|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06915 |
PRK06915 |
peptidase; |
1-422 |
0e+00 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 832.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 1 MKQLKKQVCDYIESHEEESVKFLTRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIWEPSFSKMKDHPYFVSPRTSFSDS 80
Cdd:PRK06915 1 MEQLKKQICDYIESHEEEAVKLLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIWEPSFKKLKDHPYFVSPRTSFSDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 81 PNIVATLKGSGDGKSMILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDI 160
Cdd:PRK06915 81 PNIVATLKGSGGGKSMILNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 161 YFQSVIEEESGGAGTLATILRGYKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLR 240
Cdd:PRK06915 161 IFQSVIEEESGGAGTLAAILRGYKADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 241 KLEEKRNGRITDPLFKGIPIPIPINIGKIEGGSWPSSVPDSLILEGRYGIAPNETIEAAKEEFESWIAELHDVDNWFVEN 320
Cdd:PRK06915 241 KLEEKRNDRITDPLYKGIPIPIPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAELNDVDEWFVEH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 321 PVEVEWFGARWVPGELEENHELITTLQHNFVEIEGKEPMIEASPWGTDGGLFTQISGVPTIVFGPGETKVAHYPNEYIEI 400
Cdd:PRK06915 321 PVEVEWFGARWVPGELEENHPLMTTLEHNFVEIEGNKPIIEASPWGTDGGLLTQIAGVPTIVFGPGETKVAHYPNEYIEV 400
|
410 420
....*....|....*....|..
gi 446734265 401 DKMIAAAKIIACTLLDWCEVKK 422
Cdd:PRK06915 401 DKMIAAAKIIALTLLDWCEVKK 422
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
21-418 |
2.85e-161 |
|
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: 459.85 E-value: 2.85e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 21 KFLTRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIWEPSFSKMKDHPYFVSPRTSFSDSPNIVATLKGSGD-GKSMILN 99
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDRWEIDVEKLKHHPGFSPVAVDYAGAPNVVGTHRPRGEtGRSLILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 100 GHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEESGGAGTLATI 179
Cdd:cd03895 81 GHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNGALAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 180 LRGYKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEEKRNGR-ITDPLFKGI 258
Cdd:cd03895 161 MRGYRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEREWNARkKSHPHFSDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 259 PIPIPINIGKIEGGSWPSSVPDSLILEGRYGIAPNETIEAAKEEFESWIAELHDVDNWFVENPVEVEWFGARWVPGELEE 338
Cdd:cd03895 241 PHPINFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVADAAATDPWLSNHPPEVEWNGFQAEGYVLEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 339 NHELITTLQHNFVEIEGKEPMIEASPWGTDGGLFTQISGVPTIVFGPGEtKVAHYPNEYIEIDKMIAAAKIIACTLLDWC 418
Cdd:cd03895 321 GSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGDIPALCYGPGS-RDAHGFDESVDLESLRKITKTIALFIAEWC 399
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
20-409 |
1.94e-118 |
|
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: 349.78 E-value: 1.94e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 20 VKFLTRLIQEKSVS---GDESGAQAIVIEKLRELGLDLDIWEPSFSKMKDHPyfvsprtsfsdspNIVATLKGSGDGKSM 96
Cdd:TIGR01910 1 VELLKDLISIPSVNppgGNEETIANYIKDLLREFGFSTDVIEITDDRLKVLG-------------KVVVKEPGNGNEKSL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 97 ILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEESGGAGTL 176
Cdd:TIGR01910 68 IFNGHYDVVPAGDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 177 ATILRGYK--ADGVIIPEPTN-MKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEEKRNGRITDp 253
Cdd:TIGR01910 148 YLLQRGYFkdADGVLIPEPSGgDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEEHIYARNSY- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 254 lfKGIPIPIPINIGKIEGGSWPSSVPDSLILEGRYGIAPNETIEAAKEEFESWIAELHDVDNWFVENPVEVEWFGarwvP 333
Cdd:TIGR01910 227 --GFIPGPITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYENEPVVKWSG----P 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446734265 334 GELEENHELITTLQHNFVEIEGKEPMIEASPWGTDGGLFTQiSGVPTIVFGPGETKVAHYPNEYIEIDKMIAAAKI 409
Cdd:TIGR01910 301 NETPPDSRLVKALEAIIKKVRGIEPEVLVSTGGTDARFLRK-AGIPSIVYGPGDLETAHQVNEYISIKNLVESTKV 375
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
7-419 |
3.32e-111 |
|
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: 331.85 E-value: 3.32e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 7 QVCDYIESHEEESVKFLTRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIWEPSFSKmkdhpyfvsprtsfsdsPNIVAT 86
Cdd:COG0624 2 AVLAAIDAHLDEALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVPPGR-----------------PNLVAR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 87 LKGSGDGKSMILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVI 166
Cdd:COG0624 65 RPGDGGGPTLLLYGHLDVVPPGDLELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 167 EEESGGAGT---LATILRGYKADGVIIPEPTN-MKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKL 242
Cdd:COG0624 145 DEEVGSPGAralVEELAEGLKADAAIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 243 EEKRNgriTDPLFkgipIPIPINIGKIEGGSWPSSVPDSLILEGRYGIAPNETIEAAKEEFESWIAELHDVDNwfvenpV 322
Cdd:COG0624 225 EFDGR---ADPLF----GRTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVE------V 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 323 EVEWFGARWVPGELEENHELITTLQHNFVEIEGKEPMIEASPWGTDGGLFTQISGVPTIVFGPGETKVAHYPNEYIEIDK 402
Cdd:COG0624 292 EVEVLGDGRPPFETPPDSPLVAAARAAIREVTGKEPVLSGVGGGTDARFFAEALGIPTVVFGPGDGAGAHAPDEYVELDD 371
|
410
....*....|....*..
gi 446734265 403 MIAAAKIIACTLLDWCE 419
Cdd:COG0624 372 LEKGARVLARLLERLAG 388
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
3-422 |
7.09e-111 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 332.35 E-value: 7.09e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 3 QLKKQVCDYIESHEEESVKFLTRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIWEPSFSKMKDHPYFVSPRTSFSDSPN 82
Cdd:PRK06837 6 DLTQRILAAVDAGFDAQVAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDRWSIDPDDLKSHPGAGPVEIDYSGAPN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 83 IVATLKGSGD-GKSMILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIY 161
Cdd:PRK06837 86 VVGTYRPAGKtGRSLILQGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 162 FQSVIEEESGGAGTLATILRGYKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRK 241
Cdd:PRK06837 166 FQSVIEEESTGNGALSTLQRGYRADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 242 LEEKRNGRIT-DPLFKGIPIPIPINIGKIEGGSWPSSVPDSLILEGRYGIAPNETIEAAKEEFESWIAELHDVDNWFVEN 320
Cdd:PRK06837 246 LEAEWNARKAsDPHFEDVPHPINFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAADAQAEIEACLAAAARDDRFLSNN 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 321 PVEVEWFGARWVPGELEENHELITTLQHNFVEIEGKEPMIEASPWGTDGGLFTQISGVPTIVFGPgETKVAHYPNEYIEI 400
Cdd:PRK06837 326 PPEVVWSGFLAEGYVLEPGSEAEAALARAHAAVFGGPLRSFVTTAYTDTRFYGLYYGIPALCYGP-SGEGIHGFDERVDL 404
|
410 420
....*....|....*....|..
gi 446734265 401 DKMIAAAKIIACTLLDWCEVKK 422
Cdd:PRK06837 405 ESVRKVTKTIALFVAEWCGVEP 426
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
21-411 |
2.13e-88 |
|
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: 272.64 E-value: 2.13e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 21 KFLTRLIQEKSVSGDESGAQAIVIEKLRELGLDLDiwepsfskmkdhpyfvspRTSFSDSPNIVATLkGSGDGKSMILNG 100
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIE------------------STIVEGRGNLVATV-GGGDGPVLLLNG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 101 HIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEESGGAGTLATIL 180
Cdd:cd08659 62 HIDTVPPGDGDKWSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 181 RGY--KADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKsmfVIDHLRKLEEKRNGRITDPLFkgi 258
Cdd:cd08659 142 AGYadRLDALIVGEPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYA---LADFLAELRTLFEELPAHPLL--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 259 pIPIPINIGKIEGGSWPSSVPDSLILEGRYGIAPNETIEAAKEEFESwIAELHdvdnwfvENPVEVEWFGARWVPGELEE 338
Cdd:cd08659 216 -GPPTLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEA-ILEEH-------EAKLTVEVSLDGDPPFFTDP 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446734265 339 NHELITTLQhNFVEIEGKEPMIEASPWGTDGGLFTQISGVPTIVFGPGETKVAHYPNEYIEIDKMIAAAKIIA 411
Cdd:cd08659 287 DHPLVQALQ-AAARALGGDPVVRPFTGTTDASYFAKDLGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYK 358
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
1-422 |
1.97e-71 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 230.70 E-value: 1.97e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 1 MKQLKKQVcdyiESHEEESVKFLTRLIQEKSVSG---DESGAQAIVIEKLRELGLDLDIWEpsfskmkdhpyfvsprtSF 77
Cdd:PRK08596 1 VSQLLEQI----ELRKDELLELLKTLVRFETPAPparNTNEAQEFIAEFLRKLGFSVDKWD-----------------VY 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 78 SDSPNIVATLKG--SGDGKSMILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVE 155
Cdd:PRK08596 60 PNDPNVVGVKKGteSDAYKSLIINGHMDVAEVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 156 LKGDIYFQSVIEEESGGAGTLATILRGYKADGVIIPEPTNMKFfpKQQGSM---WfrLHVKGKAA-HGGTRYE------- 224
Cdd:PRK08596 140 LPGDLIFQSVIGEEVGEAGTLQCCERGYDADFAVVVDTSDLHM--QGQGGVitgW--ITVKSPQTfHDGTRRQmihaggg 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 225 --GVSAIEKSMFVIDHLRKLEekRNGRITDPLFKGIPIPIPINIGKIEGGSWPSSVPDslilEGRYGIA----PNETIEA 298
Cdd:PRK08596 216 lfGASAIEKMMKIIQSLQELE--RHWAVMKSYPGFPPGTNTINPAVIEGGRHAAFIAD----ECRLWITvhfyPNETYEQ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 299 AKEEFESWIAELHDVDNWFVENPVEVEWFGARWV-------PG-ELEENHELITTLQHNFVEIEGKEPMIEASPWGTDGG 370
Cdd:PRK08596 290 VIKEIEEYIGKVAAADPWLRENPPQFKWGGESMIedrgeifPSlEIDSEHPAVKTLSSAHESVLSKNAILDMSTTVTDGG 369
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446734265 371 LFTQiSGVPTIVFGPGETKVAHYPNEYIEIDKMIAAAKIIACTLLDWCEVKK 422
Cdd:PRK08596 370 WFAE-FGIPAVIYGPGTLEEAHSVNEKVEIEQLIEYTKVITAFIYEWCHTKK 420
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
12-415 |
1.23e-62 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 207.15 E-value: 1.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 12 IESHEEESVKFLTRLIQEKSVSGDESGAQAIV---IEKLRELGLDLDIWEPSfskmKDHPYFVSPRtsfsdSPNIVAtLK 88
Cdd:PRK08651 1 VEAMMFDIVEFLKDLIKIPTVNPPGENYEEIAeflRDTLEELGFSTEIIEVP----NEYVKKHDGP-----RPNLIA-RR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 89 GSGDgKSMILNGHIDVVPEGDvnQWDHH-PYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGvelKGDIYFQSVIE 167
Cdd:PRK08651 71 GSGN-PHLHFNGHYDVVPPGE--GWSVNvPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAG---DGNIELAIVPD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 168 EESGGAGTLATILRGY-KADGVIIPEPTnmkfFPK-----QQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRK 241
Cdd:PRK08651 145 EETGGTGTGYLVEEGKvTPDYVIVGEPS----GLDnicigHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 242 LEEKRNGRITDPLFKGIPIPIPINIGKIEGGSWPSSVPDSLILEGRYGIAPNETIEAAKEEFESWIAELHDVDNWFVEnp 321
Cdd:PRK08651 221 SLSTIKSKYEYDDERGAKPTVTLGGPTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEVAPELGIEVE-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 322 VEVEWFGArwvPGELEENHELITTLQHNFVEIEGKEPMIEASPWGTDGgLFTQISGVPTIVFGPGETKVAHYPNEYIEID 401
Cdd:PRK08651 299 FEITPFSE---AFVTDPDSELVKALREAIREVLGVEPKKTISLGGTDA-RFFGAKGIPTVVYGPGELELAHAPDEYVEVK 374
|
410
....*....|....
gi 446734265 402 KMIAAAKIIACTLL 415
Cdd:PRK08651 375 DVEKAAKVYEEVLK 388
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
20-414 |
5.21e-60 |
|
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: 199.15 E-value: 5.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 20 VKFLTRLIQEKSVS--GDESGAQAIVI-EKLRELGLDLDIWEPSFSKmkdhpyfvsprtsfsdsPNIVATLKGSGDGKSM 96
Cdd:cd08011 1 VKLLQELVQIPSPNppGDNTSAIAAYIkLLLEDLGYPVELHEPPEEI-----------------YGVVSNIVGGRKGKRL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 97 ILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEESGG-AGT 175
Cdd:cd08011 64 LFNGHYDVVPAGDGEGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGrAGT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 176 LATILRGYKA-DGVIIPEPT---NMKFfpKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEEKRN-GRI 250
Cdd:cd08011 144 KYLLEKVRIKpNDVLIGEPSgsdNIRI--GEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELEKTVNpGVI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 251 tdplfkgipipipinigkiEGGSWPSSVPDSLILEGRYGIAPNETIEAAkeefeswIAELHDVdnwfVENPVEVEW-FGA 329
Cdd:cd08011 222 -------------------KGGVKVNLVPDYCEFSVDIRLPPGISTDEV-------LSRIIDH----LDSIEEVSFeIKS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 330 RWVPGELEENHELITTLQHNFVEIEGKEPMIEASpWGTDGGLFTQISGVPTIVFGPGETKVAHYPNEYIEIDKMIAAAKI 409
Cdd:cd08011 272 FYSPTVSNPDSEIVKKTEEAITEVLGIRPKEVIS-VGASDARFYRNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKV 350
|
....*
gi 446734265 410 IACTL 414
Cdd:cd08011 351 HALVA 355
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
97-416 |
1.64e-53 |
|
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: 180.62 E-value: 1.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 97 ILNGHIDVVPEGDVNQWdhhPYSGeKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVeLKGDIYFQSVIEEESGGAGTL 176
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKS-TEDGKLYGRGHDDMKGGLLAALEALRALKEEGL-KKGTVKLLFQPDEEGGMGGAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 177 ATI----LRGYKAD---GVIIPEPTNM------KFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLE 243
Cdd:pfam01546 76 ALIedglLEREKVDavfGLHIGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 244 ekrnGRITDPLFkgIPIPIPINIGKIEGGSwpSSVPDSLILEGRYGIAPNETIEAAKEEFESWIAELHDVDNWFVEnpVE 323
Cdd:pfam01546 156 ----SRNVDPLD--PAVVTVGNITGIPGGV--NVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVKVE--VE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 324 VEWFGARWVpgelEENHELITTLQHNFVEIEGKEPMIEASPW--GTDGGLFTQisGVP--TIVFGPGEtKVAHYPNEYIE 399
Cdd:pfam01546 226 YVEGGAPPL----VNDSPLVAALREAAKELFGLKVELIVSGSmgGTDAAFFLL--GVPptVVFFGPGS-GLAHSPNEYVD 298
|
330
....*....|....*..
gi 446734265 400 IDKMIAAAKIIACTLLD 416
Cdd:pfam01546 299 LDDLEKGAKVLARLLLK 315
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
79-418 |
5.99e-53 |
|
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: 181.14 E-value: 5.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 79 DSPNIVATLKGSGDGKSMILNGHIDVVpegDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGveLKG 158
Cdd:cd08013 54 GRPSVVGVVRGTGGGKSLMLNGHIDTV---TLDGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAG--LRG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 159 DIYFQSVIEEESGGAGTLATILRGYKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDH 238
Cdd:cd08013 129 DVILAAVADEEDASLGTQEVLAAGWRADAAIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 239 LRKLEEKRNGRITDPLFkgipIPIPINIGKIEGGSWPSSVPDSLILEGRYGIAPNETIEAAKEEFESWIAEL-HDVDNWF 317
Cdd:cd08013 209 LEEYQQELPERPVDPLL----GRASVHASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTAILGELaQTVPNFS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 318 VENPVEVEWFGarwvPGELEENHELITTLQHNFVEIEGKEPMIEASPWGTDGGLFTQiSGVPTIVFGPGETKvAHYPNEY 397
Cdd:cd08013 285 YREPRITLSRP----PFEVPKEHPFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAE-AGIPSVVFGPSGAG-LHAKEEW 358
|
330 340
....*....|....*....|.
gi 446734265 398 IEIDKMIAAAKIIACTLLDWC 418
Cdd:cd08013 359 VDVESIRQLREVLSAVVREFC 379
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
81-411 |
6.45e-50 |
|
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: 172.78 E-value: 6.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 81 PNIVATLKGSGDGKsMILNGHIDVVP-EGDVnqWDHHPYSGEKIGNRIYGRGTTDMKGGnVALMLAM-EAIIESGveLKG 158
Cdd:cd03894 46 ANLLATLGPGGEGG-LLLSGHTDVVPvDGQK--WSSDPFTLTERDGRLYGRGTCDMKGF-LAAVLAAvPRLLAAK--LRK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 159 DIYFQSVIEEESG--GAGTLA--TILRGYKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMF 234
Cdd:cd03894 120 PLHLAFSYDEEVGclGVRHLIaaLAARGGRPDAAIVGEPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAAR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 235 VIDHLRKLEEKRNGRITDPLFKGIPIPIPINIGkiEGGSWPSSVPDSLILEGRYGIAPNETIEAAKEEFESWIAELHDVD 314
Cdd:cd03894 200 LIGKLRELADRLAPGLRDPPFDPPYPTLNVGLI--HGGNAVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 315 nwfvENPVEVEWFgARWVPGELEENHELITTLQhnfvEIEGKEPMIeASPWGTDGGLFtQISGVPTIVFGPGETKVAHYP 394
Cdd:cd03894 278 ----EAGIEVEPL-FEVPGLETDEDAPLVRLAA----ALAGDNKVR-TVAYGTEAGLF-QRAGIPTVVCGPGSIAQAHTP 346
|
330
....*....|....*..
gi 446734265 395 NEYIEIDKMIAAAKIIA 411
Cdd:cd03894 347 DEFVELEQLDRCEEFLR 363
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
13-421 |
3.11e-48 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 169.35 E-value: 3.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 13 ESHEEESVKFLTRLIQEKSVSGDESGAQAIVIEKLRELGldldiwepsFSKMKDHPYfvsprtsfsdsPNIVATLKGsgd 92
Cdd:PRK13004 11 EKYKADMTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVG---------FDKVEIDPM-----------GNVLGYIGH--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 93 GKSMIL-NGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEESG 171
Cdd:PRK13004 68 GKKLIAfDAHIDTVGIGDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEEDC 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 172 GAGTLATIL--RGYKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEEKRN-- 247
Cdd:PRK13004 148 DGLCWRYIIeeDKIKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNLKed 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 248 ---GR----ITDPLFkgipipipinigkieggSWPS--SVPDSL-------ILEG---RYGIAPNETIEAAKeEFESWIA 308
Cdd:PRK13004 228 pflGKgtltVSDIFS-----------------TSPSrcAVPDSCaisidrrLTVGetwESVLAEIRALPAVK-KANAKVS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 309 ELHDVDNWFVENPVEVEWFGARWVpgeLEENHELITTLQHNFVEIEGKEPMIEASPWGTDGGLFTQISGVPTIVFGPGET 388
Cdd:PRK13004 290 MYNYDRPSYTGLVYPTECYFPTWL---YPEDHEFVKAAVEAYKGLFGKAPEVDKWTFSTNGVSIAGRAGIPTIGFGPGKE 366
|
410 420 430
....*....|....*....|....*....|...
gi 446734265 389 KVAHYPNEYIEIDKMIAAAKIIACTLLDWCEVK 421
Cdd:PRK13004 367 PLAHAPNEYTWKEQLVKAAAMYAAIPKSLLKKK 399
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
16-415 |
7.69e-45 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 159.66 E-value: 7.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 16 EEESVKFLTRLIQEKSVSGDEsgaqAIVIEKLRELGLDLDIwepsfsKMKDHPYfvSPRTSfsdspNIVATLkgsGDGKS 95
Cdd:PRK08588 1 EEEKIQILADIVKINSVNDNE----IEVANYLQDLFAKHGI------ESKIVKV--NDGRA-----NLVAEI---GSGSP 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 96 MI-LNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEESGGAG 174
Cdd:PRK08588 61 VLaLSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLLNGTIRLLATAGEEVGELG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 175 TLATILRGY--KADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEE---KRNGR 249
Cdd:PRK08588 141 AKQLTEKGYadDLDALIIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYFDsikKHNPY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 250 ITDPLFkgipipipiNIGKIEGGSWPSSVPDSLILEGRYGIAPNETIEAAKEEFESWIAELHDVDNWFVENPVEVEWFga 329
Cdd:PRK08588 221 LGGLTH---------VVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNQNGAAQLSLDIYSNHR-- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 330 rwvPGELEENHELITTLQHNFVEIEGKEPMIEASPWGTDGGLFTQIS-GVPTIVFGPGETKVAHYPNEYIEID---KMIA 405
Cdd:PRK08588 290 ---PVASDKDSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKpDFPVIIFGPGNNLTAHQVDEYVEKDmylKFID 366
|
410
....*....|
gi 446734265 406 AAKIIACTLL 415
Cdd:PRK08588 367 IYKEIIIQYL 376
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
20-407 |
1.64e-41 |
|
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: 151.03 E-value: 1.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 20 VKFLTRLIQEKSVSGDESGAQAIVIEKLRELGLDldiwepsfskmkdhpyfvsprTSFSDS-PNIVATLKGsgdGKSMIL 98
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGFD---------------------EVEIDPmGNVIGYIGG---GKKKIL 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 99 -NGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESG-VELKGDIYFQSVIEEE--SGGAG 174
Cdd:cd05649 57 fDGHIDTVGIGNIDNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGlRDFAYTILVAGTVQEEdcDGVCW 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 175 TLATILRGYKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEEKRNgriTDPL 254
Cdd:cd05649 137 QYISKADKIKPDFVVSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFP---EAPF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 255 FKGIPIPIPINIGKIEGGswpSSVPDS---------LILEGRYG-IAPNETIEAAKE--EFESWIAELHDVDNWfVENPV 322
Cdd:cd05649 214 LGRGTLTVTDIFSTSPSR---CAVPDScrisidrrlTVGETWEGcLEEIRALPAVKKygDDVAVSMYNYDRPSY-TGEVY 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 323 EVEWFGARWVpgeLEENHELITTLQHNFVEIEGKEPMIEASPWGTDGGLFTQISGVPTIVFGPGETKVAHYPNEYIEIDK 402
Cdd:cd05649 290 ESERYFPTWL---LPEDHELVKALLEAYKALFGARPLIDKWTFSTNGVSIMGRAGIPCIGFGPGAENQAHAPNEYTWKED 366
|
....*
gi 446734265 403 MIAAA 407
Cdd:cd05649 367 LVRCA 371
|
|
| selenium_YgeY |
TIGR03526 |
putative selenium metabolism hydrolase; SelD, selenophosphate synthase, is the selenium donor ... |
5-411 |
1.99e-40 |
|
putative selenium metabolism hydrolase; SelD, selenophosphate synthase, is the selenium donor protein for both selenocysteine and selenouridine biosynthesis systems, but it occurs also in a few prokaryotes that have neither of those pathways. The method of partial phylogenetic profiling, starting from such orphan-selD genomes, identifies this protein as one of those most strongly correlated to SelD occurrence. Its distribution is also well correlated with that of family TIGR03309, a putative accessory protein of labile selenium (non-selenocysteine) enzyme maturation. This family includes the uncharacterized YgeY of Escherichia coli, and belongs to a larger family of metalloenzymes in which some are known peptidases, others enzymes of different types.
Pssm-ID: 132565 [Multi-domain] Cd Length: 395 Bit Score: 148.41 E-value: 1.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 5 KKQVCDYIESHEEESVKFLTRLIQEKSVSGDESGAQAIVIEKLRELGLDldiwepsfskmkdhPYFVSPRTsfsdspNIV 84
Cdd:TIGR03526 1 FNQIKSEAEKYRGDMIRFLRDLVAIPSESGDEGRVALRIKQEMEKLGFD--------------KVEIDPMG------NVL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 85 ATLkgsGDGKSMIL-NGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQ 163
Cdd:TIGR03526 61 GYI---GHGPKLIAmDAHIDTVGIGDMDQWQFDPYEGYEDEEIIYGRGASDQEGGIASMVYAGKIIKDLGLLDDYTLLVT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 164 SVIEEES--GGAGTLATILRGYKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRK 241
Cdd:TIGR03526 138 GTVQEEDcdGLCWQYIIEEDKIKPEFVVITEPTDMNIYRGQRGRMEIKVTVKGVSCHGSAPERGDNAIYKMAPILKELSQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 242 LEekrNGRITDPLFKGIPIPIPINIGkieggSWPS--SVPDSLILEGRYGIAPNETIEAAKEEFESwIAELHDVDN---- 315
Cdd:TIGR03526 218 LN---ANLVEDPFLGKGTLTVSEIFF-----SSPSrcAVADGCTISIDRRLTWGETWEYALEQIRN-LPAVQGAEAevem 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 316 ------WFVENPVEVEWFGARWVpgeLEENHELITTLQHNFVEIEGKEPMIEASPWGTDGGLFTQISGVPTIVFGPGETK 389
Cdd:TIGR03526 289 yeydrpSYTGLVYPTECYFPTWV---LPEDHLITKAALETYKRLFGKEPGVDKWTFSTNGVSIMGRHGIPVIGFGPGDED 365
|
410 420
....*....|....*....|..
gi 446734265 390 VAHYPNEYIEIDKMIAAAKIIA 411
Cdd:TIGR03526 366 QAHAPNEKTWKEDLVKAAAMYA 387
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
82-416 |
5.97e-40 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 147.60 E-value: 5.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 82 NIVATLKGSGDGKSMILNGHIDVVPEGdvNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIY 161
Cdd:PRK13013 73 NLVARRQGARDGDCVHFNSHHDVVEVG--HGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 162 FQSVIEEESGGAGTLATIL-RGY----KADGVIIPEPTNM-KFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFV 235
Cdd:PRK13013 151 ISGTADEESGGFGGVAYLAeQGRfspdRVQHVIIPEPLNKdRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 236 IDHL-RKLEEKRNGRITD-PLFKGIPIPIPINIGKIEGGS---------WPSS-VPDS--LILEGRYGIAPN-------- 293
Cdd:PRK13013 231 LAEIeERLFPLLATRRTAmPVVPEGARQSTLNINSIHGGEpeqdpdytgLPAPcVADRcrIVIDRRFLIEEDldevkaei 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 294 ----ETIEAAKEEFESWIAELHDVdnwfvenpvevewfgarwVPGELEENHELITTLQHNFVEIEGKEPMIEASPWGTDG 369
Cdd:PRK13013 311 tallERLKRARPGFAYEIRDLFEV------------------LPTMTDRDAPVVRSVAAAIERVLGRQADYVVSPGTYDQ 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446734265 370 GLFTQISGVPT-IVFGPGETKVAHYPNEYIEIDKMIAAAKIIACTLLD 416
Cdd:PRK13013 373 KHIDRIGKLKNcIAYGPGILDLAHQPDEWVGIADMVDSAKVMALVLAD 420
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
82-411 |
1.66e-38 |
|
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130947 [Multi-domain] Cd Length: 364 Bit Score: 142.27 E-value: 1.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 82 NIVATLKGSGDGkSMILNGHIDVVPeGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGgnvALMLAMEAIIESGVE-LKGDI 160
Cdd:TIGR01892 48 NLVAVIGPSGAG-GLALSGHTDVVP-YDDAAWTRDPFRLTEKDGRLYGRGTCDMKG---FLACALAAAPDLAAEqLKKPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 161 YFQSVIEEESGGAGT---LATILRgyKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVID 237
Cdd:TIGR01892 123 HLALTADEEVGCTGApkmIEAGAG--RPRHAIIGEPTRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 238 HLRKLEEKRNGRITDPLFkgIPIPIPINIGKIEGGSWPSSVPDSLILEGRYGIAPNETIEAAKEEFESWIAELHDVDNWF 317
Cdd:TIGR01892 201 RLVHLADTLLREDLDEGF--TPPYTTLNIGVIQGGKAVNIIPGACEFVFEWRPIPGMDPEELLQLLETIAQALVRDEPGF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 318 venpvEVEWFGARWVPG-ELEENHELITTLQhnfvEIEGKEPmiEASPWGTDGGLFTQIsGVPTIVFGPGETKVAHYPNE 396
Cdd:TIGR01892 279 -----EVQIEVVSTDPGvNTEPDAELVAFLE----ELSGNAP--EVVSYGTEAPQFQEL-GAEAVVCGPGDIRQAHQPDE 346
|
330
....*....|....*
gi 446734265 397 YIEIDKMIAAAKIIA 411
Cdd:TIGR01892 347 YVEIEDLVRCRAVLA 361
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
20-411 |
7.19e-35 |
|
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: 132.01 E-value: 7.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 20 VKFLTRLIQEKSVSGDESGAQAIVIEKLRELGldldiwepsfskmkdhpYFVS-PRTSFSDSPNIVATLkGSGDGKSMIL 98
Cdd:cd05652 2 LSLHKSLVEIPSISGNEAAVGDFLAEYLESLG-----------------FTVEkQPVENKDRFNVYAYP-GSSRQPRVLL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 99 NGHIDVVPEgdvnqwdHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEESGGAGTLA- 177
Cdd:cd05652 64 TSHIDTVPP-------FIPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETGGDGMKAf 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 178 --TILRGYKAdgVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKL---EEKRNGRITd 252
Cdd:cd05652 137 ndLGLNTWDA--VIFGEPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDAdlpSSELLGPTT- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 253 plfkgipipipINIGKIEGGSWPSSVPDSLILEGRYGIA--PNETIEAAKEEfeswIAELHDvdnwfVENPVEVEWFGAR 330
Cdd:cd05652 214 -----------LNIGRISGGVAANVVPAAAEASVAIRLAagPPEVKDIVKEA----VAGILT-----DTEDIEVTFTSGY 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 331 wVPGELEenhelittlqhnfVEIEGKEPMIEAspWGTDGGLFTQisGVPTIVFGPGETKVAHYPNEYIEIDKMIAAA--- 407
Cdd:cd05652 274 -GPVDLD-------------CDVDGFETDVVA--YGTDIPYLKG--DHKRYLYGPGSILVAHGPDEAITVSELEEAVegy 335
|
....*
gi 446734265 408 -KIIA 411
Cdd:cd05652 336 kKLIL 340
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
82-418 |
2.35e-34 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 131.46 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 82 NIVATLkGSGDGKSMILNGHIDVVP-EGdvNQWDHHPYSGEKIGNRIYGRGTTDMKGgNVALMLAM-EAIIESgvELKGD 159
Cdd:PRK07522 54 NLFATI-GPADRGGIVLSGHTDVVPvDG--QAWTSDPFRLTERDGRLYGRGTCDMKG-FIAAALAAvPELAAA--PLRRP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 160 IYFQSVIEEESG--GAGTLATIL--RGYKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFV 235
Cdd:PRK07522 128 LHLAFSYDEEVGclGVPSMIARLpeRGVKPAGCIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 236 IDHLRKLEE--KRNGRiTDPLFkgipipipinigkieggswpsSVPDSLILEGRY--GIAPNETIEAAKEEFE-SWIAEL 310
Cdd:PRK07522 208 IAHLRDLADrlAAPGP-FDALF---------------------DPPYSTLQTGTIqgGTALNIVPAECEFDFEfRNLPGD 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 311 hDVDNWF--VENPVEVEW----------FGARW-----VPG-ELEENHELITTLQhnfvEIEGKEPMIEASpWGTDGGLF 372
Cdd:PRK07522 266 -DPEAILarIRAYAEAELlpemravhpeAAIEFeplsaYPGlDTAEDAAAARLVR----ALTGDNDLRKVA-YGTEAGLF 339
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446734265 373 TQIsGVPTIVFGPGETKVAHYPNEYIEIDKMIAAAKIIAcTLLDWC 418
Cdd:PRK07522 340 QRA-GIPTVVCGPGSIEQAHKPDEFVELAQLAACEAFLR-RLLASL 383
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
13-411 |
5.26e-32 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 125.35 E-value: 5.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 13 ESHEEESVKFLTRLIQEKSVSGDESG----AQAIVIE-KLRELGLDlDIWEpsfSKMKDhpyfvsPRTSFSDSPNIVATL 87
Cdd:PRK13983 1 DELRDEMIELLSELIAIPAVNPDFGGegekEKAEYLEsLLKEYGFD-EVER---YDAPD------PRVIEGVRPNIVAKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 88 KGSGDGKSMILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIE 167
Cdd:PRK13983 71 PGGDGKRTLWIISHMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 168 EESG---GAGTLATILRGY--KADGVIIPEptnmkfFPKQQGSM---------WFRLHVKGKAAHGGTRYEGVSAIEKSM 233
Cdd:PRK13983 151 EETGskyGIQYLLKKHPELfkKDDLILVPD------AGNPDGSFieiaeksilWLKFTVKGKQCHASTPENGINAHRAAA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 234 FVIDHL-RKLEEKRNGRitDPLFKGipipipinigkieggswPSS----------------VP--DSLILEGRygIAP-- 292
Cdd:PRK13983 225 DFALELdEALHEKFNAK--DPLFDP-----------------PYStfeptkkeanvdnintIPgrDVFYFDCR--VLPdy 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 293 --NETIEAAKEEFESwIAELHDVDnwfvenpVEVEWFGARWVPGELEENHELITTLQHNFVEIEGKEPmieaSPWGTDGG 370
Cdd:PRK13983 284 dlDEVLKDIKEIADE-FEEEYGVK-------IEVEIVQREQAPPPTPPDSEIVKKLKRAIKEVRGIEP----KVGGIGGG 351
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 446734265 371 LFTQI---SGVPTIVFGPGEtKVAHYPNEYIEIDKMIAAAKIIA 411
Cdd:PRK13983 352 TVAAFlrkKGYPAVVWSTLD-ETAHQPNEYAKISNLIEDAKVFA 394
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
20-218 |
2.63e-29 |
|
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: 117.22 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 20 VKFLTRLIQEKSVSGDESGAQAIVIEKLRELGldldiwepsfskmkdhpyFVSPRTSFSDSPNIVATlKGSGdGKSMILN 99
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALG------------------FTCERLEFGGVKNLWAR-RGTG-GPHLCFA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 100 GHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGnVALML-AMEAIIESGVELKGDIYFqsVI---EEESGGAGT 175
Cdd:cd03891 61 GHTDVVPPGDLEGWSSDPFSPTIKDGMLYGRGAADMKGG-IAAFVaAAERFVAKHPNHKGSISF--LItsdEEGPAIDGT 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446734265 176 LATI--L--RGYKADGVIIPEPTNmkffPKQ---------QGSMWFRLHVKGKAAH 218
Cdd:cd03891 138 KKVLewLkaRGEKIDYCIVGEPTS----EKKlgdtikigrRGSLNGKLTIKGKQGH 189
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
17-410 |
1.85e-28 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 114.47 E-value: 1.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 17 EESVKFLTRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIwePSFSKMKDhpYFVSPrtsfsDSPNIVATlkgsgdgksm 96
Cdd:PRK08652 2 ERAKELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHI--ESDGEVIN--IVVNS-----KAELFVEV---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 97 ilngHIDVVPegdvnqwdhhPYSGEKI-GNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSviEEESGGAGT 175
Cdd:PRK08652 63 ----HYDTVP----------VRAEFFVdGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFVS--DEEEGGRGS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 176 lATILRGYKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEEKRNGRITDPLf 255
Cdd:PRK08652 127 -ALFAERYRPKMAIVLEPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPHI- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 256 kgipipipiNIGKIEGGSWPSSVPD--SLILEGRygIAPNETIEAAKEEFESWIaelhdvDNWFVENPVEVEWFGarWVP 333
Cdd:PRK08652 205 ---------GIQEIIGGSPEYSIPAlcRLRLDAR--IPPEVEVEDVLDEIDPIL------DEYTVKYEYTEIWDG--FEL 265
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446734265 334 GELEEnhelITTLQHNFVEIEGKEPMIEASPWGTDGGLFTQiSGVPTIVFGPGETKVAHYPNEYIEIDKMIAAAKII 410
Cdd:PRK08652 266 DEDEE----IVQLLEKAMKEVGLEPEFTVMRSWTDAINFRY-NGTKTVVWGPGELDLCHTKFERIDVREVEKAKEFL 337
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
17-411 |
7.02e-28 |
|
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: 113.71 E-value: 7.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 17 EESVKFLTRLIQEKSVS----GDESGAQAIVIEK-LRELGldldiwEPSFSKMKDHPYFVSPRtsfsdsPNIVATLKGsG 91
Cdd:cd05650 1 EEIIELERDLIRIPAVNpesgGEGEKEKADYLEKkLREYG------FYTLERYDAPDERGIIR------PNIVAKIPG-G 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 92 DGKSMILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEESG 171
Cdd:cd05650 68 NDKTLWIISHLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 172 GAGTLATILRGY----KADGVIIPE---PTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSA-IEKSMFVIDHLRKLE 243
Cdd:cd05650 148 SEYGIQYLLNKFdlfkKDDLIIVPDfgtEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAfVAASNFALELDELLH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 244 EKRNGRitDPLFKGIPIPIPINIGKIEGGSwPSSVP--DSLILEGRygIAPNETIEAAKEEFESWIAELHDVDnwfvENP 321
Cdd:cd05650 228 EKFDEK--DDLFNPPYSTFEPTKKEANVPN-VNTIPgyDVFYFDCR--VLPTYKLDEVLKFVNKIISDFENSY----GAG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 322 VEVEWFGARWVPGELEENHELITTLQHNFVEIEGkepmIEASPWGTDGGL---FTQISGVPTIVFGPGEtKVAHYPNEYI 398
Cdd:cd05650 299 ITYEIVQKEQAPPATPEDSEIVVRLSKAIKKVRG----REAKLIGIGGGTvaaFLRKKGYPAVVWSTLD-ETAHQPNEYI 373
|
410
....*....|...
gi 446734265 399 EIDKMIAAAKIIA 411
Cdd:cd05650 374 RISHIVKDAKVFA 386
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
20-411 |
8.42e-28 |
|
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: 113.07 E-value: 8.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 20 VKFLTRLIQEKSVSGDESG---AQAIVIEKLRELGLDLDIwepsfskmkdhpyfvSPRTSFSDspNIVATLKGSGdGKSM 96
Cdd:cd03885 2 LDLLERLVNIESGTYDKEGvdrVAELLAEELEALGFTVER---------------RPLGEFGD--HLIATFKGTG-GKRV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 97 ILNGHIDVV-PEGDVNQWdhhPYSgeKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEESGGAGT 175
Cdd:cd03885 64 LLIGHMDTVfPEGTLAFR---PFT--VDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 176 LATILR-GYKADGVIIPEP--------TNMKffpkqqGSMWFRLHVKGKAAHGGTRYE-GVSAIEKSMFVIDHLRKLEEK 245
Cdd:cd03885 139 RELIEEeAKGADYVLVFEParadgnlvTARK------GIGRFRLTVKGRAAHAGNAPEkGRSAIYELAHQVLALHALTDP 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 246 RNGRITDPlfkgipipipiniGKIEGGSWPSSVPD--SLILEGRYgiapneTIEAAKEEFESWIAELhdVDNWFVENpVE 323
Cdd:cd03885 213 EKGTTVNV-------------GVISGGTRVNVVPDhaEAQVDVRF------ATAEEADRVEEALRAI--VATTLVPG-TS 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 324 VEWFGAR----WVPGelEENHELITTLQHNFVEIeGKEPMIEASPWGTDGGlFTQISGVPTI-VFGP-GetKVAHYPNEY 397
Cdd:cd03885 271 VELTGGLnrppMEET--PASRRLLARAQEIAAEL-GLTLDWEATGGGSDAN-FTAALGVPTLdGLGPvG--GGAHTEDEY 344
|
410
....*....|....
gi 446734265 398 IEIDKMIAAAKIIA 411
Cdd:cd03885 345 LELDSLVPRIKLLA 358
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
20-218 |
2.21e-27 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 112.10 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 20 VKFLTRLIQEKSVSGDESGAQAIVIEKLRELGldldiwepsfskmkdhpyFVSPRTSFSDSPNIVATLKGsgDGKSMILN 99
Cdd:PRK13009 5 LELAQDLIRRPSVTPDDAGCQDLLAERLEALG------------------FTCERMDFGDVKNLWARRGT--EGPHLCFA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 100 GHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGnVALML-AMEAIIESGVELKGDIYFqsVI---EEESGGAGT 175
Cdd:PRK13009 65 GHTDVVPPGDLEAWTSPPFEPTIRDGMLYGRGAADMKGS-LAAFVvAAERFVAAHPDHKGSIAF--LItsdEEGPAINGT 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446734265 176 LATI--L--RGYKADGVIIPEPTNmkffPKQ---------QGSMWFRLHVKGKAAH 218
Cdd:PRK13009 142 VKVLewLkaRGEKIDYCIVGEPTS----TERlgdvikngrRGSLTGKLTVKGVQGH 193
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
20-219 |
3.48e-25 |
|
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: 106.67 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 20 VKFLTRLIQEKSV-----SGDESGAQAIVIEKLRELGLDLDIWEPSfskmkDHPyfvsPRTsfsdspNIVATLKGSGDG- 93
Cdd:cd05675 1 VDLLQELIRIDTTnsgdgTGSETRAAEVLAARLAEAGIQTEIFVVE-----SHP----GRA------NLVARIGGTDPSa 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 94 KSMILNGHIDVVPeGDVNQWDHHPYSGEKIGNRIYGRGTTDMKgGNVALMLA-MEAIIESGVELKGDIYFQSVIEEESGG 172
Cdd:cd05675 66 GPLLLLGHIDVVP-ADASDWSVDPFSGEIKDGYVYGRGAVDMK-NMAAMMLAvLRHYKREGFKPKRDLVFAFVADEEAGG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446734265 173 AGTLATILRGYK-----ADGVI-------IPEPTNMKFFPKQ---QGSMWFRLHVKGKAAHG 219
Cdd:cd05675 144 ENGAKWLVDNHPelfdgATFALneggggsLPVGKGRRLYPIQvaeKGIAWMKLTVRGRAGHG 205
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
20-418 |
5.43e-25 |
|
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: 104.87 E-value: 5.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 20 VKFLTRLIQEKSVSGDESGAQAIVIEKLRELGL-DLDIwepsfskmkdhpyfvsprtsfSDSPNIVATLKGSGDGKSMIL 98
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGLgDVER---------------------DGRGNVVGRLRGTGGGPALLF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 99 NGHID-VVPEGDvnqwdhhPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVI-EEESG---GA 173
Cdd:cd03896 60 SAHLDtVFPGDT-------PATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVgEEGLGdlrGA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 174 GTLATILRgYKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEEKRNGRITdp 253
Cdd:cd03896 133 RYLLSAHG-ARLDYFVVAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAPYVPKTT-- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 254 lfkgipipipINIGKIEGGSWPSSVPD--SLILEGRYgiAPNETIEAAKEEFESWIAEL----HDVDnwfvenpVEVEWF 327
Cdd:cd03896 210 ----------FAAIRGGGGTSVNRIANlcSMYLDIRS--NPDAELADVQREVEAVVSKLaakhLRVK-------ARVKPV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 328 GARwvPGELEENHELITTLQHNFVEIEGKEPMIeaSPWGTDGGLFTQIsGVPTIVFGPGETKVAHYPNEYIEIDKMIAAA 407
Cdd:cd03896 271 GDR--PGGEAQGTEPLVNAAVAAHREVGGDPRP--GSSSTDANPANSL-GIPAVTYGLGRGGNAHRGDEYVLKDDMLKGA 345
|
410
....*....|.
gi 446734265 408 KIIACTLLDWC 418
Cdd:cd03896 346 KAYLMLAAALC 356
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
19-218 |
1.05e-23 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 101.72 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 19 SVKFLTRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIWEpsfskmkdhpyfvsprtsFSDSPNIVATlKGSGdGKSMIL 98
Cdd:TIGR01246 1 VTELAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMH------------------FGDTKNLWAT-RGTG-EPVLAF 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 99 NGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEES----GGAG 174
Cdd:TIGR01246 61 AGHTDVVPAGPEEQWSSPPFEPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGtaidGTKK 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446734265 175 TLATIL-RGYKADGVIIPEPTNMKFFPK-----QQGSMWFRLHVKGKAAH 218
Cdd:TIGR01246 141 VVETLMaRDELIDYCIVGEPSSVKKLGDvikngRRGSITGNLTIKGIQGH 190
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
18-409 |
2.30e-23 |
|
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: 100.08 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 18 ESVKFLTRLIQEKSVSGDESGAQAIVIEKLRELGLdldiwepSFSKMKDHPYFVSPrtSFSDSPnivatlkgsgdgKSMI 97
Cdd:cd05651 1 EAIELLKSLIATPSFSREEHKTADLIENYLEQKGI-------PFKRKGNNVWAENG--HFDEGK------------PTLL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 98 LNGHIDVVPEgdVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGvELKGDIYFQSVIEEESGGAGTLA 177
Cdd:cd05651 60 LNSHHDTVKP--NAGWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEG-PLNYNLIYAASAEEEISGKNGIE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 178 TILRGY-KADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGtRYEGVSAIEKSMFVIDHLRKLEEKRNGRITDPlfk 256
Cdd:cd05651 137 SLLPHLpPLDLAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAA-RNEGDNAIYKALDDIQWLRDFRFDKVSPLLGP--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 257 gipipIPINIGKIEGGSWPSSVPDS--LILEGR----YGIApnETIEAAKEEFESwiaelhdvdnwfvenpvEVEWFGAR 330
Cdd:cd05651 213 -----VKMTVTQINAGTQHNVVPDSctFVVDIRtteaYTNE--EIFEIIRGNLKS-----------------EIKPRSFR 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446734265 331 WVPGELEENHELITTLQHnfveiEGKEPMieASPWGTDGGLFtqisGVPTIVFGPGETKVAHYPNEYIEIDKMIAAAKI 409
Cdd:cd05651 269 LNSSAIPPDHPIVQAAIA-----AGRTPF--GSPTLSDQALM----PFPSVKIGPGDSSRSHTADEFIELSEIEEGIDI 336
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
23-410 |
3.09e-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: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 23 LTRLIQEKSVSGDEsGAQAIVIEK-LRELgldldiwePSFSKMKDHPYFVSpRTSFsdspnivatlkgsGDGKSMILNGH 101
Cdd:cd05647 5 TAALVDIPSVSGNE-KPIADEIEAaLRTL--------PHLEVIRDGNTVVA-RTER-------------GLASRVILAGH 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 102 IDVVPEGDvnqwdHHPYSGEKIGnRIYGRGTTDMKGGnVALMLAMEAIIeSGVELKGDIYF-----QSVIEEESGgagtL 176
Cdd:cd05647 62 LDTVPVAG-----NLPSRVEEDG-VLYGCGATDMKAG-DAVQLKLAATL-AAATLKHDLTLifydcEEVAAELNG----L 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 177 ATILRGYK----ADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEEKRngritd 252
Cdd:cd05647 130 GRLAEEHPewlaADFAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLAAYEPRT------ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 253 PLFKGIPIPIPINIGKIEGGSWPSSVPDSLILEGRYGIAPNETIEAAkeefeswIAELHDVDNWF-VENPVEVEWFGARw 331
Cdd:cd05647 204 VNIDGLTYREGLNAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEA-------IAHVREVFEGLgYEIEVTDLSPGAL- 275
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446734265 332 vPGeleenheLITTLQHNFVEIEGKEPmiEASPWGTDGGLFTQIsGVPTIVFGPGETKVAHYPNEYIEIDKMIAAAKII 410
Cdd:cd05647 276 -PG-------LDHPVARDLIEAVGGKV--RAKYGWTDVARFSAL-GIPAVNFGPGDPLLAHKRDEQVPVEQITACAAIL 343
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
23-401 |
2.30e-19 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 89.11 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 23 LTRLIQEKSVSG-----DESGAQaiVIEKL----RELGLDLDIWEpsfskMKDHPyfvsprtsfsDSPNIVATLkGSGDG 93
Cdd:PRK05111 11 YRALIATPSISAtdpalDQSNRA--VIDLLagwfEDLGFNVEIQP-----VPGTR----------GKFNLLASL-GSGEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 94 kSMILNGHIDVVPEgDVNQWDHHPYSGEKIGNRIYGRGTTDMKGgnvALMLAMEAIIESGVE-LKGDIYFQSVIEEESG- 171
Cdd:PRK05111 73 -GLLLAGHTDTVPF-DEGRWTRDPFTLTEHDGKLYGLGTADMKG---FFAFILEALRDIDLTkLKKPLYILATADEETSm 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 172 -GAGTLA--TILRGykaDGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEEKRNG 248
Cdd:PRK05111 148 aGARAFAeaTAIRP---DCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 249 RITDPLFkgipipipinigkieggswpsSVPdslilegrY----------GIAPNEtIEAAkeefeswiAELH------- 311
Cdd:PRK05111 225 RYHNPAF---------------------TVP--------YptlnlghihgGDAPNR-ICGC--------CELHfdirplp 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 312 -----DVDNWFVEN--PVEVEWfGARW--------VPG-ELEENHELITTLQhnfvEIEGKEPmiEASPWGTDGGLFTQI 375
Cdd:PRK05111 267 gmtleDLRGLLREAlaPVSERW-PGRItvaplhppIPGyECPADHQLVRVVE----KLLGHKA--EVVNYCTEAPFIQQL 339
|
410 420
....*....|....*....|....*.
gi 446734265 376 sGVPTIVFGPGETKVAHYPNEYIEID 401
Cdd:PRK05111 340 -GCPTLVLGPGSIEQAHQPDEYLELS 364
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
86-189 |
4.25e-19 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 89.23 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 86 TLKGSG-DGKSMILNGHIDVVP--EGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYF 162
Cdd:PRK08262 103 TWKGSDpSLKPIVLMAHQDVVPvaPGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYL 182
|
90 100 110
....*....|....*....|....*....|.
gi 446734265 163 QSVIEEESGGAGT--LATIL--RGYKADGVI 189
Cdd:PRK08262 183 AFGHDEEVGGLGAraIAELLkeRGVRLAFVL 213
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
17-414 |
9.00e-19 |
|
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: 87.02 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 17 EESVKFLTRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIwepsfskmkdhpyfvsprtsfSDSPNIVATlKGSGdGKSM 96
Cdd:cd05653 1 QDAVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWV---------------------DEAGNAVGG-AGSG-PPDV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 97 ILNGHIDVVPeGDVNQwdhhpysgeKI-GNRIYGRGTTDMKGGNVALMLAmeaIIESGVELKGDIYFQSVIEEESGGAGT 175
Cdd:cd05653 58 LLLGHIDTVP-GEIPV---------RVeGGVLYGRGAVDAKGPLAAMILA---ASALNEELGARVVVAGLVDEEGSSKGA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 176 LATILRGYKADGVIIPEPTNMKFFP-KQQGSMWFRLHVKGKAAH--GGTRYEGVSAIEKsmfvIDHLRKLEEKRNGRITD 252
Cdd:cd05653 125 RELVRRGPRPDYIIIGEPSGWDGITlGYRGSLLVKIRCEGRSGHssSPERNAAEDLIKK----WLEVKKWAEGYNVGGRD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 253 plfkgipiPIPINIGKIEGGSWPSSVPDS--LILEGRYGIaPNETIEAAKEEFESWI-AELHDVDNwfvENPVEVewfga 329
Cdd:cd05653 201 --------FDSVVPTLIKGGESSNGLPQRaeATIDLRLPP-RLSPEEAIALATALLPtCELEFIDD---TEPVKV----- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 330 rwvpgelEENHELITTLQHNFVEiEGKEPMIeASPWGT-DGGLFTQISGVPTIVFGPGETKVAHYPNEYIEIDKMIAAAK 408
Cdd:cd05653 264 -------SKNNPLARAFRRAIRK-QGGKPRL-KRKTGTsDMNVLAPLWTVPIVAYGPGDSTLDHTPNEHIELAEIERAAA 334
|
....*.
gi 446734265 409 IIACTL 414
Cdd:cd05653 335 VLKGAL 340
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
20-410 |
9.68e-19 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 87.03 E-value: 9.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 20 VKFLTRLIQEKSVSGDESGAQAIVIEKLRELGLDldiwepsfskmkdhpyfvsprTSFSDSPNIVATLKGS--GDGKSMI 97
Cdd:COG2195 6 LERFLEYVKIPTPSDHEEALADYLVEELKELGLE---------------------VEEDEAGNVIATLPATpgYNVPTIG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 98 LNGHIDVVPEgdvnqwdhhpYSGEKI-----GNRIYGRGTT----DMKGGNVALMLAMEAIIESGVElKGDIYFQSVIEE 168
Cdd:COG2195 65 LQAHMDTVPQ----------FPGDGIkpqidGGLITADGTTtlgaDDKAGVAAILAALEYLKEPEIP-HGPIEVLFTPDE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 169 ESGGAGTLA---TILRGYKA-------DGVIIPE-PTNMKFfpkqqgsmwfRLHVKGKAAHGGTRYE-GVSAIEKSMFVI 236
Cdd:COG2195 134 EIGLRGAKAldvSKLGADFAytldggeEGELEYEcAGAADA----------KITIKGKGGHSGDAKEkMINAIKLAARFL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 237 DHLRKLE--EKRNGRITDplfkgipipipinigkIEGGSWPSSVPDSLILEgryGIAPNETIEAAKEEFESWIAELHDVD 314
Cdd:COG2195 204 AALPLGRipEETEGNEGF----------------IHGGSATNAIPREAEAV---YIIRDHDREKLEARKAELEEAFEEEN 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 315 NWFVENPVEVEWFGArwVPG-ELEENHELITTLQHNFVEIeGKEPMIEASPWGTDGGLFTQIsGVPTIVFGPGETKVaHY 393
Cdd:COG2195 265 AKYGVGVVEVEIEDQ--YPNwKPEPDSPIVDLAKEAYEEL-GIEPKIKPIRGGLDGGILSFK-GLPTPNLGPGGHNF-HS 339
|
410
....*....|....*..
gi 446734265 394 PNEYIEIDKMIAAAKII 410
Cdd:COG2195 340 PDERVSIESMEKAWELL 356
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
81-252 |
9.70e-19 |
|
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: 87.33 E-value: 9.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 81 PNIVATLKGSG-DGKSMILNGHIDVVPEGDvNQWDHHPYSGEKIGN-RIYGRGTTDMKGGNVALMLAMEAIIESGVELKG 158
Cdd:cd05646 51 PVVVLTWEGSNpELPSILLNSHTDVVPVFE-EKWTHDPFSAHKDEDgNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 159 DIYFQSVIEEESGGAGTLATILR---------GYKAD-GVIIPEPTNMKFFpKQQGSMWFRLHVKGKAAHGGTRYEGvSA 228
Cdd:cd05646 130 TIHLSFVPDEEIGGHDGMEKFVKteefkklnvGFALDeGLASPTEEYRVFY-GERSPWWVVITAPGTPGHGSKLLEN-TA 207
|
170 180
....*....|....*....|....
gi 446734265 229 IEKSMFVIDHLRKLEEKRNGRITD 252
Cdd:cd05646 208 GEKLRKVIESIMEFRESQKQRLKS 231
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
82-195 |
1.83e-18 |
|
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: 83.25 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 82 NIVATLKGSGDGKSMILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIY 161
Cdd:cd18669 1 NVIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 446734265 162 FQSVIEEESGGAGTLATILRG-----YKADGVIIPEPTN 195
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLSKDaleedLKVDYLFVGDATP 119
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
10-411 |
1.87e-18 |
|
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: 86.92 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 10 DYIESHEEESVKFLTRLIQEKSVSGDESGAQ------AIVIEKLRELGLDLDIwepsfsKMKDHPyfvsprtsfsdspNI 83
Cdd:cd03888 1 EEIDKYKDEILEDLKELVAIPSVRDEATEGApfgegpRKALDKFLDLAKRLGF------KTKNID-------------NY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 84 VATLK-GSGDGKSMILnGHIDVVPEGDvnQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELK----- 157
Cdd:cd03888 62 AGYAEyGEGEEVLGIL-GHLDVVPAGE--GWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKkkirl 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 158 ----------GDI--YFQS---------------VIEEESG------------GAGTLATILRGYKADGVI-------IP 191
Cdd:cd03888 139 ifgtdeetgwKCIehYFEHeeypdfgftpdaefpVINGEKGivtvdltfkiddDKGYRLISIKGGEATNMVpdkaeavIP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 192 EPTNMK----FFPKQQGSMW-----FRLHVKGKAAHGGTRYEGVSAIeksMFVIDHLRKLE-----------------EK 245
Cdd:cd03888 219 GKDKEElalsAATDLKGNIEiddggVELTVTGKSAHASAPEKGVNAI---TLLAKFLAELNkdgndkdfikflaknlhED 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 246 RNGR-----ITDPLFKGIPIPIPINIGKIEGGswpssvpdSLILEGRY--GIAPNETIEAAKEEFESWiaelhdvdnwfv 318
Cdd:cd03888 296 YNGKklginFEDEVMGELTLNPGIITLDDGKL--------ELGLNVRYpvGTSAEDIIKQIEEALEKY------------ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 319 enPVEVEWFGAR---WVPgeleENHELITTLQHNFVEIEGKepmiEASPWGTDGGlfTQISGVPTIV-FG---PGETKVA 391
Cdd:cd03888 356 --GVEVEGHKHQkplYVP----KDSPLVKTLLKVYEEQTGK----EGEPVAIGGG--TYARELPNGVaFGpefPGQKDTM 423
|
490 500
....*....|....*....|
gi 446734265 392 HYPNEYIEIDKMIAAAKIIA 411
Cdd:cd03888 424 HQANEFIPIDDLIKALAIYA 443
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
15-416 |
7.07e-18 |
|
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: 84.91 E-value: 7.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 15 HEEESVKFLTRLIQ--EKSVSGDESGAQAIVIEKLRELGLDLDiwepsfskmkDHPY---FVSPRTSFSDSPNIVATLKG 89
Cdd:cd02697 1 HFDEEVRFLQKLVRvpTDTPPGNNAPHAERTAALLQGFGFEAE----------RHPVpeaEVRAYGMESITNLIVRRRYG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 90 SGdGKSMILNGHIDVVPEGDvnQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEE 169
Cdd:cd02697 71 DG-GRTVALNAHGDVVPPGD--GWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 170 SGGAGTLATILR-GYKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHL-------RK 241
Cdd:cd02697 148 FGGELGPGWLLRqGLTKPDLLIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALyalnaqyRQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 242 LEEKRNGrITDPLFkgipipipiNIGKIEGGSWPSSVPDSLILEGRYGIAPNETIEAAKEEFESWIAELH--------DV 313
Cdd:cd02697 228 VSSQVEG-ITHPYL---------NVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAasmpgisvDI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 314 DNWFVENPVevewfgaRWVPGeleeNHELITTLQHNFVEIEGKEPMIEASPWGTDGGLFTQiSGVPTIVFGPGETKV--- 390
Cdd:cd02697 298 RRLLLANSM-------RPLPG----NAPLVEAIQTHGEAVFGEPVPAMGTPLYTDVRLYAE-AGIPGVIYGAGPRTVles 365
|
410 420
....*....|....*....|....*..
gi 446734265 391 -AHYPNEYIEIDKMIAAAKIIACTLLD 416
Cdd:cd02697 366 hAKRADERLQLEDLRRATKVIARSLRD 392
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
26-410 |
2.12e-17 |
|
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: 83.27 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 26 LIQEKSVSGDESGAQAIVIEKLRELGLDldIWEPSFSKMKDHpyfvsprtsfsDSPNIVATLKGSGDGKSMIL-NGHIDV 104
Cdd:cd05683 12 LVQIDSETLHEKEISKVLKKKFENLGLS--VIEDDAGKTTGG-----------GAGNLICTLKADKEEVPKILfTSHMDT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 105 VPEGDVNQwdhhPYSGEkiGNRIYGRGTT----DMKGGNVALMLAMEAIIESGVElKGDIYFQSVIEEESG--GAGTLAT 178
Cdd:cd05683 79 VTPGINVK----PPQIA--DGYIYSDGTTilgaDDKAGIAAILEAIRVIKEKNIP-HGQIQFVITVGEESGlvGAKALDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 179 IL----RGYKADG------VIIPEPTNMKFFPKqqgsmwfrlhVKGKAAHGGTRYE-GVSAIEKSMFVIDHLrKLeekrn 247
Cdd:cd05683 152 ELidadYGYALDSegdvgtIIVGAPTQDKINAK----------IYGKTAHAGTSPEkGISAINIAAKAISNM-KL----- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 248 GRITDplfkgipiPIPINIGKIEGGSWPSSVPDSLILEGRYGIAPNETIEAA----KEEFESWIAELHdvdnwfVENPVE 323
Cdd:cd05683 216 GRIDE--------ETTANIGKFQGGTATNIVTDEVNIEAEARSLDEEKLDAQvkhmKETFETTAKEKG------AHAEVE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 324 VEwfgaRWVPG-ELEENHELITTLQHNFVEIeGKEPMIEASPWGTDGGLFTQIsGVPTIVFGPGETKvAHYPNEYIEIDK 402
Cdd:cd05683 282 VE----TSYPGfKINEDEEVVKLAKRAANNL-GLEINTTYSGGGSDANIINGL-GIPTVNLGIGYEN-IHTTNERIPIED 354
|
....*...
gi 446734265 403 MIAAAKII 410
Cdd:cd05683 355 LYDTAVLV 362
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
20-180 |
4.29e-17 |
|
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: 83.07 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 20 VKFLTRLIQEKSVSGDESGAQaivieklrelglDLDIWEPSFSKMkdHPYFvspRTSFsdsPNI--------------VA 85
Cdd:cd05674 1 IERLSGAVQIPTVSFDDMPPI------------DEDERWDAFYKF--HDYL---EKTF---PLVhktlkvevvneyglLY 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 86 TLKGSGDG-KSMILNGHIDVVP--EGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYF 162
Cdd:cd05674 61 TWEGSDPSlKPLLLMAHQDVVPvnPETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTIIL 140
|
170 180
....*....|....*....|.
gi 446734265 163 QSVIEEESGG---AGTLATIL 180
Cdd:cd05674 141 AFGHDEEVGGergAGAIAELL 161
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
20-219 |
2.76e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 80.28 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 20 VKFLTRLIQ-EKSVSGDESG-----AQAIVIEKLRELGLDLDIWEPsfskmkdHPyfvsPRTsfsdspNIVATLKGSGDG 93
Cdd:PRK07906 2 VDLCSELIRiDTTNTGDGTGkgereAAEYVAEKLAEVGLEPTYLES-------AP----GRA------NVVARLPGADPS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 94 KS-MILNGHIDVVPeGDVNQWDHHPYSGEKIGNRIYGRGTTDMKgGNVALMLA-MEAIIESGVELKGDIYFQSVIEEESG 171
Cdd:PRK07906 65 RPaLLVHGHLDVVP-AEAADWSVHPFSGEIRDGYVWGRGAVDMK-DMDAMMLAvVRHLARTGRRPPRDLVFAFVADEEAG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446734265 172 GAgtlatilrgYKA-----------DGVI--IPE--------PTNMKFFPKQ---QGSMWFRLHVKGKAAHG 219
Cdd:PRK07906 143 GT---------YGAhwlvdnhpelfEGVTeaISEvggfsltvPGRDRLYLIEtaeKGLAWMRLTARGRAGHG 205
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
82-195 |
4.10e-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: 76.31 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 82 NIVATLKGSGDGKSMILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIY 161
Cdd:cd03873 1 NLIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 446734265 162 FQSVIEEE---SGGAGTLAT--ILRGYKADGVIIPEPTN 195
Cdd:cd03873 81 VAFTADEEvgsGGGKGLLSKflLAEDLKVDAAFVIDATA 119
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
91-162 |
5.29e-15 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 76.27 E-value: 5.29e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446734265 91 GDGKSMI-LNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYF 162
Cdd:PRK07205 72 GQGEELLaILCHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRF 144
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
8-174 |
6.84e-15 |
|
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: 76.10 E-value: 6.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 8 VCDYIESHEEESVKFLTRLIQEKSVSGDES------GAQAIVIEKLRELGLDLDIWEPSFSKMKDHPYFVSPrtsfsdsP 81
Cdd:cd05676 1 VFKYIDEHQDEFIERLREAVAIQSVSADPEkrpeliRMMEWAAERLEKLGFKVELVDIGTQTLPDGEELPLP-------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 82 NIVATLKGSGDGKSMILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIY 161
Cdd:cd05676 74 VLLGRLGSDPSKKTVLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLK 153
|
170
....*....|....*
gi 446734265 162 FqsVIE--EESGGAG 174
Cdd:cd05676 154 F--CFEgmEESGSEG 166
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
35-250 |
1.47e-14 |
|
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic N-acyl-L-amino-acid amidohydrolases active on fatty acid and acetyl amides of L-amino acids.
Pssm-ID: 273850 [Multi-domain] Cd Length: 400 Bit Score: 74.83 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 35 DESGAQAIVIEKLRELGLDLDIWEPSfskmkdhpyfvsprtsfSDSPNIVATLKGSG-DGKSMILNGHIDVVPEGDVNqW 113
Cdd:TIGR01880 29 DYAACVDFLIKQADELGLARKTIEFV-----------------PGKPVVVLTWPGSNpELPSILLNSHTDVVPVFREH-W 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 114 DHHPYSGEK-IGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEESGG--------AGTLATILR-GY 183
Cdd:TIGR01880 91 THPPFSAFKdEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGhdgmekfaKTDEFKALNlGF 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446734265 184 KAD-GviIPEPTN-MKFFPKQQGSMWFRLHVKGKAAHGGTRYEGvSAIEKSMFVIDHLRKLEEKRNGRI 250
Cdd:TIGR01880 171 ALDeG--LASPDDvYRVFYAERVPWWVVVTAPGNPGHGSKLMEN-TAMEKLEKSVESIRRFRESQFQLL 236
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
6-229 |
2.18e-14 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 74.28 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 6 KQVCDYIESHEEESVKFLTRLIQEKSVSGDESGAQ---AIVIEKLRELGLDLdiwepsfsKMKDhpyfvsprTSFSDSPN 82
Cdd:PRK06133 26 AELLAAAQQEQPAYLDTLKELVSIESGSGDAEGLKqvaALLAERLKALGAKV--------ERAP--------TPPSAGDM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 83 IVATLKGSGDGKSMiLNGHIDVV-PEGDVNQwdhHPYSGEkiGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIY 161
Cdd:PRK06133 90 VVATFKGTGKRRIM-LIAHMDTVyLPGMLAK---QPFRID--GDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLT 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446734265 162 FQSVIEEESGGAGTLATILR-GYKADGVIIPEPTNMK--FFPKQQGSMWFRLHVKGKAAHGGTRYE-GVSAI 229
Cdd:PRK06133 164 VLFNPDEETGSPGSRELIAElAAQHDVVFSCEPGRAKdaLTLATSGIATALLEVKGKASHAGAAPElGRNAL 235
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
20-174 |
2.19e-14 |
|
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: 74.29 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 20 VKFLTRLIQEKSVSGDESGAQ-----AIVIEK-LRELGLDLDIwepsfskmkdhpYFVSPRTsfsdsPNIVATLKGSGDG 93
Cdd:cd03893 1 LQTLAELVAIPSVSAQPDRREelrraAEWLADlLRRLGFTVEI------------VDTSNGA-----PVVFAEFPGAPGA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 94 KSMILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFqsVIE--EESG 171
Cdd:cd03893 64 PTVLLYGHYDVQPAGDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKF--IIEgeEESG 141
|
...
gi 446734265 172 GAG 174
Cdd:cd03893 142 SPS 144
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
100-411 |
9.20e-14 |
|
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: 72.80 E-value: 9.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 100 GHIDVVPEGDvnQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEESGGAGT---- 175
Cdd:TIGR01887 74 GHLDVVPAGD--GWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEESGWKCIdyyf 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 176 ----LATI---------------------------------LRGYKADGV--IIPEPTN-----MKFFPKQQGSMWF--- 208
Cdd:TIGR01887 152 eheeMPDIgftpdaefpiiygekgittleikfkddtegdvvLESFKAGEAynMVPDHATavisgKKLTEVEQLKFVFfia 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 209 --------------RLHVKGKAAHGGTRYEGVSAIEKSMFVIDHL--------------RKLEEKRNGR-----ITDPLF 255
Cdd:TIGR01887 232 kelegdfevndgtlTITLEGKSAHGSAPEKGINAATYLALFLAQLnlaggakaflqflaEYLHEDHYGEklgikFHDDVS 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 256 KGIPIPIPINIGKIEGGSwpssvpdSLILEGRYGIAPNETIEAAKEEFEswIAELHDVDNWFVENPVevewfgarWVPGe 335
Cdd:TIGR01887 312 GDLTMNVGVIDYENAEAG-------LIGLNVRYPVGNDPDTMLKNELAK--ESGVVEVTLNGYLKPL--------YVPK- 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 336 leeNHELITTLQHNFVEIEGKepmiEASPWGTDGGLFTQIsgVPTIV-FG---PGETKVAHYPNEYIEIDKMIAAAKIIA 411
Cdd:TIGR01887 374 ---DDPLVQTLMKVYEKQTGD----EGEPVAIGGGTYARL--MPNGVaFGalfPGEEDTMHQANEYIMIDDLLLATAIYA 444
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
16-229 |
2.72e-13 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 71.42 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 16 EEESVKFLTRLIQEKSVSG--DESGAQAIVIEKLRELgldldiwePSFSKMKDHpYFVSPrtsFSDSP----NIVATLKG 89
Cdd:COG4187 7 KEQLEELLCELVSIPSVTGteGEKEVAEFIYEKLSEL--------PYFQENPEH-LGLHP---LPDDPlgrkNVTALVKG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 90 SGDGK-SMILNGHIDVVPEGDVNQWDHHPYSGEKI-------------------GNRIYGRGTTDMKGGnVALMLAMEAI 149
Cdd:COG4187 75 KGESKkTVILISHFDVVDVEDYGSLKPLAFDPEELtealkeiklpedvrkdlesGEWLFGRGTMDMKAG-LALHLALLEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 150 IESGVELKGDIYFQSVIEEESGGAGTLATI-----LR---GYKADGVIIPEPTnmkfFPKQQGSMWFRLH---------- 211
Cdd:COG4187 154 ASENEEFPGNLLLLAVPDEEVNSAGMRAAVpllaeLKekyGLEYKLAINSEPS----FPKYPGDETRYIYtgsigklmpg 229
|
250 260
....*....|....*....|
gi 446734265 212 --VKGKAAHGGTRYEGVSAI 229
Cdd:COG4187 230 fyCYGKETHVGEPFSGLNAN 249
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
97-403 |
3.23e-13 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 70.62 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 97 ILNGHIDVVPegDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIiesgvelKGDIYFQSVIEEESGGAGTL 176
Cdd:PRK08737 67 LFNVHLDTVP--DSPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANAG-------DGDAAFLFSSDEEANDPRCV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 177 ATIL-RGYKADGVIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHG-GTRYEGVSAIEKSMF----VIDHLRKLEEKRNGRI 250
Cdd:PRK08737 138 AAFLaRGIPYEAVLVAEPTMSEAVLAHRGISSVLMRFAGRAGHAsGKQDPSASALHQAMRwggqALDHVESLAHARFGGL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 251 TDPLFKGIPipipinigkIEGGSWPSSVPDSliLEGRYGI--APNETIEAAKEEFESwIAELHDVDnwfvenpVEVEWFG 328
Cdd:PRK08737 218 TGLRFNIGR---------VEGGIKANMIAPA--AELRFGFrpLPSMDVDGLLATFAG-FAEPAAAT-------FEETFRG 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446734265 329 ARWVPGELEENHELITTLQHNFVEIEgkEPMIEASPWGTDGGLFTQiSGVPTIVFGPGETKVAHYPNEYIEIDKM 403
Cdd:PRK08737 279 PSLPSGDIARAEERRLAARDVADALD--LPIGNAVDFWTEASLFSA-AGYTALVYGPGDIAQAHTADEFVTLDQL 350
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
91-411 |
7.42e-13 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 69.87 E-value: 7.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 91 GDGKSM--ILnGHIDVVPEGDvnQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDI-------- 160
Cdd:PRK07318 76 GEGEEVlgIL-GHLDVVPAGD--GWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVrfivgtde 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 161 ---------YFQS---------------VI--------------EEESGGAGTLATILRGYKAD--------GVIIPEPT 194
Cdd:PRK07318 153 esgwkcmdyYFEHeeapdfgfspdaefpIIngekgittfdlvhfEGENEGDYVLVSFKSGLRENmvpdsaeaVITGDDLD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 195 NM--KF--FPKQQG--------SMWFRLHVKGKAAHGGTRYEGVSAIeksMFVIDHLRKLE------------------- 243
Cdd:PRK07318 233 DLiaAFeaFLAENGlkgeleeeGGKLVLTVIGKSAHGSTPEKGVNAA---TYLAKFLNQLNldgdakafldfaaeylhed 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 244 ---EKRNGRITDPLFKGIPIPIPINIGKIEGGSwpssvpdSLILEGRY--GIAPNETIEAAKEEFESWIAELHDVDNwfv 318
Cdd:PRK07318 310 trgEKLGIAYEDDVMGDLTMNVGVFSFDEEKGG-------TLGLNFRYpvGTDFEKIKAKLEKLIGVTGVELSEHEH--- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 319 ENPvevewfgaRWVPGeleeNHELITTLQHNFVEIEGKepmiEASPWGTDGGLFTQI--SGVPtivFG---PGETKVAHY 393
Cdd:PRK07318 380 QKP--------HYVPK----DDPLVKTLLKVYEKQTGL----KGEEQVIGGGTYARLlkRGVA---FGamfPGSEDTMHQ 440
|
410
....*....|....*...
gi 446734265 394 PNEYIEIDKMIAAAKIIA 411
Cdd:PRK07318 441 ANEYIEIDDLIKAAAIYA 458
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
202-310 |
9.84e-13 |
|
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: 64.29 E-value: 9.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 202 QQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKLEEKRNGRITDPLFkgipipipiNIGKIEGGSWPSSVPDS 281
Cdd:pfam07687 3 HKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGFDFPRTTL---------NITGIEGGTATNVIPAE 73
|
90 100
....*....|....*....|....*....
gi 446734265 282 LILEGRYGIAPNETIEAAKEEFESWIAEL 310
Cdd:pfam07687 74 AEAKFDIRLLPGEDLEELLEEIEAILEKE 102
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
17-253 |
4.95e-12 |
|
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: 67.37 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 17 EESVKFLTRLIQEKSVSGDEsgAQAIVIEKLRELGLDLdiwePSFskmKDHPYFVSPRTSFSD--SPNIVATLKGSGDGK 94
Cdd:cd05654 1 ERLEQLLKSLVSWPSVTGTE--GERSFADFLKEILKEL----PYF---KENPSHVWQLLPPDDlgRRNVTALVKGKKPSK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 95 -SMILNGHIDVVPEGDVNQWDHHPYSGEKI---------------------GNRIYGRGTTDMKGGnvaLMLAMEAIIES 152
Cdd:cd05654 72 rTIILISHFDTVGIEDYGELKDIAFDPDELtkafseyveeldeevredllsGEWLFGRGTMDMKSG---LAVHLALLEQA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 153 GV--ELKGDIYFQSVIEEESGGAGTLATI--LRGYKAD------GVIIPEPTnmkfFPKQQGSMWFRLH----------- 211
Cdd:cd05654 149 SEdeDFDGNLLLMAVPDEEVNSRGMRAAVpaLLELKKKhdleykLAINSEPI----FPQYDGDQTRYIYtgsigkilpgf 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446734265 212 -VKGKAAHGGTRYEGVSAIEKSMFVIDHLR---KLEEKRNGRITDP 253
Cdd:cd05654 225 lCYGKETHVGEPFAGINANLMASEITARLElnaDLCEKVEGEITPP 270
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
23-195 |
6.28e-12 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 66.85 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 23 LTRLIQEKSVSGD-------ESGAQAiVIEKLRELGldldiwepsfskmkdhpyFVSPRTSFSD-SPNIVATLKGSGDGK 94
Cdd:PRK07907 24 LEELVRIPSVAADpfrreevARSAEW-VADLLREAG------------------FDDVRVVSADgAPAVIGTRPAPPGAP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 95 SMILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIiesGVELKGDIYFqsVIE--EESGG 172
Cdd:PRK07907 85 TVLLYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRAL---GGDLPVGVTV--FVEgeEEMGS 159
|
170 180
....*....|....*....|....*..
gi 446734265 173 AGtLATILRGYK----ADGVIIPEPTN 195
Cdd:PRK07907 160 PS-LERLLAEHPdllaADVIVIADSGN 185
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
21-189 |
7.44e-11 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 63.51 E-value: 7.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 21 KFLTRLIQEKSVSGDESGAQAI---VIEKLRELGLDLDIWEPsfskmKDHPYfvsprtsfsdspnIVATLKgSGDGKSMI 97
Cdd:cd05681 3 EDLRDLLKIPSVSAQGRGIPETadfLKEFLRRLGAEVEIFET-----DGNPI-------------VYAEFN-SGDAKTLL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 98 LNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFqsVIE-EESGGAGTL 176
Cdd:cd05681 64 FYNHYDVQPAEPLELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKF--LVEgEEEVGSPNL 141
|
170
....*....|....*..
gi 446734265 177 ATILRGY----KADGVI 189
Cdd:cd05681 142 EKFVAEHadllKADGCI 158
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
17-193 |
8.93e-11 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 63.05 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 17 EESVKFLTRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIWEpsfskmkdhpyfvsprtsfsdSPNIVATlKGSGdGKSM 96
Cdd:PRK04443 6 LEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREAWVDE---------------------AGNARGP-AGDG-PPLV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 97 ILNGHIDVVPeGDVnqwdhhPYSGEkiGNRIYGRGTTDMKGGNVALMLAMeaiIESGVELKGDIYFQSVIEEE---SGGA 173
Cdd:PRK04443 63 LLLGHIDTVP-GDI------PVRVE--DGVLWGRGSVDAKGPLAAFAAAA---ARLEALVRARVSFVGAVEEEapsSGGA 130
|
170 180
....*....|....*....|
gi 446734265 174 gtlATILRGYKADGVIIPEP 193
Cdd:PRK04443 131 ---RLVADRERPDAVIIGEP 147
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
77-174 |
2.96e-10 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 61.91 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 77 FSDSPNIV--ATLKGSGDGKSMILNgHIDVVP------EGDVNQWDhhPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEA 148
Cdd:PRK06156 92 YRNVDNRVleIGLGGSGSDKVGILT-HADVVPanpelwVLDGTRLD--PFKVTLVGDRLYGRGTEDDKGAIVTALYAMKA 168
|
90 100
....*....|....*....|....*.
gi 446734265 149 IIESGVELKGDIYFQSVIEEESGGAG 174
Cdd:PRK06156 169 IKDSGLPLARRIELLVYTTEETDGDP 194
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
82-184 |
4.31e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 61.17 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 82 NIVATLKGSGDGKSMILNGHIDVVpEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGnVALMLAMEA------------I 149
Cdd:PRK09133 90 NLVARLRGTDPKKPILLLAHMDVV-EAKREDWTRDPFKLVEENGYFYGRGTSDDKAD-AAIWVATLIrlkregfkpkrdI 167
|
90 100 110
....*....|....*....|....*....|....*
gi 446734265 150 IesgVELKGDiyfqsvieEESGGAGTLATILRGYK 184
Cdd:PRK09133 168 I---LALTGD--------EEGTPMNGVAWLAENHR 191
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
80-184 |
4.65e-10 |
|
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: 61.21 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 80 SPNIVATLKGSGD---GKSMILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGvEL 156
Cdd:cd05677 55 NPIVLATFSGNSSdakRKRILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQEG-EL 133
|
90 100
....*....|....*....|....*...
gi 446734265 157 KGDIYFQSVIEEESGGAGtLATILRGYK 184
Cdd:cd05677 134 DNDVVFLIEGEEESGSPG-FKEVLRKNK 160
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
40-418 |
5.98e-10 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 60.18 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 40 QAIVIEKLRELGLD-LDIWEPSFSKMKDHPYF--VSPR--TSFSDSPNIVATLKGSGDGksmILNGHIDVVPEgdvnqwd 114
Cdd:PRK00466 5 KELVKQKAKELLLDlLSIYTPSGNETNATKFFekISNElnLKLEILPDSNSFILGEGDI---LLASHVDTVPG------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 115 hhpYSGEKI-GNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKgdiyFQSVIEEESGGAGTLATILRGYKADGVIIPEP 193
Cdd:PRK00466 75 ---YIEPKIeGEVIYGRGAVDAKGPLISMIIAAWLLNEKGIKVM----VSGLADEESTSIGAKELVSKGFNFKHIIVGEP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 194 TN-MKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVsAIEKSMFVIDHLRKLEEKRNGRITDPLFkgipipipinigkiEGG 272
Cdd:PRK00466 148 SNgTDIVVEYRGSIQLDIMCEGTPEHSSSAKSNL-IVDISKKIIEVYKQPENYDKPSIVPTII--------------RAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 273 SWPSSVPDSLIL--EGRYGIaPNETIEAAKE---EFESwiAELHDVDNWfveNPVEVewfgarwvpgelEENHELITTLQ 347
Cdd:PRK00466 213 ESYNVTPAKLYLhfDVRYAI-NNKRDDLISEikdKFQE--CGLKIVDET---PPVKV------------SINNPVVKALM 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446734265 348 HNFVEiEGKEPMIEASPWGTDGGLFTQISgvPTIV-FGPGETKVAHYPNEYIEIDKMIAAAKIIACTLLDWC 418
Cdd:PRK00466 275 RALLK-QNIKPRLVRKAGTSDMNILQKIT--TSIAtYGPGNSMLEHTNQEKITLDEIYIAVKTYMLAIEELW 343
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
17-189 |
7.46e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 57.46 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 17 EESVKFLTRLIQEKSVS----GDESGAQAIViEKLRELGLDLDIwepsfSKMKDHPYfvsprtsfsdspniVATLKGSGD 92
Cdd:PRK06446 2 DEELYTLIEFLKKPSISatgeGIEETANYLK-DTMEKLGIKANI-----ERTKGHPV--------------VYGEINVGA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 93 GKSMILNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGgnvALMLAMEAIIESGVELKGDIYFQSVIE-EESG 171
Cdd:PRK06446 62 KKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKG---TLMARLFAIKHLIDKHKLNVNVKFLYEgEEEI 138
|
170 180
....*....|....*....|..
gi 446734265 172 GAGTLATILRGY----KADGVI 189
Cdd:PRK06446 139 GSPNLEDFIEKNknklKADSVI 160
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
16-233 |
1.32e-08 |
|
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: 56.70 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 16 EEESVKFLTRLIQE-KSVSGD-------ESGAQAIVIEKLRelgldldiwepSFSKMKDHPYFVSPRTSFSDSPNIVATL 87
Cdd:cd08012 3 EERFVSLLGKLIGEsKYLQNNppqlvpkEDNAGRHVLEALT-----------PYSTENGGPLVIDHVSYVKGRGNIIVEY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 88 KGSGDGKSMILNG-HIDVVPeGDVNQWDHHPYSGEKIGNRIYGRGTTDMKgGNVALMLA-MEAIIESGVELKGDIYFQSV 165
Cdd:cd08012 72 PGTVDGKTVSFVGsHMDVVT-ANPETWEFDPFSLSIDGDKLYGRGTTDCL-GHVALVTElFRQLATEKPALKRTVVAVFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 166 IEEESG---GAGTLATILRGykadgviipEPTNMKFFP--------KQQ-----GSMWFRLHVKGKAAHGGTRYEGVSAI 229
Cdd:cd08012 150 ANEENSeipGVGVDALVKSG---------LLDNLKSGPlywvdsadSQPcigtgGMVTWKLTATGKLFHSGLPHKAINAL 220
|
....
gi 446734265 230 EKSM 233
Cdd:cd08012 221 ELVM 224
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
97-310 |
1.37e-08 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 56.51 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 97 ILNGHIDVV-PEGdvnqwdhHPYsgEKI----GNRIYGRGTTDMKGGnVALMLAMEAIIESGvELKGDIYFQSVI--EEE 169
Cdd:PRK07338 96 LLTGHMDTVfPAD-------HPF--QTLswldDGTLNGPGVADMKGG-IVVMLAALLAFERS-PLADKLGYDVLInpDEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 170 SGGAGT---LATILRGYKAdgVIIPEPTnmkfFPK------QQGSMWFRLHVKGKAAHGGTRY-EGVSAIEKSMFVIDHL 239
Cdd:PRK07338 165 IGSPASaplLAELARGKHA--ALTYEPA----LPDgtlagaRKGSGNFTIVVTGRAAHAGRAFdEGRNAIVAAAELALAL 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446734265 240 RKLEEKRNG------RItdplfkgipipipinigkiEGGSWPSSVPDSLILegRYGIAPNEtiEAAKEEFESWIAEL 310
Cdd:PRK07338 239 HALNGQRDGvtvnvaKI-------------------DGGGPLNVVPDNAVL--RFNIRPPT--PEDAAWAEAELKKL 292
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
91-173 |
2.44e-08 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 55.55 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 91 GDGKSMIL-NGHIDVVPEGDvNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESgvELKGDIYFQSVIEEE 169
Cdd:PRK08554 60 GEGKPKLLfMAHFDVVPVNP-EEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKE--PLNGKVIFAFTGDEE 136
|
....
gi 446734265 170 SGGA 173
Cdd:PRK08554 137 IGGA 140
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
23-190 |
7.64e-08 |
|
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: 54.24 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 23 LTRLIQEKSVS------GDESGAQAIVIEKLRELGLD-LDIWEPSfskmkDHPYFVSPRTSFSDSPNIVatlkgsgdgks 95
Cdd:cd05680 4 LFELLRIPSVSadpahkGDVRRAAEWLADKLTEAGFEhTEVLPTG-----GHPLVYAEWLGAPGAPTVL----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 96 miLNGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFqsVIE-EESGGAG 174
Cdd:cd05680 68 --VYGHYDVQPPDPLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKF--LIEgEEEIGSP 143
|
170 180
....*....|....*....|
gi 446734265 175 TLATILRGYK----ADGVII 190
Cdd:cd05680 144 SLPAFLEENAerlaADVVLV 163
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
7-194 |
8.00e-07 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 50.90 E-value: 8.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 7 QVCDYIESHEEESVKFLTRLIQEKSVS------GDESGAQAIVIEKLRELGLDldiwEPSFSKMKDHPyfvsprtsfsds 80
Cdd:PRK08201 4 QVEAYLRERREAHLEELKEFLRIPSISalsehkEDVRKAAEWLAGALEKAGLE----HVEIMETAGHP------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 81 pnIVATLKGSGDGKSMIL-NGHIDVVPEGDVNQWDHHPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGD 159
Cdd:PRK08201 68 --IVYADWLHAPGKPTVLiYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVN 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446734265 160 IYFqsVIE-EESGGAGTLATILRGYK----ADGVIIPEPT 194
Cdd:PRK08201 146 VKF--CIEgEEEIGSPNLDSFVEEEKdklaADVVLISDTT 183
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
100-229 |
1.08e-06 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 50.55 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 100 GHIDVV-PEGDVNQWdhhPYSGEkiGNRIYGRGTTDMKGGNVALMLAMEAIIESGVELKGDIYFQSVIEEESGGAGTLAT 178
Cdd:PRK07473 82 GHMDTVhPVGTLEKL---PWRRE--GNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFTPDEEVGTPSTRDL 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446734265 179 I-LRGYKADGVIIPEP--TNMKFFPKQQGSMWFRLHVKGKAAHGGTRY-EGVSAI 229
Cdd:PRK07473 157 IeAEAARNKYVLVPEPgrPDNGVVTGRYAIARFNLEATGRPSHAGATLsEGRSAI 211
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
1-174 |
1.32e-05 |
|
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: 47.11 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 1 MKQLKKQVCDYIESHEEESVKFLTRLIQEKsvsgdesgaqaiVIEKLRELGLDldiwepsfSKMKDHPyfvsprtSFSDS 80
Cdd:cd05679 7 LAELARRVAVPTESQEPARKPELRAYLDQE------------MRPRFERLGFT--------VHIHDNP-------VAGRA 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 81 PNIVATLKGSGDGKSMILNGHIDVVPeGDVNQWDH--HPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIES-GVELK 157
Cdd:cd05679 60 PFLIAERIEDPSLPTLLIYGHGDVVP-GYEGRWRDgrDPWTVTVWGERWYGRGTADNKGQHSINMAALRQVLEArGGKLG 138
|
170
....*....|....*..
gi 446734265 158 GDIYFQSVIEEESGGAG 174
Cdd:cd05679 139 FNVKFLIEMGEEMGSPG 155
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
100-213 |
1.71e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 46.83 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 100 GHIDVVPeGDVNQWDH--HPYSGEKIGNRIYGRGTTDMKGGNVALMLAMEAIIES-----GVELKgdiyfqSVIE--EES 170
Cdd:PRK07079 92 GHGDVVR-GYDEQWREglSPWTLTEEGDRWYGRGTADNKGQHTINLAALEQVLAArggrlGFNVK------LLIEmgEEI 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446734265 171 GGAGtLATILRGYK----------ADG--VIIPEPTnmkFFPKQQGSMWFRLHVK 213
Cdd:PRK07079 165 GSPG-LAEVCRQHRealaadvliaSDGprLSAERPT---LFLGSRGAVNFRLRVN 215
|
|
| M28_like |
cd03877 |
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ... |
80-171 |
2.12e-04 |
|
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Some proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution.
Pssm-ID: 349874 [Multi-domain] Cd Length: 206 Bit Score: 42.23 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 80 SPNIVATLKGSGD-GKSMILNGHidvvpegdvnqWDHHPYSGEKIGNRIYgRGTTDMKGGnVALMLAMEAIIESGVELKG 158
Cdd:cd03877 1 GHNVVGVLEGSDLpDETIVIGAH-----------YDHLGIGGGDSGDKIY-NGADDNASG-VAAVLELARYFAKQKTPKR 67
|
90
....*....|...
gi 446734265 159 DIYFQSVIEEESG 171
Cdd:cd03877 68 SIVFAAFTAEEKG 80
|
|
| M28_like_PA |
cd05660 |
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ... |
34-171 |
6.37e-04 |
|
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.
Pssm-ID: 349910 [Multi-domain] Cd Length: 290 Bit Score: 41.58 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 34 GDESGAQAI--VIEKLRELGLdldiwEPSFSK---MKDHPyFVSPRtSFSDSPNIVATLKGSG-DGKSMILNGHidvvpe 107
Cdd:cd05660 15 GSEGEKKTVdyLAEQFKELGL-----KPAGSDgsyLQAVP-LVSKI-EYSTSHNVVAILPGSKlPDEYIVLSAH------ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446734265 108 gdvnqWDHHPYSGEKIGNRIYgRGTTDmKGGNVALMLAM-EAIIESGVELKGDIYFQSVIEEESG 171
Cdd:cd05660 82 -----WDHLGIGPPIGGDEIY-NGAVD-NASGVAAVLELaRVFAAQDQRPKRSIVFLAVTAEEKG 139
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
40-395 |
8.99e-04 |
|
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: 41.05 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 40 QAIVIEKLRELGLDldiwepsfskmkdhpyfvsPRTsFSDSPNIVATLKGSGDGKSMILNGHIDVVP--EgdvnQWDHHP 117
Cdd:cd03886 22 AARIAEELRELGLE-------------------VRT-GVGGTGVVATLKGGGPGPTVALRADMDALPiqE----ETGLPF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 118 YSGEKignriygrGTTDMKG--GNVALML-AMEAIIESGVELKGDI--YFQSViEEESGGAGTL--ATILRGYKAD---- 186
Cdd:cd03886 78 ASKHE--------GVMHACGhdGHTAMLLgAAKLLAERRDPLKGTVrfIFQPA-EEGPGGAKAMieEGVLENPGVDaafg 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 187 ---------GVIIPEPTNMkffpkQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHL-----RKLEEKRNGRITD 252
Cdd:cd03886 149 lhvwpglpvGTVGVRSGAL-----MASADEFEITVKGKGGHGASPHLGVDPIVAAAQIVLALqtvvsRELDPLEPAVVTV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 253 PLFkgipipipinigkiEGGSWPSSVPDSLILEGRYGIAPNETIEAAKEEFESW---IAELHDVDnwfvenpVEVEWFGA 329
Cdd:cd03886 224 GKF--------------HAGTAFNVIPDTAVLEGTIRTFDPEVREALEARIKRLaegIAAAYGAT-------VELEYGYG 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 330 RWVpgeLEENHELITTLQHNFVEIEGKEP--MIEASPWGTDGGLFTQIsgVPTIVF--GPGETKVAHYPN 395
Cdd:cd03886 283 YPA---VINDPELTELVREAAKELLGEEAvvEPEPVMGSEDFAYYLEK--VPGAFFwlGAGEPDGENPGL 347
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
32-229 |
1.04e-03 |
|
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: 41.17 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 32 VSGDESGAQAIVIEKLRELGLdldiwepsfskmkdhPYFVSPRTSFsdspniVATLKGSGDGKSMILNGHIDVVPegdVN 111
Cdd:cd08019 14 LSLKEERTSKRIKEELDKLGI---------------PYVETGGTGV------IATIKGGKAGKTVALRADIDALP---VE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 112 QWDHHPYSGEKIGNriygrgttdMKG----GNVALML-AMEAIIESGVELKGDI--YFQSViEEESGGAGTLATILRGYK 184
Cdd:cd08019 70 ECTDLEYKSKNPGL---------MHAcghdGHTAMLLgAAKILNEIKDTIKGTVklIFQPA-EEVGEGAKQMIEEGVLED 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446734265 185 ADGVI-------IPEPT-NMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAI 229
Cdd:cd08019 140 VDAVFgihlwsdVPAGKiSVEAGPRMASADIFKIEVKGKGGHGSMPHQGIDAV 192
|
|
| FrvX |
COG1363 |
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and ... |
17-103 |
2.57e-03 |
|
Putative aminopeptidase FrvX [Amino acid transport and metabolism, Carbohydrate transport and metabolism];
Pssm-ID: 440974 [Multi-domain] Cd Length: 353 Bit Score: 39.72 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 17 EESVKFLTRLIQEKSVSGDESGAQAIVIEKLRELGLdldiwEPSFSKMKdhpyfvsprtsfsdspNIVATLKGSGDGKSM 96
Cdd:COG1363 2 DYLLELLKELTEAPGPSGFEDEVREYIKEELEPLGD-----EVETDRLG----------------NLIATKKGKGDGPKV 60
|
....*..
gi 446734265 97 ILNGHID 103
Cdd:COG1363 61 MLAAHMD 67
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
81-186 |
9.76e-03 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 37.96 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446734265 81 PNIVATLKG-SGDGKSMILNGHIDVVPEGDVNQWDHHPY--------SGEKIgnrIYGRGTTDMKGgnvALMLAMEAI-- 149
Cdd:PRK09104 69 PMVVAHHEGpTGDAPHVLFYGHYDVQPVDPLDLWESPPFepriketpDGRKV---IVARGASDDKG---QLMTFVEACra 142
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446734265 150 ---IESGVELKGDIYFQSviEEESGGAGtLATILRGYKAD 186
Cdd:PRK09104 143 wkaVTGSLPVRVTILFEG--EEESGSPS-LVPFLEANAEE 179
|
|
| |
