|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
11-419 |
0e+00 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 722.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 11 EGLRDEMVKTLVELIKIPAISPDYGYEGEYDKAQKLLEIIKDWPFDKVEVYNAPDERAKNGVRPNILAYYYGEKGEEseR 90
Cdd:PRK13983 1 DELRDEMIELLSELIAIPAVNPDFGGEGEKEKAEYLESLLKEYGFDEVERYDAPDPRVIEGVRPNIVAKIPGGDGKR--T 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 91 LWILTHLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKY 170
Cdd:PRK13983 79 LWIISHMDVVPPGDLSLWE-TDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 171 GIGWLMKEHPELFREDDLVLVPDGGNEDGTFIEVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAYNLDKRLHEK 250
Cdd:PRK13983 158 GIQYLLKKHPELFKKDDLILVPDAGNPDGSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRAAADFALELDEALHEK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 251 YSERDELFDPPESTFEPTMGGNLADSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKERHRkeldgkvlPEIEV 330
Cdd:PRK13983 238 FNAKDPLFDPPYSTFEPTKKEANVDNINTIPGRDVFYFDCRVLPDYDLDEVLKDIKEIADEFEEEYG--------VKIEV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 331 EVLQRGDPAPPTNPNSEIVRLLKEAIKELRGKEAKVGGIGGGTFAAFFRRKGIPAVVWATLDEMAHQPNEYAKIDNMVED 410
Cdd:PRK13983 310 EIVQREQAPPPTPPDSEIVKKLKRAIKEVRGIEPKVGGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYAKISNLIED 389
|
....*....
gi 1828881018 411 AKVMAYLAL 419
Cdd:PRK13983 390 AKVFALLLL 398
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
15-415 |
5.47e-170 |
|
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: 481.57 E-value: 5.47e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 15 DEMVKTLVELIKIPAISPDYGYEGEYDKAQKLLEIIKDWPFDKVEVYNAPDERAKngVRPNILAYYygeKGEESERLWIL 94
Cdd:cd05650 1 EEIIELERDLIRIPAVNPESGGEGEKEKADYLEKKLREYGFYTLERYDAPDERGI--IRPNIVAKI---PGGNDKTLWII 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 95 THLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKYGIGW 174
Cdd:cd05650 76 SHLDTVPPGDLSLWE-TDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEYGIQY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 175 LMKEHpELFREDDLVLVPDGGNEDGTFIEVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAYNLDKRLHEKYSER 254
Cdd:cd05650 155 LLNKF-DLFKKDDLIIVPDFGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFALELDELLHEKFDEK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 255 DELFDPPESTFEPTMGGNLADSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVkERHRKEldgkvlpEIEVEVLQ 334
Cdd:cd05650 234 DDLFNPPYSTFEPTKKEANVPNVNTIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDF-ENSYGA-------GITYEIVQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 335 RGDPAPPTNPNSEIVRLLKEAIKELRGKEAKVGGIGGGTFAAFFRRKGIPAVVWATLDEMAHQPNEYAKIDNMVEDAKVM 414
Cdd:cd05650 306 KEQAPPATPEDSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYIRISHIVKDAKVF 385
|
.
gi 1828881018 415 A 415
Cdd:cd05650 386 A 386
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
6-420 |
1.76e-111 |
|
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 332.62 E-value: 1.76e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 6 VLKEVEGLRDEMVKTLVELIKIPAISPDygyegEYDKAQKLLEIIKDWPFDkVEVYNAPDERakngvrPNILAYYYGEKG 85
Cdd:COG0624 3 VLAAIDAHLDEALELLRELVRIPSVSGE-----EAAAAELLAELLEALGFE-VERLEVPPGR------PNLVARRPGDGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 86 EEseRLWILTHLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEE 165
Cdd:COG0624 71 GP--TLLLYGHLDVVPPGDLELWT-SDPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 166 TGSkYGIGWLMKEHPELFReDDLVLVPDGGNEDGtfIEVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAYNLDK 245
Cdd:COG0624 148 VGS-PGARALVEELAEGLK-ADAAIVGEPTGVPT--IVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 246 rlHEKYSERDELFDPPesTFEPTM--GGnlaDSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKERhrkeldgk 323
Cdd:COG0624 224 --LEFDGRADPLFGRT--TLNVTGieGG---TAVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAAPG-------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 324 vlPEIEVEVLQRGDPAPPTNPNSEIVRLLKEAIKELRGKEAKVGGIGGGTFAAFFRRK-GIPAVVWATLD-EMAHQPNEY 401
Cdd:COG0624 289 --VEVEVEVLGDGRPPFETPPDSPLVAAARAAIREVTGKEPVLSGVGGGTDARFFAEAlGIPTVVFGPGDgAGAHAPDEY 366
|
410
....*....|....*....
gi 1828881018 402 AKIDNMVEDAKVMAYLALR 420
Cdd:COG0624 367 VELDDLEKGARVLARLLER 385
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
18-413 |
6.43e-91 |
|
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: 279.28 E-value: 6.43e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 18 VKTLVELIKIPaiSPDYGYEGEYDKAQKLLEIIKDWPFdKVEVYNAPDERAKngVRPNILAYYYGEKGEESerLWILTHL 97
Cdd:TIGR01910 1 VELLKDLISIP--SVNPPGGNEETIANYIKDLLREFGF-STDVIEITDDRLK--VLGKVVVKEPGNGNEKS--LIFNGHY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 98 DVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSkYGIGWLMK 177
Cdd:TIGR01910 74 DVVPAGDLELWK-TDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEESGE-AGTLYLLQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 178 EhpELFREDDLVLVPDGGNEDGTFIEvaEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAYNLDKRLHEKYSERDEL 257
Cdd:TIGR01910 152 R--GYFKDADGVLIPEPSGGDNIVIG--HKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEEHIYARNSYG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 258 FDPPESTFEPTM--GGnlaDSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKERHRkeldgkVLPEIEVEVLQR 335
Cdd:TIGR01910 228 FIPGPITFNPGVikGG---DWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALSKSDG------WLYENEPVVKWS 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828881018 336 GdpAPPTNPNSEIVRLLKEAIKELRGKEAKVGGIGGGTFAAFFRRKGIPAVVW-ATLDEMAHQPNEYAKIDNMVEDAKV 413
Cdd:TIGR01910 299 G--PNETPPDSRLVKALEAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYgPGDLETAHQVNEYISIKNLVESTKV 375
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
10-420 |
1.53e-77 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 245.67 E-value: 1.53e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 10 VEGLRDEMVKTLVELIKIPAISPdygyEGE-YDKAQKLL-EIIKDWPFDkVEVYNAPDERAK--NGVRPNILAYyygeKG 85
Cdd:PRK08651 1 VEAMMFDIVEFLKDLIKIPTVNP----PGEnYEEIAEFLrDTLEELGFS-TEIIEVPNEYVKkhDGPRPNLIAR----RG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 86 EESERLWILTHLDVVPPGDLskWTVTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGirpKRTVILAFVSDEE 165
Cdd:PRK08651 72 SGNPHLHFNGHYDVVPPGEG--WSVNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAG---DGNIELAIVPDEE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 166 TGSKyGIGWLMKEhpeLFREDDLVLVPDGGNEDgtFIEVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAYNLDK 245
Cdd:PRK08651 147 TGGT-GTGYLVEE---GKVTPDYVIVGEPSGLD--NICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 246 RLHEKYSERDelFDPPESTFE-PTMGGNLADSP---NIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVkerhRKELD 321
Cdd:PRK08651 221 SLSTIKSKYE--YDDERGAKPtVTLGGPTVEGGtktNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDEV----APELG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 322 gkvlPEIEVEVLQRGDPAPpTNPNSEIVRLLKEAIKELRGKEAKVGGIGGGTFAAFFRRKGIPAVVWATLD-EMAHQPNE 400
Cdd:PRK08651 295 ----IEVEFEITPFSEAFV-TDPDSELVKALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGElELAHAPDE 369
|
410 420
....*....|....*....|
gi 1828881018 401 YAKIDNMVEDAKVMAYLALR 420
Cdd:PRK08651 370 YVEVKDVEKAAKVYEEVLKR 389
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
96-420 |
3.95e-63 |
|
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: 205.66 E-value: 3.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 96 HLDVVPPGDLSKWtvtePFKPlVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPkRTVILAFVSDEETGSkYGIGWL 175
Cdd:pfam01546 5 HMDVVPDEETWGW----PFKS-TEDGKLYGRGHDDMKGGLLAALEALRALKEEGLKK-GTVKLLFQPDEEGGM-GGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 176 MKEHPELFREDDLVL---VPDGGNEDGTF---IEVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAynldKRLHE 249
Cdd:pfam01546 78 IEDGLLEREKVDAVFglhIGEPTLLEGGIaigVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLI----LALQD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 250 KYSERDELFDPPESTFepTMGGNLADSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKERHRKeldgkvlpEIE 329
Cdd:pfam01546 154 IVSRNVDPLDPAVVTV--GNITGIPGGVNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGV--------KVE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 330 VEVLQRGdpAPPTNPNSEIVRLLKEAIKELRGKEAK--VGGIGGGTFAAFFRRKGIPAVVWA-TLDEMAHQPNEYAKIDN 406
Cdd:pfam01546 224 VEYVEGG--APPLVNDSPLVAALREAAKELFGLKVEliVSGSMGGTDAAFFLLGVPPTVVFFgPGSGLAHSPNEYVDLDD 301
|
330
....*....|....
gi 1828881018 407 MVEDAKVMAYLALR 420
Cdd:pfam01546 302 LEKGAKVLARLLLK 315
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
18-418 |
2.10e-61 |
|
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: 202.62 E-value: 2.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 18 VKTLVELIKIPAISPDygyEGEYDK-AQKLLEIIKDWPFDkVEVYNAPDEraKNGVRPNIlayyygEKGEESERLWILTH 96
Cdd:cd08011 1 VKLLQELVQIPSPNPP---GDNTSAiAAYIKLLLEDLGYP-VELHEPPEE--IYGVVSNI------VGGRKGKRLLFNGH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 97 LDVVPPGDLSKWTVtEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKYGIGWLM 176
Cdd:cd08011 69 YDVVPAGDGEGWTV-DPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYLL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 177 KEHpeLFREDDLVLVPDGGNEDgtfIEVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAYNLDKRlhekyserde 256
Cdd:cd08011 148 EKV--RIKPNDVLIGEPSGSDN---IRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYEL---------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 257 lfdppESTFEPTM--GGNladSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEvkerhrkeldgkvLPEIEVEVLQ 334
Cdd:cd08011 213 -----EKTVNPGVikGGV---KVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDS-------------IEEVSFEIKS 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 335 RGDPaPPTNPNSEIVRLLKEAIKELRGKEAKVGGIGGGTFAAFFRRKGIPAVVWA-TLDEMAHQPNEYAKIDNMVEDAKV 413
Cdd:cd08011 272 FYSP-TVSNPDSEIVKKTEEAITEVLGIRPKEVISVGASDARFYRNAGIPAIVYGpGRLGQMHAPNEYVEIDELIKVIKV 350
|
....*
gi 1828881018 414 MAYLA 418
Cdd:cd08011 351 HALVA 355
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
21-413 |
2.36e-61 |
|
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: 202.53 E-value: 2.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 21 LVELIKIPAISPDygyEGEydkAQKLLeiiKDWpFDKvEVYNAPDERAKNgvRPNILAYyygeKGEESERLWILT-HLDV 99
Cdd:cd08659 3 LQDLVQIPSVNPP---EAE---VAEYL---AEL-LAK-RGYGIESTIVEG--RGNLVAT----VGGGDGPVLLLNgHIDT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 100 VPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKyGIGWLMkeh 179
Cdd:cd08659 66 VPPGDGDKWS-FPPFSGRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSD-GARALL--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 180 PELFRED-DLVLVPDGGNEDgtfIEVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAYNLDKrlHEKYSERDELF 258
Cdd:cd08659 141 EAGYADRlDALIVGEPTGLD---VVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRT--LFEELPAHPLL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 259 DPPesTFEPTM--GGnlaDSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKerhrkeldgkvlPEIEVEVLQRG 336
Cdd:cd08659 216 GPP--TLNVGVinGG---TQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHE------------AKLTVEVSLDG 278
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828881018 337 DPAPPTNPNSEIVRLLKEAIKELrGKEAKVGGIGGGTFAAFFRR-KGIPAVVWATLD-EMAHQPNEYAKIDNMVEDAKV 413
Cdd:cd08659 279 DPPFFTDPDHPLVQALQAAARAL-GGDPVVRPFTGTTDASYFAKdLGFPVVVYGPGDlALAHQPDEYVSLEDLLRAAEI 356
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
20-418 |
2.21e-52 |
|
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: 179.33 E-value: 2.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 20 TLVELIKIPAISPdygyEGEYDKAQKLLEIIKDWPFDKVEVYNAPDERAkngvrpNILAYYYGEKGEeserlWIL--THL 97
Cdd:cd03894 2 LLARLVAFDTVSR----NSNLALIEYVADYLAALGVKSRRVPVPEGGKA------NLLATLGPGGEG-----GLLlsGHT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 98 DVVPPgDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMmnLGIRPKRTVILAFVSDEETGSKyGIGWLMK 177
Cdd:cd03894 67 DVVPV-DGQKWS-SDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRL--LAAKLRKPLHLAFSYDEEVGCL-GVRHLIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 178 EHPELFREDDLVLVpdgGNEDGTFIEVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDL-AYNLDKRLHEKYSERDE 256
Cdd:cd03894 142 ALAARGGRPDAAIV---GEPTSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLiGKLRELADRLAPGLRDP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 257 LFDPPESTFEPTM--GGNladSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKERHRkeldgkvlPEIEVEVLQ 334
Cdd:cd03894 219 PFDPPYPTLNVGLihGGN---AVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPE--------AGIEVEPLF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 335 RgDPAPPTNPNSEIVRLLKEAikelrGKEAKVGGIGGGTFAAFFRRKGIPAVVWATLD-EMAHQPNEYAKIDNMVEDAKV 413
Cdd:cd03894 288 E-VPGLETDEDAPLVRLAAAL-----AGDNKVRTVAYGTEAGLFQRAGIPTVVCGPGSiAQAHTPDEFVELEQLDRCEEF 361
|
....*
gi 1828881018 414 MAYLA 418
Cdd:cd03894 362 LRRLI 366
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
18-385 |
5.90e-45 |
|
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: 161.37 E-value: 5.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 18 VKTLVELIKIPAISPDYGYEGEYDKAQKLLEIIKDWPFdKVEVYNAPD--ERAkngvrpNILAYYYGEkGEESERLWILT 95
Cdd:cd05675 1 VDLLQELIRIDTTNSGDGTGSETRAAEVLAARLAEAGI-QTEIFVVEShpGRA------NLVARIGGT-DPSAGPLLLLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 96 HLDVVPpGDLSKWTVtEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKYGIGWL 175
Cdd:cd05675 73 HIDVVP-ADASDWSV-DPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 176 MKEHPELFREDDLVL-------VPDGGNEDGTFIEVAEKGILWFRLKVKGQQVHASMPDKGlNA--------HRVAldlA 240
Cdd:cd05675 151 VDNHPELFDGATFALneggggsLPVGKGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRPTDD-NAitrlaealRRLG---A 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 241 YNLDKRLHEKYSER---DELFDPPESTFEPT----------MGGNLAD-------------------SPNIIPGEHEVVF 288
Cdd:cd05675 227 HNFPVRLTDETAYFaqmAELAGGEGGALMLTavpvldpalaKLGPSAPllnamlrntasptmldagyATNVLPGRATAEV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 289 DCRVLPRYSLDDILRDVedvakevkerhrKELDGKvlPEIEVEVLQRgDPAPPTNPNSEIVRLLKEAIKELrGKEAKVGG 368
Cdd:cd05675 307 DCRILPGQSEEEVLDTL------------DKLLGD--PDVSVEAVHL-EPATESPLDSPLVDAMEAAVQAV-DPGAPVVP 370
|
410
....*....|....*....
gi 1828881018 369 I--GGGTFAAFFRRKGIPA 385
Cdd:cd05675 371 YmsPGGTDAKYFRRLGIPG 389
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
8-416 |
6.00e-41 |
|
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: 150.86 E-value: 6.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 8 KEVEGLRDEMVKTLVELIKIPAI----SPDYGY-EGEYDKAQKLLEIIKDWPFDKVEVYNapderakngvrpnilayYYG 82
Cdd:cd03888 1 EEIDKYKDEILEDLKELVAIPSVrdeaTEGAPFgEGPRKALDKFLDLAKRLGFKTKNIDN-----------------YAG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 83 --EKGEESERLWILTHLDVVPPGDLskWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAF 160
Cdd:cd03888 64 yaEYGEGEEVLGILGHLDVVPAGEG--WT-TDPFKPVIKDGKLYGRGTIDDKGPTIAALYALKILKDLGLPLKKKIRLIF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 161 VSDEETGSKyGIGWLMKEHPelfrEDDLVLVPDGGnedgtF-IEVAEKGILWFRLK------------------------ 215
Cdd:cd03888 141 GTDEETGWK-CIEHYFEHEE----YPDFGFTPDAE-----FpVINGEKGIVTVDLTfkidddkgyrlisikggeatnmvp 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 216 -------------------------------------VKGQQVHASMPDKGLNA-HRVALDLA-YNLDKRLHEKYSERDE 256
Cdd:cd03888 211 dkaeavipgkdkeelalsaatdlkgnieiddggveltVTGKSAHASAPEKGVNAiTLLAKFLAeLNKDGNDKDFIKFLAK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 257 LFdpPESTFEPTMGGNLAD--------SPNII---PGEHEVVFDCRVLPRYSLDDILRDVEdvakevkerhrkeldgKVL 325
Cdd:cd03888 291 NL--HEDYNGKKLGINFEDevmgeltlNPGIItldDGKLELGLNVRYPVGTSAEDIIKQIE----------------EAL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 326 PEIEVEVLQRGDPAPP-TNPNSEIVRLLKEAIKELRGKEAKVGGIGGGTFAAFFRRkGI------PAVvwatlDEMAHQP 398
Cdd:cd03888 353 EKYGVEVEGHKHQKPLyVPKDSPLVKTLLKVYEEQTGKEGEPVAIGGGTYARELPN-GVafgpefPGQ-----KDTMHQA 426
|
490
....*....|....*...
gi 1828881018 399 NEYAKIDNMVEDAKVMAY 416
Cdd:cd03888 427 NEFIPIDDLIKALAIYAE 444
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
96-407 |
2.30e-40 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 147.64 E-value: 2.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 96 HLDVVPPgDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMmnLGIRPKRTVILAFVSDEETGSKyGIGWL 175
Cdd:PRK07522 72 HTDVVPV-DGQAWT-SDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPEL--AAAPLRRPLHLAFSYDEEVGCL-GVPSM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 176 MKEHPELFREDDLVLVpdgGNEDGTFIEVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAYNLDkRLHEKYSE-- 253
Cdd:PRK07522 147 IARLPERGVKPAGCIV---GEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLR-DLADRLAApg 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 254 -RDELFDPPESTFEPTM--GGNladSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKERHRKeldgKVLPEIEV 330
Cdd:PRK07522 223 pFDALFDPPYSTLQTGTiqGGT---ALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAELLPEMR----AVHPEAAI 295
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828881018 331 EVLQRGD-PAPPTNPNSEIVRLLkeaiKELRGKEAKvGGIGGGTFAAFFRRKGIPAVVWATLD-EMAHQPNEYAKIDNM 407
Cdd:PRK07522 296 EFEPLSAyPGLDTAEDAAAARLV----RALTGDNDL-RKVAYGTEAGLFQRAGIPTVVCGPGSiEQAHKPDEFVELAQL 369
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
73-415 |
1.97e-39 |
|
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: 145.53 E-value: 1.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 73 RPNILAYYYGEKgeESERLWILT-HLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIR 151
Cdd:cd03895 60 APNVVGTHRPRG--ETGRSLILNgHIDVVPEGPVELWT-RPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 152 PKRTVILAFVSDEETGSKYGIGWLMKEHpelfrEDDLVLVPDGGNEDgtfIEVAEKGILWFRLKVKGQQVHASMPDKGLN 231
Cdd:cd03895 137 PAADVHFQSVVEEECTGNGALAALMRGY-----RADAALIPEPTELK---LVRAQVGVIWFRVKVRGTPAHVAEASEGVN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 232 AHRVALDLAYNLdKRLHEKYSER---DELFD--PPESTFEPTM--GGnlaDSPNIIPGehEVVFDCRV--LPRYSLDDIL 302
Cdd:cd03895 209 AIEKAMHLIQAL-QELEREWNARkksHPHFSdhPHPINFNIGKieGG---DWPSSVPA--WCVLDCRIgiYPGESPEEAR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 303 RDVEDVAKEVKERHRKeldgkvLPEIEVEVLQRGDPAPP--TNPNSEIVRLLKEAIKELRGKEAKVGGIGGGTFAAFFRR 380
Cdd:cd03895 283 REIEECVADAAATDPW------LSNHPPEVEWNGFQAEGyvLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVL 356
|
330 340 350
....*....|....*....|....*....|....*.
gi 1828881018 381 KG-IPAVVWATLDEMAHQPNEYAKIDNMVEDAKVMA 415
Cdd:cd03895 357 YGdIPALCYGPGSRDAHGFDESVDLESLRKITKTIA 392
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
23-405 |
3.92e-39 |
|
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: 144.18 E-value: 3.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 23 ELIKIPAISP-DYGyegeydkAQKLL-EIIKDWPFdKVEVYNapderaKNGVrPNILAYyygeKGEESERLWILTHLDVV 100
Cdd:cd03891 6 ELIRRPSVTPdDAG-------AQDLIaERLKALGF-TCERLE------FGGV-KNLWAR----RGTGGPHLCFAGHTDVV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 101 PPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKYG----IGWLM 176
Cdd:cd03891 67 PPGDLEGWS-SDPFSPTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGtkkvLEWLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 177 KEHpELFredDLVLV--PDGGNEDGTFIEVAEKGILWFRLKVKGQQVHASMPDKGLNA-HRVA--LD--LAYNLDkrlhe 249
Cdd:cd03891 146 ARG-EKI---DYCIVgePTSEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLADNPiHLLApiLAelTATVLD----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 250 kysERDELFDPpeSTFEPTM--GGNLADspNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKevkerhrkeldgKVLPE 327
Cdd:cd03891 217 ---EGNEFFPP--SSLQITNidVGNGAT--NVIPGELKAKFNIRFNDEHTGESLKARIEAILD------------KHGLD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 328 IEVEVLQRGDP--APPtnpnSEIVRLLKEAIKELRGKEAKVGGIGGGTFAAFFRRKGIPAVVWATLDEMAHQPNEYAKID 405
Cdd:cd03891 278 YDLEWKLSGEPflTKP----GKLVDAVSAAIKEVTGITPELSTSGGTSDARFIASYGCPVVEFGLVNATIHKVNERVSVA 353
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
73-383 |
2.31e-34 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 132.28 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 73 RPNILAYYygeKGEESER--LWILTHLDVVPpGDLSKWTVtEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGI 150
Cdd:PRK07906 51 RANVVARL---PGADPSRpaLLVHGHLDVVP-AEAADWSV-HPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTGR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 151 RPKRTVILAFVSDEETGSKYGIGWLMKEHPELFrEDdlvlVPDGGNEDGTF------------IEVAEKGILWFRLKVKG 218
Cdd:PRK07906 126 RPPRDLVFAFVADEEAGGTYGAHWLVDNHPELF-EG----VTEAISEVGGFsltvpgrdrlylIETAEKGLAWMRLTARG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 219 QQVHASMPDKG------------LNAHRVALDLAYNLDKRLHEKYSERDELFDP--PESTFEPT------MGGNLADS-- 276
Cdd:PRK07906 201 RAGHGSMVNDDnavtrlaeavarIGRHRWPLVLTPTVRAFLDGVAELTGLEFDPddPDALLAKLgpaarmVGATLRNTan 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 277 P---------NIIPGEHEVVFDCRVLPRYSlDDILRDVedvakevkerhrKELDGkvlPEIEVEVLQRgDPAPPTNPNSE 347
Cdd:PRK07906 281 PtmlkagykvNVIPGTAEAVVDGRFLPGRE-EEFLATV------------DELLG---PDVEREWVHR-DPALETPFDGP 343
|
330 340 350
....*....|....*....|....*....|....*...
gi 1828881018 348 IVRLLKEAIkELRGKEAKVGG--IGGGTFAAFFRRKGI 383
Cdd:PRK07906 344 LVDAMNAAL-LAEDPGARVVPymLSGGTDAKAFSRLGI 380
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
18-417 |
9.35e-34 |
|
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: 130.53 E-value: 9.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 18 VKTLVELIKIPAISPDYGYEGEYDK-AQKLLEIIKDWPFDkVEVYNAPD-------ERAKNGVRPNILAYyygekgeese 89
Cdd:cd03893 1 LQTLAELVAIPSVSAQPDRREELRRaAEWLADLLRRLGFT-VEIVDTSNgapvvfaEFPGAPGAPTVLLY---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 90 rlwilTHLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSk 169
Cdd:cd03893 70 -----GHYDVQPAGDEDGWD-SDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEESGS- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 170 YGIGWLMKEHPELFREdDLVLVPDG---GNEDGTfIEVAEKGILWFRLKVKG--QQVH-------------------ASM 225
Cdd:cd03893 143 PSLDQLVEAHRDLLAA-DAIVISDStwvGQEQPT-LTYGLRGNANFDVEVKGldHDLHsglyggvvpdpmtalaqllASL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 226 PDK-------GLNAHRVALDLA-YNLDKRLHEKYSE--RDELFDPPESTFEPTM-------GGNLADSPNIIPGEHEVVF 288
Cdd:cd03893 221 RDEtgrilvpGLYDAVRELPEEeFRLDAGVLEEVEIigGTTGSVAERLWTRPALtvlgidgGFPGEGSKTVIPPRARAKI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 289 DCRVLPryslddiLRDVEDVAKEVK---ERHRKELDgkvlpEIEVEVLQRGDPApPTNPNSEIVRLLKEAIKELRGKEAK 365
Cdd:cd03893 301 SIRLVP-------GQDPEEASRLLEahlEKHAPSGA-----KVTVSYVEGGMPW-RSDPSDPAYQAAKDALRTAYGVEPP 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1828881018 366 VGGIGG-GTFAAFFRRK-GIPAVVWATL--DEMAHQPNEYAKIDNMVEDAKVMAYL 417
Cdd:cd03893 368 LTREGGsIPFISVLQEFpQAPVLLIGVGdpDDNAHSPNESLRLGNYKEGTQAEAAL 423
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
70-406 |
4.59e-33 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 127.69 E-value: 4.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 70 NGVRPNILAyyygEKGEESERLWILTHLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVAslyAVRAMMNL- 148
Cdd:PRK08588 45 NDGRANLVA----EIGSGSPVLALSGHMDVVAAGDVDKWT-YDPFELTEKDGKLYGRGATDMKSGLAA---LVIAMIELk 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 149 --GIRPKRTV-ILAFVSDE--ETGSKygigwlmkehpeLFRE----DDLvlvpDG---GNEDGTFIEVAEKGILWFRLKV 216
Cdd:PRK08588 117 eqGQLLNGTIrLLATAGEEvgELGAK------------QLTEkgyaDDL----DAliiGEPSGHGIVYAHKGSMDYKVTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 217 KGQQVHASMPDKGLNAHRVALDLaYNLDKRLHEKYSERDELFDPPesTFEPTM--GGNladSPNIIPGEHEVVFDCRVLP 294
Cdd:PRK08588 181 TGKAAHSSMPELGVNAIDPLLEF-YNEQKEYFDSIKKHNPYLGGL--THVVTIinGGE---QVNSVPDEAELEFNIRTIP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 295 RYSLDDILRDVEDVAKEVKErhrkelDGKVlpEIEVEVLQRGDPApPTNPNSEIVRLLKEAIKELRGKEAKVGGIGGGTF 374
Cdd:PRK08588 255 EYDNDQVISLLQEIINEVNQ------NGAA--QLSLDIYSNHRPV-ASDKDSKLVQLAKDVAKSYVGQDIPLSAIPGATD 325
|
330 340 350
....*....|....*....|....*....|....*
gi 1828881018 375 AAFFRRKG--IPAVVW-ATLDEMAHQPNEYAKIDN 406
Cdd:PRK08588 326 ASSFLKKKpdFPVIIFgPGNNLTAHQVDEYVEKDM 360
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
14-415 |
1.17e-31 |
|
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: 125.18 E-value: 1.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 14 RDEMVKTLVELIKIPAI----SPDYGY---EGEYDKAQKLLEIIKDWPFDKVEVYNApderakngvrpnilaYYYGEKGE 86
Cdd:TIGR01887 1 KDEILEDLKELIAIDSVedleKAKEGApfgEGPRKALDKFLEIAKRDGFTTENVDNY---------------AGYIEYGQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 87 ESERLWILTHLDVVPPGDlsKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEET 166
Cdd:TIGR01887 66 GEEVLGILGHLDVVPAGD--GWT-SPPFEPTIKDGRIYGRGTLDDKGPTIAAYYAMKILKELGLKLKKKIRFIFGTDEES 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 167 GSKygigwLMKEHPELFREDDLVLVPdggneDGTF-IEVAEKGILWFRLK------------------------------ 215
Cdd:TIGR01887 143 GWK-----CIDYYFEHEEMPDIGFTP-----DAEFpIIYGEKGITTLEIKfkddtegdvvlesfkageaynmvpdhatav 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 216 ------------------------------------VKGQQVHASMPDKGLNA-HRVALDLA-YNLDKRLHEKYSERDEL 257
Cdd:TIGR01887 213 isgkklteveqlkfvffiakelegdfevndgtltitLEGKSAHGSAPEKGINAaTYLALFLAqLNLAGGAKAFLQFLAEY 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 258 FDppESTFEPTMG--------GNLADSPNIIPGEHEVVFDCRVLPRYSlddILRDVEDVAKEVKERhrkelDGKVLPEIE 329
Cdd:TIGR01887 293 LH--EDHYGEKLGikfhddvsGDLTMNVGVIDYENAEAGLIGLNVRYP---VGNDPDTMLKNELAK-----ESGVVEVTL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 330 VEVLqrgdpaPPT--NPNSEIVRLLKEAIKELRGKEAKVGGIGGGTFAAFFRRkgipAVVWATL----DEMAHQPNEYAK 403
Cdd:TIGR01887 363 NGYL------KPLyvPKDDPLVQTLMKVYEKQTGDEGEPVAIGGGTYARLMPN----GVAFGALfpgeEDTMHQANEYIM 432
|
490
....*....|..
gi 1828881018 404 IDNMVEDAKVMA 415
Cdd:TIGR01887 433 IDDLLLATAIYA 444
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
17-415 |
1.53e-31 |
|
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: 123.47 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 17 MVKTLVELIKIPaiSPDYGYEGeYDKAQKLL-EIIKDWPFDkvevynaPDERAKNGVRPNILAYYygeKGEESERLWILT 95
Cdd:cd03885 1 MLDLLERLVNIE--SGTYDKEG-VDRVAELLaEELEALGFT-------VERRPLGEFGDHLIATF---KGTGGKRVLLIG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 96 HLDVV-PPGDLSKWtvtePFKplVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKYGIGW 174
Cdd:cd03885 68 HMDTVfPEGTLAFR----PFT--VDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSPGSREL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 175 LMKEHpelfREDDLVLVPDGGNEDGTFIeVAEKGILWFRLKVKGQQVHASM-PDKGLNAhrvALDLAYNLDkRLHekyse 253
Cdd:cd03885 142 IEEEA----KGADYVLVFEPARADGNLV-TARKGIGRFRLTVKGRAAHAGNaPEKGRSA---IYELAHQVL-ALH----- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 254 rdELFDP-PESTFEPTM--GGNladSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKerhrkeldgkvLPEIEV 330
Cdd:cd03885 208 --ALTDPeKGTTVNVGVisGGT---RVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTL-----------VPGTSV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 331 EVlQRGDPAPPTNPNSEIVRLLK--EAIKELRGKEAKVGGIGGGTFAAFFRRKGIPavvwaTLDEM------AHQPNEYA 402
Cdd:cd03885 272 EL-TGGLNRPPMEETPASRRLLAraQEIAAELGLTLDWEATGGGSDANFTAALGVP-----TLDGLgpvgggAHTEDEYL 345
|
410
....*....|...
gi 1828881018 403 KIDNMVEDAKVMA 415
Cdd:cd03885 346 ELDSLVPRIKLLA 358
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
11-407 |
4.80e-31 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 123.27 E-value: 4.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 11 EGLRDEMVKTLVELIKIPAispdYGYEGE---------YDKAQKLLEIIKDWPFDkveVYNAPDerakngvrpnilAYY- 80
Cdd:PRK07205 7 EKVQDACVAAIKTLVSYPS----VLNEGEngtpfgqaiQDVLEATLDLCQGLGFK---TYLDPK------------GYYg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 81 YGEKGEESERLWILTHLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAF 160
Cdd:PRK07205 68 YAEIGQGEELLAILCHLDVVPEGDLSDWQ-TPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 161 VSDEET-------------GSKYGIG-----------------WLM-KEHPELFRE--DDLVLVPDGGNEDGTFIE--VA 205
Cdd:PRK07205 147 GTDEETlwrcmnryneveeQATMGFApdssfpltyaekgllqaKLVgPGSDQLELEvgQAFNVVPAKASYQGPKLEavKK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 206 EKGILWFRLKVKGQQV-------HASMPDKGLNAhrvALDLAYNLDKrlhekyserdeLFDPPESTF------EPTMG-- 270
Cdd:PRK07205 227 ELDKLGFEYVVKENEVtvlgksvHAKDAPQGINA---VIRLAKALVV-----------LEPHPALDFlanvigEDATGln 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 271 --GNLADSPN-----------IIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVkERHRKELDgkVLPEIEVevlqrgd 337
Cdd:PRK07205 293 ifGDIEDEPSgklsfniagltITKEKSEIRIDIRIPVLADKEKLVQQLSQKAQEY-GLTYEEFD--YLAPLYV------- 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828881018 338 papPTnpNSEIVRLLKEAIKELRGKEAKVGGIGGGTFA-------AFfrrkgipAVVWATLDEMAHQPNEYAKIDNM 407
Cdd:PRK07205 363 ---PL--DSELVSTLMSVYQEKTGDDSPAQSSGGATFArtmpncvAF-------GALFPGAPQTEHQANEHIVLEDL 427
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
15-409 |
5.08e-31 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 123.90 E-value: 5.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 15 DEMVKTLVELIKIPAISPDYGYE---GEYDKAQKLLEiikdwpfdkvEVYNAPDERAKNgVRPNILAYYYGEKGEESER- 90
Cdd:PRK08262 44 DAAAERLSEAIRFRTISNRDRAEddaAAFDALHAHLE----------ESYPAVHAALER-EVVGGHSLLYTWKGSDPSLk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 91 -LWILTHLDVVP--PGDLSKWTVtEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETG 167
Cdd:PRK08262 113 pIVLMAHQDVVPvaPGTEGDWTH-PPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQGFQPRRTIYLAFGHDEEVG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 168 SKYG--IGWLMKE---HPELFREDDLVLVPD---GGNEDGTFIEVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDL 239
Cdd:PRK08262 192 GLGAraIAELLKErgvRLAFVLDEGGAITEGvlpGVKKPVALIGVAEKGYATLELTARATGGHSSMPPRQTAIGRLARAL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 240 AyNLDK-----RLHEKYSE------------------RDELFDP---------PES------TFEPTM--GGNLAdspNI 279
Cdd:PRK08262 272 T-RLEDnplpmRLRGPVAEmfdtlapemsfaqrvvlaNLWLFEPlllrvlaksPETaamlrtTTAPTMlkGSPKD---NV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 280 IPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEvkerhrkeldgkvlPEIEVEVLQ-RGDPAPPTNPNSEIVRLLKEAIKE 358
Cdd:PRK08262 348 LPQRATATVNFRILPGDSVESVLAHVRRAVAD--------------DRVEIEVLGgNSEPSPVSSTDSAAYKLLAATIRE 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 359 LRGKEAKVGGI-GGGTFAAFFrrKGI-PAV-----VWATLDEMA--HQPNEYAKIDNMVE 409
Cdd:PRK08262 414 VFPDVVVAPYLvVGATDSRHY--SGIsDNVyrfspLRLSPEDLArfHGTNERISVANYAR 471
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
73-415 |
1.39e-29 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 118.95 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 73 RPNILAYYYGEKgeESERLWILT-HLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIR 151
Cdd:PRK06837 83 APNVVGTYRPAG--KTGRSLILQgHIDVVPEGPLDLWS-RPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 152 PKRTVILAFVSDEETGskyGIGWLMKehpeLFR--EDDLVLVPDggNEDGTFIEvAEKGILWFRLKVKGQQVHASMPDKG 229
Cdd:PRK06837 160 PAARVHFQSVIEEEST---GNGALST----LQRgyRADACLIPE--PTGEKLVR-AQVGVIWFRLRVRGAPVHVREAGTG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 230 LNahrvALDLAYNLDKRL--HEKYSERDELFDPPESTFEPTMGGNL-----ADSPNIIPGehEVVFDCRV--LPRYSLDD 300
Cdd:PRK06837 230 AN----AIDAAYHLIQALreLEAEWNARKASDPHFEDVPHPINFNVgiikgGDWASSVPA--WCDLDCRIaiYPGVTAAD 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 301 ILRDVEDVAKEVKERHRkeldgkVLPEIEVEVLQRGDPAPPT--NPNSEIVRLLKEAIKELRGKEAKVGGIGGGTFAAFF 378
Cdd:PRK06837 304 AQAEIEACLAAAARDDR------FLSNNPPEVVWSGFLAEGYvlEPGSEAEAALARAHAAVFGGPLRSFVTTAYTDTRFY 377
|
330 340 350
....*....|....*....|....*....|....*...
gi 1828881018 379 R-RKGIPAVVWATLDEMAHQPNEYAKIDNMVEDAKVMA 415
Cdd:PRK06837 378 GlYYGIPALCYGPSGEGIHGFDERVDLESVRKVTKTIA 415
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
6-408 |
4.22e-29 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 117.42 E-value: 4.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 6 VLKEVEGLRDEMVKTLVELIKIPAISPDYgyEGeydkaqklLEIIKDWPFDKVEVYNAPDER--AKNGVRPNILAYYyge 83
Cdd:PRK06133 28 LLAAAQQEQPAYLDTLKELVSIESGSGDA--EG--------LKQVAALLAERLKALGAKVERapTPPSAGDMVVATF--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 84 KGEESERLWILTHLDVV-PPGDLSkwtvTEPFKplVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVS 162
Cdd:PRK06133 95 KGTGKRRIMLIAHMDTVyLPGMLA----KQPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 163 DEETGSKyGIGWLMKehpELFREDDLVLVPDGGNEDGTFIeVAEKGILWFRLKVKGQQVHA-SMPDKGLNAhrvALDLAY 241
Cdd:PRK06133 169 DEETGSP-GSRELIA---ELAAQHDVVFSCEPGRAKDALT-LATSGIATALLEVKGKASHAgAAPELGRNA---LYELAH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 242 NLdkrLHEKyserdELFDP-PESTFEPTM--GGnlaDSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEvkerhrk 318
Cdd:PRK06133 241 QL---LQLR-----DLGDPaKGTTLNWTVakAG---TNRNVIPASASAQADVRYLDPAEFDRLEADLQEKVKN------- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 319 eldgKVLPEIEVEV-LQRGDPAPPTNPNSEivRLLKEA---IKELRGK-EAKVGGIGGGTFAAFFRRKGIPAVvwatLDE 393
Cdd:PRK06133 303 ----KLVPDTEVTLrFERGRPPLEANAASR--ALAEHAqgiYGELGRRlEPIDMGTGGGTDAAFAAGSGKAAV----LEG 372
|
410 420
....*....|....*....|.
gi 1828881018 394 M------AHQPNEYAKIDNMV 408
Cdd:PRK06133 373 FglvgfgAHSNDEYIELNSIV 393
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
23-405 |
4.79e-29 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 116.72 E-value: 4.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 23 ELIKIPAISPDygyegeyDK-AQKLL-EIIKDWPFdKVEVYNapderaKNGVrPNILAYyygeKGEESERLWILTHLDVV 100
Cdd:PRK13009 10 DLIRRPSVTPD-------DAgCQDLLaERLEALGF-TCERMD------FGDV-KNLWAR----RGTEGPHLCFAGHTDVV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 101 PPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKYG----IGWLM 176
Cdd:PRK13009 71 PPGDLEAWT-SPPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGtvkvLEWLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 177 KEHpELFredDLVLV--PDGGNEDGTFIEVAEKGILWFRLKVKGQQVHASMPDKGLNA-HRVA--LD--LAYNLDkrlhe 249
Cdd:PRK13009 150 ARG-EKI---DYCIVgePTSTERLGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPiHLAApaLAelAATEWD----- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 250 kysERDELFDPpeSTFEPTM--GGNLADspNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKerhrkeldgkvlPE 327
Cdd:PRK13009 221 ---EGNEFFPP--TSLQITNidAGTGAT--NVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHG------------LD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 328 IEVEVLQRGDP--APPtnpnSEIVRLLKEAIKelrgkeaKVGGI------GGGTF-AAFFRRKGIPAVVWATLDEMAHQP 398
Cdd:PRK13009 282 YTLEWTLSGEPflTPP----GKLVDAVVAAIE-------AVTGItpelstSGGTSdARFIADYGAQVVEFGPVNATIHKV 350
|
....*..
gi 1828881018 399 NEYAKID 405
Cdd:PRK13009 351 NECVSVA 357
|
|
| PRK06915 |
PRK06915 |
peptidase; |
74-415 |
5.59e-29 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 117.10 E-value: 5.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 74 PNILAYYYGEKGEESerlWILT-HLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRP 152
Cdd:PRK06915 81 PNIVATLKGSGGGKS---MILNgHIDVVPEGDVNQWD-HHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIEL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 153 KRTVILAFVSDEETGSKYGIGWLMKEHpelfrEDDLVLVPDGGNEDgtfIEVAEKGILWFRLKVKGQQVHASMPDKGLNA 232
Cdd:PRK06915 157 KGDVIFQSVIEEESGGAGTLAAILRGY-----KADGAIIPEPTNMK---FFPKQQGSMWFRLHVKGKAAHGGTRYEGVSA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 233 HRVALDLAYNLdKRLHEKYSER--DELFD----PPESTFEPTMGGnlaDSPNIIPGEHEVVFDCRVLPRYSLDDILRDVE 306
Cdd:PRK06915 229 IEKSMFVIDHL-RKLEEKRNDRitDPLYKgipiPIPINIGKIEGG---SWPSSVPDSVILEGRCGIAPNETIEAAKEEFE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 307 DVAKEVKER------HRKELD---GKVLP-EIEvevlqrgdpapptnPNSEIVRLLKEAIKELRGK----EAKVGGIGGG 372
Cdd:PRK06915 305 NWIAELNDVdewfveHPVEVEwfgARWVPgELE--------------ENHPLMTTLEHNFVEIEGNkpiiEASPWGTDGG 370
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1828881018 373 TFAAFfrrKGIPAVVWAT-LDEMAHQPNEYAKIDNMVEDAKVMA 415
Cdd:PRK06915 371 LLTQI---AGVPTIVFGPgETKVAHYPNEYIEVDKMIAAAKIIA 411
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
6-415 |
7.19e-29 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 117.17 E-value: 7.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 6 VLKEVEGLRDEMVKTLVELIKIPAISP---DYGYEGEYdKAQKLLEiiKDWPFDKVEVYNAPdERAKNGVRPNILAYYYG 82
Cdd:PRK13013 5 LFAAIEARRDDLVALTQDLIRIPTLNPpgrAYREICEF-LAARLAP--RGFEVELIRAEGAP-GDSETYPRWNLVARRQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 83 ekGEESERLWILTHLDVVPPGDlsKWTVtEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVS 162
Cdd:PRK13013 81 --ARDGDCVHFNSHHDVVEVGH--GWTR-DPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 163 DEETGSKYGIGWLMKEHPELFREDDLVLVPDGGNEDGtfIEVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAYN 242
Cdd:PRK13013 156 DEESGGFGGVAYLAEQGRFSPDRVQHVIIPEPLNKDR--ICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 243 LDKRLHEKY-SERDELFDPPESTFEPTM------GGNLADSPNI-------IPGEHEVVFDCRVLPRYSLDDILRDVEDV 308
Cdd:PRK13013 234 IEERLFPLLaTRRTAMPVVPEGARQSTLninsihGGEPEQDPDYtglpapcVADRCRIVIDRRFLIEEDLDEVKAEITAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 309 AKEVKeRHRKELDGKVLPEIEVEVLQRGDPAPptnpnseIVRLLKEAIKELRGKEAKVgGIGGGTF-----AAFFRRKGI 383
Cdd:PRK13013 314 LERLK-RARPGFAYEIRDLFEVLPTMTDRDAP-------VVRSVAAAIERVLGRQADY-VVSPGTYdqkhiDRIGKLKNC 384
|
410 420 430
....*....|....*....|....*....|..
gi 1828881018 384 PAVVWATLDeMAHQPNEYAKIDNMVEDAKVMA 415
Cdd:PRK13013 385 IAYGPGILD-LAHQPDEWVGIADMVDSAKVMA 415
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
17-406 |
2.01e-27 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 112.82 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 17 MVKTLVELIKIPAISpdygyegeydKAQKLLEIIKDWPFDKVEVYNAPDERAKNGVRPnilaYYYGEKGEESER-LWILT 95
Cdd:cd05681 1 YLEDLRDLLKIPSVS----------AQGRGIPETADFLKEFLRRLGAEVEIFETDGNP----IVYAEFNSGDAKtLLFYN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 96 HLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKyGIGWL 175
Cdd:cd05681 67 HYDVQPAEPLELWT-SDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSP-NLEKF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 176 MKEHPELFREDDLVLVPDGGNEDGTF-IEVAEKGILWFRLKVKG--QQVHASMPD----------KGLNAHRVA------ 236
Cdd:cd05681 145 VAEHADLLKADGCIWEGGGKNPKGRPqISLGVKGIVYVELRVKTadFDLHSSYGAivenpawrlvQALNSLRDEdgrvli 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 237 ---LDLAYNLDKRLHEKYSERDelFDPPE---------------------STFEPTM-------GGNLADSPNIIPGEHE 285
Cdd:cd05681 225 pgfYDDVRPLSEAERALIDTYD--FDPEElrktyglkrplqvegkdplraLFTEPTCningiysGYTGEGSKTILPSEAF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 286 VVFDCRVLPRyslddilRDVEDVAKEVkerhRKELDGKVLPEIEVEVLQrGDPAPPTNPNSEIVRLLKEAIKELRGKEAK 365
Cdd:cd05681 303 AKLDFRLVPD-------QDPAKILSLL----RKHLDKNGFDDIEIHDLL-GEKPFRTDPDAPFVQAVIESAKEVYGQDPI 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1828881018 366 V--GGIGGGTFAAFFRRKGIPAVVW--ATLDEMAHQPNEYAKIDN 406
Cdd:cd05681 371 VlpNSAGTGPMYPFYDALEVPVVAIgvGNAGSNAHAPNENIRIAD 415
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
96-409 |
3.66e-27 |
|
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: 112.73 E-value: 3.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 96 HLDVVP--PGDLSKWTVtEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKYGIG 173
Cdd:cd05674 77 HQDVVPvnPETEDQWTH-PPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPRRTIILAFGHDEEVGGERGAG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 174 WLMKEHPELFREDDLVLVPD--GGNEDGTFIE-------VAEKGILWFRLKVKGQQVHASMPDK----GLNAHRVAL--- 237
Cdd:cd05674 156 AIAELLLERYGVDGLAAILDegGAVLEGVFLGvpfalpgVAEKGYMDVEITVHTPGGHSSVPPKhtgiGILSEAVAAlea 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 238 -----------------------------DLAYNLDKRLHEKYSERDELF---DPP-----ESTFEPTM--GGNladSPN 278
Cdd:cd05674 236 npfppkltpgnpyygmlqclaehsplpprSLKSNLWLASPLLKALLASELlstSPLtrallRTTQAVDIinGGV---KIN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 279 IIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKERHRKEL----DGKVLPEIEVEVLQRGD---PAPPTNPNSEIVRL 351
Cdd:cd05674 313 ALPETATATVNHRIAPGSSVEEVLEHVKNLIADIAVKYGLGLsafgGDVIYSTNGTKLLTSLLspePSPVSSTSSPVWQL 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828881018 352 LKEAIK---ELRGKEAKV--GGIGGGTFAAFFRR--KGI----PAVVWATLDEMAHQPNEYAKIDNMVE 409
Cdd:cd05674 393 LAGTIRqvfEQFGEDLVVapGIMTGNTDTRHYWNltKNIyrftPIRLNPEDLGRIHGVNERISIDDYLE 461
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
16-313 |
9.38e-27 |
|
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: 109.71 E-value: 9.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 16 EMVKTLVELIKIPAISpdygyeGEYDKAQKLLEiikDWpfdkVEVYNAPDERAKNgvrpNILAYYyGEKGEESERLWILT 95
Cdd:cd05651 1 EAIELLKSLIATPSFS------REEHKTADLIE---NY----LEQKGIPFKRKGN----NVWAEN-GHFDEGKPTLLLNS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 96 HLDVVPPGdlSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGiRPKRTVILAFVSDEETGSKYGIGWL 175
Cdd:cd05651 63 HHDTVKPN--AGWT-KDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEG-PLNYNLIYAASAEEEISGKNGIESL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 176 MKEHPELfredDLVLVpdgGNEDGTFIEVAEKGILWFRLKVKGQQVHASMPDkGLNA-HRVALDLAYNLDKRLHEKyser 254
Cdd:cd05651 139 LPHLPPL----DLAIV---GEPTEMQPAIAEKGLLVLDCTARGKAGHAARNE-GDNAiYKALDDIQWLRDFRFDKV---- 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1828881018 255 DELFDPPESTFEPTMGGNladSPNIIPGEHEVVFDCRVLPRYSLDDIlrdVEDVAKEVK 313
Cdd:cd05651 207 SPLLGPVKMTVTQINAGT---QHNVVPDSCTFVVDIRTTEAYTNEEI---FEIIRGNLK 259
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
8-415 |
2.09e-26 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 110.32 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 8 KEVEGLRDEMVKTLVELIKIPAI------SPDYGY-EGEYDKAQKLLEIIKDWPFDKVEVYNapderakngvrpnilayY 80
Cdd:PRK07318 7 KEVEKRKDDLIEDLQELLRINSVrddskaKEGAPFgPGPVKALEKFLEIAERDGFKTKNVDN-----------------Y 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 81 YG--EKGEESERLWILTHLDVVPPGDlsKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVIL 158
Cdd:PRK07318 70 AGhiEYGEGEEVLGILGHLDVVPAGD--GWD-TDPYEPVIKDGKIYARGTSDDKGPTMAAYYALKIIKELGLPLSKKVRF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 159 AFVSDEETGSK----Y------------------------GIGWLMKEHPELFREDDLVL-----------VPD------ 193
Cdd:PRK07318 147 IVGTDEESGWKcmdyYfeheeapdfgfspdaefpiingekGITTFDLVHFEGENEGDYVLvsfksglrenmVPDsaeavi 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 194 GGNEDGTFIE-----VAEKGILW--------FRLKVKGQQVHASMPDKGLNAhrvALDLA-----YNLDKRLHEKYSERD 255
Cdd:PRK07318 227 TGDDLDDLIAafeafLAENGLKGeleeeggkLVLTVIGKSAHGSTPEKGVNA---ATYLAkflnqLNLDGDAKAFLDFAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 256 ELFDppESTFEPTMG--------GNLADSPNIIPGEHEV--VFDCRVlpRY----SLDDILRDVEDVAKEVkerhrkeld 321
Cdd:PRK07318 304 EYLH--EDTRGEKLGiayeddvmGDLTMNVGVFSFDEEKggTLGLNF--RYpvgtDFEKIKAKLEKLIGVT--------- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 322 gkvlpEIEVEVlqrGDPAPP--TNPNSEIVRLLKEAIKELRGKEAKVGGIGGGTFAAFFRRkGIP--AVVWATLDEMaHQ 397
Cdd:PRK07318 371 -----GVELSE---HEHQKPhyVPKDDPLVKTLLKVYEKQTGLKGEEQVIGGGTYARLLKR-GVAfgAMFPGSEDTM-HQ 440
|
490
....*....|....*...
gi 1828881018 398 PNEYAKIDNMVEDAKVMA 415
Cdd:PRK07318 441 ANEYIEIDDLIKAAAIYA 458
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
1-419 |
2.27e-26 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 109.64 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 1 MEFEGVLKEVEGLRDEMVKTLVELIKIPAISPDygyegEYDKAQKLLEIIKDWPFDKVEVynapDeraKNGvrpNILAYY 80
Cdd:PRK13004 1 IPFKLILMLAEKYKADMTRFLRDLIRIPSESGD-----EKRVVKRIKEEMEKVGFDKVEI----D---PMG---NVLGYI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 81 YGEKgeesERLWILTHLDVVPPGDLSKWTVtEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAF 160
Cdd:PRK13004 66 GHGK----KLIAFDAHIDTVGIGDIKNWDF-DPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 161 VSDEETGSkyGIGWLmkehpELFRED----DLVLV--PDGGNedgtfIEVAEKGILWFRLKVKGQQVHASMPDKGLNAHR 234
Cdd:PRK13004 141 TVQEEDCD--GLCWR-----YIIEEDkikpDFVVItePTDLN-----IYRGQRGRMEIRVETKGVSCHGSAPERGDNAIY 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 235 VALDLAYNLdKRLHEKYSERDEL-----------FDPPestfeptmggnladSPNIIPGEHEVVFDCRVLPRYSLDDILR 303
Cdd:PRK13004 209 KMAPILNEL-EELNPNLKEDPFLgkgtltvsdifSTSP--------------SRCAVPDSCAISIDRRLTVGETWESVLA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 304 DVEDVaKEVkerhrKELDGKVlpeiEVEVLQR----GDPAPPT--------NPNSEIVRLLKEAIKELRGKEAKVG---- 367
Cdd:PRK13004 274 EIRAL-PAV-----KKANAKV----SMYNYDRpsytGLVYPTEcyfptwlyPEDHEFVKAAVEAYKGLFGKAPEVDkwtf 343
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1828881018 368 -----GIGGgtfaaffrRKGIPAVVWATLDE-MAHQPNEYAKIDNMVEDAKVMAYLAL 419
Cdd:PRK13004 344 stngvSIAG--------RAGIPTIGFGPGKEpLAHAPNEYTWKEQLVKAAAMYAAIPK 393
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
93-384 |
2.32e-26 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 110.48 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 93 ILTHLDVV--PPGDlskWTvTEPFKPLVKDGKVYGRGSEDNgQSLVASLyaVRAMMNL---GIRPKRTVILAFVSDEETG 167
Cdd:PRK09133 106 LLAHMDVVeaKRED---WT-RDPFKLVEENGYFYGRGTSDD-KADAAIW--VATLIRLkreGFKPKRDIILALTGDEEGT 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 168 SKYGIGWLMKEHPELFrEDDLVLvPDGG----NEDGT----FIEVAEKGILWFRLKVKGQQVHASMPDKGlNA-HRVALD 238
Cdd:PRK09133 179 PMNGVAWLAENHRDLI-DAEFAL-NEGGggtlDEDGKpvllTVQAGEKTYADFRLEVTNPGGHSSRPTKD-NAiYRLAAA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 239 L----AYNLDKRLHE---KYSERDELFDPPE--------------------------------STFEPTM--GGNladSP 277
Cdd:PRK09133 256 LsrlaAYRFPVMLNDvtrAYFKQSAAIETGPlaaamrafaanpadeaaiallsadpsynamlrTTCVATMleGGH---AE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 278 NIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEvkerhrkeldgkvlPEIEVEVLQRGDPAPPTNPNSEIVRllkeAIK 357
Cdd:PRK09133 333 NALPQRATANVNCRIFPGDTIEAVRATLKQVVAD--------------PAIKITRIGDPSPSPASPLRPDIMK----AVE 394
|
330 340 350
....*....|....*....|....*....|....
gi 1828881018 358 ELRGkeAKVGGI-------GGGTFAAFFRRKGIP 384
Cdd:PRK09133 395 KLTA--AMWPGVpvipsmsTGATDGRYLRAAGIP 426
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
23-409 |
7.57e-25 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 104.90 E-value: 7.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 23 ELIKIPAISpdyGYEGEYDKA-QKLLEIIKDWPFD---KVEVYNAPDERAKNgvrpNILAYY-YGEKGeeserLWILTHL 97
Cdd:PRK05111 13 ALIATPSIS---ATDPALDQSnRAVIDLLAGWFEDlgfNVEIQPVPGTRGKF----NLLASLgSGEGG-----LLLAGHT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 98 DVVPpGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAM-MNLGIRPKRtvILAfVSDEET---GSKYgig 173
Cdd:PRK05111 81 DTVP-FDEGRWT-RDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIdLTKLKKPLY--ILA-TADEETsmaGARA--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 174 wLMKEHPelFRED--------DLVLVpdggnedgtfieVAEKGILWFRLKVKGQQVHASMPDKGLNA----HRVALDLaY 241
Cdd:PRK05111 153 -FAEATA--IRPDcaiigeptSLKPV------------RAHKGHMSEAIRITGQSGHSSDPALGVNAielmHDVIGEL-L 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 242 NLDKRLHEKYseRDELFDPPestfEPTM------GGnlaDSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKER 315
Cdd:PRK05111 217 QLRDELQERY--HNPAFTVP----YPTLnlghihGG---DAPNRICGCCELHFDIRPLPGMTLEDLRGLLREALAPVSER 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 316 HrkelDGKvlpeIEVEVLQRGDPAPPTNPNSEIVRLlkeaIKELRGKEAKVggIGGGTFAAFFRRKGIPAVVWATLD-EM 394
Cdd:PRK05111 288 W----PGR----ITVAPLHPPIPGYECPADHQLVRV----VEKLLGHKAEV--VNYCTEAPFIQQLGCPTLVLGPGSiEQ 353
|
410
....*....|....*...
gi 1828881018 395 AHQPNEY---AKIDNMVE 409
Cdd:PRK05111 354 AHQPDEYlelSFIKPTRE 371
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
21-417 |
1.28e-24 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 103.69 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 21 LVELIKIPaiSPDyGYEGEYdkAQKLLEIIKDWPFDkveVYNAPDERAKNGVRpnilayyygekgEESERLWILTHLDVV 100
Cdd:PRK08652 8 LKQLVKIP--SPS-GQEDEI--ALHIMEFLESLGYD---VHIESDGEVINIVV------------NSKAELFVEVHYDTV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 101 PPgdlskwtVTEPFkplVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVilAFVSDEETGSKyGIGWLMKEHP 180
Cdd:PRK08652 68 PV-------RAEFF---VDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGI--AFVSDEEEGGR-GSALFAERYR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 181 ELFReddLVLVPdggnedgTFIEVAEK--GILWFRLKVKGQQVHASMPDKGLNahrvALDLAYNLDKRLHEKYSERDELF 258
Cdd:PRK08652 135 PKMA---IVLEP-------TDLKVAIAhyGNLEAYVEVKGKPSHGACPESGVN----AIEKAFEMLEKLKELLKALGKYF 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 259 DPPEStFEPTMGGNladSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKE--VKERHRKELDGKVLPEIEvevlqrg 336
Cdd:PRK08652 201 DPHIG-IQEIIGGS---PEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEytVKYEYTEIWDGFELDEDE------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 337 dpapptnpnsEIVRLLKEAIKELrGKEAKVGGIGGGTFAAFFRRKGIPAVVWATLD-EMAHQPNEYAKIDNMVEDAKVMA 415
Cdd:PRK08652 270 ----------EIVQLLEKAMKEV-GLEPEFTVMRSWTDAINFRYNGTKTVVWGPGElDLCHTKFERIDVREVEKAKEFLK 338
|
..
gi 1828881018 416 YL 417
Cdd:PRK08652 339 AL 340
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
15-415 |
8.34e-24 |
|
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: 102.25 E-value: 8.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 15 DEMVKTLVELIKIPAISPDyGYEGEYdkAQKLLEIIKDWPFDkVEVYNAPDERAKNGVRPNILAYYYGEK-GEESERLWI 93
Cdd:cd02697 3 DEEVRFLQKLVRVPTDTPP-GNNAPH--AERTAALLQGFGFE-AERHPVPEAEVRAYGMESITNLIVRRRyGDGGRTVAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 94 LTHLDVVPPGDlsKWTVtEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKYGIG 173
Cdd:cd02697 79 NAHGDVVPPGD--GWTR-DPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGELGPG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 174 WLMKEHpeLFREDDLVLVpdggnedGTFIEV--AEKGILWFRLKVKGQQVHASMPDKGLNAHRVA---LDLAYNLDKRLH 248
Cdd:cd02697 156 WLLRQG--LTKPDLLIAA-------GFSYEVvtAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAvaiLNALYALNAQYR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 249 EKYSERDELFDPPESTFEPTMGGNladsPNIIPGEHEVVFDCRVLPryslddilrdvEDVAKEVKERHRKELDG--KVLP 326
Cdd:cd02697 227 QVSSQVEGITHPYLNVGRIEGGTN----TNVVPGKVTFKLDRRMIP-----------EENPVEVEAEIRRVIADaaASMP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 327 EIEVEV--LQRGDPAPPTNPNSEIVRLLKEAIKELRGKEAKVGGIGGGTFAAFFRRKGIPAVVWAT-----LDEMAHQPN 399
Cdd:cd02697 292 GISVDIrrLLLANSMRPLPGNAPLVEAIQTHGEAVFGEPVPAMGTPLYTDVRLYAEAGIPGVIYGAgprtvLESHAKRAD 371
|
410
....*....|....*.
gi 1828881018 400 EYAKIDNMVEDAKVMA 415
Cdd:cd02697 372 ERLQLEDLRRATKVIA 387
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
96-385 |
1.21e-23 |
|
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: 101.58 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 96 HLDVVPPGDlSKWTVtEPFKP-LVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKYGIGW 174
Cdd:cd05646 72 HTDVVPVFE-EKWTH-DPFSAhKDEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGHDGMEK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 175 LMKeHPElFREDDLVLVPDGG--NEDGTF-IEVAEKGILWFRLKVKGQQVHAS--MPDK-GLNAHRValdlaynLDKRLH 248
Cdd:cd05646 150 FVK-TEE-FKKLNVGFALDEGlaSPTEEYrVFYGERSPWWVVITAPGTPGHGSklLENTaGEKLRKV-------IESIME 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 249 EKYSERDELFDPPE------STFEPTM-GGNLAdsPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKErhrkeld 321
Cdd:cd05646 221 FRESQKQRLKSNPNltlgdvTTVNLTMlKGGVQ--MNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGR------- 291
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828881018 322 gkvlpEIEVEVLQRGDPAPPTNPNSEIV--RLLKEAIKELrGKEAKVGGIGGGTFAAFFRRKGIPA 385
Cdd:cd05646 292 -----GVTYEFEQKSPEKDPTSLDDSNPwwAAFKKAVKEM-GLKLKPEIFPAATDSRYIRALGIPA 351
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
204-317 |
3.58e-23 |
|
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: 93.18 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 204 VAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAYNLDKRLHekyserDELFDPPESTFEPTM--GGNladSPNIIP 281
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYG------DIGFDFPRTTLNITGieGGT---ATNVIP 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 1828881018 282 GEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKERHR 317
Cdd:pfam07687 72 AEAEAKFDIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
18-419 |
1.12e-22 |
|
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly(aspartic acid) hydrolase (PAA hydrolase)-like subfamily. PAA hydrolase enzymes are involved in alpha,beta-poly(D,L-aspartic acid) (tPAA) biodegradation. PAA is being extensively studied as a replacement for commercial polycarboxylate components since it can be degraded by enzymes from isolated tPAA degrading bacteria. Thus far, two types of PAA degrading bacteria (Sphingomonas sp. KT-1 and Pedobacter sp. KP-2) have been investigated in detail; the former can completely degrade tPAA of low-molecular weights below 5000, while the latter can degrade high molecular weight tPAA to release oligo(aspartic acid) (OAA) as a product, suggesting two kinds of PAA degrading enzymes. It has been shown that PAA hydrolase-1 from Sphingomonas sp. KT-1 hydrolyzes beta,beta-aspartic acid units in tPAA to produce OAA, and it is suggested that PAA hydrolase-2 hydrolyzes OAA to aspartic acid. Also included in this family is Bradyrhizobium 5-nitroanthranilic acid (5NAA)-aminohydrolase (5NAA-A), a biodegradation enzyme that converts 5NAA to 5-nitrosalicylic acid; 5NAA is a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, and metabolized by Bradyrhizobium species strain JS329.
Pssm-ID: 349891 [Multi-domain] Cd Length: 357 Bit Score: 98.32 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 18 VKTLVELIKIPAisPDYGyegEYDKAQKLLEIIKDWPFDKVEVynapDERAkngvrpNILAYYYGEKGEESerLWILTHL 97
Cdd:cd03896 1 VDTAIELGEIPA--PTFR---EGARADLVAEWMADLGLGDVER----DGRG------NVVGRLRGTGGGPA--LLFSAHL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 98 DVVPPGDlskwtvtEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVIL-AFVSDEETGSKYGIGWLM 176
Cdd:cd03896 64 DTVFPGD-------TPATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFaANVGEEGLGDLRGARYLL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 177 KEHPELFredDLVLVPDGGNedgTFIEVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAYNLDKrLHEKYSerde 256
Cdd:cd03896 137 SAHGARL---DYFVVAEGTD---GVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYE-WAAPYV---- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 257 lfdpPESTFEPTMGGNlADSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKERHrkeldgkvlPEIEVEVLQRG 336
Cdd:cd03896 206 ----PKTTFAAIRGGG-GTSVNRIANLCSMYLDIRSNPDAELADVQREVEAVVSKLAAKH---------LRVKARVKPVG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 337 D-PAPPTNPNSEIVRLLKEAIKELRGKEakvggigggTFAAFFR------RKGIPAVVWATLD-EMAHQPNEYAKIDNMV 408
Cdd:cd03896 272 DrPGGEAQGTEPLVNAAVAAHREVGGDP---------RPGSSSTdanpanSLGIPAVTYGLGRgGNAHRGDEYVLKDDML 342
|
410
....*....|.
gi 1828881018 409 EDAKVMAYLAL 419
Cdd:cd03896 343 KGAKAYLMLAA 353
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
14-414 |
1.31e-21 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 95.50 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 14 RDEMVKTLVELIKIPAISpdyGYEGE-----YDKAQKL-LEIIKDwpfdkvevynapderaKNGvrpNILAYYYGEKGEE 87
Cdd:COG2195 2 PERLLERFLEYVKIPTPS---DHEEAladylVEELKELgLEVEED----------------EAG---NVIATLPATPGYN 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 88 SERLWILTHLDVVPPGDlskwtvTEPFKPLVKDGKVYGRGSE----DNGQSLVASLYAVRAMMNLGIrPKRTVILAFVSD 163
Cdd:COG2195 60 VPTIGLQAHMDTVPQFP------GDGIKPQIDGGLITADGTTtlgaDDKAGVAAILAALEYLKEPEI-PHGPIEVLFTPD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 164 EETGskygigwlMK--EH--PELFREDDLvLVPDGGNEDGTFIEVAekGILWFRLKVKGQQVHA-SMPDKGLNAHRVALD 238
Cdd:COG2195 133 EEIG--------LRgaKAldVSKLGADFA-YTLDGGEEGELEYECA--GAADAKITIKGKGGHSgDAKEKMINAIKLAAR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 239 LAYNLDKrlhekySERDELFDPPESTFEptmGGNLadsPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKERHRK 318
Cdd:COG2195 202 FLAALPL------GRIPEETEGNEGFIH---GGSA---TNAIPREAEAVYIIRDHDREKLEARKAELEEAFEEENAKYGV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 319 eldGKVlpEIEVEvlqrgDPAPP--TNPNSEIVRLLKEAIKELrGKEAKVGGIGGGTFAAFFRRKGIPAVVWATLDEMAH 396
Cdd:COG2195 270 ---GVV--EVEIE-----DQYPNwkPEPDSPIVDLAKEAYEEL-GIEPKIKPIRGGLDGGILSFKGLPTPNLGPGGHNFH 338
|
410
....*....|....*...
gi 1828881018 397 QPNEYAKIDNMVEDAKVM 414
Cdd:COG2195 339 SPDERVSIESMEKAWELL 356
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
75-226 |
1.72e-21 |
|
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: 91.72 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 75 NILAYYYGEKGEEseRLWILTHLDVVPPGDlSKWTVTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKR 154
Cdd:cd03873 1 NLIARLGGGEGGK--SVALGAHLDVVPAGE-GDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1828881018 155 TVILAFVSDEETGSKYGIGWLMKEHPELFREDDLVLVPDGGNEDGTFIEVAEKGILWFRL-----KVKGQQVHASMP 226
Cdd:cd03873 78 TIVVAFTADEEVGSGGGKGLLSKFLLAEDLKVDAAFVIDATAGPILQKGVVIRNPLVDALrkaarEVGGKPQRASVI 154
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
21-406 |
7.07e-21 |
|
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: 93.91 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 21 LVELIKIPAISPDYGYEGEYDKAQK-LLEIIKDWPFDKVEVYNAPD------ERAKNGVRPNILayYYGekgeeserlwi 93
Cdd:cd05680 4 LFELLRIPSVSADPAHKGDVRRAAEwLADKLTEAGFEHTEVLPTGGhplvyaEWLGAPGAPTVL--VYG----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 94 ltHLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRG-SEDNGQSLVAsLYAVRAMMNLGIRPKRTVILAFVSDEETGSKyGI 172
Cdd:cd05680 71 --HYDVQPPDPLELWT-SPPFEPVVRDGRLYARGaSDDKGQVFIH-IKAVEAWLAVEGALPVNVKFLIEGEEEIGSP-SL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 173 GWLMKEHPELFREdDLVLVPDGG--NEDGTFIEVAEKGILWFRLKVKG--QQVHASM----PDKGLNA------------ 232
Cdd:cd05680 146 PAFLEENAERLAA-DVVLVSDTSmwSPDTPTITYGLRGLAYLEISVTGpnRDLHSGSyggaVPNPANAlarllaslhded 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 233 HRVALDLAYN--LDKRLHEK-------YSER--------DELFDPPE-STFE-----PTM------GGNL-ADSPNIIPG 282
Cdd:cd05680 225 GRVAIPGFYDdvRPLTDAEReawaalpFDEAafkaslgvPALGGEAGyTTLErlwarPTLdvngiwGGYQgEGSKTVIPS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 283 EHEVVFDCRVLPRYSLDDILRDVEDVAKEVkerhrkeldgkVLPEIEVEVlQRGDPAPP--TNPNSEIVRLLKEAIKELR 360
Cdd:cd05680 305 KAHAKISMRLVPGQDPDAIADLLEAHLRAH-----------APPGVTLSV-KPLHGGRPylVPTDHPALQAAERALEEAF 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1828881018 361 GKEAkVGGIGGGTF--AAFFRRK-GIPAVV--WATLDEMAHQPNEYAKIDN 406
Cdd:cd05680 373 GKPP-VFVREGGSIpiVALFEKVlGIPTVLmgFGLPDDAIHAPNEKFRLEC 422
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
95-401 |
8.10e-21 |
|
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: 93.70 E-value: 8.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 95 THLDVVPPGDlSKWTvTEPFKPLV-KDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKYGIG 173
Cdd:TIGR01880 78 SHTDVVPVFR-EHWT-HPPFSAFKdEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGME 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 174 WLMKEhpELFREDDLVLVPDGG--NEDGTF-IEVAEKGILWFRLKVKGQQVHAS--MPDKGLNahrvaldlayNLDKRLH 248
Cdd:TIGR01880 156 KFAKT--DEFKALNLGFALDEGlaSPDDVYrVFYAERVPWWVVVTAPGNPGHGSklMENTAME----------KLEKSVE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 249 EKYSERDELFDPPESTFEPTMGG----NLAD-----SPNIIPGEHEVVFDCRVLPrySLDdilrdvedvAKEVKERhrke 319
Cdd:TIGR01880 224 SIRRFRESQFQLLQSNPDLAIGDvtsvNLTKlkggvQSNVIPSEAEAGFDIRLAP--SVD---------FEEMENR---- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 320 LDGKVLP-----EIEVEVLQRGDPAPPTNPNSEIVRLLKEAIKELrGKEAKVGGIGGGTFAAFFRRKGIPAVVWATLDE- 393
Cdd:TIGR01880 289 LDEWCADagegvTYEFSQHSGKPLVTPHDDSNPWWVAFKDAVKEM-GCTFKPEILPGSTDSRYIRAAGVPALGFSPMNNt 367
|
330
....*....|
gi 1828881018 394 --MAHQPNEY 401
Cdd:TIGR01880 368 pvLLHDHNEF 377
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
75-226 |
8.33e-21 |
|
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: 89.80 E-value: 8.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 75 NILAYYygEKGEESERLWILTHLDVVPPGDlSKWTVTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKR 154
Cdd:cd18669 1 NVIARY--GGGGGGKRVLLGAHIDVVPAGE-GDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1828881018 155 TVILAFVSDEETGSKYGIGWLMKEHPELFREDDLVLVPDGGNEDGTFIEVAEKGILWFRL---KVKGQQVHASMP 226
Cdd:cd18669 78 TVVVAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTPLVDALSEaarKVFGKPQHAEGT 152
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
14-406 |
5.46e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 91.35 E-value: 5.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 14 RDEMVKTLVELIKIPAISPdyGYEGEYDKAQKLLEIIKDwpfdkvevynapderakNGVRPNIL-----AYYYGEKGEES 88
Cdd:PRK06446 1 MDEELYTLIEFLKKPSISA--TGEGIEETANYLKDTMEK-----------------LGIKANIErtkghPVVYGEINVGA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 89 ER-LWILTHLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGiRPKRTVILAFVSDEETG 167
Cdd:PRK06446 62 KKtLLIYNHYDVQPVDPLSEWK-RDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKH-KLNVNVKFLYEGEEEIG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 168 SKyGIGWLMKEHPELFREDDLVLVPDGGNEDGT-FIEVAEKGILWFRLKVKGQQ--VHASMPD----------KGLNA-- 232
Cdd:PRK06446 140 SP-NLEDFIEKNKNKLKADSVIMEGAGLDPKGRpQIVLGVKGLLYVELVLRTGTkdLHSSNAPivrnpawdlvKLLSTlv 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 233 ---HRVALDLAYNLDKRLHE-------------------------KYSERDE----LFDPPESTFEPTMGGNLAD-SPNI 279
Cdd:PRK06446 219 dgeGRVLIPGFYDDVRELTEeerellkkydidveelrkalgfkelKYSDREKiaeaLLTEPTCNIDGFYSGYTGKgSKTI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 280 IPGEHEVVFDCRVLPRYSLDDILRDVEDVAKevkerhrkeldgKVLPEIEVEVLQRGDPApPTNPNSEIVRLLKEAIKEL 359
Cdd:PRK06446 299 VPSRAFAKLDFRLVPNQDPYKIFELLKKHLQ------------KVGFNGEIIVHGFEYPV-RTSVNSKVVKAMIESAKRV 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1828881018 360 RGKEAKV--GGIGGGTFAAFFRRKGIPAVVWA----TLDEMAHQPNEYAKIDN 406
Cdd:PRK06446 366 YGTEPVVipNSAGTQPMGLFVYKLGIRDIVSAigvgGYYSNAHAPNENIRIDD 418
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
10-198 |
6.39e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 91.51 E-value: 6.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 10 VEGLRDEMVKTLVELIKIPAISPDYGYEGEYDK-AQKLLEIIKDWPFDKVEVYNAPDERAKNGVR------PNILAYyyg 82
Cdd:PRK07907 13 VAELLPRVRADLEELVRIPSVAADPFRREEVARsAEWVADLLREAGFDDVRVVSADGAPAVIGTRpappgaPTVLLY--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 83 ekgeeserlwilTHLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAmmnLGIRPKRTVILAFVS 162
Cdd:PRK07907 90 ------------AHHDVQPPGDPDAWD-SPPFELTERDGRLYGRGAADDKGGIAMHLAALRA---LGGDLPVGVTVFVEG 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 1828881018 163 DEETGSkYGIGWLMKEHPELFREdDLVLVPDGGNED 198
Cdd:PRK07907 154 EEEMGS-PSLERLLAEHPDLLAA-DVIVIADSGNWS 187
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
73-420 |
5.69e-19 |
|
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: 88.28 E-value: 5.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 73 RPNILAYYYGEkGEESERLWILTHLDVVPpGDLSKWTVtEPFKpLVKDG-KVYGRGSED--NGQSLVASLyavraMMNLG 149
Cdd:cd08012 64 RGNIIVEYPGT-VDGKTVSFVGSHMDVVT-ANPETWEF-DPFS-LSIDGdKLYGRGTTDclGHVALVTEL-----FRQLA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 150 -IRP--KRTVILAFVSDEETGSKYGIGWLMkehpelfreddlvLVPDG---GNEDGT--FIEVAEK-------GILWFRL 214
Cdd:cd08012 135 tEKPalKRTVVAVFIANEENSEIPGVGVDA-------------LVKSGlldNLKSGPlyWVDSADSqpcigtgGMVTWKL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 215 KVKGQQVHASMPDKGLNAHRVALDLAYNLDKRLHEKY----SERDELFDPPeSTFEPTMGGNLADSPNIIPGEHEVVFDC 290
Cdd:cd08012 202 TATGKLFHSGLPHKAINALELVMEALAEIQKRFYIDFpphpKEEVYGFATP-STMKPTQWSYPGGSINQIPGECTICGDC 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 291 RVLPRYSLDDILRDVEDVAKEV-----KERHRKELDGKVLPE------IEVEVLQRGDPAPPTNPNSEIVRLLKEAIKEL 359
Cdd:cd08012 281 RLTPFYDVKEVREKLEEYVDDInanieELPTRGPVSKYVLPAeglrgrVSLEFDEAAASGVACNLDSPGFHALCKATSEV 360
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1828881018 360 RGKEAKVGGIGggtfaaffrrkGIPAVVWAT------------LDEMAHQPNEYAKIDNMVEDAKVMAYLALR 420
Cdd:cd08012 361 VGYVKPYAITG-----------SLPLIRELQdegfdvqitgygLMATYHAKNEYCLLSDFQNGFKVLARTIAQ 422
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
18-418 |
1.74e-18 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 86.32 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 18 VKTLVELIKIPAISPDygyegEYDKAQKLLEIIKDWPFDKVEVynapDERAkngvrpNILAYYygekGEESERLWILTHL 97
Cdd:cd05649 1 TRFLRDLIQIPSESGE-----EKGVVERIEEEMEKLGFDEVEI----DPMG------NVIGYI----GGGKKKILFDGHI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 98 DVVPPGDLSKWTVtEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRP-KRTVILAFVSDEETGSkyGIGWlm 176
Cdd:cd05649 62 DTVGIGNIDNWKF-DPYEGYETDGKIYGRGTSDQKGGLASMVYAAKIMKDLGLRDfAYTILVAGTVQEEDCD--GVCW-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 177 kehPELFRED----DLVLV--PDGGNedgtfIEVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAYNLdKRLHEK 250
Cdd:cd05649 137 ---QYISKADkikpDFVVSgePTDGN-----IYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDI-RQLNPN 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 251 YSERDELFDppeSTFEPTMGGNLADSPNIIPGEHEVVFDCRVL---PRYSLDDILRDV-------EDVAKEVKERHRKEL 320
Cdd:cd05649 208 FPEAPFLGR---GTLTVTDIFSTSPSRCAVPDSCRISIDRRLTvgeTWEGCLEEIRALpavkkygDDVAVSMYNYDRPSY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 321 DGKVlpeIEVEvlqRGDPAPPTNPNSEIVRLLKEAIKELRGKEAkvgGIGGGTFA----AFFRRKGIPAVVWATLDE-MA 395
Cdd:cd05649 285 TGEV---YESE---RYFPTWLLPEDHELVKALLEAYKALFGARP---LIDKWTFStngvSIMGRAGIPCIGFGPGAEnQA 355
|
410 420
....*....|....*....|...
gi 1828881018 396 HQPNEYAKIDNMVEDAKVMAYLA 418
Cdd:cd05649 356 HAPNEYTWKEDLVRCAAGYAAIP 378
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
16-362 |
3.52e-18 |
|
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: 85.10 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 16 EMVKTLVELIKIPAISpdygyEGEYDKAQKLLEIIKDWPFDkVEVynapDErAKNgvrpnilayYYGEKGEESERLWILT 95
Cdd:cd05653 2 DAVELLLDLLSIYSPS-----GEEARAAKFLEEIMKELGLE-AWV----DE-AGN---------AVGGAGSGPPDVLLLG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 96 HLDVVPpGDLskwtvtepfKPLVKDGKVYGRGSEDNGQSLVASLYA-VRAMMNLGIRpkrtVILAFVSDEEtGSKYGIGW 174
Cdd:cd05653 62 HIDTVP-GEI---------PVRVEGGVLYGRGAVDAKGPLAAMILAaSALNEELGAR----VVVAGLVDEE-GSSKGARE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 175 LMKEHPElfreDDLVLVPDGGNEDGtfIEVAEKGILWFRLKVKGQQVHASMPDKglNAHRVALDLAYNLDKRLhEKYSER 254
Cdd:cd05653 127 LVRRGPR----PDYIIIGEPSGWDG--ITLGYRGSLLVKIRCEGRSGHSSSPER--NAAEDLIKKWLEVKKWA-EGYNVG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 255 DELFDppesTFEPTmGGNLADSPNIIPGEHEVVFDCRVLPRYSlddilrdvedvakevKERHRKELDGKvLPEIEVEVlq 334
Cdd:cd05653 198 GRDFD----SVVPT-LIKGGESSNGLPQRAEATIDLRLPPRLS---------------PEEAIALATAL-LPTCELEF-- 254
|
330 340 350
....*....|....*....|....*....|
gi 1828881018 335 rGDPAPP--TNPNSEIVRLLKEAIKELRGK 362
Cdd:cd05653 255 -IDDTEPvkVSKNNPLARAFRRAIRKQGGK 283
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
15-414 |
5.91e-18 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 84.84 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 15 DEMVKTLVELIKIPAISPD---YGYEGEYDKAQKLLEIIKDWPFDKVEVYNAPDerakngvRPNILAYYYGEKGEESerL 91
Cdd:cd08013 1 DDPVSLTQTLVRINSSNPSlsaTGGAGEAEIATYVAAWLAHRGIEAHRIEGTPG-------RPSVVGVVRGTGGGKS--L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 92 WILTHLDVVP----PGDlskwtvtePFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKrtVILAFVSDEE-- 165
Cdd:cd08013 72 MLNGHIDTVTldgyDGD--------PLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGLRGD--VILAAVADEEda 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 166 ---TGSKYGIGWlmkehpelfREDDLVlVPDGGNEDgtfIEVAEKGILWFRLKVKGQQVHASMPDKGLNA------HRVA 236
Cdd:cd08013 142 slgTQEVLAAGW---------RADAAI-VTEPTNLQ---IIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAilkagyFLVA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 237 LDlayNLDKRLHEKYSerDELFDPPESTFEPTMGGnlaDSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKERH 316
Cdd:cd08013 209 LE---EYQQELPERPV--DPLLGRASVHASLIKGG---EEPSSYPARCTLTIERRTIPGETDESVLAELTAILGELAQTV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 317 rkeldgkvlPEIEVEVLQRGDPAPPTNPNSE--IVRLLKEAIKELRGKEAKVGGIGGGTFAAFFRRKGIPAVVWATLDEM 394
Cdd:cd08013 281 ---------PNFSYREPRITLSRPPFEVPKEhpFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGAG 351
|
410 420
....*....|....*....|
gi 1828881018 395 AHQPNEYAKIDNMVEDAKVM 414
Cdd:cd08013 352 LHAKEEWVDVESIRQLREVL 371
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
79-420 |
6.85e-17 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 82.13 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 79 YY--YGEKGEESERLWILTHLDVVPPGdlSKWTVTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKrtV 156
Cdd:PRK08554 52 YYavYGEIGEGKPKLLFMAHFDVVPVN--PEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLNGK--V 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 157 ILAFVSDEETGSKYGIGWLMKEHPELFREDDLVlvpdggNEDGTFI-------------------EVAEKGIL---WFRL 214
Cdd:PRK08554 128 IFAFTGDEEIGGAMAMHIAEKLREEGKLPKYMI------NADGIGMkpiirrrkgfgvtirvpseKVKVKGKLreqTFEI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 215 KVKGQQV-HASMPDKGLNAHRVaLDLAYNLDKRLHEKYSERDELFD----PPESTF---EPTMGGNLADSPN-------I 279
Cdd:PRK08554 202 RTPVVETrHAAYFLPGVDTHPL-IAASHFLRESNVLAVSLEGKFLKgnvvPGEVTLtylEPGEGEEVEVDLGltrllkaI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 280 IP---------------------------GEHEVVFDCRVLpRYSLDDILRDVEDVAKEvkerhrkeldgkVLPEIEVEV 332
Cdd:PRK08554 281 VPlvrapikaekysdygvsitpnvysfaeGKHVLKLDIRAM-SYSKEDIERTLKEVLEF------------NLPEAEVEI 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 333 LQRGDPAPP-TNPNSEIVRLLKEAIKELrGKEAKVGGIGGGTFAAFFRRKGIPAVVWATLDEMAHQPNEYAKIDNMVEDA 411
Cdd:PRK08554 348 RTNEKAGYLfTPPDEEIVKVALRVLKEL-GEDAEPVEGPGASDSRYFTPYGVKAIDFGPKGGNIHGPNEYVEIDSLKKMP 426
|
....*....
gi 1828881018 412 KVMAYLALR 420
Cdd:PRK08554 427 EVYKRIALR 435
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
6-417 |
1.88e-16 |
|
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: 81.11 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 6 VLKEVEGLRDEMVKTLVELIKIPAISPDYGYEGEYDKAQKLL-EIIKDWPFdKVEVYNAPDERAKNG----VRPNILAYY 80
Cdd:cd05676 1 VFKYIDEHQDEFIERLREAVAIQSVSADPEKRPELIRMMEWAaERLEKLGF-KVELVDIGTQTLPDGeelpLPPVLLGRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 81 YGEKGEESerLWILTHLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAF 160
Cdd:cd05676 80 GSDPSKKT--VLIYGHLDVQPAKLEDGWD-TDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 161 VSDEETGSKyGIGWLMKEHPELFRED-DLVLVPDG---GNED-----GTfievaeKGILWFRLKVK-----------GQQ 220
Cdd:cd05676 157 EGMEESGSE-GLDELIEARKDTFFSDvDYVCISDNywlGKKKpcltyGL------RGICYFFIEVEgpnkdlhsgvfGGS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 221 VHASMPD-----------------KGLNAHRVAL---------DLAYNLDKrLHEKYSERDELFDPPESTF-----EPTM 269
Cdd:cd05676 230 VHEPMTDlialmsslvdsdgkiliPGIYDAVAPLteeewelyeKIDFDMEE-YREDIGVRRLLYDNKEELLmhrwrYPSL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 270 ---GGNLADSPN----IIPGehEVV--FDCRVLPRYSLDDILRDVEDVAKEVKerhrKELDGKvlPEIEVEVLQRGDP-- 338
Cdd:cd05676 309 sihGIEGAFSGPgaktVIPA--KVIgkFSIRLVPNMDPEVVEKQVTDYLEKVF----AELKSP--NKLKVYMGHGGKPwv 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 339 APPTNPNSEIVRllkEAIKELRGKEAKVGGIGGGT-FAAFFRR---KGIPAVVWATLDEMAHQPNEYAKIDNMVEDAKVM 414
Cdd:cd05676 381 ADPDHPNYKAAR---KATKRVFGVEPDLTREGGSIpITLTFQEatgKNVMLLPIGAADDGAHSQNEKINRRNYIEGTKLL 457
|
....
gi 1828881018 415 -AYL 417
Cdd:cd05676 458 aAYF 461
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
23-338 |
9.57e-16 |
|
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: 77.70 E-value: 9.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 23 ELIKIPAISPDygyegEYDKAQKLLEII--KDWPFDKVEVynapderaKNGVRPNILAYYygeKGEESERLWILTHLDVV 100
Cdd:cd05652 7 SLVEIPSISGN-----EAAVGDFLAEYLesLGFTVEKQPV--------ENKDRFNVYAYP---GSSRQPRVLLTSHIDTV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 101 PPgdlskwtvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGskyGIGwlMKEHP 180
Cdd:cd05652 71 PP--------FIPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETG---GDG--MKAFN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 181 ELFRED-DLVLVpdGGNEDGTFIeVAEKGILWFRLKVKGQQVHASMPDKGLNAHRVALDLAYNLDKR-LhekysERDELF 258
Cdd:cd05652 138 DLGLNTwDAVIF--GEPTELKLA-SGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDAdL-----PSSELL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 259 DPpeSTFE-PTMGGNLAdsPNIIPGEHEVVFDCRVlpryslddiLRDVEDVAKEVKERHRKELDGKvlPEIEVEVLQRGD 337
Cdd:cd05652 210 GP--TTLNiGRISGGVA--ANVVPAAAEASVAIRL---------AAGPPEVKDIVKEAVAGILTDT--EDIEVTFTSGYG 274
|
.
gi 1828881018 338 P 338
Cdd:cd05652 275 P 275
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
14-412 |
1.25e-15 |
|
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: 77.88 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 14 RDEMVKTLVELIKIPAISpdyGYEGEYDK--AQKL----LEIIKDwpfdkvevynapDERAKNGVRPNILAYYYGEKGEE 87
Cdd:cd05683 2 EDRLINTFLELVQIDSET---LHEKEISKvlKKKFenlgLSVIED------------DAGKTTGGGAGNLICTLKADKEE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 88 SERLWILTHLDVVPPGDLSKwtvtepfKPLVKDGKVYGRGS----EDNGQSLVASLYAVRAMMNLGIrPKRTVILAFVSD 163
Cdd:cd05683 67 VPKILFTSHMDTVTPGINVK-------PPQIADGYIYSDGTtilgADDKAGIAAILEAIRVIKEKNI-PHGQIQFVITVG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 164 EETGSkygIGwlMKE-HPELFrEDDLVLVPDGGNEDGTFIeVAEKGILWFRLKVKGQQVHASM-PDKGLNAHRVALDLAY 241
Cdd:cd05683 139 EESGL---VG--AKAlDPELI-DADYGYALDSEGDVGTII-VGAPTQDKINAKIYGKTAHAGTsPEKGISAINIAAKAIS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 242 NLdkrlheKYSERDELFDPPESTFEptmGGNladSPNIIPGEHEVVFDCRVLPRYSLDDILRDVedvaKEVKERHRKELD 321
Cdd:cd05683 212 NM------KLGRIDEETTANIGKFQ---GGT---ATNIVTDEVNIEAEARSLDEEKLDAQVKHM----KETFETTAKEKG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 322 GKVlpEIEVEVLQrgdPAPPTNPNSEIVRLLKEAIKELrGKEAKVGGIGGGTFAAFFRRKGIPAVVWATLDEMAHQPNEY 401
Cdd:cd05683 276 AHA--EVEVETSY---PGFKINEDEEVVKLAKRAANNL-GLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNER 349
|
410
....*....|.
gi 1828881018 402 AKIDNMVEDAK 412
Cdd:cd05683 350 IPIEDLYDTAV 360
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
6-415 |
1.14e-14 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 75.46 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 6 VLKEVEGLRDEMVKTLVELIKIPAISPDygyEGEYDKAQKLLE-IIKDWPF--DKVEVYnaPDErakngvrPNILAYYYG 82
Cdd:PRK08596 4 LLEQIELRKDELLELLKTLVRFETPAPP---ARNTNEAQEFIAeFLRKLGFsvDKWDVY--PND-------PNVVGVKKG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 83 EKGEESERLWILTHLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVS 162
Cdd:PRK08596 72 TESDAYKSLIINGHMDVAEVSADEAWE-TNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 163 DEETGSKyGigwlMKEHPELFREDDLVLVPD---------GGNEDGtFIEVAEKGIlwFRLKVKGQQVHASMPDKGLNah 233
Cdd:PRK08596 151 GEEVGEA-G----TLQCCERGYDADFAVVVDtsdlhmqgqGGVITG-WITVKSPQT--FHDGTRRQMIHAGGGLFGAS-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 234 rvALDLAYNLDKRLHEkySERDELFDPPESTFEPtmGGNLADsPNIIPGEHEVVF---DCRV------LPRYSLDDILRD 304
Cdd:PRK08596 221 --AIEKMMKIIQSLQE--LERHWAVMKSYPGFPP--GTNTIN-PAVIEGGRHAAFiadECRLwitvhfYPNETYEQVIKE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 305 VED----VAKE---VKErHRK----------ELDGKVLPEIEVevlqrgdpaPPTNPNseiVRLLKEAIKELRGKEAKVG 367
Cdd:PRK08596 294 IEEyigkVAAAdpwLRE-NPPqfkwggesmiEDRGEIFPSLEI---------DSEHPA---VKTLSSAHESVLSKNAILD 360
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1828881018 368 GIGGGTFAAFFRRKGIPAVVW--ATLDEmAHQPNEYAKIDNMVEDAKVMA 415
Cdd:PRK08596 361 MSTTVTDGGWFAEFGIPAVIYgpGTLEE-AHSVNEKVEIEQLIEYTKVIT 409
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
16-198 |
1.91e-13 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 71.60 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 16 EMVKTLVELIKIPAISPdyGYEGEYDK---AQKLLEIIKDW------PFDKVEVYNAPDE------RAKNGVRPNILAYY 80
Cdd:cd05682 1 EILPALSDYIRIPNQSP--LFDPEWATnglLEKAANLIADWvkaqniKGAKVEVVELEGRtpllfvEIPGTEQDDDTVLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 81 YGekgeeserlwiltHLDVVPPgdLSKWTV-TEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILa 159
Cdd:cd05682 79 YG-------------HMDKQPP--FTGWDEgLGPTKPVIRGDKLYGRGGADDGYAIFASLTAIKALQEQGIPHPRCVVL- 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 1828881018 160 FVSDEETGSKYGIGWLMKEHPELfREDDLVLVPDGGNED 198
Cdd:cd05682 143 IEACEESGSADLPFYLDKLKERI-GNVDLVVCLDSGCGN 180
|
|
| PepT-like |
TIGR01883 |
peptidase T-like protein; This model represents a clade of enzymes closely related to ... |
17-416 |
7.11e-13 |
|
peptidase T-like protein; This model represents a clade of enzymes closely related to Peptidase T, an aminotripeptidase found in bacteria. This clade consists of gram positive bacteria of which several additionally contain a Peptidase T gene.
Pssm-ID: 162579 [Multi-domain] Cd Length: 361 Bit Score: 69.58 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 17 MVKTLVELIKIPAISpdyGYEGEYdkAQKLLEIIKDWPFDkVEVYNAPDERAKNGvrpNILAYYYGEKGEESerLWILTH 96
Cdd:TIGR01883 2 LKKYFLELIQIDSES---GKEKAI--LTYLKKQITKLGIP-VSLDEVPAEVSNDN---NLIARLPGTVKFDT--IFFCGH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 97 LDVVPPGDlskwtvtePFKPLVKDGKVYGRGSE----DNGQSLVASLYAVRAMMNLGIrPKRTVILAFVSDEETGSkygI 172
Cdd:TIGR01883 71 MDTVPPGA--------GPEPVVEDGIFTSLGGTilgaDDKAGVAAMLEAMDVLSTEET-PHGTIEFIFTVKEELGL---I 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 173 GwlMKEHPELFREDDLVLVPDGGNEDGTFIeVAEKGILWFRLKVKGQQVHASM-PDKGLNAHRVAldlaynlDKRLHEKY 251
Cdd:TIGR01883 139 G--MRLFDESKITAAYGYCLDAPGEVGNIQ-LAAPTQVKVDATIAGKDAHAGLvPEDGISAISVA-------RMAIHAMR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 252 SER-DElfdppESTFE-PTMGGNLADSpNIIPGEHEVVFDCRVLPRYSLDDILRdvedvAKEVKERHRKELDGKVlpEIE 329
Cdd:TIGR01883 209 LGRiDE-----ETTANiGSFSGGVNTN-IVQDEQLIVAEARSLSFRKAEAQVQT-----MRERFEQAAEKYGATL--EEE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 330 VEVLQRGDPAPPTNPNSEIVRLLKEAIkelrGKEAKVGGIGGGTFAAFFRRKGIPAVVWATLDEMAHQPNEYAKIDNMVE 409
Cdd:TIGR01883 276 TRLIYEGFKIHPQHPLMNIFKKAAKKI----GLKTSEIFSGGGSDANVLNEKGVPTVNLSAGYVHAHTEKETISIEQLVK 351
|
....*...
gi 1828881018 410 DAK-VMAY 416
Cdd:TIGR01883 352 LAElVIAL 359
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
14-406 |
8.76e-12 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 66.69 E-value: 8.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 14 RDEMVKTLVELIKIPAISPDYGYEGEYDKA-QKLLEIIKDWPFDKVEVYnapderaKNGVRPNILAYYYGEKGEESerLW 92
Cdd:PRK08201 13 REAHLEELKEFLRIPSISALSEHKEDVRKAaEWLAGALEKAGLEHVEIM-------ETAGHPIVYADWLHAPGKPT--VL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 93 ILTHLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRG-SEDNGQSLVaSLYAVRAMMNLGIRPKRTVILAFVSDEETGSKYg 171
Cdd:PRK08201 84 IYGHYDVQPVDPLNLWE-TPPFEPTIRDGKLYARGaSDDKGQVFM-HLKAVEALLKVEGTLPVNVKFCIEGEEEIGSPN- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 172 IGWLMKEHPELFREDDLVLVPDGGNEDGT-FIEVAEKGILWFRLKVKGQ---------------------QVHASMPDKg 229
Cdd:PRK08201 161 LDSFVEEEKDKLAADVVLISDTTLLGPGKpAICYGLRGLAALEIDVRGAkgdlhsglyggavpnalhalvQLLASLHDE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 230 lnAHRVALDLAYN----LDKRLHEKYSER-------------DELFDPPESTF------EPTM------GGNLAD-SPNI 279
Cdd:PRK08201 240 --HGTVAVEGFYDgvrpLTPEEREEFAALgfdeeklkrelgvDELFGEEGYTAlertwaRPTLelngvyGGFQGEgTKTV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 280 IPGEHEVVFDCRVLPRYSLDDILRDVEdvakevkerhrKELDGKVLPEIEVEVlQRGDPAPP--TNPNSEIVRLLKEAIK 357
Cdd:PRK08201 318 IPAEAHAKITCRLVPDQDPQEILDLIE-----------AHLQAHTPAGVRVTI-RRFDKGPAfvAPIDHPAIQAAARAYE 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1828881018 358 ELRGKEAKVGGIGGG--TFAAFFRRKGIPAVV--WATLDEMAHQPNEYAKIDN 406
Cdd:PRK08201 386 AVYGTEAAFTRMGGSipVVETFSSQLHIPIVLmgFGLPSENFHAPNEHFHLEN 438
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
6-218 |
5.81e-10 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 60.69 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 6 VLKEVEGLRDEMVKTLVELIKIPAISPDYGYEGEYDKA-QKLLEIIKDWPFDkVEVYNAP-------DERAKNGVRPNIL 77
Cdd:PRK09104 8 VLDHIDANLDASLERLFALLRIPSISTDPAYAADCRKAaDWLVADLASLGFE-ASVRDTPghpmvvaHHEGPTGDAPHVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 78 ayYYGekgeeserlwiltHLDVVPPGDLSKWTvTEPFKPLVKD----GKV-YGRGSEDN-GQsLVASLYAVRAMMNL-GI 150
Cdd:PRK09104 87 --FYG-------------HYDVQPVDPLDLWE-SPPFEPRIKEtpdgRKViVARGASDDkGQ-LMTFVEACRAWKAVtGS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 151 RPKRTVILaFVSDEETGSKYGIGWLMKEHPELfrEDDLVLVPDGG--NEDGTFIEVAEKGILWFRLKVKG 218
Cdd:PRK09104 150 LPVRVTIL-FEGEEESGSPSLVPFLEANAEEL--KADVALVCDTGmwDRETPAITTSLRGLVGEEVTITA 216
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
85-237 |
1.04e-09 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 60.37 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 85 GEESERLWILTHLDVVPpGDLSKW----TVTEPFK-PLVKDgKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILA 159
Cdd:PRK06156 106 GSGSDKVGILTHADVVP-ANPELWvldgTRLDPFKvTLVGD-RLYGRGTEDDKGAIVTALYAMKAIKDSGLPLARRIELL 183
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828881018 160 FVSDEETGskygiGWLMKEHPELFREDDLVLVPDGGNEdgtfIEVAEKGilWfrlkvkgQQVHASMPDKGLNAHRVAL 237
Cdd:PRK06156 184 VYTTEETD-----GDPLKYYLERYTPPDYNITLDAEYP----VVTAEKG--W-------GTIMATFPKRAADGKGAEI 243
|
|
| hydantase |
TIGR01879 |
amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds ... |
111-415 |
1.17e-08 |
|
amidase, hydantoinase/carbamoylase family; Enzymes in this subfamily hydrolize the amide bonds of compounds containing carbamoyl groups or hydantoin rings. These enzymes are members of the broader family of amidases represented by pfam01546.
Pssm-ID: 200138 [Multi-domain] Cd Length: 400 Bit Score: 56.74 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 111 TEPFKPLVKDGK----VYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTV-ILAFVsdEETGSKYGIG-WLMKEHPELFR 184
Cdd:TIGR01879 63 TEPPLEVVLSGShldtVVNGGNFDGQLGVLAGIEVVDALKEAYVVPLHPIeVVAFT--EEEGSRFPYGmWGSRNMVGLAN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 185 EDDLVLVPDGGN---------------------------------EDGTFIEV---------AEKGILWFRLKVKGQQVH 222
Cdd:TIGR01879 141 PEDVRNICDAKGisfaeamkacgpdlpnqplrprgdikayvelhiEQGPVLESngqpigvvnAIAGQRWYKVTLNGESNH 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 223 ASMPDKGLnaHRVALDLAYNLDKRLHEKYSERDelfdppestfePTMG--GNLADSP---NIIPGEHEVVFDCRVLPRYS 297
Cdd:TIGR01879 221 AGTTPMSL--RRDPLVAASRIIHQVEEKAKRGD-----------PTVGtvGKVEARPngvNVIPGKVTFTLDLRHTDAAV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 298 LDDILRDVEDVAKEV-KERHrkeldgkvlPEIEVEVLQRgdpAPPTNPNSEIVRLLKEAIKELrGKEAKVGGIGGGTFAA 376
Cdd:TIGR01879 288 LRDFTQQLENDIKAIsDERD---------IGIDIERWMD---EPPVPCSEELVAALTELCERL-GYNARVMVSGAGHDAQ 354
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1828881018 377 FFR-RKGIPAVVWATLDEMAHQPNEYAKIDNMVEDAKVMA 415
Cdd:TIGR01879 355 ILApIVPIGMIFIPSINGISHNPAEWSNITDCAEGAKVLY 394
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
88-419 |
1.18e-08 |
|
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: 56.30 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 88 SERLWILTHLDVVP-PGDL-SKWTVtepfkplvkDGKVYGRGSEDNGQSLVASLYAvrAMMNLGIRPKRTVILAFVSDEE 165
Cdd:cd05647 53 ASRVILAGHLDTVPvAGNLpSRVEE---------DGVLYGCGATDMKAGDAVQLKL--AATLAAATLKHDLTLIFYDCEE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 166 TGS-KYGIGWLMKEHPELFRED-DLVLVPDGGNedgtfIEVAEKGILWFRLKVKGQQVHASMPDKGLNA-HRVALDLAyn 242
Cdd:cd05647 122 VAAeLNGLGRLAEEHPEWLAADfAVLGEPTDGT-----IEGGCQGTLRFKVTTHGVRAHSARSWLGENAiHKLAPILA-- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 243 ldkRLHEkYSERDELFDPPE------STFEPTMGGNladspNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVakevkerh 316
Cdd:cd05647 195 ---RLAA-YEPRTVNIDGLTyreglnAVFISGGVAG-----NVIPDEARVNLNYRFAPDKSLAEAIAHVREV-------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 317 rkeLDGKVLpEIEVEvlqrgDPAPPTNP--NSEIVRLLKEAIKElrgkeaKVGGIGGGTFAAFFRRKGIPAVVWAtldem 394
Cdd:cd05647 258 ---FEGLGY-EIEVT-----DLSPGALPglDHPVARDLIEAVGG------KVRAKYGWTDVARFSALGIPAVNFG----- 317
|
330 340
....*....|....*....|....*
gi 1828881018 395 AHQPNEYAKIDNMVEDAKVMAYLAL 419
Cdd:cd05647 318 PGDPLLAHKRDEQVPVEQITACAAI 342
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
15-362 |
1.27e-08 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 56.12 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 15 DEMVKTLVELIKIPAISPDygyegEYDKAQKLLEIIKDWPFdkvEVYnaPDErAKNGVrpnilayyyGEKGEESERLWIL 94
Cdd:PRK04443 6 LEARELLKGLVEIPSPSGE-----EAAAAEFLVEFMESHGR---EAW--VDE-AGNAR---------GPAGDGPPLVLLL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 95 THLDVVPpGDLskwtvtePFKplVKDGKVYGRGSEDNGQSLVASLYAVRAmmnLGIRPKRTVILAFVSDEETGSKYGIGW 174
Cdd:PRK04443 66 GHIDTVP-GDI-------PVR--VEDGVLWGRGSVDAKGPLAAFAAAAAR---LEALVRARVSFVGAVEEEAPSSGGARL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 175 LM-KEHPelfredDLVLV--PDGGneDGtfIEVAEKGILWFRLKVKGQQVHASMPdkGLNAHRVALDLAYNLDKRLhEKY 251
Cdd:PRK04443 133 VAdRERP------DAVIIgePSGW--DG--ITLGYKGRLLVTYVATSESFHSAGP--EPNAAEDAIEWWLAVEAWF-EAN 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 252 SERDELFD---PPESTFEPTMGGnladspniIPGEHEVVFDCRVLPRYSLDDIlrdvedvakevkerhRKELDGKvLPEI 328
Cdd:PRK04443 200 DGRERVFDqvtPKLVDFDSSSDG--------LTVEAEMTVGLRLPPGLSPEEA---------------REILDAL-LPTG 255
|
330 340 350
....*....|....*....|....*....|....*.
gi 1828881018 329 EVEVlqrGDPAPP--TNPNSEIVRLLKEAIKELRGK 362
Cdd:PRK04443 256 TVTF---TGAVPAymVSKRTPLARAFRVAIREAGGT 288
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
69-191 |
3.36e-08 |
|
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: 55.43 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 69 KNGVRPNILAYYYGEKGEESER--LWiLTHLDVVPPGDLSKWTvTEPFKPLVKDGKVYGRGSEDNGQSLVASLYAVramM 146
Cdd:cd05677 51 GPGTNPIVLATFSGNSSDAKRKriLF-YGHYDVIPAGETDGWD-TDPFTLTCENGYLYGRGVSDNKGPLLAAIYAV---A 125
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1828881018 147 NLGIRPKRTVILAFV--SDEETGSKyGIGWLMKEHPELFREDDLVLV 191
Cdd:cd05677 126 ELFQEGELDNDVVFLieGEEESGSP-GFKEVLRKNKELIGDIDWILL 171
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
96-420 |
9.75e-08 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 53.81 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 96 HLDVVPPGDlskwtvtEPFKPL--VKDGKVYGRGSEDNGQSLVASLYAVRAM------MNLGIRpkrtVILAfvSDEETG 167
Cdd:PRK07338 100 HMDTVFPAD-------HPFQTLswLDDGTLNGPGVADMKGGIVVMLAALLAFersplaDKLGYD----VLIN--PDEEIG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 168 SkYGIGWLMKehpELFREDDLVLVPDGGNEDGTFIEvAEKGILWFRLKVKGQQVHASM-PDKGLNAHRVALDLAYnldkR 246
Cdd:PRK07338 167 S-PASAPLLA---ELARGKHAALTYEPALPDGTLAG-ARKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAELAL----A 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 247 LHEKYSERDELfdppesTFEPTM--GGNladSPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKERHrkeldgkv 324
Cdd:PRK07338 238 LHALNGQRDGV------TVNVAKidGGG---PLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRH-------- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 325 lpEIEVEVLQR-GDPAPPTNPNSEIVRLLKEAIKELRGKEAK---VGGI--GGGTFAAffrrkGIPavvwaTLDEMA--- 395
Cdd:PRK07338 301 --GVSLHLHGGfGRPPKPIDAAQQRLFEAVQACGAALGLTIDwkdSGGVcdGNNLAAA-----GLP-----VVDTLGvrg 368
|
330 340
....*....|....*....|....*...
gi 1828881018 396 ---HQPNEYAKIDNMVEDAKVMAYLALR 420
Cdd:PRK07338 369 gniHSEDEFVILDSLVERAQLSALILMR 396
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
212-366 |
2.94e-07 |
|
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: 52.22 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 212 FRLKVKGQQVHASMPDKGLNAHRVALDLAYnldkRLHEKYSERdelFDPPES------TFEptmGGNladSPNIIPGEHE 285
Cdd:cd03886 174 FEITVKGKGGHGASPHLGVDPIVAAAQIVL----ALQTVVSRE---LDPLEPavvtvgKFH---AGT---AFNVIPDTAV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 286 VVFDCRVLPRYSLDDILRDVEDVAKEVKERHRKELDgkvlpeievevLQRGDPAPPTNPNSEIVRLLKEAIKELRGKEAK 365
Cdd:cd03886 241 LEGTIRTFDPEVREALEARIKRLAEGIAAAYGATVE-----------LEYGYGYPAVINDPELTELVREAAKELLGEEAV 309
|
.
gi 1828881018 366 V 366
Cdd:cd03886 310 V 310
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
96-414 |
4.89e-07 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 51.72 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 96 HLDVvPPGDLSKWTVTEPFKPLVK--DGK--------------------VYGRGSEDNGQSLVASLYAVRAMMNLGIRPK 153
Cdd:cd05678 68 HLDG-QPVDPSKWDQKSPYTPVLKrkDAAgnweeinwdaifsnldpewrVFARAAADDKGPIMMMLAALDALKAGGIAPK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 154 RTVILAFVSDEETGSKyGIGWLMKEHPELFREDDLVLVpDG-----GNEDGTFievAEKGILWFRLKVKGQQV--H---- 222
Cdd:cd05678 147 FNVKIILDSEEEKGSP-SLPKAVKEYKELLAADALIIM-DGpahatNKPTLTF---GCRGIATATLTTYGAKVpqHsghy 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 223 ---------------ASMPDK-----------GLNAHRVALDLAYN-------LDKRLHEKYSER-----DELFDPPEST 264
Cdd:cd05678 222 gnyapnpafrlssllASMKDDtgkvtipgfydGISIDEETQKILAAvpddeesINKRLGIAQTDKvgrnyQEALQYPSLN 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 265 FEPTMGGNLADSP-NIIPGEHEVVFDCRVLP----RYSLDDILRDVE---------DVAKEVKERHRKeldgkvlpeIEV 330
Cdd:cd05678 302 VRGMESGWKGDKVrTIIPEIAEAEIDIRLVPesdgPYLLDLVKAHIEkqgyfvtdrAPTDEERLAHDK---------IAK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 331 EVLQRGDPAPPTNPNSEIVRLLKEAIKELRGKEAKVGGIGGGT--FAAFFRRKGIPAVVWATL--DEMAHQPNEYAKIDN 406
Cdd:cd05678 373 FTYRNGADAFRTDINSPIGNWLRKALTDEFGEEPIQIRMMGGTvpIAPFVNVLDIPAIIVPMVnmDNNQHSPNENLRIGN 452
|
....*...
gi 1828881018 407 MVEDAKVM 414
Cdd:cd05678 453 IRTGIRTC 460
|
|
| PRK12892 |
PRK12892 |
allantoate amidohydrolase; Reviewed |
75-420 |
5.54e-07 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 183817 [Multi-domain] Cd Length: 412 Bit Score: 51.25 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 75 NILAYYYGEKGEESerLWILTHLDVVPPGdlskwtvtepfkplvkdgkvygrGSEDNGQSLVASLYAVRAMMNLGIRPKR 154
Cdd:PRK12892 63 NVFGRLPGPGPGPA--LLVGSHLDSQNLG-----------------------GRYDGALGVVAGLEAARALNEHGIATRH 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 155 TVILAFVSDEEtGSKYGIGWL-MKEHPELFREDDLVLVPDGGN----------------------------------EDG 199
Cdd:PRK12892 118 PLDVVAWCDEE-GSRFTPGFLgSRAYAGRLDPADALAARCRSDgvplrdalaaaglagrprpaadrarpkgyleahiEQG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 200 TFIEVAE---------KGILWFRLKVKGQQVHA-SMP-----DKGLNAHR--VALDlaynldkrlhekysERDELFDPPE 262
Cdd:PRK12892 197 PVLEQAGlpvgvvtgiVGIWQYRITVTGEAGHAgTTPmalrrDAGLAAAEmiAAID--------------EHFPRVCGPA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 263 STfepTMGGNLAD--SPNIIPGEHEVVFDCRVLPRYSLDDILRDVEDVAKEVKERHRKELDgkvlpeieVEVLQRGDPAP 340
Cdd:PRK12892 263 VV---TVGRVALDpgSPSIIPGRVEFSFDARHPSPPVLQRLVALLEALCREIARRRGCRVS--------VDRIAEYAPAP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 341 ptnPNSEIVRLLKEAIKELRGKEAKVGGiGGGTFAAFFRRKGIPAVVWA-TLDEMAHQPNEYAKIDNMVEDAKVMAYLAL 419
Cdd:PRK12892 332 ---CDAALVDALRAAAEAAGGPYLEMPS-GAGHDAQNMARIAPSAMLFVpSKGGISHNPAEDTSPADLAQGARVLADTLR 407
|
.
gi 1828881018 420 R 420
Cdd:PRK12892 408 R 408
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
15-261 |
2.25e-06 |
|
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: 49.65 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 15 DEMVKTLVELIKIPAISpdyGYEGEYDKAQKLLEIIKDWPFdkvevYNAPDERAKNGV------RPNILAYYYGEKgeES 88
Cdd:cd05654 1 ERLEQLLKSLVSWPSVT---GTEGERSFADFLKEILKELPY-----FKENPSHVWQLLppddlgRRNVTALVKGKK--PS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 89 ERLWILT-HLDVVPPGDLSKWT--------VTEPFKPLV--------KDGK----VYGRGSEDNGQSLVASLYAVRAMMN 147
Cdd:cd05654 71 KRTIILIsHFDTVGIEDYGELKdiafdpdeLTKAFSEYVeeldeevrEDLLsgewLFGRGTMDMKSGLAVHLALLEQASE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 148 LGIRPKrTVILAFVSDEETGSKyGIGWLMKEHPELFREDDL---------VLVPDGGNEDGTFIEVAEKGILWFRLKVKG 218
Cdd:cd05654 151 DEDFDG-NLLLMAVPDEEVNSR-GMRAAVPALLELKKKHDLeyklainsePIFPQYDGDQTRYIYTGSIGKILPGFLCYG 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1828881018 219 QQVHASMPDKGLNAHRVALDLAYNLDKRLHEKYSERDELFDPP 261
Cdd:cd05654 229 KETHVGEPFAGINANLMASEITARLELNADLCEKVEGEITPPP 271
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
212-363 |
3.36e-06 |
|
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273857 [Multi-domain] Cd Length: 363 Bit Score: 48.88 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 212 FRLKVKGQQVHASMPDKGLNAhrvaLDLAYNLDKRLHEKYSERDELFDPPESTFEPTMGGNladSPNIIPGEHEVVFDCR 291
Cdd:TIGR01891 173 FEVTIHGKGAHAARPHLGRDA----LDAAAQLVVALQQIVSRNVDPSRPAVVSVGIIEAGG---APNVIPDKASMSGTVR 245
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828881018 292 VLPRYSLDDILRDVEDVAKEVKERHRkeldGKVlpEIEVEVLqrgdpAPPTNPNSEIVRLLKEAIKELRGKE 363
Cdd:TIGR01891 246 SLDPEVRDQIIDRIERIVEGAAAMYG----AKV--ELNYDRG-----LPAVTNDPALTQILKEVARHVVGPE 306
|
|
| PRK09290 |
PRK09290 |
allantoate amidohydrolase; Reviewed |
75-415 |
6.46e-06 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 47.84 E-value: 6.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 75 NILAYYygeKGEESERLWILT--HLDVVPPGdlskwtvtepfkplvkdGK---VYGrgsedngqsLVASLYAVRAMMNLG 149
Cdd:PRK09290 61 NLFGRL---EGRDPDAPAVLTgsHLDTVPNG-----------------GRfdgPLG---------VLAGLEAVRTLNERG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 150 IRPKRTV-ILAFvSDEEtGSKYGI---------GWLMKEHPELFREDDLVLVPD-----GGNED------------GTFI 202
Cdd:PRK09290 112 IRPRRPIeVVAF-TNEE-GSRFGPamlgsrvftGALTPEDALALRDADGVSFAEalaaiGYDGDeavgaararrdiKAFV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 203 EV---------AEK----------GILWFRLKVKGQQVHA---SMP---DKGLNAHRVALDLaynldkrlHEKYSERDel 257
Cdd:PRK09290 190 ELhieqgpvleAEGlpigvvtgivGQRRYRVTFTGEANHAgttPMAlrrDALLAAAEIILAV--------ERIAAAHG-- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 258 fDPPESTFeptmgGNLA---DSPNIIPGehEVVF--DCRVLPRYSLDDILRDVEDVAKEVKERHrkeldgKVlpEIEVEV 332
Cdd:PRK09290 260 -PDLVATV-----GRLEvkpNSVNVIPG--EVTFtlDIRHPDDAVLDALVAELRAAAEAIAARR------GV--EVEIEL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 333 LQRgdpAPPTNPNSEIVRLLKEAIKELrGKEAKVGGIGGGTFAAFFRRkGIPAvvwATL-----DEMAHQPNEYAKIDNM 407
Cdd:PRK09290 324 ISR---RPPVPFDPGLVAALEEAAERL-GLSYRRLPSGAGHDAQILAA-VVPT---AMIfvpsvGGISHNPAEFTSPEDC 395
|
....*...
gi 1828881018 408 VEDAKVMA 415
Cdd:PRK09290 396 AAGANVLL 403
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
212-420 |
7.92e-06 |
|
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 47.80 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 212 FRLKVKGQQVHASMPDKGLNAhrvaLDLAYNLDKRLHEKYSERdelFDPPES------TFEptmGGnlaDSPNIIPGEHE 285
Cdd:COG1473 186 FEITIKGKGGHAAAPHLGIDP----IVAAAQIVTALQTIVSRN---VDPLDPavvtvgIIH---GG---TAPNVIPDEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 286 VVFDCRVLPRYSLDDILRDVEDVAKEVKERHRKeldgkvlpEIEVEVLQRgdpAPPTNPNSEIVRLLKEAIKELRGKEA- 364
Cdd:COG1473 253 LEGTVRTFDPEVRELLEERIERIAEGIAAAYGA--------TAEVEYLRG---YPPTVNDPELTELAREAAREVLGEENv 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828881018 365 -KVGGIGGGT-FAAFFRRkgIPAVVW------ATLDEMAHQPneYAKIDnmvED-----AKVMAYLALR 420
Cdd:COG1473 322 vDAEPSMGSEdFAYYLQK--VPGAFFflgagnPGTVPPLHSP--KFDFD---EKalpigAKALAALALD 383
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
75-415 |
2.22e-05 |
|
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.
Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 46.36 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 75 NILAYYygeKGEESERLWILT--HLDVVPPGdlskwtvtepfkplvkdGK---VYGrgsedngqsLVASLYAVRAMMNLG 149
Cdd:cd03884 53 NLFGRL---EGTDPDAPPVLTgsHLDTVPNG-----------------GRydgILG---------VLAGLEALRALKEAG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 150 IRPKRTVILAFVSDEE--------TGSKYGIGWLMKEHPELFREDDLVLVPD-----GGNED-----------GTFIE-- 203
Cdd:cd03884 104 IRPRRPIEVVAFTNEEgsrfppsmLGSRAFAGTLDLEELLSLRDADGVSLAEalkaiGYDGDrpasarrpgdiKAYVElh 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 204 -----VAEK------------GILWFRLKVKGQQVHA---SMP---DKGLNAHRVAL---DLAYNLDKRLHekyserdel 257
Cdd:cd03884 184 ieqgpVLEEeglpigvvtgiaGQRWLEVTVTGEAGHAgttPMAlrrDALLAAAELILaveEIALEHGDDLV--------- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 258 fdppeSTFeptmgGNLA---DSPNIIPGEHEVVFDCRvlprySLDDILRD--VEDVAKEVKERHRKEldgKVlpEIEVEV 332
Cdd:cd03884 255 -----ATV-----GRIEvkpNAVNVIPGEVEFTLDLR-----HPDDAVLDamVERIRAEAEAIAAER---GV--EVEVER 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 333 LQRgdpAPPTNPNSEIVRLLKEAIKELrGKEAKVGGIGGGTFAAFFRRKG------IPAVvwatlDEMAHQPNEYAKIDN 406
Cdd:cd03884 315 LWD---SPPVPFDPELVAALEAAAEAL-GLSYRRMPSGAGHDAMFMARICptamifVPSR-----DGISHNPAEYTSPED 385
|
....*....
gi 1828881018 407 MVEDAKVMA 415
Cdd:cd03884 386 LAAGVQVLL 394
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
93-223 |
3.58e-04 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 42.46 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 93 ILTHLDVVPP-GDLSKWtvtePFKplVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKYG 171
Cdd:PRK07473 80 IAGHMDTVHPvGTLEKL----PWR--REGNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFTPDEEVGTPST 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1828881018 172 IGWLMKEHpelfREDDLVLVPDGGNEDGTFIeVAEKGILWFRLKVKGQQVHA 223
Cdd:PRK07473 154 RDLIEAEA----ARNKYVLVPEPGRPDNGVV-TGRYAIARFNLEATGRPSHA 200
|
|
| Iap |
COG2234 |
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ... |
130-170 |
5.00e-04 |
|
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism];
Pssm-ID: 441835 [Multi-domain] Cd Length: 257 Bit Score: 41.66 E-value: 5.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1828881018 130 DNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEET---GSKY 170
Cdd:COG2234 81 DNASGVAALLELARALAALGPKPKRTIRFVAFGAEEQgllGSRY 124
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
96-194 |
8.03e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 41.44 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 96 HLDVVPpGDLSKWTV-TEPFKPLVKDGKVYGRGSEDN-GQSLV--ASLYAVRAMMN--LGIRPKrtviLAFVSDEETGSk 169
Cdd:PRK07079 93 HGDVVR-GYDEQWREgLSPWTLTEEGDRWYGRGTADNkGQHTInlAALEQVLAARGgrLGFNVK----LLIEMGEEIGS- 166
|
90 100
....*....|....*....|....*
gi 1828881018 170 YGIGWLMKEHPELFREdDLVLVPDG 194
Cdd:PRK07079 167 PGLAEVCRQHREALAA-DVLIASDG 190
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
96-357 |
8.32e-04 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 41.31 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 96 HLDVVPpGDLskwtvtepfKPLVKDGKVYGRGSEDNGQSLVASLYAVRAMMNLGIRpkrtVILAFVSDEETGSKYGigwl 175
Cdd:PRK00466 68 HVDTVP-GYI---------EPKIEGEVIYGRGAVDAKGPLISMIIAAWLLNEKGIK----VMVSGLADEESTSIGA---- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 176 mkehPELFREDD---LVLVPDGGNEDGTFIEVaeKGILWFRLKVKGQQVHASMPDKGLnahrvALDLAynldKRLHEKYs 252
Cdd:PRK00466 130 ----KELVSKGFnfkHIIVGEPSNGTDIVVEY--RGSIQLDIMCEGTPEHSSSAKSNL-----IVDIS----KKIIEVY- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 253 ERDELFDPPESTfePTMGGNlADSPNIIPGEHEVVFDCRVLPRYSLDDILrdvedvakevKERHRKeldgkvLPEIEVEV 332
Cdd:PRK00466 194 KQPENYDKPSIV--PTIIRA-GESYNVTPAKLYLHFDVRYAINNKRDDLI----------SEIKDK------FQECGLKI 254
|
250 260 270
....*....|....*....|....*....|..
gi 1828881018 333 lqrGDPAPP--TNPNSEIVR-----LLKEAIK 357
Cdd:PRK00466 255 ---VDETPPvkVSINNPVVKalmraLLKQNIK 283
|
|
| Peptidase_M28 |
pfam04389 |
Peptidase family M28; |
120-182 |
1.22e-03 |
|
Peptidase family M28;
Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 39.58 E-value: 1.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1828881018 120 DGKVYGRGSEDNGQSLVASLYAVRAMMNLGiRPKRTVILAFVSDEET---GSKYgigwLMKEHPEL 182
Cdd:pfam04389 22 DSVGTGPGADDNASGVAALLELARVLAAGQ-RPKRSVRFLFFDAEEAgllGSHH----FAKSHPPL 82
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
215-371 |
1.72e-03 |
|
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. 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: 349939 [Multi-domain] Cd Length: 365 Bit Score: 40.34 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 215 KVKGQQVHASMPDKGLNAHRVAlDLAYNLDKRLHekyserdelFDPPES-TFEPTMGGNLADSPNIIPGEHEVVFDCRVL 293
Cdd:cd08018 173 TIKGKQAHGARPHLGINAIEAA-SAIVNAVNAIH---------LDPNIPwSVKMTKLQAGGEATNIIPDKAKFALDLRAQ 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828881018 294 PRYSLDDILRDVEDVAKEVkerhrkeldgKVLPEIEVEVLQRGDpAPPTNPNSEIVRLLKEAIKELRGKEAKVGGIGG 371
Cdd:cd08018 243 SNEAMEELKEKVEHAIEAA----------AALYGASIEITEKGG-MPAAEYDEEAVELMEEAITEVLGEEKLAGPCVT 309
|
|
| M20_Acy1L2 |
cd03887 |
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, ... |
212-419 |
2.05e-03 |
|
M20 Peptidase Aminoacylase 1-like protein 2, amidohydrolase family; Peptidase M20 family, Aminoacylase 1-like protein 2 (ACY1L2; amidohydrolase) subfamily. This group contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in Escherichia coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Aminoacylase 1 (ACY1) proteins 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 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: 349883 [Multi-domain] Cd Length: 360 Bit Score: 39.87 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 212 FRLKVKGQQVHA-SMPDKGLNAhrvaLD---LAYN----LdkRLHEKYSERdelfdppestFEPTM--GGnlaDSPNIIP 281
Cdd:cd03887 161 LRVEFHGKAAHAaAAPWEGINA----LDaavLAYNnisaL--RQQLKPTVR----------VHGIIteGG---KAPNIIP 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 282 GEHEVVFDCRVLPRYSLDDILRDVEDVAKevkerhrkelDGKVLPEIEVEVLQRGDPAPPTNPNSEIVRLLKEAIKEL-R 360
Cdd:cd03887 222 DYAEAEFYVRAPTLKELEELTERVIACFE----------GAALATGCEVEIEELEGYYDELLPNKTLANIYAENMEALgE 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1828881018 361 GKEAKVGGIGGG------------TFAAFFrrkGIPavvwaTLDEMAHQPnEYAKIDN-------MVEDAKVMAYLAL 419
Cdd:cd03887 292 EVLDGDEGVGSGstdfgnvsyvvpGIHPYF---GIP-----PPGAANHTP-EFAEAAGteeaheaALKAAKALAMTAL 360
|
|
| M28_like |
cd08015 |
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ... |
125-193 |
4.33e-03 |
|
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions.
Pssm-ID: 349937 [Multi-domain] Cd Length: 218 Bit Score: 38.34 E-value: 4.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1828881018 125 GRGSEDNGQSLVASLYAVRAMMNLGIRPKRTVILAFVSDEETGSKYGIGWLMKeHPELFREddLVLVPD 193
Cdd:cd08015 30 ATGATDNGAGTAVMMEAMRILKAIGSKPKRTIRVALWGSEEQGLHGSRAYVEK-HFGDPPT--MQLQRD 95
|
|
| M20_Acy1-like |
cd05667 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
212-362 |
9.24e-03 |
|
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: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1828881018 212 FRLKVKGQQVHASMPDKGLNAHRVALDLAYNLDKRLhekySERDELFDPPES-TFEPTMGGNladSPNIIPGEHEVVFDC 290
Cdd:cd05667 198 FRITVKGKQTHGSRPWDGIDPIMASAQIIQGLQTII----SRRIDLTKEPAViSIGKINGGT---RGNIIPEDAEMVGTI 270
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1828881018 291 RVLPRYSLDDILRDVEDVAKEVKERHRKeldgkvlpEIEVEVLQrgdPAPPTNPNSEIVRLLKEAIKELRGK 362
Cdd:cd05667 271 RTFDPEMREDIFARLKTIAEHIAKAYGA--------TAEVEFAN---GYPVTYNDPALTAKMLPTLQKAVGK 331
|
|
| |
