|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
2-374 |
0e+00 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 753.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 2 TCPVIELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFTIERMPFGDTNNFWAYRG-IGPTLAFAGHTDVVPAGDESQWEY 80
Cdd:PRK13009 1 MSDVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDFGDVKNLWARRGtEGPHLCFAGHTDVVPPGDLEAWTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 81 PPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKATHGTVKVVEALMSRNERLDYCLI 160
Cdd:PRK13009 81 PPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVLEWLKARGEKIDYCIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 161 GEPSSQHRLGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIHRVLPALQTLVNTHWDEGNEFFPATSMQIANIHAGT 240
Cdd:PRK13009 161 GEPTSTERLGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEGNEFFPPTSLQITNIDAGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 241 GSHNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNYTIEWILAGQPFLTAKGELVNAVIQSIDQYCGYQPELST 320
Cdd:PRK13009 241 GATNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDYTLEWTLSGEPFLTPPGKLVDAVVAAIEAVTGITPELST 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 499459479 321 SGGTSDGRFIAQMGAQVVELGPLNSTIHKVNESVSAADLQQLSRIYQRVMEQLI 374
Cdd:PRK13009 321 SGGTSDARFIADYGAQVVEFGPVNATIHKVNECVSVADLEKLTRIYERILERLL 374
|
|
| M20_DapE_proteobac |
cd03891 |
M20 Peptidase proteobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
6-370 |
0e+00 |
|
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: 680.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 6 IELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFTIERMPFGDTNNFWAYRG-IGPTLAFAGHTDVVPAGDESQWEYPPFE 84
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFGGVKNLWARRGtGGPHLCFAGHTDVVPPGDLEGWSSDPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 85 PTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKATHGTVKVVEALMSRNERLDYCLIGEPS 164
Cdd:cd03891 81 PTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKIDYCIVGEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 165 SQHRLGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIHRVLPALQTLVNTHWDEGNEFFPATSMQIANIHAGTGSHN 244
Cdd:cd03891 161 SEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLDEGNEFFPPSSLQITNIDVGNGATN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 245 VIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNYTIEWILAGQPFLTAKGELVNAVIQSIDQYCGYQPELSTSGGT 324
Cdd:cd03891 241 VIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELSTSGGT 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499459479 325 SDGRFIAQMGAQVVELGPLNSTIHKVNESVSAADLQQLSRIYQRVM 370
Cdd:cd03891 321 SDARFIASYGCPVVEFGLVNATIHKVNERVSVADLEKLTDIYERIL 366
|
|
| dapE_proteo |
TIGR01246 |
succinyl-diaminopimelate desuccinylase, proteobacterial clade; This model describes a ... |
5-373 |
0e+00 |
|
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: 606.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFTIERMPFGDTNNFWAYRGIG-PTLAFAGHTDVVPAGDESQWEYPPF 83
Cdd:TIGR01246 1 VTELAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGDTKNLWATRGTGePVLAFAGHTDVVPAGPEEQWSSPPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 84 EPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKATHGTVKVVEALMSRNERLDYCLIGEP 163
Cdd:TIGR01246 81 EPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVETLMARDELIDYCIVGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 164 SSQHRLGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIHRVLPALQTLVNTHWDEGNEFFPATSMQIANIHAGTGSH 243
Cdd:TIGR01246 161 SSVKKLGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAIKWDEGNEFFPPTSLQITNIHAGTGAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 244 NVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNYTIEWILAGQPFLTAKGELVNAVIQSIDQYCGYQPELSTSGG 323
Cdd:TIGR01246 241 NVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELSTGGG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 499459479 324 TSDGRFIAQMGAQVVELGPLNSTIHKVNESVSAADLQQLSRIYQRVMEQL 373
Cdd:TIGR01246 321 TSDGRFIALMGAEVVEFGPVNATIHKVNECVSIEDLEKLSDVYQDLLENL 370
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
5-373 |
1.78e-129 |
|
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: 376.53 E-value: 1.78e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFTIERMPF-GDTNNFWAYR---GIGPTLAFAGHTDVVPAGDESQWEY 80
Cdd:COG0624 14 ALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVpPGRPNLVARRpgdGGGPTLLLYGHLDVVPPGDLELWTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 81 PPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKAtHGTVKVVEALMsRNERLDYCLI 160
Cdd:COG0624 94 DPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGS-PGARALVEELA-EGLKADAAIV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 161 GEPSSqhrlGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIHRVLPALQTLVNTHWD-EGNEFFPATSMQIANIHAG 239
Cdd:COG0624 172 GEPTG----VPTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDgRADPLFGRTTLNVTGIEGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 240 TgSHNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNH--NLNYTIEWIL-AGQPFLTAK-GELVNAVIQSIDQYCGYQ 315
Cdd:COG0624 248 T-AVNVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAapGVEVEVEVLGdGRPPFETPPdSPLVAAARAAIREVTGKE 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 316 PELSTSGGTSDGRFIAQ-MGAQVVELGPLN-STIHKVNESVSAADLQQLSRIYQRVMEQL 373
Cdd:COG0624 327 PVLSGVGGGTDARFFAEaLGIPTVVFGPGDgAGAHAPDEYVELDDLEKGARVLARLLERL 386
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
7-369 |
1.52e-111 |
|
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: 330.03 E-value: 1.52e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 7 ELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFTIERMPFGDTNNFWAYRG--IGPTLAFAGHTDVVPAGDESQWEYPPFE 84
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVATVGggDGPVLLLNGHIDTVPPGDGDKWSFPPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 85 PTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKAThGTVKVVEALMSrnERLDYCLIGEPS 164
Cdd:cd08659 81 GRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGSD-GARALLEAGYA--DRLDALIVGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 165 sqhrlGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIHRVLPALQTLVNTHWDEG-NEFFPATSMQIANIHAGTGSh 243
Cdd:cd08659 158 -----GLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPaHPLLGPPTLNVGVINGGTQV- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 244 NVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNYTIEWILAGQP--FLTAKGELVNAVIQSIDQYCGyQPELSTS 321
Cdd:cd08659 232 NSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPpfFTDPDHPLVQALQAAARALGG-DPVVRPF 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 499459479 322 GGTSDGRFIAQM-GAQVVELGPLN-STIHKVNESVSAADLQQLSRIYQRV 369
Cdd:cd08659 311 TGTTDASYFAKDlGFPVVVYGPGDlALAHQPDEYVSLEDLLRAAEIYKEI 360
|
|
| Peptidase_M20 |
pfam01546 |
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
62-372 |
2.01e-86 |
|
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: 264.21 E-value: 2.01e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 62 AFAGHTDVVPAGDESQWeypPFEPTIrNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNhNGRLAFLITSDEEAkATHGT 141
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEEG-GMGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 142 VKVVEALMSRNERLDYCL---IGEPSS-QHRLGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIHRVLPALQTLVNT 217
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFglhIGEPTLlEGGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 218 HWDEGNEFFPA--TSMQIANIHAGTgshNVIPGNVQVQFNFRFSTELTDSQIREQVETILKN----HNLNYTIEWILAGQ 291
Cdd:pfam01546 155 VSRNVDPLDPAvvTVGNITGIPGGV---NVIPGEAELKGDIRLLPGEDLEELEERIREILEAiaaaYGVKVEVEYVEGGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 292 PFLTAKGELVNAVIQSIDQYCGYQPELSTSG--GTSDGRFIAQ-MGAQVVELGPLNSTIHKVNESVSAADLQQLSRIYQR 368
Cdd:pfam01546 232 PPLVNDSPLVAALREAAKELFGLKVELIVSGsmGGTDAAFFLLgVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLAR 311
|
....
gi 499459479 369 VMEQ 372
Cdd:pfam01546 312 LLLK 315
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
6-365 |
4.00e-58 |
|
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: 193.38 E-value: 4.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 6 IELAQQLIRQPSISP---DDKGCQDIMIAHLQTIGFTIERMPFGDTNNFWAYR--------GIGPTLAFAGHTDVVPAGD 74
Cdd:TIGR01910 1 VELLKDLISIPSVNPpggNEETIANYIKDLLREFGFSTDVIEITDDRLKVLGKvvvkepgnGNEKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 75 ESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAkathGTVKVVEALMSR-NE 153
Cdd:TIGR01910 81 LELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEES----GEAGTLYLLQRGyFK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 154 RLDYCLIGEPSSqhrlGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIH---RVLPALQTLVNtHWDEGNEFfpATS 230
Cdd:TIGR01910 157 DADGVLIPEPSG----GDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMklaKLITELNELEE-HIYARNSY--GFI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 231 MQIANIHAGT---GSH-NVIPGNVQVQFNFRFSTELTDSQIREQVETILK----NHNLNYTIEWILA--GQPFLTAKGEL 300
Cdd:TIGR01910 230 PGPITFNPGVikgGDWvNSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKalskSDGWLYENEPVVKwsGPNETPPDSRL 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499459479 301 VNAVIQSIDQYCGYQPELSTSGGTSDGRFIAQMGAQVVELGP-LNSTIHKVNESVSAADLQQLSRI 365
Cdd:TIGR01910 310 VKALEAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPgDLETAHQVNEYISIKNLVESTKV 375
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
7-371 |
2.63e-53 |
|
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: 180.48 E-value: 2.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 7 ELAQQLIRQPSISPDDKGCqdiMIAHLQ----TIGFTIERMPFGDTN--NFWAYRG--IGPTLAFAGHTDVVPAgDESQW 78
Cdd:cd03894 1 ELLARLVAFDTVSRNSNLA---LIEYVAdylaALGVKSRRVPVPEGGkaNLLATLGpgGEGGLLLSGHTDVVPV-DGQKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 79 EYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNgrLAFLITSDEEAKAThGTVKVVEALMSRNERLDYC 158
Cdd:cd03894 77 SSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKLRKP--LHLAFSYDEEVGCL-GVRHLIAALAARGGRPDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 159 LIGEPSSqhrlgdM-VKNGRRGSLTANLTVHGIQGHVAYPHLADNPIH---RVLPAL----QTLVNTHWDEGnefF--PA 228
Cdd:cd03894 154 IVGEPTS------LqPVVAHKGIASYRIRVRGRAAHSSLPPLGVNAIEaaaRLIGKLrelaDRLAPGLRDPP---FdpPY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 229 TSMQIANIHAGTgSHNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNY----TIEWILAGQPFLTAKGElvnAV 304
Cdd:cd03894 225 PTLNVGLIHGGN-AVNIVPAECEFEFEFRPLPGEDPEAIDARLRDYAEALLEFPeagiEVEPLFEVPGLETDEDA---PL 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 305 IQSIDQYCGYQPELSTSGGTsDGRFIAQMGAQVVELGPlnSTI---HKVNESVSAADLQQLSRIYQRVME 371
Cdd:cd03894 301 VRLAAALAGDNKVRTVAYGT-EAGLFQRAGIPTVVCGP--GSIaqaHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
5-374 |
1.68e-51 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 176.33 E-value: 1.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDDKGCQDI---MIAHLQTIGF--TIERMP--FGDTNNFWAYRGIG------PTLAFAGHTDVVP 71
Cdd:PRK08651 8 IVEFLKDLIKIPTVNPPGENYEEIaefLRDTLEELGFstEIIEVPneYVKKHDGPRPNLIArrgsgnPHLHFNGHYDVVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 72 AGDesQW-EYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAaerFVAAHPNHNGRLAFLITSDEEAKAThGTVKVVEALMS 150
Cdd:PRK08651 88 PGE--GWsVNVPFEPKVKDGKVYGRGASDMKGGIAALLAA---FERLDPAGDGNIELAIVPDEETGGT-GTGYLVEEGKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 151 rneRLDYCLIGEPSSQhrlgDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIH---RVLPALQTLVNTHWDEGNEFFP 227
Cdd:PRK08651 162 ---TPDYVIVGEPSGL----DNICIGHRGLVWGVVKVYGKQAHASTPWLGINAFEaaaKIAERLKSSLSTIKSKYEYDDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 228 ATSMQIANIHA----GTGSHNVIPGNVQVQFNFRFSTELTDSQ----IREQVETILKNHNLNYTIEWILAGQPFLTAKG- 298
Cdd:PRK08651 235 RGAKPTVTLGGptveGGTKTNIVPGYCAFSIDRRLIPEETAEEvrdeLEALLDEVAPELGIEVEFEITPFSEAFVTDPDs 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499459479 299 ELVNAVIQSIDQYCGYQPELSTSGGTSDGRFIAQMGAQVVELGPLN-STIHKVNESVSAADLQQLSRIYQRVMEQLI 374
Cdd:PRK08651 315 ELVKALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPGElELAHAPDEYVEVKDVEKAAKVYEEVLKRLA 391
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-370 |
1.22e-50 |
|
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: 172.96 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 6 IELAQQLIRQPSISPDDKGCQDIMIA---HLQTIGFTIERMPF-----GDTNNFWAYRGiGPTLAFAGHTDVVPAGDESQ 77
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDNTSAIAAYiklLLEDLGYPVELHEPpeeiyGVVSNIVGGRK-GKRLLFNGHYDVVPAGDGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 78 WEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKATHGTVKVVEALMSRNerlDY 157
Cdd:cd08011 80 WTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYLLEKVRIKP---ND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 158 CLIGEPSSQhrlgDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIHRVLPALQTLVNTHwdegneffpaTSMQIANIH 237
Cdd:cd08011 157 VLIGEPSGS----DNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELE----------KTVNPGVIK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 238 AGTgSHNVIPGNVQVQFNFRF----STELTDSQIREQVET-------ILKNHNLNYTiewilagqpflTAKGELVNAVIQ 306
Cdd:cd08011 223 GGV-KVNLVPDYCEFSVDIRLppgiSTDEVLSRIIDHLDSieevsfeIKSFYSPTVS-----------NPDSEIVKKTEE 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499459479 307 SIDQYCGYQPELSTSGGTSDGRFIAQMGAQVVELGPLN-STIHKVNESVSAADLQQLSRIYQRVM 370
Cdd:cd08011 291 AITEVLGIRPKEVISVGASDARFYRNAGIPAIVYGPGRlGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
44-375 |
4.97e-43 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 153.50 E-value: 4.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 44 PFGDTN-NFWAYRGIG-PTLAFAGHTDVVPAGDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNH 121
Cdd:PRK08588 43 KVNDGRaNLVAEIGSGsPVLALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQGQLL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 122 NGRLAFLITSDEE-----AKA--THGTVKVVEALmsrnerldycLIGEPSsqhrlGDMVKNGRRGSLTANLTVHGIQGHV 194
Cdd:PRK08588 123 NGTIRLLATAGEEvgelgAKQltEKGYADDLDAL----------IIGEPS-----GHGIVYAHKGSMDYKVTSTGKAAHS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 195 AYPHLADNPIHrvlpALQTLVNthwdEGNEFFpATSMQIANIhAGTGSHNV-----------IPGNVQVQFNFRFSTELT 263
Cdd:PRK08588 188 SMPELGVNAID----PLLEFYN----EQKEYF-DSIKKHNPY-LGGLTHVVtiinggeqvnsVPDEAELEFNIRTIPEYD 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 264 DSQIREQVETILKNHNLNY----TIEWILAGQPFLTAK-GELVNaVIQSI-DQYCGYQPELSTSGGTSDGRFIAQMGA-- 335
Cdd:PRK08588 258 NDQVISLLQEIINEVNQNGaaqlSLDIYSNHRPVASDKdSKLVQ-LAKDVaKSYVGQDIPLSAIPGATDASSFLKKKPdf 336
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 499459479 336 QVVELGP-LNSTIHKVNESVSAADLQQLSRIYQRVMEQLIQ 375
Cdd:PRK08588 337 PVIIFGPgNNLTAHQVDEYVEKDMYLKFIDIYKEIIIQYLK 377
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
5-375 |
5.91e-40 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 145.72 E-value: 5.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDDKGCqdiMIA----HLQTIGFTIERM--PFGDTNNFWAYrgIGPT----LAFAGHTDVVPAgD 74
Cdd:PRK07522 6 SLDILERLVAFDTVSRDSNLA---LIEwvrdYLAAHGVESELIpdPEGDKANLFAT--IGPAdrggIVLSGHTDVVPV-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 75 ESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAA---HPNHngrLAFliTSDEEAkathGTVKV---VEAL 148
Cdd:PRK07522 80 GQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAplrRPLH---LAF--SYDEEV----GCLGVpsmIARL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 149 MSRNERLDYCLIGEPSSqhrlgdM-VKNGRRGSLTANLTVHGIQGHVAYPHLADNPIH---RVLPALQTLVN--THWDEG 222
Cdd:PRK07522 151 PERGVKPAGCIVGEPTS------MrPVVGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEyaaRLIAHLRDLADrlAAPGPF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 223 NEFF--PATSMQIANIHAGTgSHNVIPGNVQVQFNFR----FSTELTDSQIREQVETIL----KNHNLNYTIEW-ILAGQ 291
Cdd:PRK07522 225 DALFdpPYSTLQTGTIQGGT-ALNIVPAECEFDFEFRnlpgDDPEAILARIRAYAEAELlpemRAVHPEAAIEFePLSAY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 292 PFLTAKGElvNAVIQSIDQYCGyQPELST-SGGTSDGRFiAQMGAQVVELGPlnSTI---HKVNESVSAADLQQLSRIYQ 367
Cdd:PRK07522 304 PGLDTAED--AAAARLVRALTG-DNDLRKvAYGTEAGLF-QRAGIPTVVCGP--GSIeqaHKPDEFVELAQLAACEAFLR 377
|
....*...
gi 499459479 368 RVMEQLIQ 375
Cdd:PRK07522 378 RLLASLAA 385
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-296 |
1.73e-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 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: 143.22 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFTIERMpfgdTNNFWAYRGIG----PTLAFAGHTDVVPAGdeSQWEY 80
Cdd:cd05651 2 AIELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRK----GNNVWAENGHFdegkPTLLLNSHHDTVKPN--AGWTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 81 PPFEPTIRNGMLYGRGAADMKGSLAAMIvAAERFVAAHPNHNGRLAFLITSDEEAKATHGtvkvVEALMSRNERLDYCLI 160
Cdd:cd05651 76 DPFEPVEKGGKLYGLGSNDAGASVVSLL-ATFLHLYSEGPLNYNLIYAASAEEEISGKNG----IESLLPHLPPLDLAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 161 GEPSSQHrlgdmVKNGRRGSLTANLTVHGIQGHVAYPHlADNPIHRVLPALQTLVNTHWDEGNEFFPATSMQIANIHAGT 240
Cdd:cd05651 151 GEPTEMQ-----PAIAEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDIQWLRDFRFDKVSPLLGPVKMTVTQINAGT 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 241 gSHNVIPGN----VQVQFNFRFSTELTDSQIREQVETILKNHNLNYTIEWILAGQPFLTA 296
Cdd:cd05651 225 -QHNVVPDSctfvVDIRTTEAYTNEEIFEIIRGNLKSEIKPRSFRLNSSAIPPDHPIVQA 283
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-292 |
6.10e-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 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: 141.64 E-value: 6.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFTIER--MPFGDTNNFWAYRG--IGPTLAFAGHTDVVPAgdesqweY 80
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKqpVENKDRFNVYAYPGssRQPRVLLTSHIDTVPP-------F 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 81 PPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAkathGTVKVVEALMSRNERLDYCLI 160
Cdd:cd05652 74 IPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEET----GGDGMKAFNDLGLNTWDAVIF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 161 GEPSSqhrlGDMVKnGRRGSLTANLTVHGIQGHVAYPHLADNPIHRVLPALQTLVNTHWdEGNEFFPATSMQIANIHAGT 240
Cdd:cd05652 150 GEPTE----LKLAS-GHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADL-PSSELLGPTTLNIGRISGGV 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 499459479 241 gSHNVIPGNVQVQFNFRFSTEltDSQIREQVETILKNHNLNY---TIEWILAGQP 292
Cdd:cd05652 224 -AANVVPAAAEASVAIRLAAG--PPEVKDIVKEAVAGILTDTediEVTFTSGYGP 275
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
5-374 |
3.29e-38 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 141.82 E-value: 3.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDDKG---CQDIMIAHLQTIGFTIERM-----PfGDTNNF--W------AYRGIGPTLAFAGHTD 68
Cdd:PRK13013 16 LVALTQDLIRIPTLNPPGRAyreICEFLAARLAPRGFEVELIraegaP-GDSETYprWnlvarrQGARDGDCVHFNSHHD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 69 VVPAGDesQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKATHGTVKVVEAL 148
Cdd:PRK13013 95 VVEVGH--GWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGGVAYLAEQG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 149 MSRNERLDYCLIGEPSSQHRlgdmVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIH-----------RVLPALQTLvNT 217
Cdd:PRK13013 173 RFSPDRVQHVIIPEPLNKDR----ICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRhmgavlaeieeRLFPLLATR-RT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 218 HWDEGNEFFPATSMQIANIHAG--------TG--SHNViPGNVQVQFNFRFSTELTDSQIREQVETILKN-----HNLNY 282
Cdd:PRK13013 248 AMPVVPEGARQSTLNINSIHGGepeqdpdyTGlpAPCV-ADRCRIVIDRRFLIEEDLDEVKAEITALLERlkrarPGFAY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 283 TIEWILAGQPFLTAKGE-LVNAVIQSIDQYCGYQPELSTSGGTSDGRFIAQMGA--QVVELGP-LNSTIHKVNESVSAAD 358
Cdd:PRK13013 327 EIRDLFEVLPTMTDRDApVVRSVAAAIERVLGRQADYVVSPGTYDQKHIDRIGKlkNCIAYGPgILDLAHQPDEWVGIAD 406
|
410
....*....|....*.
gi 499459479 359 LQQLSRIYQRVMEQLI 374
Cdd:PRK13013 407 MVDSAKVMALVLADLL 422
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
5-359 |
8.79e-38 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 140.08 E-value: 8.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFT-IERMPFGdtnNFWAYRGIGPTL-AFAGHTDVVPAGDESQWEYPP 82
Cdd:PRK13004 17 MTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFDkVEIDPMG---NVLGYIGHGKKLiAFDAHIDTVGIGDIKNWDFDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 83 FEPTIRNGMLYGRGAADMKGSLAAMIVAAERFvaAHPNHNGRLAFLITsdeeakathGTV--KVVEALMSR------NER 154
Cdd:PRK13004 94 FEGEEDDGRIYGRGTSDQKGGMASMVYAAKII--KDLGLDDEYTLYVT---------GTVqeEDCDGLCWRyiieedKIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 155 LDYCLIGEPSSqhrLGdmVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIH---RVLPALQTLVNTHWDegNEFFPATSM 231
Cdd:PRK13004 163 PDFVVITEPTD---LN--IYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYkmaPILNELEELNPNLKE--DPFLGKGTL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 232 QIANIHAGTGSHNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNYTIEWILAGQPFLTAKG------------- 298
Cdd:PRK13004 236 TVSDIFSTSPSRCAVPDSCAISIDRRLTVGETWESVLAEIRALPAVKKANAKVSMYNYDRPSYTGLVyptecyfptwlyp 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 299 ---ELVNAVIQSIDQYCGYQPEL-----STSGGTSDGRFiaqmGAQVVELGP-LNSTIHKVNESVSAADL 359
Cdd:PRK13004 316 edhEFVKAAVEAYKGLFGKAPEVdkwtfSTNGVSIAGRA----GIPTIGFGPgKEPLAHAPNEYTWKEQL 381
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
5-373 |
1.14e-36 |
|
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: 135.94 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFTIERmpfGDTNNFWAYRGIG-PTLAFAGHTDVVPAgdesqweypPF 83
Cdd:cd05653 3 AVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWV---DEAGNAVGGAGSGpPDVLLLGHIDTVPG---------EI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 84 EPTIRNGMLYGRGAADMKGSLAAMIVAAerfVAAHPNHNGRLAFLITSDEEAKAthgtvKVVEALMSRNERLDYCLIGEP 163
Cdd:cd05653 71 PVRVEGGVLYGRGAVDAKGPLAAMILAA---SALNEELGARVVVAGLVDEEGSS-----KGARELVRRGPRPDYIIIGEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 164 SSqhrlGDMVKNGRRGSLTANLTVHGIQGHVAYPhlADNPIHRVLPALQTLvnTHWDEGNE--FFPATSMQIaNIHAGTG 241
Cdd:cd05653 143 SG----WDGITLGYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLIKKWLEV--KKWAEGYNvgGRDFDSVVP-TLIKGGE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 242 SHNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNlnytIEWILAGQPFLTAKGE-LVNAVIQSIDQYcGYQPELST 320
Cdd:cd05653 214 SSNGLPQRAEATIDLRLPPRLSPEEAIALATALLPTCE----LEFIDDTEPVKVSKNNpLARAFRRAIRKQ-GGKPRLKR 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 499459479 321 SGGTSDGRFIAQ-MGAQVVELGPLNSTI-HKVNESVSAADLQQLSRIYQRVMEQL 373
Cdd:cd05653 289 KTGTSDMNVLAPlWTVPIVAYGPGDSTLdHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| AcOrn-deacetyl |
TIGR01892 |
acetylornithine deacetylase (ArgE); This model represents a clade of acetylornithine ... |
31-374 |
3.07e-35 |
|
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: 132.64 E-value: 3.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 31 AHLQTIGFTIERMPF-GDTNNFWAYRGIGPT----LAFAGHTDVVPAgDESQWEYPPFEPTIRNGMLYGRGAADMKGSLA 105
Cdd:TIGR01892 26 AYLEALGFSVEVQPFpDGAEKSNLVAVIGPSgaggLALSGHTDVVPY-DDAAWTRDPFRLTEKDGRLYGRGTCDMKGFLA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 106 AMIVAAERFVAAhpNHNGRLAFLITSDEEAKAThGTVKVVEALMSRNerlDYCLIGEPSsqhrlgDMVK-NGRRGSLTAN 184
Cdd:TIGR01892 105 CALAAAPDLAAE--QLKKPLHLALTADEEVGCT-GAPKMIEAGAGRP---RHAIIGEPT------RLIPvRAHKGYASAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 185 LTVHGIQGHVAYPHLADNPIHRVLPALQTLV----NTHWDEGNEFF--PATSMQIANIHAGTGShNVIPGNVQVQFNFRF 258
Cdd:TIGR01892 173 VTVRGRSGHSSYPDSGVNAIFRAGRFLQRLVhladTLLREDLDEGFtpPYTTLNIGVIQGGKAV-NIIPGACEFVFEWRP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 259 STELTDSQIREQVETI---LKNHNLNYTIEW-ILAGQPFLT--AKGELVNAViqsiDQYCGYQPElSTSGGTSDGrFIAQ 332
Cdd:TIGR01892 252 IPGMDPEELLQLLETIaqaLVRDEPGFEVQIeVVSTDPGVNtePDAELVAFL----EELSGNAPE-VVSYGTEAP-QFQE 325
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 499459479 333 MGAQVVELGPLN-STIHKVNESVSAADLQQLsriyQRVMEQLI 374
Cdd:TIGR01892 326 LGAEAVVCGPGDiRQAHQPDEYVEIEDLVRC----RAVLARLV 364
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-366 |
4.31e-33 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 127.42 E-value: 4.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 7 ELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFT----------IERMP-FGDTNnfWAYRG-------------IGPTLA 62
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTvdrweidvekLKHHPgFSPVA--VDYAGapnvvgthrprgeTGRSLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 63 FAGHTDVVPAGDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAkathGTV 142
Cdd:cd03895 79 LNGHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEEC----TGN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 143 KVVEALMsRNERLDYCLIGEPSsqhrlGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPI---HRVLPALQTLvNTHW 219
Cdd:cd03895 155 GALAALM-RGYRADAALIPEPT-----ELKLVRAQVGVIWFRVKVRGTPAHVAEASEGVNAIekaMHLIQALQEL-EREW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 220 DEGNEFFPATS-------MQIANIHAGTGSHNVIPgnvQVQFNFR------FSTELTDSQIREQVETILKNH----NLNY 282
Cdd:cd03895 228 NARKKSHPHFSdhphpinFNIGKIEGGDWPSSVPA---WCVLDCRigiypgESPEEARREIEECVADAAATDpwlsNHPP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 283 TIEWILAG-QPFLTAKGELVNAVIQSIDQYC-GYQPELSTSGGTSDGRFIAQMGA-QVVELGPLNSTIHKVNESVSAADL 359
Cdd:cd03895 305 EVEWNGFQaEGYVLEPGSDAEQVLAAAHQAVfGTPPVQSAMTATTDGRFFVLYGDiPALCYGPGSRDAHGFDESVDLESL 384
|
....*..
gi 499459479 360 QQLSRIY 366
Cdd:cd03895 385 RKITKTI 391
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
10-365 |
1.36e-32 |
|
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: 126.29 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 10 QQLIRQPSISPDDKGCQDIMIAH------LQTIGFTIERMPFGDTNNF-WAYRG---IGPTLAFAGHTDVVPAGDESQWE 79
Cdd:cd03893 5 AELVAIPSVSAQPDRREELRRAAewladlLRRLGFTVEIVDTSNGAPVvFAEFPgapGAPTVLLYGHYDVQPAGDEDGWD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 80 YPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAkATHGTVKVVEAlmsRNERL--DY 157
Cdd:cd03893 85 SDPFELTERDGRLYGRGAADDKGPILAHLAALRALMQQGGDLPVNVKFIIEGEEES-GSPSLDQLVEA---HRDLLaaDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 158 CLIGEPSSQHRLGDMVKNGRRGSLTANLTVHGIQGHV---AYPHLADNPIHRVLPALQTLVN------------------ 216
Cdd:cd03893 161 IVISDSTWVGQEQPTLTYGLRGNANFDVEVKGLDHDLhsgLYGGVVPDPMTALAQLLASLRDetgrilvpglydavrelp 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 217 -------THWDEGNEFFPATSMQIA---------NIHA------GTGSHNVIPGNVQVQFNFRFSTELTDSQIREQVETI 274
Cdd:cd03893 241 eeefrldAGVLEEVEIIGGTTGSVAerlwtrpalTVLGidggfpGEGSKTVIPPRARAKISIRLVPGQDPEEASRLLEAH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 275 LKNH---NLNYTIEWILAGQPFLT-AKGELVNAVIQSIDQYCGYQPELSTSGGT--SDGRFIAQMGAQVVELGPLNST-- 346
Cdd:cd03893 321 LEKHapsGAKVTVSYVEGGMPWRSdPSDPAYQAAKDALRTAYGVEPPLTREGGSipFISVLQEFPQAPVLLIGVGDPDdn 400
|
410
....*....|....*....
gi 499459479 347 IHKVNESVSAADLQQLSRI 365
Cdd:cd03893 401 AHSPNESLRLGNYKEGTQA 419
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
27-366 |
1.10e-31 |
|
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, Glutamate carboxypeptidase (carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; CPDG2; CPG2; Folate hydrolase G2; Pteroylmonoglutamic acid hydrolase G2; Glucarpidase; E.C. 3.4.17.11) subfamily. CPDG2 is a periplasmic enzyme that is synthesized with a signal peptide. It is a dimeric zinc-dependent exopeptidase, with two domains, a catalytic domain, which provides the ligands for the two zinc ions in the active site, and a dimerization domain. CPDG2 cleaves the C-terminal glutamate moiety from a wide range of N-acyl groups, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl, and pteroyl groups to release benzoic acid, phenol, and aniline mustards. It is used clinically to treat methotrexate toxicity by hydrolyzing it to inactive and non-toxic metabolites. It is also proposed for use in antibody-directed enzyme prodrug therapy; for example, glutamate can be cleaved from glutamated benzoyl nitrogen mustards, producing nitrogen mustards with effective cytotoxicity against tumor cells.
Pssm-ID: 349881 [Multi-domain] Cd Length: 362 Bit Score: 122.70 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 27 DIMIAHLQTIGFTIERMPFGDTNN--FWAYRG-IGPTLAFAGHTDVV-PAGDESQWeypPFepTIRNGMLYGRGAADMKG 102
Cdd:cd03885 26 ELLAEELEALGFTVERRPLGEFGDhlIATFKGtGGKRVLLIGHMDTVfPEGTLAFR---PF--TVDGDRAYGPGVADMKG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 103 SLAAMIVAAERFVAAHPNHNGRLAFLITSDEE-AKATHGTVKVVEALMSrnerlDYCLIGEPSsqhRLGDMVKNGRRGSL 181
Cdd:cd03885 101 GLVVILHALKALKAAGGRDYLPITVLLNSDEEiGSPGSRELIEEEAKGA-----DYVLVFEPA---RADGNLVTARKGIG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 182 TANLTVHGIQGHV-AYPHLADNPI----HRVLpALQTLVNthwdegneFFPATSMQIANIHAGTGShNVIPGNVQVQFNF 256
Cdd:cd03885 173 RFRLTVKGRAAHAgNAPEKGRSAIyelaHQVL-ALHALTD--------PEKGTTVNVGVISGGTRV-NVVPDHAEAQVDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 257 RFSTELTDSQIREQVETILKNH-----NLNYTIEwiLAGQPFL-TAKGELVNAVIQSIDQYCGYQPELSTSGGTSDGRFI 330
Cdd:cd03885 243 RFATAEEADRVEEALRAIVATTlvpgtSVELTGG--LNRPPMEeTPASRRLLARAQEIAAELGLTLDWEATGGGSDANFT 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 499459479 331 AQMGAQVVE-LGPLNSTIHKVNESvsaADLQQLS-RIY 366
Cdd:cd03885 321 AALGVPTLDgLGPVGGGAHTEDEY---LELDSLVpRIK 355
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
5-370 |
2.84e-31 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 122.26 E-value: 2.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPD-------DKGcqDIMIAHLQTIGFT-IERMPFGDTNNFWAYR--------GIGP--TLAFAGH 66
Cdd:PRK13983 7 MIELLSELIAIPAVNPDfggegekEKA--EYLESLLKEYGFDeVERYDAPDPRVIEGVRpnivakipGGDGkrTLWIISH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 67 TDVVPAGDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAH--PNHNGRLAFLitSDEEAKATHGT--- 141
Cdd:PRK13983 85 MDVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGirPKYNLGLAFV--SDEETGSKYGIqyl 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 142 VKVVEALMSRNErldycLIGEPSSQHRLGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPiHRV----LPALQTLVNT 217
Cdd:PRK13983 163 LKKHPELFKKDD-----LILVPDAGNPDGSFIEIAEKSILWLKFTVKGKQCHASTPENGINA-HRAaadfALELDEALHE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 218 HWDEGNEFF--PATSMQIANIHAGTGSHNVIPGNVQVQFNFRF--STELTD--SQIREQVETILKNHNLNYTIEWILAGQ 291
Cdd:PRK13983 237 KFNAKDPLFdpPYSTFEPTKKEANVDNINTIPGRDVFYFDCRVlpDYDLDEvlKDIKEIADEFEEEYGVKIEVEIVQREQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 292 --PFLTAKGELVNAVIQSIDQYCGYQPELSTSGGTSDGRFIAQMGAQVVELGPLNSTIHKVNESVSAADLQQLSRIYQRV 369
Cdd:PRK13983 317 apPPTPPDSEIVKKLKRAIKEVRGIEPKVGGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYAKISNLIEDAKVFALL 396
|
.
gi 499459479 370 M 370
Cdd:PRK13983 397 L 397
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
5-370 |
5.91e-30 |
|
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: 117.93 E-value: 5.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDDKGCQDIMIAHLQTIG-FTIERmpfgDTNNFWAYRGIGP--TLAFAGHTDVVPAGDEsqweyp 81
Cdd:cd05647 1 PIELTAALVDIPSVSGNEKPIADEIEAALRTLPhLEVIR----DGNTVVARTERGLasRVILAGHLDTVPVAGN------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 82 pFEPTIRN-GMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNgrLAFLITSDEE-AKATHGTVKVVEALmsrNERL--DY 157
Cdd:cd05647 71 -LPSRVEEdGVLYGCGATDMKAGDAVQLKLAATLAAATLKHD--LTLIFYDCEEvAAELNGLGRLAEEH---PEWLaaDF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 158 CLIGEPSsqhrlGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIHRVLPALQTLvnthwdegNEFFPAT-------- 229
Cdd:cd05647 145 AVLGEPT-----DGTIEGGCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARL--------AAYEPRTvnidglty 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 230 --SMQIANIHAGTGShNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNYTIEWILAGqpfltAKGELVNAVIQS 307
Cdd:cd05647 212 reGLNAVFISGGVAG-NVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEIEVTDLSPG-----ALPGLDHPVARD 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499459479 308 IDQYCGYQPElSTSGGTSDGRFiAQMGAQVVELGPLNSTI-HKVNESVSAADLQQLSRIYQRVM 370
Cdd:cd05647 286 LIEAVGGKVR-AKYGWTDVARF-SALGIPAVNFGPGDPLLaHKRDEQVPVEQITACAAILRRWL 347
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-271 |
1.60e-27 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 111.74 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 6 IELAQQLIRQPSISPDDKGCQDIMIAHLQTIGF-TIERMPFGdtnNFWAYRGIGPT-LAFAGHTDVVPAGDESQWEYPPF 83
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGFdEVEIDPMG---NVIGYIGGGKKkILFDGHIDTVGIGNIDNWKFDPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 84 EPTIRNGMLYGRGAADMKGSLAAMIVAAERFvaAH---PNHNGRLAFLITSDEEAKATHGTVKVVEAlmsRNERLDYCLI 160
Cdd:cd05649 78 EGYETDGKIYGRGTSDQKGGLASMVYAAKIM--KDlglRDFAYTILVAGTVQEEDCDGVCWQYISKA---DKIKPDFVVS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 161 GEPSsqhrlgDM-VKNGRRGSLTANLTVHGIQGHVAYPHLADNPIHRVLPALQTL--VNTHWDEgNEFFPATSMQIANIH 237
Cdd:cd05649 153 GEPT------DGnIYRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIrqLNPNFPE-APFLGRGTLTVTDIF 225
|
250 260 270
....*....|....*....|....*....|....
gi 499459479 238 AGTGSHNVIPGNVQVQFNFRfsteLTDSQIREQV 271
Cdd:cd05649 226 STSPSRCAVPDSCRISIDRR----LTVGETWEGC 255
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-370 |
3.26e-27 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are 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: 111.01 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPD-----DKGCQDIMIAHLQTIGF-TIERMPFGDTNNFW-------AYRGIGPTLAFAGHTDVVP 71
Cdd:cd05650 3 IIELERDLIRIPAVNPEsggegEKEKADYLEKKLREYGFyTLERYDAPDERGIIrpnivakIPGGNDKTLWIISHLDTVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 72 AGDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAH--PNHNGRLAFLitSDEEAKATHGTVKVVEA-- 147
Cdd:cd05650 83 PGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGitPKYNFGLLFV--ADEEDGSEYGIQYLLNKfd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 148 LMSRNErldycLIGEPSSQHRLGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPI---HRVLPALQTLVNTHWDEGNE 224
Cdd:cd05650 161 LFKKDD-----LIIVPDFGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFvaaSNFALELDELLHEKFDEKDD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 225 FF--PATSMQIANIHAGTGSHNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNY----TIEWILAGQ--PFLTA 296
Cdd:cd05650 236 LFnpPYSTFEPTKKEANVPNVNTIPGYDVFYFDCRVLPTYKLDEVLKFVNKIISDFENSYgagiTYEIVQKEQapPATPE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499459479 297 KGELVNAVIQSIDQYCGYQPELSTSGGTSDGRFIAQMGAQVVELGPLNSTIHKVNESVSAADLQQLSRIYQRVM 370
Cdd:cd05650 316 DSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYIRISHIVKDAKVFAEML 389
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
6-214 |
4.22e-27 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 111.25 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 6 IELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFT----------IERMP-FGDTNnfWAYRG-------------IGPTL 61
Cdd:PRK06837 23 VAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEvdrwsidpddLKSHPgAGPVE--IDYSGapnvvgtyrpagkTGRSL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 62 AFAGHTDVVPAGDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKAthgt 141
Cdd:PRK06837 101 ILQGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFALDALRAAGLAPAARVHFQSVIEEESTG---- 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499459479 142 vkvVEALMS--RNERLDYCLIGEPssqhrLGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPI---HRVLPALQTL 214
Cdd:PRK06837 177 ---NGALSTlqRGYRADACLIPEP-----TGEKLVRAQVGVIWFRLRVRGAPVHVREAGTGANAIdaaYHLIQALREL 246
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
58-375 |
4.53e-27 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 109.87 E-value: 4.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 58 GPTLAFAGHTDVVPAGdesqweyppFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFvaahpNHNG-RLAFLITSDEEak 136
Cdd:PRK00466 60 EGDILLASHVDTVPGY---------IEPKIEGEVIYGRGAVDAKGPLISMIIAAWLL-----NEKGiKVMVSGLADEE-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 137 athGTVKVVEALMSRNERLDYCLIGEPSSqhrlGDMVKNGRRGSLTANLTVHGIQGHVAYPhlADNPIHRVLPALQTLVn 216
Cdd:PRK00466 124 ---STSIGAKELVSKGFNFKHIIVGEPSN----GTDIVVEYRGSIQLDIMCEGTPEHSSSA--KSNLIVDISKKIIEVY- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 217 thwdEGNEFFPATSMQIANIHAGTgSHNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNyTIEWIlagQPFLTA 296
Cdd:PRK00466 194 ----KQPENYDKPSIVPTIIRAGE-SYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQECGLK-IVDET---PPVKVS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 297 -KGELVNAVIQSIDQYcGYQPELSTSGGTSDGRFIAQMGAQVVELGPLNSTI-HKVNESVSAADLQQLSRIYQRVMEQLI 374
Cdd:PRK00466 265 iNNPVVKALMRALLKQ-NIKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLeHTNQEKITLDEIYIAVKTYMLAIEELW 343
|
.
gi 499459479 375 Q 375
Cdd:PRK00466 344 Q 344
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
175-283 |
7.16e-27 |
|
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: 102.81 E-value: 7.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 175 NGRRGSLTANLTVHGIQGHVAYPHLADNPIHRVLPALQTLVNTHWDEGNeFFPATSMQIANIHAGTgSHNVIPGNVQVQF 254
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGF-DFPRTTLNITGIEGGT-ATNVIPAEAEAKF 78
|
90 100
....*....|....*....|....*....
gi 499459479 255 NFRFSTELTDSQIREQVETILKNHNLNYT 283
Cdd:pfam07687 79 DIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
10-373 |
1.28e-26 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 110.42 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 10 QQLIRQPSISPDDKGCQDI-----MIAHLQT----IGFTIERMPFGDTNNFWAYRGIGPTLA---FAGHTDVVPA--GDE 75
Cdd:PRK08262 51 SEAIRFRTISNRDRAEDDAaafdaLHAHLEEsypaVHAALEREVVGGHSLLYTWKGSDPSLKpivLMAHQDVVPVapGTE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 76 SQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAA--HPNHNGRLAFliTSDEEAkATHGTVKVVEALMSRNE 153
Cdd:PRK08262 131 GDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQgfQPRRTIYLAF--GHDEEV-GGLGARAIAELLKERGV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 154 RLDYCL-----IGE---PSSQHRLGdMVKNGRRGSLTANLTVHGIQGHVAYP--------------HLADNP-------- 203
Cdd:PRK08262 208 RLAFVLdeggaITEgvlPGVKKPVA-LIGVAEKGYATLELTARATGGHSSMPprqtaigrlaraltRLEDNPlpmrlrgp 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 204 ----IHRVLPAL-----QTLVNThWDEG---NEFFPATSMQIANIH--------AGTGSHNVIPGNVQVQFNFRFSTELT 263
Cdd:PRK08262 287 vaemFDTLAPEMsfaqrVVLANL-WLFEpllLRVLAKSPETAAMLRtttaptmlKGSPKDNVLPQRATATVNFRILPGDS 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 264 DSQIREQVETILKnhNLNYTIEWILAGQ------PFLTAKGELVNAVIQSIDQYCGYQPELSTSGgtSDGRFIAQMGAQV 337
Cdd:PRK08262 366 VESVLAHVRRAVA--DDRVEIEVLGGNSepspvsSTDSAAYKLLAATIREVFPDVVVAPYLVVGA--TDSRHYSGISDNV 441
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 499459479 338 VELGPLN------STIHKVNESVSAADLQQLSRIYQRVMEQL 373
Cdd:PRK08262 442 YRFSPLRlspedlARFHGTNERISVANYARMIRFYYRLIENA 483
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
6-374 |
8.63e-26 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 107.43 E-value: 8.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 6 IELAQQLIRQPSISP---DDKGCQDIMIAHLQTIGFTIER--MPFGDTNNFWAYRGIGPT----LAFAGHTDVVPAGDES 76
Cdd:PRK08596 16 LELLKTLVRFETPAPparNTNEAQEFIAEFLRKLGFSVDKwdVYPNDPNVVGVKKGTESDayksLIINGHMDVAEVSADE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 77 QWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAkATHGTVKVVEalmsRNERLD 156
Cdd:PRK08596 96 AWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEV-GEAGTLQCCE----RGYDAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 157 YCLIGEPSSQHRLgdmvknGRRGSLTANLTVHGIQGHvaypH--LADNPIH---------------RVLPALQTLvNTHW 219
Cdd:PRK08596 171 FAVVVDTSDLHMQ------GQGGVITGWITVKSPQTF----HdgTRRQMIHaggglfgasaiekmmKIIQSLQEL-ERHW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 220 D--EGNEFFPatsmqianihAGTGSHN--VIPGN-------------VQVQFnfrFSTELTDSQIREQVETI-------- 274
Cdd:PRK08596 240 AvmKSYPGFP----------PGTNTINpaVIEGGrhaafiadecrlwITVHF---YPNETYEQVIKEIEEYIgkvaaadp 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 275 -LKNHNLnyTIEWilAGQPFLTAKGEL------------VNAVIQSIDQYCGYQPELSTSGGTSDGRFIAQMGAQVVELG 341
Cdd:PRK08596 307 wLRENPP--QFKW--GGESMIEDRGEIfpsleidsehpaVKTLSSAHESVLSKNAILDMSTTVTDGGWFAEFGIPAVIYG 382
|
410 420 430
....*....|....*....|....*....|....
gi 499459479 342 PLNST-IHKVNESVSAADLQQlsriYQRVMEQLI 374
Cdd:PRK08596 383 PGTLEeAHSVNEKVEIEQLIE----YTKVITAFI 412
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
4-342 |
1.52e-25 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 106.06 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 4 PVIELAQQLIRQPSISPDD-------KGCQDIMIAHLQTIGFTIERMPFGDTN---NFWAYRGIGPT-LAFAGHTDVVPA 72
Cdd:PRK05111 6 SFIEMYRALIATPSISATDpaldqsnRAVIDLLAGWFEDLGFNVEIQPVPGTRgkfNLLASLGSGEGgLLLAGHTDTVPF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 73 gDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAA---HPnhngrLAFLITSDEE-----AK--ATHGTV 142
Cdd:PRK05111 86 -DEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLTklkKP-----LYILATADEEtsmagARafAEATAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 143 kvvealmsrneRLDYCLIGEPSSQHRLgdmvkNGRRGSLTANLTVHGIQGHVAYPHLADNPI---HRVLPALQTLVNtHW 219
Cdd:PRK05111 160 -----------RPDCAIIGEPTSLKPV-----RAHKGHMSEAIRITGQSGHSSDPALGVNAIelmHDVIGELLQLRD-EL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 220 DEG--NEFF--PATSMQIANIHAGTGShNVIPGNVQVQFNFR----FSTELTDSQIREQVETILKNHNLNYTIEWILAG- 290
Cdd:PRK05111 223 QERyhNPAFtvPYPTLNLGHIHGGDAP-NRICGCCELHFDIRplpgMTLEDLRGLLREALAPVSERWPGRITVAPLHPPi 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 499459479 291 QPFLTAKGelvNAVIQSIDQYCGYQPElSTSGGTsDGRFIAQMGAQVVELGP 342
Cdd:PRK05111 302 PGYECPAD---HQLVRVVEKLLGHKAE-VVNYCT-EAPFIQQLGCPTLVLGP 348
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
5-366 |
1.75e-25 |
|
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: 106.95 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDD-------KGCQDIMIAHLQ---TIGFTiermpFGDTNNFWAYRGIG---PTLAFAGHTDVVP 71
Cdd:cd03888 10 ILEDLKELVAIPSVRDEAtegapfgEGPRKALDKFLDlakRLGFK-----TKNIDNYAGYAEYGegeEVLGILGHLDVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 72 AGDesQWEYPPFEPTIRNGMLYGRGAADMKG-SLAA-------------------MIVAA---------ERFVAAHPNHN 122
Cdd:cd03888 85 AGE--GWTTDPFKPVIKDGKLYGRGTIDDKGpTIAAlyalkilkdlglplkkkirLIFGTdeetgwkciEHYFEHEEYPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 123 ----------------GRLAFLITSDEEAKATHGTVKV------------VEALMSRNERLDYCLIGEpssQHRLGDM-V 173
Cdd:cd03888 163 fgftpdaefpvingekGIVTVDLTFKIDDDKGYRLISIkggeatnmvpdkAEAVIPGKDKEELALSAA---TDLKGNIeI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 174 KNGrrgslTANLTVHGIQGHVAYPHLADNPIHRVLPALQTLvnthwDEGNEFFPATSMQIANIHAGT------------- 240
Cdd:cd03888 240 DDG-----GVELTVTGKSAHASAPEKGVNAITLLAKFLAEL-----NKDGNDKDFIKFLAKNLHEDYngkklginfedev 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 241 --------GSHNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNYTIEWILagQPFLTAK-GELVNAVIQSIDQY 311
Cdd:cd03888 310 mgeltlnpGIITLDDGKLELGLNVRYPVGTSAEDIIKQIEEALEKYGVEVEGHKHQ--KPLYVPKdSPLVKTLLKVYEEQ 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 499459479 312 CGYQPELSTSGGTSDGRFIAQMgaqvVELGPL----NSTIHKVNESVSAADLQQLSRIY 366
Cdd:cd03888 388 TGKEGEPVAIGGGTYARELPNG----VAFGPEfpgqKDTMHQANEFIPIDDLIKALAIY 442
|
|
| PRK06915 |
PRK06915 |
peptidase; |
6-193 |
4.55e-25 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 105.54 E-value: 4.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 6 IELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFTI------------------ERMPFGDTNNF---WAYRGIGPTLAFA 64
Cdd:PRK06915 20 VKLLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLdiwepsfkklkdhpyfvsPRTSFSDSPNIvatLKGSGGGKSMILN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 65 GHTDVVPAGDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKAThGTVKV 144
Cdd:PRK06915 100 GHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEESGGA-GTLAA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499459479 145 VEalmsRNERLDYCLIGEPSSQHRLgdmVKngRRGSLTANLTVHGIQGH 193
Cdd:PRK06915 179 IL----RGYKADGAIIPEPTNMKFF---PK--QQGSMWFRLHVKGKAAH 218
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
6-361 |
5.76e-25 |
|
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: 105.11 E-value: 5.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 6 IELAQQLIRQPSISPDDKG---CQDIMIAHLQTIGFTIERMPfGDTNNF-WAYRGIG--PTLAFAGHTDVVPAGDESQWE 79
Cdd:cd05681 2 LEDLRDLLKIPSVSAQGRGipeTADFLKEFLRRLGAEVEIFE-TDGNPIvYAEFNSGdaKTLLFYNHYDVQPAEPLELWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 80 YPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKATHgtvkvVEALMSRNERL---D 156
Cdd:cd05681 81 SDPFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPN-----LEKFVAEHADLlkaD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 157 YCLI--GEPSSQHRLgdMVKNGRRGSLTANLTVHGIQG--HVAYPHLADNPIHRVLPALQTLVnthwDEGNE-------- 224
Cdd:cd05681 156 GCIWegGGKNPKGRP--QISLGVKGIVYVELRVKTADFdlHSSYGAIVENPAWRLVQALNSLR----DEDGRvlipgfyd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 225 -------------------------------------------FFPATSMQIANIHAG---TGSHNVIPGNVQVQFNFRF 258
Cdd:cd05681 230 dvrplseaeralidtydfdpeelrktyglkrplqvegkdplraLFTEPTCNINGIYSGytgEGSKTILPSEAFAKLDFRL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 259 STELTD----SQIREQVEtilKNHNLNYTIEWILAGQPFLT-AKGELVNAVIQSIDQYCGYQPE-LSTSGGTSD-GRFIA 331
Cdd:cd05681 310 VPDQDPakilSLLRKHLD---KNGFDDIEIHDLLGEKPFRTdPDAPFVQAVIESAKEVYGQDPIvLPNSAGTGPmYPFYD 386
|
410 420 430
....*....|....*....|....*....|..
gi 499459479 332 QMGAQVVE--LGPLNSTIHKVNESVSAADLQQ 361
Cdd:cd05681 387 ALEVPVVAigVGNAGSNAHAPNENIRIADYYK 418
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
8-369 |
1.37e-24 |
|
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: 103.98 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 8 LAQQLIRQPSISPDDKGCQDI-----MIAHLQTIGFTI-----ERMPfGDTNNFWAYRGIGPT---LAFAGHTDVVPAgD 74
Cdd:cd05675 3 LLQELIRIDTTNSGDGTGSETraaevLAARLAEAGIQTeifvvESHP-GRANLVARIGGTDPSagpLLLLGHIDVVPA-D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 75 ESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKATHGTVKVVEALMSRNER 154
Cdd:cd05675 81 ASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDNHPELFDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 155 LDYClIGE------PSSQHRLGDMVKNGRRGSLTANLTVHGIQGHVAYPHlADNPIHRVLPALQTLVNTHW----DEGNE 224
Cdd:cd05675 161 ATFA-LNEggggslPVGKGRRLYPIQVAEKGIAWMKLTVRGRAGHGSRPT-DDNAITRLAEALRRLGAHNFpvrlTDETA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 225 FFP------------------------------------ATSMQIANIHAGTGSH--NVIPGNVQVQFNFRFSTELTDSQ 266
Cdd:cd05675 239 YFAqmaelaggeggalmltavpvldpalaklgpsapllnAMLRNTASPTMLDAGYatNVLPGRATAEVDCRILPGQSEEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 267 IREQVETILKNHNLnyTIEWILAGQPFLT-AKGELVNAVIQSIDQycgYQPELST----SGGTSDGRFIAQMGAQVVELG 341
Cdd:cd05675 319 VLDTLDKLLGDPDV--SVEAVHLEPATESpLDSPLVDAMEAAVQA---VDPGAPVvpymSPGGTDAKYFRRLGIPGYGFA 393
|
410 420 430
....*....|....*....|....*....|....*.
gi 499459479 342 PL--------NSTIHKVNESVSAADLQQLSRIYQRV 369
Cdd:cd05675 394 PLflppeldyTGLFHGVDERVPVESLYFGVRFLDRL 429
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
50-176 |
2.46e-24 |
|
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: 98.66 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 50 NFWAYRG---IGPTLAFAGHTDVVPAGDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLA 126
Cdd:cd18669 1 NVIARYGgggGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 499459479 127 FLITSDEEAKATHGTVKVVEALMSRNERLDYCLIGEPSSQHRLGDMVKNG 176
Cdd:cd18669 81 VAFTPDEEVGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTP 130
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
6-373 |
5.31e-23 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 98.29 E-value: 5.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 6 IELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFTIERMPFGDTNNFWAYRGigPTLAFAGHTDVVPagdesqweyPPFEP 85
Cdd:PRK08652 5 KELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIESDGEVINIVVNSK--AELFVEVHYDTVP---------VRAEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 86 TIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLitSDEEaKATHGTVKVVEALMSRnerldYCLIGEPSS 165
Cdd:PRK08652 74 FVDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFV--SDEE-EGGRGSALFAERYRPK-----MAIVLEPTD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 166 QHrlgdmVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIHRVLPALQTLVNTHWDEGNEFFPATSMQIAnihAGTGSHNV 245
Cdd:PRK08652 146 LK-----VAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPHIGIQEI---IGGSPEYS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 246 IPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNY--TIEWilagQPFLTAKGELVNAVIQSIDQYCGYQPELSTSGG 323
Cdd:PRK08652 218 IPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYeyTEIW----DGFELDEDEEIVQLLEKAMKEVGLEPEFTVMRS 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 499459479 324 TSDGRFIAQMGAQVVELGPLNSTI-HKVNESVSAADLQQLSRIYQRVMEQL 373
Cdd:PRK08652 294 WTDAINFRYNGTKTVVWGPGELDLcHTKFERIDVREVEKAKEFLKALNEIL 344
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
58-173 |
2.92e-21 |
|
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues).
Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 90.56 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 58 GPTLAFAGHTDVVPAGDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKA 137
Cdd:cd03873 12 GKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGS 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 499459479 138 THGTVKVVEALMSRNERLDYCLIGEPSSQHRLGDMV 173
Cdd:cd03873 92 GGGKGLLSKFLLAEDLKVDAAFVIDATAGPILQKGV 127
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
12-212 |
5.10e-21 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 93.91 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 12 LIRQPSIS--PDDKG----CQDIMIAHLQTIGF-TIERMP-------FGDtnnfWAYRGIGPTLAFAGHTDVVPAGDESQ 77
Cdd:cd05680 7 LLRIPSVSadPAHKGdvrrAAEWLADKLTEAGFeHTEVLPtgghplvYAE----WLGAPGAPTVLVYGHYDVQPPDPLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 78 WEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKATHgtvkvVEALMSRN-ERL- 155
Cdd:cd05680 83 WTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIGSPS-----LPAFLEENaERLa 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499459479 156 -DYCLIGEpSSQHRLGD-MVKNGRRGSLTANLTVHGI-----QGHvaYPHLADNPIH---RVLPALQ 212
Cdd:cd05680 158 aDVVLVSD-TSMWSPDTpTITYGLRGLAYLEISVTGPnrdlhSGS--YGGAVPNPANalaRLLASLH 221
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-372 |
1.25e-20 |
|
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. 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: 92.15 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDDKGCQ--------DIMIAHLQTIGFT---IERMPfGDTNNFWAYRGIG--PTLAFAGHTDVVP 71
Cdd:cd08013 3 PVSLTQTLVRINSSNPSLSATGgageaeiaTYVAAWLAHRGIEahrIEGTP-GRPSVVGVVRGTGggKSLMLNGHIDTVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 72 AgdeSQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPnhNGRLAFLITSDEEaKATHGTVKVVEAlmsr 151
Cdd:cd08013 82 L---DGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGL--RGDVILAAVADEE-DASLGTQEVLAA---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 152 NERLDYCLIGEPSSQhrlgdMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPI---HRVLPALQTLVNT-HWDEGNEFFP 227
Cdd:cd08013 152 GWRADAAIVTEPTNL-----QIIHAHKGFVWFEVDIHGRAAHGSRPDLGVDAIlkaGYFLVALEEYQQElPERPVDPLLG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 228 ATSMQIANIHAGTgSHNVIPGNVQVQFNFRFSTELTDSQIREQVETIL----KNH-NLNYTIEWILAGQPFLTAKGE--L 300
Cdd:cd08013 227 RASVHASLIKGGE-EPSSYPARCTLTIERRTIPGETDESVLAELTAILgelaQTVpNFSYREPRITLSRPPFEVPKEhpF 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499459479 301 VNAVIQSIDQYCGYQPELSTSGGTSDGRFIAQMGAQVVELGPLNSTIHKVNESVSAADLQQLSRIYQRVMEQ 372
Cdd:cd08013 306 VQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGAGLHAKEEWVDVESIRQLREVLSAVVRE 377
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
6-134 |
2.22e-20 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 92.06 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 6 IELAQQLIRQPS-ISPDDKGC---QDI------MIAHLQTIGFTIERMPFGdtnnFWAYRGIG---PTLAFAGHTDVVPA 72
Cdd:PRK07205 14 VAAIKTLVSYPSvLNEGENGTpfgQAIqdvleaTLDLCQGLGFKTYLDPKG----YYGYAEIGqgeELLAILCHLDVVPE 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499459479 73 GDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEE 134
Cdd:PRK07205 90 GDLSDWQTPPFEAVEKDGCLFGRGTQDDKGPSMAALYAVKALLDAGVQFNKRIRFIFGTDEE 151
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
5-374 |
2.96e-20 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 91.76 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDDKG------CQDIMIAHLQTIGFTIERMpfgDTNNFWAYRG-IG---PTLAFAGHTDVVPAGD 74
Cdd:PRK08554 3 VLELLSSLVSFETVNDPSKGikpskeCPKFIKDTLESWGIESELI---EKDGYYAVYGeIGegkPKLLFMAHFDVVPVNP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 75 EsQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFvaAHPNHNGRLAFLITSDEE---AKATHgtvkVVEALMSR 151
Cdd:PRK08554 80 E-EWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKEL--SKEPLNGKVIFAFTGDEEiggAMAMH----IAEKLREE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 152 NERLDYCLIGE-----PSSQHRLG-----------DMVKnGRRGSLTANLTVHGIQG-HVAY--------PHLADNPIHR 206
Cdd:PRK08554 153 GKLPKYMINADgigmkPIIRRRKGfgvtirvpsekVKVK-GKLREQTFEIRTPVVETrHAAYflpgvdthPLIAASHFLR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 207 VLPALQTLVNTHWDEGNeFFPAtSMQIANIHAGTGSH------------NVIP-------------GNVQVQFN-FRFST 260
Cdd:PRK08554 232 ESNVLAVSLEGKFLKGN-VVPG-EVTLTYLEPGEGEEvevdlgltrllkAIVPlvrapikaekysdYGVSITPNvYSFAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 261 E----LTD----SQIREQVETILKnHNLNYTI---EWIL-----AGQPFLTAKGELVNAVIQsIDQYCGYQPELSTSGGT 324
Cdd:PRK08554 310 GkhvlKLDiramSYSKEDIERTLK-EVLEFNLpeaEVEIrtnekAGYLFTPPDEEIVKVALR-VLKELGEDAEPVEGPGA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 499459479 325 SDGRFIAQMGAQVVELGPLNSTIHKVNESVSAADLQQLSRIYQRVMEQLI 374
Cdd:PRK08554 388 SDSRYFTPYGVKAIDFGPKGGNIHGPNEYVEIDSLKKMPEVYKRIALRLL 437
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
5-211 |
4.70e-19 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 87.98 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSI---SPDDKG---CQDIMIAHLQTIGFT---IERMPfGDTNNFWAYRGIGPT---LAFAGHTDVVPA 72
Cdd:PRK07906 1 VVDLCSELIRIDTTntgDGTGKGereAAEYVAEKLAEVGLEptyLESAP-GRANVVARLPGADPSrpaLLVHGHLDVVPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 73 gDESQWEYPPFEPTIRNGMLYGRGAADMKGsLAAMIVAAERFVAAH---PNHNGRLAFLitSDEEAKATHGTVKVVEalm 149
Cdd:PRK07906 80 -EAADWSVHPFSGEIRDGYVWGRGAVDMKD-MDAMMLAVVRHLARTgrrPPRDLVFAFV--ADEEAGGTYGAHWLVD--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499459479 150 SRNERLDYCL--IGEP-------SSQHRLGdMVKNGRRGSLTANLTVHGIQGHVAYPHlADNPIHRVLPAL 211
Cdd:PRK07906 153 NHPELFEGVTeaISEVggfsltvPGRDRLY-LIETAEKGLAWMRLTARGRAGHGSMVN-DDNAVTRLAEAV 221
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
55-371 |
5.96e-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: 88.08 E-value: 5.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 55 RGIGPTLA---FAGHTDVVPA--GDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAH--PNHNGRLAF 127
Cdd:cd05674 63 EGSDPSLKpllLMAHQDVVPVnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGfkPRRTIILAF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 128 liTSDEEAKATHGTVKVVEALM-SRNERLDYCLIGEPS---SQHRLGD---MVKNGRRGSLTANLTVHGIQGHVAYPH-- 198
Cdd:cd05674 143 --GHDEEVGGERGAGAIAELLLeRYGVDGLAAILDEGGavlEGVFLGVpfaLPGVAEKGYMDVEITVHTPGGHSSVPPkh 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 199 ------------LADNP----IHRVLPALQTL--VNTHWDEGNEFFPA-----------------------------TSM 231
Cdd:cd05674 221 tgigilseavaaLEANPfppkLTPGNPYYGMLqcLAEHSPLPPRSLKSnlwlaspllkallasellstspltrallrTTQ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 232 QIANIHAGTgSHNVIPGNVQVQFNFRF----STELTDSQIREQVETILKNHNLNYTIE-----WILAGQPFLTAKGELVN 302
Cdd:cd05674 301 AVDIINGGV-KINALPETATATVNHRIapgsSVEEVLEHVKNLIADIAVKYGLGLSAFggdviYSTNGTKLLTSLLSPEP 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 303 AVIQSI-------------DQYCGYQPELSTSGGTSDG---------------RFIA-QMGAQVVelgplnSTIHKVNES 353
Cdd:cd05674 380 SPVSSTsspvwqllagtirQVFEQFGEDLVVAPGIMTGntdtrhywnltkniyRFTPiRLNPEDL------GRIHGVNER 453
|
410
....*....|....*...
gi 499459479 354 VSAADLQQLSRIYQRVME 371
Cdd:cd05674 454 ISIDDYLETVAFYYQLIQ 471
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
1-373 |
2.37e-18 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 85.01 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 1 MTCPVIELAQQLIRQPSISPDDKGCQDIMIAHLQTIGFTIE-------RMPFGDtnnfwayrgIGPTLAFAGHTDVVPaG 73
Cdd:PRK04443 4 SALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREAWvdeagnaRGPAGD---------GPPLVLLLGHIDTVP-G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 74 DesqweyPPFEptIRNGMLYGRGAADMKGSLAAMIVAAERfvaAHPNHNGRLAFLITSDEEAKATHGTVKVVEalmsrNE 153
Cdd:PRK04443 74 D------IPVR--VEDGVLWGRGSVDAKGPLAAFAAAAAR---LEALVRARVSFVGAVEEEAPSSGGARLVAD-----RE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 154 RLDYCLIGEPSSQhrlgDMVKNGRRGSLTANLTVHGIQGHVAYPHLAdnpihrvlpALQTLVNtHWDEGNEFFPATsmqi 233
Cdd:PRK04443 138 RPDAVIIGEPSGW----DGITLGYKGRLLVTYVATSESFHSAGPEPN---------AAEDAIE-WWLAVEAWFEAN---- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 234 aniHAGTGSHNVIPGNVqVQFN-----FRFSTELtDSQIR-------EQVETILKNHNLNYTIEWILAGQPFLTAK-GEL 300
Cdd:PRK04443 200 ---DGRERVFDQVTPKL-VDFDsssdgLTVEAEM-TVGLRlppglspEEAREILDALLPTGTVTFTGAVPAYMVSKrTPL 274
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499459479 301 VNAVIQSIDQYcGYQPELSTSGGTSDGRFIAQM-GAQVVELGPLNSTI-HKVNESVSAADLQQLSRIYQRVMEQL 373
Cdd:PRK04443 275 ARAFRVAIREA-GGTPRLKRKTGTSDMNVVAPAwGCPMVAYGPGDSDLdHTPDEHLPLAEYLRAIAVLTDVLERL 348
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
4-373 |
3.77e-17 |
|
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: 82.15 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 4 PVIELAQQLIRQPSI--SPDDKGCQDIMIAHLQTIGFTIERMPFGDTNNF--WAYRGIGPTLA---FAGHTDVVPAGDEs 76
Cdd:TIGR01880 10 IAVTRFREYLRINTVqpNPDYAACVDFLIKQADELGLARKTIEFVPGKPVvvLTWPGSNPELPsilLNSHTDVVPVFRE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 77 QWEYPPFEPTI-RNGMLYGRGAADMKgSLAAMIVAAER--FVAAH-PNHNGRLAFLitSDEEAKATHGTVKVVEALMSRN 152
Cdd:TIGR01880 89 HWTHPPFSAFKdEDGNIYARGAQDMK-CVGVQYLEAVRnlKASGFkFKRTIHISFV--PDEEIGGHDGMEKFAKTDEFKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 153 ERLDYCL---IGEPSSQHRlgdmVKNGRRGSLTANLTVHGIQGHVA--YPHLADNPIHRVLPALQTLVNTHWD------- 220
Cdd:TIGR01880 166 LNLGFALdegLASPDDVYR----VFYAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRRFRESQFQllqsnpd 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 221 --EGNeffpATSMQIANIHAGTGShNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNYTIEWI-LAGQPFLTAK 297
Cdd:TIGR01880 242 laIGD----VTSVNLTKLKGGVQS-NVIPSEAEAGFDIRLAPSVDFEEMENRLDEWCADAGEGVTYEFSqHSGKPLVTPH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 298 -------GELVNAVIQsidQYCGYQPELSTsgGTSDGRFIAQMGAQVVELGPLNST---IHKVNESVSAADLQQLSRIYQ 367
Cdd:TIGR01880 317 ddsnpwwVAFKDAVKE---MGCTFKPEILP--GSTDSRYIRAAGVPALGFSPMNNTpvlLHDHNEFLNEAVFLRGIEIYQ 391
|
....*.
gi 499459479 368 RVMEQL 373
Cdd:TIGR01880 392 TLISAL 397
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
60-187 |
9.53e-17 |
|
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: 81.24 E-value: 9.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 60 TLAFAGHTDVVPAGDESQWEYPPFEPTIRNGMLYGRGAADMKG-SLAAMIVAAERFVAAHPNHNgrLAFLITSDEEAkAT 138
Cdd:cd05677 73 RILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGpLLAAIYAVAELFQEGELDND--VVFLIEGEEES-GS 149
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 499459479 139 HGTVKVVEALMSRNERLDYCLIgepSSQHRLGDMV---KNGRRGSLTANLTV 187
Cdd:cd05677 150 PGFKEVLRKNKELIGDIDWILL---SNSYWLDDNIpclNYGLRGVIHATIVV 198
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
27-214 |
1.46e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 80.82 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 27 DIMIAHLQTIGFT---IERM-PFGDTNNFWA-YRGIGPT--LAFAGHTDVVPAgDESQWEYPPFEPTIRNGMLYGRGAAD 99
Cdd:PRK09133 63 EAMAARLKAAGFAdadIEVTgPYPRKGNLVArLRGTDPKkpILLLAHMDVVEA-KREDWTRDPFKLVEENGYFYGRGTSD 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 100 MKgSLAAMIVAA------ERFVaahPNHNGRLAFliTSDEEAkathGTVKVVEALMSRNERL---DYCLiGEPSSqhrlG 170
Cdd:PRK09133 142 DK-ADAAIWVATlirlkrEGFK---PKRDIILAL--TGDEEG----TPMNGVAWLAENHRDLidaEFAL-NEGGG----G 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499459479 171 DMVKNGRRGSLTA----------NLTVHGIQGHVAYPhLADNPIHRVLPALQTL 214
Cdd:PRK09133 207 TLDEDGKPVLLTVqagektyadfRLEVTNPGGHSSRP-TKDNAIYRLAAALSRL 259
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
59-134 |
4.83e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 79.18 E-value: 4.83e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499459479 59 PTLAFAGHTDVVPAGDESQWEYPPFEPTIRNGMLYGRGAADMKGSLaAMIVAAERFVAAHPNHNgrLAFLITSDEE 134
Cdd:PRK07907 84 PTVLLYAHHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGI-AMHLAALRALGGDLPVG--VTVFVEGEEE 156
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
10-374 |
9.82e-16 |
|
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. These hypothetical proteins have been inferred by homology to be exopeptidases: carboxypeptidases, dipeptidases and a specialized aminopeptidase. In general, the peptidase hydrolyzes the late products of protein degradation in order to complete the conversion of proteins to free amino acids. Members of this subfamily may bind metal ions such as zinc.
Pssm-ID: 349869 [Multi-domain] Cd Length: 394 Bit Score: 77.98 E-value: 9.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 10 QQLIRQPSISPDDKGC--QDIMIAHLQTIGFTIERMPFGDTN----------NFWAYRGIGP---TLAFAGHTDVVPAGD 74
Cdd:cd02697 10 QKLVRVPTDTPPGNNAphAERTAALLQGFGFEAERHPVPEAEvraygmesitNLIVRRRYGDggrTVALNAHGDVVPPGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 75 esQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAKATHGTVKVVEALMSRNer 154
Cdd:cd02697 90 --GWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGELGPGWLLRQGLTKP-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 155 lDYCLIGEPSSQhrlgdmVKNGRRGSLTANLTVHGIQGHVAYPHLAdnpiHRVLPALQTLVNTHWDEGNEFFPATS---- 230
Cdd:cd02697 166 -DLLIAAGFSYE------VVTAHNGCLQMEVTVHGKQAHAAIPDTG----VDALQGAVAILNALYALNAQYRQVSSqveg 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 231 -----MQIANIHAGTGShNVIPGNVQVQFNFRFSTE----LTDSQIREQVETILKNH-NLNYTIEWILAGQPF--LTAKG 298
Cdd:cd02697 235 ithpyLNVGRIEGGTNT-NVVPGKVTFKLDRRMIPEenpvEVEAEIRRVIADAAASMpGISVDIRRLLLANSMrpLPGNA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 299 ELVNAVIQSIDQYCGyqpELSTSGGT---SDGRFIAQMGAQVVELGP-----LNSTIHKVNESVSAADLQQLSRIYQRVM 370
Cdd:cd02697 314 PLVEAIQTHGEAVFG---EPVPAMGTplyTDVRLYAEAGIPGVIYGAgprtvLESHAKRADERLQLEDLRRATKVIARSL 390
|
....
gi 499459479 371 EQLI 374
Cdd:cd02697 391 RDLL 394
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
10-257 |
3.19e-15 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 76.01 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 10 QQLI----RQPSISPDDKGCQDIMIAHLQtiGFTIERMPFGDTN-NFWAYRGIgPTLAFAGHTDVVPAGDesQWEYPPFE 84
Cdd:PRK08737 13 QALVsfdtRNPPRAITTGGIFDYLRAQLP--GFQVEVIDHGAGAvSLYAVRGT-PKYLFNVHLDTVPDSP--HWSADPHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 85 PTIRNGMLYGRGAADMKGSLAAMIVAAERfvaahpnHNGRLAFLITSDEEAkathGTVKVVEALMSRNERLDYCLIGEPS 164
Cdd:PRK08737 88 MRRTDDRVIGLGVCDIKGAAAALLAAANA-------GDGDAAFLFSSDEEA----NDPRCVAAFLARGIPYEAVLVAEPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 165 sqhrLGDMVKnGRRGSLTANLTVHGIQGHVAYPH-LADNPIH-------RVLPALQTLVNTHWdeGNefFPATSMQIANI 236
Cdd:PRK08737 157 ----MSEAVL-AHRGISSVLMRFAGRAGHASGKQdPSASALHqamrwggQALDHVESLAHARF--GG--LTGLRFNIGRV 227
|
250 260
....*....|....*....|.
gi 499459479 237 HAGTGShNVIPGNVQVQFNFR 257
Cdd:PRK08737 228 EGGIKA-NMIAPAAELRFGFR 247
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
63-363 |
3.23e-15 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 76.54 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 63 FAGHTDVV-PAGDesqweypPFE--PTIRNGMLYGRGAADMKGSLAAMIVAAERFvAAHPnHNGRLAF--LITSDEEAkA 137
Cdd:PRK07338 97 LTGHMDTVfPADH-------PFQtlSWLDDGTLNGPGVADMKGGIVVMLAALLAF-ERSP-LADKLGYdvLINPDEEI-G 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 138 THGTVKVVEALMSRNerlDYCLIGEPSSQHrlGDMVKNgRRGSLTANLTVHGIQGHVAY-PHLADNPI---HRVLPALQT 213
Cdd:PRK07338 167 SPASAPLLAELARGK---HAALTYEPALPD--GTLAGA-RKGSGNFTIVVTGRAAHAGRaFDEGRNAIvaaAELALALHA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 214 LvnthwdegNEFFPATSMQIANIHAGtGSHNVIPGNVQVQFNFRFSTE----LTDSQIREQVETILKNHnlNYTIEwiLA 289
Cdd:PRK07338 241 L--------NGQRDGVTVNVAKIDGG-GPLNVVPDNAVLRFNIRPPTPedaaWAEAELKKLIAQVNQRH--GVSLH--LH 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 290 GQ------PFLTAKGELVNAViQSIDQYCGYQPELSTSGGTSDGRFIAQMGAQVVE-LGPLNSTIHKVNESV---SAADL 359
Cdd:PRK07338 308 GGfgrppkPIDAAQQRLFEAV-QACGAALGLTIDWKDSGGVCDGNNLAAAGLPVVDtLGVRGGNIHSEDEFVildSLVER 386
|
....
gi 499459479 360 QQLS 363
Cdd:PRK07338 387 AQLS 390
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
5-134 |
1.42e-14 |
|
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely related to the characterized non-specific dipeptidase, PepV. Many enzymes in this clade have been given names including the terms "Xaa-His" and "carnosinase" due to the early mis-characterization of the Lactobacillus delbrueckii PepV enzyme. These names are likely too specific.
Pssm-ID: 273854 [Multi-domain] Cd Length: 447 Bit Score: 74.72 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 5 VIELAQQLIRQPSISPDDK---------GCQDIMIAHL---QTIGFTIErmpfgDTNNFWAYRGIGP---TLAFAGHTDV 69
Cdd:TIGR01887 4 ILEDLKELIAIDSVEDLEKakegapfgeGPRKALDKFLeiaKRDGFTTE-----NVDNYAGYIEYGQgeeVLGILGHLDV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499459479 70 VPAGDEsqWEYPPFEPTIRNGMLYGRGAADMKG----SLAAMIVAAERFVAAhpnhNGRLAFLITSDEE 134
Cdd:TIGR01887 79 VPAGDG--WTSPPFEPTIKDGRIYGRGTLDDKGptiaAYYAMKILKELGLKL----KKKIRFIFGTDEE 141
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
11-358 |
3.59e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 73.25 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 11 QLIRQPSISPDDKGCQD---IMIAHLQTIGF--TIERMP-----FGDTNNfwayrGIGPTLAFAGHTDVVPAGDESQWEY 80
Cdd:PRK06446 10 EFLKKPSISATGEGIEEtanYLKDTMEKLGIkaNIERTKghpvvYGEINV-----GAKKTLLIYNHYDVQPVDPLSEWKR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 81 PPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAH-PNHNgrLAFLITSDEEAkathGTVKVVEALMSRNERL--DY 157
Cdd:PRK06446 85 DPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKHkLNVN--VKFLYEGEEEI----GSPNLEDFIEKNKNKLkaDS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 158 cLIGEPSSQHRLG-DMVKNGRRGSLTANLTVHGIQG--HVAYPHLADNPIHRVLPALQTLV------------------- 215
Cdd:PRK06446 159 -VIMEGAGLDPKGrPQIVLGVKGLLYVELVLRTGTKdlHSSNAPIVRNPAWDLVKLLSTLVdgegrvlipgfyddvrelt 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 216 ----------------------------NTHWDEGNEFFPATSMQIANIHA---GTGSHNVIPGNVQVQFNFRFSTELTD 264
Cdd:PRK06446 238 eeerellkkydidveelrkalgfkelkySDREKIAEALLTEPTCNIDGFYSgytGKGSKTIVPSRAFAKLDFRLVPNQDP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 265 SQIREQVETILKNHNLNYTIEWILAGQPFLTA-KGELVNAVIQSIDQYCGYQPE-LSTSGGTSD-GRFIAQMG----AQV 337
Cdd:PRK06446 318 YKIFELLKKHLQKVGFNGEIIVHGFEYPVRTSvNSKVVKAMIESAKRVYGTEPVvIPNSAGTQPmGLFVYKLGirdiVSA 397
|
410 420
....*....|....*....|.
gi 499459479 338 VELGPLNSTIHKVNESVSAAD 358
Cdd:PRK06446 398 IGVGGYYSNAHAPNENIRIDD 418
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
11-365 |
9.93e-14 |
|
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: 71.71 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 11 QLIRQPSISPDDKGCQDIMIAHLQTIGFTI-----ERMPFGDTNNFWAY----RGIGPTLAFAGHTDVVPAGDESqweyP 81
Cdd:cd05683 11 ELVQIDSETLHEKEISKVLKKKFENLGLSVieddaGKTTGGGAGNLICTlkadKEEVPKILFTSHMDTVTPGINV----K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 82 PfePTIRNGMLYGRG----AADMKGSLAAmIVAAERFVAAHPNHNGRLAFLITSDEEAKathgtvkVVEALMSRNERLD- 156
Cdd:cd05683 87 P--PQIADGYIYSDGttilGADDKAGIAA-ILEAIRVIKEKNIPHGQIQFVITVGEESG-------LVGAKALDPELIDa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 157 ---YCLIGepssqhrlgdmvkNGRRGSLTA--------NLTVHGIQGHVAYphladNP---IHRVLPALQTLVNTHWDEG 222
Cdd:cd05683 157 dygYALDS-------------EGDVGTIIVgaptqdkiNAKIYGKTAHAGT-----SPekgISAINIAAKAISNMKLGRI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 223 NEFfpaTSMQIANIHAGTGShNVIPGNVQVQFNFR-FSTELTDSQIR---EQVETILKNHNLNYTIEWILAGQPFLTAKG 298
Cdd:cd05683 219 DEE---TTANIGKFQGGTAT-NIVTDEVNIEAEARsLDEEKLDAQVKhmkETFETTAKEKGAHAEVEVETSYPGFKINED 294
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499459479 299 ELVNAVIQSIDQYCGYQPELSTSGGTSDGRFIAQMGAQVVELGPLNSTIHKVNESVSAADLQQLSRI 365
Cdd:cd05683 295 EEVVKLAKRAANNLGLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAVL 361
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
58-218 |
2.62e-13 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 70.93 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 58 GPTLAFAGHTDVVPAGDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAhpnhNGRL----AFLITSDE 133
Cdd:PRK08201 79 KPTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKV----EGTLpvnvKFCIEGEE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 134 EAKATHgtvkVVEALMSRNERL--DYCLIGEPSSQHRLGDMVKNGRRGSLTANLTVHGIQGHV---AYPHLADNPIHRVL 208
Cdd:PRK08201 155 EIGSPN----LDSFVEEEKDKLaaDVVLISDTTLLGPGKPAICYGLRGLAALEIDVRGAKGDLhsgLYGGAVPNALHALV 230
|
170
....*....|
gi 499459479 209 PALQTLVNTH 218
Cdd:PRK08201 231 QLLASLHDEH 240
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
60-106 |
2.78e-13 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 70.64 E-value: 2.78e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 499459479 60 TLAFAGHTDVVPAGDesQWEYPPFEPTIRNGMLYGRGAADMKG-SLAA 106
Cdd:PRK07318 81 VLGILGHLDVVPAGD--GWDTDPYEPVIKDGKIYARGTSDDKGpTMAA 126
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
6-118 |
7.59e-13 |
|
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase M20 family, CNDP (cytosolic nonspecific dipeptidase) subfamily including anserinase (Xaa-methyl-His dipeptidase, EC 3.4.13.5), 'serum' carnosinase (beta-alanyl-L-histidine dipeptidase; EC 3.4.13.20), and some uncharacterized proteins. Two genes, CN1 and CN2, coding for proteins that degrade carnosine (beta-alanyl-L-histidine) and homocarnosine (gamma-aminobutyric acid-L-histidine), two naturally occurring dipeptides with potential neuroprotective and neurotransmitter functions, have been identified. CN1 encodes for serum carnosinase and has narrow substrate specificity for Xaa-His dipeptides, where Xaa can be beta-alanine (carnosine), N-methyl beta-alanine, alanine, glycine and gamma-aminobutyric acid (homocarnosine). CN2 corresponds to the cytosolic nonspecific dipeptidase (CNDP; EC 3.4.13.18) and is not limited to Xaa-His dipeptides. CNDP requires Mn(2+) for full activity and does not hydrolyze homocarnosine. Anserinase is a dipeptidase that mainly catalyzes the hydrolysis of N-alpha-acetylhistidine.
Pssm-ID: 349925 [Multi-domain] Cd Length: 467 Bit Score: 69.55 E-value: 7.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 6 IELAQQLIRQPSIS--PDDKG----CQDIMIAHLQTIGFTIERMPFGD-TNNFWAYRGIGP-------------TLAFAG 65
Cdd:cd05676 13 IERLREAVAIQSVSadPEKRPelirMMEWAAERLEKLGFKVELVDIGTqTLPDGEELPLPPvllgrlgsdpskkTVLIYG 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 499459479 66 HTDVVPAGDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAH 118
Cdd:cd05676 93 HLDVQPAKLEDGWDTDPFELTEKDGKLYGRGSTDDKGPVLGWLNAIEAYQKLG 145
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
11-135 |
5.86e-12 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 66.85 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 11 QLIRQPSISPD---DKGCQ---DIMIAHLQTIGFTIER-------MPFGDTNnfwAYRGIGPTLAFAGHTDVVPAGDESQ 77
Cdd:PRK09104 25 ALLRIPSISTDpayAADCRkaaDWLVADLASLGFEASVrdtpghpMVVAHHE---GPTGDAPHVLFYGHYDVQPVDPLDL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499459479 78 WEYPPFEPTIR---NG--MLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEA 135
Cdd:PRK09104 102 WESPPFEPRIKetpDGrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEES 164
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
58-373 |
7.34e-11 |
|
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: 63.25 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 58 GPTLAFAG-HTDVVPAgDESQWEYPPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAK 136
Cdd:cd08012 77 GKTVSFVGsHMDVVTA-NPETWEFDPFSLSIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVVAVFIANEENS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 137 ATHGTvkVVEALMSRNErLDYCLIG------EPSSQHRLGDMvkngrrGSLTANLTVHGIQGHVAYPHLADNPIHRVLPA 210
Cdd:cd08012 156 EIPGV--GVDALVKSGL-LDNLKSGplywvdSADSQPCIGTG------GMVTWKLTATGKLFHSGLPHKAINALELVMEA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 211 LQTL-------VNTHWDEGNEFFPATS-MQIANIHAGTGSHNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLN- 281
Cdd:cd08012 227 LAEIqkrfyidFPPHPKEEVYGFATPStMKPTQWSYPGGSINQIPGECTICGDCRLTPFYDVKEVREKLEEYVDDINANi 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 282 ----------------------YTIEWILAGQPFLTAKGELV--NAVIQSIDQYCGYQPELSTSGGTSDGRFIAQMGAQV 337
Cdd:cd08012 307 eelptrgpvskyvlpaeglrgrVSLEFDEAAASGVACNLDSPgfHALCKATSEVVGYVKPYAITGSLPLIRELQDEGFDV 386
|
330 340 350
....*....|....*....|....*....|....*..
gi 499459479 338 VELG-PLNSTIHKVNESVSAADLQQLSRIYQRVMEQL 373
Cdd:cd08012 387 QITGyGLMATYHAKNEYCLLSDFQNGFKVLARTIAQL 423
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
177-287 |
1.61e-10 |
|
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; Metal-dependent amidase/aminoacylase/carboxypeptidase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441082 [Multi-domain] Cd Length: 386 Bit Score: 62.06 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 177 RRGSLTAN-----LTVHGIQGHVAYPHLADNPIH---RVLPALQTLVNTHwdegnefFPATSMQ---IANIHAGTgSHNV 245
Cdd:COG1473 175 RPGPIMAAadsfeITIKGKGGHAAAPHLGIDPIVaaaQIVTALQTIVSRN-------VDPLDPAvvtVGIIHGGT-APNV 246
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 499459479 246 IPGNVQVQFNFR-FSTELTDsQIREQVETILKN----HNLNYTIEWI 287
Cdd:COG1473 247 IPDEAELEGTVRtFDPEVRE-LLEERIERIAEGiaaaYGATAEVEYL 292
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
59-373 |
2.35e-10 |
|
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; acylase I; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. Acylase I is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) and is considered as a potential target of antimicrobial agents. Porcine AcyI is also shown to deacetylate certain quorum-sensing N-acylhomoserine lactones, while the rat enzyme has been implicated in degradation of chemotactic peptides of commensal bacteria. Prokaryotic arginine synthesis usually involves the transfer of an acetyl group to glutamate by ornithine acetyltransferase in order to form ornithine. However, Escherichia coli acetylornithine deacetylase (acetylornithinase, ArgE) (EC 3.5.1.16) catalyzes the deacylation of N2-acetyl-L-ornithine to yield ornithine and acetate. Phylogenetic evidence suggests that the clustering of the arg genes in one continuous sequence pattern arose in an ancestor common to Enterobacteriaceae and Vibrionaceae, where ornithine acetyltransferase was lost and replaced by a deacylase. Elevated levels of serum aminoacylase-1 autoantibody have been seen in the disease progression of chronic hepatitis B (CHB), making ACY1 autoantibody a valuable serum biomarker for discriminating hepatitis B virus (HBV) related liver cirrhosis from CHB.
Pssm-ID: 349898 [Multi-domain] Cd Length: 391 Bit Score: 61.52 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 59 PTLAFAGHTDVVPAgDESQWEYPPFEPTI-RNGMLYGRGAADMKGSLAAMIVAAERFVAA--HPNHNGRLAFLitSDEEA 135
Cdd:cd05646 65 PSILLNSHTDVVPV-FEEKWTHDPFSAHKdEDGNIYARGAQDMKCVGIQYLEAIRRLKASgfKPKRTIHLSFV--PDEEI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 136 KATHGTVKVVEALMSRNERLDYCL---IGEPSSQHRlgdmVKNGRRGSLTANLTVHGIQGHVA--YPHLADNPIHRVLPA 210
Cdd:cd05646 142 GGHDGMEKFVKTEEFKKLNVGFALdegLASPTEEYR----VFYGERSPWWVVITAPGTPGHGSklLENTAGEKLRKVIES 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 211 LQTLVNTHWD--EGNEFFP---ATSMQIANIHAGTgSHNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNHNLNYTIE 285
Cdd:cd05646 218 IMEFRESQKQrlKSNPNLTlgdVTTVNLTMLKGGV-QMNVVPSEAEAGFDLRIPPTVDLEEFEKQIDEWCAEAGRGVTYE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 286 WILAGQPFLTAKGELVNAVIQSIDQYCG-----YQPELSTSGgtSDGRFIAQMGAQVVELGPLNST---IHKVNESVSAA 357
Cdd:cd05646 297 FEQKSPEKDPTSLDDSNPWWAAFKKAVKemglkLKPEIFPAA--TDSRYIRALGIPALGFSPMNNTpilLHDHNEFLNED 374
|
330
....*....|....*.
gi 499459479 358 DLQQLSRIYQRVMEQL 373
Cdd:cd05646 375 VFLRGIEIYEKIIPAL 390
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
33-286 |
2.44e-10 |
|
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of those sequences detected by pfam01546. Included within this group are hydrolases of hippurate (N-benzylglycine), indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. These hydrolases are of the carboxypeptidase-type, most likely utilizing a zinc ion in the active site. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273857 [Multi-domain] Cd Length: 363 Bit Score: 61.21 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 33 LQTIGFTIERmPFGDTNNFWA---YRGIGPTLAFAGHTDVVPAGDESQWEYPPFEPtirnGMLYGRGaadmKGSLAAMIV 109
Cdd:TIGR01891 29 LESLGIEVRR-GVGGATGVVAtigGGKPGPVVALRADMDALPIQEQTDLPYKSTNP----GVMHACG----HDLHTAILL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 110 AAERFVAAHPNH-NGRLAFLITSDEEAkaTHGTVKVVEA-LMSRnerLDYCLIGEPSSqhrlGDMVKNG--RRGSLTA-- 183
Cdd:TIGR01891 100 GTAKLLKKLADLlEGTVRLIFQPAEEG--GGGATKMIEDgVLDD---VDAILGLHPDP----SIPAGTVglRPGTIMAaa 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 184 ---NLTVHGIQGHVAYPHLADNPI---HRVLPALQTLVNTHWDegneffPATSM--QIANIHAGTGShNVIPGNVQVQFN 255
Cdd:TIGR01891 171 dkfEVTIHGKGAHAARPHLGRDALdaaAQLVVALQQIVSRNVD------PSRPAvvSVGIIEAGGAP-NVIPDKASMSGT 243
|
250 260 270
....*....|....*....|....*....|....*
gi 499459479 256 FRFSTELTDSQIREQVETILKN----HNLNYTIEW 286
Cdd:TIGR01891 244 VRSLDPEVRDQIIDRIERIVEGaaamYGAKVELNY 278
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
56-266 |
3.87e-10 |
|
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: 60.57 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 56 GIGPTLAFAGHTDVVPAGDEsqweypPFEPTIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEA 135
Cdd:cd03896 52 GGGPALLFSAHLDTVFPGDT------PATVRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 136 KAThgTVKVVEALMSRNERLDYCLIGEPSsqhrlGDMVKNGRRGSLTANLTVHGIQGHVAYPHLADNPIHrvlpALQTLV 215
Cdd:cd03896 126 LGD--LRGARYLLSAHGARLDYFVVAEGT-----DGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIV----AMAKLV 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 499459479 216 nthwdEGNEFFPATSMQIANIHAGTGSH----NVIPGNVQVQFNFRF--STELTDSQ 266
Cdd:cd03896 195 -----EALYEWAAPYVPKTTFAAIRGGGgtsvNRIANLCSMYLDIRSnpDAELADVQ 246
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
105-313 |
1.72e-09 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 58.77 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 105 AAMIVAAERFVAAHPNH-NGRLAFLITSDEEAkaTHGTVKVVEALMSRNERLDYCLigepsSQHrLGDMVKNG----RRG 179
Cdd:cd03886 94 TAMLLGAAKLLAERRDPlKGTVRFIFQPAEEG--PGGAKAMIEEGVLENPGVDAAF-----GLH-VWPGLPVGtvgvRSG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 180 SLTA-----NLTVHGIQGHVAYPHLADNPIH---RVLPALQTLVNthwDEGNEFFPATsMQIANIHAGTGShNVIPGNVQ 251
Cdd:cd03886 166 ALMAsadefEITVKGKGGHGASPHLGVDPIVaaaQIVLALQTVVS---RELDPLEPAV-VTVGKFHAGTAF-NVIPDTAV 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 252 VQFNFRfsTEltDSQIREQVETILKN--------HNLNYTIEWIlAGQPFLTAKGELVNAVIQSIDQYCG 313
Cdd:cd03886 241 LEGTIR--TF--DPEVREALEARIKRlaegiaaaYGATVELEYG-YGYPAVINDPELTELVREAAKELLG 305
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
105-276 |
1.83e-09 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349914 [Multi-domain] Cd Length: 399 Bit Score: 58.89 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 105 AAMIVAAERFVAAHPNHNGRLAFLITSDEE----AKAThgtvkVVEALMSRNERLDYCLigepsSQH----RLGDMV-KN 175
Cdd:cd05664 105 AALLGAARLLVEAKDAWSGTLIAVFQPAEEtgggAQAM-----VDDGLYDKIPKPDVVL-----AQHvmpgPAGTVGtRP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 176 GRRGSLTANL--TVHGIQGHVAYPHLADNPIhrVLPA-----LQTLVnthwdeGNEFFPATS--MQIANIHAGTGShNVI 246
Cdd:cd05664 175 GRFLSAADSLdiTIFGRGGHGSMPHLTIDPV--VMAAsivtrLQTIV------SREVDPQEFavVTVGSIQAGSAE-NII 245
|
170 180 190
....*....|....*....|....*....|
gi 499459479 247 PGNVQVQFNFRFSTELTDSQIREQVETILK 276
Cdd:cd05664 246 PDEAELKLNVRTFDPEVREKVLNAIKRIVR 275
|
|
| PepD2 |
COG2195 |
Di- or tripeptidase [Amino acid transport and metabolism]; |
59-373 |
4.54e-09 |
|
Di- or tripeptidase [Amino acid transport and metabolism];
Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 57.37 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 59 PTLAFAGHTDVVPagdesqwEYP--PFEPTIRNGMLYGRGA----ADMKGSLAAMIVAAERFVaaHPN--HnGRLAFLIT 130
Cdd:COG2195 61 PTIGLQAHMDTVP-------QFPgdGIKPQIDGGLITADGTttlgADDKAGVAAILAALEYLK--EPEipH-GPIEVLFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 131 SDEEAK---ATHGTVKVVEAlmsrnerlDYCLI--GEPssqhrLGDMVkNGRRGSLTANLTVHGIQGHvayPHLAD---- 201
Cdd:COG2195 131 PDEEIGlrgAKALDVSKLGA--------DFAYTldGGE-----EGELE-YECAGAADAKITIKGKGGH---SGDAKekmi 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 202 NPIHRVLPALQTLVNTHWDEgneffpATSMQIANIHAGTgSHNVIPGNVQVQFNFR-FSTELTDSQ---IREQVETILKN 277
Cdd:COG2195 194 NAIKLAARFLAALPLGRIPE------ETEGNEGFIHGGS-ATNAIPREAEAVYIIRdHDREKLEARkaeLEEAFEEENAK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 278 HNLNyTIEWILAGQ--PF-LTAKGELVNAVIQSIDQyCGYQPELSTSGGTSDGRFIAQMGAQVVELGPlnsTIHKV---N 351
Cdd:COG2195 267 YGVG-VVEVEIEDQypNWkPEPDSPIVDLAKEAYEE-LGIEPKIKPIRGGLDGGILSFKGLPTPNLGP---GGHNFhspD 341
|
330 340
....*....|....*....|..
gi 499459479 352 ESVSAADLQQLSRIYQRVMEQL 373
Cdd:COG2195 342 ERVSIESMEKAWELLVEILKLI 363
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
27-218 |
1.56e-07 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349928 [Multi-domain] Cd Length: 448 Bit Score: 52.89 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 27 DIMIAHLQTIGFTI--------ERMPFgdtnnFWAYR---GIGPTLAFAGHTDVVPaGDESQWE--YPPFEPTIRNGMLY 93
Cdd:cd05679 35 QEMRPRFERLGFTVhihdnpvaGRAPF-----LIAERiedPSLPTLLIYGHGDVVP-GYEGRWRdgRDPWTVTVWGERWY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 94 GRGAADMKGSLAAMIVAAERFVAAhpnHNGRLAF----LITSDEEAkathGTVKVVEALMSRNERLDYCLIgEPSSQHRL 169
Cdd:cd05679 109 GRGTADNKGQHSINMAALRQVLEA---RGGKLGFnvkfLIEMGEEM----GSPGLRAFCFSHREALKADLF-IASDGPRL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 499459479 170 G---DMVKNGRRGSLTANLTVHGIQG--HVA-YPHLADNPIHRVLPALQTLVNTH 218
Cdd:cd05679 181 AadrPTMFLGSRGGLNFELRVNLREGghHSGnWGGLLANPGIILANAIASLVDGK 235
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
177-286 |
1.62e-07 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 52.66 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 177 RRGSLTA-----NLTVHGIQGHVAYPHLADNPI---HRVLPALQTLVNTHWDEgnefFPATSMQIANIHAGTgSHNVIPG 248
Cdd:cd08021 173 RPGAIMAapdefDITIKGKGGHGSMPHETVDPIviaAQIVTALQTIVSRRVDP----LDPAVVTIGTFQGGT-SFNVIPD 247
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 499459479 249 NVQVQFNFRFSTELTDSQIREQVETILKN----HNLNYTIEW 286
Cdd:cd08021 248 TVELKGTVRTFDEEVREQVPKRIERIVKGiceaYGASYELEY 289
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
186-323 |
2.42e-07 |
|
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized subfamily of proteins predicted as putative amidohydrolases, including the amhX gene product from Bacillus subtilis. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349939 [Multi-domain] Cd Length: 365 Bit Score: 51.90 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 186 TVHGIQGHVAYPHLADNPIHRVLPALQTLVNTHWDEGNeffpATSMQIANIHAGTGSHNVIPGNVQVQFNFRFSTELTDS 265
Cdd:cd08018 173 TIKGKQAHGARPHLGINAIEAASAIVNAVNAIHLDPNI----PWSVKMTKLQAGGEATNIIPDKAKFALDLRAQSNEAME 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499459479 266 QIREQVETILKNHNLNY--TIEWI-LAGQPFLTAKGELVNAVIQSIDQYCGYQ---PELSTSGG 323
Cdd:cd08018 249 ELKEKVEHAIEAAAALYgaSIEITeKGGMPAAEYDEEAVELMEEAITEVLGEEklaGPCVTPGG 312
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
27-135 |
2.78e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 52.22 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 27 DIMIAHLQTIGFTIERMPfgdtnNFWAYRG---IG--------PTLAFAGHTDVVPaGDESQWEYP--PFEPTIRNGMLY 93
Cdd:PRK07079 48 DEIAPALAALGFTCRIVD-----NPVAGGGpflIAerieddalPTVLIYGHGDVVR-GYDEQWREGlsPWTLTEEGDRWY 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499459479 94 GRGAADMKG----SLAAM-IVAAERfvaahpnhNGRLAF----LITSDEEA 135
Cdd:PRK07079 122 GRGTADNKGqhtiNLAALeQVLAAR--------GGRLGFnvklLIEMGEEI 164
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
19-333 |
1.70e-06 |
|
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: 49.44 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 19 SPDDKGCQDIMIAHLQTIGFTIERMPFGdtNNFWAYRGI---GPTLAFAGHTDVVPAGdesqweyppfeptirngmlyGR 95
Cdd:cd03884 25 TDEDRAARDLFVEWMEEAGLSVRVDAVG--NLFGRLEGTdpdAPPVLTGSHLDTVPNG--------------------GR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 96 --GAAdmkGSLAAmIVAAERFVAAH--PNHNgrLAFLITSDEEA----------KATHGTVKVVEALMSRN--------- 152
Cdd:cd03884 83 ydGIL---GVLAG-LEALRALKEAGirPRRP--IEVVAFTNEEGsrfppsmlgsRAFAGTLDLEELLSLRDadgvslaea 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 153 -ERLDYcLIGEPSSQHRLGDMV--------------KNGRR-GSLTA-------NLTVHGIQGH-------------VAY 196
Cdd:cd03884 157 lKAIGY-DGDRPASARRPGDIKayvelhieqgpvleEEGLPiGVVTGiagqrwlEVTVTGEAGHagttpmalrrdalLAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 197 PHLADNpIHRVlpALQTLVNTHwdegneffpATsmqIANIHAGTGSHNVIPGNVQVQFNFRfSTELT-----DSQIREQV 271
Cdd:cd03884 236 AELILA-VEEI--ALEHGDDLV---------AT---VGRIEVKPNAVNVIPGEVEFTLDLR-HPDDAvldamVERIRAEA 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499459479 272 ETILKNHNLNYTIEWILAGQPFLTAKgELVNAVIQSIDQyCGYQPELSTSGGTSDGRFIAQM 333
Cdd:cd03884 300 EAIAAERGVEVEVERLWDSPPVPFDP-ELVAALEAAAEA-LGLSYRRMPSGAGHDAMFMARI 359
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
4-278 |
1.11e-05 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 46.93 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 4 PVIELAQQLIRQPSISPDDKGCQ---DIMIAHLQTIGFTIERMPfgdtnnfwAYRGIGPTL--AFAG----------HTD 68
Cdd:PRK06133 38 AYLDTLKELVSIESGSGDAEGLKqvaALLAERLKALGAKVERAP--------TPPSAGDMVvaTFKGtgkrrimliaHMD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 69 VV-PAGDESQweyPPFEptIRNGMLYGRGAADMKGSLAAMIVAAERFVAAHPNHNGRLAFLITSDEEAkATHGTVKVVEA 147
Cdd:PRK06133 110 TVyLPGMLAK---QPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEET-GSPGSRELIAE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 148 LMSRNerlDYCLIGEPSsqhRLGDMVKNGRRGSLTANLTVHGIQGHV-AYPHLADNPI----HRVL-------PALQTLV 215
Cdd:PRK06133 184 LAAQH---DVVFSCEPG---RAKDALTLATSGIATALLEVKGKASHAgAAPELGRNALyelaHQLLqlrdlgdPAKGTTL 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499459479 216 NthWdegneffpatsmqiANIHAGTgSHNVIPGNVQVQFNFRFSTELTDSQIREQVETILKNH 278
Cdd:PRK06133 258 N--W--------------TVAKAGT-NRNVIPASASAQADVRYLDPAEFDRLEADLQEKVKNK 303
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
31-203 |
1.61e-05 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 46.57 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 31 AHLQTIGFTIERMPFGDTNNFWAYRGIGP---TLAFAGHTDVVPAGDESQWEYPPFEPTIRNGM---------------- 91
Cdd:cd05654 41 ENPSHVWQLLPPDDLGRRNVTALVKGKKPskrTIILISHFDTVGIEDYGELKDIAFDPDELTKAfseyveeldeevredl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 92 -----LYGRGAADMKGSLAAMIVAAERFvAAHPNHNGRLAFLITSDEEAKAThGTVKVVEAL--MSRNERLDY--CLIGE 162
Cdd:cd05654 121 lsgewLFGRGTMDMKSGLAVHLALLEQA-SEDEDFDGNLLLMAVPDEEVNSR-GMRAAVPALleLKKKHDLEYklAINSE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499459479 163 PSSQHRLGDMVK---NGRRGSLTANLTVHGIQGHVAYPHLADNP 203
Cdd:cd05654 199 PIFPQYDGDQTRyiyTGSIGKILPGFLCYGKETHVGEPFAGINA 242
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
106-274 |
2.55e-05 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349916 [Multi-domain] Cd Length: 373 Bit Score: 45.98 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 106 AMIVAAERFVAAHPNHNGRLAFLITSDEE----AKAThgtvkVVEALMsrnERLD----YCL---IGEPSSQH--RLGDM 172
Cdd:cd05666 97 TMLLGAARYLAETRNFDGTVHFIFQPAEEggggAKAM-----IEDGLF---ERFPcdavYGLhnmPGLPAGKFavRPGPM 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 173 VKngrrGSLTANLTVHGIQGHVAYPHLADNPI----HRVLpALQTLVNTHWDegneffPATS--MQIANIHAGTgSHNVI 246
Cdd:cd05666 169 MA----SADTFEITIRGKGGHAAMPHLGVDPIvaaaQLVQ-ALQTIVSRNVD------PLDAavVSVTQIHAGD-AYNVI 236
|
170 180 190
....*....|....*....|....*....|..
gi 499459479 247 PGNVQVQFNFR-FSTE---LTDSQIREQVETI 274
Cdd:cd05666 237 PDTAELRGTVRaFDPEvrdLIEERIREIADGI 268
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
177-322 |
3.25e-05 |
|
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349919 [Multi-domain] Cd Length: 371 Bit Score: 45.36 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 177 RRGSLTAN-----LTVHGIQGHVAYPHLADNPI---HRVLPALQTLVNthwdegNEFFPATS--MQIANIHAGTgSHNVI 246
Cdd:cd05669 164 KSGALMAAvdrfeIEIAGKGAHAAKPENGVDPIvaaSQIINALQTIVS------RNISPLESavVSVTRIHAGN-TWNVI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 247 PGNVQVQFNFR-FSTELTDsQIREQVETILKN--HNLNYTIE--WIlAGQPFLTAKGELVNAVIQsIDQYCGYQ---PEL 318
Cdd:cd05669 237 PDSAELEGTVRtFDAEVRQ-LVKERFEQIVEGiaAAFGAKIEfkWH-SGPPAVINDEELTDLASE-VAAQAGYEvvhAEP 313
|
....
gi 499459479 319 STSG 322
Cdd:cd05669 314 SLGG 317
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
7-164 |
4.89e-05 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 45.23 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 7 ELAQQLIRQPSISPDD--KGCQDIMIAHLQTI-GFT----------IERMPFGdTNNFWA-YRGIGP---TLAFAGHTDV 69
Cdd:COG4187 12 ELLCELVSIPSVTGTEgeKEVAEFIYEKLSELpYFQenpehlglhpLPDDPLG-RKNVTAlVKGKGEskkTVILISHFDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 70 VPAGDESQWEYPPFEP-----TIRNGML--------------YGRGAADMKGSLAAMIVAAERFvAAHPNHNGRLAFLIT 130
Cdd:COG4187 91 VDVEDYGSLKPLAFDPeelteALKEIKLpedvrkdlesgewlFGRGTMDMKAGLALHLALLEEA-SENEEFPGNLLLLAV 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 499459479 131 SDEEAKaTHGTVKVVEAL--MSRNERLDY--CLIGEPS 164
Cdd:COG4187 170 PDEEVN-SAGMRAAVPLLaeLKEKYGLEYklAINSEPS 206
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
58-187 |
5.43e-05 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 45.02 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 58 GPTLAFAGHTDVVPagDESQWE--YPPFEPTIRNGMLYGRGAAD----MKGSLAAmIVAAERFVAAHPnhngRLAFLITS 131
Cdd:cd05682 73 DDTVLLYGHMDKQP--PFTGWDegLGPTKPVIRGDKLYGRGGADdgyaIFASLTA-IKALQEQGIPHP----RCVVLIEA 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 499459479 132 DEEAKATHgTVKVVEALMSRNERLDY--CLIGEPSSQHRLgdMVKNGRRGSLTANLTV 187
Cdd:cd05682 146 CEESGSAD-LPFYLDKLKERIGNVDLvvCLDSGCGNYEQL--WLTTSLRGVLGGDLTV 200
|
|
| PRK07473 |
PRK07473 |
M20/M25/M40 family metallo-hydrolase; |
33-193 |
1.01e-04 |
|
M20/M25/M40 family metallo-hydrolase;
Pssm-ID: 168961 [Multi-domain] Cd Length: 376 Bit Score: 44.01 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 33 LQTIGFTIERMP----FGDT--NNFWAYRGIGPTLAFAGHTDVV-PAGDESQWeypPFEptIRNGMLYGRGAADMKG--- 102
Cdd:PRK07473 44 MAIMGATIERIPgrqgFGDCvrARFPHPRQGEPGILIAGHMDTVhPVGTLEKL---PWR--REGNKCYGPGILDMKGgny 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 103 -SLAAMI-VAAERFVAAHPnhngrLAFLITSDEEAkATHGTVKVVEALMSRNErldYCLIGEPSsqhRLGDMVKNGRRGS 180
Cdd:PRK07473 119 lALEAIRqLARAGITTPLP-----ITVLFTPDEEV-GTPSTRDLIEAEAARNK---YVLVPEPG---RPDNGVVTGRYAI 186
|
170
....*....|...
gi 499459479 181 LTANLTVHGIQGH 193
Cdd:PRK07473 187 ARFNLEATGRPSH 199
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
177-276 |
5.09e-04 |
|
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; Peptidase M20 family, aminoacyclase-1 YkuR-like subfamily including YkuR and Ama/HipO/HyuC proteins, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349920 [Multi-domain] Cd Length: 367 Bit Score: 41.86 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 177 RRGSLTAN-----LTVHGIQGHVAYPHLADNPIhrVLPA-----LQTLVNTHWDEGNeffpATSMQIANIHAGTgSHNVI 246
Cdd:cd05670 164 RSGTLFAGtselhIDFIGKSGHAAYPHNANDMV--VAAAnfvtqLQTIVSRNVDPID----GAVVTIGKIHAGT-ARNVI 236
|
90 100 110
....*....|....*....|....*....|
gi 499459479 247 PGNVQVQFNFRFSTELTDSQIREQVETILK 276
Cdd:cd05670 237 AGTAHLEGTIRTLTQEMMELVKQRVRDIAE 266
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
35-207 |
1.31e-03 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 40.55 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 35 TIGFTIERMPFGDTNNFWAYRGIGP---TLAFAGHTDVVPAgDESQW-EYPPFEPTIR---------------------- 88
Cdd:cd05678 34 KRGFKTSQLPTSGLPLLLAEKPISDarkTVLFYMHLDGQPV-DPSKWdQKSPYTPVLKrkdaagnweeinwdaifsnldp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 89 NGMLYGRGAADMKGSLaAMIVAAERFVAAhpnHNGRLAF---LITSDEEAKATHGTVKVVEAlmsRNERL--DYCLIGEP 163
Cdd:cd05678 113 EWRVFARAAADDKGPI-MMMLAALDALKA---GGIAPKFnvkIILDSEEEKGSPSLPKAVKE---YKELLaaDALIIMDG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499459479 164 SSQHRLGDMVKNGRRGSLTANLTVHGIQ-----GHvaYPHLADNPIHRV 207
Cdd:cd05678 186 PAHATNKPTLTFGCRGIATATLTTYGAKvpqhsGH--YGNYAPNPAFRL 232
|
|
| M20_IAA_Hyd |
cd08017 |
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant ... |
55-293 |
2.39e-03 |
|
M20 Peptidase Indole-3-acetic acid amino acid hydrolase; Peptidase M20 family, plant aminoacyclase-1 indole-3-acetic-L-aspartic acid hydrolase (IAA-Asp hydrolase; IAAspH; IAAH; IAA amidohydrolase; EC 3.5.1.-) subfamily. IAAspH hydrolyzes indole-3-acetyl-N-aspartic acid (IAA or auxin) to indole-3-acetic acid. Genes encoding IAA-amidohydrolases were first cloned from Arabidopsis; ILR1, IAR3, ILL1 and ILL2 encode active IAA- amino acid hydrolases, and three additional amidohydrolase-like genes (ILL3, ILL5, ILL6) have been isolated. In higher plants, the growth regulator indole-3-acetic acid (IAA or auxin) is found both free and conjugated via amide bonding to a variety of amino acids and peptides, and via an ester linkage to carbohydrates. IAA-Asp conjugates are involved in homeostatic control, protection, storing and subsequent use of free IAA. IAA-Asp is also found in some plants as a unique intermediate for entering into IAA non-decarboxylative oxidative pathway. IAA amidohydrolase cleaves the amide bond between the auxin and the conjugated amino acid. Enterobacter agglomerans IAAspH has very strong enzyme activity and substrate specificity towards IAA-Asp, although its substrate affinity is weaker compared to Arabidopsis enzymes of the ILR1 gene family. Enhanced IAA-hydrolase activity has been observed during clubroot disease in Chinese cabbage.
Pssm-ID: 349938 [Multi-domain] Cd Length: 376 Bit Score: 39.61 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 55 RGIGPTLAFAGHTDVVPAGDESQWEYPPFEPtirngmlyGRGAADMKGSLAAMIVAAERFVAAHPNH-NGRLAFLITSDE 133
Cdd:cd08017 51 SGSPPVVALRADMDALPIQELVEWEHKSKVD--------GKMHACGHDAHVAMLLGAAKLLKARKHLlKGTVRLLFQPAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 134 EAKA------THGTVKVVEALMSRnerldYCLIGEPSSqhrlgdmVKNGRRGSLTA-----NLTVHGIQGHVAYPHLADN 202
Cdd:cd08017 123 EGGAgakemiKEGALDDVEAIFGM-----HVSPALPTG-------TIASRPGPFLAgagrfEVVIRGKGGHAAMPHHTVD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 203 PI---HRVLPALQTLVNTHWDegneffPATS--MQIANIHAGTGShNVIPGNVQVQFNFR-FSTElTDSQIREQVETILK 276
Cdd:cd08017 191 PVvaaSSAVLALQQLVSRETD------PLDSqvVSVTRFNGGHAF-NVIPDSVTFGGTLRaLTTE-GFYRLRQRIEEVIE 262
|
250 260
....*....|....*....|.
gi 499459479 277 N----HNLNYTIEWILAGQPF 293
Cdd:cd08017 263 GqaavHRCNATVDFSEDERPP 283
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
186-285 |
3.49e-03 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 39.24 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499459479 186 TVHGIQGHVAYPHLADNPI---HRVLPALQTLVNTHWDEGNeffPATsMQIANIHAGTgSHNVIPGNVQVQFNFRFSTEL 262
Cdd:cd08019 174 EVKGKGGHGSMPHQGIDAVlaaASIVMNLQSIVSREIDPLE---PVV-VTVGKLNSGT-RFNVIADEAKIEGTLRTFNPE 248
|
90 100
....*....|....*....|...
gi 499459479 263 TDSQIREQVETILKNHNLNYTIE 285
Cdd:cd08019 249 TREKTPEIIERIAKHTAASYGAE 271
|
|
| PRK06156 |
PRK06156 |
dipeptidase; |
66-110 |
7.25e-03 |
|
dipeptidase;
Pssm-ID: 235720 [Multi-domain] Cd Length: 520 Bit Score: 38.41 E-value: 7.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 499459479 66 HTDVVPAgDESQWEYP-----PFEPTIRNGMLYGRGAADMKGSLAAMIVA 110
Cdd:PRK06156 117 HADVVPA-NPELWVLDgtrldPFKVTLVGDRLYGRGTEDDKGAIVTALYA 165
|
|
| |
