|
Name |
Accession |
Description |
Interval |
E-value |
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
20-404 |
0e+00 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 707.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 20 PISLPWVTRLVSMDTVSRNPNLGLIETVRDELRAVGIEATLTHGKGGKWANLFATIPAHDgetNGGVVLSGHTDVVPVDG 99
Cdd:PRK07522 4 MSSLDILERLVAFDTVSRDSNLALIEWVRDYLAAHGVESELIPDPEGDKANLFATIGPAD---RGGIVLSGHTDVVPVDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 100 QQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKPIHFALSFDEEVGCVGAPLLIADLMKRGVKPDGC 179
Cdd:PRK07522 81 QAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAPLRRPLHLAFSYDEEVGCLGVPSMIARLPERGVKPAGC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 180 IVGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQFRAQGPFDELYDVPFSTAQTSTI 259
Cdd:PRK07522 161 IVGEPTSMRPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLADRLAAPGPFDALFDPPYSTLQTGTI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 260 TGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARETLLPKMLREHSSAAIEITKIAAAPGLDSSEQAAITQLVRA 339
Cdd:PRK07522 241 QGGTALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAELLPEMRAVHPEAAIEFEPLSAYPGLDTAEDAAAARLVRA 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648533650 340 LTADQDKRKVAYGTEAGLFSNAGIPSIVCGPGDIQQAHKANEFVELEQLVACERFLRKFIHSMSV 404
Cdd:PRK07522 321 LTGDNDLRKVAYGTEAGLFQRAGIPTVVCGPGSIEQAHKPDEFVELAQLAACEAFLRRLLASLAA 385
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
25-400 |
0e+00 |
|
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: 540.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 25 WVTRLVSMDTVSRNPNLGLIETVRDELRAVGIEATLTHGKGGKWANLFATIPAHDGetnGGVVLSGHTDVVPVDGQQWDS 104
Cdd:cd03894 2 LLARLVAFDTVSRNSNLALIEYVADYLAALGVKSRRVPVPEGGKANLLATLGPGGE---GGLLLSGHTDVVPVDGQKWSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 105 DPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKPIHFALSFDEEVGCVGAPLLIADLMKRGVKPDGCIVGEP 184
Cdd:cd03894 79 DPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKPLHLAFSYDEEVGCLGVRHLIAALAARGGRPDAAIVGEP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 185 TSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQFrAQGPFDELYDVPFSTAQTSTITGGNA 264
Cdd:cd03894 159 TSLQPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELADRL-APGLRDPPFDPPYPTLNVGLIHGGNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 265 INTVPAECQFQFEFRNLPTLDPEQIFARIDSYARETLlpkmlrEHSSAAIEITKIAAAPGLDSSEQAAITQLVRALTADQ 344
Cdd:cd03894 238 VNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALL------EFPEAGIEVEPLFEVPGLETDEDAPLVRLAAALAGDN 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 648533650 345 DKRKVAYGTEAGLFSNAGIPSIVCGPGDIQQAHKANEFVELEQLVACERFLRKFIH 400
Cdd:cd03894 312 KVRTVAYGTEAGLFQRAGIPTVVCGPGSIAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
27-399 |
1.59e-118 |
|
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine deacetylases from proteobacteria. This enzyme is the final step of the "acetylated" ornithine biosynthesis pathway. The enzyme is closely related to dapE, succinyl-diaminopimelate desuccinylase, and outside of this clade annotation is very inaccurate as to which function should be ascribed to genes. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130947 [Multi-domain] Cd Length: 364 Bit Score: 349.12 E-value: 1.59e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 27 TRLVSMDTVSRNPNLGLIETVRDELRAVGIEATLTHGKGGK-WANLFATIpahDGETNGGVVLSGHTDVVPVDGQQWDSD 105
Cdd:TIGR01892 4 TKLVAFDSTSFRPNVDLIDWAQAYLEALGFSVEVQPFPDGAeKSNLVAVI---GPSGAGGLALSGHTDVVPYDDAAWTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 106 PFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKPIHFALSFDEEVGCVGAPLLIADLMKRgvkPDGCIVGEPT 185
Cdd:TIGR01892 81 PFRLTEKDGRLYGRGTCDMKGFLACALAAAPDLAAEQLKKPLHLALTADEEVGCTGAPKMIEAGAGR---PRHAIIGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 186 SMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQFRaQGPFDELYDVPFSTAQTSTITGGNAI 265
Cdd:TIGR01892 158 RLIPVRAHKGYASAEVTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVHLADTLL-REDLDEGFTPPYTTLNIGVIQGGKAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 266 NTVPAECQFQFEFRNLPTLDPEQIFARIdsyarETLLPKMLREHSSAAIEITKIAAAPGLDSSEQAAITQLVRALTADQd 345
Cdd:TIGR01892 237 NIIPGACEFVFEWRPIPGMDPEELLQLL-----ETIAQALVRDEPGFEVQIEVVSTDPGVNTEPDAELVAFLEELSGNA- 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 648533650 346 KRKVAYGTEAGLFSNAGIPSIVCGPGDIQQAHKANEFVELEQLVACERFLRKFI 399
Cdd:TIGR01892 311 PEVVSYGTEAPQFQELGAEAVVCGPGDIRQAHQPDEYVEIEDLVRCRAVLARLV 364
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
28-403 |
5.34e-110 |
|
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: 328.38 E-value: 5.34e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 28 RLVSMDTVSRNpNLGLIETVRDELRAVGIEATLTHGKGGKwANLFATIPAHDGEtnGGVVLSGHTDVVPVDGQ-QWDSDP 106
Cdd:COG0624 20 ELVRIPSVSGE-EAAAAELLAELLEALGFEVERLEVPPGR-PNLVARRPGDGGG--PTLLLYGHLDVVPPGDLeLWTSDP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 107 FKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRT--KLAKPIHFALSFDEEVGCVGAPLLIADLmKRGVKPDGCIVGEP 184
Cdd:COG0624 96 FEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAglRLPGNVTLLFTGDEEVGSPGARALVEEL-AEGLKADAAIVGEP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 185 TS-MRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQFRAQGPFDElydvpfSTAQTSTITGGN 263
Cdd:COG0624 175 TGvPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDGRADPLFGR------TTLNVTGIEGGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 264 AINTVPAECQFQFEFRNLPTLDPEQIFARIDSYAREtllpkmlrEHSSAAIEITKIA-AAPGLDSSEQAAITQLVRALTA 342
Cdd:COG0624 249 AVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAA--------AAPGVEVEVEVLGdGRPPFETPPDSPLVAAARAAIR 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648533650 343 DQDKRK-----VAYGTEAGLFSN-AGIPSIVCGPGDIQQAHKANEFVELEQLVACERFLRKFIHSMS 403
Cdd:COG0624 321 EVTGKEpvlsgVGGGTDARFFAEaLGIPTVVFGPGDGAGAHAPDEYVELDDLEKGARVLARLLERLA 387
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
28-399 |
3.74e-81 |
|
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: 253.38 E-value: 3.74e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 28 RLVSMDTVsrNPNLGLI-ETVRDELRAVG--IEATLTHGKGgkwaNLFATIPahdGETNGGVVLSGHTDVVPV-DGQQWD 103
Cdd:cd08659 5 DLVQIPSV--NPPEAEVaEYLAELLAKRGygIESTIVEGRG----NLVATVG---GGDGPVLLLNGHIDTVPPgDGDKWS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 104 SDPFKPEIRGDKLYGRGTCDMKGfiGTAlALVPDMQRTKLAKP-----IHFALSFDEEVGCVGAPLLIADLMKRgvKPDG 178
Cdd:cd08659 76 FPPFSGRIRDGRLYGRGACDMKG--GLA-AMVAALIELKEAGAllggrVALLATVDEEVGSDGARALLEAGYAD--RLDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 179 CIVGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQfRAQGPFdelydVPFSTAQTST 258
Cdd:cd08659 151 LIVGEPTGLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEE-LPAHPL-----LGPPTLNVGV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 259 ITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYAREtllpkmlrEHSSAAIEITKIAAAPGLDSSEQAAITQLVR 338
Cdd:cd08659 225 INGGTQVNSIPDEATLRVDIRLVPGETNEGVIARLEAILEE--------HEAKLTVEVSLDGDPPFFTDPDHPLVQALQA 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648533650 339 A---LTADQDKRKVAYGTEAGLFSNA-GIPSIVCGPGDIQQAHKANEFVELEQLVACERFLRKFI 399
Cdd:cd08659 297 AaraLGGDPVVRPFTGTTDASYFAKDlGFPVVVYGPGDLALAHQPDEYVSLEDLLRAAEIYKEII 361
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
39-400 |
7.04e-76 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 240.49 E-value: 7.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 39 PNLGLIETVRDELRAVG--IEATLTHGKGGKWaNLFATIpahdGETNGGVVLSGHTDVVPVDGQQWDSDPFKPEIRGDKL 116
Cdd:PRK05111 30 SNRAVIDLLAGWFEDLGfnVEIQPVPGTRGKF-NLLASL----GSGEGGLLLAGHTDTVPFDEGRWTRDPFTLTEHDGKL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 117 YGRGTCDMKGFIGTALALVPDMQRTKLAKPIHFALSFDEEVGCVGAPLLIAdlmKRGVKPDGCIVGEPTSMRPIIAHKGI 196
Cdd:PRK05111 105 YGLGTADMKGFFAFILEALRDIDLTKLKKPLYILATADEETSMAGARAFAE---ATAIRPDCAIIGEPTSLKPVRAHKGH 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 197 NAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQFRAQgPFDELYDVPFSTAQTSTITGGNAINTVPAECQFQF 276
Cdd:PRK05111 182 MSEAIRITGQSGHSSDPALGVNAIELMHDVIGELLQLRDELQER-YHNPAFTVPYPTLNLGHIHGGDAPNRICGCCELHF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 277 EFRNLPTLDPEQIFARIdsyaRETLLPkmLREHSSAAIEITKI-AAAPGLDSSEQAAITQLVRALTAdQDKRKVAYGTEA 355
Cdd:PRK05111 261 DIRPLPGMTLEDLRGLL----REALAP--VSERWPGRITVAPLhPPIPGYECPADHQLVRVVEKLLG-HKAEVVNYCTEA 333
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 648533650 356 GLFSNAGIPSIVCGPGDIQQAHKANEFVELEQLVACERFLRKFIH 400
Cdd:PRK05111 334 PFIQQLGCPTLVLGPGSIEQAHQPDEYLELSFIKPTRELLRQLIH 378
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
28-404 |
6.21e-62 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 204.84 E-value: 6.21e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 28 RLVSMDTVsrNPNLG----LIETVRDELRAVGIEATLTHGKGGKWANLFATIPAHDGETNGG---VVLSGHTDVVPVdGQ 100
Cdd:PRK08651 14 DLIKIPTV--NPPGEnyeeIAEFLRDTLEELGFSTEIIEVPNEYVKKHDGPRPNLIARRGSGnphLHFNGHYDVVPP-GE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 101 QWDS-DPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKPIhFALSFDEEVGCVGAPLLIADLmkrGVKPDGC 179
Cdd:PRK08651 91 GWSVnVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERLDPAGDGNIE-LAIVPDEETGGTGTGYLVEEG---KVTPDYV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 180 IVGEPTSMRPI-IAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQFRAQGPFDELYD-VPFSTAQTS 257
Cdd:PRK08651 167 IVGEPSGLDNIcIGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYEYDDERGaKPTVTLGGP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 258 TITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIdsyarETLLPKMLREHsSAAIEITKIAAAPGLDSSEQAAITQLV 337
Cdd:PRK08651 247 TVEGGTKTNIVPGYCAFSIDRRLIPEETAEEVRDEL-----EALLDEVAPEL-GIEVEFEITPFSEAFVTDPDSELVKAL 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648533650 338 RALTADQDKRKVAY-----GTEAGLFSNAGIPSIVCGPGDIQQAHKANEFVELEQLVACERFLRKFIHSMSV 404
Cdd:PRK08651 321 REAIREVLGVEPKKtislgGTDARFFGAKGIPTVVYGPGELELAHAPDEYVEVKDVEKAAKVYEEVLKRLAK 392
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
87-399 |
1.93e-60 |
|
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: 198.34 E-value: 1.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 87 VLSGHTDVVPvDGQQWDsDPFKPEIRGdKLYGRGTCDMKGFIGTALALVPDMQRTKLAK-PIHFALSFDEEVGCVGAPLL 165
Cdd:pfam01546 1 LLRGHMDVVP-DEETWG-WPFKSTEDG-KLYGRGHDDMKGGLLAALEALRALKEEGLKKgTVKLLFQPDEEGGMGGARAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 166 IADLMKRGVKPDGCI---VGEPTSM------RPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADq 236
Cdd:pfam01546 78 IEDGLLEREKVDAVFglhIGEPTLLeggiaiGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDIVS- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 237 fRAQGPFDELydvPFSTAQTSTITGGnaINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARETLLPKMLRehssAAIEI 316
Cdd:pfam01546 157 -RNVDPLDPA---VVTVGNITGIPGG--VNVIPGEAELKGDIRLLPGEDLEELEERIREILEAIAAAYGVK----VEVEY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 317 TKIAAAPGLDSSEqaaITQLVRALTADQDKRKV-------AYGTEAGLFSnAGIPS--IVCGPGDiQQAHKANEFVELEQ 387
Cdd:pfam01546 227 VEGGAPPLVNDSP---LVAALREAAKELFGLKVelivsgsMGGTDAAFFL-LGVPPtvVFFGPGS-GLAHSPNEYVDLDD 301
|
330
....*....|..
gi 648533650 388 LVACERFLRKFI 399
Cdd:pfam01546 302 LEKGAKVLARLL 313
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
28-389 |
1.28e-55 |
|
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: 187.61 E-value: 1.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 28 RLVSMDTVsrNPNLGLIETV----RDELRAVGIEA---TLTHGKGGKWANLFATIPAHDGETNggVVLSGHTDVVPV-DG 99
Cdd:TIGR01910 6 DLISIPSV--NPPGGNEETIanyiKDLLREFGFSTdviEITDDRLKVLGKVVVKEPGNGNEKS--LIFNGHYDVVPAgDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 100 QQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKP--IHFALSFDEEVGCVGAplliADLMKRGVK-- 175
Cdd:TIGR01910 82 ELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNgnIILQSVVDEESGEAGT----LYLLQRGYFkd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 176 PDGCIVGEPT-SMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQFRAQGPF-DELYDVPFST 253
Cdd:TIGR01910 158 ADGVLIPEPSgGDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEEHIYARNSYgFIPGPITFNP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 254 AqtsTITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYAretllpKMLREHSSAAIEITKIAAAPG-LDSSEQAA 332
Cdd:TIGR01910 238 G---VIKGGDWVNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVV------KALSKSDGWLYENEPVVKWSGpNETPPDSR 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648533650 333 ITQLVRALTADQDKRKV-----AYGTEAGLFSNAGIPSIVCGPGDIQQAHKANEFVELEQLV 389
Cdd:TIGR01910 309 LVKALEAIIKKVRGIEPevlvsTGGTDARFLRKAGIPSIVYGPGDLETAHQVNEYISIKNLV 370
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
47-396 |
2.77e-47 |
|
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: 165.25 E-value: 2.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 47 VRDELRAVGIEATLTHGKGGKWaNLFATIpaHDGETNGGVVLSGHTDVVPV-DGQQWDSDPFKPEIRGDKLYGRGTCDMK 125
Cdd:cd08011 27 IKLLLEDLGYPVELHEPPEEIY-GVVSNI--VGGRKGKRLLFNGHYDVVPAgDGEGWTVDPYSGKIKDGKLYGRGSSDMK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 126 GFIGT---ALALVPDMqRTKLAKPIHFALSFDEE-VGCVGAPLLiadLMKRGVKPDGCIVGEPTSMRPI-IAHKGINAYQ 200
Cdd:cd08011 104 GGIAAsiiAVARLADA-KAPWDLPVVLTFVPDEEtGGRAGTKYL---LEKVRIKPNDVLIGEPSGSDNIrIGEKGLVWVI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 201 CCVRGQAAHSSLTPKGLNAIEYAARLIcyirdmadqfraqgpfDELYDVpFSTAQTSTITGGNAINTVPAECQFQFEFRN 280
Cdd:cd08011 180 IEITGKPAHGSLPHRGESAVKAAMKLI----------------ERLYEL-EKTVNPGVIKGGVKVNLVPDYCEFSVDIRL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 281 LPTLDPEQIFARIdsyarETLLPKMlrehsSAAIEITKIAAAPGLDSSEQAAITQLVRALTADQDKRKVAY----GTEAG 356
Cdd:cd08011 243 PPGISTDEVLSRI-----IDHLDSI-----EEVSFEIKSFYSPTVSNPDSEIVKKTEEAITEVLGIRPKEVisvgASDAR 312
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 648533650 357 LFSNAGIPSIVCGPGDIQQAHKANEFVELEQLVACERFLR 396
Cdd:cd08011 313 FYRNAGIPAIVYGPGRLGQMHAPNEYVEIDELIKVIKVHA 352
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
29-386 |
8.84e-47 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 164.29 E-value: 8.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 29 LVSMDTVSRNpNLGLIETVRDELRAVGIEATLTHGKGGKwANLFATIpahdGETNGGVVLSGHTDVV-PVDGQQWDSDPF 107
Cdd:PRK08588 11 IVKINSVNDN-EIEVANYLQDLFAKHGIESKIVKVNDGR-ANLVAEI----GSGSPVLALSGHMDVVaAGDVDKWTYDPF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 108 KPEIRGDKLYGRGTCDMKGfiGTAlALVPDM-----QRTKLAKPIHFALSFDEEVGCVGAplliADLMKRGVKPD--GCI 180
Cdd:PRK08588 85 ELTEKDGKLYGRGATDMKS--GLA-ALVIAMielkeQGQLLNGTIRLLATAGEEVGELGA----KQLTEKGYADDldALI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 181 VGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEyaaRLICYIRDMADQFRAQGPFDELYDVPfsTAQTSTIT 260
Cdd:PRK08588 158 IGEPSGHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVNAID---PLLEFYNEQKEYFDSIKKHNPYLGGL--THVVTIIN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 261 GGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYAREtllpkmLREHSSAAIEITKIAAAPGLDSSEQAAITQLVRAL 340
Cdd:PRK08588 233 GGEQVNSVPDEAELEFNIRTIPEYDNDQVISLLQEIINE------VNQNGAAQLSLDIYSNHRPVASDKDSKLVQLAKDV 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 648533650 341 TADQDKRKVAY-----GTEAGLF--SNAGIPSIVCGPGDIQQAHKANEFVELE 386
Cdd:PRK08588 307 AKSYVGQDIPLsaipgATDASSFlkKKPDFPVIIFGPGNNLTAHQVDEYVEKD 359
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
82-399 |
2.61e-44 |
|
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: 158.02 E-value: 2.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 82 TNGG--VVLSGHTDVVPVDGqqWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKPIHFALSFDEEVGC 159
Cdd:cd08013 65 TGGGksLMLNGHIDTVTLDG--YDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGLRGDVILAAVADEEDAS 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 160 VGAplliADLMKRGVKPDGCIVGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQFRa 239
Cdd:cd08013 143 LGT----QEVLAAGWRADAAIVTEPTNLQIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALEEYQQELP- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 240 QGPFDELYDVPfsTAQTSTITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSyaretLLPKMLREHSSAAIEITKI 319
Cdd:cd08013 218 ERPVDPLLGRA--SVHASLIKGGEEPSSYPARCTLTIERRTIPGETDESVLAELTA-----ILGELAQTVPNFSYREPRI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 320 AAA-PGLDSSEQAAITQLVRALTA-----DQDKRKVAYGTEAGLFSNAGIPSIVCGPgDIQQAHKANEFVELEQLVACER 393
Cdd:cd08013 291 TLSrPPFEVPKEHPFVQLVAAHAAkvlgeAPQIRSETFWTDAALLAEAGIPSVVFGP-SGAGLHAKEEWVDVESIRQLRE 369
|
....*.
gi 648533650 394 FLRKFI 399
Cdd:cd08013 370 VLSAVV 375
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
29-388 |
4.26e-44 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 156.90 E-value: 4.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 29 LVSMDTvsRNP-----NLGLIETVRDELRAVGIEATlTHGKGGkwANLFATipahDGETNggVVLSGHTDVVPvDGQQWD 103
Cdd:PRK08737 15 LVSFDT--RNPpraitTGGIFDYLRAQLPGFQVEVI-DHGAGA--VSLYAV----RGTPK--YLFNVHLDTVP-DSPHWS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 104 SDPFKPEIRGDKLYGRGTCDMKGfigTALALVPDMQRTKlaKPIHFALSFDEEVGcvgAPLLIADLMKRGVKPDGCIVGE 183
Cdd:PRK08737 83 ADPHVMRRTDDRVIGLGVCDIKG---AAAALLAAANAGD--GDAAFLFSSDEEAN---DPRCVAAFLARGIPYEAVLVAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 184 PTSMRPIIAHKGINAYQCCVRGQAAHSSLTPK-GLNAIEYAARLICYIRDMAdQFRAQGPFDELYDVPFSTAQtstITGG 262
Cdd:PRK08737 155 PTMSEAVLAHRGISSVLMRFAGRAGHASGKQDpSASALHQAMRWGGQALDHV-ESLAHARFGGLTGLRFNIGR---VEGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 263 NAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYAretllpkmlrehSSAAIEITKIAAAPGLDSSEQAaitqlvRALTA 342
Cdd:PRK08737 231 IKANMIAPAAELRFGFRPLPSMDVDGLLATFAGFA------------EPAAATFEETFRGPSLPSGDIA------RAEER 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 648533650 343 DQDKRKVAYG------------TEAGLFSNAGIPSIVCGPGDIQQAHKANEFVELEQL 388
Cdd:PRK08737 293 RLAARDVADAldlpignavdfwTEASLFSAAGYTALVYGPGDIAQAHTADEFVTLDQL 350
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
78-399 |
1.35e-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: 145.91 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 78 HDGETNGG--VVLSGHTDVVPVDG-QQWDSDPFKPEIRGDKLYGRGTCDMKGfiGTALALVP-DMQRT---KLAKPIHFA 150
Cdd:cd03895 67 HRPRGETGrsLILNGHIDVVPEGPvELWTRPPFEATIVDGWMYGRGAGDMKA--GLAANLFAlDALRAaglQPAADVHFQ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 151 LSFDEEVGCVGApllIADLMkRGVKPDGCIVGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYI 230
Cdd:cd03895 145 SVVEEECTGNGA---LAALM-RGYRADAALIPEPTELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQAL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 231 RDMADQFRAQGPFDELYD-----VPFSTAqtsTITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARETLL--P 303
Cdd:cd03895 221 QELEREWNARKKSHPHFSdhphpINFNIG---KIEGGDWPSSVPAWCVLDCRIGIYPGESPEEARREIEECVADAAAtdP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 304 KmLREHssaAIEITKIAA-APGLDSSEQAAITQLVR-----ALTADQDKRKVAYGTEAGLFSNAG-IPSIVCGPGDiQQA 376
Cdd:cd03895 298 W-LSNH---PPEVEWNGFqAEGYVLEPGSDAEQVLAaahqaVFGTPPVQSAMTATTDGRFFVLYGdIPALCYGPGS-RDA 372
|
330 340
....*....|....*....|...
gi 648533650 377 HKANEFVELEQLVACERFLRKFI 399
Cdd:cd03895 373 HGFDESVDLESLRKITKTIALFI 395
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
63-390 |
3.05e-37 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 139.21 E-value: 3.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 63 GKGGKWANLFATIPAHDGETNGGVVlsGHTDVVPV-DGQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRT 141
Cdd:PRK13983 58 VIEGVRPNIVAKIPGGDGKRTLWII--SHMDVVPPgDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 142 KLAKPIHFALSF--DEEVGC-VGapllIADLMK--RGV-KPDGCIV----GEPTSMRPIIAHKGINAYQCCVRGQAAHSS 211
Cdd:PRK13983 136 GIRPKYNLGLAFvsDEETGSkYG----IQYLLKkhPELfKKDDLILvpdaGNPDGSFIEIAEKSILWLKFTVKGKQCHAS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 212 LTPKGLNAIEYAARLICYIRD-MADQFRAQgpfDELYDVPFSTAQtSTITGGNA--INTVPAECQFQFEFRNLPTLDPEQ 288
Cdd:PRK13983 212 TPENGINAHRAAADFALELDEaLHEKFNAK---DPLFDPPYSTFE-PTKKEANVdnINTIPGRDVFYFDCRVLPDYDLDE 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 289 IFARIDSYAREtllpkmLREHSSAAIEITKI----AAAPGLDSSEqaAITQLVRALtadQDKRKVAY-------GTEAGL 357
Cdd:PRK13983 288 VLKDIKEIADE------FEEEYGVKIEVEIVqreqAPPPTPPDSE--IVKKLKRAI---KEVRGIEPkvggiggGTVAAF 356
|
330 340 350
....*....|....*....|....*....|...
gi 648533650 358 FSNAGIPSIVCGPGDiQQAHKANEFVELEQLVA 390
Cdd:PRK13983 357 LRKKGYPAVVWSTLD-ETAHQPNEYAKISNLIE 388
|
|
| PRK06915 |
PRK06915 |
peptidase; |
82-391 |
2.10e-34 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 132.12 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 82 TNGG--VVLSGHTDVVPV-DGQQWDSDPFKPEIRGDKLYGRGTCDMKGfiGTaLALVPDMQ-----RTKLAKPIHFALSF 153
Cdd:PRK06915 90 SGGGksMILNGHIDVVPEgDVNQWDHHPYSGEVIGGRIYGRGTTDMKG--GN-VALLLAMEaliesGIELKGDVIFQSVI 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 154 DEEVGcvGAPLLIADLmkRGVKPDGCIVGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDM 233
Cdd:PRK06915 167 EEESG--GAGTLAAIL--RGYKADGAIIPEPTNMKFFPKQQGSMWFRLHVKGKAAHGGTRYEGVSAIEKSMFVIDHLRKL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 234 aDQFRAQGPFDELYD-----VPFSTAqtsTITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYAREtlLPKM--- 305
Cdd:PRK06915 243 -EEKRNDRITDPLYKgipipIPINIG---KIEGGSWPSSVPDSVILEGRCGIAPNETIEAAKEEFENWIAE--LNDVdew 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 306 LREHssaAIEITKIAA--APGLDSSEQAAITQL---VRALTADQDKRKVA-YGTEAGLFSNAG-IPSIVCGPGDIQQAHK 378
Cdd:PRK06915 317 FVEH---PVEVEWFGArwVPGELEENHPLMTTLehnFVEIEGNKPIIEASpWGTDGGLLTQIAgVPTIVFGPGETKVAHY 393
|
330
....*....|...
gi 648533650 379 ANEFVELEQLVAC 391
Cdd:PRK06915 394 PNEYIEVDKMIAA 406
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
70-399 |
1.44e-33 |
|
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: 128.78 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 70 NLFATIpahdgeTNGGVVL--SGHTDVVPV-DGQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVpdMQRTKLAKP 146
Cdd:cd03891 45 NLWARR------GTGGPHLcfAGHTDVVPPgDLEGWSSDPFSPTIKDGMLYGRGAADMKGGIAAFVAAA--ERFVAKHPN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 147 IHFALSF----DEE-VGCVGAPLLIADLMKRGVKPDGCIVGEPTSMRPI-----IAHKG-INAYqCCVRGQAAHSSLTPK 215
Cdd:cd03891 117 HKGSISFlitsDEEgPAIDGTKKVLEWLKARGEKIDYCIVGEPTSEKKLgdtikIGRRGsLNGK-LTIKGKQGHVAYPHL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 216 GLNAIEYAARLICYIRDMadqfraqgPFDELYD-VPFSTAQTSTITGGN-AINTVPAECQFQFEFRNLPTLDPEQIFARI 293
Cdd:cd03891 196 ADNPIHLLAPILAELTAT--------VLDEGNEfFPPSSLQITNIDVGNgATNVIPGELKAKFNIRFNDEHTGESLKARI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 294 DSYARETLLPKMLREHSSAAIEITKiaaapglDSSEQAAITQLVRALTADQDKRKVAYGT-EAGLFSNAGIPSIVCGP-G 371
Cdd:cd03891 268 EAILDKHGLDYDLEWKLSGEPFLTK-------PGKLVDAVSAAIKEVTGITPELSTSGGTsDARFIASYGCPVVEFGLvN 340
|
330 340
....*....|....*....|....*...
gi 648533650 372 DiqQAHKANEFVELEQLVACERFLRKFI 399
Cdd:cd03891 341 A--TIHKVNERVSVADLEKLTDIYERIL 366
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
28-402 |
1.63e-33 |
|
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: 129.79 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 28 RLVSMDTVSRNPNLG----LIETVRDELRAVGI--EATLTHGKGGKwANLFATIPAHDGETnGGVVLSGHTDVVPVDGQQ 101
Cdd:cd05675 6 ELIRIDTTNSGDGTGsetrAAEVLAARLAEAGIqtEIFVVESHPGR-ANLVARIGGTDPSA-GPLLLLGHIDVVPADASD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 102 WDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRT--KLAKPIHFALSFDEEV-GCVGAPLLIADLMKRGVKPDG 178
Cdd:cd05675 84 WSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREgfKPKRDLVFAFVADEEAgGENGAKWLVDNHPELFDGATF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 179 CI---------VGEPTSMRPI-IAHKGINAYQCCVRGQAAHSSlTPKGLNAI----EYAARLICY-----IRDMADQFRA 239
Cdd:cd05675 164 ALneggggslpVGKGRRLYPIqVAEKGIAWMKLTVRGRAGHGS-RPTDDNAItrlaEALRRLGAHnfpvrLTDETAYFAQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 240 QGPF----------------DELYDV-----PFSTAQTST------ITGGNAINTVPAECQFQFEFRNLPTLDPEQIFAR 292
Cdd:cd05675 243 MAELaggeggalmltavpvlDPALAKlgpsaPLLNAMLRNtasptmLDAGYATNVLPGRATAEVDCRILPGQSEEEVLDT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 293 IDsyaRETLLPKMLREHSSAaieitKIAAAPGLDSSEQAAITQLVRALtaDQDKRKVAY----GTEAGLFSNAGIPS--- 365
Cdd:cd05675 323 LD---KLLGDPDVSVEAVHL-----EPATESPLDSPLVDAMEAAVQAV--DPGAPVVPYmspgGTDAKYFRRLGIPGygf 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 648533650 366 --IVCGPGDIQ--QAHKANEFVELEQLvaceRFLRKFIHSM 402
Cdd:cd05675 393 apLFLPPELDYtgLFHGVDERVPVESL----YFGVRFLDRL 429
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
28-389 |
5.85e-33 |
|
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.
Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 126.94 E-value: 5.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 28 RLVSMDTVSRNPN--LGLIETVRDELRAVGIEATLT-HGKGGkwANLFATIPAHDGetnGGVVLSGHTDVVPVDGqqwdS 104
Cdd:cd03885 7 RLVNIESGTYDKEgvDRVAELLAEELEALGFTVERRpLGEFG--DHLIATFKGTGG---KRVLLIGHMDTVFPEG----T 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 105 DPFKP-EIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAK--PIHFALSFDEEVGCVGAPLLIADLMKRGvkpDGCIV 181
Cdd:cd03885 78 LAFRPfTVDGDRAYGPGVADMKGGLVVILHALKALKAAGGRDylPITVLLNSDEEIGSPGSRELIEEEAKGA---DYVLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 182 GEPTsmRP----IIAHKGINAYQCCVRGQAAHSSLTP-KGLNAIEYAARLICYIRDMADQFRAqgpfdelydvpfSTAQT 256
Cdd:cd03885 155 FEPA--RAdgnlVTARKGIGRFRLTVKGRAAHAGNAPeKGRSAIYELAHQVLALHALTDPEKG------------TTVNV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 257 STITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARETLLPKMlreHSSAAIEITKIAAAPGlDSSEQ--AAIT 334
Cdd:cd03885 221 GVISGGTRVNVVPDHAEAQVDVRFATAEEADRVEEALRAIVATTLVPGT---SVELTGGLNRPPMEET-PASRRllARAQ 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 648533650 335 QLVRALTADQDKRKVAYGTEAGLFSNAGIPSIvCG---PGDiqQAHKANEFVELEQLV 389
Cdd:cd03885 297 EIAAELGLTLDWEATGGGSDANFTAALGVPTL-DGlgpVGG--GAHTEDEYLELDSLV 351
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
70-399 |
1.03e-32 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349902 [Multi-domain] Cd Length: 341 Bit Score: 125.88 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 70 NLFATIPAHDgETNGGVVLSGHTDVV-PVDGqqWDSDPFKPEIRGDKLYGRGTCDMKG-FIGTALALVPDMQRTKLAKPI 147
Cdd:cd05651 43 NVWAENGHFD-EGKPTLLLNSHHDTVkPNAG--WTKDPFEPVEKGGKLYGLGSNDAGAsVVSLLATFLHLYSEGPLNYNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 148 HFALSFDEEVGcvgAPLLIADLMKRGVKPDGCIVGEPTSMRPIIAHKGINAYQCCVRGQAAHSSlTPKGLNAIEYAARLI 227
Cdd:cd05651 120 IYAASAEEEIS---GKNGIESLLPHLPPLDLAIVGEPTEMQPAIAEKGLLVLDCTARGKAGHAA-RNEGDNAIYKALDDI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 228 CYIRDMadQFRAQGPFdeLYDVpfsTAQTSTITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARETLLPKMLR 307
Cdd:cd05651 196 QWLRDF--RFDKVSPL--LGPV---KMTVTQINAGTQHNVVPDSCTFVVDIRTTEAYTNEEIFEIIRGNLKSEIKPRSFR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 308 EHSSAaieitkIAAAPGLDSSEQAAITQLVRALTA-DQdkrkvaygteaglfSNAGIPSIVCGPGDIQQAHKANEFVELE 386
Cdd:cd05651 269 LNSSA------IPPDHPIVQAAIAAGRTPFGSPTLsDQ--------------ALMPFPSVKIGPGDSSRSHTADEFIELS 328
|
330
....*....|...
gi 648533650 387 QLVACERFLRKFI 399
Cdd:cd05651 329 EIEEGIDIYIELL 341
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
66-389 |
2.73e-31 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 122.95 E-value: 2.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 66 GKW-ANLFATIPAHDGETnggVVLSGHTDVVPV-DGQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKL 143
Cdd:cd05650 54 GIIrPNIVAKIPGGNDKT---LWIISHLDTVPPgDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 144 AKPIHFALSF--DEEVGC-VGAPLLiadLMKRGV-KPDGCIV----GEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPK 215
Cdd:cd05650 131 TPKYNFGLLFvaDEEDGSeYGIQYL---LNKFDLfKKDDLIIvpdfGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPEN 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 216 GLNAIEYAARLICYIRDMADQFRAQgpFDELYDVPFSTAQtSTITGGNA--INTVPAECQFQFEFRNLPTLDPEQIFARI 293
Cdd:cd05650 208 GINAFVAASNFALELDELLHEKFDE--KDDLFNPPYSTFE-PTKKEANVpnVNTIPGYDVFYFDCRVLPTYKLDEVLKFV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 294 DSYAREtllpkmLREHSSAAI--EITKIAAAPGLDSSEQAAITQLVRALTADQDKRK----VAYGTEAGLFSNAGIPSIV 367
Cdd:cd05650 285 NKIISD------FENSYGAGItyEIVQKEQAPPATPEDSEIVVRLSKAIKKVRGREAkligIGGGTVAAFLRKKGYPAVV 358
|
330 340
....*....|....*....|..
gi 648533650 368 CGPGDiQQAHKANEFVELEQLV 389
Cdd:cd05650 359 WSTLD-ETAHQPNEYIRISHIV 379
|
|
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
70-399 |
1.29e-30 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 120.58 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 70 NLFATIpAHDGETnggVVLSGHTDVVPV-DGQQWDSDPFKPEIRGDKLYGRGTCDMKG----FIGTALALVPDMQRTKLA 144
Cdd:PRK13009 49 NLWARR-GTEGPH---LCFAGHTDVVPPgDLEAWTSPPFEPTIRDGMLYGRGAADMKGslaaFVVAAERFVAAHPDHKGS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 145 kpIHFALSFDEE-VGCVGAPLLIADLMKRGVKPDGCIVGEPTSMRPI-----IAHKG-INAYqCCVRGQAAHSSLTPKGL 217
Cdd:PRK13009 125 --IAFLITSDEEgPAINGTVKVLEWLKARGEKIDYCIVGEPTSTERLgdvikNGRRGsLTGK-LTVKGVQGHVAYPHLAD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 218 NAIEYAARLICYIRDMadqfraqgPFDELYD-VPFSTAQTSTITGGN-AINTVPAECQFQFEFRNLPTLDPEQIFARIDS 295
Cdd:PRK13009 202 NPIHLAAPALAELAAT--------EWDEGNEfFPPTSLQITNIDAGTgATNVIPGELEAQFNFRFSTEHTAESLKARVEA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 296 YARETLLPKMLREHSSAAIEITKiaaaPG--LDSSEQA--AITQLVRAL-----TADqdkrkvaygteAGLFSNAGIPSI 366
Cdd:PRK13009 274 ILDKHGLDYTLEWTLSGEPFLTP----PGklVDAVVAAieAVTGITPELstsggTSD-----------ARFIADYGAQVV 338
|
330 340 350
....*....|....*....|....*....|....*..
gi 648533650 367 VCGPGDiQQAHKANEFV---ELEQLVAC-ERFLRKFI 399
Cdd:PRK13009 339 EFGPVN-ATIHKVNECVsvaDLEKLTRIyERILERLL 374
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
29-399 |
1.62e-30 |
|
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 162269 [Multi-domain] Cd Length: 370 Bit Score: 120.60 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 29 LVSMDTVSRNpNLGLIETVRDELRAVGIEATLTHGKGGKwaNLFATipahDGETNGGVVLSGHTDVVPV-DGQQWDSDPF 107
Cdd:TIGR01246 8 LISRPSVTPN-DAGCQDIIAERLEKLGFEIEWMHFGDTK--NLWAT----RGTGEPVLAFAGHTDVVPAgPEEQWSSPPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 108 KPEIRGDKLYGRGTCDMKG----FIGTALALV---PDMQRTklakpIHFALSFDEEVGCVGAPLLIAD-LMKRGVKPDGC 179
Cdd:TIGR01246 81 EPVERDGKLYGRGAADMKGslaaFIVAAERFVkknPDHKGS-----ISLLITSDEEGTAIDGTKKVVEtLMARDELIDYC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 180 IVGEPTSMRPI-----IAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAA----RLICYIRDMADQFraqgpfdelydVP 250
Cdd:TIGR01246 156 IVGEPSSVKKLgdvikNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAApalaELTAIKWDEGNEF-----------FP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 251 FSTAQTSTITGGN-AINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARETLLPKMLREHSSAAIEITKiaaapglDSSE 329
Cdd:TIGR01246 225 PTSLQITNIHAGTgANNVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTN-------DGKL 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648533650 330 QAAITQLVRALTADQDKRKVAYGTEAGLF-SNAGIPSIVCGPGDiQQAHKANEFVELEQLVACERFLRKFI 399
Cdd:TIGR01246 298 IDKAREAIEETNGIKPELSTGGGTSDGRFiALMGAEVVEFGPVN-ATIHKVNECVSIEDLEKLSDVYQDLL 367
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
49-388 |
5.95e-30 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 119.72 E-value: 5.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 49 DELRAVGIE---------ATLTHGKGGKWANLFATIP----AHDGETNGG--VVLSGHTDVVPVD-GQQWDSDPFKPEIR 112
Cdd:PRK06837 48 RAFRERGYEvdrwsidpdDLKSHPGAGPVEIDYSGAPnvvgTYRPAGKTGrsLILQGHIDVVPEGpLDLWSRPPFDPVIV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 113 GDKLYGRGTCDMK-GFIGTALALvpDMQRT---KLAKPIHFALSFDEEVGCVGApllIADLMkRGVKPDGCIVGEPTSMR 188
Cdd:PRK06837 128 DGWMYGRGAADMKaGLAAMLFAL--DALRAaglAPAARVHFQSVIEEESTGNGA---LSTLQ-RGYRADACLIPEPTGEK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 189 PIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQFRAQGPFDELY-DVP----FSTAQtstITGGN 263
Cdd:PRK06837 202 LVRAQVGVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRELEAEWNARKASDPHFeDVPhpinFNVGI---IKGGD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 264 AINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARETLL-PKMLREHsSAAIEITKIAAAPGLDSSEQAAITQLVRALTA 342
Cdd:PRK06837 279 WASSVPAWCDLDCRIAIYPGVTAADAQAEIEACLAAAARdDRFLSNN-PPEVVWSGFLAEGYVLEPGSEAEAALARAHAA 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 648533650 343 dqdkrkvAYGTEAGLFS------------NAGIPSIVCGPgdIQQA-HKANEFVELEQL 388
Cdd:PRK06837 358 -------VFGGPLRSFVttaytdtrfyglYYGIPALCYGP--SGEGiHGFDERVDLESV 407
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
23-386 |
5.73e-29 |
|
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: 117.06 E-value: 5.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 23 LPWVTRLVSMDTVSRNpNLGLIET---VRDELRAVGIEATLTHGKGGKWanLFATIPAHDGETnggVVLSGHTDVVPVDG 99
Cdd:cd05681 2 LEDLRDLLKIPSVSAQ-GRGIPETadfLKEFLRRLGAEVEIFETDGNPI--VYAEFNSGDAKT---LLFYNHYDVQPAEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 100 -QQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKPIHFALSFD--EEVGCVGAPLLIADLMKRgVKP 176
Cdd:cd05681 76 lELWTSDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEgeEEVGSPNLEKFVAEHADL-LKA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 177 DGCIV---GEPTSMRPII--AHKGINAYQCCVRGQAA--HSSLTPKGLNAIEYAARLICYIRDMADQFRAQGPFDEL--- 246
Cdd:cd05681 155 DGCIWeggGKNPKGRPQIslGVKGIVYVELRVKTADFdlHSSYGAIVENPAWRLVQALNSLRDEDGRVLIPGFYDDVrpl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 247 ----------YDVP------------------------FSTAQTSTITG------GNAINTV-PAECQFQFEFRNLPTLD 285
Cdd:cd05681 235 seaeralidtYDFDpeelrktyglkrplqvegkdplraLFTEPTCNINGiysgytGEGSKTIlPSEAFAKLDFRLVPDQD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 286 PEQIFaridsyaretllpKMLREHSSAA----IEITKIAAAPGLDSSEQAAITQLVRALTadqdkrKVAYGTE------- 354
Cdd:cd05681 315 PAKIL-------------SLLRKHLDKNgfddIEIHDLLGEKPFRTDPDAPFVQAVIESA------KEVYGQDpivlpns 375
|
410 420 430
....*....|....*....|....*....|....*....
gi 648533650 355 AG------LFSNAGIPSIVCGPGDIQ-QAHKANEFVELE 386
Cdd:cd05681 376 AGtgpmypFYDALEVPVVAIGVGNAGsNAHAPNENIRIA 414
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
86-398 |
1.92e-28 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 114.09 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 86 VVLSGHTDVVPVDGqqwdsdpfKPEIRGDKLYGRGTCDMKGfiGTALALVPDMQRTKLAKPIHFALSF--DEEVGCVGAP 163
Cdd:PRK08652 58 LFVEVHYDTVPVRA--------EFFVDGVYVYGTGACDAKG--GVAAILLALEELGKEFEDLNVGIAFvsDEEEGGRGSA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 164 LLIADLmkrgvKPDGCIVGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMaDQFRAQGpf 243
Cdd:PRK08652 128 LFAERY-----RPKMAIVLEPTDLKVAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKEL-LKALGKY-- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 244 delYDVPFSTAQtstITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARETLLPKMLREhssaaieitkiaAAP 323
Cdd:PRK08652 200 ---FDPHIGIQE---IIGGSPEYSIPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEYTE------------IWD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 324 GLDSSEQAAITQLVRALTaDQDKRKVAYG-----TEAGLFSNAGIPSIVCGPGDIQQAHKANEFVELEQLVACERFLRKF 398
Cdd:PRK08652 262 GFELDEDEEIVQLLEKAM-KEVGLEPEFTvmrswTDAINFRYNGTKTVVWGPGELDLCHTKFERIDVREVEKAKEFLKAL 340
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
28-399 |
4.34e-28 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 113.61 E-value: 4.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 28 RLVSMDTVSrNPNLGLIETVRDELRAVGIEATLThgkggKWANLFATIPAHDGETNGGVVLSGHTDVVPvdgqQWDSDPF 107
Cdd:COG2195 11 EYVKIPTPS-DHEEALADYLVEELKELGLEVEED-----EAGNVIATLPATPGYNVPTIGLQAHMDTVP----QFPGDGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 108 KPEIRGDKLYGRGT----CDMKGFIGTALALV-----PDMQRtklaKPIHFALSFDEEVGCVGAplliadlmkRGVKP-- 176
Cdd:COG2195 81 KPQIDGGLITADGTttlgADDKAGVAAILAALeylkePEIPH----GPIEVLFTPDEEIGLRGA---------KALDVsk 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 177 ---------DGCIVGEptsmrpiIAHKGINAYQC--CVRGQAAHSSLTPKGL-NAIEYAARLIcyirdmadqfrAQGPFD 244
Cdd:COG2195 148 lgadfaytlDGGEEGE-------LEYECAGAADAkiTIKGKGGHSGDAKEKMiNAIKLAARFL-----------AALPLG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 245 ELYDvpFSTAQTSTITGGNAINTVPAECQFQFEFRNLptlDPEQIFARIDSYarETLLPKMLREHSSAAIEITKIAAAPG 324
Cdd:COG2195 210 RIPE--ETEGNEGFIHGGSATNAIPREAEAVYIIRDH---DREKLEARKAEL--EEAFEEENAKYGVGVVEVEIEDQYPN 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648533650 325 LDSSEQAAITQLVRALTADQDKR-KVAY---GTEAGLFSNAGIPSIVCGPGdIQQAHKANEFVELEQLVACERFLRKFI 399
Cdd:COG2195 283 WKPEPDSPIVDLAKEAYEELGIEpKIKPirgGLDGGILSFKGLPTPNLGPG-GHNFHSPDERVSIESMEKAWELLVEIL 360
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
20-399 |
5.84e-27 |
|
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: 110.22 E-value: 5.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 20 PISLpwVTRLVSMDTVSRNPNlGLIETVRDELRAVGIEATLTHGKggkwanlfaTIPAHdgeTNGG----VVLSGHTDVV 95
Cdd:cd05647 1 PIEL--TAALVDIPSVSGNEK-PIADEIEAALRTLPHLEVIRDGN---------TVVAR---TERGlasrVILAGHLDTV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 96 PVDGqqwdSDPFKPEIRGdKLYGRGTCDMKGFIGTALALVPDMQRTKLAKPIHFALSFDEEVGCVGAPLL-IADLMKRGV 174
Cdd:cd05647 66 PVAG----NLPSRVEEDG-VLYGCGATDMKAGDAVQLKLAATLAAATLKHDLTLIFYDCEEVAAELNGLGrLAEEHPEWL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 175 KPDGCIVGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLIcyirDMADQFRAQGP-FDEL--YDVPF 251
Cdd:cd05647 141 AADFAVLGEPTDGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPIL----ARLAAYEPRTVnIDGLtyREGLN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 252 STAqtstITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIdsyaRETLlpkmlrEHSSAAIEITKIAAA--PGLDsse 329
Cdd:cd05647 217 AVF----ISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHV----REVF------EGLGYEIEVTDLSPGalPGLD--- 279
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648533650 330 QAAITQLVRALtadqdKRKVA--YG-TEAGLFSNAGIPSIVCGPGDIQQAHKANEFVELEQLVACERFLRKFI 399
Cdd:cd05647 280 HPVARDLIEAV-----GGKVRakYGwTDVARFSALGIPAVNFGPGDPLLAHKRDEQVPVEQITACAAILRRWL 347
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
90-391 |
1.81e-24 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 103.87 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 90 GHTDVVPV-DGQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKL--AKPIHFALSFDEEVgCVG-APLL 165
Cdd:PRK13004 76 AHIDTVGIgDIKNWDFDPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLddEYTLYVTGTVQEED-CDGlCWRY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 166 IADlmKRGVKPDGCIVGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQfraqgpfde 245
Cdd:PRK13004 155 IIE--EDKIKPDFVVITEPTDLNIYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPN--------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 246 LYDVPFSTAQTSTIT-------GGNAintVPAECQFQFEFRNLPTLDPEQIFARIDSYARETLLP---KMLRE----HSS 311
Cdd:PRK13004 224 LKEDPFLGKGTLTVSdifstspSRCA---VPDSCAISIDRRLTVGETWESVLAEIRALPAVKKANakvSMYNYdrpsYTG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 312 AAIEITKIaaAPGLDSSEQAAITQ-LVRALTAdqdkrkvAYGTEAGL----FSN--------AGIPSIVCGPGDIQQAHK 378
Cdd:PRK13004 301 LVYPTECY--FPTWLYPEDHEFVKaAVEAYKG-------LFGKAPEVdkwtFSTngvsiagrAGIPTIGFGPGKEPLAHA 371
|
330
....*....|...
gi 648533650 379 ANEFVELEQLVAC 391
Cdd:PRK13004 372 PNEYTWKEQLVKA 384
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
191-303 |
5.05e-24 |
|
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: 95.49 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 191 IAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMadqfraqgPFDELYDVPFSTAQTSTITGGNAINTVPA 270
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAE--------YGDIGFDFPRTTLNITGIEGGTATNVIPA 72
|
90 100 110
....*....|....*....|....*....|...
gi 648533650 271 ECQFQFEFRNLPTLDPEQIFARIDSYARETLLP 303
Cdd:pfam07687 73 EAEAKFDIRLLPGEDLEELLEEIEAILEKELPE 105
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
42-391 |
1.49e-23 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 100.96 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 42 GLIETVRDELRAVGIEATLTHGKGgkwaNLFATIpahdGETNGGVVLSGHTDVVPV-DGQQWDSDPFKPEIRGDKLYGRG 120
Cdd:cd05649 19 GVVERIEEEMEKLGFDEVEIDPMG----NVIGYI----GGGKKKILFDGHIDTVGIgNIDNWKFDPYEGYETDGKIYGRG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 121 TCDMKGFIGT---ALALVPDMQRTKLAKPIHFALSFDEEVgCVG-APLLIADlmKRGVKPDGCIVGEPTSMRPIIAHKGI 196
Cdd:cd05649 91 TSDQKGGLASmvyAAKIMKDLGLRDFAYTILVAGTVQEED-CDGvCWQYISK--ADKIKPDFVVSGEPTDGNIYRGQRGR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 197 NAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQFRAQgPF-----DELYDVPFSTAqtstitggnAINTVPAE 271
Cdd:cd05649 168 MEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFPEA-PFlgrgtLTVTDIFSTSP---------SRCAVPDS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 272 CQFQFEFRNL------PTLDPEQIFARIDSY-ARETLLPKMLREHSSAAIEITKIAAAPGLDSSEQAAITQ-LVRALtad 343
Cdd:cd05649 238 CRISIDRRLTvgetweGCLEEIRALPAVKKYgDDVAVSMYNYDRPSYTGEVYESERYFPTWLLPEDHELVKaLLEAY--- 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 344 qdkrKVAYGTEAGL----FSN--------AGIPSIVCGPGDIQQAHKANEFVELEQLVAC 391
Cdd:cd05649 315 ----KALFGARPLIdkwtFSTngvsimgrAGIPCIGFGPGAENQAHAPNEYTWKEDLVRC 370
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
40-399 |
6.45e-22 |
|
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: 95.98 E-value: 6.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 40 NLGLiETVRDELRAvgieaTLTHGKGgkwaNLFATIPAhDGETNGGVVLSGHTD-VVPVDGQQwdsdpfKPEIRGDKLYG 118
Cdd:cd05683 35 NLGL-SVIEDDAGK-----TTGGGAG----NLICTLKA-DKEEVPKILFTSHMDtVTPGINVK------PPQIADGYIYS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 119 RGT----CDMKGFIGTALALVPDMQRTKLA-KPIHFALSFDEEVGCVGAPLLIADLMK--------RGVKPDGCIVGEPT 185
Cdd:cd05683 98 DGTtilgADDKAGIAAILEAIRVIKEKNIPhGQIQFVITVGEESGLVGAKALDPELIDadygyaldSEGDVGTIIVGAPT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 186 SMRpiiahkgINAYqccVRGQAAHSSLTP-KGLNAIEYAARLICYIRdmadqfraQGPFDElydvpFSTAQTSTITGGNA 264
Cdd:cd05683 178 QDK-------INAK---IYGKTAHAGTSPeKGISAINIAAKAISNMK--------LGRIDE-----ETTANIGKFQGGTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 265 INTVPAECQFQFEFRnlpTLDPEQIFARIdSYARETLLpKMLREHsSAAIEITKIAAAPGLDSSEQAAITQL-VRALTAD 343
Cdd:cd05683 235 TNIVTDEVNIEAEAR---SLDEEKLDAQV-KHMKETFE-TTAKEK-GAHAEVEVETSYPGFKINEDEEVVKLaKRAANNL 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 648533650 344 QDKRKVAY---GTEAGLFSNAGIPSIVCGPGdIQQAHKANEFVELEQLVACERFLRKFI 399
Cdd:cd05683 309 GLEINTTYsggGSDANIINGLGIPTVNLGIG-YENIHTTNERIPIEDLYDTAVLVVEII 366
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
26-399 |
1.58e-21 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 95.49 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 26 VTRLVSMDTVS---RNPNlGLIETVRDELRAVGIEATlthgkggKWA------NLFATIPAHDGETNGGVVLSGHTDVVP 96
Cdd:PRK08596 19 LKTLVRFETPAppaRNTN-EAQEFIAEFLRKLGFSVD-------KWDvypndpNVVGVKKGTESDAYKSLIINGHMDVAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 97 VDG-QQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKP--IHFALSFDEEVGCVGAplliADLMKRG 173
Cdd:PRK08596 91 VSAdEAWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPgdLIFQSVIGEEVGEAGT----LQCCERG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 174 VKPD----------------GCIVGEPTSMRPIIAHKGinayqccVRGQAAHSSLTPKGLNAIEYAARLICYI----RDM 233
Cdd:PRK08596 167 YDADfavvvdtsdlhmqgqgGVITGWITVKSPQTFHDG-------TRRQMIHAGGGLFGASAIEKMMKIIQSLqeleRHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 234 ADQFRAQGpfdelYDVPFSTAQTSTITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARETLLPKM-LREH--- 309
Cdd:PRK08596 240 AVMKSYPG-----FPPGTNTINPAVIEGGRHAAFIADECRLWITVHFYPNETYEQVIKEIEEYIGKVAAADPwLRENppq 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 310 -----SSAAIEITKIAAAPGLDsSEQAAITQLVRALTADQDKRKV----AYGTEAGLFSNAGIPSIVCGPGDIQQAHKAN 380
Cdd:PRK08596 315 fkwggESMIEDRGEIFPSLEID-SEHPAVKTLSSAHESVLSKNAIldmsTTVTDGGWFAEFGIPAVIYGPGTLEEAHSVN 393
|
410
....*....|....*....
gi 648533650 381 EFVELEQLVACERFLRKFI 399
Cdd:PRK08596 394 EKVEIEQLIEYTKVITAFI 412
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
70-400 |
2.50e-21 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 93.88 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 70 NLFATIPAHDgetNGGVVLSGHTDVVPvdgqqwdsdPFKP---EIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKP 146
Cdd:cd05652 48 NVYAYPGSSR---QPRVLLTSHIDTVP---------PFIPysiSDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 147 IHFALSF--DEEVGCVGApLLIADLMKRGvkPDGCIVGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAA 224
Cdd:cd05652 116 GDLGLLFvvGEETGGDGM-KAFNDLGLNT--WDAVIFGEPTELKLASGHKGMLGFKLTAKGKAGHSGYPWLGISAIEILV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 225 RlICYIRDMADQfraqgPFDELYDVpfSTAQTSTITGGNAINTVPAECQFQFEFRnlPTLDPEQIFARIDSYARETLLPK 304
Cdd:cd05652 193 E-ALVKLIDADL-----PSSELLGP--TTLNIGRISGGVAANVVPAAAEASVAIR--LAAGPPEVKDIVKEAVAGILTDT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 305 mlrehssAAIEITKIAAAPGLDsseqaaitqlvraLTADQDKRK---VAYGTEAGLFSnAGIPSIVCGPGDIQQAHKANE 381
Cdd:cd05652 263 -------EDIEVTFTSGYGPVD-------------LDCDVDGFEtdvVAYGTDIPYLK-GDHKRYLYGPGSILVAHGPDE 321
|
330
....*....|....*....
gi 648533650 382 FVELEQLVACERFLRKFIH 400
Cdd:cd05652 322 AITVSELEEAVEGYKKLIL 340
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
23-198 |
7.16e-21 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 94.07 E-value: 7.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 23 LPWVTRLVSMDTVSrNPNLGLI------ETVRDELRAVGIEATLTHGKGgkwanlfatIPAHDGETNGG---VVLSGHTD 93
Cdd:PRK08554 4 LELLSSLVSFETVN-DPSKGIKpskecpKFIKDTLESWGIESELIEKDG---------YYAVYGEIGEGkpkLLFMAHFD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 94 VVPVDGQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKPIHFALSFDEEVGCVGAPLLIADLMKRG 173
Cdd:PRK08554 74 VVPVNPEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLNGKVIFAFTGDEEIGGAMAMHIAEKLREEG 153
|
170 180
....*....|....*....|....*.
gi 648533650 174 VKPDGCIVGEPTSMRPII-AHKGINA 198
Cdd:PRK08554 154 KLPKYMINADGIGMKPIIrRRKGFGV 179
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
26-363 |
1.34e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 92.99 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 26 VTRLVSMDTVSRNPNLGLIET-----VRDELRAVGIEATLTHGKGGKwANLFATIPAHDgETNGGVVLSGHTDVVPVDGQ 100
Cdd:PRK07906 5 CSELIRIDTTNTGDGTGKGEReaaeyVAEKLAEVGLEPTYLESAPGR-ANVVARLPGAD-PSRPALLVHGHLDVVPAEAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 101 QWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRT--KLAKPIHFALSFDEEVGCV-GAPLLI---ADLMkrgv 174
Cdd:PRK07906 83 DWSVHPFSGEIRDGYVWGRGAVDMKDMDAMMLAVVRHLARTgrRPPRDLVFAFVADEEAGGTyGAHWLVdnhPELF---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 175 kpDGCI------------VGEPTSMRPI-IAHKGINAYQCCVRGQAAHSSLTPKGlNAI----EYAARLICY-----IRD 232
Cdd:PRK07906 159 --EGVTeaisevggfsltVPGRDRLYLIeTAEKGLAWMRLTARGRAGHGSMVNDD-NAVtrlaEAVARIGRHrwplvLTP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 233 MADQFRAQgpFDELYDVPFS------------------------TAQTSTITGGNAINTVPAECQFQFEFRNLPTLDpEQ 288
Cdd:PRK07906 236 TVRAFLDG--VAELTGLEFDpddpdallaklgpaarmvgatlrnTANPTMLKAGYKVNVIPGTAEAVVDGRFLPGRE-EE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 289 IFARIDsyarETLLPKMLRE--HSSAAIEITkiaaapgLDSseqAAITQLVRALTA-DQDKRKVAY----GTEAGLFSNA 361
Cdd:PRK07906 313 FLATVD----ELLGPDVEREwvHRDPALETP-------FDG---PLVDAMNAALLAeDPGARVVPYmlsgGTDAKAFSRL 378
|
..
gi 648533650 362 GI 363
Cdd:PRK07906 379 GI 380
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
28-389 |
2.01e-20 |
|
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE)/acetyl-lysine deacetylase (LysK) subfamily. Proteins in this subfamily are mainly archaeal with related bacterial species and are deacetylases with specificity for both N-acetyl-ornithine and N-acetyl-lysine found within a lysine biosynthesis operon. ArgE catalyzes the conversion of N-acetylornithine to ornithine, while LysK, a homolog of ArgE, has deacetylating activities for both N-acetyllysine and N-acetylornithine at almost equal efficiency. These results suggest that LysK which may share an ancestor with ArgE functions not only for lysine biosynthesis, but also for arginine biosynthesis in species such as Thermus thermophilus. The substrate specificity of ArgE is quite broad in that several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349904 [Multi-domain] Cd Length: 343 Bit Score: 91.64 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 28 RLVSMDTVSRNPNLgLIETVRDELRAVGIEATLTHGKggkwaNLFATipahDGETNGGVVLSGHTDVVPvdgqqwdsDPF 107
Cdd:cd05653 9 DLLSIYSPSGEEAR-AAKFLEEIMKELGLEAWVDEAG-----NAVGG----AGSGPPDVLLLGHIDTVP--------GEI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 108 KPEIRGDKLYGRGTCDMKG----FIGTALALVPdmqrtKLAKPIHFALSFDEEVGCVGAPLLIAdlmkRGVKPDGCIVGE 183
Cdd:cd05653 71 PVRVEGGVLYGRGAVDAKGplaaMILAASALNE-----ELGARVVVAGLVDEEGSSKGARELVR----RGPRPDYIIIGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 184 PTSMRPI-IAHKGINAYQCCVRGQAAHSSLtPKGlNAIEyaaRLICYIRDMADQFRAqgpfDELYDVPFSTAQTSTITGG 262
Cdd:cd05653 142 PSGWDGItLGYRGSLLVKIRCEGRSGHSSS-PER-NAAE---DLIKKWLEVKKWAEG----YNVGGRDFDSVVPTLIKGG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 263 NAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYAREtllpkmlrehssaaIEITKIAAAPGLDSSEQAAITQ-LVRALT 341
Cdd:cd05653 213 ESSNGLPQRAEATIDLRLPPRLSPEEAIALATALLPT--------------CELEFIDDTEPVKVSKNNPLARaFRRAIR 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 648533650 342 AD--QDKRKVAYGTEAG--LFSNAGIPSIVCGPGDIQQAHKANEFVELEQLV 389
Cdd:cd05653 279 KQggKPRLKRKTGTSDMnvLAPLWTVPIVAYGPGDSTLDHTPNEHIELAEIE 330
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
78-389 |
9.00e-20 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 90.59 E-value: 9.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 78 HDGETNGGVV-LSGHTDVVPVdGQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRT--KLAKPIHFALSFD 154
Cdd:PRK13013 78 RQGARDGDCVhFNSHHDVVEV-GHGWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVypDFAGSIEISGTAD 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 155 EEVGCVGApllIADLMKRG----VKPDGCIVGEPTSM-RPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICY 229
Cdd:PRK13013 157 EESGGFGG---VAYLAEQGrfspDRVQHVIIPEPLNKdRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 230 IRD----MADQFRAQGPFdelydVP----FSTAQTSTITGGNAINT----------VPAECQFQFEFRNLPTLDPEQIFA 291
Cdd:PRK13013 234 IEErlfpLLATRRTAMPV-----VPegarQSTLNINSIHGGEPEQDpdytglpapcVADRCRIVIDRRFLIEEDLDEVKA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 292 RIDSyaretLLPKMLREHSSAAIEITKIAAAPGLDSSEQAAITQLVRALTADQDKRKVAYGTEAGLFSN------AGIPS 365
Cdd:PRK13013 309 EITA-----LLERLKRARPGFAYEIRDLFEVLPTMTDRDAPVVRSVAAAIERVLGRQADYVVSPGTYDQkhidriGKLKN 383
|
330 340
....*....|....*....|....*
gi 648533650 366 -IVCGPGDIQQAHKANEFVELEQLV 389
Cdd:PRK13013 384 cIAYGPGILDLAHQPDEWVGIADMV 408
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
86-299 |
5.55e-19 |
|
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: 88.47 E-value: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 86 VVLSGHTDVVPV---DGQQWDSDPFKPEIRGDKLYGRGTCDMKG-FIGT--ALAL------VPdmQRTklakpIHFALSF 153
Cdd:cd05674 72 LLLMAHQDVVPVnpeTEDQWTHPPFSGHYDGGYIWGRGALDDKNsLIGIleAVELllkrgfKP--RRT-----IILAFGH 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 154 DEEV-GCVGAPLLIADLMKR-GVKP------------DGCIVGEPTSMrPIIAHKGINAYQCCVRGQAAHSSLTPKGlNA 219
Cdd:cd05674 145 DEEVgGERGAGAIAELLLERyGVDGlaaildeggavlEGVFLGVPFAL-PGVAEKGYMDVEITVHTPGGHSSVPPKH-TG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 220 IEYAARLICYIRD--MADQFRAQGPFDELYDV--PFSTA-----------------------------------QTST-- 258
Cdd:cd05674 223 IGILSEAVAALEAnpFPPKLTPGNPYYGMLQClaEHSPLpprslksnlwlaspllkallasellstspltrallRTTQav 302
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 648533650 259 --ITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARE 299
Cdd:cd05674 303 diINGGVKINALPETATATVNHRIAPGSSVEEVLEHVKNLIAD 345
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
85-389 |
1.53e-18 |
|
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: 86.38 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 85 GVVLSGHTD-VVPVDgqqwdsDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRT--KLAKPIHFALSFDEE--VGC 159
Cdd:cd03896 56 ALLFSAHLDtVFPGD------TPATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAgaALKGDVVFAANVGEEglGDL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 160 VGAPLLIAdlmKRGVKPDGCIVGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQFra 239
Cdd:cd03896 130 RGARYLLS---AHGARLDYFVVAEGTDGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEALYEWAAPY-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 240 qgpfdelydVPFSTAQTSTITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIdsyarETLLPKMLREHSSAAIEITKI 319
Cdd:cd03896 205 ---------VPKTTFAAIRGGGGTSVNRIANLCSMYLDIRSNPDAELADVQREV-----EAVVSKLAAKHLRVKARVKPV 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648533650 320 AAAPGldsSEQAAITQLVRALTADQ-----DKRKVAYGTEAGLFSNAGIPSIVCGPGDIQQAHKANEFVELEQLV 389
Cdd:cd03896 271 GDRPG---GEAQGTEPLVNAAVAAHrevggDPRPGSSSTDANPANSLGIPAVTYGLGRGGNAHRGDEYVLKDDML 342
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
86-402 |
1.97e-18 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 86.92 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 86 VVLSGHTDVVPVDG---QQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDM-------QRTklakpIHFALSFDE 155
Cdd:PRK08262 114 IVLMAHQDVVPVAPgteGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALlaqgfqpRRT-----IYLAFGHDE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 156 EVGCVGAPLLIADLMKRGVKPD-----GCIVGE---PTSMRPI----IAHKGINAYQCCVRGQAAHSSLTPKGlNAIEYA 223
Cdd:PRK08262 189 EVGGLGARAIAELLKERGVRLAfvldeGGAITEgvlPGVKKPValigVAEKGYATLELTARATGGHSSMPPRQ-TAIGRL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 224 ARLICYIRD----------MADQFRAQGP-FDELYDVPFS--------------------------TAQTsTITGGNAIN 266
Cdd:PRK08262 268 ARALTRLEDnplpmrlrgpVAEMFDTLAPeMSFAQRVVLAnlwlfeplllrvlakspetaamlrttTAPT-MLKGSPKDN 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 267 TVPAECQFQFEFRNLPTLDPEQIFARIDSYAREtllpkmlrehSSAAIEITKIAAAPGLDSSEQAAITQLVRALTAD--Q 344
Cdd:PRK08262 347 VLPQRATATVNFRILPGDSVESVLAHVRRAVAD----------DRVEIEVLGGNSEPSPVSSTDSAAYKLLAATIREvfP 416
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648533650 345 DKRKVAY----GTEAGLFSnaGIPSIVC-------GPGDIQQAHKANEFVELEQLVACERFLRKFIHSM 402
Cdd:PRK08262 417 DVVVAPYlvvgATDSRHYS--GISDNVYrfsplrlSPEDLARFHGTNERISVANYARMIRFYYRLIENA 483
|
|
| selenium_YgeY |
TIGR03526 |
putative selenium metabolism hydrolase; SelD, selenophosphate synthase, is the selenium donor ... |
42-394 |
7.34e-18 |
|
putative selenium metabolism hydrolase; SelD, selenophosphate synthase, is the selenium donor protein for both selenocysteine and selenouridine biosynthesis systems, but it occurs also in a few prokaryotes that have neither of those pathways. The method of partial phylogenetic profiling, starting from such orphan-selD genomes, identifies this protein as one of those most strongly correlated to SelD occurrence. Its distribution is also well correlated with that of family TIGR03309, a putative accessory protein of labile selenium (non-selenocysteine) enzyme maturation. This family includes the uncharacterized YgeY of Escherichia coli, and belongs to a larger family of metalloenzymes in which some are known peptidases, others enzymes of different types.
Pssm-ID: 132565 [Multi-domain] Cd Length: 395 Bit Score: 84.46 E-value: 7.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 42 GLIETVRDELRAVGIEATLTHGKGgkwaNLFATIpahdGETNGGVVLSGHTDVVPV-DGQQWDSDPFKPEIRGDKLYGRG 120
Cdd:TIGR03526 34 RVALRIKQEMEKLGFDKVEIDPMG----NVLGYI----GHGPKLIAMDAHIDTVGIgDMDQWQFDPYEGYEDEEIIYGRG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 121 TCDMKGFIGTALalvpdmQRTKLAKPIHFALSFD-------EEVGCVG-APLLIadLMKRGVKPDGCIVGEPTSMRPIIA 192
Cdd:TIGR03526 106 ASDQEGGIASMV------YAGKIIKDLGLLDDYTllvtgtvQEEDCDGlCWQYI--IEEDKIKPEFVVITEPTDMNIYRG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 193 HKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQFRaqgpfdelyDVPFSTAQTSTIT----GGNAINTV 268
Cdd:TIGR03526 178 QRGRMEIKVTVKGVSCHGSAPERGDNAIYKMAPILKELSQLNANLV---------EDPFLGKGTLTVSeiffSSPSRCAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 269 PAECQFQF---------------EFRNLPTLDPEQIFARIDSYAR----------ETLLP--KMLREH--SSAAIEITK- 318
Cdd:TIGR03526 249 ADGCTISIdrrltwgetweyaleQIRNLPAVQGAEAEVEMYEYDRpsytglvyptECYFPtwVLPEDHliTKAALETYKr 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648533650 319 -IAAAPGLDsseqaaitqlvraltadqdkrKVAYGTEA-GLFSNAGIPSIVCGPGDIQQAHKANEFVELEQLVACERF 394
Cdd:TIGR03526 329 lFGKEPGVD---------------------KWTFSTNGvSIMGRHGIPVIGFGPGDEDQAHAPNEKTWKEDLVKAAAM 385
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
86-388 |
1.82e-17 |
|
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: 83.37 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 86 VVLSGHTDVVPvDGQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQrtKLAKPIHFA----LSFDEEVGCVG 161
Cdd:cd02697 76 VALNAHGDVVP-PGDGWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALE--SLGAPLRGAvelhFTYDEEFGGEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 162 APlliADLMKRGV-KPDgCIVGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARLICYIRDMADQFRAQ 240
Cdd:cd02697 153 GP---GWLLRQGLtKPD-LLIAAGFSYEVVTAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNALYALNAQYRQV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 241 GPFDELYDVPFstAQTSTITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARETllpkmLREHSSAAIEITKIA 320
Cdd:cd02697 229 SSQVEGITHPY--LNVGRIEGGTNTNVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIADA-----AASMPGISVDIRRLL 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648533650 321 AA------PGLDSSEQAAITQLVRALTADQDKRKVAYGTEAGLFSNAGIPSIVCGPGDI----QQAHKANEFVELEQL 388
Cdd:cd02697 302 LAnsmrplPGNAPLVEAIQTHGEAVFGEPVPAMGTPLYTDVRLYAEAGIPGVIYGAGPRtvleSHAKRADERLQLEDL 379
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
80-297 |
2.19e-17 |
|
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: 83.28 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 80 GETNGGVV--LSGHTDVVPVDGQQWDSDPFKPEIRGDKLYGRGTCDMKGFIgtalALVPDMQRtKLA--KP--------I 147
Cdd:cd08012 73 GTVDGKTVsfVGSHMDVVTANPETWEFDPFSLSIDGDKLYGRGTTDCLGHV----ALVTELFR-QLAteKPalkrtvvaV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 148 HFALSFDEEVGCVGAPLLIADLMKRGVKpDGCIVGEPTS-MRPIIAHKGINAYQCCVRGQAAHSSLTPKGLNAIEYAARL 226
Cdd:cd08012 148 FIANEENSEIPGVGVDALVKSGLLDNLK-SGPLYWVDSAdSQPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVMEA 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648533650 227 ICYI-RDMADQFRAQgPFDELYDvpFSTAQTSTIT----GGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYA 297
Cdd:cd08012 227 LAEIqKRFYIDFPPH-PKEEVYG--FATPSTMKPTqwsyPGGSINQIPGECTICGDCRLTPFYDVKEVREKLEEYV 299
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
90-389 |
2.67e-17 |
|
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: 83.45 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 90 GHTDVVPVdGQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGT---ALALVPDMQrTKLAKPIHFALSFDEEVGCVGAPLL- 165
Cdd:cd03888 78 GHLDVVPA-GEGWTTDPFKPVIKDGKLYGRGTIDDKGPTIAalyALKILKDLG-LPLKKKIRLIFGTDEETGWKCIEHYf 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 166 ----IADLmkrGVKPDG---CIVGE-------------PTSMRPIIAHKGINAY-------------------------- 199
Cdd:cd03888 156 eheeYPDF---GFTPDAefpVINGEkgivtvdltfkidDDKGYRLISIKGGEATnmvpdkaeavipgkdkeelalsaatd 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 200 ------------QCCVRGQAAHSSLTPKGLNAIEYAARLIC----------YIRDMADQ----FRAQGPFDELYDvPFST 253
Cdd:cd03888 233 lkgnieiddggvELTVTGKSAHASAPEKGVNAITLLAKFLAelnkdgndkdFIKFLAKNlhedYNGKKLGINFED-EVMG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 254 AQTSTITggnAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARETLLPkmlrehssaaIEITKIaAAPGLDSSEqaai 333
Cdd:cd03888 312 ELTLNPG---IITLDDGKLELGLNVRYPVGTSAEDIIKQIEEALEKYGVE----------VEGHKH-QKPLYVPKD---- 373
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 334 TQLVRALTAdqdkrkvAY----GTEAGLFSNAG------IPSIVC-G---PGDIQQAHKANEFVELEQLV 389
Cdd:cd03888 374 SPLVKTLLK-------VYeeqtGKEGEPVAIGGgtyareLPNGVAfGpefPGQKDTMHQANEFIPIDDLI 436
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
25-398 |
2.48e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 80.33 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 25 WVTRLVSMDTVS-----RNPNLGLIETVRDELRAVGIEATLTHGKGGKWAnLFATIPAHDGETNggVVLSGHTDVVPV-D 98
Cdd:PRK07907 23 DLEELVRIPSVAadpfrREEVARSAEWVADLLREAGFDDVRVVSADGAPA-VIGTRPAPPGAPT--VLLYAHHDVQPPgD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 99 GQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTAL----ALVPDMqrtklakPIHFALsF---DEEVGCVGAPLLIA---D 168
Cdd:PRK07907 100 PDAWDSPPFELTERDGRLYGRGAADDKGGIAMHLaalrALGGDL-------PVGVTV-FvegEEEMGSPSLERLLAehpD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 169 LMKRGVkpdgcI---------VGEP---TSMRPIIahkginayQCCVR----GQAAHSSL----TPKGLNAieyAARLIC 228
Cdd:PRK07907 172 LLAADV-----IviadsgnwsVGVPaltTSLRGNA--------DVVVTvrtlEHAVHSGQfggaAPDALTA---LVRLLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 229 YIRDMA---------------------DQFRAQ-GPFD--ELY---DVPFS--TAQTSTITG------GNAINTVPAECQ 273
Cdd:PRK07907 236 TLHDEDgnvavdgldatepwlgvdydeERFRADaGVLDgvELIgtgSVADRlwAKPAITVIGidappvAGASNALPPSAR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 274 FQFEFRNLPTLDPEQIFAridsyaretLLPKMLREHS--SAAIEITKI-AAAPGLDSSEQAAITQLVRALTAdqdkrkvA 350
Cdd:PRK07907 316 ARLSLRVAPGQDAAEAQD---------ALVAHLEAHApwGAHVTVERGdAGQPFAADASGPAYDAARAAMRE-------A 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648533650 351 YGTE----------------AGLFSNAGIpsIVCGPGDIQ-QAHKANEFV---ELEQLVACER-FLRKF 398
Cdd:PRK07907 380 WGKDpvdmgmggsipfiaelQEAFPQAEI--LVTGVEDPKtRAHSPNESVhlgELERAAVAEAlLLARL 446
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
45-388 |
2.48e-16 |
|
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: 80.43 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 45 ETVRDELRAVGIEATLTHGKGGKWANLFATIPAHDGETnggVVLSGHTDVVPVDG-QQWDSDPFKPEIRGDKLYGRGTCD 123
Cdd:cd05680 28 EWLADKLTEAGFEHTEVLPTGGHPLVYAEWLGAPGAPT---VLVYGHYDVQPPDPlELWTSPPFEPVVRDGRLYARGASD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 124 MKGFIGTALALVPDMQRTKLAKP--IHFALSFDEEVGCVGAPLLIADLMKRgVKPDGCIVGEpTSM----RPIIAH--KG 195
Cdd:cd05680 105 DKGQVFIHIKAVEAWLAVEGALPvnVKFLIEGEEEIGSPSLPAFLEENAER-LAADVVLVSD-TSMwspdTPTITYglRG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 196 INAYQCCVRG--QAAHSSLTPKGL-NAIEYAARLIC--------------Y--IRDMADQFR---AQGPFDE-------- 245
Cdd:cd05680 183 LAYLEISVTGpnRDLHSGSYGGAVpNPANALARLLAslhdedgrvaipgfYddVRPLTDAEReawAALPFDEaafkaslg 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 246 LYDVP----FSTAQTST---------ITGG---NAINTV-PAECQFQFEFRNLPTLDPEQIFARIDSYaretllpkmLRE 308
Cdd:cd05680 263 VPALGgeagYTTLERLWarptldvngIWGGyqgEGSKTViPSKAHAKISMRLVPGQDPDAIADLLEAH---------LRA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 309 HSSAAIEITKI---AAAPGLDSSEQAAITQLVRALTAdqdkrkvAYGTEA------------GLFSNA-GIPSIVCGPG- 371
Cdd:cd05680 334 HAPPGVTLSVKplhGGRPYLVPTDHPALQAAERALEE-------AFGKPPvfvreggsipivALFEKVlGIPTVLMGFGl 406
|
410
....*....|....*..
gi 648533650 372 DIQQAHKANEFVELEQL 388
Cdd:cd05680 407 PDDAIHAPNEKFRLECF 423
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
70-186 |
6.53e-16 |
|
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: 75.55 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 70 NLFATIPAhdGETNGGVVLSGHTDVVPV-DGQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDM--QRTKLAKP 146
Cdd:cd18669 1 NVIARYGG--GGGGKRVLLGAHIDVVPAgEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLkeNGFKLKGT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 648533650 147 IHFALSFDEEVGCVGAPLLIADLMKR-GVKPDGCIVGEPTS 186
Cdd:cd18669 79 VVVAFTPDEEVGSGAGKGLLSKDALEeDLKVDYLFVGDATP 119
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
29-389 |
7.05e-16 |
|
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: 78.91 E-value: 7.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 29 LVSMDTVSRNP-NLGLI----ETVRDELRAVGIEATLTHGKGGKWAnLFATIPAHDGEtnGGVVLSGHTDVVPVDGQQ-W 102
Cdd:cd03893 7 LVAIPSVSAQPdRREELrraaEWLADLLRRLGFTVEIVDTSNGAPV-VFAEFPGAPGA--PTVLLYGHYDVQPAGDEDgW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 103 DSDPFKPEIRGDKLYGRGTCDMKGFIGTAL-ALVPDMQRTKLAKP-IHFALSFDEEVGCVGAPLLIADLmKRGVKPDGCI 180
Cdd:cd03893 84 DSDPFELTERDGRLYGRGAADDKGPILAHLaALRALMQQGGDLPVnVKFIIEGEEESGSPSLDQLVEAH-RDLLAADAIV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 181 VGEPTSM---RPIIAH--KGINAYQCCVRGQAA--HSSLTpkG---LNAIEYAARLICYIRD-----------------M 233
Cdd:cd03893 163 ISDSTWVgqeQPTLTYglRGNANFDVEVKGLDHdlHSGLY--GgvvPDPMTALAQLLASLRDetgrilvpglydavrelP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 234 ADQFRAQGPFDELYDVPFSTAQTS----------TITG------GNAINTV-PAECQFQFEFRNLPTLDPEQIfaridsy 296
Cdd:cd03893 241 EEEFRLDAGVLEEVEIIGGTTGSVaerlwtrpalTVLGidggfpGEGSKTViPPRARAKISIRLVPGQDPEEA------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 297 arETLLPKMLREH--SSAAIEIT-----KIAAAPGLDSSEQAAItqlvRALTADQDKrKVAYGTEAGLFSNA-------G 362
Cdd:cd03893 314 --SRLLEAHLEKHapSGAKVTVSyveggMPWRSDPSDPAYQAAK----DALRTAYGV-EPPLTREGGSIPFIsvlqefpQ 386
|
410 420
....*....|....*....|....*...
gi 648533650 363 IPSIVCGPGDIQ-QAHKANEFVELEQLV 389
Cdd:cd03893 387 APVLLIGVGDPDdNAHSPNESLRLGNYK 414
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
70-185 |
2.25e-15 |
|
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: 74.38 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 70 NLFATIPAhdGETNGGVVLSGHTDVVPVD-GQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDM--QRTKLAKP 146
Cdd:cd03873 1 NLIARLGG--GEGGKSVALGAHLDVVPAGeGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLkeNGFKPKGT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 648533650 147 IHFALSFDEEVGCVGAP-LLIADLMKRGVKPDGCIVGEPT 185
Cdd:cd03873 79 IVVAFTADEEVGSGGGKgLLSKFLLAEDLKVDAAFVIDAT 118
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
33-246 |
4.29e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 73.63 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 33 DTVSRNpNLGLIET---VRDELRAVGIEATLTHGKGGkwanlfatiPAHDGETNGG----VVLSGHTDVVPVDG-QQWDS 104
Cdd:PRK06446 15 PSISAT-GEGIEETanyLKDTMEKLGIKANIERTKGH---------PVVYGEINVGakktLLIYNHYDVQPVDPlSEWKR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 105 DPFKPEIRGDKLYGRGTCDMKG-FIGTALALVPDMQRTKLAKPIHFALSFDEEVGCVGAPLLIADLMKRgVKPDGCIV-- 181
Cdd:PRK06446 85 DPFSATIENGRIYARGASDNKGtLMARLFAIKHLIDKHKLNVNVKFLYEGEEEIGSPNLEDFIEKNKNK-LKADSVIMeg 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 182 -GEPTSMRPIIAH--KGINAYQCCVRGQAA--HSSLTPKGLNAIEYAARLICYIRDMADQFRAQGPFDEL 246
Cdd:PRK06446 164 aGLDPKGRPQIVLgvKGLLYVELVLRTGTKdlHSSNAPIVRNPAWDLVKLLSTLVDGEGRVLIPGFYDDV 233
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
86-393 |
4.52e-14 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 73.07 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 86 VVLSGHTDVV-PVDgqqwdsDPFK--PEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKPIHF--ALSFDEEVGCV 160
Cdd:PRK07338 95 VLLTGHMDTVfPAD------HPFQtlSWLDDGTLNGPGVADMKGGIVVMLAALLAFERSPLADKLGYdvLINPDEEIGSP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 161 GAPLLIADLMKRG--------VKPDGCIVGeptsmrpiiAHKGINAYQCCVRGQAAHSSLTP-KGLNAIEYAARLICYIR 231
Cdd:PRK07338 169 ASAPLLAELARGKhaaltyepALPDGTLAG---------ARKGSGNFTIVVTGRAAHAGRAFdEGRNAIVAAAELALALH 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 232 DMADQfraqgpfdeLYDVPFSTAQtstITGGNAINTVPAECQFQFEFRnLPTLDPEQIF-ARIDsyareTLLPKMLREHS 310
Cdd:PRK07338 240 ALNGQ---------RDGVTVNVAK---IDGGGPLNVVPDNAVLRFNIR-PPTPEDAAWAeAELK-----KLIAQVNQRHG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 311 SAAIEITKIAAAPGLDSSEQAAITQLVRALTAD--QDKRKVAYG--TEAGLFSNAGIPSI----VCGpGDIqqaHKANEF 382
Cdd:PRK07338 302 VSLHLHGGFGRPPKPIDAAQQRLFEAVQACGAAlgLTIDWKDSGgvCDGNNLAAAGLPVVdtlgVRG-GNI---HSEDEF 377
|
330
....*....|.
gi 648533650 383 VELEQLVacER 393
Cdd:PRK07338 378 VILDSLV--ER 386
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
28-389 |
6.42e-14 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 72.74 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 28 RLVSMDTVSRN-PNLGLI-ETVRDELRAVGIEATLTHGKGGKWANLFATIpahDGETNGGVVLSGHTDVVPVDGQQwDSD 105
Cdd:PRK06133 45 ELVSIESGSGDaEGLKQVaALLAERLKALGAKVERAPTPPSAGDMVVATF---KGTGKRRIMLIAHMDTVYLPGML-AKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 106 PFKpeIRGDKLYGRGTCDMKGFIGT---ALALVPDMQRTKLAKpIHFALSFDEEVGCVGAPLLIADLmkrGVKPDGCIVG 182
Cdd:PRK06133 121 PFR--IDGDRAYGPGIADDKGGVAVilhALKILQQLGFKDYGT-LTVLFNPDEETGSPGSRELIAEL---AAQHDVVFSC 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 183 EPTSMRP--IIAHKGINAYQCCVRGQAAHSSLTPK-GLNAIEYAARLICYIRDMADqfraqgpfdelyDVPFSTAQTSTI 259
Cdd:PRK06133 195 EPGRAKDalTLATSGIATALLEVKGKASHAGAAPElGRNALYELAHQLLQLRDLGD------------PAKGTTLNWTVA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 260 TGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARETLLP----KMLREHSSAAIEITkiAAAPGLDSSEQAAITQ 335
Cdd:PRK06133 263 KAGTNRNVIPASASAQADVRYLDPAEFDRLEADLQEKVKNKLVPdtevTLRFERGRPPLEAN--AASRALAEHAQGIYGE 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 648533650 336 LVRALTADqDKRkVAYGTEAGLFSNAGIPSIVCGPGDIQ-QAHKANEFVELEQLV 389
Cdd:PRK06133 341 LGRRLEPI-DMG-TGGGTDAAFAAGSGKAAVLEGFGLVGfGAHSNDEYIELNSIV 393
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
90-196 |
9.32e-14 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 72.57 E-value: 9.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 90 GHTDVVPVdGQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTA---LALVPDMQrTKLAKPIHFALSFDEEVGCVGaplli 166
Cdd:PRK07318 86 GHLDVVPA-GDGWDTDPYEPVIKDGKIYARGTSDDKGPTMAAyyaLKIIKELG-LPLSKKVRFIVGTDEESGWKC----- 158
|
90 100 110
....*....|....*....|....*....|....*
gi 648533650 167 adlMKRGVK----PDgcIVGEPTSMRPII-AHKGI 196
Cdd:PRK07318 159 ---MDYYFEheeaPD--FGFSPDAEFPIInGEKGI 188
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
28-403 |
3.83e-13 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 70.80 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 28 RLVSMDTV-SRNPNLGLIETVRDELRAVG-----IEATLTHGKGGkwaNLFATIPAHDgeTNGGVVLSGHTDVVPVDGQQ 101
Cdd:PRK09133 45 ELIEINTTaSTGSTTPAAEAMAARLKAAGfadadIEVTGPYPRKG---NLVARLRGTD--PKKPILLLAHMDVVEAKRED 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 102 WDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRT--KLAKPIHFALSFDEEVGCV-GAPLLIADLmKRGVKPDG 178
Cdd:PRK09133 120 WTRDPFKLVEENGYFYGRGTSDDKADAAIWVATLIRLKREgfKPKRDIILALTGDEEGTPMnGVAWLAENH-RDLIDAEF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 179 CI----------VGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLtPKGLNAI-EYAARLI----------------CYIR 231
Cdd:PRK09133 199 ALneggggtldeDGKPVLLTVQAGEKTYADFRLEVTNPGGHSSR-PTKDNAIyRLAAALSrlaayrfpvmlndvtrAYFK 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 232 DMADQFR----------AQGPFDE-----LYDVPFSTAQTST------ITGGNAINTVPAECQFQFEFRNLPTLDPEQIF 290
Cdd:PRK09133 278 QSAAIETgplaaamrafAANPADEaaialLSADPSYNAMLRTtcvatmLEGGHAENALPQRATANVNCRIFPGDTIEAVR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 291 ARIdsyarETLL--PKMlrehssaAIEIT---KIAAAPGLDSSEQAAITQLVRALTAD------QDkrkvAYGTEAGLFS 359
Cdd:PRK09133 358 ATL-----KQVVadPAI-------KITRIgdpSPSPASPLRPDIMKAVEKLTAAMWPGvpvipsMS----TGATDGRYLR 421
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 648533650 360 NAGIPS-----IVCGPGDIqQAHKANEFVELEQLVACERFLRKFIHSMS 403
Cdd:PRK09133 422 AAGIPTygvsgLFGDPDDT-FAHGLNERIPVASFYEGRDFLYELVKDLA 469
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
90-183 |
1.93e-12 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 68.56 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 90 GHTDVVPVdGQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGT---ALALVPDMQrTKLAKPIHFALSFDEEVG--CVGAPL 164
Cdd:TIGR01887 74 GHLDVVPA-GDGWTSPPFEPTIKDGRIYGRGTLDDKGPTIAayyAMKILKELG-LKLKKKIRFIFGTDEESGwkCIDYYF 151
|
90 100
....*....|....*....|..
gi 648533650 165 LIADLMKRGVKPDG---CIVGE 183
Cdd:TIGR01887 152 EHEEMPDIGFTPDAefpIIYGE 173
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
86-388 |
2.80e-12 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 67.29 E-value: 2.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 86 VVLSGHTDVVPVDgqqwdsdpfKP-EIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKpIHFALSFDEEVGCVGAPL 164
Cdd:PRK04443 62 VLLLGHIDTVPGD---------IPvRVEDGVLWGRGSVDAKGPLAAFAAAAARLEALVRAR-VSFVGAVEEEAPSSGGAR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 165 LIADLMkrgvKPDGCIVGEPTSMRPI-IAHKGINAYQCCVRGQAAHSSltPKGLNAIEyaaRLICYIRDMADQFRAQGPF 243
Cdd:PRK04443 132 LVADRE----RPDAVIIGEPSGWDGItLGYKGRLLVTYVATSESFHSA--GPEPNAAE---DAIEWWLAVEAWFEANDGR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 244 DELYDvpfstAQTSTItggNAINTVPAECQFQ----FEFRNLPTLDPEQIFARIDSYAretllpkmlrehssAAIEITKI 319
Cdd:PRK04443 203 ERVFD-----QVTPKL---VDFDSSSDGLTVEaemtVGLRLPPGLSPEEAREILDALL--------------PTGTVTFT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 320 AAAPGLDSSEQaaiTQLVRAL-----TADQDKR-KVAYGTE-----AGLFsnaGIPSIVCGPGDIQQAHKANEFVELEQL 388
Cdd:PRK04443 261 GAVPAYMVSKR---TPLARAFrvairEAGGTPRlKRKTGTSdmnvvAPAW---GCPMVAYGPGDSDLDHTPDEHLPLAEY 334
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
86-299 |
1.01e-11 |
|
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: 66.14 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 86 VVLSGHTDVVPVDGQQWDSDPFKPEIRGD-KLYGRGTCDMK----GFIGTALALVpdMQRTKLAKPIHfaLSF--DEEVG 158
Cdd:cd05646 67 ILLNSHTDVVPVFEEKWTHDPFSAHKDEDgNIYARGAQDMKcvgiQYLEAIRRLK--ASGFKPKRTIH--LSFvpDEEIG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 159 CV-GAPLLIA-DLMKR---GVKPDGCIVGEPTSMRPIIAHKGINAYQCCVRGQAAHSSLTPKGlNAIEYAARLICYIRDm 233
Cdd:cd05646 143 GHdGMEKFVKtEEFKKlnvGFALDEGLASPTEEYRVFYGERSPWWVVITAPGTPGHGSKLLEN-TAGEKLRKVIESIME- 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648533650 234 adqFRAQgPFDELYDVP------FSTAQTSTITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSYARE 299
Cdd:cd05646 221 ---FRES-QKQRLKSNPnltlgdVTTVNLTMLKGGVQMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAE 288
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
86-403 |
1.02e-11 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 66.31 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 86 VVLSGHTDVVPVDG-QQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKPIH--FALSFDEEVGCVGA 162
Cdd:PRK08201 82 VLIYGHYDVQPVDPlNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNvkFCIEGEEEIGSPNL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 163 PLLIADlMKRGVKPDGCIVGEpTSM----RPIIAH--KGINAYQCCVRGQAA--HSSLTPKGL-NAIEYAARLICYIRD- 232
Cdd:PRK08201 162 DSFVEE-EKDKLAADVVLISD-TTLlgpgKPAICYglRGLAALEIDVRGAKGdlHSGLYGGAVpNALHALVQLLASLHDe 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 233 -------------------MADQFRAQGpFDE-----------LYDVPFSTAQTST-------ITG------GNAINTV- 268
Cdd:PRK08201 240 hgtvavegfydgvrpltpeEREEFAALG-FDEeklkrelgvdeLFGEEGYTALERTwarptleLNGvyggfqGEGTKTVi 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 269 PAECQFQFEFRNLPTLDPEQIFARIDSYaretllpkmLREHSSAAIEIT-------KIAAAPGLDSSEQAAitqlVRALT 341
Cdd:PRK08201 319 PAEAHAKITCRLVPDQDPQEILDLIEAH---------LQAHTPAGVRVTirrfdkgPAFVAPIDHPAIQAA----ARAYE 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648533650 342 AdqdkrkvAYGTEAgLFSNAG--------------IPSIVCGPG-DIQQAHKANEFVELEQLVACERFLRKFIHSMS 403
Cdd:PRK08201 386 A-------VYGTEA-AFTRMGgsipvvetfssqlhIPIVLMGFGlPSENFHAPNEHFHLENFDKGLRTLVEYWHQLA 454
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
90-388 |
9.41e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 63.17 E-value: 9.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 90 GHTDVVPV-DGQQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDM--QRTKLAKPIHFALSFDEEV--GCVGAPL 164
Cdd:PRK07205 82 CHLDVVPEgDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALldAGVQFNKRIRFIFGTDEETlwRCMNRYN 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 165 LIADLMKRGVKPDgcivgeptSMRPII-AHKGI------------------NAY-------------------------- 199
Cdd:PRK07205 162 EVEEQATMGFAPD--------SSFPLTyAEKGLlqaklvgpgsdqlelevgQAFnvvpakasyqgpkleavkkeldklgf 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 200 -------QCCVRGQAAHSSLTPKGLNAIeyaARLICYIRDMADQ----FRAQGpFDElydvpfstaqtsTITGGNAINTV 268
Cdd:PRK07205 234 eyvvkenEVTVLGKSVHAKDAPQGINAV---IRLAKALVVLEPHpaldFLANV-IGE------------DATGLNIFGDI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 269 PAECQFQFEFrNLP--TLDPEQIFARID-----SYARETLLPKmlrehssaaieITKIAAAPGLDSSE---QAAI----- 333
Cdd:PRK07205 298 EDEPSGKLSF-NIAglTITKEKSEIRIDiripvLADKEKLVQQ-----------LSQKAQEYGLTYEEfdyLAPLyvpld 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648533650 334 TQLVRAL-------TADQDKRKVAYGTEaglFSNAgIPSIV----CGPGDIQQAHKANEFVELEQL 388
Cdd:PRK07205 366 SELVSTLmsvyqekTGDDSPAQSSGGAT---FART-MPNCVafgaLFPGAPQTEHQANEHIVLEDL 427
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
26-161 |
1.56e-09 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 59.43 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 26 VTRLVSMDTVSRNPNLG------LIETVRDELRAVGIEATLTHGK-GGKWANLFATipAHDGETNGGVVLSGHTDVVPVD 98
Cdd:cd05679 10 LARRVAVPTESQEPARKpelrayLDQEMRPRFERLGFTVHIHDNPvAGRAPFLIAE--RIEDPSLPTLLIYGHGDVVPGY 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648533650 99 GQQWDS--DPFKPEIRGDKLYGRGTCDMKG--FIG-TALALVPDMQRTKLAKPIHFALSFDEEVGCVG 161
Cdd:cd05679 88 EGRWRDgrDPWTVTVWGERWYGRGTADNKGqhSINmAALRQVLEARGGKLGFNVKFLIEMGEEMGSPG 155
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
34-296 |
4.50e-09 |
|
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: 57.88 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 34 TVSRNPNLG-LIETVRDELRAVGIEATLTHGKGGK------WANLFATIPAhdgetnggVVLSGHTDVVPVDGQQWDSDP 106
Cdd:TIGR01880 23 TVQPNPDYAaCVDFLIKQADELGLARKTIEFVPGKpvvvltWPGSNPELPS--------ILLNSHTDVVPVFREHWTHPP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 107 FKPEIRGD-KLYGRGTCDMKGFIGTALALVPDMQRT--KLAKPIHFALSFDEEVGCV-GAPLLIA-DLMKR---GVKPDG 178
Cdd:TIGR01880 95 FSAFKDEDgNIYARGAQDMKCVGVQYLEAVRNLKASgfKFKRTIHISFVPDEEIGGHdGMEKFAKtDEFKAlnlGFALDE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 179 CIVGEPTSMRPIIAHKGINAYQCCVRGQAAHSS--LTPKGLNAIEYAARLICYIRDMADQFRAQGPFDELYDVpfSTAQT 256
Cdd:TIGR01880 175 GLASPDDVYRVFYAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRRFRESQFQLLQSNPDLAIGDV--TSVNL 252
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 648533650 257 STITGGNAINTVPAECQFQFEFRNLPTLDPEQIFARIDSY 296
Cdd:TIGR01880 253 TKLKGGVQSNVIPSEAEAGFDIRLAPSVDFEEMENRLDEW 292
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
84-389 |
8.37e-09 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 56.72 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 84 GGVVLSGHTDVVPvdGQqwdsdpFKPEIRGDKLYGRGTCDMKGFIgTALALVPDMQRTKLAKPIHFALSfDEEVGCVGAp 163
Cdd:PRK00466 61 GDILLASHVDTVP--GY------IEPKIEGEVIYGRGAVDAKGPL-ISMIIAAWLLNEKGIKVMVSGLA-DEESTSIGA- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 164 lliADLMKRGVKPDGCIVGEPTSMRPI-IAHKGINAYQCCVRGQAAHSSLTPKGLnAIEYAARLICYIRDmadqfraqgp 242
Cdd:PRK00466 130 ---KELVSKGFNFKHIIVGEPSNGTDIvVEYRGSIQLDIMCEGTPEHSSSAKSNL-IVDISKKIIEVYKQ---------- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 243 fDELYDVPfsTAQTSTITGGNAINTVPAECQFQFEFR-NLPTLDpEQIFARIDSYARETLLpkmlreHSSAAIEITKIaa 321
Cdd:PRK00466 196 -PENYDKP--SIVPTIIRAGESYNVTPAKLYLHFDVRyAINNKR-DDLISEIKDKFQECGL------KIVDETPPVKV-- 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648533650 322 apgldSSEQAAITQLVRALTADQDKRKVAY--GT-EAGLFSNAgIPSIVC-GPGDIQQAHKANEFVELEQLV 389
Cdd:PRK00466 264 -----SINNPVVKALMRALLKQNIKPRLVRkaGTsDMNILQKI-TTSIATyGPGNSMLEHTNQEKITLDEIY 329
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
85-272 |
1.68e-08 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 55.95 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 85 GVVLSGHTDVV-PVDGQQwdSDPFKPEirGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKPIHFALSF--DEEVGCVG 161
Cdd:PRK07473 77 GILIAGHMDTVhPVGTLE--KLPWRRE--GNKCYGPGILDMKGGNYLALEAIRQLARAGITTPLPITVLFtpDEEVGTPS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 162 APLLIADLMKR---------GVKPDGCIVGeptsmRPIIAHKGINAYqccvrGQAAHSSLTPK-GLNAIEYAARLICYIR 231
Cdd:PRK07473 153 TRDLIEAEAARnkyvlvpepGRPDNGVVTG-----RYAIARFNLEAT-----GRPSHAGATLSeGRSAIREMARQILAID 222
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 648533650 232 DMADQfraqgpfdelyDVPFSTAqtsTITGGNAINTVPAEC 272
Cdd:PRK07473 223 AMTTE-----------DCTFSVG---IVHGGQWVNCVATTC 249
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
91-132 |
1.78e-08 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 56.13 E-value: 1.78e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 648533650 91 HTDVVPVDGQQW-----DSDPFKPEIRGDKLYGRGTCDMKGFIGTAL 132
Cdd:PRK06156 117 HADVVPANPELWvldgtRLDPFKVTLVGDRLYGRGTEDDKGAIVTAL 163
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
90-168 |
2.32e-08 |
|
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: 55.69 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 90 GHTDVVPV---DGqqWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKPIHFALSFD--EEVGCVGAPL 164
Cdd:cd05676 92 GHLDVQPAkleDG--WDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLGQELPVNLKFCFEgmEESGSEGLDE 169
|
....
gi 648533650 165 LIAD 168
Cdd:cd05676 170 LIEA 173
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
29-161 |
7.65e-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: 53.89 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 29 LVSMDTVSRNPNLGLIET-------VRDELRAVGIEAT-LTHGKGGKWANLFATIPAHDGETNGGVVL-SGHTDVVPVDG 99
Cdd:cd05677 8 FIAFQTVSQSPTTENAEDsrrcaifLRQLFKKLGATNClLLPSGPGTNPIVLATFSGNSSDAKRKRILfYGHYDVIPAGE 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 648533650 100 -QQWDSDPFKPEIRGDKLYGRGTCDMKGFIGTALALVPDM-QRTKLAKPIHFALSFDEEVGCVG 161
Cdd:cd05677 88 tDGWDTDPFTLTCENGYLYGRGVSDNKGPLLAAIYAVAELfQEGELDNDVVFLIEGEEESGSPG 151
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
27-169 |
1.18e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 53.38 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 27 TRLVSMDTVSRNPNLG------LIETVRDELRAVGIEATLTHG-KGGKWANLFATipAHDGETNGGVVLSGHTDVVPVDG 99
Cdd:PRK07079 24 ARRVAYRTESQNPDRApalrayLTDEIAPALAALGFTCRIVDNpVAGGGPFLIAE--RIEDDALPTVLIYGHGDVVRGYD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 100 QQWDS--DPFKPEIRGDKLYGRGTCDMKG--FIG-TALALVPDMQRTKLAKPIHFALSFDEEVGCVG--------APLLI 166
Cdd:PRK07079 102 EQWREglSPWTLTEEGDRWYGRGTADNKGqhTINlAALEQVLAARGGRLGFNVKLLIEMGEEIGSPGlaevcrqhREALA 181
|
...
gi 648533650 167 ADL 169
Cdd:PRK07079 182 ADV 184
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
70-238 |
1.91e-07 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 52.94 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 70 NLFATIPaHDGETNGGVVLSGHTDVVPVD--GQqWDSDPFKPEI-------------------RGDKLYGRGTCDMKGFI 128
Cdd:COG4187 67 NVTALVK-GKGESKKTVILISHFDVVDVEdyGS-LKPLAFDPEEltealkeiklpedvrkdleSGEWLFGRGTMDMKAGL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 129 GTALALVPD-MQRTKLAKPIHFALSFDEEVGCVG----APLLiADLMKR-GVKPDGCIVGEPT-SMRPIIAHKGI----- 196
Cdd:COG4187 145 ALHLALLEEaSENEEFPGNLLLLAVPDEEVNSAGmraaVPLL-AELKEKyGLEYKLAINSEPSfPKYPGDETRYIytgsi 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 648533650 197 -----NAYqccVRGQAAHSSLTPKGLNAIEYAARLICYIR---DMADQFR 238
Cdd:COG4187 224 gklmpGFY---CYGKETHVGEPFSGLNANLLASELTRELElnpDFCEEVG 270
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
48-126 |
3.35e-06 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 49.13 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 48 RDELRAVGIEATL--THGKggkwanlfATIPAHDGETNGG---VVLSGHTDVVPVDGQQ-WDSDPFKPEIR----GDK-L 116
Cdd:PRK09104 50 VADLASLGFEASVrdTPGH--------PMVVAHHEGPTGDaphVLFYGHYDVQPVDPLDlWESPPFEPRIKetpdGRKvI 121
|
90
....*....|
gi 648533650 117 YGRGTCDMKG 126
Cdd:PRK09104 122 VARGASDDKG 131
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
71-177 |
4.03e-06 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 48.87 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 71 LFATIPAHDgETNGGVVLSGHTDVVP-VDGqqWDSD--PFKPEIRGDKLYGRGTCDMKGFIGTALALVPDMQRTKLAKP- 146
Cdd:cd05682 62 LFVEIPGTE-QDDDTVLLYGHMDKQPpFTG--WDEGlgPTKPVIRGDKLYGRGGADDGYAIFASLTAIKALQEQGIPHPr 138
|
90 100 110
....*....|....*....|....*....|.
gi 648533650 147 IHFALSFDEEVGCVGAPLLIADLMKRGVKPD 177
Cdd:cd05682 139 CVVLIEACEESGSADLPFYLDKLKERIGNVD 169
|
|
| M20_pepD |
cd03890 |
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, ... |
70-162 |
7.23e-05 |
|
M20 Peptidase D has specificity for beta-alanyl-L-histidine dipeptide; Peptidase M20 family, Peptidase D (PepD, Xaa-His dipeptidase; X-His dipeptidase; aminoacylhistidine dipeptidase; dipeptidase D; Beta-alanyl-histidine dipeptidase; pepD g.p. (Escherichia coli); EC 3.4.13.3) subfamily. PepD is a cytoplasmic enzyme family characterized by its unusual specificity for the dipeptides beta-alanyl-L-histidine (L-carnosine or beta-Ala-His) and gamma-aminobutyryl histidine (L-homocarnosine or gamma-amino-butyl-His). Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA), acting as a GABA reservoir, and may mediate anti-seizure effects of GABAergic therapies. It has also been reported that glucose metabolism could be influenced by L-carnosine. PepD also includes a lid domain that forms a homodimer; however, the physiological function of this extra domain remains unclear.
Pssm-ID: 349885 [Multi-domain] Cd Length: 474 Bit Score: 44.82 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 70 NLFATIPAhdgeTNG-----GVVLSGHTDVVPV--DGQQWD--SDPFKPEIRGDKLYGRGT---CDmKGfIGTALALV-- 135
Cdd:cd03890 46 NVIIRKPA----TPGyenapPVILQGHMDMVCEknADSEHDfeKDPIKLRIDGDWLKATGTtlgAD-NG-IGVAYALAil 119
|
90 100
....*....|....*....|....*....
gi 648533650 136 --PDMQRtklaKPIHFALSFDEEVGCVGA 162
Cdd:cd03890 120 edKDIEH----PPLEVLFTVDEETGMTGA 144
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
195-340 |
1.73e-04 |
|
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: 43.28 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 195 GINAYQCCVRGQAAHSSLTPKGL--NAIEYAARLICYIRDMADQFRAQGpfdelydvpfsTAQTSTITGG-NAINTVPAE 271
Cdd:cd03884 205 GQRWLEVTVTGEAGHAGTTPMALrrDALLAAAELILAVEEIALEHGDDL-----------VATVGRIEVKpNAVNVIPGE 273
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648533650 272 CQFQFEFRNL--PTLDP--EQIFARIDSYARETllpkmlrehsSAAIEITKIAAAPG--LDSSEQAAITQLVRAL 340
Cdd:cd03884 274 VEFTLDLRHPddAVLDAmvERIRAEAEAIAAER----------GVEVEVERLWDSPPvpFDPELVAALEAAAEAL 338
|
|
| PRK12893 |
PRK12893 |
Zn-dependent hydrolase; |
195-362 |
4.99e-04 |
|
Zn-dependent hydrolase;
Pssm-ID: 237250 [Multi-domain] Cd Length: 412 Bit Score: 42.18 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 195 GINAYQCCVRGQAAHSSLTPKGL--NAIEYAARLICYIRDMAdqfRAQGPfdelydvpfstaqTSTITGG------NAIN 266
Cdd:PRK12893 213 GIRWLEVTVEGQAAHAGTTPMAMrrDALVAAARIILAVERIA---AALAP-------------DGVATVGrlrvepNSRN 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 267 TVPAECQFQFEFRNLPTLDPEQIFARIDSYAREtllpkmLREHSSAAIEITKIAAAPGLDSSeqAAITQLVRALTadqdk 346
Cdd:PRK12893 277 VIPGKVVFTVDIRHPDDARLDAMEAALRAACAK------IAAARGVQVTVETVWDFPPVPFD--PALVALVEAAA----- 343
|
170
....*....|....*.
gi 648533650 347 RKVAYGTEAgLFSNAG 362
Cdd:PRK12893 344 EALGLSHMR-MVSGAG 358
|
|
| PRK13799 |
PRK13799 |
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional |
195-363 |
1.02e-03 |
|
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional
Pssm-ID: 106740 [Multi-domain] Cd Length: 591 Bit Score: 41.15 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 195 GINAYQCCVRGQAAHSSLTPKGL--NAIEYAARLICYIRDMADQfraqgpfDELYDVPFSTAQTSTITGgnAINTVPAEC 272
Cdd:PRK13799 391 GSARYICEFIGMASHAGTTPMDMrkDAAAAAAEIALYIEKRAAQ-------DQHASLVATMGQLNVPSG--STNVIPGRC 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 273 QFQFEFRNLPTLDPEQIFARIDSYARETLLPKMLREHSSAAIEITKIAAAPGLDSSEQAAITQL-VR----ALTADQDKR 347
Cdd:PRK13799 462 QFSLDIRAATDEIRDAAVADILAEIAAIAARRGIEYKAELAMKAAAAPCAPELMKQLEAATDAAgVPlfelASGAGHDAM 541
|
170 180
....*....|....*....|
gi 648533650 348 KVAYGTE-AGLFS---NAGI 363
Cdd:PRK13799 542 KIAEIMDqAMLFTrcgNAGI 561
|
|
| PRK12891 |
PRK12891 |
allantoate amidohydrolase; Reviewed |
144-340 |
3.31e-03 |
|
allantoate amidohydrolase; Reviewed
Pssm-ID: 237249 Cd Length: 414 Bit Score: 39.42 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 144 AKPIHFALSFDEEVGcvgaPLLIadlmkRGVKPDGCIVGeptsmrpiiaHKGINAYQCCVRGQAAHSSLTPKGL--NAIE 221
Cdd:PRK12891 181 GYPVHAAYELHIEQG----AILE-----RAGKTIGVVTA----------GQGQRWYEVTLTGVDAHAGTTPMAFrrDALV 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 222 YAARLICYIRDMADQFraqgpfdelydvpfstAQTSTITGG------NAINTVPAECQFQFEFRNlptLDPEqIFARIDS 295
Cdd:PRK12891 242 GAARMIAFLDALGRRD----------------APDARATVGmidarpNSRNTVPGECFFTVEFRH---PDDA-VLDRLDA 301
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 648533650 296 YARETLLPKMLREHSSAAIE-ITKIAAAPgLDSSEQAAITQLVRAL 340
Cdd:PRK12891 302 ALRAELARIADETGLRADIEqIFGYAPAP-FAPGCIDAVRDAARAL 346
|
|
| PRK15026 |
PRK15026 |
aminoacyl-histidine dipeptidase; Provisional |
69-162 |
8.78e-03 |
|
aminoacyl-histidine dipeptidase; Provisional
Pssm-ID: 184986 [Multi-domain] Cd Length: 485 Bit Score: 38.13 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648533650 69 ANLFATIPAHDG-ETNGGVVLSGHTDVVPVDG----QQWDSDPFKPEIRGDKLYGRGTC-DMKGFIGTALALVPDMQRTK 142
Cdd:PRK15026 53 GNILIRKPATAGmENRKPVVLQAHLDMVPQKNndtvHDFTKDPIQPYIDGEWVKARGTTlGADNGIGMASALAVLADENV 132
|
90 100
....*....|....*....|
gi 648533650 143 LAKPIHFALSFDEEVGCVGA 162
Cdd:PRK15026 133 VHGPLEVLLTMTEEAGMDGA 152
|
|
| |
