAIKALQEQGIPHPRcVVLI 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1586368115 167 QSviGEEVGEAGTLQ----CCKRGYDADFAVVVD-----------TSNLHmqgqgGVITGWITVK 216
Cdd:cd05682 144 EA--CEESGSADLPFyldkLKERIGNVDLVVCLDsgcgnyeqlwlTTSLR-----GVLGGDLTVQ 201
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
100-294 |
2.02e-03 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 40.15 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 100 LIINGHMD-VAEVSIDEAWetnpfePFIKDDWLV-GRGAADMKGGLAGSLFAIQLLEEAGIE--LPGNLIFQSviGEEVG 175
Cdd:PRK07473 78 ILIAGHMDtVHPVGTLEKL------PWRREGNKCyGPGILDMKGGNYLALEAIRQLARAGITtpLPITVLFTP--DEEVG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 176 EAGTLQCCKRGYDADFAVVVDTSNlhmQGQGGVITGWITVKspRTFHDATRRQMiHAGGRLF-GASAIEKMMKIVQSLQE 254
Cdd:PRK07473 150 TPSTRDLIEAEAARNKYVLVPEPG---RPDNGVVTGRYAIA--RFNLEATGRPS-HAGATLSeGRSAIREMARQILAIDA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1586368115 255 LErhwavmktyegypSGTTTINPAVIEGGRHAAFIADECR 294
Cdd:PRK07473 224 MT-------------TEDCTFSVGIVHGGQWVNCVATTCT 250
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
84-270 |
2.56e-03 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. 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: 349934 [Multi-domain] Cd Length: 423 Bit Score: 40.13 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 84 NVVGVKKGTESGTYKSLIiNGHMDVAEVSIDEaWETNPFEPFIKDDWLVGRGAADMKG-----------------GLAGS 146
Cdd:cd08012 66 NIIVEYPGTVDGKTVSFV-GSHMDVVTANPET-WEFDPFSLSIDGDKLYGRGTTDCLGhvalvtelfrqlatekpALKRT 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 147 LFAIQLLEEAGIELPGnlifqsvIG-EEVGEAGTLQCCKRGYdadfAVVVDTSNLH-MQGQGGVITgWitvksprtfhda 224
Cdd:cd08012 144 VVAVFIANEENSEIPG-------VGvDALVKSGLLDNLKSGP----LYWVDSADSQpCIGTGGMVT-W------------ 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1586368115 225 trrqMIHAGGRLFGAS----AIEKMMKIVQSLQELERHWavmktYEGYPS 270
Cdd:cd08012 200 ----KLTATGKLFHSGlphkAINALELVMEALAEIQKRF-----YIDFPP 240
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
149-393 |
3.00e-03 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 39.51 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 149 AIQLLEEAGIELPGN--LIFQSviGEEVG-------EAGTLQccKRGYDADFAVVVDTsnlhmqgqgGVITGWITVKSPR 219
Cdd:cd03886 100 AAKLLAERRDPLKGTvrFIFQP--AEEGPggakamiEEGVLE--NPGVDAAFGLHVWP---------GLPVGTVGVRSGA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 220 TFhdATRRQMI--------HAGGRLFGASAIEKMMKIVQSLQElerhwavMKTYEGYPSGTTTINPAVIEGGRHAAFIAD 291
Cdd:cd03886 167 LM--ASADEFEitvkgkggHGASPHLGVDPIVAAAQIVLALQT-------VVSRELDPLEPAVVTVGKFHAGTAFNVIPD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 292 ECRLWITVHFYPNETHEQIIEEIEAYIRKVAAAdpwlsenppqfkwGGESMIVDRGEIFPSLEVDSEHVAvkTLSAVHES 371
Cdd:cd03886 238 TAVLEGTIRTFDPEVREALEARIKRLAEGIAAA-------------YGATVELEYGYGYPAVINDPELTE--LVREAAKE 302
|
250 260
....*....|....*....|....
gi 1586368115 372 ILSKNAIL--DMSATVTDGGWFSE 393
Cdd:cd03886 303 LLGEEAVVepEPVMGSEDFAYYLE 326
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
117-196 |
6.44e-03 |
|
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: 38.62 E-value: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1586368115 117 WETNPFEPF---IKDDWLV-GRGAADMKGGLAGSLFAIQLLEEAGIELPGN--LIFQSviGEEVGEAG---TLQCCKRGY 187
Cdd:cd05678 98 WEEINWDAIfsnLDPEWRVfARAAADDKGPIMMMLAALDALKAGGIAPKFNvkIILDS--EEEKGSPSlpkAVKEYKELL 175
|
....*....
gi 1586368115 188 DADFAVVVD 196
Cdd:cd05678 176 AADALIIMD 184
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
123-199 |
9.94e-03 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 37.84 E-value: 9.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1586368115 123 EPFIKDDWLVGRGAADMKGGLAGSLFAIQLLEEAGIElpgnLIFQSVIGEEVGEAGTLQCCKRGYDADFAVVVDTSN 199
Cdd:PRK00466 77 EPKIEGEVIYGRGAVDAKGPLISMIIAAWLLNEKGIK----VMVSGLADEESTSIGAKELVSKGFNFKHIIVGEPSN 149
|
|
| |
