|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13009 |
PRK13009 |
succinyl-diaminopimelate desuccinylase; Reviewed |
2-375 |
0e+00 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 237265 [Multi-domain] Cd Length: 375 Bit Score: 761.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 2 SCPVIELTQQLIRRPSLSPDDAGCQALMIERLRAIGFTVERMDFGDTQNFWAWRG-QGETLAFAGHTDVVPAGDADRWIN 80
Cdd:PRK13009 1 MSDVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDFGDVKNLWARRGtEGPHLCFAGHTDVVPPGDLEAWTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAHNGTVKVVEALMARNERLDYCLV 160
Cdd:PRK13009 81 PPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVLEWLKARGEKIDYCIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 161 GEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWDKGNEFFPPTSMQIANVKAGT 240
Cdd:PRK13009 161 GEPTSTERLGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEGNEFFPPTSLQITNIDAGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 241 GSNNVIPGDFFVQFNFRFSTELTDETIKARVVALLEKYNLRYTVDWWLSGQPFLTQRGKLVDAVVNAIEHYNEIKPQLLT 320
Cdd:PRK13009 241 GATNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDYTLEWTLSGEPFLTPPGKLVDAVVAAIEAVTGITPELST 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1330962843 321 TGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQLVA 375
Cdd:PRK13009 321 SGGTSDARFIADYGAQVVEFGPVNATIHKVNECVSVADLEKLTRIYERILERLLA 375
|
|
| 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: 685.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 6 IELTQQLIRRPSLSPDDAGCQALMIERLRAIGFTVERMDFGDTQNFWAWRGQ-GETLAFAGHTDVVPAGDADRWINPPFE 84
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFGGVKNLWARRGTgGPHLCFAGHTDVVPPGDLEGWSSDPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAHNGTVKVVEALMARNERLDYCLVGEPS 164
Cdd:cd03891 81 PTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKIDYCIVGEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 165 STEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWDKGNEFFPPTSMQIANVKAGTGSNN 244
Cdd:cd03891 161 SEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLDEGNEFFPPSSLQITNIDVGNGATN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 245 VIPGDFFVQFNFRFSTELTDETIKARVVALLEKYNLRYTVDWWLSGQPFLTQRGKLVDAVVNAIEHYNEIKPQLLTTGGT 324
Cdd:cd03891 241 VIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELSTSGGT 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1330962843 325 SDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIM 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: 623.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPSLSPDDAGCQALMIERLRAIGFTVERMDFGDTQNFWAWRGQGE-TLAFAGHTDVVPAGDADRWINPPF 83
Cdd:TIGR01246 1 VTELAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGDTKNLWATRGTGEpVLAFAGHTDVVPAGPEEQWSSPPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 84 EPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAHNGTVKVVEALMARNERLDYCLVGEP 163
Cdd:TIGR01246 81 EPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVETLMARDELIDYCIVGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 164 SSTEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWDKGNEFFPPTSMQIANVKAGTGSN 243
Cdd:TIGR01246 161 SSVKKLGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAIKWDEGNEFFPPTSLQITNIHAGTGAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 244 NVIPGDFFVQFNFRFSTELTDETIKARVVALLEKYNLRYTVDWWLSGQPFLTQRGKLVDAVVNAIEHYNEIKPQLLTTGG 323
Cdd:TIGR01246 241 NVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELSTGGG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1330962843 324 TSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQL 373
Cdd:TIGR01246 321 TSDGRFIALMGAEVVEFGPVNATIHKVNECVSIEDLEKLSDVYQDLLENL 370
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
5-375 |
7.88e-125 |
|
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: 364.59 E-value: 7.88e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPSLSPDDAGCQALMIERLRAIGFTVERMDF-GDTQNFWAWR---GQGETLAFAGHTDVVPAGDADRWIN 80
Cdd:COG0624 14 ALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVpPGRPNLVARRpgdGGGPTLLLYGHLDVVPPGDLELWTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAhNGTVKVVEALmARNERLDYCLV 160
Cdd:COG0624 94 DPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGS-PGARALVEEL-AEGLKADAAIV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 161 GEPSSTevvgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWD-KGNEFFPPTSMQIANVKAG 239
Cdd:COG0624 172 GEPTGV----PTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDgRADPLFGRTTLNVTGIEGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 240 TGSnNVIPGDFFVQFNFRFSTELTDETIKARVVALLEK--YNLRYTVDWWL-SGQPFLT-QRGKLVDAVVNAIEHYNEIK 315
Cdd:COG0624 248 TAV-NVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAaaPGVEVEVEVLGdGRPPFETpPDSPLVAAARAAIREVTGKE 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330962843 316 PQLLTTGGTSDGRFIAR-MGAQVVELGPVN-ATIHKINECVNAADLQLLARMYQRIMEQLVA 375
Cdd:COG0624 327 PVLSGVGGGTDARFFAEaLGIPTVVFGPGDgAGAHAPDEYVELDDLEKGARVLARLLERLAG 388
|
|
| M20_ArgE_DapE-like |
cd08659 |
Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) ... |
7-369 |
5.23e-112 |
|
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: 331.19 E-value: 5.23e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 7 ELTQQLIRRPSLSPDDAGCQALMIERLRAIGFTVERMDFGDTQNFWAWRGQGE--TLAFAGHTDVVPAGDADRWINPPFE 84
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVATVGGGDgpVLLLNGHIDTVPPGDGDKWSFPPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAhNGTVKVVEALMArnERLDYCLVGEPS 164
Cdd:cd08659 81 GRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVGS-DGARALLEAGYA--DRLDALIVGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 165 stevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWDKG-NEFFPPTSMQIANVKAGTGSn 243
Cdd:cd08659 158 -----GLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPaHPLLGPPTLNVGVINGGTQV- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 244 NVIPGDFFVQFNFRFSTELTDETIKARVVALLEKYNLRYTVDWWLSGQP--FLTQRGKLVDAVVNAIEHYNeIKPQLLTT 321
Cdd:cd08659 232 NSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPpfFTDPDHPLVQALQAAARALG-GDPVVRPF 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1330962843 322 GGTSDGRFIARM-GAQVVELGP-VNATIHKINECVNAADLQLLARMYQRI 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 |
5.78e-85 |
|
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: 260.36 E-value: 5.78e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 62 AFAGHTDVVPAGDADRWinpPFEPTIrDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNhKNRLAFLITSDEEaSAHNGT 141
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEE-GGMGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 142 VKVVEALMARNERLDYCL---VGEPSSTE-VVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGI 217
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFglhIGEPTLLEgGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 218 EWDKGNEFFPP--TSMQIANVKAGTgsnNVIPGDFFVQFNFRFSTELTDETIKARVVALLEK----YNLRYTVDWWLSGQ 291
Cdd:pfam01546 155 VSRNVDPLDPAvvTVGNITGIPGGV---NVIPGEAELKGDIRLLPGEDLEELEERIREILEAiaaaYGVKVEVEYVEGGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 292 PFLTQRGKLVDAVVNAIEHYNEIKPQLLTTG--GTSDGRFIA-RMGAQVVELGPVNATIHKINECVNAADLQLLARMYQR 368
Cdd:pfam01546 232 PPLVNDSPLVAALREAAKELFGLKVELIVSGsmGGTDAAFFLlGVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLAR 311
|
....
gi 1330962843 369 IMEQ 372
Cdd:pfam01546 312 LLLK 315
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
6-352 |
5.72e-54 |
|
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: 182.21 E-value: 5.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 6 IELTQQLIRRPSLSP---DDAGCQALMIERLRAIGFTVERMDFGDTQNFWAWR--------GQGETLAFAGHTDVVPAGD 74
Cdd:TIGR01910 1 VELLKDLISIPSVNPpggNEETIANYIKDLLREFGFSTDVIEITDDRLKVLGKvvvkepgnGNEKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 75 ADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEaSAHNGTVKVVEALMARNEr 154
Cdd:TIGR01910 81 LELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEE-SGEAGTLYLLQRGYFKDA- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 155 lDYCLVGEPSStevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNEL--VGIEWDKGNE--FFP-PT 229
Cdd:TIGR01910 159 -DGVLIPEPSG----GDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELneLEEHIYARNSygFIPgPI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 230 SMQIANVKAGTGSnNVIPGDFFVQFNFRFSTELTDETIKARVVALLEKY------NLRYTVDWWLSGQPFLTQRGKLVDA 303
Cdd:TIGR01910 234 TFNPGVIKGGDWV-NSVPDYCEFSIDVRIIPEENLDEVKQIIEDVVKALsksdgwLYENEPVVKWSGPNETPPDSRLVKA 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1330962843 304 VVNAIEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGP-VNATIHKINE 352
Cdd:TIGR01910 313 LEAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPgDLETAHQVNE 362
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
7-371 |
1.69e-52 |
|
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16) subfamily. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349889 [Multi-domain] Cd Length: 367 Bit Score: 178.17 E-value: 1.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 7 ELTQQLIRRPSLSPddAGCQALmIE----RLRAIGFTVERMDFGDTQ--NFWAWRGQG--ETLAFAGHTDVVPAgDADRW 78
Cdd:cd03894 1 ELLARLVAFDTVSR--NSNLAL-IEyvadYLAALGVKSRRVPVPEGGkaNLLATLGPGgeGGLLLSGHTDVVPV-DGQKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 79 INPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQhPNHKNrLAFLITSDEEASaHNGTVKVVEALMARNERLDYC 158
Cdd:cd03894 77 SSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAA-KLRKP-LHLAFSYDEEVG-CLGVRHLIAALAARGGRPDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 159 LVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGI--EWDKGNE---FFPPTS-MQ 232
Cdd:cd03894 154 IVGEPTSLQPV-----VAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRELadRLAPGLRdppFDPPYPtLN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 233 IANVKAGTGSnNVIPGDFFVQFNFRF----STELTDETIKARVVALLEKYNLRYTVDWWLSGQPFLTQRGklvDAVVNAI 308
Cdd:cd03894 229 VGLIHGGNAV-NIVPAECEFEFEFRPlpgeDPEAIDARLRDYAEALLEFPEAGIEVEPLFEVPGLETDED---APLVRLA 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330962843 309 EHYNEIKPQLLTTGGTsDGRFIARMGAQVVELGPVN-ATIHKINECVNAADLQLLARMYQRIME 371
Cdd:cd03894 305 AALAGDNKVRTVAYGT-EAGLFQRAGIPTVVCGPGSiAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
5-375 |
2.13e-50 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 173.64 E-value: 2.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPSLSP---DDAGCQALMIERLRAIGFTVERMDFGDT---------QNFWAWRGQGET-LAFAGHTDVVP 71
Cdd:PRK08651 8 IVEFLKDLIKIPTVNPpgeNYEEIAEFLRDTLEELGFSTEIIEVPNEyvkkhdgprPNLIARRGSGNPhLHFNGHYDVVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 72 AGDADRwINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFvaqHPNHKNRLAFLITSDEEaSAHNGTVKVVEALMAr 151
Cdd:PRK08651 88 PGEGWS-VNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERL---DPAGDGNIELAIVPDEE-TGGTGTGYLVEEGKV- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 152 neRLDYCLVGEPSSTEVVGdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWDK--GNEFFPPT 229
Cdd:PRK08651 162 --TPDYVIVGEPSGLDNIC----IGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIksKYEYDDER 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 230 SMQI------ANVKAGTgSNNVIPGDFFVQFNFRFSTELTDETIKARVVALLE----KYNLRYTVDWWLSGQPFLTQRG- 298
Cdd:PRK08651 236 GAKPtvtlggPTVEGGT-KTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDevapELGIEVEFEITPFSEAFVTDPDs 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330962843 299 KLVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGP-VNATIHKINECVNAADLQLLARMYQRIMEQLVA 375
Cdd:PRK08651 315 ELVKALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPgELELAHAPDEYVEVKDVEKAAKVYEEVLKRLAK 392
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-370 |
1.16e-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. 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: 144.07 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 6 IELTQQLIRRPSLSPDDAG---CQALMIERLRAIGFTVERMDF-----GDTQNFWAWRGqGETLAFAGHTDVVPAGDADR 77
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDNtsaIAAYIKLLLEDLGYPVELHEPpeeiyGVVSNIVGGRK-GKRLLFNGHYDVVPAGDGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 78 WINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAHNGTVKVVEALMARNerlDY 157
Cdd:cd08011 80 WTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYLLEKVRIKP---ND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 158 CLVGEPSSTevvgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEwdkgneffppTSMQIANVK 237
Cdd:cd08011 157 VLIGEPSGS----DNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELE----------KTVNPGVIK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 238 AGTgSNNVIPGDFFVQFNFRF----STELTDETIKaRVVALLEKYNLRytVDWWLSGqPFLTQRGKLVDAVVNAIEHYNE 313
Cdd:cd08011 223 GGV-KVNLVPDYCEFSVDIRLppgiSTDEVLSRII-DHLDSIEEVSFE--IKSFYSP-TVSNPDSEIVKKTEEAITEVLG 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1330962843 314 IKPQLLTTGGTSDGRFIARMGAQVVELGPVN-ATIHKINECVNAADLQLLARMYQRIM 370
Cdd:cd08011 298 IRPKEVISVGASDARFYRNAGIPAIVYGPGRlGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
56-372 |
3.79e-38 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 140.40 E-value: 3.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 56 GQGE-TLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ-HPNHkNRLAFLITSDE 133
Cdd:PRK08588 56 GSGSpVLALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQgQLLN-GTIRLLATAGE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 134 EaSAHNGTVKVVEALMARNerLDYCLVGEPSstevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNpvhrAAPMLNE 213
Cdd:PRK08588 135 E-VGELGAKQLTEKGYADD--LDALIIGEPS-----GHGIVYAHKGSMDYKVTSTGKAAHSSMPELGVN----AIDPLLE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 214 LVGIE------WDKGNEFFPPTSMQIANVKAGTGSNNvIPGDFFVQFNFRFSTELTDETIKARVVALLEKYN------LR 281
Cdd:PRK08588 203 FYNEQkeyfdsIKKHNPYLGGLTHVVTIINGGEQVNS-VPDEAELEFNIRTIPEYDNDQVISLLQEIINEVNqngaaqLS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 282 YTVDwwLSGQPFLTQR-GKLVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGA--QVVELGP-VNATIHKINECVNAA 357
Cdd:PRK08588 282 LDIY--SNHRPVASDKdSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKPdfPVIIFGPgNNLTAHQVDEYVEKD 359
|
330
....*....|....*
gi 1330962843 358 DLQLLARMYQRIMEQ 372
Cdd:PRK08588 360 MYLKFIDIYKEIIIQ 374
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
28-365 |
3.03e-36 |
|
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: 135.03 E-value: 3.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 28 LMIERLRAIGFTVERMDFGDTQN--FWAWRGQGET-LAFAGHTDVV-PAGDADRWinpPFepTIRDGMLFGRGAADMKGS 103
Cdd:cd03885 27 LLAEELEALGFTVERRPLGEFGDhlIATFKGTGGKrVLLIGHMDTVfPEGTLAFR---PF--TVDGDRAYGPGVADMKGG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 104 LAAMVVAAERFVAQHPNHKNRLAFLITSDEE-ASAHNGTVKVVEALMArnerlDYCLVGEPSSTevvGDVVKNGRRGSLT 182
Cdd:cd03885 102 LVVILHALKALKAAGGRDYLPITVLLNSDEEiGSPGSRELIEEEAKGA-----DYVLVFEPARA---DGNLVTARKGIGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 183 CNLTIHGVQGHV-AYPHLADNPVHRAAPMLNELVGIewdkgNEFFPPTSMQIANVKAGTGSnNVIPGDFFVQFNFRFST- 260
Cdd:cd03885 174 FRLTVKGRAAHAgNAPEKGRSAIYELAHQVLALHAL-----TDPEKGTTVNVGVISGGTRV-NVVPDHAEAQVDVRFATa 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 261 ---ELTDETIKARV-VALLEKYNLRYTVDwwLSGQPFLTQRG--KLVDAVVNAiehYNEIKPQLLT--TGGTSDGRFIAR 332
Cdd:cd03885 248 eeaDRVEEALRAIVaTTLVPGTSVELTGG--LNRPPMEETPAsrRLLARAQEI---AAELGLTLDWeaTGGGSDANFTAA 322
|
330 340 350
....*....|....*....|....*....|....*...
gi 1330962843 333 MGAQVVE-LGPVNATIHKINECVNAADL----QLLARM 365
Cdd:cd03885 323 LGVPTLDgLGPVGGGAHTEDEYLELDSLvpriKLLARL 360
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
5-364 |
4.04e-36 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 136.04 E-value: 4.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPSLSPDDAG---CQALMIERLRAIGFTVERMDF----GDTQNFWAW--------RGQGETLAFAGHTDV 69
Cdd:PRK13013 16 LVALTQDLIRIPTLNPPGRAyreICEFLAARLAPRGFEVELIRAegapGDSETYPRWnlvarrqgARDGDCVHFNSHHDV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 70 VPAGDAdrWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAHNGTVKVVEALM 149
Cdd:PRK13013 96 VEVGHG--WTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGGVAYLAEQGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 150 ARNERLDYCLVGEPSSTevvgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNElvgIEwdkgNEFFP-- 227
Cdd:PRK13013 174 FSPDRVQHVIIPEPLNK----DRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAE---IE----ERLFPll 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 228 ---PTSMQIA---------NVKAGTGSNNVIPGDFF------------VQFNFRFSTELTDETIKARVVALLEKY----- 278
Cdd:PRK13013 243 atrRTAMPVVpegarqstlNINSIHGGEPEQDPDYTglpapcvadrcrIVIDRRFLIEEDLDEVKAEITALLERLkrarp 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 279 NLRYTVDWWLSGQPFLTQRGK-LVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGA--QVVELGP-VNATIHKINECV 354
Cdd:PRK13013 323 GFAYEIRDLFEVLPTMTDRDApVVRSVAAAIERVLGRQADYVVSPGTYDQKHIDRIGKlkNCIAYGPgILDLAHQPDEWV 402
|
410
....*....|
gi 1330962843 355 NAADLQLLAR 364
Cdd:PRK13013 403 GIADMVDSAK 412
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
5-276 |
2.20e-34 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 130.69 E-value: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPSLS--PDDAgcqalMIE----RLRAIGFTVERM--DFGDTQNFWAWRGQGET--LAFAGHTDVVPAgD 74
Cdd:PRK07522 6 SLDILERLVAFDTVSrdSNLA-----LIEwvrdYLAAHGVESELIpdPEGDKANLFATIGPADRggIVLSGHTDVVPV-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 75 ADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ---HPNHknrLAFliTSDEEAsahnGTVKV---VEAL 148
Cdd:PRK07522 80 GQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAplrRPLH---LAF--SYDEEV----GCLGVpsmIARL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 149 MARNERLDYCLVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGI-EWDKGNEFF- 226
Cdd:PRK07522 151 PERGVKPAGCIVGEPTSMRPV-----VGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLaDRLAAPGPFd 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1330962843 227 ----PP-TSMQIANVKAGTgSNNVIPGDFFVQFNFRFSTELTDETIKARVVALLE 276
Cdd:PRK07522 226 alfdPPySTLQTGTIQGGT-ALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAE 279
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
5-214 |
4.78e-34 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 130.06 E-value: 4.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPSLSPDDAGCQALMIERLRAIGFT-VERMDFGdtqNFWAWRGQGETL-AFAGHTDVVPAGDADRWINPP 82
Cdd:PRK13004 17 MTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFDkVEIDPMG---NVLGYIGHGKKLiAFDAHIDTVGIGDIKNWDFDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 83 FEPTIRDGMLFGRGAADMKGSLAAMVVAAERFvaQHPNHKNRLAFLITsdeeasahnGTV--KVVEALMAR------NER 154
Cdd:PRK13004 94 FEGEEDDGRIYGRGTSDQKGGMASMVYAAKII--KDLGLDDEYTLYVT---------GTVqeEDCDGLCWRyiieedKIK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 155 LDYCLVGEPSSTEvvgdvVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNEL 214
Cdd:PRK13004 163 PDFVVITEPTDLN-----IYRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNEL 217
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-282 |
2.10e-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 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: 127.04 E-value: 2.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPSLSPDDAGCQALMIERLRAIGFTVERMDfgdtQNFWAWRGQGE----TLAFAGHTDVVPAGDAdrWIN 80
Cdd:cd05651 2 AIELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRKG----NNVWAENGHFDegkpTLLLNSHHDTVKPNAG--WTK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNrLAFLITSDEEASAHNGtvkvVEALMARNERLDYCLV 160
Cdd:cd05651 76 DPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGPLNYN-LIYAASAEEEISGKNG----IESLLPHLPPLDLAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 161 GEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHlADNPVHRAAPMLNELVGIEWDKGNEFFPPTSMQIANVKAGT 240
Cdd:cd05651 151 GEPTEMQPA-----IAEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDIQWLRDFRFDKVSPLLGPVKMTVTQINAGT 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1330962843 241 gSNNVIPG--DFFVQF--NFRFSTELTDETIKARVVALLEKYNLRY 282
Cdd:cd05651 225 -QHNVVPDscTFVVDIrtTEAYTNEEIFEIIRGNLKSEIKPRSFRL 269
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-370 |
7.01e-32 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly 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: 123.72 E-value: 7.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPSLSPDDAG------CQALMiERLRAIGF-TVERMDFGDTQNFW-------AWRGQGETLAFAGHTDVV 70
Cdd:cd05650 3 IIELERDLIRIPAVNPESGGegekekADYLE-KKLREYGFyTLERYDAPDERGIIrpnivakIPGGNDKTLWIISHLDTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 71 PAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAHNGTVKVVEAL-M 149
Cdd:cd05650 82 PPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGITPKYNFGLLFVADEEDGSEYGIQYLLNKFdL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 150 ARNErlDYCLVgePSSTEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWDKGNE----F 225
Cdd:cd05650 162 FKKD--DLIIV--PDFGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFALELDELLHEKFDEkddlF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 226 FPPTSMQIANVKAGTGSN-NVIPGDFFVQFNFRF--STELTD--ETIKARVVALLEKYNLRYTVDWWLSGQ--PFLTQRG 298
Cdd:cd05650 238 NPPYSTFEPTKKEANVPNvNTIPGYDVFYFDCRVlpTYKLDEvlKFVNKIISDFENSYGAGITYEIVQKEQapPATPEDS 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330962843 299 KLVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIM 370
Cdd:cd05650 318 EIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYIRISHIVKDAKVFAEML 389
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-271 |
1.86e-30 |
|
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: 118.92 E-value: 1.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPSLSPDDAGCQALMIERLRAIGFTVER--MDFGDTQNFWAWRGQGET--LAFAGHTDVVPagdadrwin 80
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEKqpVENKDRFNVYAYPGSSRQprVLLTSHIDTVP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 81 P--PFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASaHNGTVKVVEALmarNERLDYC 158
Cdd:cd05652 72 PfiPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEETG-GDGMKAFNDLG---LNTWDAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 159 LVGEPssTEvvGDVVKnGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWDKgNEFFPPTSMQIANVKA 238
Cdd:cd05652 148 IFGEP--TE--LKLAS-GHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPS-SELLGPTTLNIGRISG 221
|
250 260 270
....*....|....*....|....*....|....*
gi 1330962843 239 GTGSnNVIPGDFFVQFNFRFSTELTD--ETIKARV 271
Cdd:cd05652 222 GVAA-NVVPAAAEASVAIRLAAGPPEvkDIVKEAV 255
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-364 |
1.95e-30 |
|
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: 120.11 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 7 ELTQQLIRRPSLSPDDAGCQALMIERLRAIGFTVERM-----------DFGDtqNFWAWRG-------------QGETLA 62
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDRWeidveklkhhpGFSP--VAVDYAGapnvvgthrprgeTGRSLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 63 FAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEaSAHNGTV 142
Cdd:cd03895 79 LNGHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEE-CTGNGAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 143 kvveALMARNERLDYCLVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIE--W- 219
Cdd:cd03895 158 ----AALMRGYRADAALIPEPTELKLV-----RAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEreWn 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 220 -----DKGNEFFP-PTSMQIANVKAGTGSNNVIPgdfFVQFNFR--FSTELTDETIKARVVALLEKYNLRytvDWWLSGQ 291
Cdd:cd03895 229 arkksHPHFSDHPhPINFNIGKIEGGDWPSSVPA---WCVLDCRigIYPGESPEEARREIEECVADAAAT---DPWLSNH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 292 PF-------------LTQRGKLVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGA-QVVELGPVNATIHKINECVNAA 357
Cdd:cd03895 303 PPevewngfqaegyvLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGDiPALCYGPGSRDAHGFDESVDLE 382
|
....*..
gi 1330962843 358 DLQLLAR 364
Cdd:cd03895 383 SLRKITK 389
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
5-368 |
2.88e-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: 118.70 E-value: 2.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPSLSpDDAGCQALMIER-LRAIG-FTVERmdFGDTQNFWAWRGQGETLAFAGHTDVVPAGDadrwiNPP 82
Cdd:cd05647 1 PIELTAALVDIPSVS-GNEKPIADEIEAaLRTLPhLEVIR--DGNTVVARTERGLASRVILAGHLDTVPVAG-----NLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 83 fePTIR-DGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKnrLAFLITSDEE-ASAHNGTVKVVEALmarNERL--DYC 158
Cdd:cd05647 73 --SRVEeDGVLYGCGATDMKAGDAVQLKLAATLAAATLKHD--LTLIFYDCEEvAAELNGLGRLAEEH---PEWLaaDFA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 159 LVGEPSSTEVVGdvvknGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEwdkgneffpPTSMQI----- 233
Cdd:cd05647 146 VLGEPTDGTIEG-----GCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLAAYE---------PRTVNIdglty 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 234 -----ANVKAGTGSNNVIPGDFFVQFNFRFSTELTDETIKARVVALLEKYNLRYTV-DWWLSGQPFLTQR--GKLVDAVv 305
Cdd:cd05647 212 reglnAVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEIEVtDLSPGALPGLDHPvaRDLIEAV- 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330962843 306 naiehYNEIKPQLlttGGTSDGRFiARMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQR 368
Cdd:cd05647 291 -----GGKVRAKY---GWTDVARF-SALGIPAVNFGPGDPLLaHKRDEQVPVEQITACAAILRR 345
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
5-370 |
7.67e-30 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 118.41 E-value: 7.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPSLSPDDAG------CQALMiERLRAIGFT-VERMDFGDTQNFWAWR--------GQGE--TLAFAGHT 67
Cdd:PRK13983 7 MIELLSELIAIPAVNPDFGGegekekAEYLE-SLLKEYGFDeVERYDAPDPRVIEGVRpnivakipGGDGkrTLWIISHM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 68 DVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAHNGtvkvVEA 147
Cdd:PRK13983 86 DVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYG----IQY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 148 LMARNERL----DYCLV---GEPSstevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWD 220
Cdd:PRK13983 162 LLKKHPELfkkdDLILVpdaGNPD-----GSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRAAADFALELDEALHE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 221 KGNE----FFPPTS-MQIANVKAGTGSNNVIPGDFFVQFNFRF--STELTD--ETIKARVVALLEKYNLRYTVDWWLSGQ 291
Cdd:PRK13983 237 KFNAkdplFDPPYStFEPTKKEANVDNINTIPGRDVFYFDCRVlpDYDLDEvlKDIKEIADEFEEEYGVKIEVEIVQREQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 292 --PFLTQRGKLVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRI 369
Cdd:PRK13983 317 apPPTPPDSEIVKKLKRAIKEVRGIEPKVGGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYAKISNLIEDAKVFALL 396
|
.
gi 1330962843 370 M 370
Cdd:PRK13983 397 L 397
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
5-373 |
9.08e-30 |
|
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: 117.07 E-value: 9.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPSLSPDDAGCQALMIERLRAIGFTVERMDFGdtqNFWAWRGQGE-TLAFAGHTDVVPAgdadrwinpPF 83
Cdd:cd05653 3 AVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEAG---NAVGGAGSGPpDVLLLGHIDTVPG---------EI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 84 EPTIRDGMLFGRGAADMKGSLAAMVVAAerfVAQHPNHKNRLAFLITSDEEASAhngtvKVVEALMARNERLDYCLVGEP 163
Cdd:cd05653 71 PVRVEGGVLYGRGAVDAKGPLAAMILAA---SALNEELGARVVVAGLVDEEGSS-----KGARELVRRGPRPDYIIIGEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 164 SSTEvvGDVVknGRRGSLTCNLTIHGVQGHVAYPhlADNPVHRAAPMLNELVgiEWDKGNE--FFPPTSMQIANVKAGTg 241
Cdd:cd05653 143 SGWD--GITL--GYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLIKKWLEVK--KWAEGYNvgGRDFDSVVPTLIKGGE- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 242 SNNVIPGDFFVQFNFRFSTELTDETIKARVVALLEKYNLRYTVDwwlsGQPFLT-QRGKLVDAVVNAIEHYNeIKPQLLT 320
Cdd:cd05653 214 SSNGLPQRAEATIDLRLPPRLSPEEAIALATALLPTCELEFIDD----TEPVKVsKNNPLARAFRRAIRKQG-GKPRLKR 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1330962843 321 TGGTSDGRFIA-RMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRIMEQL 373
Cdd:cd05653 289 KTGTSDMNVLApLWTVPIVAYGPGDSTLdHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
6-218 |
1.58e-28 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 115.10 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 6 IELTQQLIRRPSLSPDDAGCQALMIERLRAIGFTVER--MDFGDTQNF-----WAW---------------RGQGETLAF 63
Cdd:PRK06837 23 VAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDRwsIDPDDLKSHpgagpVEIdysgapnvvgtyrpaGKTGRSLIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 64 AGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVA--AERFVAQHPnhKNRLaFLITSDEEASAHNGt 141
Cdd:PRK06837 103 QGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFAldALRAAGLAP--AARV-HFQSVIEEESTGNG- 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330962843 142 vkvveALMA--RNERLDYCLVGEPSSTEVVGDVVkngrrGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIE 218
Cdd:PRK06837 179 -----ALSTlqRGYRADACLIPEPTGEKLVRAQV-----GVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALRELE 247
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
175-283 |
1.11e-26 |
|
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: 102.42 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 175 NGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWDKGNeFFPPTSMQIANVKAGTgSNNVIPGDFFVQF 254
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGF-DFPRTTLNITGIEGGT-ATNVIPAEAEAKF 78
|
90 100
....*....|....*....|....*....
gi 1330962843 255 NFRFSTELTDETIKARVVALLEKYNLRYT 283
Cdd:pfam07687 79 DIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
5-366 |
7.39e-26 |
|
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: 107.72 E-value: 7.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPS-LSPDDAGC-------QAL--MIERLRAIGFTVERMDfgdtqNF--WAWRGQG-ETLAFAGHTDVVP 71
Cdd:cd03888 10 ILEDLKELVAIPSvRDEATEGApfgegprKALdkFLDLAKRLGFKTKNID-----NYagYAEYGEGeEVLGILGHLDVVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 72 AGDAdrWINPPFEPTIRDGMLFGRGAADMKG-SLAAMVvaAERFVAQH---PNHKNRlaFLITSDEEAS--------AHN 139
Cdd:cd03888 85 AGEG--WTTDPFKPVIKDGKLYGRGTIDDKGpTIAALY--ALKILKDLglpLKKKIR--LIFGTDEETGwkciehyfEHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 140 GTVK----------VVEA------LMAR-------NERLDYCLVGE-----PSSTEVVGDVVKNGRRGSLTCN------- 184
Cdd:cd03888 159 EYPDfgftpdaefpVINGekgivtVDLTfkidddkGYRLISIKGGEatnmvPDKAEAVIPGKDKEELALSAATdlkgnie 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 185 -------LTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWDKG-----NEFFPPTS------MQIANVKAG-----TG 241
Cdd:cd03888 239 iddggveLTVTGKSAHASAPEKGVNAITLLAKFLAELNKDGNDKDfikflAKNLHEDYngkklgINFEDEVMGeltlnPG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 242 SNNVIPGDFFVQFNFRFSTELTDETIKARVVALLEKYNLRYTVDwwLSGQPFLTQR-GKLVDAVVNAIEHYNEIKPQLLT 320
Cdd:cd03888 319 IITLDDGKLELGLNVRYPVGTSAEDIIKQIEEALEKYGVEVEGH--KHQKPLYVPKdSPLVKTLLKVYEEQTGKEGEPVA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1330962843 321 TGGTSDGRFIARMgaqvVELGP----VNATIHKINECVNAADLQLLARMY 366
Cdd:cd03888 397 IGGGTYARELPNG----VAFGPefpgQKDTMHQANEFIPIDDLIKALAIY 442
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
33-359 |
7.43e-26 |
|
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: 107.80 E-value: 7.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 33 LRAIGFTVERMDFGDTQNF-WAWRGQGE---TLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMV 108
Cdd:cd03893 34 LRRLGFTVEIVDTSNGAPVvFAEFPGAPgapTVLLYGHYDVQPAGDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 109 VAAERFVAQHPNHKNRLAFLITSDEEAsahnGTVKVVEALMARNERL--DYCLVGEPSSTEVVGDVVKNGRRGSLTCNLT 186
Cdd:cd03893 114 AALRALMQQGGDLPVNVKFIIEGEEES----GSPSLDQLVEAHRDLLaaDAIVISDSTWVGQEQPTLTYGLRGNANFDVE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 187 I----HGV--------------------------QGHVAYPHLADNP------VHRAAPMLNELVG-IEWDKG----NEF 225
Cdd:cd03893 190 VkgldHDLhsglyggvvpdpmtalaqllaslrdeTGRILVPGLYDAVrelpeeEFRLDAGVLEEVEiIGGTTGsvaeRLW 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 226 FPPT----SMQIANVkaGTGSNNVIPGDFFVQFNFRFSTELTDETIKARVVALLEK---YNLRYTVDWWLSGQPFLTQ-R 297
Cdd:cd03893 270 TRPAltvlGIDGGFP--GEGSKTVIPPRARAKISIRLVPGQDPEEASRLLEAHLEKhapSGAKVTVSYVEGGMPWRSDpS 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330962843 298 GKLVDAVVNAIEHYNEIKPQLLTTGGT--SDGRFIARMGAQVVELGPVNAT--IHKINECVNAADL 359
Cdd:cd03893 348 DPAYQAAKDALRTAYGVEPPLTREGGSipFISVLQEFPQAPVLLIGVGDPDdnAHSPNESLRLGNY 413
|
|
| PRK06915 |
PRK06915 |
peptidase; |
6-193 |
3.43e-25 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 105.54 E-value: 3.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 6 IELTQQLIRRPSLSPDDAGCQALMIERLRAIG------------------FTVERMDFGDTQNFWA-WRGQGE--TLAFA 64
Cdd:PRK06915 20 VKLLKRLIQEKSVSGDESGAQAIVIEKLRELGldldiwepsfkklkdhpyFVSPRTSFSDSPNIVAtLKGSGGgkSMILN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 65 GHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEaSAHNGTVKV 144
Cdd:PRK06915 100 GHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEE-SGGAGTLAA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1330962843 145 VEalmaRNERLDYCLVGEPSSTEVvgdVVKngRRGSLTCNLTIHGVQGH 193
Cdd:PRK06915 179 IL----RGYKADGAIIPEPTNMKF---FPK--QQGSMWFRLHVKGKAAH 218
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
56-373 |
7.92e-25 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 103.71 E-value: 7.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 56 GQGETLaFAGHTDVVPAGdadrwinppFEPTIRDGMLFGRGAADMKGSLAAMVVAAerFVAQHPNHKNRLAFLitSDEEa 135
Cdd:PRK00466 59 GEGDIL-LASHVDTVPGY---------IEPKIEGEVIYGRGAVDAKGPLISMIIAA--WLLNEKGIKVMVSGL--ADEE- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 136 sahnGTVKVVEALMARNERLDYCLVGEPSSTEvvgDVVKnGRRGSLTCNLTIHGVQGHvayphlADNPVHRAAPMLNELV 215
Cdd:PRK00466 124 ----STSIGAKELVSKGFNFKHIIVGEPSNGT---DIVV-EYRGSIQLDIMCEGTPEH------SSSAKSNLIVDISKKI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 216 gIEWDKGNEFFPPTSMQIANVKAGTgSNNVIPGDFFVQFNFRFSTELTDETIKARVVALLEKYNLRyTVDwwlSGQPFLT 295
Cdd:PRK00466 190 -IEVYKQPENYDKPSIVPTIIRAGE-SYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQECGLK-IVD---ETPPVKV 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 296 Q-RGKLVDAVVNAIEHYNeIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRIMEQL 373
Cdd:PRK00466 264 SiNNPVVKALMRALLKQN-IKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLeHTNQEKITLDEIYIAVKTYMLAIEEL 342
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-366 |
3.63e-24 |
|
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: 102.11 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 6 IELTQQLIRRPSLSPDDAGCQALMIERLRAIGF-TVERMDFGdtqNFWAWRGQGET-LAFAGHTDVVPAGDADRWINPPF 83
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGFdEVEIDPMG---NVIGYIGGGKKkILFDGHIDTVGIGNIDNWKFDPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 84 EPTIRDGMLFGRGAADMKGSLAAMVVAAERFvaqhpnhkNRLAFLITSDEEASAhnGTV--KVVEALMAR------NERL 155
Cdd:cd05649 78 EGYETDGKIYGRGTSDQKGGLASMVYAAKIM--------KDLGLRDFAYTILVA--GTVqeEDCDGVCWQyiskadKIKP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 156 DYCLVGEPSSTEVvgdvvKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWDKG-NEFFPPTSMQIA 234
Cdd:cd05649 148 DFVVSGEPTDGNI-----YRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFPeAPFLGRGTLTVT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 235 NVKAGTGSNNVIPGDFFVQFNFRFSTELTDETIKA--RVVALLEKYNL----------------------RYTVDWWLSG 290
Cdd:cd05649 223 DIFSTSPSRCAVPDSCRISIDRRLTVGETWEGCLEeiRALPAVKKYGDdvavsmynydrpsytgevyeseRYFPTWLLPE 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330962843 291 QPFLTQRgkLVDAVVNAIEHYNEIKPQLLTTGGTSdgrFIARMGAQVVELGP-VNATIHKINECVNAADLQLLARMY 366
Cdd:cd05649 303 DHELVKA--LLEAYKALFGARPLIDKWTFSTNGVS---IMGRAGIPCIGFGPgAENQAHAPNEYTWKEDLVRCAAGY 374
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
55-176 |
6.15e-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: 97.89 E-value: 6.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 55 RGQGETLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEE 134
Cdd:cd18669 9 GGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1330962843 135 ASAHNGTVKVVEALMARNERLDYCLVGEPSSTEVVGDVVKNG 176
Cdd:cd18669 89 VGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTP 130
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
8-368 |
6.45e-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: 102.05 E-value: 6.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 8 LTQQLIRRPSLSPDDAGCQA-----LMIERLRAIGFTVERMDF----GDTQNFWAWRGQGET---LAFAGHTDVVPAgDA 75
Cdd:cd05675 3 LLQELIRIDTTNSGDGTGSEtraaeVLAARLAEAGIQTEIFVVeshpGRANLVARIGGTDPSagpLLLLGHIDVVPA-DA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 76 DRWINPPFEPTIRDGMLFGRGAADMKGsLAAMVVAAERFVAQHPNHKNR-LAFLITSDEEASAHNGTVKVVEALMARNER 154
Cdd:cd05675 82 SDWSVDPFSGEIKDGYVYGRGAVDMKN-MAAMMLAVLRHYKREGFKPKRdLVFAFVADEEAGGENGAKWLVDNHPELFDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 155 LDYCL--VGEPSSTEVVGDV---VKNGRRGSLTCNLTIHGVQGHVAYPHlADNPVHRAAPMLNELVGIEW----DKGNEF 225
Cdd:cd05675 161 ATFALneGGGGSLPVGKGRRlypIQVAEKGIAWMKLTVRGRAGHGSRPT-DDNAITRLAEALRRLGAHNFpvrlTDETAY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 226 F-------PP--------------------------------TSMQIANVKAGTgSNNVIPGDFFVQFNFRFSTELTDET 266
Cdd:cd05675 240 FaqmaelaGGeggalmltavpvldpalaklgpsapllnamlrNTASPTMLDAGY-ATNVLPGRATAEVDCRILPGQSEEE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 267 IKARVVALLEKYnlRYTVDW-WLSGQPFLTQRGKLVDAVVNAIEHYN---EIKPQLLTtgGTSDGRFIARMGAQVVELGP 342
Cdd:cd05675 319 VLDTLDKLLGDP--DVSVEAvHLEPATESPLDSPLVDAMEAAVQAVDpgaPVVPYMSP--GGTDAKYFRRLGIPGYGFAP 394
|
410 420 430
....*....|....*....|....*....|....
gi 1330962843 343 VNAT--------IHKINECVNAADLQLLARMYQR 368
Cdd:cd05675 395 LFLPpeldytglFHGVDERVPVESLYFGVRFLDR 428
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
54-373 |
2.36e-22 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 98.09 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 54 WRGQGETLA---FAGHTDVVPA--GDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ--HPNHKNRLA 126
Cdd:PRK08262 104 WKGSDPSLKpivLMAHQDVVPVapGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQgfQPRRTIYLA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 127 FliTSDEEASAHnGTVKVVEALMARNERLDyCLVGEpsSTEVVGDVVKN----------GRRGSLTCNLTIHGVQGHVAY 196
Cdd:PRK08262 184 F--GHDEEVGGL-GARAIAELLKERGVRLA-FVLDE--GGAITEGVLPGvkkpvaligvAEKGYATLELTARATGGHSSM 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 197 P--------------HLADNP------------VHRAAP--------MLNELVGIEWDKGNEFF--PPTSMQIANVKAGT 240
Cdd:PRK08262 258 PprqtaigrlaraltRLEDNPlpmrlrgpvaemFDTLAPemsfaqrvVLANLWLFEPLLLRVLAksPETAAMLRTTTAPT 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 241 ---GSN--NVIPGDFFVQFNFRFSTELTDETIKARVVALLEkyNLRYTVDW-----------WLSGQPFltqrgKLVDAV 304
Cdd:PRK08262 338 mlkGSPkdNVLPQRATATVNFRILPGDSVESVLAHVRRAVA--DDRVEIEVlggnsepspvsSTDSAAY-----KLLAAT 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 305 VnaiehyNEIKPQL-----LTTGGTsDGRFIARMGAQVVELGPVNAT------IHKINECVNAADLQLLARMYQRIMEQL 373
Cdd:PRK08262 411 I------REVFPDVvvapyLVVGAT-DSRHYSGISDNVYRFSPLRLSpedlarFHGTNERISVANYARMIRFYYRLIENA 483
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
6-284 |
8.16e-21 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 92.13 E-value: 8.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 6 IELTQQLIRRPSLSPDDAGCQALMIERLRAIGFTVERMDFGDTQNFWAwrGQGETLAFAGHTDVVPagdadrwinPPFEP 85
Cdd:PRK08652 5 KELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIESDGEVINIVV--NSKAELFVEVHYDTVP---------VRAEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 86 TIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLitSDEEASAHNgtvkvvEALMARNERLDYCLVGEPSS 165
Cdd:PRK08652 74 FVDGVYVYGTGACDAKGGVAAILLALEELGKEFEDLNVGIAFV--SDEEEGGRG------SALFAERYRPKMAIVLEPTD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 166 TEVvgdvvKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWDKGNEFFPPTSMQIAnvkAGTGSNNV 245
Cdd:PRK08652 146 LKV-----AIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPHIGIQEI---IGGSPEYS 217
|
250 260 270
....*....|....*....|....*....|....*....
gi 1330962843 246 IPGDFFVQFNFRFSTELTDETIKARVVALLEKYNLRYTV 284
Cdd:PRK08652 218 IPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEY 256
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
10-257 |
1.33e-20 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 91.80 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 10 QQLIRRPSLSPDDAGCQALMIERLRAI--GFTVERMDFGD-TQNFWAWRGQGETLaFAGHTDVVPagDADRWINPPFEPT 86
Cdd:PRK08737 13 QALVSFDTRNPPRAITTGGIFDYLRAQlpGFQVEVIDHGAgAVSLYAVRGTPKYL-FNVHLDTVP--DSPHWSADPHVMR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 87 IRDGMLFGRGAADMKGSLAAMVVAAERfvaqhpnHKNRLAFLITSDEEAsahnGTVKVVEALMARNERLDYCLVGEPSST 166
Cdd:PRK08737 90 RTDDRVIGLGVCDIKGAAAALLAAANA-------GDGDAAFLFSSDEEA----NDPRCVAAFLARGIPYEAVLVAEPTMS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 167 EVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPH-LADNPVHRAAPMLNELVGIEWDKGNEFFPPTS---MQIANVKAGTGS 242
Cdd:PRK08737 159 EAV-----LAHRGISSVLMRFAGRAGHASGKQdPSASALHQAMRWGGQALDHVESLAHARFGGLTglrFNIGRVEGGIKA 233
|
250
....*....|....*
gi 1330962843 243 NNVIPGdFFVQFNFR 257
Cdd:PRK08737 234 NMIAPA-AELRFGFR 247
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
12-215 |
3.47e-20 |
|
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: 91.22 E-value: 3.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 12 LIRRPSLS------PDDAGCQALMIERLRAIGF-TVERMD-------FGDtqnfWAWRGQGETLAFAGHTDVVPAGDADR 77
Cdd:cd05680 7 LLRIPSVSadpahkGDVRRAAEWLADKLTEAGFeHTEVLPtgghplvYAE----WLGAPGAPTVLVYGHYDVQPPDPLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 78 WINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAHNgtvkvVEALMARN-ERL- 155
Cdd:cd05680 83 WTSPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVEGALPVNVKFLIEGEEEIGSPS-----LPAFLEENaERLa 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330962843 156 -DYCLVGEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQ-----GHvaYPHLADNPVHRAAPMLNELV 215
Cdd:cd05680 158 aDVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPNrdlhsGS--YGGAVPNPANALARLLASLH 221
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-372 |
3.95e-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: 90.61 E-value: 3.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIR----RPSLSPDDAGCQALMIERLRAI----GFTVERMDF--GDTQNFWAWRGQG--ETLAFAGHTDVVpa 72
Cdd:cd08013 3 PVSLTQTLVRinssNPSLSATGGAGEAEIATYVAAWlahrGIEAHRIEGtpGRPSVVGVVRGTGggKSLMLNGHIDTV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 73 gDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLitSDEEaSAHNGTvkvvEALMARN 152
Cdd:cd08013 81 -TLDGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGLRGDVILAAV--ADEE-DASLGT----QEVLAAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 153 ERLDYCLVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVG----IEWDKGNEFFPP 228
Cdd:cd08013 153 WRADAAIVTEPTNLQII-----HAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALEEyqqeLPERPVDPLLGR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 229 TSMQIANVKAGTGSNNViPGDFFVQFNFRFSTELTDETIKARVVALLE---------KYNLRYTVdwwLSGQPF-LTQRG 298
Cdd:cd08013 228 ASVHASLIKGGEEPSSY-PARCTLTIERRTIPGETDESVLAELTAILGelaqtvpnfSYREPRIT---LSRPPFeVPKEH 303
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330962843 299 KLVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQ 372
Cdd:cd08013 304 PFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGAGLHAKEEWVDVESIRQLREVLSAVVRE 377
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
55-175 |
1.13e-19 |
|
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: 85.94 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 55 RGQGETLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEE 134
Cdd:cd03873 9 GEGGKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1330962843 135 ASAHNGTVKVVEALMARNERLDYCLVGEPS--STEVVGDVVKN 175
Cdd:cd03873 89 VGSGGGKGLLSKFLLAEDLKVDAAFVIDATagPILQKGVVIRN 131
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
6-170 |
1.49e-19 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 89.33 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 6 IELTQQLIRRPSLSP---DDAGCQALMIERLRAIGFTVERMDF--GDTQNFWAWRGQGET----LAFAGHTDVVPAGDAD 76
Cdd:PRK08596 16 LELLKTLVRFETPAPparNTNEAQEFIAEFLRKLGFSVDKWDVypNDPNVVGVKKGTESDayksLIINGHMDVAEVSADE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 77 RWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEAsAHNGTVKVVEalmaRNERLD 156
Cdd:PRK08596 96 AWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEV-GEAGTLQCCE----RGYDAD 170
|
170
....*....|....
gi 1330962843 157 YCLVGEPSSTEVVG 170
Cdd:PRK08596 171 FAVVVDTSDLHMQG 184
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
4-165 |
3.38e-19 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 87.96 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 4 PVIELTQQLIRRPSLS---PD-DAGCQALmIERL----RAIGFTVERM---DFGDTQNFWAWRGQGET-LAFAGHTDVVP 71
Cdd:PRK05111 6 SFIEMYRALIATPSISatdPAlDQSNRAV-IDLLagwfEDLGFNVEIQpvpGTRGKFNLLASLGSGEGgLLLAGHTDTVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 72 AgDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVA---QHPnhknrLAFLITSDEEaSAHNGTVKVVEal 148
Cdd:PRK05111 85 F-DEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLtklKKP-----LYILATADEE-TSMAGARAFAE-- 155
|
170
....*....|....*..
gi 1330962843 149 mARNERLDYCLVGEPSS 165
Cdd:PRK05111 156 -ATAIRPDCAIIGEPTS 171
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
12-216 |
3.88e-19 |
|
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: 88.17 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 12 LIRRPSLSPDDAG---CQALMIERLRAIGFTVER-------MDFGDTQNfwawrGQGETLAFAGHTDVVPAGDADRWINP 81
Cdd:cd05681 8 LLKIPSVSAQGRGipeTADFLKEFLRRLGAEVEIfetdgnpIVYAEFNS-----GDAKTLLFYNHYDVQPAEPLELWTSD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 82 PFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAHNgtvkvVEALMARNERL---DYC 158
Cdd:cd05681 83 PFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPN-----LEKFVAEHADLlkaDGC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330962843 159 L-----VGEPSSTEVVGdvvknGRRGSLTCNLTIHG--VQGHVAYPHLADNPVHRAAPMLNELVG 216
Cdd:cd05681 158 IwegggKNPKGRPQISL-----GVKGIVYVELRVKTadFDLHSSYGAIVENPAWRLVQALNSLRD 217
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
4-373 |
1.00e-18 |
|
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: 86.77 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 4 PVIELTQQLIRRPSL--SPDDAGCQALMIERLRAIGFTVERMDF--GDTQNFWAWRGQGETLA---FAGHTDVVPAGDaD 76
Cdd:TIGR01880 10 IAVTRFREYLRINTVqpNPDYAACVDFLIKQADELGLARKTIEFvpGKPVVVLTWPGSNPELPsilLNSHTDVVPVFR-E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 77 RWINPPFEPTI-RDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAHNGTVKVVEALMARNERL 155
Cdd:TIGR01880 89 HWTHPPFSAFKdEDGNIYARGAQDMKCVGVQYLEAVRNLKASGFKFKRTIHISFVPDEEIGGHDGMEKFAKTDEFKALNL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 156 DYCL-VGEPSSTEVVgdVVKNGRRGSLTCNLTIHGVQGHVA--YPHLADNPVHRAAPMLNELVGIEWD--KGNEFFPP-- 228
Cdd:TIGR01880 169 GFALdEGLASPDDVY--RVFYAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRRFRESQFQllQSNPDLAIgd 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 229 -TSMQIANVKAGTGSnNVIPGDFFVQFNFRFSTELTDETIKARVvallekynlrytVDWW-------------LSGQPFL 294
Cdd:TIGR01880 247 vTSVNLTKLKGGVQS-NVIPSEAEAGFDIRLAPSVDFEEMENRL------------DEWCadagegvtyefsqHSGKPLV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 295 TQrgklVD-------AVVNAIEHYN-EIKPQLLTtgGTSDGRFIARMGAQVVELGPVNAT---IHKINECVNAADLQLLA 363
Cdd:TIGR01880 314 TP----HDdsnpwwvAFKDAVKEMGcTFKPEILP--GSTDSRYIRAAGVPALGFSPMNNTpvlLHDHNEFLNEAVFLRGI 387
|
410
....*....|
gi 1330962843 364 RMYQRIMEQL 373
Cdd:TIGR01880 388 EIYQTLISAL 397
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
1-197 |
1.43e-18 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 85.78 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 1 MSCPVIELTQQLIRRPSLSPDDAGCQALMIERLRAIGFTVERMDFGdtqNFWAWRGQG-ETLAFAGHTDVVPaGDAdrwi 79
Cdd:PRK04443 4 SALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREAWVDEAG---NARGPAGDGpPLVLLLGHIDTVP-GDI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 80 npPFEptIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPnhkNRLAFLITSDEEASAHNGTvkvveALMARNERLDYCL 159
Cdd:PRK04443 76 --PVR--VEDGVLWGRGSVDAKGPLAAFAAAAARLEALVR---ARVSFVGAVEEEAPSSGGA-----RLVADRERPDAVI 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 1330962843 160 VGEPSSTevvgDVVKNGRRGSLTCNLTIHGVQGHVAYP 197
Cdd:PRK04443 144 IGEPSGW----DGITLGYKGRLLVTYVATSESFHSAGP 177
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
54-215 |
1.48e-17 |
|
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group mostly contains proteins that have been uncharacterized to date, but also includes vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis. Also included in this subfamily is peptidase M20 domain containing 1 (PM20D1), that is enriched in uncoupling protein 1, UCP1(+) versus UCP1(-) adipocytes is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction; N-acyl amino acids directly bind mitochondria and function as endogenous uncouplers of UCP1-independent respiration. Mice studies show increased circulating PM20D1 augments respiration and increases N-acyl amino acids in blood, and administration of N-acyl amino acids improves glucose homeostasis and increases energy expenditure.
Pssm-ID: 349923 [Multi-domain] Cd Length: 471 Bit Score: 83.84 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 54 WRGQGETLA---FAGHTDVVPA--GDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQH--PNHKNRLA 126
Cdd:cd05674 62 WEGSDPSLKpllLMAHQDVVPVnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGfkPRRTIILA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 127 FliTSDEEASAHNGTVKVVEALMAR-NERLDYCLVGEPS---STEVVGD---VVKNGRRGSLTCNLTIHGVQGHVAYPhl 199
Cdd:cd05674 142 F--GHDEEVGGERGAGAIAELLLERyGVDGLAAILDEGGavlEGVFLGVpfaLPGVAEKGYMDVEITVHTPGGHSSVP-- 217
|
170
....*....|....*.
gi 1330962843 200 adnPVHRAAPMLNELV 215
Cdd:cd05674 218 ---PKHTGIGILSEAV 230
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
65-334 |
1.85e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 83.36 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 65 GHTDVVPAgDADRWINPPFEPTIRDGMLFGRGAADMKGsLAAMVVAAERFVAQH---PNHKNRLAFLitSDEEASAHNGT 141
Cdd:PRK07906 72 GHLDVVPA-EAADWSVHPFSGEIRDGYVWGRGAVDMKD-MDAMMLAVVRHLARTgrrPPRDLVFAFV--ADEEAGGTYGA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 142 VKVVEalmARNERLDYClvgepssTEVVGDV---------------VKNGRRGSLTCNLTIHGVQGHVAYPHlADNPVHR 206
Cdd:PRK07906 148 HWLVD---NHPELFEGV-------TEAISEVggfsltvpgrdrlylIETAEKGLAWMRLTARGRAGHGSMVN-DDNAVTR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 207 AA-----------PM------------LNELVGIEWDKGNeffPPTSM----QIANVKAGTGSN-------------NVI 246
Cdd:PRK07906 217 LAeavarigrhrwPLvltptvrafldgVAELTGLEFDPDD---PDALLaklgPAARMVGATLRNtanptmlkagykvNVI 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 247 PGDFFVQFNFRFsteL--TDETIKARVVALLEKYnlrytVDW-WLSGQPFL--TQRGKLVDAVVNAIEHYN---EIKPQL 318
Cdd:PRK07906 294 PGTAEAVVDGRF---LpgREEEFLATVDELLGPD-----VEReWVHRDPALetPFDGPLVDAMNAALLAEDpgaRVVPYM 365
|
330
....*....|....*.
gi 1330962843 319 LtTGGTsDGRFIARMG 334
Cdd:PRK07906 366 L-SGGT-DAKAFSRLG 379
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
27-214 |
4.12e-17 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 82.36 E-value: 4.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 27 ALMIERLRAIGFT---VERMD-FGDTQNFWA-WRGQGET--LAFAGHTDVVPAGDADrWINPPFEPTIRDGMLFGRGAAD 99
Cdd:PRK09133 63 EAMAARLKAAGFAdadIEVTGpYPRKGNLVArLRGTDPKkpILLLAHMDVVEAKRED-WTRDPFKLVEENGYFYGRGTSD 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 100 MKgSLAAMVVAA------ERFVaqhPNHKNRLAFliTSDEEASAHNGTVKVVE-------ALMARNE----RLDYclVGE 162
Cdd:PRK09133 142 DK-ADAAIWVATlirlkrEGFK---PKRDIILAL--TGDEEGTPMNGVAWLAEnhrdlidAEFALNEggggTLDE--DGK 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330962843 163 PSSTEVVGdvvknGRRGSLTCNLTIHGVQGHVAYPhLADNPVHRAA------------PMLNEL 214
Cdd:PRK09133 214 PVLLTVQA-----GEKTYADFRLEVTNPGGHSSRP-TKDNAIYRLAaalsrlaayrfpVMLNDV 271
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
5-134 |
8.39e-17 |
|
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: 81.27 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 5 VIELTQQLIRRPSLSPDDAGCQ----------AL--MIERLRAIGFTVErmDFGDTQNFWAWrGQG-ETLAFAGHTDVVP 71
Cdd:TIGR01887 4 ILEDLKELIAIDSVEDLEKAKEgapfgegprkALdkFLEIAKRDGFTTE--NVDNYAGYIEY-GQGeEVLGILGHLDVVP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330962843 72 AGDAdrWINPPFEPTIRDGMLFGRGAADMKG----SLAAMVVAAERFVAQhpnhKNRLAFLITSDEE 134
Cdd:TIGR01887 81 AGDG--WTSPPFEPTIKDGRIYGRGTLDDKGptiaAYYAMKILKELGLKL----KKKIRFIFGTDEE 141
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
6-134 |
1.71e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 80.51 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 6 IELTQQLIRRPS-LSPDDAGC---QAL------MIERLRAIGFTVermdFGDTQNFW--AWRGQG-ETLAFAGHTDVVPA 72
Cdd:PRK07205 14 VAAIKTLVSYPSvLNEGENGTpfgQAIqdvleaTLDLCQGLGFKT----YLDPKGYYgyAEIGQGeELLAILCHLDVVPE 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330962843 73 GDADRWINPPFEPTIRDGMLFGRGAADMKG-SLAAMvVAAERFVAQHPNHKNRLAFLITSDEE 134
Cdd:PRK07205 90 GDLSDWQTPPFEAVEKDGCLFGRGTQDDKGpSMAAL-YAVKALLDAGVQFNKRIRFIFGTDEE 151
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
63-373 |
3.11e-15 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 76.54 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 63 FAGHTDVV-PAGDadrwinpPFE--PTIRDGMLFGRGAADMKGSLAAMVVAAERFvAQHPnHKNRLAF--LITSDEE--- 134
Cdd:PRK07338 97 LTGHMDTVfPADH-------PFQtlSWLDDGTLNGPGVADMKGGIVVMLAALLAF-ERSP-LADKLGYdvLINPDEEigs 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 135 -ASAhngtvkVVEALMARneRLDYCLVGEPSSTEvvGDVVKNgRRGSLTCNLTIHGVQGHVAY-PHLADNPVHRAAPMLN 212
Cdd:PRK07338 168 pASA------PLLAELAR--GKHAALTYEPALPD--GTLAGA-RKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAELAL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 213 ELVGIewdkgNEFFPPTSMQIANVkAGTGSNNVIPGDFFVQFNFRFSTELTDETIKARVVALLEKYNLRYTVDWWLSGQ- 291
Cdd:PRK07338 237 ALHAL-----NGQRDGVTVNVAKI-DGGGPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHGVSLHLHGGf 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 292 -----PFLTQRGKLVDAVVNAIEHYN-EIKPQllTTGGTSDGRFIARMGAQVVE-LGPVNATIHKINECVNAADLQLLAR 364
Cdd:PRK07338 311 grppkPIDAAQQRLFEAVQACGAALGlTIDWK--DSGGVCDGNNLAAAGLPVVDtLGVRGGNIHSEDEFVILDSLVERAQ 388
|
....*....
gi 1330962843 365 MYQRIMEQL 373
Cdd:PRK07338 389 LSALILMRL 397
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
6-106 |
2.35e-14 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 74.11 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 6 IELTQQLIRRPS---LSPDDAG-------CQAL-----MIERLraiGFTVERMDfgdtqNFwAWR---GQG-ETLAFAGH 66
Cdd:PRK07318 17 IEDLQELLRINSvrdDSKAKEGapfgpgpVKALekfleIAERD---GFKTKNVD-----NY-AGHieyGEGeEVLGILGH 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1330962843 67 TDVVPAGDAdrWINPPFEPTIRDGMLFGRGAADMKG-SLAA 106
Cdd:PRK07318 88 LDVVPAGDG--WDTDPYEPVIKDGKIYARGTSDDKGpTMAA 126
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
11-113 |
3.11e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 73.79 E-value: 3.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 11 QLIRRPSLSPD-------DAGCQALmIERLRAIGF-TVERMDFGDTQNFWAWR----GQGETLAFAgHTDVVPAGDADRW 78
Cdd:PRK07907 26 ELVRIPSVAADpfrreevARSAEWV-ADLLREAGFdDVRVVSADGAPAVIGTRpappGAPTVLLYA-HHDVQPPGDPDAW 103
|
90 100 110
....*....|....*....|....*....|....*
gi 1330962843 79 INPPFEPTIRDGMLFGRGAADMKGSLaAMVVAAER 113
Cdd:PRK07907 104 DSPPFELTERDGRLYGRGAADDKGGI-AMHLAALR 137
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
61-374 |
7.05e-14 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 72.50 E-value: 7.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 61 LAFAGHTDVVPAGdADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFliTSDEEASAHNG 140
Cdd:PRK08554 66 LLFMAHFDVVPVN-PEEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKEPLNGKVIFAF--TGDEEIGGAMA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 141 tVKVVEALMARNERLDYCLVGEPSSTEVV-------GDVVK--------NGRRGSLTCNLTIHGVQG-HVAY--PHLADN 202
Cdd:PRK08554 143 -MHIAEKLREEGKLPKYMINADGIGMKPIirrrkgfGVTIRvpsekvkvKGKLREQTFEIRTPVVETrHAAYflPGVDTH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 203 PVHRAAPMLNE-------LVGiEWDKGNEFfpPTSMQIANVKAGTGSN------------NVIP---------------- 247
Cdd:PRK08554 222 PLIAASHFLREsnvlavsLEG-KFLKGNVV--PGEVTLTYLEPGEGEEvevdlgltrllkAIVPlvrapikaekysdygv 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 248 -----------GDFFVQFNFR---FSTELTDETIKARVVALLEKYNLRYTVDwWLSGQPFLTQRGKLVDAVVNAIEHYNE 313
Cdd:PRK08554 299 sitpnvysfaeGKHVLKLDIRamsYSKEDIERTLKEVLEFNLPEAEVEIRTN-EKAGYLFTPPDEEIVKVALRVLKELGE 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330962843 314 iKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQLV 374
Cdd:PRK08554 378 -DAEPVEGPGASDSRYFTPYGVKAIDFGPKGGNIHGPNEYVEIDSLKKMPEVYKRIALRLL 437
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
58-160 |
7.98e-14 |
|
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: 72.38 E-value: 7.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 58 GETLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKG-SLAAMVVAAERFvaQHPNHKNRLAFLITSDEEaS 136
Cdd:cd05677 71 RKRILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGpLLAAIYAVAELF--QEGELDNDVVFLIEGEEE-S 147
|
90 100
....*....|....*....|....
gi 1330962843 137 AHNGTVKVVEALMARNERLDYCLV 160
Cdd:cd05677 148 GSPGFKEVLRKNKELIGDIDWILL 171
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
29-118 |
3.42e-12 |
|
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: 67.24 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 29 MIERLRAIGFTVERMDFGDTQNfwawrGQGE-------------------TLAFAGHTDVVPAGDADRWINPPFEPTIRD 89
Cdd:cd05676 42 AAERLEKLGFKVELVDIGTQTL-----PDGEelplppvllgrlgsdpskkTVLIYGHLDVQPAKLEDGWDTDPFELTEKD 116
|
90 100
....*....|....*....|....*....
gi 1330962843 90 GMLFGRGAADMKGSLAAMVVAAERFVAQH 118
Cdd:cd05676 117 GKLYGRGSTDDKGPVLGWLNAIEAYQKLG 145
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
10-276 |
7.22e-12 |
|
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: 66.04 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 10 QQLIRRPSLSP--DDAGCQALMIERLRAIGFTVER--------MDFG--DTQNFWAWRGQGE---TLAFAGHTDVVPAGD 74
Cdd:cd02697 10 QKLVRVPTDTPpgNNAPHAERTAALLQGFGFEAERhpvpeaevRAYGmeSITNLIVRRRYGDggrTVALNAHGDVVPPGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 75 AdrWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAHNGTVKVVEALMARNer 154
Cdd:cd02697 90 G--WTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGELGPGWLLRQGLTKP-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 155 lDYcLVGEPSSTEVVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELvgieWDKGNEFFPPTS---- 230
Cdd:cd02697 166 -DL-LIAAGFSYEVV-----TAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNAL----YALNAQYRQVSSqveg 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1330962843 231 -----MQIANVKAGTGSnNVIPGDFFVQFNFRFSTELTDETIKARVVALLE 276
Cdd:cd02697 235 ithpyLNVGRIEGGTNT-NVVPGKVTFKLDRRMIPEENPVEVEAEIRRVIA 284
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
58-139 |
3.88e-11 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 64.00 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 58 GETLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASA 137
Cdd:PRK08201 79 KPTVLIYGHYDVQPVDPLNLWETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKVEGTLPVNVKFCIEGEEEIGS 158
|
..
gi 1330962843 138 HN 139
Cdd:PRK08201 159 PN 160
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
56-215 |
1.01e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 62.85 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 56 GQGETLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNrLAFLITSDEEA 135
Cdd:PRK06446 60 GAKKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKHKLNVN-VKFLYEGEEEI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 136 SAHNgtvkvVEALMARNERL---DYCLV-GEPSSTEVVGDVVKnGRRGSLTCNLTIHGVQG--HVAYPHLADNPVHRAAP 209
Cdd:PRK06446 139 GSPN-----LEDFIEKNKNKlkaDSVIMeGAGLDPKGRPQIVL-GVKGLLYVELVLRTGTKdlHSSNAPIVRNPAWDLVK 212
|
....*.
gi 1330962843 210 MLNELV 215
Cdd:PRK06446 213 LLSTLV 218
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
11-371 |
1.05e-10 |
|
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: 62.47 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 11 QLIRRPSLSPDDAGCQALMIERLRAIGFTVERMDFGDTQNFWA------WRGQGE---TLAFAGHTDVVPAGDadrwINP 81
Cdd:cd05683 11 ELVQIDSETLHEKEISKVLKKKFENLGLSVIEDDAGKTTGGGAgnlictLKADKEevpKILFTSHMDTVTPGI----NVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 82 PfePTIRDGMLFGRG----AADMKGSLAAMVVAAERFVAQHPNHKnRLAFLITSDEEASahngtvkVVEALMARNERLD- 156
Cdd:cd05683 87 P--PQIADGYIYSDGttilGADDKAGIAAILEAIRVIKEKNIPHG-QIQFVITVGEESG-------LVGAKALDPELIDa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 157 ---YCLVGEpsstevvGDVvkngrrGSLTC--------NLTIHGVQGHVA-YPHLADNPVHRAAPMLNELvgiEWDKGNE 224
Cdd:cd05683 157 dygYALDSE-------GDV------GTIIVgaptqdkiNAKIYGKTAHAGtSPEKGISAINIAAKAISNM---KLGRIDE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 225 FfppTSMQIANVKAGTGSNnVIPGDFFVQFNFRfstELTDETIKARVVALLE-------KYNLRYTVDWWLSGQPF-LTQ 296
Cdd:cd05683 221 E---TTANIGKFQGGTATN-IVTDEVNIEAEAR---SLDEEKLDAQVKHMKEtfettakEKGAHAEVEVETSYPGFkINE 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330962843 297 RGKLVDAVVNAIEHYnEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIME 371
Cdd:cd05683 294 DEEVVKLAKRAANNL-GLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAVLVVEIIK 367
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
11-160 |
3.79e-10 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 61.07 E-value: 3.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 11 QLIRRPSLSPDDA---GCQA---LMIERLRAIGFTVER-------MDFGDTQnfwAWRGQGETLAFAGHTDVVPAGDADR 77
Cdd:PRK09104 25 ALLRIPSISTDPAyaaDCRKaadWLVADLASLGFEASVrdtpghpMVVAHHE---GPTGDAPHVLFYGHYDVQPVDPLDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 78 WINPPFEPTIRDG-----MLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEasahNGTVKVVEALMARN 152
Cdd:PRK09104 102 WESPPFEPRIKETpdgrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEE----SGSPSLVPFLEANA 177
|
170
....*....|
gi 1330962843 153 ERL--DYCLV 160
Cdd:PRK09104 178 EELkaDVALV 187
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
6-308 |
4.12e-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: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 6 IELTQQLIRRPSLSPDDAGCQALMIERLRAIGF-TVERMDFGDTQNFWAWRGQGETLAFAGHTDVVPAGDAdrwinpPFE 84
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGLgDVERDGRGNVVGRLRGTGGGPALLFSAHLDTVFPGDT------PAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAHNGTVKvvEALMARNERLDYCLVGEPS 164
Cdd:cd03896 75 VRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEGLGDLRGAR--YLLSAHGARLDYFVVAEGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 165 stevvGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELvgiewdkgNEFFPPTSMQIaNVKAGTG--- 241
Cdd:cd03896 153 -----DGVPHTGAVGSKRFRITTVGPGGHSYGAFGSPSAIVAMAKLVEAL--------YEWAAPYVPKT-TFAAIRGggg 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330962843 242 -SNNVIPGDFFVQFNFRF--STELTDetIKARVVALLEKYNLRYT-----VDWWLSGQPFLTQR-GKLVDAVVNAI 308
Cdd:cd03896 219 tSVNRIANLCSMYLDIRSnpDAELAD--VQREVEAVVSKLAAKHLrvkarVKPVGDRPGGEAQGtEPLVNAAVAAH 292
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
4-373 |
1.03e-09 |
|
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: 59.59 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 4 PVIELTQQLIRRPSL--SPDDAGCQALMIERLRAIGFTVERMDFgDTQNFWA---WRGQGETLA---FAGHTDVVPAGDa 75
Cdd:cd05646 3 PAVTRFREYLRINTVhpNPDYDACVEFLKRQADELGLPVRVIEV-VPGKPVVvltWEGSNPELPsilLNSHTDVVPVFE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 76 DRWINPPFEPTI-RDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAHNGTVKVVEALMARNER 154
Cdd:cd05646 81 EKWTHDPFSAHKdEDGNIYARGAQDMKCVGIQYLEAIRRLKASGFKPKRTIHLSFVPDEEIGGHDGMEKFVKTEEFKKLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 155 LDYCL-VGEPSSTEVVgdVVKNGRRGSLTCNLTIHGVQGHVA--YPHLADNPVHRAAPMLNELVGIEWD--KGNEFFPP- 228
Cdd:cd05646 161 VGFALdEGLASPTEEY--RVFYGERSPWWVVITAPGTPGHGSklLENTAGEKLRKVIESIMEFRESQKQrlKSNPNLTLg 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 229 --TSMQIANVKAGTgSNNVIPGDFFVQFNFRFSTELTDETIKARVvallekynlrytVDWWLSGQPFLT----QRGKLVD 302
Cdd:cd05646 239 dvTTVNLTMLKGGV-QMNVVPSEAEAGFDLRIPPTVDLEEFEKQI------------DEWCAEAGRGVTyefeQKSPEKD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 303 ------------AVVNAIEHYN-EIKPQLLTtgGTSDGRFIARMGAQVVELGPVNAT---IHKINECVNAADLQLLARMY 366
Cdd:cd05646 306 ptslddsnpwwaAFKKAVKEMGlKLKPEIFP--AATDSRYIRALGIPALGFSPMNNTpilLHDHNEFLNEDVFLRGIEIY 383
|
....*..
gi 1330962843 367 QRIMEQL 373
Cdd:cd05646 384 EKIIPAL 390
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
4-372 |
1.11e-09 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 59.64 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 4 PVIELTQQLIRRPSLSPDDAGCQ---ALMIERLRAIGFTVERMD----FGDtqNFWA-WRGQGE-TLAFAGHTDVV-PAG 73
Cdd:PRK06133 38 AYLDTLKELVSIESGSGDAEGLKqvaALLAERLKALGAKVERAPtppsAGD--MVVAtFKGTGKrRIMLIAHMDTVyLPG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 74 DADRwinPPFEptIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEASAhNGTVKVVEALMARNe 153
Cdd:PRK06133 116 MLAK---QPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGS-PGSRELIAELAAQH- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 154 rlDYCLVGEPSSTEvvgDVVKNGRRGSLTCNLTIHGVQGHV-AYPHLADNPVHRAAPMLNELVgiewDKGNEfFPPTSMQ 232
Cdd:PRK06133 189 --DVVFSCEPGRAK---DALTLATSGIATALLEVKGKASHAgAAPELGRNALYELAHQLLQLR----DLGDP-AKGTTLN 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 233 IANVKAGTgSNNVIPGDFFVQFNFRFS-TELTD-------ETIKARVVALLEkYNLRYTVdwwlsGQPFL--TQRGKLVD 302
Cdd:PRK06133 259 WTVAKAGT-NRNVIPASASAQADVRYLdPAEFDrleadlqEKVKNKLVPDTE-VTLRFER-----GRPPLeaNAASRALA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 303 AVVNAIehYNEI----KPQLLTTGGTSDGRFIARMG-AQVVE-LGPVNATIHKINECVN----AADLQLLARMyqrIMEQ 372
Cdd:PRK06133 332 EHAQGI--YGELgrrlEPIDMGTGGGTDAAFAAGSGkAAVLEgFGLVGFGAHSNDEYIElnsiVPRLYLLTRM---IMEL 406
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
56-249 |
1.22e-08 |
|
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, acetylornithine deacetylase (ArgE, Acetylornithinase, AO, N2-acetyl-L-ornithine amidohydrolase, EC 3.5.1.16)-related subfamily. Proteins in this subfamily have not yet been characterized, but have been predicted to have deacetylase activity. ArgE catalyzes the conversion of N-acetylornithine to ornithine, which can then be incorporated into the urea cycle for the final stage of arginine synthesis. The substrate specificity of ArgE is quite broad; several alpha-N-acyl-L-amino acids can be hydrolyzed, including alpha-N-acetylmethionine and alpha-N-formylmethionine. ArgE shares significant sequence homology and biochemical features, and possibly a common origin, with glutamate carboxypeptidase (CPG2) and succinyl-diaminopimelate desuccinylase (DapE), and aminoacylase I (ACY1), having all metal ligand binding residues conserved.
Pssm-ID: 349934 [Multi-domain] Cd Length: 423 Bit Score: 56.31 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 56 GQGETLAFAG-HTDVVPAgDADRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEE 134
Cdd:cd08012 75 VDGKTVSFVGsHMDVVTA-NPETWEFDPFSLSIDGDKLYGRGTTDCLGHVALVTELFRQLATEKPALKRTVVAVFIANEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 135 ASAHNGTvkVVEALMARNErLDYCLVGEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNEl 214
Cdd:cd08012 154 NSEIPGV--GVDALVKSGL-LDNLKSGPLYWVDSADSQPCIGTGGMVTWKLTATGKLFHSGLPHKAINALELVMEALAE- 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1330962843 215 vgIEWDKGNEFFP-----------PTSMQIANVKAGTGSNNVIPGD 249
Cdd:cd08012 230 --IQKRFYIDFPPhpkeevygfatPSTMKPTQWSYPGGSINQIPGE 273
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
105-311 |
1.76e-08 |
|
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; acylase I; amido acid deacylase; IAA-amino acid hydrolase; dehydropeptidase II; N-acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) subfamily. ACY1 is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. It is encoded by the aminoacylase 1 gene (Acy1) on chromosome 3p21 that comprises 15 exons. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney, suggest a role of the enzyme in amino acid metabolism of these organs. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D), resulting in a metabolic disorder manifesting encephalopathy and psychomotor delay.
Pssm-ID: 349882 [Multi-domain] Cd Length: 371 Bit Score: 55.68 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 105 AAMVVAAERFVAQHPNHKN-RLAFLITSDEEASAhnGTVKVVEALMARNERLDYCLvGEPSSTEV-VGDVVknGRRGSLT 182
Cdd:cd03886 94 TAMLLGAAKLLAERRDPLKgTVRFIFQPAEEGPG--GAKAMIEEGVLENPGVDAAF-GLHVWPGLpVGTVG--VRSGALM 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 183 C-----NLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIewdKGNEFFPPTS--MQIANVKAGTGsNNVIPGDFFVQFN 255
Cdd:cd03886 169 AsadefEITVKGKGGHGASPHLGVDPIVAAAQIVLALQTV---VSRELDPLEPavVTVGKFHAGTA-FNVIPDTAVLEGT 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 256 FRFSTELTDETIKARVVALLEK----YNLRYTVDwWLSGQPFLTQRGKLVDAVVNAIEHY 311
Cdd:cd03886 245 IRTFDPEVREALEARIKRLAEGiaaaYGATVELE-YGYGYPAVINDPELTELVREAAKEL 303
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
44-171 |
2.29e-07 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 52.55 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 44 DFGDTQNFWA-WRGQGE---TLAFAGHTDVVPAGDADRWINPPFEP-----TIRDGML--------------FGRGAADM 100
Cdd:COG4187 61 DPLGRKNVTAlVKGKGEskkTVILISHFDVVDVEDYGSLKPLAFDPeelteALKEIKLpedvrkdlesgewlFGRGTMDM 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330962843 101 KGSLAAMVVAAERFvAQHPNHKNRLAFLITSDEEASaHNGTVKVVEAL--MARNERLDY--CLVGEPSSTEVVGD 171
Cdd:COG4187 141 KAGLALHLALLEEA-SENEEFPGNLLLLAVPDEEVN-SAGMRAAVPLLaeLKEKYGLEYklAINSEPSFPKYPGD 213
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
27-310 |
6.55e-07 |
|
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: 50.81 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 27 ALMIERLRAIGFTVERmDFGDTQNFWAWRGQG---ETLAFAGHTDVVPAGDADRWinpPFEPTIrDGMLFGRGaadmKGS 103
Cdd:TIGR01891 23 SLIAEALESLGIEVRR-GVGGATGVVATIGGGkpgPVVALRADMDALPIQEQTDL---PYKSTN-PGVMHACG----HDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 104 LAAMVVAAERFVAQHPNH-KNRLAFLITSDEEAsaHNGTVKVVEA-LMarnERLDYCLVGEPSSTEVVGDVVKngRRGSL 181
Cdd:TIGR01891 94 HTAILLGTAKLLKKLADLlEGTVRLIFQPAEEG--GGGATKMIEDgVL---DDVDAILGLHPDPSIPAGTVGL--RPGTI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 182 T-----CNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIewdkgneffppTSMQIANVKAGT---------GSNNVIP 247
Cdd:TIGR01891 167 MaaadkFEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQI-----------VSRNVDPSRPAVvsvgiieagGAPNVIP 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330962843 248 GDFFVQFNFRFSTELTDETIKARVVALLE--------KYNLRytvdwWLSGQPFLTQRGKLVDAVVNAIEH 310
Cdd:TIGR01891 236 DKASMSGTVRSLDPEVRDQIIDRIERIVEgaaamygaKVELN-----YDRGLPAVTNDPALTQILKEVARH 301
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
180-323 |
8.22e-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: 50.36 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 180 SLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWDKGNeffpPTSMQIANVKAGTGSNNVIPGDFFVQFNFRFS 259
Cdd:cd08018 167 STFLEGTIKGKQAHGARPHLGINAIEAASAIVNAVNAIHLDPNI----PWSVKMTKLQAGGEATNIIPDKAKFALDLRAQ 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330962843 260 TELTDETIKARVVALLEK----YNLRYTVDwWLSGQPFLTQRGKLVDAVVNAI-EHYNE--IKPQLLTTGG 323
Cdd:cd08018 243 SNEAMEELKEKVEHAIEAaaalYGASIEIT-EKGGMPAAEYDEEAVELMEEAItEVLGEekLAGPCVTPGG 312
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
105-271 |
2.64e-06 |
|
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: 48.87 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 105 AAMVVAAERFVAQHPNHKNRLAFLITSDEEASAhnGTVKVVE-ALMARNERLDYCL----VGEPSSTevVGdvVKNGRRG 179
Cdd:cd05664 105 AALLGAARLLVEAKDAWSGTLIAVFQPAEETGG--GAQAMVDdGLYDKIPKPDVVLaqhvMPGPAGT--VG--TRPGRFL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 180 SLTCNL--TIHGVQGHVAYPHLADNPVHRAAPMLNELVGIewdKGNEFFP--PTSMQIANVKAGTgSNNVIPGDFFVQFN 255
Cdd:cd05664 179 SAADSLdiTIFGRGGHGSMPHLTIDPVVMAASIVTRLQTI---VSREVDPqeFAVVTVGSIQAGS-AENIIPDEAELKLN 254
|
170
....*....|....*.
gi 1330962843 256 FRFSTELTDETIKARV 271
Cdd:cd05664 255 VRTFDPEVREKVLNAI 270
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
92-255 |
4.92e-06 |
|
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine utilization protein, RocB; arginine degradation protein, RocB) subfamily. This group of proteins is possibly related to acetylornithine deacetylase (ArgE) and may be involved in the arginine and/or ornithine degradation pathway. In Bacillus subtilis, RocB is one of the three genes found in the rocABC operon, which is sigma L dependent and induced by arginine. The function of members of this family is as yet unknown, although they are predicted as deacetylases.
Pssm-ID: 349905 Cd Length: 534 Bit Score: 48.49 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 92 LFGRGAADMKGSLAAMVVAAERFVAQHPNHKNrLAFLITSDEEaSAHNGTVKVVEAL--MARNERLDY--CLVGEPSSTE 167
Cdd:cd05654 126 LFGRGTMDMKSGLAVHLALLEQASEDEDFDGN-LLLMAVPDEE-VNSRGMRAAVPALleLKKKHDLEYklAINSEPIFPQ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 168 VVGDVVK---NGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPMLNElvgIEW-------DKGNEFFPPTSMQIANVK 237
Cdd:cd05654 204 YDGDQTRyiyTGSIGKILPGFLCYGKETHVGEPFAGINANLMASEITAR---LELnadlcekVEGEITPPPVCLKQKDLK 280
|
170
....*....|....*....
gi 1330962843 238 AgtgSNNV-IPGDFFVQFN 255
Cdd:cd05654 281 E---SYSVqTPVRAVAYFN 296
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
177-311 |
2.48e-05 |
|
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: 45.88 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 177 RRGSLTCN-----LTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIewdkGNEFFPPTSMQ---IANVKAGTgSNNVIPG 248
Cdd:COG1473 175 RPGPIMAAadsfeITIKGKGGHAAAPHLGIDPIVAAAQIVTALQTI----VSRNVDPLDPAvvtVGIIHGGT-APNVIPD 249
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330962843 249 DFFVQFNFRFSTELTDETIKARVVALLEK----YNLRYTVDwWLSGQPFLTQRGKLVDAVVNAIEHY 311
Cdd:COG1473 250 EAELEGTVRTFDPEVRELLEERIERIAEGiaaaYGATAEVE-YLRGYPPTVNDPELTELAREAAREV 315
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
29-113 |
4.64e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 45.29 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 29 MIERLRAIGFTVERMDFGDTQN---FWAWRGQGE---TLAFAGHTDVVPaGDADRWINP--PFEPTIRDGMLFGRGAADM 100
Cdd:PRK07079 50 IAPALAALGFTCRIVDNPVAGGgpfLIAERIEDDalpTVLIYGHGDVVR-GYDEQWREGlsPWTLTEEGDRWYGRGTADN 128
|
90
....*....|....*...
gi 1330962843 101 KG----SLAAM-VVAAER 113
Cdd:PRK07079 129 KGqhtiNLAALeQVLAAR 146
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
79-211 |
5.73e-05 |
|
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.
Pssm-ID: 349927 [Multi-domain] Cd Length: 466 Bit Score: 44.78 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 79 INPPFEPTIRdgmLFGRGAADMKGSLAAMVVAAERFVAQHPNHKNRLAFLITSDEEAsahnGTVKVVEALMARNERL--D 156
Cdd:cd05678 106 IFSNLDPEWR---VFARAAADDKGPIMMMLAALDALKAGGIAPKFNVKIILDSEEEK----GSPSLPKAVKEYKELLaaD 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 157 YCLVGEPSSTEVVGDVVKNGRRGSLTCNLTIHGVQ-----GHvaYPHLADNPVHRAAPML 211
Cdd:cd05678 179 ALIIMDGPAHATNKPTLTFGCRGIATATLTTYGAKvpqhsGH--YGNYAPNPAFRLSSLL 236
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
184-285 |
8.96e-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: 41.09 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 184 NLTIHGVQGHVAYPHLADNPVHRAAPMLNELVGIEWDKGNeffPPTS--MQIANVKAGTgSNNVIPGDFFVQFNFRFSTE 261
Cdd:cd05670 176 HIDFIGKSGHAAYPHNANDMVVAAANFVTQLQTIVSRNVD---PIDGavVTIGKIHAGT-ARNVIAGTAHLEGTIRTLTQ 251
|
90 100
....*....|....*....|....*...
gi 1330962843 262 LTDETIKARVVALLE----KYNLRYTVD 285
Cdd:cd05670 252 EMMELVKQRVRDIAEgielAFDCEVKVD 279
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
58-138 |
2.01e-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. This family includes dapE (Lpg0809) from Legionella pneumophila.
Pssm-ID: 349931 [Multi-domain] Cd Length: 451 Bit Score: 40.01 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 58 GETLAFAGHTDVVPAGDADRWINPPFEPTIRDGMLFGRGAAD----MKGSLAAmVVAAERFVAQHPnhknRLAFLITSDE 133
Cdd:cd05682 73 DDTVLLYGHMDKQPPFTGWDEGLGPTKPVIRGDKLYGRGGADdgyaIFASLTA-IKALQEQGIPHP----RCVVLIEACE 147
|
....*.
gi 1330962843 134 EA-SAH 138
Cdd:cd05682 148 ESgSAD 153
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
6-309 |
2.64e-03 |
|
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and Aminoacylase 1-like protein 2 (ACY1L2). Aminoacylase 1 proteins are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. ACY1 (acyl-L-amino-acid amidohydrolase; EC 3.5.1.14) is the most abundant of the aminoacylases, a class of zinc binding homodimeric enzymes involved in 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 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. ACY1L2 family contains many uncharacterized proteins predicted as amidohydrolases, including gene products of abgA and abgB that catalyze the cleavage of p-aminobenzoyl-glutamate, a folate catabolite in E. coli, to p-aminobenzoate and glutamate. p-Aminobenzoyl-glutamate utilization is catalyzed by the abg region gene product, AbgT. Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D) resulting in a metabolic disorder manifesting with encephalopathy and psychomotor delay.
Pssm-ID: 349945 [Multi-domain] Cd Length: 366 Bit Score: 39.53 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 6 IELTQQLIRRPSLSPDDAGCQALMIERLRAIGFTVERMDfGDTQNFWAWRGQGET---LAFAGHTDVVPAGDADRWinpP 82
Cdd:cd08660 2 INIRRDIHEHPELGFEEVETSKKIRRWLEEEQIEILDVP-QLKTGVIAEIKGGEDgpvIAIRADIDALPIQEQTNL---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 83 FEPTIRdgmlfGRGAADMKGSLAAMVVAAERFVAQHPNH-KNRLAFLITSDEEASAhnGTVKVVEALMARNerLDYCLVG 161
Cdd:cd08660 78 FASKVD-----GT*HACGHDFHTTSIIGTA*LLNQRRAElKGTVVFIFQPAEEGAA--GARKVLEAGVLNG--VSAIFGI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 162 EPSSTEVVGDVvkNGRRGSLTC-----NLTIHGVQGHVAYPHLADNPVHRAAPM---LNELVGIEWDKGNEffppTSMQI 233
Cdd:cd08660 149 HNKPDLPVGTI--GVKEGPL*AsvdvfEIVIKGKGGHASIPNNSIDPIAAAGQIisgLQSVVSRNISSLQN----AVVSI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 234 ANVKAGTgSNNVIPGDFFVQFNFRFSTELTDETIKARVVALLEK----YNLRYTVDWWLSGQPFLTQRGKLVDAVVNAIE 309
Cdd:cd08660 223 TRVQGGT-AWNVIPDQAE*EGTVRAFTKEARQAVPEH*RRVAEGiaagYGCQAEFKWFPNGPSEVQNDGTLLNAFSKAAA 301
|
|
| M20_dipept_like |
cd05679 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
9-107 |
4.68e-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: 349928 [Multi-domain] Cd Length: 448 Bit Score: 39.02 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330962843 9 TQQLIRRPSLSpddAGCQALMIERLRAIGFTVERMD---FGDTQNFWAWR---GQGETLAFAGHTDVVPAGDAdRWIN-- 80
Cdd:cd05679 20 SQEPARKPELR---AYLDQEMRPRFERLGFTVHIHDnpvAGRAPFLIAERiedPSLPTLLIYGHGDVVPGYEG-RWRDgr 95
|
90 100 110
....*....|....*....|....*....|.
gi 1330962843 81 PPFEPTIRDGMLFGRGAADMKG----SLAAM 107
Cdd:cd05679 96 DPWTVTVWGERWYGRGTADNKGqhsiNMAAL 126
|
|
| |
