|
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: 762.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 2 SCPVIELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIEHMDFGDTQNFWAWRGR-GETLAFAGHTDVVPAGDVDRWIN 80
Cdd:PRK13009 1 MSDVLELAQDLIRRPSVTPDDAGCQDLLAERLEALGFTCERMDFGDVKNLWARRGTeGPHLCFAGHTDVVPPGDLEAWTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNGTVKVVEALMARNERLDYCLV 160
Cdd:PRK13009 81 PPFEPTIRDGMLYGRGAADMKGSLAAFVVAAERFVAAHPDHKGSIAFLITSDEEGPAINGTVKVLEWLKARGEKIDYCIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 161 GEPSSTEIVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRGNDFFPATSMQVANIQAGT 240
Cdd:PRK13009 161 GEPTSTERLGDVIKNGRRGSLTGKLTVKGVQGHVAYPHLADNPIHLAAPALAELAATEWDEGNEFFPPTSLQITNIDAGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 241 GSNNVIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRYTVDWWLSGQPFLTARGKLVDAVVNAIEHYNEIKPQLLT 320
Cdd:PRK13009 241 GATNVIPGELEAQFNFRFSTEHTAESLKARVEAILDKHGLDYTLEWTLSGEPFLTPPGKLVDAVVAAIEAVTGITPELST 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 447200569 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: 685.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 6 IELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIEHMDFGDTQNFWAWRG-RGETLAFAGHTDVVPAGDVDRWINPPFE 84
Cdd:cd03891 1 LELAKELIRRPSVTPDDAGAQDLIAERLKALGFTCERLEFGGVKNLWARRGtGGPHLCFAGHTDVVPPGDLEGWSSDPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNGTVKVVEALMARNERLDYCLVGEPS 164
Cdd:cd03891 81 PTIKDGMLYGRGAADMKGGIAAFVAAAERFVAKHPNHKGSISFLITSDEEGPAIDGTKKVLEWLKARGEKIDYCIVGEPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 165 STEIVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRGNDFFPATSMQVANIQAGTGSNN 244
Cdd:cd03891 161 SEKKLGDTIKIGRRGSLNGKLTIKGKQGHVAYPHLADNPIHLLAPILAELTATVLDEGNEFFPPSSLQITNIDVGNGATN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 245 VIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRYTVDWWLSGQPFLTARGKLVDAVVNAIEHYNEIKPQLLTTGGT 324
Cdd:cd03891 241 VIPGELKAKFNIRFNDEHTGESLKARIEAILDKHGLDYDLEWKLSGEPFLTKPGKLVDAVSAAIKEVTGITPELSTSGGT 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 447200569 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: 625.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 5 VIELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIEHMDFGDTQNFWAWRGRGE-TLAFAGHTDVVPAGDVDRWINPPF 83
Cdd:TIGR01246 1 VTELAKELISRPSVTPNDAGCQDIIAERLEKLGFEIEWMHFGDTKNLWATRGTGEpVLAFAGHTDVVPAGPEEQWSSPPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 84 EPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNGTVKVVEALMARNERLDYCLVGEP 163
Cdd:TIGR01246 81 EPVERDGKLYGRGAADMKGSLAAFIVAAERFVKKNPDHKGSISLLITSDEEGTAIDGTKKVVETLMARDELIDYCIVGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 164 SSTEIVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRGNDFFPATSMQVANIQAGTGSN 243
Cdd:TIGR01246 161 SSVKKLGDVIKNGRRGSITGNLTIKGIQGHVAYPHLANNPIHKAAPALAELTAIKWDEGNEFFPPTSLQITNIHAGTGAN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 244 NVIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRYTVDWWLSGQPFLTARGKLVDAVVNAIEHYNEIKPQLLTTGG 323
Cdd:TIGR01246 241 NVIPGELYVQFNLRFSTEVSDEILKQRVEAILDQHGLDYDLEWSLSGEPFLTNDGKLIDKAREAIEETNGIKPELSTGGG 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 447200569 324 TSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQL 373
Cdd:TIGR01246 321 TSDGRFIALMGAEVVEFGPVNATIHKVNECVSIEDLEKLSDVYQDLLENL 370
|
|
| ArgE |
COG0624 |
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
5-375 |
2.78e-126 |
|
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: 368.44 E-value: 2.78e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 5 VIELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIEHMDF-GDTQNFWAWR---GRGETLAFAGHTDVVPAGDVDRWIN 80
Cdd:COG0624 14 ALELLRELVRIPSVSGEEAAAAELLAELLEALGFEVERLEVpPGRPNLVARRpgdGGGPTLLLYGHLDVVPPGDLELWTS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAkNGTVKVVEALmARNERLDYCLV 160
Cdd:COG0624 94 DPFEPTIEDGRLYGRGAADMKGGLAAMLAALRALLAAGLRLPGNVTLLFTGDEEVGS-PGARALVEEL-AEGLKADAAIV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 161 GEPSSTeivgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWD-RGNDFFPATSMQVANIQAG 239
Cdd:COG0624 172 GEPTGV----PTIVTGHKGSLRFELTVRGKAAHSSRPELGVNAIEALARALAALRDLEFDgRADPLFGRTTLNVTGIEGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 240 TGSnNVIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQ--LRYTVDWWL-SGQPFLT-ARGKLVDAVVNAIEHYNEIK 315
Cdd:COG0624 248 TAV-NVIPDEAEAKVDIRLLPGEDPEEVLAALRALLAAAApgVEVEVEVLGdGRPPFETpPDSPLVAAARAAIREVTGKE 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447200569 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 |
4.92e-114 |
|
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: 336.19 E-value: 4.92e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 7 ELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIEHMDFGDTQNFWAWRG--RGETLAFAGHTDVVPAGDVDRWINPPFE 84
Cdd:cd08659 1 SLLQDLVQIPSVNPPEAEVAEYLAELLAKRGYGIESTIVEGRGNLVATVGggDGPVLLLNGHIDTVPPGDGDKWSFPPFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASaKNGTVKVVEALMArnERLDYCLVGEPS 164
Cdd:cd08659 81 GRIRDGRLYGRGACDMKGGLAAMVAALIELKEAGALLGGRVALLATVDEEVG-SDGARALLEAGYA--DRLDALIVGEPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 165 steivGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRG-NDFFPATSMQVANIQAGTGSn 243
Cdd:cd08659 158 -----GLDVVYAHKGSLWLRVTVHGKAAHSSMPELGVNAIYALADFLAELRTLFEELPaHPLLGPPTLNVGVINGGTQV- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 244 NVIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRYTVDWWLSGQP--FLTARGKLVDAVVNAIEHYNeIKPQLLTT 321
Cdd:cd08659 232 NSIPDEATLRVDIRLVPGETNEGVIARLEAILEEHEAKLTVEVSLDGDPpfFTDPDHPLVQALQAAARALG-GDPVVRPF 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 447200569 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 |
8.46e-87 |
|
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases.
Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 264.98 E-value: 8.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 62 AFAGHTDVVPAGDVDRWinpPFEPTIrDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHhRGRLAFLITSDEEaSAKNGT 141
Cdd:pfam01546 1 LLRGHMDVVPDEETWGW---PFKSTE-DGKLYGRGHDDMKGGLLAALEALRALKEEGLK-KGTVKLLFQPDEE-GGMGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 142 VKVVEALMARNERLDYCL---VGEPSSTE-IVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAI 217
Cdd:pfam01546 75 RALIEDGLLEREKVDAVFglhIGEPTLLEgGIAIGVVTGHRGSLRFRVTVKGKGGHASTPHLGVNAIVAAARLILALQDI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 218 EWDRGNDFFPA--TSMQVANIQAGTgsnNVIPGELFVQFNFRFSTELTDEMIKERVHALLEK----HQLRYTVDWWLSGQ 291
Cdd:pfam01546 155 VSRNVDPLDPAvvTVGNITGIPGGV---NVIPGEAELKGDIRLLPGEDLEELEERIREILEAiaaaYGVKVEVEYVEGGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 292 PFLTARGKLVDAVVNAIEHYNEIKPQLLTTG--GTSDGRFIA-RMGAQVVELGPVNATIHKINECVNAADLQLLARMYQR 368
Cdd:pfam01546 232 PPLVNDSPLVAALREAAKELFGLKVELIVSGsmGGTDAAFFLlGVPPTVVFFGPGSGLAHSPNEYVDLDDLEKGAKVLAR 311
|
....
gi 447200569 369 IMEQ 372
Cdd:pfam01546 312 LLLK 315
|
|
| DapE-ArgE |
TIGR01910 |
acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase; This group of sequences ... |
6-352 |
1.38e-53 |
|
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: 181.44 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 6 IELTQQLIRRPSLSP---DDAGCQALMIERLRKIGFTIEHMDFGDTQNFWAWR--------GRGETLAFAGHTDVVPAGD 74
Cdd:TIGR01910 1 VELLKDLISIPSVNPpggNEETIANYIKDLLREFGFSTDVIEITDDRLKVLGKvvvkepgnGNEKSLIFNGHYDVVPAGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 75 VDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEaSAKNGTVKVVEALMARNEr 154
Cdd:TIGR01910 81 LELWKTDPFKPVEKDGKLYGRGATDMKGGLVALLYALKAIREAGIKPNGNIILQSVVDEE-SGEAGTLYLLQRGYFKDA- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 155 lDYCLVGEPSSteivGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRGNDFFPATSMQVA 234
Cdd:TIGR01910 159 -DGVLIPEPSG----GDNIVIGHKGSIWFKLRVKGKQAHASFPQFGVNAIMKLAKLITELNELEEHIYARNSYGFIPGPI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 235 NIQAGT--GSNNV--IPGELFVQFNFRFSTELTDEMIKERVHAL---LEKHQ---LRYTVDWWLSGQPFLTARGKLVDAV 304
Cdd:TIGR01910 234 TFNPGVikGGDWVnsVPDYCEFSIDVRIIPEENLDEVKQIIEDVvkaLSKSDgwlYENEPVVKWSGPNETPPDSRLVKAL 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 447200569 305 VNAIEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGP-VNATIHKINE 352
Cdd:TIGR01910 314 EAIIKKVRGIEPEVLVSTGGTDARFLRKAGIPSIVYGPgDLETAHQVNE 362
|
|
| M20_ArgE |
cd03894 |
M20 Peptidase acetylornithine deacetylase; Peptidase M20 family, acetylornithine deacetylase ... |
7-371 |
3.01e-50 |
|
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: 172.39 E-value: 3.01e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 7 ELTQQLIRRPSLSPddAGCQALmIE----RLRKIGFTIEHMDFGDTQ--NFWAWRG--RGETLAFAGHTDVVPAgDVDRW 78
Cdd:cd03894 1 ELLARLVAFDTVSR--NSNLAL-IEyvadYLAALGVKSRRVPVPEGGkaNLLATLGpgGEGGLLLSGHTDVVPV-DGQKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 79 INPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPhhRGRLAFLITSDEEASAKnGTVKVVEALMARNERLDYC 158
Cdd:cd03894 77 SSDPFTLTERDGRLYGRGTCDMKGFLAAVLAAVPRLLAAKL--RKPLHLAFSYDEEVGCL-GVRHLIAALAARGGRPDAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 159 LVGEPSSTEIVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELV--AIEWDRG--NDFF--PATSMQ 232
Cdd:cd03894 154 IVGEPTSLQPV-----VAHKGIASYRIRVRGRAAHSSLPPLGVNAIEAAARLIGKLRelADRLAPGlrDPPFdpPYPTLN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 233 VANIQAGTGSnNVIPGELFVQFNFRF----STELTDEMIKERVHALLEKHQLRYTVDWWLSGQPFLTARGklvDAVVNAI 308
Cdd:cd03894 229 VGLIHGGNAV-NIVPAECEFEFEFRPlpgeDPEAIDARLRDYAEALLEFPEAGIEVEPLFEVPGLETDED---APLVRLA 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447200569 309 EHYNEIKPQLLTTGGTsDGRFIARMGAQVVELGPVN-ATIHKINECVNAADLQLLARMYQRIME 371
Cdd:cd03894 305 AALAGDNKVRTVAYGT-EAGLFQRAGIPTVVCGPGSiAQAHTPDEFVELEQLDRCEEFLRRLIA 367
|
|
| PRK08651 |
PRK08651 |
succinyl-diaminopimelate desuccinylase; Reviewed |
5-375 |
7.52e-48 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 236323 [Multi-domain] Cd Length: 394 Bit Score: 166.70 E-value: 7.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 5 VIELTQQLIRRPSLSP---DDAGCQALMIERLRKIGFTIEHMDFGDT---------QNFWAWRGRGET-LAFAGHTDVVP 71
Cdd:PRK08651 8 IVEFLKDLIKIPTVNPpgeNYEEIAEFLRDTLEELGFSTEIIEVPNEyvkkhdgprPNLIARRGSGNPhLHFNGHYDVVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 72 AGDVDRwINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFvaqHPHHRGRLAFLITSDEEaSAKNGTVKVVEALMAr 151
Cdd:PRK08651 88 PGEGWS-VNVPFEPKVKDGKVYGRGASDMKGGIAALLAAFERL---DPAGDGNIELAIVPDEE-TGGTGTGYLVEEGKV- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 152 neRLDYCLVGEPSSTEIVGdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRGNDFF----- 226
Cdd:PRK08651 162 --TPDYVIVGEPSGLDNIC----IGHRGLVWGVVKVYGKQAHASTPWLGINAFEAAAKIAERLKSSLSTIKSKYEydder 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 227 ---PATSMQVANIQAGTgSNNVIPGELFVQFNFRFSTELTDEMIKERVHALLE----KHQLRYTVDWWLSGQPFLTARG- 298
Cdd:PRK08651 236 gakPTVTLGGPTVEGGT-KTNIVPGYCAFSIDRRLIPEETAEEVRDELEALLDevapELGIEVEFEITPFSEAFVTDPDs 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447200569 299 KLVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGP-VNATIHKINECVNAADLQLLARMYQRIMEQLVA 375
Cdd:PRK08651 315 ELVKALREAIREVLGVEPKKTISLGGTDARFFGAKGIPTVVYGPgELELAHAPDEYVEVKDVEKAAKVYEEVLKRLAK 392
|
|
| PRK08588 |
PRK08588 |
succinyl-diaminopimelate desuccinylase; Reviewed |
61-372 |
8.16e-40 |
|
succinyl-diaminopimelate desuccinylase; Reviewed
Pssm-ID: 181490 [Multi-domain] Cd Length: 377 Bit Score: 145.03 E-value: 8.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 61 LAFAGHTDVVPAGDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ-HPHHrGRLAFLITSDEEaSAKN 139
Cdd:PRK08588 62 LALSGHMDVVAAGDVDKWTYDPFELTEKDGKLYGRGATDMKSGLAALVIAMIELKEQgQLLN-GTIRLLATAGEE-VGEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 140 GTVKVVEALMARNerLDYCLVGEPSSTEIVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAI-- 217
Cdd:PRK08588 140 GAKQLTEKGYADD--LDALIIGEPSGHGIV-----YAHKGSMDYKVTSTGKAAHSSMPELGVNAIDPLLEFYNEQKEYfd 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 218 EWDRGNDFFPATSMQVANIQAGTGSNNvIPGELFVQFNFRFSTELTDEMIKERVHALLEK------HQLRYTVDwwLSGQ 291
Cdd:PRK08588 213 SIKKHNPYLGGLTHVVTIINGGEQVNS-VPDEAELEFNIRTIPEYDNDQVISLLQEIINEvnqngaAQLSLDIY--SNHR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 292 PFLTAR-GKLVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGA--QVVELGP-VNATIHKINECVNAADLQLLARMYQ 367
Cdd:PRK08588 290 PVASDKdSKLVQLAKDVAKSYVGQDIPLSAIPGATDASSFLKKKPdfPVIIFGPgNNLTAHQVDEYVEKDMYLKFIDIYK 369
|
....*
gi 447200569 368 RIMEQ 372
Cdd:PRK08588 370 EIIIQ 374
|
|
| M20_ArgE_DapE-like |
cd08011 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-370 |
7.15e-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: 142.14 E-value: 7.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 6 IELTQQLIRRPSLSPDDAG---CQALMIERLRKIGFTIEHMDF-----GDTQNFWAWRGrGETLAFAGHTDVVPAGDVDR 77
Cdd:cd08011 1 VKLLQELVQIPSPNPPGDNtsaIAAYIKLLLEDLGYPVELHEPpeeiyGVVSNIVGGRK-GKRLLFNGHYDVVPAGDGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 78 WINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNGTVKVVEALMARNerlDY 157
Cdd:cd08011 80 WTVDPYSGKIKDGKLYGRGSSDMKGGIAASIIAVARLADAKAPWDLPVVLTFVPDEETGGRAGTKYLLEKVRIKP---ND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 158 CLVGEPSSTeivgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEwdrgndffpaTSMQVANIQ 237
Cdd:cd08011 157 VLIGEPSGS----DNIRIGEKGLVWVIIEITGKPAHGSLPHRGESAVKAAMKLIERLYELE----------KTVNPGVIK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 238 AGTgSNNVIPGELFVQFNFRFSTELTDEMIKERVHALLEK-HQLRYTVDWWLSGqPFLTARGKLVDAVVNAIEHYNEIKP 316
Cdd:cd08011 223 GGV-KVNLVPDYCEFSVDIRLPPGISTDEVLSRIIDHLDSiEEVSFEIKSFYSP-TVSNPDSEIVKKTEEAITEVLGIRP 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 447200569 317 QLLTTGGTSDGRFIARMGAQVVELGPVN-ATIHKINECVNAADLQLLARMYQRIM 370
Cdd:cd08011 301 KEVISVGASDARFYRNAGIPAIVYGPGRlGQMHAPNEYVEIDELIKVIKVHALVA 355
|
|
| M20_CPDG2 |
cd03885 |
M20 Peptidase Glutamate carboxypeptidase, a periplasmic enzyme; Peptidase M20 family, ... |
28-365 |
2.30e-35 |
|
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: 132.71 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 28 LMIERLRKIGFTIE---HMDFGDTQNF-WAWRGRGETLaFAGHTDVV-PAGDVDRWinpPFepTIRDGMLFGRGAADMKG 102
Cdd:cd03885 27 LLAEELEALGFTVErrpLGEFGDHLIAtFKGTGGKRVL-LIGHMDTVfPEGTLAFR---PF--TVDGDRAYGPGVADMKG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 103 SLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKnGTVKVVEALmARNErlDYCLVGEPSSTeivGDVVKNGRRGSLT 182
Cdd:cd03885 101 GLVVILHALKALKAAGGRDYLPITVLLNSDEEIGSP-GSRELIEEE-AKGA--DYVLVFEPARA---DGNLVTARKGIGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 183 CNLTIHGVQGHV-AYPHLADNPVHRAAPFLNELVAIewdrgNDFFPATSMQVANIQAGTGSnNVIPGELFVQFNFRFSTE 261
Cdd:cd03885 174 FRLTVKGRAAHAgNAPEKGRSAIYELAHQVLALHAL-----TDPEKGTTVNVGVISGGTRV-NVVPDHAEAQVDVRFATA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 262 LTDEMIKERVHALLEKHQL---RYTVDWWLSGQPFLTARG--KLVDAVVNAiehYNEIKPQLLT--TGGTSDGRFIARMG 334
Cdd:cd03885 248 EEADRVEEALRAIVATTLVpgtSVELTGGLNRPPMEETPAsrRLLARAQEI---AAELGLTLDWeaTGGGSDANFTAALG 324
|
330 340 350
....*....|....*....|....*....|....*.
gi 447200569 335 AQVVE-LGPVNATIHKINECVNAADL----QLLARM 365
Cdd:cd03885 325 VPTLDgLGPVGGGAHTEDEYLELDSLvpriKLLARL 360
|
|
| PRK07522 |
PRK07522 |
acetylornithine deacetylase; Provisional |
65-375 |
2.52e-35 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236039 [Multi-domain] Cd Length: 385 Bit Score: 133.01 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 65 GHTDVVPAgDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ---HPHHrgrLAFliTSDEEAsaknGT 141
Cdd:PRK07522 71 GHTDVVPV-DGQAWTSDPFRLTERDGRLYGRGTCDMKGFIAAALAAVPELAAAplrRPLH---LAF--SYDEEV----GC 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 142 VKV---VEALMARNERLDYCLVGEPSSTEIVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAI- 217
Cdd:PRK07522 141 LGVpsmIARLPERGVKPAGCIVGEPTSMRPV-----VGHKGKAAYRCTVRGRAAHSSLAPQGVNAIEYAARLIAHLRDLa 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 218 ----EWDRGNDFF--PATSMQVANIQAGTgSNNVIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLrytvdwwlsgq 291
Cdd:PRK07522 216 drlaAPGPFDALFdpPYSTLQTGTIQGGT-ALNIVPAECEFDFEFRNLPGDDPEAILARIRAYAEAELL----------- 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 292 PFLTARGKLVDAVVNAIEHYneikPQLLT-------------TG---------GTSDGRFiARMGAQVVELGPVN-ATIH 348
Cdd:PRK07522 284 PEMRAVHPEAAIEFEPLSAY----PGLDTaedaaaarlvralTGdndlrkvayGTEAGLF-QRAGIPTVVCGPGSiEQAH 358
|
330 340
....*....|....*....|....*..
gi 447200569 349 KINECVNAADLQLLARMYQRIMEQLVA 375
Cdd:PRK07522 359 KPDEFVELAQLAACEAFLRRLLASLAA 385
|
|
| M20_ArgE_LysK |
cd05653 |
M20 Peptidase acetylornithine deacetylase/acetyl-lysine deacetylase; Peptidase M20 family, ... |
5-373 |
3.33e-35 |
|
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: 131.71 E-value: 3.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 5 VIELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIEHMDFGdtqNFWAWRGRGE-TLAFAGHTDVVPaGDVdrwinppf 83
Cdd:cd05653 3 AVELLLDLLSIYSPSGEEARAAKFLEEIMKELGLEAWVDEAG---NAVGGAGSGPpDVLLLGHIDTVP-GEI-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 84 EPTIRDGMLFGRGAADMKGSLAAMVVAAerfVAQHPHHRGRLAFLITSDEEASAKnGTvkvvEALMARNERLDYCLVGEP 163
Cdd:cd05653 71 PVRVEGGVLYGRGAVDAKGPLAAMILAA---SALNEELGARVVVAGLVDEEGSSK-GA----RELVRRGPRPDYIIIGEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 164 SSTEivGDVVknGRRGSLTCNLTIHGVQGHVAYPhlADNPVHRAAPFLNELVAI--EWDRGNdfFPATSMQVANIQAGTg 241
Cdd:cd05653 143 SGWD--GITL--GYRGSLLVKIRCEGRSGHSSSP--ERNAAEDLIKKWLEVKKWaeGYNVGG--RDFDSVVPTLIKGGE- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 242 SNNVIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRYTVDwwlsGQPFLTA-RGKLVDAVVNAIEHYNeIKPQLLT 320
Cdd:cd05653 214 SSNGLPQRAEATIDLRLPPRLSPEEAIALATALLPTCELEFIDD----TEPVKVSkNNPLARAFRRAIRKQG-GKPRLKR 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 447200569 321 TGGTSDGRFIA-RMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRIMEQL 373
Cdd:cd05653 289 KTGTSDMNVLApLWTVPIVAYGPGDSTLdHTPNEHIELAEIERAAAVLKGALEEL 343
|
|
| PRK13004 |
PRK13004 |
YgeY family selenium metabolism-linked hydrolase; |
5-375 |
5.30e-35 |
|
YgeY family selenium metabolism-linked hydrolase;
Pssm-ID: 183836 [Multi-domain] Cd Length: 399 Bit Score: 132.37 E-value: 5.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 5 VIELTQQLIRRPSLSPDDAGCQALMIERLRKIGF---TIEHMDfgdtqNFWAWRGRGETL-AFAGHTDVVPAGDVDRWIN 80
Cdd:PRK13004 17 MTRFLRDLIRIPSESGDEKRVVKRIKEEMEKVGFdkvEIDPMG-----NVLGYIGHGKKLiAFDAHIDTVGIGDIKNWDF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 81 PPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEasakngtvkVVEALMAR------NER 154
Cdd:PRK13004 92 DPFEGEEDDGRIYGRGTSDQKGGMASMVYAAKIIKDLGLDDEYTLYVTGTVQEE---------DCDGLCWRyiieedKIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 155 LDYCLVGEPSSTEIvgdvvKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRGND-FFPATSMQV 233
Cdd:PRK13004 163 PDFVVITEPTDLNI-----YRGQRGRMEIRVETKGVSCHGSAPERGDNAIYKMAPILNELEELNPNLKEDpFLGKGTLTV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 234 ANIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRYTVDWW------LSGQPFLTAR---------- 297
Cdd:PRK13004 238 SDIFSTSPSRCAVPDSCAISIDRRLTVGETWESVLAEIRALPAVKKANAKVSMYnydrpsYTGLVYPTECyfptwlyped 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 298 GKLVDAVVNAIEHYNEIKPQL----LTTGGTSdgrfIA-RMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRIME 371
Cdd:PRK13004 318 HEFVKAAVEAYKGLFGKAPEVdkwtFSTNGVS----IAgRAGIPTIGFGPGKEPLaHAPNEYTWKEQLVKAAAMYAAIPK 393
|
....
gi 447200569 372 QLVA 375
Cdd:PRK13004 394 SLLK 397
|
|
| M20_ArgE_DapE-like |
cd05651 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-282 |
4.55e-34 |
|
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: 128.58 E-value: 4.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 5 VIELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIEHMDfgdtQNFWAWRGRGE----TLAFAGHTDVVP--AGdvdrW 78
Cdd:cd05651 2 AIELLKSLIATPSFSREEHKTADLIENYLEQKGIPFKRKG----NNVWAENGHFDegkpTLLLNSHHDTVKpnAG----W 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 79 INPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPhHRGRLAFLITSDEEASAKNGtvkvVEALMARNERLDYC 158
Cdd:cd05651 74 TKDPFEPVEKGGKLYGLGSNDAGASVVSLLATFLHLYSEGP-LNYNLIYAASAEEEISGKNG----IESLLPHLPPLDLA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 159 LVGEPSSTEivgdvVKNGRRGSLTCNLTIHGVQGHVAYPHlADNPVHRAAPFLNELVAIEWDRGNDFFPATSMQVANIQA 238
Cdd:cd05651 149 IVGEPTEMQ-----PAIAEKGLLVLDCTARGKAGHAARNE-GDNAIYKALDDIQWLRDFRFDKVSPLLGPVKMTVTQINA 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 447200569 239 GTgSNNVIPGE----LFVQFNFRFSTELTDEMIKERVHALLEKHQLRY 282
Cdd:cd05651 223 GT-QHNVVPDSctfvVDIRTTEAYTNEEIFEIIRGNLKSEIKPRSFRL 269
|
|
| PRK13013 |
PRK13013 |
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein; |
5-364 |
5.31e-34 |
|
acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase family protein;
Pssm-ID: 237268 [Multi-domain] Cd Length: 427 Bit Score: 130.26 E-value: 5.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 5 VIELTQQLIRRPSLSPDDAG---CQALMIERLRKIGFTIE----HMDFGDTQNFWAW--------RGRGETLAFAGHTDV 69
Cdd:PRK13013 16 LVALTQDLIRIPTLNPPGRAyreICEFLAARLAPRGFEVEliraEGAPGDSETYPRWnlvarrqgARDGDCVHFNSHHDV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 70 VPAGDvdRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNGTVKVVEALM 149
Cdd:PRK13013 96 VEVGH--GWTRDPFGGEVKDGRIYGRGACDMKGGLAASIIAAEAFLAVYPDFAGSIEISGTADEESGGFGGVAYLAEQGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 150 ARNERLDYCLVGEPSSTeivgDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNElvaIEwdrgNDFFPA- 228
Cdd:PRK13013 174 FSPDRVQHVIIPEPLNK----DRICLGHRGVWWAEVETRGRIAHGSMPFLGDSAIRHMGAVLAE---IE----ERLFPLl 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 229 ----TSMQVA---------NIQAGTGSNNV------------IPGELFVQFNFRFSTELTDEMIKERVHALLEK-----H 278
Cdd:PRK13013 243 atrrTAMPVVpegarqstlNINSIHGGEPEqdpdytglpapcVADRCRIVIDRRFLIEEDLDEVKAEITALLERlkrarP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 279 QLRYTVDWWLSGQPFLTARGK-LVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGA--QVVELGP-VNATIHKINECV 354
Cdd:PRK13013 323 GFAYEIRDLFEVLPTMTDRDApVVRSVAAAIERVLGRQADYVVSPGTYDQKHIDRIGKlkNCIAYGPgILDLAHQPDEWV 402
|
410
....*....|
gi 447200569 355 NAADLQLLAR 364
Cdd:PRK13013 403 GIADMVDSAK 412
|
|
| M20_ArgE_DapE-like |
cd03895 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
7-364 |
2.09e-31 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349890 [Multi-domain] Cd Length: 400 Bit Score: 122.80 E-value: 2.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 7 ELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIE-----------HMDFGDtqNFWAWRGR-------------GETLA 62
Cdd:cd03895 1 AFLQDLVRFPSLRGEEAAAQDLVAAALRSRGYTVDrweidveklkhHPGFSP--VAVDYAGApnvvgthrprgetGRSLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 63 FAGHTDVVPAGDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEaSAKNGTV 142
Cdd:cd03895 79 LNGHIDVVPEGPVELWTRPPFEATIVDGWMYGRGAGDMKAGLAANLFALDALRAAGLQPAADVHFQSVVEEE-CTGNGAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 143 kvveALMARNERLDYCLVGEPSSTEIVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIE--W- 219
Cdd:cd03895 158 ----AALMRGYRADAALIPEPTELKLV-----RAQVGVIWFRVKVRGTPAHVAEASEGVNAIEKAMHLIQALQELEreWn 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 220 -----DRGNDFFP-ATSMQVANIQAGTGSNNViPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRytvDWWLSGQPF 293
Cdd:cd03895 229 arkksHPHFSDHPhPINFNIGKIEGGDWPSSV-PAWCVLDCRIGIYPGESPEEARREIEECVADAAAT---DPWLSNHPP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 294 -------------LTARGKLVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGA-QVVELGPVNATIHKINECVNAADL 359
Cdd:cd03895 305 evewngfqaegyvLEPGSDAEQVLAAAHQAVFGTPPVQSAMTATTDGRFFVLYGDiPALCYGPGSRDAHGFDESVDLESL 384
|
....*
gi 447200569 360 QLLAR 364
Cdd:cd03895 385 RKITK 389
|
|
| M20_DapE_actinobac |
cd05647 |
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; ... |
5-368 |
7.85e-30 |
|
M20 Peptidase actinobacterial DapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase; Peptidase M20 family, actinobacterial dapE encoded N-succinyl-L,L-diaminopimelic acid desuccinylase (DapE) subfamily. This group is composed of predominantly actinobacterial DapE proteins. DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. It has been shown that DapE is essential for cell growth and proliferation. DapEs have been purified from proteobacteria such as Escherichia coli and Haemophilus influenzae, while genes that encode for DapEs have been sequenced from several bacterial sources such as the actinobacteria Corynebacterium glutamicum and Mycobacterium tuberculosis. DapE is a small, dimeric enzyme (41.6 kDa per subunit) that requires 2 atoms of zinc per molecule of polypeptide for full enzymatic activity. All of the amino acids that function as metal binding ligands are strictly conserved in DapE.
Pssm-ID: 349899 [Multi-domain] Cd Length: 347 Bit Score: 117.54 E-value: 7.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 5 VIELTQQLIRRPSLSPDDA-----------GCQALMIERlrkigftiehmdFGDTQNFWAWRGRGETLAFAGHTDVVP-A 72
Cdd:cd05647 1 PIELTAALVDIPSVSGNEKpiadeieaalrTLPHLEVIR------------DGNTVVARTERGLASRVILAGHLDTVPvA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 73 GDV-DRWINppfeptirDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRgrLAFLITSDEE-ASAKNGTVKVVEALma 150
Cdd:cd05647 69 GNLpSRVEE--------DGVLYGCGATDMKAGDAVQLKLAATLAAATLKHD--LTLIFYDCEEvAAELNGLGRLAEEH-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 151 rNERL--DYCLVGEPSSTEIVGdvvknGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDR----GND 224
Cdd:cd05647 137 -PEWLaaDFAVLGEPTDGTIEG-----GCQGTLRFKVTTHGVRAHSARSWLGENAIHKLAPILARLAAYEPRTvnidGLT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 225 FFPATSmqvANIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRYTV-DWWLSGQPFLT---ARGkL 300
Cdd:cd05647 211 YREGLN---AVFISGGVAGNVIPDEARVNLNYRFAPDKSLAEAIAHVREVFEGLGYEIEVtDLSPGALPGLDhpvARD-L 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447200569 301 VDAVvnaiehYNEIKPQLlttGGTSDGRFiARMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQR 368
Cdd:cd05647 287 IEAV------GGKVRAKY---GWTDVARF-SALGIPAVNFGPGDPLLaHKRDEQVPVEQITACAAILRR 345
|
|
| M20_ArgE_DapE-like |
cd05650 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-370 |
1.15e-29 |
|
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: 117.94 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 5 VIELTQQLIRRPSLSPDDAG------CQALMiERLRKIGF-TIEHMDFGDTQNFW-------AWRGRGETLAFAGHTDVV 70
Cdd:cd05650 3 IIELERDLIRIPAVNPESGGegekekADYLE-KKLREYGFyTLERYDAPDERGIIrpnivakIPGGNDKTLWIISHLDTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 71 PAGDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQH--PHHRGRLAFLitSDEEASAKNGTVKVVEAL 148
Cdd:cd05650 82 PPGDLSLWETDPWEPVVKDGKIYGRGVEDNQQGIVSSLLALKAIIKNGitPKYNFGLLFV--ADEEDGSEYGIQYLLNKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 149 -MARNErlDYCLVgePSSTEIVGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPF---LNELVAIEWDRGND 224
Cdd:cd05650 160 dLFKKD--DLIIV--PDFGTEDGEFIEIAEKSILWIKVNVKGKQCHASTPENGINAFVAASNFaleLDELLHEKFDEKDD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 225 FF--PATSMQVANIQAGTGSNNVIPGELFVQFNFRF--STELTD--EMIKERVHALLEKHQLRYTVDWWLSGQ--PFLTA 296
Cdd:cd05650 236 LFnpPYSTFEPTKKEANVPNVNTIPGYDVFYFDCRVlpTYKLDEvlKFVNKIISDFENSYGAGITYEIVQKEQapPATPE 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447200569 297 RGKLVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIM 370
Cdd:cd05650 316 DSEIVVRLSKAIKKVRGREAKLIGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYIRISHIVKDAKVFAEML 389
|
|
| M20_ArgE_DapE-like_fungal |
cd05652 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
5-279 |
3.64e-29 |
|
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: 115.45 E-value: 3.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 5 VIELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIE--HMDFGDTQNFWAWRG--RGETLAFAGHTDVVPagdvdrwin 80
Cdd:cd05652 1 LLSLHKSLVEIPSISGNEAAVGDFLAEYLESLGFTVEkqPVENKDRFNVYAYPGssRQPRVLLTSHIDTVP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 81 P--PFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEasakNGTVKVVEALMARNERLDYC 158
Cdd:cd05652 72 PfiPYSISDGGDTIYGRGSVDAKGSVAAQIIAVEELLAEGEVPEGDLGLLFVVGEE----TGGDGMKAFNDLGLNTWDAV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 159 LVGEPssTEivGDVVKnGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRgNDFFPATSMQVANIQA 238
Cdd:cd05652 148 IFGEP--TE--LKLAS-GHKGMLGFKLTAKGKAGHSGYPWLGISAIEILVEALVKLIDADLPS-SELLGPTTLNIGRISG 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 447200569 239 GTGSnNVIPGELFVQFNFRFSTEltDEMIKERVHALLEKHQ 279
Cdd:cd05652 222 GVAA-NVVPAAAEASVAIRLAAG--PPEVKDIVKEAVAGIL 259
|
|
| M20_dimer |
pfam07687 |
Peptidase dimerization domain; This domain consists of 4 beta strands and two alpha helices ... |
175-283 |
8.76e-29 |
|
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: 107.82 E-value: 8.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 175 NGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRGNdFFPATSMQVANIQAGTgSNNVIPGELFVQF 254
Cdd:pfam07687 1 IGHKGLAGGHLTVKGKAGHSGAPGKGVNAIKLLARLLAELPAEYGDIGF-DFPRTTLNITGIEGGT-ATNVIPAEAEAKF 78
|
90 100
....*....|....*....|....*....
gi 447200569 255 NFRFSTELTDEMIKERVHALLEKHQLRYT 283
Cdd:pfam07687 79 DIRLLPGEDLEELLEEIEAILEKELPEGE 107
|
|
| PRK06837 |
PRK06837 |
ArgE/DapE family deacylase; |
6-221 |
9.44e-28 |
|
ArgE/DapE family deacylase;
Pssm-ID: 180721 [Multi-domain] Cd Length: 427 Bit Score: 113.17 E-value: 9.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 6 IELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIE--HMDFGDTQNF-----WAW------------RGRGET---LAF 63
Cdd:PRK06837 23 VAFTQDLVRFPSTRGAEAPCQDFLARAFRERGYEVDrwSIDPDDLKSHpgagpVEIdysgapnvvgtyRPAGKTgrsLIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 64 AGHTDVVPAGDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVA--AERFVAQHPHHRgrlAFLITSDEEASAKNGt 141
Cdd:PRK06837 103 QGHIDVVPEGPLDLWSRPPFDPVIVDGWMYGRGAADMKAGLAAMLFAldALRAAGLAPAAR---VHFQSVIEEESTGNG- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 142 vkvveALMA--RNERLDYCLVGEPSSTEIVGDVVkngrrGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNEL--VAI 217
Cdd:PRK06837 179 -----ALSTlqRGYRADACLIPEPTGEKLVRAQV-----GVIWFRLRVRGAPVHVREAGTGANAIDAAYHLIQALreLEA 248
|
....
gi 447200569 218 EWDR 221
Cdd:PRK06837 249 EWNA 252
|
|
| M20_ArgE_DapE-like |
cd05649 |
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
6-274 |
7.79e-27 |
|
M20 Peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate desuccinylases; Peptidase M20 family, uncharacterized protein subfamily with similarity to acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) subfamily. This group includes the hypothetical protein ygeY from Escherichia coli, a putative deacetylase, but many in this subfamily are classified as unassigned peptidases. ArgE/DapE enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this subfamily are mostly bacterial and archaeal, and have been inferred by homology as being related to both ArgE and DapE.
Pssm-ID: 349900 [Multi-domain] Cd Length: 381 Bit Score: 109.82 E-value: 7.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 6 IELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIEHMD-FGdtqNFWAWRGRGET-LAFAGHTDVVPAGDVDRWINPPF 83
Cdd:cd05649 1 TRFLRDLIQIPSESGEEKGVVERIEEEMEKLGFDEVEIDpMG---NVIGYIGGGKKkILFDGHIDTVGIGNIDNWKFDPY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 84 EPTIRDGMLFGRGAADMKGSLAAMVVAAERFvaqhpHHRGRLAFlitSDEEASAknGTV--KVVEALMAR------NERL 155
Cdd:cd05649 78 EGYETDGKIYGRGTSDQKGGLASMVYAAKIM-----KDLGLRDF---AYTILVA--GTVqeEDCDGVCWQyiskadKIKP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 156 DYCLVGEPSSTEIvgdvvKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRGND-FFPATSMQVA 234
Cdd:cd05649 148 DFVVSGEPTDGNI-----YRGQRGRMEIRVDTKGVSCHGSAPERGDNAVYKMADIIQDIRQLNPNFPEApFLGRGTLTVT 222
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 447200569 235 NIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKERVHAL 274
Cdd:cd05649 223 DIFSTSPSRCAVPDSCRISIDRRLTVGETWEGCLEEIRAL 262
|
|
| PRK13983 |
PRK13983 |
M20 family metallo-hydrolase; |
5-370 |
4.62e-26 |
|
M20 family metallo-hydrolase;
Pssm-ID: 237578 [Multi-domain] Cd Length: 400 Bit Score: 108.01 E-value: 4.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 5 VIELTQQLIRRPSLSPDDAG------CQALMiERLRKIGFT-IEHMDFGDTQNFWAWR--------GRGE--TLAFAGHT 67
Cdd:PRK13983 7 MIELLSELIAIPAVNPDFGGegekekAEYLE-SLLKEYGFDeVERYDAPDPRVIEGVRpnivakipGGDGkrTLWIISHM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 68 DVVPAGDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNGtvkvVEA 147
Cdd:PRK13983 86 DVVPPGDLSLWETDPFKPVVKDGKIYGRGSEDNGQGIVSSLLALKALMDLGIRPKYNLGLAFVSDEETGSKYG----IQY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 148 LMARNERL----DYCLV---GEPSsteivGDVVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELvaiewD 220
Cdd:PRK13983 162 LLKKHPELfkkdDLILVpdaGNPD-----GSFIEIAEKSILWLKFTVKGKQCHASTPENGINAHRAAADFALEL-----D 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 221 RG--------NDFF--PATSMQ-------VANIqagtgsnNVIPGElfVQFNF------RFSTELTDEMIKERVHALLEK 277
Cdd:PRK13983 232 EAlhekfnakDPLFdpPYSTFEptkkeanVDNI-------NTIPGR--DVFYFdcrvlpDYDLDEVLKDIKEIADEFEEE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 278 HQLRYTVDWWLSGQ--PFLTARGKLVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVN 355
Cdd:PRK13983 303 YGVKIEVEIVQREQapPPTPPDSEIVKKLKRAIKEVRGIEPKVGGIGGGTVAAFLRKKGYPAVVWSTLDETAHQPNEYAK 382
|
410
....*....|....*
gi 447200569 356 AADLQLLARMYQRIM 370
Cdd:PRK13983 383 ISNLIEDAKVFALLL 397
|
|
| M20_Dipept_like |
cd03893 |
M20 Dipeptidases; Peptidase M20 family, dipeptidase-like subfamily. This group contains a ... |
33-359 |
7.21e-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: 7.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 33 LRKIGFTIEHMDFGDTQNF-WAWRGRGE---TLAFAGHTDVVPAGDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMV 108
Cdd:cd03893 34 LRRLGFTVEIVDTSNGAPVvFAEFPGAPgapTVLLYGHYDVQPAGDEDGWDSDPFELTERDGRLYGRGAADDKGPILAHL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 109 VAAERFVAQHPHHRGRLAFLITSDEEAsaknGTVKVVEALMARNERL--DYCLVGEPSSTEIVGDVVKNGRRGSLTCNLT 186
Cdd:cd03893 114 AALRALMQQGGDLPVNVKFIIEGEEES----GSPSLDQLVEAHRDLLaaDAIVISDSTWVGQEQPTLTYGLRGNANFDVE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 187 I----HGV--------------------------QGHVAYPHLADNP------VHRAAPFLNELVA-IEWDRGND----- 224
Cdd:cd03893 190 VkgldHDLhsglyggvvpdpmtalaqllaslrdeTGRILVPGLYDAVrelpeeEFRLDAGVLEEVEiIGGTTGSVaerlw 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 225 FFPATSMQ-VANIQAGTGSNNVIPGELfvqfNFRFSTELTDEMIKERVHALLEKH-------QLRYTVDWWLSGQPFLT- 295
Cdd:cd03893 270 TRPALTVLgIDGGFPGEGSKTVIPPRA----RAKISIRLVPGQDPEEASRLLEAHlekhapsGAKVTVSYVEGGMPWRSd 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447200569 296 ARGKLVDAVVNAIEHYNEIKPQLLTTGGT--SDGRFIARMGAQVVELGPVNAT--IHKINECVNAADL 359
Cdd:cd03893 346 PSDPAYQAAKDALRTAYGVEPPLTREGGSipFISVLQEFPQAPVLLIGVGDPDdnAHSPNESLRLGNY 413
|
|
| M20_PepV |
cd03888 |
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, ... |
5-366 |
3.02e-25 |
|
M20 Peptidase Xaa-His dipeptidase (PepV) degrades hydrophobic dipeptides; Peptidase M20 family, Peptidase V (Xaa-His dipeptidase; PepV g.p. (Lactobacillus lactis); X-His dipeptidase; beta-Ala-His dipeptidase; carnosinase) subfamily. The PepV group of proteins is widely distributed in lactic acid bacteria. PepV, along with PepT, functions at the end of the proteolytic processing system. PepV is a monomeric metalloenzyme that preferentially degrades hydrophobic dipeptides. The Streptococcus gordonii PepV gene is homologous to the PepV gene family from Lactobacillus and Lactococcus spp. PepV recognizes and fixes the dipeptide backbone, while the side chains are not specifically probed and can vary, rendering it a nonspecific dipeptidase. It has been shown that Lactococcus lactis subspecies lactis (L9) PepV does not hydrolyze dipeptides containing Pro or D-amino acids at the C-terminus, while PepV from Lactobaccilus has been shown to have L-carnosine hydrolyzing activity. The mammalian PepV also acts on anserine and homocarnosine (but not on homoanserine), and to a lesser extent on some other aminoacyl-L-histidine dipeptides. Also included is the Staphylococcus aureus metallopeptidase, Sapep, a Mn(2+)-dependent dipeptidase where large interdomain movements could potentially regulate the activity of this enzyme.
Pssm-ID: 349884 [Multi-domain] Cd Length: 449 Bit Score: 106.18 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 5 VIELTQQLIRRPS-LSPDDAGC-------QAL--MIERLRKIGFT-------IEHMDFGDtqnfwawrgRGETLAFAGHT 67
Cdd:cd03888 10 ILEDLKELVAIPSvRDEATEGApfgegprKALdkFLDLAKRLGFKtknidnyAGYAEYGE---------GEEVLGILGHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 68 DVVPAGDvdRWINPPFEPTIRDGMLFGRGAADMKG-SLAA-------------------MVVAA---------ERFVAQH 118
Cdd:cd03888 81 DVVPAGE--GWTTDPFKPVIKDGKLYGRGTIDDKGpTIAAlyalkilkdlglplkkkirLIFGTdeetgwkciEHYFEHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 119 PH----------------HRGRLAFLITSDEeasaKNGTVKVVEAL---MARNERLDYC-LVGEPSSTEIVGDVVKNGRR 178
Cdd:cd03888 159 EYpdfgftpdaefpvingEKGIVTVDLTFKI----DDDKGYRLISIkggEATNMVPDKAeAVIPGKDKEELALSAATDLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 179 GSLTCN-----LTIHGVQGHVAYPHLADNPVHRAAPFLNELV-------AIEW--------DRGNDFFPATSMQV----- 233
Cdd:cd03888 235 GNIEIDdggveLTVTGKSAHASAPEKGVNAITLLAKFLAELNkdgndkdFIKFlaknlhedYNGKKLGINFEDEVmgelt 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 234 ANIqagtGSNNVIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRYTVDwwLSGQPFLTAR-GKLVDAVVNAIEHYN 312
Cdd:cd03888 315 LNP----GIITLDDGKLELGLNVRYPVGTSAEDIIKQIEEALEKYGVEVEGH--KHQKPLYVPKdSPLVKTLLKVYEEQT 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 447200569 313 EIKPQLLTTGGTSDGRFIARMgaqvVELGP----VNATIHKINECVNAADLQLLARMY 366
Cdd:cd03888 389 GKEGEPVAIGGGTYARELPNG----VAFGPefpgQKDTMHQANEFIPIDDLIKALAIY 442
|
|
| PRK06915 |
PRK06915 |
peptidase; |
6-193 |
4.64e-25 |
|
peptidase;
Pssm-ID: 180745 [Multi-domain] Cd Length: 422 Bit Score: 105.16 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 6 IELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTI-----------EH-------MDFGDTQNFWA-WRGRGE--TLAFA 64
Cdd:PRK06915 20 VKLLKRLIQEKSVSGDESGAQAIVIEKLRELGLDLdiwepsfkklkDHpyfvsprTSFSDSPNIVAtLKGSGGgkSMILN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 65 GHTDVVPAGDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEaSAKNGTVKV 144
Cdd:PRK06915 100 GHIDVVPEGDVNQWDHHPYSGEVIGGRIYGRGTTDMKGGNVALLLAMEALIESGIELKGDVIFQSVIEEE-SGGAGTLAA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447200569 145 VEalmaRNERLDYCLVGEPSSTEIvgdVVKngRRGSLTCNLTIHGVQGH 193
Cdd:PRK06915 179 IL----RGYKADGAIIPEPTNMKF---FPK--QQGSMWFRLHVKGKAAH 218
|
|
| M20_yscS_like |
cd05675 |
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, ... |
8-368 |
1.57e-24 |
|
M20 Peptidase, carboxypeptidase yscS-like; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, carboxypeptidase S, carboxypeptidase a, carboxypeptidase yscS, glycine carboxypeptidase)-like subfamily. This group contains proteins that have been uncharacterized to date with similarity to vacuolar proteins involved in nitrogen metabolism which are essential for use of certain peptides that are sole nitrogen sources. YscS releases a C-terminal amino acid from a peptide that has glycine as the penultimate residue. It is synthesized as one polypeptide chain precursor which yields two active precursor molecules after carbohydrate modification in the secretory pathway. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble. Enzymes in this subfamily may also cleave intracellularly generated peptides in order to recycle amino acids for protein synthesis.
Pssm-ID: 349924 [Multi-domain] Cd Length: 431 Bit Score: 103.98 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 8 LTQQLIRRPSLSPDDAGCQA-----LMIERLRKIGFTIEHMDFGDTQnfwawrGRGETLA-------------FAGHTDV 69
Cdd:cd05675 3 LLQELIRIDTTNSGDGTGSEtraaeVLAARLAEAGIQTEIFVVESHP------GRANLVAriggtdpsagpllLLGHIDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 70 VPAgDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNGTVKVVEALM 149
Cdd:cd05675 77 VPA-DASDWSVDPFSGEIKDGYVYGRGAVDMKNMAAMMLAVLRHYKREGFKPKRDLVFAFVADEEAGGENGAKWLVDNHP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 150 ARNERLDYCL--VGEPSSTEIVGDV---VKNGRRGSLTCNLTIHGVQGHVAYPHlADNPVHRAAPFLNELVAIEWD-RGN 223
Cdd:cd05675 156 ELFDGATFALneGGGGSLPVGKGRRlypIQVAEKGIAWMKLTVRGRAGHGSRPT-DDNAITRLAEALRRLGAHNFPvRLT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 224 D-------------------FFPATSMQVANIQAGTGSN----------------------NVIPGELFVQFNFRFSTEL 262
Cdd:cd05675 235 DetayfaqmaelaggeggalMLTAVPVLDPALAKLGPSApllnamlrntasptmldagyatNVLPGRATAEVDCRILPGQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 263 TDEMIKERVHALLEKhqlrYTVDW-WLSGQPFL--TARGKLVDAVVNAIEHYN---EIKPQLLTtgGTSDGRFIARMGAQ 336
Cdd:cd05675 315 SEEEVLDTLDKLLGD----PDVSVeAVHLEPATesPLDSPLVDAMEAAVQAVDpgaPVVPYMSP--GGTDAKYFRRLGIP 388
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 447200569 337 VVELGPVNAT--------IHKINECVNAADLQLLARMYQR 368
Cdd:cd05675 389 GYGFAPLFLPpeldytglFHGVDERVPVESLYFGVRFLDR 428
|
|
| PRK00466 |
PRK00466 |
acetyl-lysine deacetylase; Validated |
56-373 |
1.10e-23 |
|
acetyl-lysine deacetylase; Validated
Pssm-ID: 166979 [Multi-domain] Cd Length: 346 Bit Score: 100.24 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 56 GRGETLaFAGHTDVVPAGdvdrwinppFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFvaqhpHHRG-RLAFLITSDEE 134
Cdd:PRK00466 59 GEGDIL-LASHVDTVPGY---------IEPKIEGEVIYGRGAVDAKGPLISMIIAAWLL-----NEKGiKVMVSGLADEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 135 asaknGTVKVVEALMARNERLDYCLVGEPSSTEivgDVVKnGRRGSLTCNLTIHGVQGHVAYPhlADNPVHRAAPFLnel 214
Cdd:PRK00466 124 -----STSIGAKELVSKGFNFKHIIVGEPSNGT---DIVV-EYRGSIQLDIMCEGTPEHSSSA--KSNLIVDISKKI--- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 215 vaIEWDRGNDFFPATSMQVANIQAGTgSNNVIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRyTVDwwlSGQPFL 294
Cdd:PRK00466 190 --IEVYKQPENYDKPSIVPTIIRAGE-SYNVTPAKLYLHFDVRYAINNKRDDLISEIKDKFQECGLK-IVD---ETPPVK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 295 TA-RGKLVDAVVNAIEHYNeIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATI-HKINECVNAADLQLLARMYQRIMEQ 372
Cdd:PRK00466 263 VSiNNPVVKALMRALLKQN-IKPRLVRKAGTSDMNILQKITTSIATYGPGNSMLeHTNQEKITLDEIYIAVKTYMLAIEE 341
|
.
gi 447200569 373 L 373
Cdd:PRK00466 342 L 342
|
|
| M20_18_42 |
cd18669 |
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
55-176 |
1.17e-23 |
|
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: 97.12 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 55 RGRGETLAFAGHTDVVPAGDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEE 134
Cdd:cd18669 9 GGGGKRVLLGAHIDVVPAGEGDPRDPPFFVDTVEEGRLYGRGALDDKGGVAAALEALKLLKENGFKLKGTVVVAFTPDEE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 447200569 135 ASAKNGTVKVVEALMARNERLDYCLVGEPSSTEIVGDVVKNG 176
Cdd:cd18669 89 VGSGAGKGLLSKDALEEDLKVDYLFVGDATPAPQKGVGIRTP 130
|
|
| PRK08262 |
PRK08262 |
M20 family peptidase; |
54-373 |
7.05e-22 |
|
M20 family peptidase;
Pssm-ID: 236208 [Multi-domain] Cd Length: 486 Bit Score: 96.55 E-value: 7.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 54 WRGRGETLA---FAGHTDVVPA--GDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQ--HPHHRGRLA 126
Cdd:PRK08262 104 WKGSDPSLKpivLMAHQDVVPVapGTEGDWTHPPFSGVIADGYVWGRGALDDKGSLVAILEAAEALLAQgfQPRRTIYLA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 127 FliTSDEEASAKnGTVKVVEALMARNERLDyCLVGEpsSTEIVGDVVKN----------GRRGSLTCNLTIHGVQGHVAY 196
Cdd:PRK08262 184 F--GHDEEVGGL-GARAIAELLKERGVRLA-FVLDE--GGAITEGVLPGvkkpvaligvAEKGYATLELTARATGGHSSM 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 197 P--------------HLADNP------------VHRAAP---FLNELV-AIEWdrgnDFFPATSMQVANIQAG------- 239
Cdd:PRK08262 258 PprqtaigrlaraltRLEDNPlpmrlrgpvaemFDTLAPemsFAQRVVlANLW----LFEPLLLRVLAKSPETaamlrtt 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 240 ------TGSN--NVIPGELFVQFNFRFSTELTDEMIKERVHALLekHQLRYTVDW-----------WLSGQPFltargKL 300
Cdd:PRK08262 334 taptmlKGSPkdNVLPQRATATVNFRILPGDSVESVLAHVRRAV--ADDRVEIEVlggnsepspvsSTDSAAY-----KL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 301 VDAVVnaiehyNEIKPQL-----LTTGGTsDGRFIARMGAQVVELGPVNAT------IHKINECVNAADLQLLARMYQRI 369
Cdd:PRK08262 407 LAATI------REVFPDVvvapyLVVGAT-DSRHYSGISDNVYRFSPLRLSpedlarFHGTNERISVANYARMIRFYYRL 479
|
....
gi 447200569 370 MEQL 373
Cdd:PRK08262 480 IENA 483
|
|
| M20_ArgE_DapE-like |
cd08013 |
M20 peptidases with similarity to acetylornithine deacetylases and succinyl-diaminopimelate ... |
56-372 |
1.77e-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: 91.77 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 56 GRGETLAFAGHTDVVpagDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPhhRGRLAFLITSDEEa 135
Cdd:cd08013 66 GGGKSLMLNGHIDTV---TLDGYDGDPLSGEIADGRVYGRGTLDMKGGLAACMAALADAKEAGL--RGDVILAAVADEE- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 136 SAKNGTvkvvEALMARNERLDYCLVGEPSSTEIVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELV 215
Cdd:cd08013 140 DASLGT----QEVLAAGWRADAAIVTEPTNLQII-----HAHKGFVWFEVDIHGRAAHGSRPDLGVDAILKAGYFLVALE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 216 A----IEWDRGNDFFPATSMQVANIQAGTGSNNViPGELFVQFNFRFSTELTDEMIKERVHALLEK-----HQLRYTV-D 285
Cdd:cd08013 211 EyqqeLPERPVDPLLGRASVHASLIKGGEEPSSY-PARCTLTIERRTIPGETDESVLAELTAILGElaqtvPNFSYREpR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 286 WWLSGQPFLTARGK-LVDAVVNAIEHYNEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLAR 364
Cdd:cd08013 290 ITLSRPPFEVPKEHpFVQLVAAHAAKVLGEAPQIRSETFWTDAALLAEAGIPSVVFGPSGAGLHAKEEWVDVESIRQLRE 369
|
....*...
gi 447200569 365 MYQRIMEQ 372
Cdd:cd08013 370 VLSAVVRE 377
|
|
| PRK08737 |
PRK08737 |
acetylornithine deacetylase; Provisional |
37-370 |
2.53e-20 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 181544 [Multi-domain] Cd Length: 364 Bit Score: 91.03 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 37 GFTIEHMDFGD-TQNFWAWRGRGETLaFAGHTDVVPagDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERfv 115
Cdd:PRK08737 42 GFQVEVIDHGAgAVSLYAVRGTPKYL-FNVHLDTVP--DSPHWSADPHVMRRTDDRVIGLGVCDIKGAAAALLAAANA-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 116 aqhphHRGRLAFLITSDEEAsaknGTVKVVEALMARNERLDYCLVGEPSSTEIVgdvvkNGRRGSLTCNLTIHGVQGHVA 195
Cdd:PRK08737 117 -----GDGDAAFLFSSDEEA----NDPRCVAAFLARGIPYEAVLVAEPTMSEAV-----LAHRGISSVLMRFAGRAGHAS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 196 YPH-LADNPVHRAAPFLNElvAIEWDRGND---FFPATSMQ--VANIQAGTGSNNVIPgELFVQFNFRFSTELTDEMIKE 269
Cdd:PRK08737 183 GKQdPSASALHQAMRWGGQ--ALDHVESLAharFGGLTGLRfnIGRVEGGIKANMIAP-AAELRFGFRPLPSMDVDGLLA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 270 RVHALLEKHQLRYTVDWWLSGQP---FLTARGKLVDA----------VVNAIEHYNEikPQLLTTGGTSdgrfiarmgaq 336
Cdd:PRK08737 260 TFAGFAEPAAATFEETFRGPSLPsgdIARAEERRLAArdvadaldlpIGNAVDFWTE--ASLFSAAGYT----------- 326
|
330 340 350
....*....|....*....|....*....|....*
gi 447200569 337 VVELGPVN-ATIHKINECVNAADLQLLARMYQRIM 370
Cdd:PRK08737 327 ALVYGPGDiAQAHTADEFVTLDQLQRYAESVHRII 361
|
|
| PRK04443 |
PRK04443 |
[LysW]-lysine hydrolase; |
1-326 |
3.51e-20 |
|
[LysW]-lysine hydrolase;
Pssm-ID: 235299 [Multi-domain] Cd Length: 348 Bit Score: 90.40 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 1 MSCPVIELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIeHMDfgDTQNFWAWRG-RGETLAFAGHTDVVPaGDVdrwi 79
Cdd:PRK04443 4 SALEARELLKGLVEIPSPSGEEAAAAEFLVEFMESHGREA-WVD--EAGNARGPAGdGPPLVLLLGHIDTVP-GDI---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 80 npPFEptIRDGMLFGRGAADMKGSLAAMVVAAERFVAQhphHRGRLAFLITSDEEASAKNGTvkvveALMARNERLDYCL 159
Cdd:PRK04443 76 --PVR--VEDGVLWGRGSVDAKGPLAAFAAAAARLEAL---VRARVSFVGAVEEEAPSSGGA-----RLVADRERPDAVI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 160 VGEPSSTeivgDVVKNGRRGSLTCNLTIHGVQGHVAypHLADNPVHRAAPFLNELVA-----IEWDRGNDffpatsmQV- 233
Cdd:PRK04443 144 IGEPSGW----DGITLGYKGRLLVTYVATSESFHSA--GPEPNAAEDAIEWWLAVEAwfeanDGRERVFD-------QVt 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 234 ANIQAGTGSNNVIPGELFVQFNFRFSTELTDEMIKERVHALLEkhqlRYTVDWWLSGQPFLTA-RGKLVDAVVNAIEHyN 312
Cdd:PRK04443 211 PKLVDFDSSSDGLTVEAEMTVGLRLPPGLSPEEAREILDALLP----TGTVTFTGAVPAYMVSkRTPLARAFRVAIRE-A 285
|
330
....*....|....
gi 447200569 313 EIKPQLLTTGGTSD 326
Cdd:PRK04443 286 GGTPRLKRKTGTSD 299
|
|
| M20_dipept_Sso-CP2 |
cd05681 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
12-358 |
4.85e-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. This family includes Sso-CP2 from Sulfolobus solfataricus.
Pssm-ID: 349930 [Multi-domain] Cd Length: 429 Bit Score: 90.86 E-value: 4.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 12 LIRRPSLSPDDAG---CQALMIERLRKIGFT--IEHMD-----FGDTQNfwawrGRGETLAFAGHTDVVPAGDVDRWINP 81
Cdd:cd05681 8 LLKIPSVSAQGRGipeTADFLKEFLRRLGAEveIFETDgnpivYAEFNS-----GDAKTLLFYNHYDVQPAEPLELWTSD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 82 PFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNgtvkvVEALMARNERL---DYC 158
Cdd:cd05681 83 PFELTIRNGKLYARGVADDKGELMARLAALRALLQHLGELPVNIKFLVEGEEEVGSPN-----LEKFVAEHADLlkaDGC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 159 L-----VGEPSSTEIVGdvvknGRRGSLTCNLTIHG--VQGHVAYPHLADNPVHRAAPFLNELVA-------------IE 218
Cdd:cd05681 158 IwegggKNPKGRPQISL-----GVKGIVYVELRVKTadFDLHSSYGAIVENPAWRLVQALNSLRDedgrvlipgfyddVR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 219 W------------------------------DRGND----FFPATSMQVANIQAG---TGSNNVIPGELFVQFNFRFSTE 261
Cdd:cd05681 233 PlseaeralidtydfdpeelrktyglkrplqVEGKDplraLFTEPTCNINGIYSGytgEGSKTILPSEAFAKLDFRLVPD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 262 LTDEMIKERVHALLEKH-----QLRYTvdwwLSGQPFLT-ARGKLVDAVVN-AIEHYNEiKPQLL-TTGGTSD-GRFIAR 332
Cdd:cd05681 313 QDPAKILSLLRKHLDKNgfddiEIHDL----LGEKPFRTdPDAPFVQAVIEsAKEVYGQ-DPIVLpNSAGTGPmYPFYDA 387
|
410 420
....*....|....*....|....*...
gi 447200569 333 MGAQVVELGPVNA--TIHKINECVNAAD 358
Cdd:cd05681 388 LEVPVVAIGVGNAgsNAHAPNENIRIAD 415
|
|
| PRK08596 |
PRK08596 |
acetylornithine deacetylase; Validated |
6-170 |
6.50e-20 |
|
acetylornithine deacetylase; Validated
Pssm-ID: 181495 [Multi-domain] Cd Length: 421 Bit Score: 90.48 E-value: 6.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 6 IELTQQLIRRPSLSP---DDAGCQALMIERLRKIGFTIEHMDFGDTQNFWAWRGRGE------TLAFAGHTDVVPAGDVD 76
Cdd:PRK08596 16 LELLKTLVRFETPAPparNTNEAQEFIAEFLRKLGFSVDKWDVYPNDPNVVGVKKGTesdaykSLIINGHMDVAEVSADE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 77 RWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEAsAKNGTVKVVEalmaRNERLD 156
Cdd:PRK08596 96 AWETNPFEPTIKDGWLYGRGAADMKGGLAGALFAIQLLHEAGIELPGDLIFQSVIGEEV-GEAGTLQCCE----RGYDAD 170
|
170
....*....|....
gi 447200569 157 YCLVGEPSSTEIVG 170
Cdd:PRK08596 171 FAVVVDTSDLHMQG 184
|
|
| Zinc_peptidase_like |
cd03873 |
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
58-173 |
1.19e-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: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 58 GETLAFAGHTDVVPAGDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASA 137
Cdd:cd03873 12 GKSVALGAHLDVVPAGEGDNRDPPFAEDTEEEGRLYGRGALDDKGGVAAALEALKRLKENGFKPKGTIVVAFTADEEVGS 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 447200569 138 KNGTVKVVEALMARNERLDYCLVGEPSSTEIVGDVV 173
Cdd:cd03873 92 GGGKGLLSKFLLAEDLKVDAAFVIDATAGPILQKGV 127
|
|
| PRK08652 |
PRK08652 |
acetylornithine deacetylase; Provisional |
6-284 |
1.79e-19 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 236324 [Multi-domain] Cd Length: 347 Bit Score: 88.28 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 6 IELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIEHMDFGDTQNFWAwRGRGEtLAFAGHTDVVPagdvdrwinPPFEP 85
Cdd:PRK08652 5 KELLKQLVKIPSPSGQEDEIALHIMEFLESLGYDVHIESDGEVINIVV-NSKAE-LFVEVHYDTVP---------VRAEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 86 TIRDGMLFGRGAADMKGSLAAMVVAAERFvaQHPHHRGRLAFLITSDEEASAKNgtvkvvEALMARNERLDYCLVGEPSS 165
Cdd:PRK08652 74 FVDGVYVYGTGACDAKGGVAAILLALEEL--GKEFEDLNVGIAFVSDEEEGGRG------SALFAERYRPKMAIVLEPTD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 166 TEivgdvVKNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRGNDFFPATSMQVAniqAGTGSNNV 245
Cdd:PRK08652 146 LK-----VAIAHYGNLEAYVEVKGKPSHGACPESGVNAIEKAFEMLEKLKELLKALGKYFDPHIGIQEI---IGGSPEYS 217
|
250 260 270
....*....|....*....|....*....|....*....
gi 447200569 246 IPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRYTV 284
Cdd:PRK08652 218 IPALCRLRLDARIPPEVEVEDVLDEIDPILDEYTVKYEY 256
|
|
| PRK05111 |
PRK05111 |
acetylornithine deacetylase; Provisional |
4-342 |
2.98e-19 |
|
acetylornithine deacetylase; Provisional
Pssm-ID: 235346 [Multi-domain] Cd Length: 383 Bit Score: 87.96 E-value: 2.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 4 PVIELTQQLIRRPSLS---PD-DAGCQALmIERL----RKIGFTIEHM---DFGDTQNFWAWRGRGET-LAFAGHTDVVP 71
Cdd:PRK05111 6 SFIEMYRALIATPSISatdPAlDQSNRAV-IDLLagwfEDLGFNVEIQpvpGTRGKFNLLASLGSGEGgLLLAGHTDTVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 72 AgDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVA---QHPhhrgrLAFLITSDEEaSAKNGTVKVVEal 148
Cdd:PRK05111 85 F-DEGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILEALRDIDLtklKKP-----LYILATADEE-TSMAGARAFAE-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 149 mARNERLDYCLVGEPSSTEIVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPV---HRAapfLNELVAI--EWDRG- 222
Cdd:PRK05111 156 -ATAIRPDCAIIGEPTSLKPV-----RAHKGHMSEAIRITGQSGHSSDPALGVNAIelmHDV---IGELLQLrdELQERy 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 223 -NDFF--PATSMQVANIQAGTGSNNvIPGELFVQFNFR----FSTELTDEMIKERVHALLEKHQLRYTVDWWLSG-QPFL 294
Cdd:PRK05111 227 hNPAFtvPYPTLNLGHIHGGDAPNR-ICGCCELHFDIRplpgMTLEDLRGLLREALAPVSERWPGRITVAPLHPPiPGYE 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 447200569 295 TARGKlvdAVVNAIEHYNEIKPQLLTTGgtSDGRFIARMGAQVVELGP 342
Cdd:PRK05111 306 CPADH---QLVRVVEKLLGHKAEVVNYC--TEAPFIQQLGCPTLVLGP 348
|
|
| M20_dipept_like |
cd05680 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
12-215 |
8.60e-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.
Pssm-ID: 349929 [Multi-domain] Cd Length: 437 Bit Score: 87.36 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 12 LIRRPSLS------PDDAGCQALMIERLRKIGFtiEHMDFGDTQNF------WAWRGRGETLAFAGHTDVVPAGDVDRWI 79
Cdd:cd05680 7 LLRIPSVSadpahkGDVRRAAEWLADKLTEAGF--EHTEVLPTGGHplvyaeWLGAPGAPTVLVYGHYDVQPPDPLELWT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 80 NPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHphhrGRLA----FLITSDEEASAKNgtvkvVEALMARN-ER 154
Cdd:cd05680 85 SPPFEPVVRDGRLYARGASDDKGQVFIHIKAVEAWLAVE----GALPvnvkFLIEGEEEIGSPS-----LPAFLEENaER 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447200569 155 L--DYCLVGEPSSTEIVGDVVKNGRRGSLTCNLTIHGV-----QGHvaYPHLADNPVHRAAPFLNELV 215
Cdd:cd05680 156 LaaDVVLVSDTSMWSPDTPTITYGLRGLAYLEISVTGPnrdlhSGS--YGGAVPNPANALARLLASLH 221
|
|
| Ac-peptdase-euk |
TIGR01880 |
N-acyl-L-amino-acid amidohydrolase; This model represents a family of eukaryotic ... |
4-373 |
1.01e-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: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 4 PVIELTQQLIRRPSL--SPDDAGCQALMIERLRKIGFTIEHMDF--GDTQNFWAWRGRGETLA---FAGHTDVVPAGDvD 76
Cdd:TIGR01880 10 IAVTRFREYLRINTVqpNPDYAACVDFLIKQADELGLARKTIEFvpGKPVVVLTWPGSNPELPsilLNSHTDVVPVFR-E 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 77 RWINPPFEPTI-RDGMLFGRGAADMKgSLAAMVVAAERFVAQHPHHRGRLAFLI-TSDEEASAKNGTVKVVEALMARNER 154
Cdd:TIGR01880 89 HWTHPPFSAFKdEDGNIYARGAQDMK-CVGVQYLEAVRNLKASGFKFKRTIHISfVPDEEIGGHDGMEKFAKTDEFKALN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 155 LDYCL-VGEPSSTEIVgdVVKNGRRGSLTCNLTIHGVQGHVA--YPHLADNPVHRAAPFLNELVAIEWDR---GNDFF-- 226
Cdd:TIGR01880 168 LGFALdEGLASPDDVY--RVFYAERVPWWVVVTAPGNPGHGSklMENTAMEKLEKSVESIRRFRESQFQLlqsNPDLAig 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 227 PATSMQVANIQAGTGSnNVIPGELFVQFNFRFSTELTDEMIKERVHallekhqlrytvDWW-------------LSGQPF 293
Cdd:TIGR01880 246 DVTSVNLTKLKGGVQS-NVIPSEAEAGFDIRLAPSVDFEEMENRLD------------EWCadagegvtyefsqHSGKPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 294 LTArgklVD-------AVVNAIEHYN-EIKPQLLTtgGTSDGRFIARMGAQVVELGPVNAT---IHKINECVNAADLQLL 362
Cdd:TIGR01880 313 VTP----HDdsnpwwvAFKDAVKEMGcTFKPEILP--GSTDSRYIRAAGVPALGFSPMNNTpvlLHDHNEFLNEAVFLRG 386
|
410
....*....|.
gi 447200569 363 ARMYQRIMEQL 373
Cdd:TIGR01880 387 IEIYQTLISAL 397
|
|
| PRK07906 |
PRK07906 |
hypothetical protein; Provisional |
65-334 |
5.41e-18 |
|
hypothetical protein; Provisional
Pssm-ID: 181163 [Multi-domain] Cd Length: 426 Bit Score: 84.90 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 65 GHTDVVPAgDVDRWINPPFEPTIRDGMLFGRGAADMKGsLAAMVVAaerfVAQHPHHRGR-------LAFLitSDEEASA 137
Cdd:PRK07906 72 GHLDVVPA-EAADWSVHPFSGEIRDGYVWGRGAVDMKD-MDAMMLA----VVRHLARTGRrpprdlvFAFV--ADEEAGG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 138 KNGTVKVVEalmARNERLDYClvgepssTEIVGDV---------------VKNGRRGSLTCNLTIHGVQGHVAYPHlADN 202
Cdd:PRK07906 144 TYGAHWLVD---NHPELFEGV-------TEAISEVggfsltvpgrdrlylIETAEKGLAWMRLTARGRAGHGSMVN-DDN 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 203 PVHRAA-----------P---------FLN---ELVAIEWDRGNdffPATSM----QVANIQAGTGSN------------ 243
Cdd:PRK07906 213 AVTRLAeavarigrhrwPlvltptvraFLDgvaELTGLEFDPDD---PDALLaklgPAARMVGATLRNtanptmlkagyk 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 244 -NVIPGELFVQFNFRFSTELTDEMIKErVHALLEKHqlrytVDW-WLSGQPFLTA--RGKLVDAVVNAIEHYN---EIKP 316
Cdd:PRK07906 290 vNVIPGTAEAVVDGRFLPGREEEFLAT-VDELLGPD-----VEReWVHRDPALETpfDGPLVDAMNAALLAEDpgaRVVP 363
|
330
....*....|....*...
gi 447200569 317 QLLtTGGTsDGRFIARMG 334
Cdd:PRK07906 364 YML-SGGT-DAKAFSRLG 379
|
|
| M20_yscS |
cd05674 |
M20 Peptidase, carboxypeptidase yscS; Peptidase M20 family, yscS (GlyX-carboxypeptidase, CPS1, ... |
54-285 |
1.15e-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: 84.23 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 54 WRGRGETLA---FAGHTDVVPA--GDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRgR---L 125
Cdd:cd05674 62 WEGSDPSLKpllLMAHQDVVPVnpETEDQWTHPPFSGHYDGGYIWGRGALDDKNSLIGILEAVELLLKRGFKPR-RtiiL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 126 AFliTSDEEASAKNGTVKVVEALMAR-NERLDYCLVGEPS---STEIVGD---VVKNGRRGSLTCNLTIHGVQGHVAYPH 198
Cdd:cd05674 141 AF--GHDEEVGGERGAGAIAELLLERyGVDGLAAILDEGGavlEGVFLGVpfaLPGVAEKGYMDVEITVHTPGGHSSVPP 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 199 --------------LADNP----VHRAAPFLNELVAI-------------------------------EWDRGNDFFPAT 229
Cdd:cd05674 219 khtgigilseavaaLEANPfppkLTPGNPYYGMLQCLaehsplpprslksnlwlaspllkallasellSTSPLTRALLRT 298
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 230 SMQVANIQAGTGSnNVIPGELFVQFNFRFSTELTDEMIKERVHALL----EKHQLRYTVD 285
Cdd:cd05674 299 TQAVDIINGGVKI-NALPETATATVNHRIAPGSSVEEVLEHVKNLIadiaVKYGLGLSAF 357
|
|
| PRK07338 |
PRK07338 |
hydrolase; |
63-373 |
2.21e-16 |
|
hydrolase;
Pssm-ID: 235995 [Multi-domain] Cd Length: 402 Bit Score: 80.01 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 63 FAGHTDVV-PAGDvdrwinpPFE--PTIRDGMLFGRGAADMKGSLAAMVVAAERFvAQHPhHRGRLAF--LITSDEE--- 134
Cdd:PRK07338 97 LTGHMDTVfPADH-------PFQtlSWLDDGTLNGPGVADMKGGIVVMLAALLAF-ERSP-LADKLGYdvLINPDEEigs 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 135 -ASAkngtvkVVEALMARneRLDYCLVGEPSSTEivGDVVKNgRRGSLTCNLTIHGVQGHVAY-PHLADNPVHRAAPFLN 212
Cdd:PRK07338 168 pASA------PLLAELAR--GKHAALTYEPALPD--GTLAGA-RKGSGNFTIVVTGRAAHAGRaFDEGRNAIVAAAELAL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 213 ELVAIewdrgNDFFPATSMQVANIQAGtGSNNVIPGELFVQFNFRFSTELTDEMIKERVHALLEKHQLRYTVDWWLSGQ- 291
Cdd:PRK07338 237 ALHAL-----NGQRDGVTVNVAKIDGG-GPLNVVPDNAVLRFNIRPPTPEDAAWAEAELKKLIAQVNQRHGVSLHLHGGf 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 292 -----PFLTARGKLVDAVVNAIEHYN-EIKPQllTTGGTSDGRFIARMGAQVVE-LGPVNATIHKINECVNAADLQLLAR 364
Cdd:PRK07338 311 grppkPIDAAQQRLFEAVQACGAALGlTIDWK--DSGGVCDGNNLAAAGLPVVDtLGVRGGNIHSEDEFVILDSLVERAQ 388
|
....*....
gi 447200569 365 MYQRIMEQL 373
Cdd:PRK07338 389 LSALILMRL 397
|
|
| PRK07205 |
PRK07205 |
hypothetical protein; Provisional |
6-134 |
6.24e-16 |
|
hypothetical protein; Provisional
Pssm-ID: 235965 [Multi-domain] Cd Length: 444 Bit Score: 78.58 E-value: 6.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 6 IELTQQLIRRPS-LSPDDAGC---QAL------MIERLRKIGFTIehmdFGDTQNFW--AWRGRG-ETLAFAGHTDVVPA 72
Cdd:PRK07205 14 VAAIKTLVSYPSvLNEGENGTpfgQAIqdvleaTLDLCQGLGFKT----YLDPKGYYgyAEIGQGeELLAILCHLDVVPE 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447200569 73 GDVDRWINPPFEPTIRDGMLFGRGAADMKG-SLAAMvVAAERFVAQHPHHRGRLAFLITSDEE 134
Cdd:PRK07205 90 GDLSDWQTPPFEAVEKDGCLFGRGTQDDKGpSMAAL-YAVKALLDAGVQFNKRIRFIFGTDEE 151
|
|
| dipeptidaselike |
TIGR01887 |
dipeptidase, putative; This model represents a clade of probable zinc dipeptidases, closely ... |
5-134 |
1.59e-15 |
|
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: 77.42 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 5 VIELTQQLIRRPSLSPDDAGCQ----------AL--MIERLRKIGFTIEhmDFGDTQNFWAWrGRG-ETLAFAGHTDVVP 71
Cdd:TIGR01887 4 ILEDLKELIAIDSVEDLEKAKEgapfgegprkALdkFLEIAKRDGFTTE--NVDNYAGYIEY-GQGeEVLGILGHLDVVP 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447200569 72 AGDvdRWINPPFEPTIRDGMLFGRGAADMKG----SLAAMVVAAERFVAqhPHHRGRlaFLITSDEE 134
Cdd:TIGR01887 81 AGD--GWTSPPFEPTIKDGRIYGRGTLDDKGptiaAYYAMKILKELGLK--LKKKIR--FIFGTDEE 141
|
|
| PRK09133 |
PRK09133 |
hypothetical protein; Provisional |
27-216 |
2.11e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 236388 [Multi-domain] Cd Length: 472 Bit Score: 74.27 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 27 ALMIERLRKIGFT---IEHMD-FGDTQNFWA-WRGRGET--LAFAGHTDVVPAGDVDrWINPPFEPTIRDGMLFGRGAAD 99
Cdd:PRK09133 63 EAMAARLKAAGFAdadIEVTGpYPRKGNLVArLRGTDPKkpILLLAHMDVVEAKRED-WTRDPFKLVEENGYFYGRGTSD 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 100 MKgSLAAMVVAA------ERFVaqhPHHRGRLAFliTSDEEASAKNGTVKVVE-------ALMARNE----RLDYclVGE 162
Cdd:PRK09133 142 DK-ADAAIWVATlirlkrEGFK---PKRDIILAL--TGDEEGTPMNGVAWLAEnhrdlidAEFALNEggggTLDE--DGK 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447200569 163 PSSTEIVGdvvknGRRGSLTCNLTIHGVQGHVAYPhLADNPVHRAAPFLNELVA 216
Cdd:PRK09133 214 PVLLTVQA-----GEKTYADFRLEVTNPGGHSSRP-TKDNAIYRLAAALSRLAA 261
|
|
| PRK08554 |
PRK08554 |
peptidase; Reviewed |
56-374 |
2.39e-14 |
|
peptidase; Reviewed
Pssm-ID: 236285 [Multi-domain] Cd Length: 438 Bit Score: 74.04 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 56 GRGETLaFAGHTDVVPAGDvDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQhpHHRGRLAFLITSDEEA 135
Cdd:PRK08554 62 GKPKLL-FMAHFDVVPVNP-EEWNTEPFKLTVKGDKAYGRGSADDKGNVASVMLALKELSKE--PLNGKVIFAFTGDEEI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 136 SAKNGtVKVVEALMARNERLDYCLVGEPSSTEIV-------GDVVK--------NGRRGSLTCNLTIHGVQG-HVAY--P 197
Cdd:PRK08554 138 GGAMA-MHIAEKLREEGKLPKYMINADGIGMKPIirrrkgfGVTIRvpsekvkvKGKLREQTFEIRTPVVETrHAAYflP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 198 HLADNPVHRAAPFLNE--LVAI----EWDRGNdFFPAtSMQVANIQAGTGSN------------NVIP------------ 247
Cdd:PRK08554 217 GVDTHPLIAASHFLREsnVLAVslegKFLKGN-VVPG-EVTLTYLEPGEGEEvevdlgltrllkAIVPlvrapikaekys 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 248 ---------------GELFVQFNFR---FSTELTDEMIKERVHALLEKHQLRYTVDwWLSGQPFLTARGKLVDAVVNAIE 309
Cdd:PRK08554 295 dygvsitpnvysfaeGKHVLKLDIRamsYSKEDIERTLKEVLEFNLPEAEVEIRTN-EKAGYLFTPPDEEIVKVALRVLK 373
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447200569 310 HYNEiKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIMEQLV 374
Cdd:PRK08554 374 ELGE-DAEPVEGPGASDSRYFTPYGVKAIDFGPKGGNIHGPNEYVEIDSLKKMPEVYKRIALRLL 437
|
|
| PRK07318 |
PRK07318 |
dipeptidase PepV; Reviewed |
6-106 |
4.27e-14 |
|
dipeptidase PepV; Reviewed
Pssm-ID: 235988 [Multi-domain] Cd Length: 466 Bit Score: 73.34 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 6 IELTQQLIRRPS---LSPDDAG-------CQAL--MIERLRKIGFTIE-------HMDFGDTQnfwawrgrgETLAFAGH 66
Cdd:PRK07318 17 IEDLQELLRINSvrdDSKAKEGapfgpgpVKALekFLEIAERDGFKTKnvdnyagHIEYGEGE---------EVLGILGH 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 447200569 67 TDVVPAGDvdRWINPPFEPTIRDGMLFGRGAADMKG-SLAA 106
Cdd:PRK07318 88 LDVVPAGD--GWDTDPYEPVIKDGKIYARGTSDDKGpTMAA 126
|
|
| PRK07907 |
PRK07907 |
hypothetical protein; Provisional |
66-113 |
5.08e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 236127 [Multi-domain] Cd Length: 449 Bit Score: 73.02 E-value: 5.08e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 447200569 66 HTDVVPAGDVDRWINPPFEPTIRDGMLFGRGAADMKGSLaAMVVAAER 113
Cdd:PRK07907 91 HHDVQPPGDPDAWDSPPFELTERDGRLYGRGAADDKGGI-AMHLAALR 137
|
|
| M20_dipept_like_DUG2_type |
cd05677 |
M20 Defective in Utilization of Glutathione-type peptidases containing WD repeats; Peptidase ... |
57-160 |
9.40e-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: 71.99 E-value: 9.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 57 RGETLAFAGHTDVVPAGDVDRWINPPFEPTIRDGMLFGRGAADMKG-SLAAMVVAAERFvaqhphHRGRL----AFLITS 131
Cdd:cd05677 70 KRKRILFYGHYDVIPAGETDGWDTDPFTLTCENGYLYGRGVSDNKGpLLAAIYAVAELF------QEGELdndvVFLIEG 143
|
90 100
....*....|....*....|....*....
gi 447200569 132 DEEASAKnGTVKVVEALMARNERLDYCLV 160
Cdd:cd05677 144 EEESGSP-GFKEVLRKNKELIGDIDWILL 171
|
|
| PRK08201 |
PRK08201 |
dipeptidase; |
10-139 |
2.69e-12 |
|
dipeptidase;
Pssm-ID: 169276 [Multi-domain] Cd Length: 456 Bit Score: 67.85 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 10 QQLIRRPSLSP------DDAGCQALMIERLRKIGFtiEHMDFGDTQNF------WAWRGRGETLAFAGHTDVVPAGDVDR 77
Cdd:PRK08201 21 KEFLRIPSISAlsehkeDVRKAAEWLAGALEKAGL--EHVEIMETAGHpivyadWLHAPGKPTVLIYGHYDVQPVDPLNL 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447200569 78 WINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQhphhRGRL----AFLITSDEEASAKN 139
Cdd:PRK08201 99 WETPPFEPTIRDGKLYARGASDDKGQVFMHLKAVEALLKV----EGTLpvnvKFCIEGEEEIGSPN 160
|
|
| M20_peptT_like |
cd05683 |
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT ... |
11-371 |
2.97e-12 |
|
M20 Peptidase T like enzymes specifically cleave tripeptides; Peptidase M20 family, PeptT (tripeptide aminopeptidase; tripeptidase)-like subfamily. This group includes bacterial tripeptidases as well as predicted tripeptidases. Peptidase T acts only on tripeptide substrates, and is thus called a tripeptidase. It catalyzes the release of N-terminal amino acids with hydrophobic side chains from tripeptides with high specificity; dipeptides, tetrapeptides or tripeptides with the N-terminus blocked are not cleaved. Tripeptidases are known to function at the final stage of proteolysis in lactococcal bacteria and release amino acids from tripeptides produced during the digestion of milk proteins such as casein.
Pssm-ID: 349932 [Multi-domain] Cd Length: 368 Bit Score: 67.09 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 11 QLIRRPSLSPDDAGCQALMIERLRKIGFTIEHMDFGDTQNFWA------WRGRGE---TLAFAGHTDVVPAGDVdrwiNP 81
Cdd:cd05683 11 ELVQIDSETLHEKEISKVLKKKFENLGLSVIEDDAGKTTGGGAgnlictLKADKEevpKILFTSHMDTVTPGIN----VK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 82 PfePTIRDGMLFGRG----AADMKGSLAAMVVAAERFVAQHPHHrGRLAFLITSDEEASakngtvkVVEALMARNERLD- 156
Cdd:cd05683 87 P--PQIADGYIYSDGttilGADDKAGIAAILEAIRVIKEKNIPH-GQIQFVITVGEESG-------LVGAKALDPELIDa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 157 ---YCLVGEPSSTEIV-----GDVVkngrrgsltcNLTIHGVQGHVA-YPHLADNPVHRAAPFLNELvaiEWDRGNDFfp 227
Cdd:cd05683 157 dygYALDSEGDVGTIIvgaptQDKI----------NAKIYGKTAHAGtSPEKGISAINIAAKAISNM---KLGRIDEE-- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 228 aTSMQVANIQAGTGSNnVIPGELFVQFNFRFSTE-----LTDEMiKERVHALLEKHQLRYTVDWWLSGQPF-LTARGKLV 301
Cdd:cd05683 222 -TTANIGKFQGGTATN-IVTDEVNIEAEARSLDEekldaQVKHM-KETFETTAKEKGAHAEVEVETSYPGFkINEDEEVV 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 302 DAVVNAIEHYnEIKPQLLTTGGTSDGRFIARMGAQVVELGPVNATIHKINECVNAADLQLLARMYQRIME 371
Cdd:cd05683 299 KLAKRAANNL-GLEINTTYSGGGSDANIINGLGIPTVNLGIGYENIHTTNERIPIEDLYDTAVLVVEIIK 367
|
|
| M20_like |
cd02697 |
M20 Zn-peptidases include exopeptidases; Peptidase M20 family; uncharacterized subfamily. ... |
10-292 |
3.05e-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: 67.19 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 10 QQLIRRPSLSP--DDAGCQALMIERLRKIGFTIEH--------MDFG--DTQNFWAWRGRGE---TLAFAGHTDVVPAGD 74
Cdd:cd02697 10 QKLVRVPTDTPpgNNAPHAERTAALLQGFGFEAERhpvpeaevRAYGmeSITNLIVRRRYGDggrTVALNAHGDVVPPGD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 75 vdRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNGTVKVVEALMARNer 154
Cdd:cd02697 90 --GWTRDPYGAVVEDGVMYGRAAAVSKSDFASFTFAVRALESLGAPLRGAVELHFTYDEEFGGELGPGWLLRQGLTKP-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 155 lDYcLVGEPSSTEIVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELvaieWDRGNDFFPATS---- 230
Cdd:cd02697 166 -DL-LIAAGFSYEVV-----TAHNGCLQMEVTVHGKQAHAAIPDTGVDALQGAVAILNAL----YALNAQYRQVSSqveg 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447200569 231 -----MQVANIQAGTGSnNVIPGELfvqfNFRFSTELTDEMIKERVHAllekhQLRYTVDWWLSGQP 292
Cdd:cd02697 235 ithpyLNVGRIEGGTNT-NVVPGKV----TFKLDRRMIPEENPVEVEA-----EIRRVIADAAASMP 291
|
|
| M20_dipept_like_CNDP |
cd05676 |
M20 cytosolic nonspecific dipeptidases including anserinase and serum carnosinase; Peptidase ... |
29-118 |
5.22e-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: 66.86 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 29 MIERLRKIGFTIEHMDFGDTQNfwawrGRGE-------------------TLAFAGHTDVVPAGDVDRWINPPFEPTIRD 89
Cdd:cd05676 42 AAERLEKLGFKVELVDIGTQTL-----PDGEelplppvllgrlgsdpskkTVLIYGHLDVQPAKLEDGWDTDPFELTEKD 116
|
90 100
....*....|....*....|....*....
gi 447200569 90 GMLFGRGAADMKGSLAAMVVAAERFVAQH 118
Cdd:cd05676 117 GKLYGRGSTDDKGPVLGWLNAIEAYQKLG 145
|
|
| M20_Acy1 |
cd03886 |
M20 Peptidase Aminoacylase 1 family; Peptidase M20 family, Aminoacylase 1 (ACY1; hippuricase; ... |
105-286 |
1.66e-10 |
|
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: 61.85 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 105 AAMVVAAERFVAQHPHH-RGRLAFLITSDEEASAknGTVKVVEALMARNERLDYCLvGEPSSTEI-VGDVVknGRRGSLT 182
Cdd:cd03886 94 TAMLLGAAKLLAERRDPlKGTVRFIFQPAEEGPG--GAKAMIEEGVLENPGVDAAF-GLHVWPGLpVGTVG--VRSGALM 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 183 C-----NLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEwDRGNDFFPATSMQVANIQAGTGsNNVIPGELFVQFNFR 257
Cdd:cd03886 169 AsadefEITVKGKGGHGASPHLGVDPIVAAAQIVLALQTVV-SRELDPLEPAVVTVGKFHAGTA-FNVIPDTAVLEGTIR 246
|
170 180 190
....*....|....*....|....*....|...
gi 447200569 258 -FSTELTD---EMIKERVHALLEKHQLRYTVDW 286
Cdd:cd03886 247 tFDPEVREaleARIKRLAEGIAAAYGATVELEY 279
|
|
| M20_PAAh_like |
cd03896 |
M20 Peptidases, Poly(aspartic acid) hydrolase-like proteins; Peptidase M20 family, Poly ... |
6-308 |
1.93e-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: 61.73 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 6 IELTQQLIRRPSLSPDDAGCQALMIERLRKIGF-TIEHMDFGDTQNFWAWRGRGETLAFAGHTDVVPAGDVdrwinpPFE 84
Cdd:cd03896 1 VDTAIELGEIPAPTFREGARADLVAEWMADLGLgDVERDGRGNVVGRLRGTGGGPALLFSAHLDTVFPGDT------PAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 85 PTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNGTVKvvEALMARNERLDYCLVGEPS 164
Cdd:cd03896 75 VRHEGGRIYGPGIGDNKGSLACLLAMARAMKEAGAALKGDVVFAANVGEEGLGDLRGAR--YLLSAHGARLDYFVVAEGT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 165 STEIVgdvvkNGRRGSLTCNLTIHGVQGHVAYPHLADNPVH---RAAPFLNELVAiewdrgnDFFPATSMQVANIQAGTg 241
Cdd:cd03896 153 DGVPH-----TGAVGSKRFRITTVGPGGHSYGAFGSPSAIVamaKLVEALYEWAA-------PYVPKTTFAAIRGGGGT- 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447200569 242 SNNVIPGELFVQFNFRF--STELTDemIKERVHALLEKHQLRYT-----VDWWLSGQPFLTAR-GKLVDAVVNAI 308
Cdd:cd03896 220 SVNRIANLCSMYLDIRSnpDAELAD--VQREVEAVVSKLAAKHLrvkarVKPVGDRPGGEAQGtEPLVNAAVAAH 292
|
|
| PRK06446 |
PRK06446 |
hypothetical protein; Provisional |
56-220 |
5.74e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 235802 [Multi-domain] Cd Length: 436 Bit Score: 60.54 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 56 GRGETLAFAGHTDVVPAGDVDRWINPPFEPTIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGrLAFLITSDEEA 135
Cdd:PRK06446 60 GAKKTLLIYNHYDVQPVDPLSEWKRDPFSATIENGRIYARGASDNKGTLMARLFAIKHLIDKHKLNVN-VKFLYEGEEEI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 136 SAKNgtvkvVEALMARNERL---DYCLV--------GEPsstEIVGDVvkngrRGSLTCNLTIHGVQG--HVAYPHLADN 202
Cdd:PRK06446 139 GSPN-----LEDFIEKNKNKlkaDSVIMegagldpkGRP---QIVLGV-----KGLLYVELVLRTGTKdlHSSNAPIVRN 205
|
170
....*....|....*...
gi 447200569 203 PVHRAAPFLNELVAIEWD 220
Cdd:PRK06446 206 PAWDLVKLLSTLVDGEGR 223
|
|
| PRK09104 |
PRK09104 |
hypothetical protein; Validated |
11-160 |
6.14e-10 |
|
hypothetical protein; Validated
Pssm-ID: 236379 [Multi-domain] Cd Length: 464 Bit Score: 60.30 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 11 QLIRRPSLSPDDA---GCQA---LMIERLRKIGFTIE------H-MDFGDTQnfwAWRGRGETLAFAGHTDVVPAGDVDR 77
Cdd:PRK09104 25 ALLRIPSISTDPAyaaDCRKaadWLVADLASLGFEASvrdtpgHpMVVAHHE---GPTGDAPHVLFYGHYDVQPVDPLDL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 78 WINPPFEPTIRDG-----MLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNgtvkVVEALMARN 152
Cdd:PRK09104 102 WESPPFEPRIKETpdgrkVIVARGASDDKGQLMTFVEACRAWKAVTGSLPVRVTILFEGEEESGSPS----LVPFLEANA 177
|
170
....*....|
gi 447200569 153 ERL--DYCLV 160
Cdd:PRK09104 178 EELkaDVALV 187
|
|
| PRK06133 |
PRK06133 |
glutamate carboxypeptidase; Reviewed |
4-372 |
8.12e-10 |
|
glutamate carboxypeptidase; Reviewed
Pssm-ID: 235710 [Multi-domain] Cd Length: 410 Bit Score: 60.03 E-value: 8.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 4 PVIELTQQLIRRPSLSPDDAGCQ---ALMIERLRKIGFTIEHMD----FGDtqNFWA-WRGRGE-TLAFAGHTDVV-PAG 73
Cdd:PRK06133 38 AYLDTLKELVSIESGSGDAEGLKqvaALLAERLKALGAKVERAPtppsAGD--MVVAtFKGTGKrRIMLIAHMDTVyLPG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 74 DVDRwinPPFEptIRDGMLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKnGTVKVVEALMARNe 153
Cdd:PRK06133 116 MLAK---QPFR--IDGDRAYGPGIADDKGGVAVILHALKILQQLGFKDYGTLTVLFNPDEETGSP-GSRELIAELAAQH- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 154 rlDYCLVGEPSSTEivgDVVKNGRRGSLTCNLTIHGVQGHV-AYPHLADNPVHRAAPFLNELVaiewDRGNdffPATSMQ 232
Cdd:PRK06133 189 --DVVFSCEPGRAK---DALTLATSGIATALLEVKGKASHAgAAPELGRNALYELAHQLLQLR----DLGD---PAKGTT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 233 VANIQAGTGSN-NVIPGELFVQFNFRFSTELTDEMIKERVHALLEKH-------QLRYTVdwwlsGQPFL--TARGKLVD 302
Cdd:PRK06133 257 LNWTVAKAGTNrNVIPASASAQADVRYLDPAEFDRLEADLQEKVKNKlvpdtevTLRFER-----GRPPLeaNAASRALA 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 303 AVVNAIehYNEI----KPQLLTTGGTSDGRFIARMG-AQVVE-LGPVNATIHKINECVN----AADLQLLARMyqrIMEQ 372
Cdd:PRK06133 332 EHAQGI--YGELgrrlEPIDMGTGGGTDAAFAAGSGkAAVLEgFGLVGFGAHSNDEYIElnsiVPRLYLLTRM---IMEL 406
|
|
| M20_Acy1-like |
cd05664 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of ... |
105-277 |
1.83e-09 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, Uncharacterized subfamily of proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349914 [Multi-domain] Cd Length: 399 Bit Score: 58.89 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 105 AAMVVAAERFVAQHPHHRGRLAFLITSDEE--ASAKngtVKVVEALMARNERLDYCL----VGEPSSTeiVGdvVKNGRR 178
Cdd:cd05664 105 AALLGAARLLVEAKDAWSGTLIAVFQPAEEtgGGAQ---AMVDDGLYDKIPKPDVVLaqhvMPGPAGT--VG--TRPGRF 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 179 GSLTCNL--TIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEwDRGNDFFPATSMQVANIQAGTgSNNVIPGELFVQFNF 256
Cdd:cd05664 178 LSAADSLdiTIFGRGGHGSMPHLTIDPVVMAASIVTRLQTIV-SREVDPQEFAVVTVGSIQAGS-AENIIPDEAELKLNV 255
|
170 180
....*....|....*....|.
gi 447200569 257 RFSteltDEMIKERVHALLEK 277
Cdd:cd05664 256 RTF----DPEVREKVLNAIKR 272
|
|
| amidohydrolases |
TIGR01891 |
amidohydrolase; This model represents a subfamily of amidohydrolases which are a subset of ... |
27-310 |
6.88e-08 |
|
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: 53.89 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 27 ALMIERLRKIGFTIEHmDFGDTQNFWAWRGRG---ETLAFAGHTDVVPAGDVDRWinpPFEPTIrDGMLFGRGaadmKGS 103
Cdd:TIGR01891 23 SLIAEALESLGIEVRR-GVGGATGVVATIGGGkpgPVVALRADMDALPIQEQTDL---PYKSTN-PGVMHACG----HDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 104 LAAMVVAAERFVAQHPHH-RGRLAFLITSDEEASAknGTVKVVEA-LMarnERLDYCLVGEPSSTEIVGDVVKngRRGSL 181
Cdd:TIGR01891 94 HTAILLGTAKLLKKLADLlEGTVRLIFQPAEEGGG--GATKMIEDgVL---DDVDAILGLHPDPSIPAGTVGL--RPGTI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 182 T-----CNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRGNDFFPATsMQVANIQAGTGSnNVIPGELFVQFNF 256
Cdd:TIGR01891 167 MaaadkFEVTIHGKGAHAARPHLGRDALDAAAQLVVALQQIVSRNVDPSRPAV-VSVGIIEAGGAP-NVIPDKASMSGTV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 447200569 257 RFSTELTDEMIKERVHALLEK----HQLRYTVDwWLSGQPFLTARGKLVDAVVNAIEH 310
Cdd:TIGR01891 245 RSLDPEVRDQIIDRIERIVEGaaamYGAKVELN-YDRGLPAVTNDPALTQILKEVARH 301
|
|
| M20_Acy1_amhX-like |
cd08018 |
M20 Peptidase aminoacylase 1 amhX-like subfamily; Peptidase M20 family, uncharacterized ... |
180-323 |
7.11e-08 |
|
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: 53.82 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 180 SLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDrgndffP--ATSMQVANIQAGTGSNNVIPGELFVQFNFR 257
Cdd:cd08018 167 STFLEGTIKGKQAHGARPHLGINAIEAASAIVNAVNAIHLD------PniPWSVKMTKLQAGGEATNIIPDKAKFALDLR 240
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447200569 258 FSTELTDEMIKERVHALLEKHQLRY--TVDW-WLSGQPFLTARGKLVDAVVNAI-EHYNE--IKPQLLTTGG 323
Cdd:cd08018 241 AQSNEAMEELKEKVEHAIEAAAALYgaSIEItEKGGMPAAEYDEEAVELMEEAItEVLGEekLAGPCVTPGG 312
|
|
| M20_ArgE-related |
cd08012 |
M20 Peptidases with similarity to acetylornithine deacetylases; Peptidase M20 family, ... |
56-249 |
8.86e-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: 53.62 E-value: 8.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 56 GRGETLAFAG-HTDVVPAgDVDRWINPPFEPTIRDGMLFGRGAADMKGSLaAMVVAAERFVAQH--PHHRGRLAFLITSd 132
Cdd:cd08012 75 VDGKTVSFVGsHMDVVTA-NPETWEFDPFSLSIDGDKLYGRGTTDCLGHV-ALVTELFRQLATEkpALKRTVVAVFIAN- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 133 EEASAKNGTvkVVEALMARNErLDYCLVG------EPSSTEIVGDVvkngrrGSLTCNLTIHGVQGHVAYPHLADNPVHR 206
Cdd:cd08012 152 EENSEIPGV--GVDALVKSGL-LDNLKSGplywvdSADSQPCIGTG------GMVTWKLTATGKLFHSGLPHKAINALEL 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 447200569 207 AAPFLNElvaIEWDRGNDFFP---------ATS--MQVANIQAGTGSNNVIPGE 249
Cdd:cd08012 223 VMEALAE---IQKRFYIDFPPhpkeevygfATPstMKPTQWSYPGGSINQIPGE 273
|
|
| M20_AcylaseI_like |
cd05646 |
M20 Aminoacylase-I like subfamily; Peptidase M20 family, aminoacylase-I like (AcyI-like; ... |
4-373 |
1.05e-07 |
|
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: 53.43 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 4 PVIELTQQLIRRPSL--SPDDAGCQALMIERLRKIGFTIEHMDFgDTQNFWA---WRGRGETLA---FAGHTDVVPAGDv 75
Cdd:cd05646 3 PAVTRFREYLRINTVhpNPDYDACVEFLKRQADELGLPVRVIEV-VPGKPVVvltWEGSNPELPsilLNSHTDVVPVFE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 76 DRWINPPFEPTI-RDGMLFGRGAADMKGSLAAMVVAAERFVAQ--HPHHRGRLAFLitSDEEASAKNGTVKVVEALMARN 152
Cdd:cd05646 81 EKWTHDPFSAHKdEDGNIYARGAQDMKCVGIQYLEAIRRLKASgfKPKRTIHLSFV--PDEEIGGHDGMEKFVKTEEFKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 153 ERLDYCL-VGEPSSTEIVgdVVKNGRRGSLTCNLTIHGVQGHVA--YPHLADNPVHRAAPFLNELVAIEWDRGNDFFPA- 228
Cdd:cd05646 159 LNVGFALdEGLASPTEEY--RVFYGERSPWWVVITAPGTPGHGSklLENTAGEKLRKVIESIMEFRESQKQRLKSNPNLt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 229 ----TSMQVANIQAGTgSNNVIPGELFVQFNFRFsTELTD-----EMIKERVHALLEKHQLRY----------TVD---- 285
Cdd:cd05646 237 lgdvTTVNLTMLKGGV-QMNVVPSEAEAGFDLRI-PPTVDleefeKQIDEWCAEAGRGVTYEFeqkspekdptSLDdsnp 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 286 WWLSGQPFLTARGKLvdavvnaiehyneIKPQLLTtgGTSDGRFIARMGAQVVELGPVNAT---IHKINECVNAADLQLL 362
Cdd:cd05646 315 WWAAFKKAVKEMGLK-------------LKPEIFP--AATDSRYIRALGIPALGFSPMNNTpilLHDHNEFLNEDVFLRG 379
|
410
....*....|.
gi 447200569 363 ARMYQRIMEQL 373
Cdd:cd05646 380 IEIYEKIIPAL 390
|
|
| RocB |
COG4187 |
Arginine utilization protein RocB [Amino acid transport and metabolism]; |
44-171 |
1.05e-07 |
|
Arginine utilization protein RocB [Amino acid transport and metabolism];
Pssm-ID: 443341 Cd Length: 550 Bit Score: 53.71 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 44 DFGDTQNFWA-WRGRGE---TLAFAGHTDVVPAGDVDRWINPPFEP-----TIRDGML--------------FGRGAADM 100
Cdd:COG4187 61 DPLGRKNVTAlVKGKGEskkTVILISHFDVVDVEDYGSLKPLAFDPeelteALKEIKLpedvrkdlesgewlFGRGTMDM 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447200569 101 KGSLAAMVVAAERFvAQHPHHRGRLAFLITSDEEA-SAknGTVKVVEAL--MARNERLDY--CLVGEPSSTEIVGD 171
Cdd:COG4187 141 KAGLALHLALLEEA-SENEEFPGNLLLLAVPDEEVnSA--GMRAAVPLLaeLKEKYGLEYklAINSEPSFPKYPGD 213
|
|
| AbgB |
COG1473 |
Metal-dependent amidase/aminoacylase/carboxypeptidase [General function prediction only]; ... |
177-286 |
1.49e-07 |
|
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: 52.81 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 177 RRGSLTCN-----LTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIeWDRGNDFFPATSMQVANIQAGTgSNNVIPGELF 251
Cdd:COG1473 175 RPGPIMAAadsfeITIKGKGGHAAAPHLGIDPIVAAAQIVTALQTI-VSRNVDPLDPAVVTVGIIHGGT-APNVIPDEAE 252
|
90 100 110
....*....|....*....|....*....|....*....
gi 447200569 252 VQFNFRFSTELTDEMIKERVHALLEK----HQLRYTVDW 286
Cdd:COG1473 253 LEGTVRTFDPEVRELLEERIERIAEGiaaaYGATAEVEY 291
|
|
| M20_Acy1_YkuR-like |
cd05670 |
M20 Peptidase aminoacyclase-1 YkuR-like proteins, including YkuR and Ama/HipO/HyuC proteins; ... |
184-276 |
2.55e-07 |
|
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: 51.88 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 184 NLTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEwDRGNDFFPATSMQVANIQAGTgSNNVIPGELFVQFNFRFSTELT 263
Cdd:cd05670 176 HIDFIGKSGHAAYPHNANDMVVAAANFVTQLQTIV-SRNVDPIDGAVVTIGKIHAGT-ARNVIAGTAHLEGTIRTLTQEM 253
|
90
....*....|...
gi 447200569 264 DEMIKERVHALLE 276
Cdd:cd05670 254 MELVKQRVRDIAE 266
|
|
| M20_ArgE_RocB |
cd05654 |
M20 Peptidase arginine utilization protein, RocB; Peptidase M20 family, ArgE RocB (arginine ... |
36-214 |
3.91e-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: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 36 IGFTIEHMDFGDTQNFWAWRGRGE---TLAFAGHTDVVPAGDVDRWINPPFEPTI-----------------RDGM---- 91
Cdd:cd05654 46 VWQLLPPDDLGRRNVTALVKGKKPskrTIILISHFDTVGIEDYGELKDIAFDPDEltkafseyveeldeevrEDLLsgew 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 92 LFGRGAADMKGSLAAMVVAAERFvAQHPHHRGRLAFLITSDEEaSAKNGTVKVVEAL--MARNERLDY--CLVGEPSSTE 167
Cdd:cd05654 126 LFGRGTMDMKSGLAVHLALLEQA-SEDEDFDGNLLLMAVPDEE-VNSRGMRAAVPALleLKKKHDLEYklAINSEPIFPQ 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 447200569 168 IVGDVVK---NGRRGSLTCNLTIHGVQGHVAYPHLADNPVHRAAPFLNEL 214
Cdd:cd05654 204 YDGDQTRyiyTGSIGKILPGFLCYGKETHVGEPFAGINANLMASEITARL 253
|
|
| M20_bAS |
cd03884 |
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
13-333 |
7.68e-06 |
|
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders.
Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 47.52 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 13 IRRPSLSPDDAGCQALMIERLRKIGFTIEHMDFGdtqNFWAWR----GRGETLAFAGHTDVVPAGDvdRWinppfeptir 88
Cdd:cd03884 19 VTRLALTDEDRAARDLFVEWMEEAGLSVRVDAVG---NLFGRLegtdPDAPPVLTGSHLDTVPNGG--RY---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 89 DGMLfgrgaadmkGSLAAMVVAAE--RFVAQHPHHrgrLAFLITSDEEAS-------------------------AKNGt 141
Cdd:cd03884 84 DGIL---------GVLAGLEALRAlkEAGIRPRRP---IEVVAFTNEEGSrfppsmlgsrafagtldleellslrDADG- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 142 VKVVEALmarnERLDYCLVGEPSSTE--------------------------IVGDVVkngrrGSLTCNLTIHGVQGH-- 193
Cdd:cd03884 151 VSLAEAL----KAIGYDGDRPASARRpgdikayvelhieqgpvleeeglpigVVTGIA-----GQRWLEVTVTGEAGHag 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 194 -VAYPHLADnPVHRAAPFLnelVAIEwDRGNDFFPATSMQVANIQAGTGSNNVIPGELFVQFNFR-FSTELTDEM---IK 268
Cdd:cd03884 222 tTPMALRRD-ALLAAAELI---LAVE-EIALEHGDDLVATVGRIEVKPNAVNVIPGEVEFTLDLRhPDDAVLDAMverIR 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447200569 269 ERVHALLEKHQLRYTVDWWLSGQPFLTArGKLVDAVVNAIEHyNEIKPQLLTTGGTSDGRFIARM 333
Cdd:cd03884 297 AEAEAIAAERGVEVEVERLWDSPPVPFD-PELVAALEAAAEA-LGLSYRRMPSGAGHDAMFMARI 359
|
|
| M20_Acy1_YhaA-like |
cd08021 |
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus ... |
185-286 |
7.99e-05 |
|
M20 Peptidase aminoacylase 1 subfamily, includes Bacillus subtilis YhaA and Staphylococcus aureus amidohydrolase, SACOL0085; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). This family includes Staphylococcus aureus amidohydrolase, SACOL0085, which contains two manganese ions in the active site, and forms a homotetramer with variations in interdomain orientation which possibly plays a role in the regulation of catalytic activity.
Pssm-ID: 349941 [Multi-domain] Cd Length: 384 Bit Score: 44.19 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 185 LTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEWDRGNDFFPATSMqVANIQAGTgSNNVIPGELFVQFNFRFSTELTD 264
Cdd:cd08021 186 ITIKGKGGHGSMPHETVDPIVIAAQIVTALQTIVSRRVDPLDPAVVT-IGTFQGGT-SFNVIPDTVELKGTVRTFDEEVR 263
|
90 100
....*....|....*....|....*.
gi 447200569 265 EMIKER----VHALLEKHQLRYTVDW 286
Cdd:cd08021 264 EQVPKRieriVKGICEAYGASYELEY 289
|
|
| M20_Acy1-like |
cd08660 |
M20 Peptidase Aminoacylase 1-like family; This family includes aminoacylase 1 (ACY1) and ... |
6-309 |
8.85e-05 |
|
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: 44.15 E-value: 8.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 6 IELTQQLIRRPSLSPDDAGCQALMIERLRKIGFTIEHMDFGDTqNFWAWRGRGET---LAFAGHTDVVPAGDVDRWinpP 82
Cdd:cd08660 2 INIRRDIHEHPELGFEEVETSKKIRRWLEEEQIEILDVPQLKT-GVIAEIKGGEDgpvIAIRADIDALPIQEQTNL---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 83 FEPTIRdgmlfGRGAADMKGSLAAMVVAAERFVAQHPHH-RGRLAFLITSDEEASAknGTVKVVEALMARNerLDYCLVG 161
Cdd:cd08660 78 FASKVD-----GT*HACGHDFHTTSIIGTA*LLNQRRAElKGTVVFIFQPAEEGAA--GARKVLEAGVLNG--VSAIFGI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 162 EPSSTEIVGDVvkNGRRGSLTC-----NLTIHGVQGHVAYPHLADNPVHRAAP---FLNELVAIEWDRGNDffpaTSMQV 233
Cdd:cd08660 149 HNKPDLPVGTI--GVKEGPL*AsvdvfEIVIKGKGGHASIPNNSIDPIAAAGQiisGLQSVVSRNISSLQN----AVVSI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 234 ANIQAGTgSNNVIPGELFVQFNFRFSTELTDEMIKERVHALLEK----HQLRYTVDWWLSGQPFLTARGKLVDAVVNAIE 309
Cdd:cd08660 223 TRVQGGT-AWNVIPDQAE*EGTVRAFTKEARQAVPEH*RRVAEGiaagYGCQAEFKWFPNGPSEVQNDGTLLNAFSKAAA 301
|
|
| PRK07079 |
PRK07079 |
hypothetical protein; Provisional |
65-136 |
1.22e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235928 [Multi-domain] Cd Length: 469 Bit Score: 43.75 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 65 GHTDVVPaGDVDRWINP--PFEPTIRDGMLFGRGAADMKG----SLAAM-VVAAERfvaqhphhRGRLAF----LITSDE 133
Cdd:PRK07079 92 GHGDVVR-GYDEQWREGlsPWTLTEEGDRWYGRGTADNKGqhtiNLAALeQVLAAR--------GGRLGFnvklLIEMGE 162
|
...
gi 447200569 134 EAS 136
Cdd:PRK07079 163 EIG 165
|
|
| M20_Acy1-like |
cd08019 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
186-278 |
1.60e-04 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349940 [Multi-domain] Cd Length: 372 Bit Score: 43.48 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 186 TIHGVQGHVAYPHLADNPVHRAAPFLNELVAIeWDRGNDFFPATSMQVANIQAGTgSNNVIPGELFVQFNFRFstelTDE 265
Cdd:cd08019 174 EVKGKGGHGSMPHQGIDAVLAAASIVMNLQSI-VSREIDPLEPVVVTVGKLNSGT-RFNVIADEAKIEGTLRT----FNP 247
|
90
....*....|...
gi 447200569 266 MIKERVHALLEKH 278
Cdd:cd08019 248 ETREKTPEIIERI 260
|
|
| M20_dipept_like |
cd05678 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
79-211 |
4.71e-04 |
|
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: 42.09 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 79 INPPFEPTIRdgmLFGRGAADMKGSLAAMVVAAERFVAQHPHHRGRLAFLITSDEEASAKNgtvkVVEALMARNERL--D 156
Cdd:cd05678 106 IFSNLDPEWR---VFARAAADDKGPIMMMLAALDALKAGGIAPKFNVKIILDSEEEKGSPS----LPKAVKEYKELLaaD 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 157 YCLVGEPSSTEIVGDVVKNGRRGSLTCNLTIHGVQ-----GHvaYPHLADNPVHRAAPFL 211
Cdd:cd05678 179 ALIIMDGPAHATNKPTLTFGCRGIATATLTTYGAKvpqhsGH--YGNYAPNPAFRLSSLL 236
|
|
| M20_Acy1_YxeP-like |
cd05669 |
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; ... |
105-322 |
1.67e-03 |
|
M20 Peptidase aminoacyclase-1 YxeP-like proteins, including YxeP, YtnL, YjiB and HipO2; Peptidase M20 family, aminoacyclase-1 YxeP-like subfamily including YxeP, YtnL, YjiB and HipO2, most of which have not been well characterized to date. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity; substrates include indoleacetic acid (IAA) N-conjugates of amino acids, N-acetyl-L-amino acids and aminobenzoylglutamate. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as in the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine). ACY1 appears to physically interact with Sphingosine kinase type 1 (SphK1) and may influence its physiological functions; SphK1 and its product sphingosine-1-phosphate have been shown to promote cell growth and inhibit apoptosis of tumor cells. Strong expression of the human gene and its mouse ortholog Acy1 in brain, liver, and kidney suggest a role of the enzyme in amino acid metabolism of these organs.
Pssm-ID: 349919 [Multi-domain] Cd Length: 371 Bit Score: 39.97 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 105 AAMVVAAERFVAQHPHHRGRLAFLITSDEEASAknGTVKVVEALMARNERldyCLVGEPSSTEI-VGDVVknGRRGSLTC 183
Cdd:cd05669 98 ASLLGAAVLLKEREAELKGTVRLIFQPAEETGA--GAKKVIEAGALDDVS---AIFGFHNKPDLpVGTIG--LKSGALMA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 184 N-----LTIHGVQGHVAYPHLADNPVHRAAPFLNELVAIEwDRGNDFFPATSMQVANIQAGTGSnNVIPGELFVQFNFR- 257
Cdd:cd05669 171 AvdrfeIEIAGKGAHAAKPENGVDPIVAASQIINALQTIV-SRNISPLESAVVSVTRIHAGNTW-NVIPDSAELEGTVRt 248
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 258 FSTELTDEmIKERVHALLEKHQLRYTVD---WWLSGQPFLTARGKLVDAVVNAIEH--YNEIKPQLLTTG 322
Cdd:cd05669 249 FDAEVRQL-VKERFEQIVEGIAAAFGAKiefKWHSGPPAVINDEELTDLASEVAAQagYEVVHAEPSLGG 317
|
|
| M20_Acy1-like |
cd05666 |
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of ... |
179-276 |
4.49e-03 |
|
M20 Peptidase aminoacylase 1 subfamily; Peptidase M20 family, uncharacterized subfamily of bacterial proteins predicted as putative amidohydrolases or hippurate hydrolases. These are a class of zinc binding homodimeric enzymes involved in hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and highly conserved process that is involved in protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. Aminoacylase 1 (ACY1) breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).
Pssm-ID: 349916 [Multi-domain] Cd Length: 373 Bit Score: 38.66 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 179 GSLTCNLTIHGVQGHVAYPHLADNPVHRAAPF---LNELVAiewdRGNDFFPATSMQVANIQAGTgSNNVIPGELFVQFN 255
Cdd:cd05666 171 SADTFEITIRGKGGHAAMPHLGVDPIVAAAQLvqaLQTIVS----RNVDPLDAAVVSVTQIHAGD-AYNVIPDTAELRGT 245
|
90 100
....*....|....*....|..
gi 447200569 256 FR-FSTElTDEMIKERVHALLE 276
Cdd:cd05666 246 VRaFDPE-VRDLIEERIREIAD 266
|
|
| M20_dipept_dapE |
cd05682 |
uncharacterized M20 dipeptidase; Peptidase M20 family, unknown dipeptidase-like subfamily ... |
58-134 |
5.41e-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: 38.47 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447200569 58 GETLAFAGHTDVVPagDVDRWINP--PFEPTIRDGMLFGRGAADmKGSLAAMVVAAERFVAQH--PHhrGRLAFLITSDE 133
Cdd:cd05682 73 DDTVLLYGHMDKQP--PFTGWDEGlgPTKPVIRGDKLYGRGGAD-DGYAIFASLTAIKALQEQgiPH--PRCVVLIEACE 147
|
.
gi 447200569 134 E 134
Cdd:cd05682 148 E 148
|
|
| |
