|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06915 |
PRK06915 |
peptidase; |
3-424 |
0e+00 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 856.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 3 MQDIERKVIEWLDQHSAKAIRLLKRLIGEKSTLGSEFNAQAVVLEKLRQFHMDIDVWEPSIKQLKQHPYFKSNRSDFHES 82
Cdd:PRK06915 1 MEQLKKQICDYIESHEEEAVKLLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLDIWEPSFKKLKDHPYFVSPRTSFSDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 83 PNIVAKKTGAGGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDV 162
Cdd:PRK06915 81 PNIVATLKGSGGGKSMILNGHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 163 LFQSVVDEECGGAGTLSAIMRGYRADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQ 242
Cdd:PRK06915 161 IFQSVIEEESGGAGTLAAILRGYKADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 243 ELEKVRNARISDPLYDNIPIPVPVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKDLEYHDEWFKRH 322
Cdd:PRK06915 241 KLEEKRNDRITDPLYKGIPIPIPINIGKIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAELNDVDEWFVEH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 323 PVQVEWFGAQWLPNDLPDDHPLISVLQSAYQKMKQTEPIIEASPWGTDGGLLYHAGDTPVIVFGPGETKTAHQANEYIEV 402
Cdd:PRK06915 321 PVEVEWFGARWVPGELEENHPLMTTLEHNFVEIEGNKPIIEASPWGTDGGLLTQIAGVPTIVFGPGETKVAHYPNEYIEV 400
|
410 420
....*....|....*....|..
gi 16079029 403 EAMIESAKIIALFVMDWCGLHT 424
Cdd:PRK06915 401 DKMIAAAKIIALTLLDWCEVKK 422
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
23-421 |
0e+00 |
|
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: 608.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 23 RLLKRLIGEKSTLGSEFNAQAVVLEKLRQFHMDIDVWEPSIKQLKQHPYFKSNRSDFHESPNIVAKKTGAG-GGRSLILN 101
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDRWEIDVEKLKHHPGFSPVAVDYAGAPNVVGTHRPRGeTGRSLILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 102 GHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDEECGGAGTLSAI 181
Cdd:cd03895 81 GHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEECTGNGALAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 182 MRGYRADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELEKVRNAR-ISDPLYDNI 260
Cdd:cd03895 161 MRGYRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEREWNARkKSHPHFSDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 261 PIPVPVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKDLEYHDEWFKRHPVQVEWFGAQWLPNDLPD 340
Cdd:cd03895 241 PHPINFNIGKIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVADAAATDPWLSNHPPEVEWNGFQAEGYVLEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 341 DHPLISVLQSAYQKMKQTEPIIEASPWGTDGGLLYHAGDTPVIVFGPGEtKTAHQANEYIEVEAMIESAKIIALFVMDWC 420
Cdd:cd03895 321 GSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGDIPALCYGPGS-RDAHGFDESVDLESLRKITKTIALFIAEWC 399
|
.
gi 16079029 421 G 421
Cdd:cd03895 400 G 400
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
22-411 |
4.66e-175 |
|
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: 494.23 E-value: 4.66e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 22 IRLLKRLIGEKS---TLGSEFNAQAVVLEKLRQFHMDIDVWEPSIKQLKQHPyfksnrsdfhespNIVAKKTGAGGGRSL 98
Cdd:TIGR01910 1 VELLKDLISIPSvnpPGGNEETIANYIKDLLREFGFSTDVIEITDDRLKVLG-------------KVVVKEPGNGNEKSL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 99 ILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDEECGGAGTL 178
Cdd:TIGR01910 68 IFNGHYDVVPAGDLELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGEAGTL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 179 SAIMRGYR--ADGALIPEPTN-MKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELEKVRNARISdp 255
Cdd:TIGR01910 148 YLLQRGYFkdADGVLIPEPSGgDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEEHIYARNS-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 256 lYDNIPIPVPVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKDLEYHDEWFKRHPVQVEWFGaqwlP 335
Cdd:TIGR01910 226 -YGFIPGPITFNPGVIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSDGWLYENEPVVKWSG----P 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16079029 336 NDLPDDHPLISVLQSAYQKMKQTEPIIEASPWGTDGGLLYHAGdTPVIVFGPGETKTAHQANEYIEVEAMIESAKI 411
Cdd:TIGR01910 301 NETPPDSRLVKALEAIIKKVRGIEPEVLVSTGGTDARFLRKAG-IPSIVYGPGDLETAHQVNEYISIKNLVESTKV 375
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
1-422 |
1.07e-119 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 355.46 E-value: 1.07e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 1 MRMQDIERKVIEWLDQHSAKAIRLLKRLIGEKSTLGSEFNAQAVVLEKLRQFHMDIDVWEPSIKQLKQHPYFKSNRSDFH 80
Cdd:PRK06837 2 MLTPDLTQRILAAVDAGFDAQVAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDRWSIDPDDLKSHPGAGPVEIDYS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 81 ESPNIVAKKTGAGG-GRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLK 159
Cdd:PRK06837 82 GAPNVVGTYRPAGKtGRSLILQGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 160 GDVLFQSVVDEECGGAGTLSAIMRGYRADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVIT 239
Cdd:PRK06837 162 ARVHFQSVIEEESTGNGALSTLQRGYRADACLIPEPTGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 240 AIQELEKVRNAR-ISDPLYDNIPIPVPVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKDLEYHDEW 318
Cdd:PRK06837 242 ALRELEAEWNARkASDPHFEDVPHPINFNVGIIKGGDWASSVPAWCDLDCRIAIYPGVTAADAQAEIEACLAAAARDDRF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 319 FKRHPVQVEWFGAQWLPNDLPDDHPLISVLQSAYQKMKQTEPIIEASPWGTDG---GLLYhagDTPVIVFGPgETKTAHQ 395
Cdd:PRK06837 322 LSNNPPEVVWSGFLAEGYVLEPGSEAEAALARAHAAVFGGPLRSFVTTAYTDTrfyGLYY---GIPALCYGP-SGEGIHG 397
|
410 420
....*....|....*....|....*..
gi 16079029 396 ANEYIEVEAMIESAKIIALFVMDWCGL 422
Cdd:PRK06837 398 FDERVDLESVRKVTKTIALFVAEWCGV 424
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
9-421 |
2.17e-112 |
|
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: 335.32 E-value: 2.17e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 9 KVIEWLDQHSAKAIRLLKRLIGEKSTLGSEFNAQAVVLEKLRQFHMDIDVWEPSikqlkqhpyfksnrsdfHESPNIVAK 88
Cdd:COG0624 2 AVLAAIDAHLDEALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVP-----------------PGRPNLVAR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 89 KTGAGGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVV 168
Cdd:COG0624 65 RPGDGGGPTLLLYGHLDVVPPGDLELWTSDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 169 DEECGGAGTLSAI---MRGYRADGALIPEPTN-MKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQEL 244
Cdd:COG0624 145 DEEVGSPGARALVeelAEGLKADAAIVGEPTGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 245 EKVRNArisDPLYDnipiPVPVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKDLEYHDEwfkrhpV 324
Cdd:COG0624 225 EFDGRA---DPLFG----RTTLNVTGIEGGTAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPGVE------V 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 325 QVEWFGAQWLPNDLPDDHPLISVLQSAYQKMKQTEPIIEASPWGTDGGLLYHAGDTPVIVFGPGETKTAHQANEYIEVEA 404
Cdd:COG0624 292 EVEVLGDGRPPFETPPDSPLVAAARAAIREVTGKEPVLSGVGGGTDARFFAEALGIPTVVFGPGDGAGAHAPDEYVELDD 371
|
410
....*....|....*..
gi 16079029 405 MIESAKIIALFVMDWCG 421
Cdd:COG0624 372 LEKGARVLARLLERLAG 388
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
9-420 |
5.98e-86 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 268.83 E-value: 5.98e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 9 KVIEWLDQHSAKAIRLLKRLIGEKSTLGSEFN---AQAVVLEKLRQFHMDIDVWEPsikqlkqhpyfksnrsdFHESPNI 85
Cdd:PRK08596 3 QLLEQIELRKDELLELLKTLVRFETPAPPARNtneAQEFIAEFLRKLGFSVDKWDV-----------------YPNDPNV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 86 VAKKTGAGGG--RSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVL 163
Cdd:PRK08596 66 VGVKKGTESDayKSLIINGHMDVAEVSADEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 164 FQSVVDEECGGAGTLSAIMRGYRADGALIPEPTNMKlfIKQQGSM---WfrITVKGLSA-HGGTRYE---------GVSA 230
Cdd:PRK08596 146 FQSVIGEEVGEAGTLQCCERGYDADFAVVVDTSDLH--MQGQGGVitgW--ITVKSPQTfHDGTRRQmihaggglfGASA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 231 IEKSMHVITAIQELEKVRNARISDPLYDniPIPVPVNIGTISGGAWPSSVADrvviEGRCGIA----PHEKPEAVKLELE 306
Cdd:PRK08596 222 IEKMMKIIQSLQELERHWAVMKSYPGFP--PGTNTINPAVIEGGRHAAFIAD----ECRLWITvhfyPNETYEQVIKEIE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 307 NWLKDLEYHDEWFKRHPVQVEWFGAQWLPN--------DLPDDHPLISVLQSAYQKMKQTEPIIEASPWGTDGGLLYHAG 378
Cdd:PRK08596 296 EYIGKVAAADPWLRENPPQFKWGGESMIEDrgeifpslEIDSEHPAVKTLSSAHESVLSKNAILDMSTTVTDGGWFAEFG 375
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 16079029 379 dTPVIVFGPGETKTAHQANEYIEVEAMIESAKIIALFVMDWC 420
Cdd:PRK08596 376 -IPAVIYGPGTLEEAHSVNEKVEIEQLIEYTKVITAFIYEWC 416
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
23-416 |
1.41e-85 |
|
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: 265.70 E-value: 1.41e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 23 RLLKRLIGEKSTLGSEFNAQAVVLEKLRQFHMDIDvwepsikqlkqhpyfksnRSDFHESPNIVAKKtGAGGGRSLILNG 102
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIE------------------STIVEGRGNLVATV-GGGDGPVLLLNG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 103 HIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDEECGGAGTLSAIM 182
Cdd:cd08659 62 HIDTVPPGDGDKWSFPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSDGARALLE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 183 RGY--RADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELEKVRNArisDPLYDni 260
Cdd:cd08659 142 AGYadRLDALIVGEPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPA---HPLLG-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 261 piPVPVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKDLEYHdewfkrhpVQVEWFGAQWLPNDLPD 340
Cdd:cd08659 217 --PPTLNVGVINGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAK--------LTVEVSLDGDPPFFTDP 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16079029 341 DHPLISVLQSAYQKMKQTEPIIEASPWgTDGGLLYHAGDTPVIVFGPGETKTAHQANEYIEVEAMIESAKIIALFV 416
Cdd:cd08659 287 DHPLVQALQAAARALGGDPVVRPFTGT-TDASYFAKDLGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
83-420 |
2.53e-67 |
|
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: 219.27 E-value: 2.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 83 PNIVAKKTGAGGGRSLILNGHIDVVpegSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALeaLHACDVKLKGDV 162
Cdd:cd08013 56 PSVVGVVRGTGGGKSLMLNGHIDTV---TLDGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAAL--ADAKEAGLRGDV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 163 LFQSVVDEECGGAGTLSAIMRGYRADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQ 242
Cdd:cd08013 131 ILAAVADEEDASLGTQEVLAAGWRADAAIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 243 ELEKVRNARISDPLYDnipiPVPVNIGTISGGAWPSSVADR--VVIEGRcgIAPHEKPEAVKLELENWLKDLEYHDEWFK 320
Cdd:cd08013 211 EYQQELPERPVDPLLG----RASVHASLIKGGEEPSSYPARctLTIERR--TIPGETDESVLAELTAILGELAQTVPNFS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 321 RHPVQVEWFGAqwlPNDLPDDHPLISVLQSAYQKMKQTEPIIEASPWGTDGGLLYHAGdTPVIVFGPGETKtAHQANEYI 400
Cdd:cd08013 285 YREPRITLSRP---PFEVPKEHPFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAG-IPSVVFGPSGAG-LHAKEEWV 359
|
330 340
....*....|....*....|
gi 16079029 401 EVEAMIESAKIIALFVMDWC 420
Cdd:cd08013 360 DVESIRQLREVLSAVVREFC 379
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
81-416 |
3.98e-61 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 203.30 E-value: 3.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 81 ESPNIVAKKtgAGGGRSLILNGHIDVVPEGSVkdWK-YEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALhacDVKLK 159
Cdd:PRK08651 62 PRPNLIARR--GSGNPHLHFNGHYDVVPPGEG--WSvNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERL---DPAGD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 160 GDVLFQSVVDEECGGAGT--LSAIMRGyRADGALIPEPTNM-KLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMH 236
Cdd:PRK08651 135 GNIELAIVPDEETGGTGTgyLVEEGKV-TPDYVIVGEPSGLdNICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 237 VitaIQELEKVRNARISDPLYDNIPIPVP-VNIG--TISGGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLkdle 313
Cdd:PRK08651 214 I---AERLKSSLSTIKSKYEYDDERGAKPtVTLGgpTVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDELEALL---- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 314 yhDEWFKRHPVQVEW----FGAqwlPNDLPDDHPLISVLQSAYQKMKQTEPIIEASPWGTDGGLLYHAGdTPVIVFGPGE 389
Cdd:PRK08651 287 --DEVAPELGIEVEFeitpFSE---AFVTDPDSELVKALREAIREVLGVEPKKTISLGGTDARFFGAKG-IPTVVYGPGE 360
|
330 340
....*....|....*....|....*..
gi 16079029 390 TKTAHQANEYIEVEAMIESAKIIALFV 416
Cdd:PRK08651 361 LELAHAPDEYVEVKDVEKAAKVYEEVL 387
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
72-416 |
1.98e-59 |
|
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: 198.20 E-value: 1.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 72 FKSNRSDFHES--PNIVAKKtGAGGGRSLILNGHIDVVP-EGsvKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFAL 148
Cdd:cd03894 33 VKSRRVPVPEGgkANLLATL-GPGGEGGLLLSGHTDVVPvDG--QKWSSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 149 EALHAcdVKLKGDVLFQSVVDEE--CGGAGTLSAIMRGY--RADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTR 224
Cdd:cd03894 110 PRLLA--AKLRKPLHLAFSYDEEvgCLGVRHLIAALAARggRPDAAIVGEPTSLQPVVAHKGIASYRIRVRGRAAHSSLP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 225 YEGVSAIEKSMHVITAIQEL-EKVRNARISDPLYdnipIPVP-VNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAVK 302
Cdd:cd03894 188 PLGVNAIEAAARLIGKLRELaDRLAPGLRDPPFD----PPYPtLNVGLIHGGNAVNIVPAECEFEFEFRPLPGEDPEAID 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 303 LELENWLKDLEYHDEwfkrHPVQVEWFGAqWLPNDLPDDHPLISVLQSAYQKMKqtepiIEASPWGTDGGLLYHAGdTPV 382
Cdd:cd03894 264 ARLRDYAEALLEFPE----AGIEVEPLFE-VPGLETDEDAPLVRLAAALAGDNK-----VRTVAYGTEAGLFQRAG-IPT 332
|
330 340 350
....*....|....*....|....*....|....
gi 16079029 383 IVFGPGETKTAHQANEYIEVEAMIESAKIIALFV 416
Cdd:cd03894 333 VVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLI 366
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
99-418 |
4.19e-58 |
|
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: 193.33 E-value: 4.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 99 ILNGHIDVVPEGSVKDWKYEPyqavEENGKIYGRGSTDMKGGNTALLFALEALHACDVKlKGDVLFQSVVDEECGGAGTL 178
Cdd:pfam01546 1 LLRGHMDVVPDEETWGWPFKS----TEDGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEGGMGGAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 179 SAI----MRGYRAD---GALIPEPTNM------KLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELE 245
Cdd:pfam01546 76 ALIedglLEREKVDavfGLHIGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 246 kvrnARISDPLyDNIPIPVpVNIGTISGGawPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKDLEyhDEWFKRHPVQ 325
Cdd:pfam01546 156 ----SRNVDPL-DPAVVTV-GNITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIA--AAYGVKVEVE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 326 VEWFGAQWLPNdlpdDHPLISVLQSAYQKMKQTEPIIEASPW--GTDGGLLYHAGDTPVIVFGPGEtKTAHQANEYIEVE 403
Cdd:pfam01546 226 YVEGGAPPLVN----DSPLVAALREAAKELFGLKVELIVSGSmgGTDAAFFLLGVPPTVVFFGPGS-GLAHSPNEYVDLD 300
|
330
....*....|....*
gi 16079029 404 AMIESAKIIALFVMD 418
Cdd:pfam01546 301 DLEKGAKVLARLLLK 315
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
22-416 |
7.60e-58 |
|
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: 193.76 E-value: 7.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 22 IRLLKRLIGEKST----LGSEfNAQAVVLEKLRQFHMDIDVWEPSikqlkqhpyfksnrsdfHESPNIVAKKTGAGGGRS 97
Cdd:cd08011 1 VKLLQELVQIPSPnppgDNTS-AIAAYIKLLLEDLGYPVELHEPP-----------------EEIYGVVSNIVGGRKGKR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 98 LILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDEECGG-AG 176
Cdd:cd08011 63 LLFNGHYDVVPAGDGEGWTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGrAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 177 TLSAIMRG-YRADGALIPEPTNMK-LFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELEKVrnarisd 254
Cdd:cd08011 143 TKYLLEKVrIKPNDVLIGEPSGSDnIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELEKT------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 255 plydnipipvpVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKDLEyhdewfkrhpvQVEWFGAQWL 334
Cdd:cd08011 216 -----------VNPGVIKGGVKVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSIE-----------EVSFEIKSFY 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 335 -PNDLPDDHPLISVLQSAYQKMKQTEPIIEASPWGTDGGLLYHAGdTPVIVFGPGETKTAHQANEYIEVEAMIESAKIIA 413
Cdd:cd08011 274 sPTVSNPDSEIVKKTEEAITEVLGIRPKEVISVGASDARFYRNAG-IPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVHA 352
|
...
gi 16079029 414 LFV 416
Cdd:cd08011 353 LVA 355
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
84-401 |
9.61e-47 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 165.06 E-value: 9.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 84 NIVAKKTGAGGGRS------------LILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEAL 151
Cdd:PRK08588 36 GIESKIVKVNDGRAnlvaeigsgspvLALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 152 HACDVKLKGDVLFQSVVDEECGGAGtlSAIMR--GY--RADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEG 227
Cdd:PRK08588 116 KEQGQLLNGTIRLLATAGEEVGELG--AKQLTekGYadDLDALIIGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 228 VSAIEksmHVITAIQELEKvrnarisdpLYDNIPI------PVPVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAV 301
Cdd:PRK08588 194 VNAID---PLLEFYNEQKE---------YFDSIKKhnpylgGLTHVVTIINGGEQVNSVPDEAELEFNIRTIPEYDNDQV 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 302 KLELENWLKDLEyhdewfKRHPVQVEW-FGAQWLPNDLPDDHPLISVLQSAYQKMKQTEPIIEASPWGTDGG-LLYHAGD 379
Cdd:PRK08588 262 ISLLQEIINEVN------QNGAAQLSLdIYSNHRPVASDKDSKLVQLAKDVAKSYVGQDIPLSAIPGATDASsFLKKKPD 335
|
330 340
....*....|....*....|..
gi 16079029 380 TPVIVFGPGETKTAHQANEYIE 401
Cdd:PRK08588 336 FPVIIFGPGNNLTAHQVDEYVE 357
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
84-413 |
2.93e-43 |
|
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: 155.36 E-value: 2.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 84 NIVAKKtGAGGGRSLILNGHIDVVPEGSVKdWKYEPYQAVEENGKIYGRGSTDMKGgntALLFALEALHACDV-KLKGDV 162
Cdd:TIGR01892 48 NLVAVI-GPSGAGGLALSGHTDVVPYDDAA-WTRDPFRLTEKDGRLYGRGTCDMKG---FLACALAAAPDLAAeQLKKPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 163 LFQSVVDEECGGAGTLSAIMRGY-RADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIeksMHVITAI 241
Cdd:TIGR01892 123 HLALTADEEVGCTGAPKMIEAGAgRPRHAIIGEPTRLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAI---FRAGRFL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 242 QELEKVRNARISDPLYDNIPIPVP-VNIGTISGGAWPSSVAD--RVVIEGRCgiAPHEKPEAVKLELENwlkdleyhdew 318
Cdd:TIGR01892 200 QRLVHLADTLLREDLDEGFTPPYTtLNIGVIQGGKAVNIIPGacEFVFEWRP--IPGMDPEELLQLLET----------- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 319 fKRHPVQVEW--FGAQW--LPND----LPDDHPLISVLQsayqkmKQTEPIIEASPWGTDGGLLYHAGdTPVIVFGPGET 390
Cdd:TIGR01892 267 -IAQALVRDEpgFEVQIevVSTDpgvnTEPDAELVAFLE------ELSGNAPEVVSYGTEAPQFQELG-AEAVVCGPGDI 338
|
330 340
....*....|....*....|...
gi 16079029 391 KTAHQANEYIEVEAMIESAKIIA 413
Cdd:TIGR01892 339 RQAHQPDEYVEIEDLVRCRAVLA 361
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
93-421 |
3.82e-43 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 155.87 E-value: 3.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 93 GGGRSLIL-NGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDEE 171
Cdd:PRK13004 66 GHGKKLIAfDAHIDTVGIGDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 172 -CGGAGTLSAIMR-GYRADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELEkvrn 249
Cdd:PRK13004 146 dCDGLCWRYIIEEdKIKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELN---- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 250 arisDPLYDNiP-----IPVPVNIGTISGGAwpSSVAD--RVVIEGRcgIAPHEKPEAVKLELENWLKDLEYHDE----W 318
Cdd:PRK13004 222 ----PNLKED-PflgkgTLTVSDIFSTSPSR--CAVPDscAISIDRR--LTVGETWESVLAEIRALPAVKKANAKvsmyN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 319 FKR-----HPVQVEWFGAQWLpndLPDDHPLISVLQSAYQKMKQTEPIIEASPWGTDGglLYHAGD--TPVIVFGPGETK 391
Cdd:PRK13004 293 YDRpsytgLVYPTECYFPTWL---YPEDHEFVKAAVEAYKGLFGKAPEVDKWTFSTNG--VSIAGRagIPTIGFGPGKEP 367
|
330 340 350
....*....|....*....|....*....|
gi 16079029 392 TAHQANEYIEVEAMIESAKIIALFVMDWCG 421
Cdd:PRK13004 368 LAHAPNEYTWKEQLVKAAAMYAAIPKSLLK 397
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
77-418 |
1.90e-42 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 154.92 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 77 SDFHESPNIVAKKTGAGGGRSLILNGHIDVVPEGsvKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDV 156
Cdd:PRK13013 66 SETYPRWNLVARRQGARDGDCVHFNSHHDVVEVG--HGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYP 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 157 KLKGDVLFQSVVDEECGGAGTLSAIM-RGY----RADGALIPEPTNM-KLFIKQQGSMWFRITVKGLSAHGGTRYEGVSA 230
Cdd:PRK13013 144 DFAGSIEISGTADEESGGFGGVAYLAeQGRfspdRVQHVIIPEPLNKdRICLGHRGVWWAEVETRGRIAHGSMPFLGDSA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 231 IEksmHVITAIQELEKVRNarisdPLYDNIPIPVPV----------NIGTISGG---------AWPSS-VAD--RVVIEG 288
Cdd:PRK13013 224 IR---HMGAVLAEIEERLF-----PLLATRRTAMPVvpegarqstlNINSIHGGepeqdpdytGLPAPcVADrcRIVIDR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 289 RCGIapHEKPEAVKLELENWLKDLEYHDEWFK---RHPVQVewfgaqwLPNDLPDDHPLISVLQSAYQKMKQTEPIIEAS 365
Cdd:PRK13013 296 RFLI--EEDLDEVKAEITALLERLKRARPGFAyeiRDLFEV-------LPTMTDRDAPVVRSVAAAIERVLGRQADYVVS 366
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 16079029 366 PWGTDGGLLYHAGDTP-VIVFGPGETKTAHQANEYIEVEAMIESAKIIALFVMD 418
Cdd:PRK13013 367 PGTYDQKHIDRIGKLKnCIAYGPGILDLAHQPDEWVGIADMVDSAKVMALVLAD 420
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
90-407 |
1.82e-41 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 151.11 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 90 TGAGGGRSLILNGHIDVVP-EGSvkDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQsvV 168
Cdd:PRK07522 59 IGPADRGGIVLSGHTDVVPvDGQ--AWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFS--Y 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 169 DEE--CGGAGTLSAIM--RGYRADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQEL 244
Cdd:PRK07522 135 DEEvgCLGVPSMIARLpeRGVKPAGCIVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 245 -EKVRNARISDPLYDnipipVP---VNIGTISGGAWPSSVADR--VVIEGRCgiAPHEKPEAVKLELENWLKDlEYHDEW 318
Cdd:PRK07522 215 aDRLAAPGPFDALFD-----PPystLQTGTIQGGTALNIVPAEceFDFEFRN--LPGDDPEAILARIRAYAEA-ELLPEM 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 319 FKRHP-VQVEW---FGAQWLpnDLPDDHPLISVLQS----------AYqkmkqtepiieaspwGTDGGLLYHAGdTPVIV 384
Cdd:PRK07522 287 RAVHPeAAIEFeplSAYPGL--DTAEDAAAARLVRAltgdndlrkvAY---------------GTEAGLFQRAG-IPTVV 348
|
330 340
....*....|....*....|....*....
gi 16079029 385 FGPGETKTAHQANEYIEV------EAMIE 407
Cdd:PRK07522 349 CGPGSIEQAHKPDEFVELaqlaacEAFLR 377
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
83-418 |
2.27e-39 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 145.76 E-value: 2.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 83 PNIVAKKTGAGGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDV 162
Cdd:PRK13983 64 PNIVAKIPGGDGKRTLWIISHMDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 163 LFQSVVDEECGGAGTLSAIMRGYR-----ADGALIP---EPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKS 234
Cdd:PRK13983 144 GLAFVSDEETGSKYGIQYLLKKHPelfkkDDLILVPdagNPDGSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRAA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 235 MHVITAIQE-LEKVRNARisDPLYD-------------NIPipvpvNIGTISGgawpssvadRVVIEGRCGIAPHEKPEA 300
Cdd:PRK13983 224 ADFALELDEaLHEKFNAK--DPLFDppystfeptkkeaNVD-----NINTIPG---------RDVFYFDCRVLPDYDLDE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 301 VKLELENWLKDLEyhdewfKRHPVQVEWFGAQWL--PNDLPDDHPLISVLQSAYQKMKQtepiIEASPWGTDGG----LL 374
Cdd:PRK13983 288 VLKDIKEIADEFE------EEYGVKIEVEIVQREqaPPPTPPDSEIVKKLKRAIKEVRG----IEPKVGGIGGGtvaaFL 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 16079029 375 YHAGdTPVIVFGPGEtKTAHQANEYIEVEAMIESAKIIALFVMD 418
Cdd:PRK13983 358 RKKG-YPAVVWSTLD-ETAHQPNEYAKISNLIEDAKVFALLLLE 399
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
93-409 |
2.05e-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. 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: 134.86 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 93 GGGRSLIL-NGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALeALHACDVKL--KGDVLFQSVVD 169
Cdd:cd05649 49 GGGKKKILfDGHIDTVGIGNIDNWKFDPYEGYETDGKIYGRGTSDQKGGLASMVYAA-KIMKDLGLRdfAYTILVAGTVQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 170 EEC--GGAGTLSAIMRGYRADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELekv 247
Cdd:cd05649 128 EEDcdGVCWQYISKADKIKPDFVVSGEPTDGNIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQL--- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 248 rNARISDPLYDNIPIPVPVNIGTISGGAwpSSVAD--RVVIEGR---------CgIAPHEKPEAVKLELENWLKDLEYHD 316
Cdd:cd05649 205 -NPNFPEAPFLGRGTLTVTDIFSTSPSR--CAVPDscRISIDRRltvgetwegC-LEEIRALPAVKKYGDDVAVSMYNYD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 317 E--WFKRHpVQVEWFGAQWLpndLPDDHPLISVLQSAYQKMKQTEPIIEASPWGTDGglLYHAGDT--PVIVFGPGETKT 392
Cdd:cd05649 281 RpsYTGEV-YESERYFPTWL---LPEDHELVKALLEAYKALFGARPLIDKWTFSTNG--VSIMGRAgiPCIGFGPGAENQ 354
|
330
....*....|....*..
gi 16079029 393 AHQANEYIEVEAMIESA 409
Cdd:cd05649 355 AHAPNEYTWKEDLVRCA 371
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
83-417 |
2.53e-33 |
|
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: 128.48 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 83 PNIVAKKTGaGGGRSLILNGHIDVV-PEGSVKDWKYEpyqavEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGD 161
Cdd:cd03885 49 DHLIATFKG-TGGKRVLLIGHMDTVfPEGTLAFRPFT-----VDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 162 VLFQSVVDEECGGAGTLSAIMR-GYRADGALIPEPT--NMKLFIKQQGSMWFRITVKGLSAHGGTRYE-GVSAIEKSMHV 237
Cdd:cd03885 123 ITVLLNSDEEIGSPGSRELIEEeAKGADYVLVFEPAraDGNLVTARKGIGRFRLTVKGRAAHAGNAPEkGRSAIYELAHQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 238 ITAIQELekvrnariSDPlydniPIPVPVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKDLEYHDe 317
Cdd:cd03885 203 VLALHAL--------TDP-----EKGTTVNVGVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTLVPG- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 318 wfkrhpVQVEW-FGAQWLP-NDLPDDHPLISVLQSAYQKMKQTEPiIEASPWGTDGGLLYHAGdTPVI-VFGP-GetKTA 393
Cdd:cd03885 269 ------TSVELtGGLNRPPmEETPASRRLLARAQEIAAELGLTLD-WEATGGGSDANFTAALG-VPTLdGLGPvG--GGA 338
|
330 340
....*....|....*....|....
gi 16079029 394 HQANEYIEVEAMIESAKIIALFVM 417
Cdd:cd03885 339 HTEDEYLELDSLVPRIKLLARLLM 362
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
81-414 |
6.98e-33 |
|
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: 127.96 E-value: 6.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 81 ESPNIVAKKTGaGGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKG 160
Cdd:cd05650 56 IRPNIVAKIPG-GNDKTLWIISHLDTVPPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKY 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 161 DVLFQSVVDEECGGAGTLSAIMRGY----RADGALIPE---PTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEK 233
Cdd:cd05650 135 NFGLLFVADEEDGSEYGIQYLLNKFdlfkKDDLIIVPDfgtEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 234 SMHVITAIQELEKvRNARISDPLYD-------------NIPipvpvNIGTISGgawpssvadRVVIEGRCGIAPHEKPEA 300
Cdd:cd05650 215 ASNFALELDELLH-EKFDEKDDLFNppystfeptkkeaNVP-----NVNTIPG---------YDVFYFDCRVLPTYKLDE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 301 VKLELENWLKDLEYHDewfkRHPVQVEWFGAQWLPNDLPDDHPLISVLQSAYQKMKQtepiIEASPWGTDGGL---LYHA 377
Cdd:cd05650 280 VLKFVNKIISDFENSY----GAGITYEIVQKEQAPPATPEDSEIVVRLSKAIKKVRG----REAKLIGIGGGTvaaFLRK 351
|
330 340 350
....*....|....*....|....*....|....*..
gi 16079029 378 GDTPVIVFGPGEtKTAHQANEYIEVEAMIESAKIIAL 414
Cdd:cd05650 352 KGYPAVVWSTLD-ETAHQPNEYIRISHIVKDAKVFAE 387
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
20-410 |
6.72e-32 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 124.49 E-value: 6.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 20 KAIRLLKRLIGEKSTLGSEFNAQAVVLEKLRQFhmDIDVWEPSIKQLKqhpyfksnrsdfhespNIVAKktgagGGRSLI 99
Cdd:PRK08652 3 RAKELLKQLVKIPSPSGQEDEIALHIMEFLESL--GYDVHIESDGEVI----------------NIVVN-----SKAELF 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 100 LNGHIDVVPegsvkdWKYEPYqavEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFqsVVDEECGGAGTlS 179
Cdd:PRK08652 60 VEVHYDTVP------VRAEFF---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAF--VSDEEEGGRGS-A 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 180 AIMRGYRADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELEKVRNARISDPlydn 259
Cdd:PRK08652 128 LFAERYRPKMAIVLEPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPH---- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 260 IPIPVpvnigtISGGAWPSSVAD--RVVIEGRcgIAPHEKPEAVKLELENWLKDLEYHDEwfkrhpVQVEWFGaqWlpnD 337
Cdd:PRK08652 204 IGIQE------IIGGSPEYSIPAlcRLRLDAR--IPPEVEVEDVLDEIDPILDEYTVKYE------YTEIWDG--F---E 264
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16079029 338 LPDDHPLISVLQSAYqKMKQTEPIIEASPWGTDGGLLYHAGdTPVIVFGPGETKTAHQANEYIEVeAMIESAK 410
Cdd:PRK08652 265 LDEDEEIVQLLEKAM-KEVGLEPEFTVMRSWTDAINFRYNG-TKTVVWGPGELDLCHTKFERIDV-REVEKAK 334
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
21-413 |
8.24e-32 |
|
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: 123.92 E-value: 8.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 21 AIRLLKRLIGEKSTLGSEFNAQAVVLEKLRqfhmdidvwEPSIKQLKQhpyFKSNRSDFhespNIVAKKTGAGGGRSLiL 100
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGDFLAEYLE---------SLGFTVEKQ---PVENKDRF----NVYAYPGSSRQPRVL-L 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 101 NGHIDVVPegsvkdwKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDV--LFqsVVDEECGGAGTL 178
Cdd:cd05652 64 TSHIDTVP-------PFIPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLglLF--VVGEETGGDGMK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 179 SA---IMRGYRAdgALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELekvrnARISDP 255
Cdd:cd05652 135 AFndlGLNTWDA--VIFGEPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDA-----DLPSSE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 256 LYDnipiPVPVNIGTISGG----AWPSSVADRVVIegRCGIAPHEKPEAVKLELENWLKDLEYhdewfkrhpVQVEWFGa 331
Cdd:cd05652 208 LLG----PTTLNIGRISGGvaanVVPAAAEASVAI--RLAAGPPEVKDIVKEAVAGILTDTED---------IEVTFTS- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 332 QWLPNDLPDDHPLISVLQSAYqkmkqtepiieaspwGTDGGLLYhaGDTPVIVFGPGETKTAHQANEYIEVEAMIESA-- 409
Cdd:cd05652 272 GYGPVDLDCDVDGFETDVVAY---------------GTDIPYLK--GDHKRYLYGPGSILVAHGPDEAITVSELEEAVeg 334
|
....*.
gi 16079029 410 --KIIA 413
Cdd:cd05652 335 ykKLIL 340
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
20-411 |
9.25e-32 |
|
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: 123.57 E-value: 9.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 20 KAIRLLKRLIGEKSTLGSEFNAqAVVLEK-LRQfhmdidvWEPSIKQLKQHPYFKSnrSDFHESPnivakktgagggRSL 98
Cdd:cd05651 1 EAIELLKSLIATPSFSREEHKT-ADLIENyLEQ-------KGIPFKRKGNNVWAEN--GHFDEGK------------PTL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 99 ILNGHIDVVPegSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALeaLHACDV-KLKGDVLFQSVVDEECGGAGT 177
Cdd:cd05651 59 LLNSHHDTVK--PNAGWTKDPFEPVEKGGKLYGLGSNDAGASVVSLLATF--LHLYSEgPLNYNLIYAASAEEEISGKNG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 178 LSAIMRGY-RADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGtRYEGVSAIEKsmhvitAIQELEKVRNARIsdPL 256
Cdd:cd05651 135 IESLLPHLpPLDLAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAA-RNEGDNAIYK------ALDDIQWLRDFRF--DK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 257 YDNIPIPVPVNIGTISGGAWPSSVADR--VVIEGRcgIAPHEKPEAVKLELENWLK-DLEYHDEWFKrhpvqvewfgaqw 333
Cdd:cd05651 206 VSPLLGPVKMTVTQINAGTQHNVVPDSctFVVDIR--TTEAYTNEEIFEIIRGNLKsEIKPRSFRLN------------- 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16079029 334 lPNDLPDDHPLIsvlqsayQKMKQTEPIIEASPWGTDGGLLyhagDTPVIVFGPGETKTAHQANEYIEVEAMIESAKI 411
Cdd:cd05651 271 -SSAIPPDHPIV-------QAAIAAGRTPFGSPTLSDQALM----PFPSVKIGPGDSSRSHTADEFIELSEIEEGIDI 336
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
84-421 |
9.15e-31 |
|
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: 121.43 E-value: 9.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 84 NIVAKKTGAGGGRSLILNGHID-VVPEGsvkdwkyEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDV 162
Cdd:cd03896 43 NVVGRLRGTGGGPALLFSAHLDtVFPGD-------TPATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 163 LFQSVVDEEcgGAGTLSAIMR-----GYRADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKsmhV 237
Cdd:cd03896 116 VFAANVGEE--GLGDLRGARYllsahGARLDYFVVAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVA---M 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 238 ITAIQELEKvrnarisdpLYDNIPIPVPVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKDLEyhdE 317
Cdd:cd03896 191 AKLVEALYE---------WAAPYVPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPDAELADVQREVEAVVSKLA---A 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 318 WFKRHPVQVEWFGAQwlPN-DLPDDHPLISVLQSAYQKMKQTEpiiEASPWGTDGGLLYHAGdTPVIVFGPGETKTAHQA 396
Cdd:cd03896 259 KHLRVKARVKPVGDR--PGgEAQGTEPLVNAAVAAHREVGGDP---RPGSSSTDANPANSLG-IPAVTYGLGRGGNAHRG 332
|
330 340
....*....|....*....|....*
gi 16079029 397 NEYIEVEAMIESAKIIALFVMDWCG 421
Cdd:cd03896 333 DEYVLKDDMLKGAKAYLMLAAALCG 357
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
84-403 |
2.05e-30 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 120.70 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 84 NIVAKK-TGAGGgrsLILNGHIDVVP--EGSvkdWKYEPYQAVEENGKIYGRGSTDMKGgntALLFALEALHACDV-KLK 159
Cdd:PRK05111 62 NLLASLgSGEGG---LLLAGHTDTVPfdEGR---WTRDPFTLTEHDGKLYGLGTADMKG---FFAFILEALRDIDLtKLK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 160 GDVLFQSVVDEECG--GAGTLSAIMRgYRADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEkSMH- 236
Cdd:PRK05111 133 KPLYILATADEETSmaGARAFAEATA-IRPDCAIIGEPTSLKPVRAHKGHMSEAIRITGQSGHSSDPALGVNAIE-LMHd 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 237 VITAIQELEKVRNARISDPLYDnipIPVP-VNIGTISGGawpsSVADRvvIEGRC----------GIAPHekpeavklEL 305
Cdd:PRK05111 211 VIGELLQLRDELQERYHNPAFT---VPYPtLNLGHIHGG----DAPNR--ICGCCelhfdirplpGMTLE--------DL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 306 ENWLKdlEYHDEWFKRHPVQVE----WFGAQwlPNDLPDDHPLISVLqsayQKMKQTEPiiEASPWGTDGGLLYHAGdTP 381
Cdd:PRK05111 274 RGLLR--EALAPVSERWPGRITvaplHPPIP--GYECPADHQLVRVV----EKLLGHKA--EVVNYCTEAPFIQQLG-CP 342
|
330 340
....*....|....*....|..
gi 16079029 382 VIVFGPGETKTAHQANEYIEVE 403
Cdd:PRK05111 343 TLVLGPGSIEQAHQPDEYLELS 364
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
22-403 |
1.94e-28 |
|
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: 114.91 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 22 IRLLKRLIGEKSTLGSEFNAQAVVLEKLRQFHmdidvwepsikqlkqhpyFKSNRSDFHESPNIVAKKtgAGGGRSLILN 101
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALG------------------FTCERLEFGGVKNLWARR--GTGGPHLCFA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 102 GHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDEEcGGA--GTLS 179
Cdd:cd03891 61 GHTDVVPPGDLEGWSSDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEE-GPAidGTKK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 180 AI----MRGYRADGALIPEPTNMKLF---IK--QQGSMWFRITVKGLSAHGGtrYEgvsaieksmhvitaiqelEKVRNa 250
Cdd:cd03891 140 VLewlkARGEKIDYCIVGEPTSEKKLgdtIKigRRGSLNGKLTIKGKQGHVA--YP------------------HLADN- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 251 risdPLYDNIPIpvpvnIGTISGGAW--------PSSVadrVVIEGRCG-----IAPHE---------KPEAVKLELENW 308
Cdd:cd03891 199 ----PIHLLAPI-----LAELTATVLdegneffpPSSL---QITNIDVGngatnVIPGElkakfnirfNDEHTGESLKAR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 309 LKDLeyhdewFKRHPVQVEwfgAQWLPNDLP---DDHPLISVLQSAYQKMKQTEPIIEASPwGT-DGGLLYHAGdTPVIV 384
Cdd:cd03891 267 IEAI------LDKHGLDYD---LEWKLSGEPfltKPGKLVDAVSAAIKEVTGITPELSTSG-GTsDARFIASYG-CPVVE 335
|
410
....*....|....*....
gi 16079029 385 FGPgETKTAHQANEYIEVE 403
Cdd:cd03891 336 FGL-VNATIHKVNERVSVA 353
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
72-220 |
9.81e-25 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 104.78 E-value: 9.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 72 FKSNRSDFHESPNIVAKKTGagGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEAL 151
Cdd:PRK13009 37 FTCERMDFGDVKNLWARRGT--EGPHLCFAGHTDVVPPGDLEAWTSPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 152 HACDVKLKGDVLFQSVVDEEcGGA--GT---LSAIM-RGYRADGALIPEPTNMKLF---IK--QQGSMWFRITVKGLSAH 220
Cdd:PRK13009 115 VAAHPDHKGSIAFLITSDEE-GPAinGTvkvLEWLKaRGEKIDYCIVGEPTSTERLgdvIKngRRGSLTGKLTVKGVQGH 193
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
84-418 |
5.37e-23 |
|
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: 99.94 E-value: 5.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 84 NIVAKKTGAGGGRSLILNGHIDVVPEGSvkDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVL 163
Cdd:cd02697 62 NLIVRRRYGDGGRTVALNAHGDVVPPGD--GWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 164 FQSVVDEECGG-AGTLSAIMRGYRADGALIPEPTNMKLFIKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAI- 241
Cdd:cd02697 140 LHFTYDEEFGGeLGPGWLLRQGLTKPDLLIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALy 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 242 ---QELEKVRNA--RISDPLydnipipvpVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKDLEYHD 316
Cdd:cd02697 220 alnAQYRQVSSQveGITHPY---------LNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADAAASM 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 317 EWFkRHPVQVEWFGAQWLPndLPDDHPLISVLQS-AYQKMKQTEPIIeASPWGTDGGLLYHAGdTPVIVFGPGETKT--- 392
Cdd:cd02697 291 PGI-SVDIRRLLLANSMRP--LPGNAPLVEAIQThGEAVFGEPVPAM-GTPLYTDVRLYAEAG-IPGVIYGAGPRTVles 365
|
330 340
....*....|....*....|....*..
gi 16079029 393 -AHQANEYIEVEAMIESAKIIALFVMD 418
Cdd:cd02697 366 hAKRADERLQLEDLRRATKVIARSLRD 392
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
63-403 |
1.02e-22 |
|
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: 99.03 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 63 IKQLKQHPyFKSNRSDFHESPNIVAKKtgAGGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNT 142
Cdd:TIGR01246 26 AERLEKLG-FEIEWMHFGDTKNLWATR--GTGEPVLAFAGHTDVVPAGPEEQWSSPPFEPVERDGKLYGRGAADMKGSLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 143 ALLFALEALHACDVKLKGDVLFQSVVDEEcGGA--GT---LSAIM-RGYRADGALIPEPTNMK-----LFIKQQGSMWFR 211
Cdd:TIGR01246 103 AFIVAAERFVKKNPDHKGSISLLITSDEE-GTAidGTkkvVETLMaRDELIDYCIVGEPSSVKklgdvIKNGRRGSITGN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 212 ITVKGLSAHGGTRYEGVSAIEKSmhvITAIQELekvrNARISDPLYDNIPiPVPVNIGTISGGAWPSSvadrvVIEGRCG 291
Cdd:TIGR01246 182 LTIKGIQGHVAYPHLANNPIHKA---APALAEL----TAIKWDEGNEFFP-PTSLQITNIHAGTGANN-----VIPGELY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 292 IA------PHEKPEAVKLELENWLK--DLEYHDEW-FKRHPVqvewfgaqwlpndLPDDHPLISVLQSAYQKMKQTEPII 362
Cdd:TIGR01246 249 VQfnlrfsTEVSDEILKQRVEAILDqhGLDYDLEWsLSGEPF-------------LTNDGKLIDKAREAIEETNGIKPEL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 16079029 363 EASPwGTDGGLLYHAGDTPVIVFGPgETKTAHQANEYIEVE 403
Cdd:TIGR01246 316 STGG-GTSDGRFIALMGAEVVEFGP-VNATIHKVNECVSIE 354
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
96-400 |
1.15e-22 |
|
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: 98.88 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 96 RSLILNGHIDVVPEGSVKdWKYEPYQAVE-ENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDEECGG 174
Cdd:cd05646 65 PSILLNSHTDVVPVFEEK-WTHDPFSAHKdEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 175 AGTlsaiMRGY---------RADGAL---IPEPTN-MKLFIKQQGSMWFRITVKGLSAHGGTRYEGvSAIEKSMHVITAI 241
Cdd:cd05646 144 HDG----MEKFvkteefkklNVGFALdegLASPTEeYRVFYGERSPWWVVITAPGTPGHGSKLLEN-TAGEKLRKVIESI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 242 QELEKVRNARI-SDPlydNIPIP--VPVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKD------L 312
Cdd:cd05646 219 MEFRESQKQRLkSNP---NLTLGdvTTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEagrgvtY 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 313 EYHDEWFKRHPVQVEwfgaqwlpndlpDDHPLISVLQSAYQKM-KQTEPIIeaSPWGTDGGLLYHAGdTPVIVFGP-GET 390
Cdd:cd05646 296 EFEQKSPEKDPTSLD------------DSNPWWAAFKKAVKEMgLKLKPEI--FPAATDSRYIRALG-IPALGFSPmNNT 360
|
330
....*....|.
gi 16079029 391 KTA-HQANEYI 400
Cdd:cd05646 361 PILlHDHNEFL 371
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
96-418 |
5.86e-22 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 96.96 E-value: 5.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 96 RSLILNGHIDVV-PEGSvkdwkyePYQAVE--ENGKIYGRGSTDMKGGNTALLFALEALHACDV--KLKGDVLFQSvvDE 170
Cdd:PRK07338 93 RQVLLTGHMDTVfPADH-------PFQTLSwlDDGTLNGPGVADMKGGIVVMLAALLAFERSPLadKLGYDVLINP--DE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 171 ECGGAGT---LSAIMRGYRAdgALIPEPT--NMKLFIKQQGSMWFRITVKGLSAHGGTRY-EGVSAIEKSMHVITAIQEL 244
Cdd:PRK07338 164 EIGSPASaplLAELARGKHA--ALTYEPAlpDGTLAGARKGSGNFTIVVTGRAAHAGRAFdEGRNAIVAAAELALALHAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 245 EKVRNArisdplydnipipVPVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKDLEyhdewfKRHPV 324
Cdd:PRK07338 242 NGQRDG-------------VTVNVAKIDGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVN------QRHGV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 325 QVEWFGAQWLPNDLPDD--HPLISVLQSAYQKMKQTepiIEASPWG--TDGGLLYHAGdTPVI----VFGPGetktAHQA 396
Cdd:PRK07338 303 SLHLHGGFGRPPKPIDAaqQRLFEAVQACGAALGLT---IDWKDSGgvCDGNNLAAAG-LPVVdtlgVRGGN----IHSE 374
|
330 340
....*....|....*....|..
gi 16079029 397 NEYIEVEAMIESAKIIALFVMD 418
Cdd:PRK07338 375 DEFVILDSLVERAQLSALILMR 396
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
102-413 |
4.12e-20 |
|
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: 91.92 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 102 GHIDVVPEGSvkDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDEECGGA------ 175
Cdd:cd03888 78 GHLDVVPAGE--GWTTDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIFGTDEETGWKciehyf 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 176 -----------------------GTLSAIMRGYRADG----------------------ALIPEPTNMKLFIKQQGSMWF 210
Cdd:cd03888 156 eheeypdfgftpdaefpvingekGIVTVDLTFKIDDDkgyrlisikggeatnmvpdkaeAVIPGKDKEELALSAATDLKG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 211 R---------ITVKGLSAHGGTRYEGVSAIeksMHVITAIQELEKVRNAR------------------ISDPLYDNIPIP 263
Cdd:cd03888 236 NieiddggveLTVTGKSAHASAPEKGVNAI---TLLAKFLAELNKDGNDKdfikflaknlhedyngkkLGINFEDEVMGE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 264 VPVNIGTIsggawpsSVADRvviEGRCGIA---PhekpeaVKLELENWLKDLEyhdEWFKRHPVQVEWFGAQwLPNDLPD 340
Cdd:cd03888 313 LTLNPGII-------TLDDG---KLELGLNvryP------VGTSAEDIIKQIE---EALEKYGVEVEGHKHQ-KPLYVPK 372
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16079029 341 DHPLISVLQSAYQKM--KQTEPIieaspwgTDGGLLYhAGDTPVIV-FG---PGETKTAHQANEYIEVEAMIESAKIIA 413
Cdd:cd03888 373 DSPLVKTLLKVYEEQtgKEGEPV-------AIGGGTY-ARELPNGVaFGpefPGQKDTMHQANEFIPIDDLIKALAIYA 443
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
64-412 |
4.30e-20 |
|
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: 90.96 E-value: 4.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 64 KQLKQHPYFKSNRsdfhESPNIVAKkTGAGGGRSLILNGHIDVVPEGSVKDWKyepyqaVEENGKIYGRGSTDMKGGNTA 143
Cdd:cd05647 27 AALRTLPHLEVIR----DGNTVVAR-TERGLASRVILAGHLDTVPVAGNLPSR------VEEDGVLYGCGATDMKAGDAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 144 LLFALEALHACDVKLKGDVLF---QSVVDEECGgagtLSAIMRGYR----ADGALIPEPTNMKLFIKQQGSMWFRITVKG 216
Cdd:cd05647 96 QLKLAATLAAATLKHDLTLIFydcEEVAAELNG----LGRLAEEHPewlaADFAVLGEPTDGTIEGGCQGTLRFKVTTHG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 217 LSAHGGTRYEGVSAIEKSMHVITAIQELEkvrnarisdplydnipiPVPVNIgtisGGAWPSSVADRVVIEGrcGIAPHE 296
Cdd:cd05647 172 VRAHSARSWLGENAIHKLAPILARLAAYE-----------------PRTVNI----DGLTYREGLNAVFISG--GVAGNV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 297 KPEAVKLELeNWL----KDLEYHdewfKRHPVQV-EWFGAQWLPND-----LPD-DHPLISVLQSAYQkmkqtEPIIEAS 365
Cdd:cd05647 229 IPDEARVNL-NYRfapdKSLAEA----IAHVREVfEGLGYEIEVTDlspgaLPGlDHPVARDLIEAVG-----GKVRAKY 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 16079029 366 PWgTDGGLLYHAGdTPVIVFGPGETKTAHQANEYIEVEAMIESAKII 412
Cdd:cd05647 299 GW-TDVARFSALG-IPAVNFGPGDPLLAHKRDEQVPVEQITACAAIL 343
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
20-416 |
5.86e-20 |
|
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: 90.49 E-value: 5.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 20 KAIRLLKRLIGEKSTLGSEFNAQAVVLEKLRQFhmDIDVWepsikqlkqhpyfksnrsdFHESPNIVAKKtgAGGGRSLI 99
Cdd:cd05653 2 DAVELLLDLLSIYSPSGEEARAAKFLEEIMKEL--GLEAW-------------------VDEAGNAVGGA--GSGPPDVL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 100 LNGHIDVVPeGSVkdwkyepyQAVEENGKIYGRGSTDMKGGNTALLFALEALHAcdvKLKGDVLFQSVVDEECGGAGTLS 179
Cdd:cd05653 59 LLGHIDTVP-GEI--------PVRVEGGVLYGRGAVDAKGPLAAMILAASALNE---ELGARVVVAGLVDEEGSSKGARE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 180 AIMRGYRADGALIPEPTNmklfikqqgsmWFRITV--KGlSAHGGTRYEGVSAiEKSMHVITAIQEL-EKVRNARISDPL 256
Cdd:cd05653 127 LVRRGPRPDYIIIGEPSG-----------WDGITLgyRG-SLLVKIRCEGRSG-HSSSPERNAAEDLiKKWLEVKKWAEG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 257 YDNIPIPVPVNIGTISGGAWPSSVAdRVVIEGRCGIA-PHEKP--EAVKLELEnwlKDLEYHDEWFKR-HPVQVewfgaq 332
Cdd:cd05653 194 YNVGGRDFDSVVPTLIKGGESSNGL-PQRAEATIDLRlPPRLSpeEAIALATA---LLPTCELEFIDDtEPVKV------ 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 333 wlpndlPDDHPLISVLQSAYQKMKqTEPIIeASPWGT-DGGLLYHAGDTPVIVFGPGETKTAHQANEYIEVEAMIESAKI 411
Cdd:cd05653 264 ------SKNNPLARAFRRAIRKQG-GKPRL-KRKTGTsDMNVLAPLWTVPIVAYGPGDSTLDHTPNEHIELAEIERAAAV 335
|
....*
gi 16079029 412 IALFV 416
Cdd:cd05653 336 LKGAL 340
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
97-400 |
7.55e-20 |
|
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: 91.01 E-value: 7.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 97 SLILNGHIDVVPEGSVKdWKYEPYQA-VEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDEECGGA 175
Cdd:TIGR01880 73 SILLNSHTDVVPVFREH-WTHPPFSAfKDEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGH 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 176 GTL-----SAIMRGYRADGAL---IPEPTN-MKLFIKQQGSMWFRITVKGLSAHGGTRYEGvSAIEKSMHVITAIQELEK 246
Cdd:TIGR01880 152 DGMekfakTDEFKALNLGFALdegLASPDDvYRVFYAERVPWWVVVTAPGNPGHGSKLMEN-TAMEKLEKSVESIRRFRE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 247 VRNARISDPLYDNIPIPVPVNIGTISGGAwPSSVADRVVIEG-RCGIAPHEKPEAVKLELENWLKD------LEYHDEWF 319
Cdd:TIGR01880 231 SQFQLLQSNPDLAIGDVTSVNLTKLKGGV-QSNVIPSEAEAGfDIRLAPSVDFEEMENRLDEWCADagegvtYEFSQHSG 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 320 KRHPVQVEwfgaqwlpndlpDDHPLISVLQSAYQKMKQT-EPiiEASPWGTDGGLLYHAGdTPVIVFGPgETKT---AHQ 395
Cdd:TIGR01880 310 KPLVTPHD------------DSNPWWVAFKDAVKEMGCTfKP--EILPGSTDSRYIRAAG-VPALGFSP-MNNTpvlLHD 373
|
....*
gi 16079029 396 ANEYI 400
Cdd:TIGR01880 374 HNEFL 378
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
102-413 |
1.29e-19 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 90.67 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 102 GHIDVVPEGSvkDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDEECG-------- 173
Cdd:PRK07318 86 GHLDVVPAGD--GWDTDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRFIVGTDEESGwkcmdyyf 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 174 --------------------------------------GAGTLSAIMRGYRAD--------GALIPEPTNMKL----FIK 203
Cdd:PRK07318 164 eheeapdfgfspdaefpiingekgittfdlvhfegeneGDYVLVSFKSGLRENmvpdsaeaVITGDDLDDLIAafeaFLA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 204 QQG--------SMWFRITVKGLSAHGGTRYEGVSAIeksMHVITAIQELEKVRNAR-----ISDPL-------------Y 257
Cdd:PRK07318 244 ENGlkgeleeeGGKLVLTVIGKSAHGSTPEKGVNAA---TYLAKFLNQLNLDGDAKafldfAAEYLhedtrgeklgiayE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 258 DNIPIPVPVNIGTISggaWPSSVADRVVIEGR--CGIapheKPEAVKLELENWLKDLEyhdewfkrhpVQVEWFGAQwLP 335
Cdd:PRK07318 321 DDVMGDLTMNVGVFS---FDEEKGGTLGLNFRypVGT----DFEKIKAKLEKLIGVTG----------VELSEHEHQ-KP 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 336 NDLPDDHPLISVLQSAYQKM--KQTEPIIEASpwGTDGGLLyhagdtPVIV-FG---PGETKTAHQANEYIEVEAMIESA 409
Cdd:PRK07318 383 HYVPKDDPLVKTLLKVYEKQtgLKGEEQVIGG--GTYARLL------KRGVaFGamfPGSEDTMHQANEYIEIDDLIKAA 454
|
....
gi 16079029 410 KIIA 413
Cdd:PRK07318 455 AIYA 458
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
84-197 |
2.04e-19 |
|
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: 85.95 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 84 NIVAKKTGAGGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVL 163
Cdd:cd18669 1 NVIARYGGGGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 16079029 164 FQSVVDEECG---GAGTLS--AIMRGYRADGALIPEPTN 197
Cdd:cd18669 81 VAFTPDEEVGsgaGKGLLSkdALEEDLKVDYLFVGDATP 119
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
91-413 |
4.62e-19 |
|
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: 88.97 E-value: 4.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 91 GAGGGRSLILnGHIDVVPEGSvkDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDE 170
Cdd:TIGR01887 64 GQGEEVLGIL-GHLDVVPAGD--GWTSPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 171 ECGGAGT---------------------------------------------LSAIMRGYRAD------GALIPEPTNMK 199
Cdd:TIGR01887 141 ESGWKCIdyyfeheempdigftpdaefpiiygekgittleikfkddtegdvvLESFKAGEAYNmvpdhaTAVISGKKLTE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 200 -------LFIKQQGSMWFR-------ITVKGLSAHGGTRYEGVSAIEKSMHVITAIQ---------------ELEKVRNA 250
Cdd:TIGR01887 221 veqlkfvFFIAKELEGDFEvndgtltITLEGKSAHGSAPEKGINAATYLALFLAQLNlaggakaflqflaeyLHEDHYGE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 251 RISDPLYDNIPIPVPVNIGTIsggAWPSSVADRVVIEGRcgiapheKPEAVKLELEnwLKDLEyhdewFKRHPVQVEWFG 330
Cdd:TIGR01887 301 KLGIKFHDDVSGDLTMNVGVI---DYENAEAGLIGLNVR-------YPVGNDPDTM--LKNEL-----AKESGVVEVTLN 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 331 AQWLPNDLPDDHPLISVLQSAYQKM--KQTEPIieaspwgTDGGLLYhAGDTPVIV-FG---PGETKTAHQANEYIEVEA 404
Cdd:TIGR01887 364 GYLKPLYVPKDDPLVQTLMKVYEKQtgDEGEPV-------AIGGGTY-ARLMPNGVaFGalfPGEEDTMHQANEYIMIDD 435
|
....*....
gi 16079029 405 MIESAKIIA 413
Cdd:TIGR01887 436 LLLATAIYA 444
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
84-416 |
4.94e-19 |
|
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.
Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 88.57 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 84 NIVAKKTGAGGGR-SLILNGHIDVVPeGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDV 162
Cdd:cd05675 53 NLVARIGGTDPSAgPLLLLGHIDVVP-ADASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 163 LFQSVVDEECG---GAGTLSA----IMRGY-----RADGALIPEPTNMKLFIKQ---QGSMWFRITVKGLSAHGG--TRY 225
Cdd:cd05675 132 VFAFVADEEAGgenGAKWLVDnhpeLFDGAtfalnEGGGGSLPVGKGRRLYPIQvaeKGIAWMKLTVRGRAGHGSrpTDD 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 226 EGVSAIEKSMHVITAIQE-----------------------LEKVRNARISDPLYDNIpIPV----------PVNIGTIS 272
Cdd:cd05675 212 NAITRLAEALRRLGAHNFpvrltdetayfaqmaelaggeggALMLTAVPVLDPALAKL-GPSapllnamlrnTASPTMLD 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 273 GGAWPSSVADRVVIEGRCGIAPHEKPEAVKLELENWLKDLEyhdewfkrhpVQVEWFGAQwLPNDLPDDHPLISVLQSAY 352
Cdd:cd05675 291 AGYATNVLPGRATAEVDCRILPGQSEEEVLDTLDKLLGDPD----------VSVEAVHLE-PATESPLDSPLVDAMEAAV 359
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16079029 353 QKMKQTEPIIE-ASPWGTDGGLLYHAGdTPVIVFGP-------GETKTAHQANEYIEVEAMIESAKIIALFV 416
Cdd:cd05675 360 QAVDPGAPVVPyMSPGGTDAKYFRRLG-IPGYGFAPlflppelDYTGLFHGVDERVPVESLYFGVRFLDRLV 430
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
84-412 |
9.57e-19 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 87.03 E-value: 9.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 84 NIVAKK--TGAGGGRSLILNGHIDVVPEGSVKdwkyePYQAVEENGKIYGRGST----DMKGGNTALLFALEALHACDVK 157
Cdd:COG2195 47 NVIATLpaTPGYNVPTIGLQAHMDTVPQFPGD-----GIKPQIDGGLITADGTTtlgaDDKAGVAAILAALEYLKEPEIP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 158 lKGD--VLFqsVVDEECG--GA-----GTLSAIMrGYRADGALIPEptnmkLFIKQQGSMWFRITVKGLSAHGGTRYE-G 227
Cdd:COG2195 122 -HGPieVLF--TPDEEIGlrGAkaldvSKLGADF-AYTLDGGEEGE-----LEYECAGAADAKITIKGKGGHSGDAKEkM 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 228 VSAIEKSMHVITAIQELEkvrnarisdplydnIPIPVPVNIGTISGGAWPSSVADRVVIEgrcGIAPHEKPEAVKLELEN 307
Cdd:COG2195 193 INAIKLAARFLAALPLGR--------------IPEETEGNEGFIHGGSATNAIPREAEAV---YIIRDHDREKLEARKAE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 308 WLKDLEyhdEWFKRHP---VQVEWFGA--QWLPNdlpDDHPLISVLQSAYQKMKQtEPIIEASPWGTDGGLLYHAGdTPV 382
Cdd:COG2195 256 LEEAFE---EENAKYGvgvVEVEIEDQypNWKPE---PDSPIVDLAKEAYEELGI-EPKIKPIRGGLDGGILSFKG-LPT 327
|
330 340 350
....*....|....*....|....*....|
gi 16079029 383 IVFGPGETKtAHQANEYIEVEAMIESAKII 412
Cdd:COG2195 328 PNLGPGGHN-FHSPDERVSIESMEKAWELL 356
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
82-415 |
1.06e-18 |
|
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: 87.77 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 82 SPNIVAKKTGAGGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGD 161
Cdd:cd03893 50 APVVFAEFPGAPGAPTVLLYGHYDVQPAGDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 162 VLFQSVVDEECGGAGtLSAIMRGYR----ADGALIPEPTNMK-----LFIKQQGSMWFRITVKGLSA--HGGTrYEGVsa 230
Cdd:cd03893 130 VKFIIEGEEESGSPS-LDQLVEAHRdllaADAIVISDSTWVGqeqptLTYGLRGNANFDVEVKGLDHdlHSGL-YGGV-- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 231 IEKSMHVitAIQELEKVRNA--RISDP-LYDNIP------------IPVPVNIGTISGGA-------WPS---------- 278
Cdd:cd03893 206 VPDPMTA--LAQLLASLRDEtgRILVPgLYDAVRelpeeefrldagVLEEVEIIGGTTGSvaerlwtRPAltvlgidggf 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 279 -------SVADRVVIEGRCGIAPHEKPEAVKLELEnwlKDLEYHDEWFKRHPVQVEWFGAQWLpndLPDDHPLISVLQSA 351
Cdd:cd03893 284 pgegsktVIPPRARAKISIRLVPGQDPEEASRLLE---AHLEKHAPSGAKVTVSYVEGGMPWR---SDPSDPAYQAAKDA 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16079029 352 YQKMKQTEPIIEaspwgTDGG------LLYHAGDTPVIVFGPGETKT-AHQANEYIEVEAMIESAKIIALF 415
Cdd:cd03893 358 LRTAYGVEPPLT-----REGGsipfisVLQEFPQAPVLLIGVGDPDDnAHSPNESLRLGNYKEGTQAEAAL 423
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
84-174 |
2.08e-17 |
|
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: 80.16 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 84 NIVAKKTGAGGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVL 163
Cdd:cd03873 1 NLIARLGGGEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIV 80
|
90
....*....|.
gi 16079029 164 FQSVVDEECGG 174
Cdd:cd03873 81 VAFTADEEVGS 91
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
202-317 |
2.69e-17 |
|
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices which make up the dimerization surface of members of the M20 family of peptidases. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 400158 [Multi-domain] Cd Length: 107 Bit Score: 77.00 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 202 IKQQGSMWFRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELEKVRNarisdplydNIPIPVPVNIGTISGGAWPSSVA 281
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIG---------FDFPRTTLNITGIEGGTATNVIP 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 16079029 282 DRVVIEGRCGIAPHEKPEAVKLELENWLKDLEYHDE 317
Cdd:pfam07687 72 AEAEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
102-421 |
9.19e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 78.97 E-value: 9.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 102 GHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDEEcggagTLSAI 181
Cdd:PRK07205 82 CHLDVVPEGDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGTDEE-----TLWRC 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 182 MRGYR--------------------ADGALI------PEPTNMKLFIKQ-----------QGSMW-----------F--- 210
Cdd:PRK07205 157 MNRYNeveeqatmgfapdssfpltyAEKGLLqaklvgPGSDQLELEVGQafnvvpakasyQGPKLeavkkeldklgFeyv 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 211 ----RITVKGLSAHGGTRYEGVSAIEK---------SMHVITAIQEL--EKVRNARISDPLYDNIPIPVPVNIG--TISg 273
Cdd:PRK07205 237 vkenEVTVLGKSVHAKDAPQGINAVIRlakalvvlePHPALDFLANVigEDATGLNIFGDIEDEPSGKLSFNIAglTIT- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 274 gawpssvadrvviegrcgiapHEKPEA-------VKLELENWLKDLEYHDEWFKRHPVQVEWFGaqwlPNDLPDDHPLIS 346
Cdd:PRK07205 316 ---------------------KEKSEIridiripVLADKEKLVQQLSQKAQEYGLTYEEFDYLA----PLYVPLDSELVS 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16079029 347 VLQSAYQkmkqtEPIIEASPWGTDGGLLYHAGDTPVIVFG---PGETKTAHQANEYIEVEAMIESAKIIALFVMDWCG 421
Cdd:PRK07205 371 TLMSVYQ-----EKTGDDSPAQSSGGATFARTMPNCVAFGalfPGAPQTEHQANEHIVLEDLYRAMDIYAEAIYRLTT 443
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
84-186 |
1.54e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 75.42 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 84 NIVAKKTGAGGGRSLILNGHIDVVpEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVL 163
Cdd:PRK09133 90 NLVARLRGTDPKKPILLLAHMDVV-EAKREDWTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREGFKPKRDII 168
|
90 100
....*....|....*....|...
gi 16079029 164 FQSVVDEECGGAGTLSAIMRGYR 186
Cdd:PRK09133 169 LALTGDEEGTPMNGVAWLAENHR 191
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
98-220 |
1.35e-13 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 72.29 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 98 LILNGHIDVVP--EGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDEECGG- 174
Cdd:cd05674 72 LLLMAHQDVVPvnPETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTIILAFGHDEEVGGe 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16079029 175 --AGTLSAIM---RGYRADGALIPE--PTNMKLFIKQQ---------GSMWFRITVKGLSAH 220
Cdd:cd05674 152 rgAGAIAELLlerYGVDGLAAILDEggAVLEGVFLGVPfalpgvaekGYMDVEITVHTPGGH 213
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
10-188 |
3.36e-13 |
|
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: 71.09 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 10 VIEWLDQHSAKAIRLLKRLIGEKS------TLGSEFNAQAVVLEKLRQFHMDIDVWEPSIKQL---KQHPYFKSNRSDFH 80
Cdd:cd05676 1 VFKYIDEHQDEFIERLREAVAIQSvsadpeKRPELIRMMEWAAERLEKLGFKVELVDIGTQTLpdgEELPLPPVLLGRLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 81 ESPNivaKKTgagggrsLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKG 160
Cdd:cd05676 81 SDPS---KKT-------VLIYGHLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPV 150
|
170 180 190
....*....|....*....|....*....|
gi 16079029 161 DVLFqsVVD--EECGGAGtLSAIMRGyRAD 188
Cdd:cd05676 151 NLKF--CFEgmEESGSEG-LDELIEA-RKD 176
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
96-188 |
2.27e-12 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 68.43 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 96 RSLILNGHIDVVP--EGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLFQSVVDEECG 173
Cdd:PRK08262 112 KPIVLMAHQDVVPvaPGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVG 191
|
90
....*....|....*....
gi 16079029 174 GAGT--LSAIM--RGYRAD 188
Cdd:PRK08262 192 GLGAraIAELLkeRGVRLA 210
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
80-412 |
2.42e-12 |
|
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349932 [Multi-domain] Cd Length: 368 Bit Score: 67.86 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 80 HESPNIVAKKTGAG-GGRSLILNGHIDVVPEGSVKDwkyepyQAVEENGKIYGRGST----DMKGGNTALLFALEALHAC 154
Cdd:cd05683 51 GGAGNLICTLKADKeEVPKILFTSHMDTVTPGINVK------PPQIADGYIYSDGTTilgaDDKAGIAAILEAIRVIKEK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 155 DVKlKGDVLFQSVVDEECG--GAGTLSAIM----RGYRADGA------LIPEPTNMKlfikqqgsmwFRITVKGLSAHGG 222
Cdd:cd05683 125 NIP-HGQIQFVITVGEESGlvGAKALDPELidadYGYALDSEgdvgtiIVGAPTQDK----------INAKIYGKTAHAG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 223 TRYE-GVSAIeksmhvITAIQELEKVRNARISDPlydnipipVPVNIGTISGGAWPSSVADRVVIEGRCGIAPHEKPEA- 300
Cdd:cd05683 194 TSPEkGISAI------NIAAKAISNMKLGRIDEE--------TTANIGKFQGGTATNIVTDEVNIEAEARSLDEEKLDAq 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 301 ---VKLELENWLKDLEYHDEwfkrhpVQVEwfgAQWLPNDLPDDHPLISVLQSAYQKMKQtEPIIEASPWGTDGGLLYHA 377
Cdd:cd05683 260 vkhMKETFETTAKEKGAHAE------VEVE---TSYPGFKINEDEEVVKLAKRAANNLGL-EINTTYSGGGSDANIINGL 329
|
330 340 350
....*....|....*....|....*....|....*
gi 16079029 378 GdTPVIVFGPGeTKTAHQANEYIEVEAMIESAKII 412
Cdd:cd05683 330 G-IPTVNLGIG-YENIHTTNERIPIEDLYDTAVLV 362
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
92-175 |
2.85e-12 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 68.26 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 92 AGGGRSLIL-NGHIDVVPEGSvKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALhaCDVKLKGDVLFQSVVDE 170
Cdd:PRK08554 59 IGEGKPKLLfMAHFDVVPVNP-EEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKEL--SKEPLNGKVIFAFTGDE 135
|
....*
gi 16079029 171 ECGGA 175
Cdd:PRK08554 136 EIGGA 140
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
83-267 |
5.05e-12 |
|
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: 67.33 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 83 PNIVAKKTGAGGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHA------CDV 156
Cdd:cd05680 51 PLVYAEWLGAPGAPTVLVYGHYDVQPPDPLELWTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAvegalpVNV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 157 KLkgdvLFQSvvDEECGGAgTLSAIMRGYR----ADGALIPEptnmklfikqqGSMW----------------FRITVKG 216
Cdd:cd05680 131 KF----LIEG--EEEIGSP-SLPAFLEENAerlaADVVLVSD-----------TSMWspdtptityglrglayLEISVTG 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16079029 217 LSA--HGGTrYEGvsAIEKSMHVITAIQELEKVRNARISDP-LYDNIpIPVPVN 267
Cdd:cd05680 193 PNRdlHSGS-YGG--AVPNPANALARLLASLHDEDGRVAIPgFYDDV-RPLTDA 242
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
85-191 |
6.76e-12 |
|
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: 66.98 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 85 IVAKKTGAGGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDVLF 164
Cdd:cd05681 49 IVYAEFNSGDAKTLLFYNHYDVQPAEPLELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKF 128
|
90 100 110
....*....|....*....|....*....|.
gi 16079029 165 qSVVDEECGGAGTLSAIMRGYR----ADGAL 191
Cdd:cd05681 129 -LVEGEEEVGSPNLEKFVAEHAdllkADGCI 158
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
79-221 |
5.13e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 64.10 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 79 FHES----PNIVAKKTGAGGGRS-LILNGHIDVVPeGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHA 153
Cdd:PRK07906 44 YLESapgrANVVARLPGADPSRPaLLVHGHLDVVP-AEAADWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 154 CDVKLKGDVLFQSVVDEECGG---------------AGTLSAIMR--GYRADgalIPEPTNMKLF-IKQQGSMWFRITVK 215
Cdd:PRK07906 123 TGRRPPRDLVFAFVADEEAGGtygahwlvdnhpelfEGVTEAISEvgGFSLT---VPGRDRLYLIeTAEKGLAWMRLTAR 199
|
....*.
gi 16079029 216 GLSAHG 221
Cdd:PRK07906 200 GRAGHG 205
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
82-403 |
5.64e-11 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 63.88 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 82 SPNIVAKKTGAGGgRSLILNGHIDVV-PEGSVKDwkyEPYQavEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKG 160
Cdd:PRK06133 87 GDMVVATFKGTGK-RRIMLIAHMDTVyLPGMLAK---QPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 161 D--VLFQSvvDEECGGAGTLSAIMR-GYRADGALIPEPTNMK--LFIKQQGSMWFRITVKGLSAHGGTRYE-GVSAIEKS 234
Cdd:PRK06133 161 TltVLFNP--DEETGSPGSRELIAElAAQHDVVFSCEPGRAKdaLTLATSGIATALLEVKGKASHAGAAPElGRNALYEL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 235 MHVITAIQELEK----------------VRN-----------ARISDPlydnipipvpvnigtisggawpsSVADRVVIE 287
Cdd:PRK06133 239 AHQLLQLRDLGDpakgttlnwtvakagtNRNvipasasaqadVRYLDP-----------------------AEFDRLEAD 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 288 GRCGIAPHEKPEA-VKLELEnwlkdleyhdewfKRHPVqvewfgaqwLPNDlPDDHPLISVLQSAYQKM-KQTEPIIEAS 365
Cdd:PRK06133 296 LQEKVKNKLVPDTeVTLRFE-------------RGRPP---------LEAN-AASRALAEHAQGIYGELgRRLEPIDMGT 352
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 16079029 366 PWGTDGGLLYHAGDTPVI----VFGPGetktAHQANEYIEVE 403
Cdd:PRK06133 353 GGGTDAAFAAGSGKAAVLegfgLVGFG----AHSNDEYIELN 390
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
82-197 |
1.38e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 63.00 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 82 SPNIVAKKTGAGGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHAcDVKLkGD 161
Cdd:PRK07907 70 APAVIGTRPAPPGAPTVLLYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLAALRALGG-DLPV-GV 147
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 16079029 162 VLFqsVVDEECGGAGTLSAIMRGYR----ADGALIPEPTN 197
Cdd:PRK07907 148 TVF--VEGEEEMGSPSLERLLAEHPdllaADVIVIADSGN 185
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
102-186 |
2.65e-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: 61.98 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 102 GHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHAcDVKLKGDVLFQSVVDEECGGAGtLSAI 181
Cdd:cd05677 78 GHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELFQ-EGELDNDVVFLIEGEEESGSPG-FKEV 155
|
....*
gi 16079029 182 MRGYR 186
Cdd:cd05677 156 LRKNK 160
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
85-290 |
4.35e-10 |
|
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: 61.20 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 85 IVAKKTGAGGGRSLILNGHIDVVPegsVKDWKYEPYQAVEEnGKIYGRGStdmKGGNTALLFALEALHACDVKLKGDV-- 162
Cdd:cd08019 44 VIATIKGGKAGKTVALRADIDALP---VEECTDLEYKSKNP-GLMHACGH---DGHTAMLLGAAKILNEIKDTIKGTVkl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 163 LFQSVvDEECGGAGTLSAIMRGYRADGAL-------IPEPtnmKLFIKQQGSM----WFRITVKGLSAHGGTRYEGVSAI 231
Cdd:cd08019 117 IFQPA-EEVGEGAKQMIEEGVLEDVDAVFgihlwsdVPAG---KISVEAGPRMasadIFKIEVKGKGGHGSMPHQGIDAV 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16079029 232 EKSMHVITAIQELEkvrnARISDPLYdnipiPVPVNIGTISGGAWPSSVADRVVIEG--RC 290
Cdd:cd08019 193 LAAASIVMNLQSIV----SREIDPLE-----PVVVTVGKLNSGTRFNVIADEAKIEGtlRT 244
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
21-274 |
4.66e-10 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 60.74 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 21 AIRLLKRLIGEKSTLGSEFNAQAVVLEKLRQFhmDIDVWepsikqlkqhpyfksnrsdFHESPNIVAKKtgAGGGRSLIL 100
Cdd:PRK04443 8 ARELLKGLVEIPSPSGEEAAAAEFLVEFMESH--GREAW-------------------VDEAGNARGPA--GDGPPLVLL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 101 NGHIDVVPeGSVkdwkyePyqaVE-ENGKIYGRGSTDMKGGNTALLFALEALHAcdvKLKGDVLFQSVVDEECGGAGTLS 179
Cdd:PRK04443 65 LGHIDTVP-GDI------P---VRvEDGVLWGRGSVDAKGPLAAFAAAAARLEA---LVRARVSFVGAVEEEAPSSGGAR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 180 AIMRGYRADGALIPEPtnmklfikqqgSMWFRITV--KGL--------SAHGGTRYEGVSAIEKSMHVITAIQELEKVRN 249
Cdd:PRK04443 132 LVADRERPDAVIIGEP-----------SGWDGITLgyKGRllvtyvatSESFHSAGPEPNAAEDAIEWWLAVEAWFEAND 200
|
250 260
....*....|....*....|....*
gi 16079029 250 ARisDPLYDNIpIPVPVNIGTISGG 274
Cdd:PRK04443 201 GR--ERVFDQV-TPKLVDFDSSSDG 222
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
64-181 |
7.80e-10 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 60.64 E-value: 7.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 64 KQLKQHPYFKSNRS---------DFHESPNIVAKKTGAGGGR-SLILNGHIDVVPE---GSVKDWKYEPY---------- 120
Cdd:COG4187 38 EKLSELPYFQENPEhlglhplpdDPLGRKNVTALVKGKGESKkTVILISHFDVVDVedyGSLKPLAFDPEeltealkeik 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16079029 121 -----QAVEENGK-IYGRGSTDMKGGNtALLFALeALHAC-DVKLKGDVLFQSVVDEECGGAGTLSAI 181
Cdd:COG4187 118 lpedvRKDLESGEwLFGRGTMDMKAGL-ALHLAL-LEEASeNEEFPGNLLLLAVPDEEVNSAGMRAAV 183
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
42-252 |
1.32e-09 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 59.41 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 42 QAVVLEKLRQFHMDI-DVWEPSIKQLKQHPYFKSNRSDFHESPNIVAK-KTGAGGGRSLILNGHIDVVPeGSVkdwkyep 119
Cdd:PRK00466 5 KELVKQKAKELLLDLlSIYTPSGNETNATKFFEKISNELNLKLEILPDsNSFILGEGDILLASHVDTVP-GYI------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 120 yQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKlkgdVLFQSVVDEECGGAGTLSAIMRGYRADGALIPEPTN-M 198
Cdd:PRK00466 77 -EPKIEGEVIYGRGAVDAKGPLISMIIAAWLLNEKGIK----VMVSGLADEESTSIGAKELVSKGFNFKHIIVGEPSNgT 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16079029 199 KLFIKQQGSMWFRITVKGLSAHGGTRYEGVsAIEKSMHVITAIQELEKVRNARI 252
Cdd:PRK00466 152 DIVVEYRGSIQLDIMCEGTPEHSSSAKSNL-IVDISKKIIEVYKQPENYDKPSI 204
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
19-268 |
2.33e-09 |
|
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: 59.28 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 19 AKAIRLLKRLIGEKSTLGSEfnAQAVVLEKLRQfhmdidvwepsikQLKQHPYFKSNRSD-FHESP-------NIVAKKT 90
Cdd:cd05654 1 ERLEQLLKSLVSWPSVTGTE--GERSFADFLKE-------------ILKELPYFKENPSHvWQLLPpddlgrrNVTALVK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 91 GAGGG-RSLILNGHIDVVPE---GSVKDWKYEP-------YQAVEENGK-----------IYGRGSTDMKGGntaLLFAL 148
Cdd:cd05654 66 GKKPSkRTIILISHFDTVGIedyGELKDIAFDPdeltkafSEYVEELDEevredllsgewLFGRGTMDMKSG---LAVHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 149 EAL-HACDVK-LKGDVLFQSVVDEECGGAGTLSAIMR--------GYRADGALIPEPTnmklFIKQQGSMWFRI------ 212
Cdd:cd05654 143 ALLeQASEDEdFDGNLLLMAVPDEEVNSRGMRAAVPAllelkkkhDLEYKLAINSEPI----FPQYDGDQTRYIytgsig 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16079029 213 ------TVKGLSAHGGTRYEGVSAieksmHVITA--IQELEKvrNARISDPlYDNIPIPVPVNI 268
Cdd:cd05654 219 kilpgfLCYGKETHVGEPFAGINA-----NLMASeiTARLEL--NADLCEK-VEGEITPPPVCL 274
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
93-173 |
6.97e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 57.46 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 93 GGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDvKLKGDVLFQSVVDEEC 172
Cdd:PRK06446 60 GAKKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKH-KLNVNVKFLYEGEEEI 138
|
.
gi 16079029 173 G 173
Cdd:PRK06446 139 G 139
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
98-281 |
7.84e-09 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 57.10 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 98 LILnGHIDVV-PEGSVKDWKYEpyqavEENGKIYGRGSTDMKGGNTALLFALEALHACDVK--LKGDVLFQSvvDEECGG 174
Cdd:PRK07473 79 LIA-GHMDTVhPVGTLEKLPWR-----REGNKCYGPGILDMKGGNYLALEAIRQLARAGITtpLPITVLFTP--DEEVGT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 175 AGTLSAI-MRGYRADGALIPEP--TNMKLFIKQQGSMWFRITVKGLSAHGGTRY-EGVSAIEKSMHVITAIQELEKvrna 250
Cdd:PRK07473 151 PSTRDLIeAEAARNKYVLVPEPgrPDNGVVTGRYAIARFNLEATGRPSHAGATLsEGRSAIREMARQILAIDAMTT---- 226
|
170 180 190
....*....|....*....|....*....|.
gi 16079029 251 riSDplydnipipVPVNIGTISGGAWPSSVA 281
Cdd:PRK07473 227 --ED---------CTFSVGIVHGGQWVNCVA 246
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
142-288 |
2.36e-08 |
|
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: 55.68 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 142 TALLFALEALHACDVKLKGDV--LFQSvvDEECGGaGTLSAIMRG----YRADGAL----IPEPTNMKLFIKQQGSMW-- 209
Cdd:cd03886 95 AMLLGAAKLLAERRDPLKGTVrfIFQP--AEEGPG-GAKAMIEEGvlenPGVDAAFglhvWPGLPVGTVGVRSGALMAsa 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 210 --FRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELekvrNARISDPLydnipIPVPVNIGTISGGAWPSSVADRVVIE 287
Cdd:cd03886 172 deFEITVKGKGGHGASPHLGVDPIVAAAQIVLALQTV----VSRELDPL-----EPAVVTVGKFHAGTAFNVIPDTAVLE 242
|
.
gi 16079029 288 G 288
Cdd:cd03886 243 G 243
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
83-265 |
1.13e-07 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 53.60 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 83 PNIVAKKTGAGGGRSLILNGHIDVVPEGSVKDWKYEPYQAVEENGKIYGRGSTDMKGGNTALLFALEALHACDVKLKGDV 162
Cdd:PRK08201 67 PIVYADWLHAPGKPTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 163 LFQSVVDEECGGAGTLSAIMRG---YRADGALIP-----EPTNMKLFIKQQGSMWFRITVKGLSA--HGGTrYEGvsAIE 232
Cdd:PRK08201 147 KFCIEGEEEIGSPNLDSFVEEEkdkLAADVVLISdttllGPGKPAICYGLRGLAALEIDVRGAKGdlHSGL-YGG--AVP 223
|
170 180 190
....*....|....*....|....*....|....
gi 16079029 233 KSMHVITAIQELEKVRNARIS-DPLYDNIPIPVP 265
Cdd:PRK08201 224 NALHALVQLLASLHDEHGTVAvEGFYDGVRPLTP 257
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
24-413 |
1.25e-07 |
|
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: 53.62 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 24 LLKRLIGEKSTLGS--------EFNAQAVVLEKLRqfhmdidvwepsikqlkqhPYFKSNRSDFHESP--------NIVA 87
Cdd:cd08012 9 LLGKLIGESKYLQNnppqlvpkEDNAGRHVLEALT-------------------PYSTENGGPLVIDHvsyvkgrgNIIV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 88 KKTGAGGGRSLILNG-HIDVVPeGSVKDWKYEPYQAVEENGKIYGRGSTDMKgGNTALLFAL-EALHACDVKLKGDVLFQ 165
Cdd:cd08012 70 EYPGTVDGKTVSFVGsHMDVVT-ANPETWEFDPFSLSIDGDKLYGRGTTDCL-GHVALVTELfRQLATEKPALKRTVVAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 166 SVVDEECG---GAGTLSAIMRG----------YRADGAlIPEPTnmklfIKQQGSMWFRITVKGLSAHGGTRYEGVSAIE 232
Cdd:cd08012 148 FIANEENSeipGVGVDALVKSGlldnlksgplYWVDSA-DSQPC-----IGTGGMVTWKLTATGKLFHSGLPHKAINALE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 233 KSMHVITAIQEL----------EKVRNARISDPLYDNIPIPVPVNIGTISGGAwpssvadrvVIEGRCGIAPHEKPEAVK 302
Cdd:cd08012 222 LVMEALAEIQKRfyidfpphpkEEVYGFATPSTMKPTQWSYPGGSINQIPGEC---------TICGDCRLTPFYDVKEVR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 303 LELENWLKDLEYHDEWFK---------------RHPVQVEWFGAQWLPNDLPDDHPLISVLQSAyqkmkqTEPII-EASP 366
Cdd:cd08012 293 EKLEEYVDDINANIEELPtrgpvskyvlpaeglRGRVSLEFDEAAASGVACNLDSPGFHALCKA------TSEVVgYVKP 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 16079029 367 WGTDGGL-----LYHAG-DTPVIvfGPGETKTAHQANEYIEVEAMIESAKIIA 413
Cdd:cd08012 367 YAITGSLplireLQDEGfDVQIT--GYGLMATYHAKNEYCLLSDFQNGFKVLA 417
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
102-215 |
3.72e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 52.22 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 102 GHIDVVPeGSVKDWK--YEPYQAVEENGKIYGRGSTDMKGGNTALLFALEA-LHACDVKLKGDVLFQSVVDEECGGAGtL 178
Cdd:PRK07079 92 GHGDVVR-GYDEQWRegLSPWTLTEEGDRWYGRGTADNKGQHTINLAALEQvLAARGGRLGFNVKLLIEMGEEIGSPG-L 169
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 16079029 179 SAIMRGYR----------ADGA-LIPE-PTnmkLFIKQQGSMWFRITVK 215
Cdd:PRK07079 170 AEVCRQHRealaadvliaSDGPrLSAErPT---LFLGSRGAVNFRLRVN 215
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
82-214 |
7.59e-06 |
|
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: 47.88 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 82 SPNIVAKKTGAGGGRSLILNGHIDVVPeGSVKDWK--YEPYQAVEENGKIYGRGSTDMKGGNTALLFALEA-LHACDVKL 158
Cdd:cd05679 59 APFLIAERIEDPSLPTLLIYGHGDVVP-GYEGRWRdgRDPWTVTVWGERWYGRGTADNKGQHSINMAALRQvLEARGGKL 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16079029 159 KGDVLFQSVVDEECGGAGtLSAIMRGYR----------ADGALI--PEPTnmkLFIKQQGSMWFRITV 214
Cdd:cd05679 138 GFNVKFLIEMGEEMGSPG-LRAFCFSHRealkadlfiaSDGPRLaaDRPT---MFLGSRGGLNFELRV 201
|
|
| M20_Acy1-like |
cd08014 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
142-290 |
5.81e-05 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of uncharacterized 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: 349936 [Multi-domain] Cd Length: 371 Bit Score: 44.96 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 142 TALLFALEALHACDVKLKGDV--LFQSVVDEECGGAGTL--SAIMRGYRADGALIPEPTNM--KLFIKQ----QGSMWFR 211
Cdd:cd08014 95 AIALGAALVLAALEEELPGRVrlIFQPAEETMPGGALDMirAGALDGVSAIFALHVDPRLPvgRVGVRYgpitAAADSLE 174
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 212 ITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELEkvrnARISDPLYdnipiPVPVNIGTISGGAWPSSVADRVVIEG--R 289
Cdd:cd08014 175 IRIQGEGGHGARPHLTVDLVWAAAQVVTDLPQAI----SRRIDPRS-----PVVLTWGSIEGGRAPNVIPDSVELSGtvR 245
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gi 16079029 290 C 290
Cdd:cd08014 246 T 246
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| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
210-288 |
8.57e-05 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. 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). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 44.57 E-value: 8.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16079029 210 FRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELEkvrnARISDPLydnipIPVPVNIGTISGGAWPSSVADRVVIEG 288
Cdd:cd08021 184 FDITIKGKGGHGSMPHETVDPIVIAAQIVTALQTIV----SRRVDPL-----DPAVVTIGTFQGGTSFNVIPDTVELKG 253
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| M20_Acy1-like |
cd05667 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
210-288 |
9.26e-03 |
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M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a 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. 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: 349917 [Multi-domain] Cd Length: 403 Bit Score: 38.18 E-value: 9.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16079029 210 FRITVKGLSAHGGTRYEGVSAIEKSMHVITAIQELEKvRNARISDPlydnipiPVPVNIGTISGGAWPSSVADRVVIEG 288
Cdd:cd05667 198 FRITVKGKQTHGSRPWDGIDPIMASAQIIQGLQTIIS-RRIDLTKE-------PAVISIGKINGGTRGNIIPEDAEMVG 268
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| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
81-178 |
9.79e-03 |
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M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.
Pssm-ID: 349885 [Multi-domain] Cd Length: 474 Bit Score: 38.27 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16079029 81 ESPNIVAKKTGAGGG---RSLILNGHIDVVPE---GSVKDWKYEPYQAVEENGKIYGRGSTdmKGGN--TALLFALEALH 152
Cdd:cd03890 43 EVGNVIIRKPATPGYenaPPVILQGHMDMVCEknaDSEHDFEKDPIKLRIDGDWLKATGTT--LGADngIGVAYALAILE 120
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90 100 110
....*....|....*....|....*....|.
gi 16079029 153 ACDVK---LkgDVLFqsVVDEE--CGGAGTL 178
Cdd:cd03890 121 DKDIEhppL--EVLF--TVDEEtgMTGALGL 147
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